data_7HCS
# 
_entry.id   7HCS 
# 
_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   7HCS         pdb_00007hcs 10.2210/pdb7hcs/pdb 
WWPDB D_1001407310 ?            ?                   
# 
_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                        7HCS 
_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 'DIMETHYL SULFOXIDE'                                                            78.133    1   ? ? ? ? 
3 non-polymer syn '[(2S,4S)-4-fluoro-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' 236.246   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                                  35.453    1   ? ? ? ? 
5 water       nat water                                                                           18.015    434 ? ? ? ? 
# 
_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 'DIMETHYL SULFOXIDE'                                                            DMS   
3 '[(2S,4S)-4-fluoro-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' A1A58 
4 'CHLORIDE ION'                                                                  CL    
5 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 
A1A58 non-polymer         . '[(2S,4S)-4-fluoro-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' ? 'C11 H13 F N4 O' 
236.246 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                            ? 'C2 H6 O S'      
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                       ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                 ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                         ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                       ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                           ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                      ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                         ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                          ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                      ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                   ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                         ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                          ? 'C3 H7 N O3'     
105.093 
THR   'L-peptide linking' y THREONINE                                                                       ? 'C4 H9 N O3'     
119.119 
TYR   'L-peptide linking' y TYROSINE                                                                        ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                          ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 DMS   1   301 301  DMS   DMS A . 
D 3 A1A58 1   302 201  A1A58 LA1 A . 
E 4 CL    1   303 1    CL    CL  A . 
F 5 HOH   1   401 2    HOH   HOH A . 
F 5 HOH   2   402 292  HOH   HOH A . 
F 5 HOH   3   403 1290 HOH   HOH A . 
F 5 HOH   4   404 1289 HOH   HOH A . 
F 5 HOH   5   405 229  HOH   HOH A . 
F 5 HOH   6   406 1301 HOH   HOH A . 
F 5 HOH   7   407 196  HOH   HOH A . 
F 5 HOH   8   408 21   HOH   HOH A . 
F 5 HOH   9   409 209  HOH   HOH A . 
F 5 HOH   10  410 625  HOH   HOH A . 
F 5 HOH   11  411 93   HOH   HOH A . 
F 5 HOH   12  412 337  HOH   HOH A . 
F 5 HOH   13  413 661  HOH   HOH A . 
F 5 HOH   14  414 247  HOH   HOH A . 
F 5 HOH   15  415 109  HOH   HOH A . 
F 5 HOH   16  416 1    HOH   HOH A . 
F 5 HOH   17  417 1310 HOH   HOH A . 
F 5 HOH   18  418 493  HOH   HOH A . 
F 5 HOH   19  419 1275 HOH   HOH A . 
F 5 HOH   20  420 1295 HOH   HOH A . 
F 5 HOH   21  421 15   HOH   HOH A . 
F 5 HOH   22  422 105  HOH   HOH A . 
F 5 HOH   23  423 124  HOH   HOH A . 
F 5 HOH   24  424 76   HOH   HOH A . 
F 5 HOH   25  425 281  HOH   HOH A . 
F 5 HOH   26  426 153  HOH   HOH A . 
F 5 HOH   27  427 33   HOH   HOH A . 
F 5 HOH   28  428 393  HOH   HOH A . 
F 5 HOH   29  429 236  HOH   HOH A . 
F 5 HOH   30  430 351  HOH   HOH A . 
F 5 HOH   31  431 49   HOH   HOH A . 
F 5 HOH   32  432 1283 HOH   HOH A . 
F 5 HOH   33  433 164  HOH   HOH A . 
F 5 HOH   34  434 3    HOH   HOH A . 
F 5 HOH   35  435 469  HOH   HOH A . 
F 5 HOH   36  436 151  HOH   HOH A . 
F 5 HOH   37  437 192  HOH   HOH A . 
F 5 HOH   38  438 132  HOH   HOH A . 
F 5 HOH   39  439 136  HOH   HOH A . 
F 5 HOH   40  440 15   HOH   HOH A . 
F 5 HOH   41  441 964  HOH   HOH A . 
F 5 HOH   42  442 140  HOH   HOH A . 
F 5 HOH   43  443 17   HOH   HOH A . 
F 5 HOH   44  444 225  HOH   HOH A . 
F 5 HOH   45  445 8    HOH   HOH A . 
F 5 HOH   46  446 12   HOH   HOH A . 
F 5 HOH   47  447 396  HOH   HOH A . 
F 5 HOH   48  448 241  HOH   HOH A . 
F 5 HOH   49  449 39   HOH   HOH A . 
F 5 HOH   50  450 630  HOH   HOH A . 
F 5 HOH   51  451 42   HOH   HOH A . 
F 5 HOH   52  452 34   HOH   HOH A . 
F 5 HOH   53  453 102  HOH   HOH A . 
F 5 HOH   54  454 18   HOH   HOH A . 
F 5 HOH   55  455 86   HOH   HOH A . 
F 5 HOH   56  456 1300 HOH   HOH A . 
F 5 HOH   57  457 74   HOH   HOH A . 
F 5 HOH   58  458 320  HOH   HOH A . 
F 5 HOH   59  459 409  HOH   HOH A . 
F 5 HOH   60  460 26   HOH   HOH A . 
F 5 HOH   61  461 165  HOH   HOH A . 
F 5 HOH   62  462 461  HOH   HOH A . 
F 5 HOH   63  463 66   HOH   HOH A . 
F 5 HOH   64  464 354  HOH   HOH A . 
F 5 HOH   65  465 56   HOH   HOH A . 
F 5 HOH   66  466 4    HOH   HOH A . 
F 5 HOH   67  467 92   HOH   HOH A . 
F 5 HOH   68  468 162  HOH   HOH A . 
F 5 HOH   69  469 169  HOH   HOH A . 
F 5 HOH   70  470 57   HOH   HOH A . 
F 5 HOH   71  471 155  HOH   HOH A . 
F 5 HOH   72  472 296  HOH   HOH A . 
F 5 HOH   73  473 2    HOH   HOH A . 
F 5 HOH   74  474 218  HOH   HOH A . 
F 5 HOH   75  475 139  HOH   HOH A . 
F 5 HOH   76  476 45   HOH   HOH A . 
F 5 HOH   77  477 662  HOH   HOH A . 
F 5 HOH   78  478 36   HOH   HOH A . 
F 5 HOH   79  479 5    HOH   HOH A . 
F 5 HOH   80  480 81   HOH   HOH A . 
F 5 HOH   81  481 148  HOH   HOH A . 
F 5 HOH   82  482 939  HOH   HOH A . 
F 5 HOH   83  483 26   HOH   HOH A . 
F 5 HOH   84  484 19   HOH   HOH A . 
F 5 HOH   85  485 78   HOH   HOH A . 
F 5 HOH   86  486 195  HOH   HOH A . 
F 5 HOH   87  487 46   HOH   HOH A . 
F 5 HOH   88  488 21   HOH   HOH A . 
F 5 HOH   89  489 366  HOH   HOH A . 
F 5 HOH   90  490 138  HOH   HOH A . 
F 5 HOH   91  491 27   HOH   HOH A . 
F 5 HOH   92  492 10   HOH   HOH A . 
F 5 HOH   93  493 1296 HOH   HOH A . 
F 5 HOH   94  494 134  HOH   HOH A . 
F 5 HOH   95  495 154  HOH   HOH A . 
F 5 HOH   96  496 35   HOH   HOH A . 
F 5 HOH   97  497 159  HOH   HOH A . 
F 5 HOH   98  498 116  HOH   HOH A . 
F 5 HOH   99  499 1308 HOH   HOH A . 
F 5 HOH   100 500 58   HOH   HOH A . 
F 5 HOH   101 501 186  HOH   HOH A . 
F 5 HOH   102 502 303  HOH   HOH A . 
F 5 HOH   103 503 83   HOH   HOH A . 
F 5 HOH   104 504 3    HOH   HOH A . 
F 5 HOH   105 505 1313 HOH   HOH A . 
F 5 HOH   106 506 67   HOH   HOH A . 
F 5 HOH   107 507 96   HOH   HOH A . 
F 5 HOH   108 508 12   HOH   HOH A . 
F 5 HOH   109 509 85   HOH   HOH A . 
F 5 HOH   110 510 1315 HOH   HOH A . 
F 5 HOH   111 511 122  HOH   HOH A . 
F 5 HOH   112 512 1094 HOH   HOH A . 
F 5 HOH   113 513 6    HOH   HOH A . 
F 5 HOH   114 514 121  HOH   HOH A . 
F 5 HOH   115 515 278  HOH   HOH A . 
F 5 HOH   116 516 5    HOH   HOH A . 
F 5 HOH   117 517 381  HOH   HOH A . 
F 5 HOH   118 518 333  HOH   HOH A . 
F 5 HOH   119 519 53   HOH   HOH A . 
F 5 HOH   120 520 68   HOH   HOH A . 
F 5 HOH   121 521 156  HOH   HOH A . 
F 5 HOH   122 522 1309 HOH   HOH A . 
F 5 HOH   123 523 25   HOH   HOH A . 
F 5 HOH   124 524 115  HOH   HOH A . 
F 5 HOH   125 525 123  HOH   HOH A . 
F 5 HOH   126 526 70   HOH   HOH A . 
F 5 HOH   127 527 1068 HOH   HOH A . 
F 5 HOH   128 528 397  HOH   HOH A . 
F 5 HOH   129 529 24   HOH   HOH A . 
F 5 HOH   130 530 4    HOH   HOH A . 
F 5 HOH   131 531 125  HOH   HOH A . 
F 5 HOH   132 532 95   HOH   HOH A . 
F 5 HOH   133 533 199  HOH   HOH A . 
F 5 HOH   134 534 51   HOH   HOH A . 
F 5 HOH   135 535 1222 HOH   HOH A . 
F 5 HOH   136 536 1279 HOH   HOH A . 
F 5 HOH   137 537 582  HOH   HOH A . 
F 5 HOH   138 538 212  HOH   HOH A . 
F 5 HOH   139 539 1286 HOH   HOH A . 
F 5 HOH   140 540 16   HOH   HOH A . 
F 5 HOH   141 541 405  HOH   HOH A . 
F 5 HOH   142 542 8    HOH   HOH A . 
F 5 HOH   143 543 7    HOH   HOH A . 
F 5 HOH   144 544 71   HOH   HOH A . 
F 5 HOH   145 545 1189 HOH   HOH A . 
F 5 HOH   146 546 73   HOH   HOH A . 
F 5 HOH   147 547 952  HOH   HOH A . 
F 5 HOH   148 548 80   HOH   HOH A . 
F 5 HOH   149 549 97   HOH   HOH A . 
F 5 HOH   150 550 94   HOH   HOH A . 
F 5 HOH   151 551 1238 HOH   HOH A . 
F 5 HOH   152 552 40   HOH   HOH A . 
F 5 HOH   153 553 944  HOH   HOH A . 
F 5 HOH   154 554 188  HOH   HOH A . 
F 5 HOH   155 555 104  HOH   HOH A . 
F 5 HOH   156 556 79   HOH   HOH A . 
F 5 HOH   157 557 576  HOH   HOH A . 
F 5 HOH   158 558 1119 HOH   HOH A . 
F 5 HOH   159 559 1134 HOH   HOH A . 
F 5 HOH   160 560 330  HOH   HOH A . 
F 5 HOH   161 561 509  HOH   HOH A . 
F 5 HOH   162 562 107  HOH   HOH A . 
F 5 HOH   163 563 163  HOH   HOH A . 
F 5 HOH   164 564 726  HOH   HOH A . 
F 5 HOH   165 565 408  HOH   HOH A . 
F 5 HOH   166 566 27   HOH   HOH A . 
F 5 HOH   167 567 756  HOH   HOH A . 
F 5 HOH   168 568 361  HOH   HOH A . 
F 5 HOH   169 569 126  HOH   HOH A . 
F 5 HOH   170 570 28   HOH   HOH A . 
F 5 HOH   171 571 556  HOH   HOH A . 
F 5 HOH   172 572 14   HOH   HOH A . 
F 5 HOH   173 573 319  HOH   HOH A . 
F 5 HOH   174 574 280  HOH   HOH A . 
F 5 HOH   175 575 801  HOH   HOH A . 
F 5 HOH   176 576 20   HOH   HOH A . 
F 5 HOH   177 577 250  HOH   HOH A . 
F 5 HOH   178 578 63   HOH   HOH A . 
F 5 HOH   179 579 1307 HOH   HOH A . 
F 5 HOH   180 580 1276 HOH   HOH A . 
F 5 HOH   181 581 342  HOH   HOH A . 
F 5 HOH   182 582 11   HOH   HOH A . 
F 5 HOH   183 583 1287 HOH   HOH A . 
F 5 HOH   184 584 135  HOH   HOH A . 
F 5 HOH   185 585 202  HOH   HOH A . 
F 5 HOH   186 586 1306 HOH   HOH A . 
F 5 HOH   187 587 370  HOH   HOH A . 
F 5 HOH   188 588 674  HOH   HOH A . 
F 5 HOH   189 589 13   HOH   HOH A . 
F 5 HOH   190 590 19   HOH   HOH A . 
F 5 HOH   191 591 919  HOH   HOH A . 
F 5 HOH   192 592 1299 HOH   HOH A . 
F 5 HOH   193 593 224  HOH   HOH A . 
F 5 HOH   194 594 521  HOH   HOH A . 
F 5 HOH   195 595 267  HOH   HOH A . 
F 5 HOH   196 596 695  HOH   HOH A . 
F 5 HOH   197 597 318  HOH   HOH A . 
F 5 HOH   198 598 711  HOH   HOH A . 
F 5 HOH   199 599 208  HOH   HOH A . 
F 5 HOH   200 600 152  HOH   HOH A . 
F 5 HOH   201 601 309  HOH   HOH A . 
F 5 HOH   202 602 17   HOH   HOH A . 
F 5 HOH   203 603 331  HOH   HOH A . 
F 5 HOH   204 604 941  HOH   HOH A . 
F 5 HOH   205 605 805  HOH   HOH A . 
F 5 HOH   206 606 356  HOH   HOH A . 
F 5 HOH   207 607 1314 HOH   HOH A . 
F 5 HOH   208 608 315  HOH   HOH A . 
F 5 HOH   209 609 7    HOH   HOH A . 
F 5 HOH   210 610 263  HOH   HOH A . 
F 5 HOH   211 611 9    HOH   HOH A . 
F 5 HOH   212 612 22   HOH   HOH A . 
F 5 HOH   213 613 1071 HOH   HOH A . 
F 5 HOH   214 614 371  HOH   HOH A . 
F 5 HOH   215 615 326  HOH   HOH A . 
F 5 HOH   216 616 180  HOH   HOH A . 
F 5 HOH   217 617 1284 HOH   HOH A . 
F 5 HOH   218 618 350  HOH   HOH A . 
F 5 HOH   219 619 363  HOH   HOH A . 
F 5 HOH   220 620 18   HOH   HOH A . 
F 5 HOH   221 621 313  HOH   HOH A . 
F 5 HOH   222 622 185  HOH   HOH A . 
F 5 HOH   223 623 429  HOH   HOH A . 
F 5 HOH   224 624 772  HOH   HOH A . 
F 5 HOH   225 625 16   HOH   HOH A . 
F 5 HOH   226 626 376  HOH   HOH A . 
F 5 HOH   227 627 1074 HOH   HOH A . 
F 5 HOH   228 628 346  HOH   HOH A . 
F 5 HOH   229 629 1292 HOH   HOH A . 
F 5 HOH   230 630 23   HOH   HOH A . 
F 5 HOH   231 631 24   HOH   HOH A . 
F 5 HOH   232 632 25   HOH   HOH A . 
F 5 HOH   233 633 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 398  HOH   HOH B . 
G 5 HOH   3   203 240  HOH   HOH B . 
G 5 HOH   4   204 549  HOH   HOH B . 
G 5 HOH   5   205 364  HOH   HOH B . 
G 5 HOH   6   206 1249 HOH   HOH B . 
G 5 HOH   7   207 232  HOH   HOH B . 
G 5 HOH   8   208 531  HOH   HOH B . 
G 5 HOH   9   209 900  HOH   HOH B . 
G 5 HOH   10  210 758  HOH   HOH B . 
G 5 HOH   11  211 50   HOH   HOH B . 
G 5 HOH   12  212 358  HOH   HOH B . 
G 5 HOH   13  213 120  HOH   HOH B . 
G 5 HOH   14  214 353  HOH   HOH B . 
G 5 HOH   15  215 743  HOH   HOH B . 
G 5 HOH   16  216 264  HOH   HOH B . 
G 5 HOH   17  217 452  HOH   HOH B . 
G 5 HOH   18  218 444  HOH   HOH B . 
G 5 HOH   19  219 1140 HOH   HOH B . 
G 5 HOH   20  220 131  HOH   HOH B . 
G 5 HOH   21  221 343  HOH   HOH B . 
G 5 HOH   22  222 332  HOH   HOH B . 
G 5 HOH   23  223 75   HOH   HOH B . 
G 5 HOH   24  224 82   HOH   HOH B . 
G 5 HOH   25  225 654  HOH   HOH B . 
G 5 HOH   26  226 128  HOH   HOH B . 
G 5 HOH   27  227 276  HOH   HOH B . 
G 5 HOH   28  228 54   HOH   HOH B . 
G 5 HOH   29  229 69   HOH   HOH B . 
G 5 HOH   30  230 166  HOH   HOH B . 
G 5 HOH   31  231 221  HOH   HOH B . 
G 5 HOH   32  232 127  HOH   HOH B . 
G 5 HOH   33  233 272  HOH   HOH B . 
G 5 HOH   34  234 325  HOH   HOH B . 
G 5 HOH   35  235 60   HOH   HOH B . 
G 5 HOH   36  236 129  HOH   HOH B . 
G 5 HOH   37  237 205  HOH   HOH B . 
G 5 HOH   38  238 1312 HOH   HOH B . 
G 5 HOH   39  239 1    HOH   HOH B . 
G 5 HOH   40  240 41   HOH   HOH B . 
G 5 HOH   41  241 1278 HOH   HOH B . 
G 5 HOH   42  242 172  HOH   HOH B . 
G 5 HOH   43  243 110  HOH   HOH B . 
G 5 HOH   44  244 133  HOH   HOH B . 
G 5 HOH   45  245 52   HOH   HOH B . 
G 5 HOH   46  246 150  HOH   HOH B . 
G 5 HOH   47  247 300  HOH   HOH B . 
G 5 HOH   48  248 31   HOH   HOH B . 
G 5 HOH   49  249 9    HOH   HOH B . 
G 5 HOH   50  250 723  HOH   HOH B . 
G 5 HOH   51  251 347  HOH   HOH B . 
G 5 HOH   52  252 72   HOH   HOH B . 
G 5 HOH   53  253 181  HOH   HOH B . 
G 5 HOH   54  254 243  HOH   HOH B . 
G 5 HOH   55  255 14   HOH   HOH B . 
G 5 HOH   56  256 143  HOH   HOH B . 
G 5 HOH   57  257 30   HOH   HOH B . 
G 5 HOH   58  258 282  HOH   HOH B . 
G 5 HOH   59  259 62   HOH   HOH B . 
G 5 HOH   60  260 144  HOH   HOH B . 
G 5 HOH   61  261 1277 HOH   HOH B . 
G 5 HOH   62  262 10   HOH   HOH B . 
G 5 HOH   63  263 47   HOH   HOH B . 
G 5 HOH   64  264 231  HOH   HOH B . 
G 5 HOH   65  265 391  HOH   HOH B . 
G 5 HOH   66  266 416  HOH   HOH B . 
G 5 HOH   67  267 61   HOH   HOH B . 
G 5 HOH   68  268 271  HOH   HOH B . 
G 5 HOH   69  269 20   HOH   HOH B . 
G 5 HOH   70  270 59   HOH   HOH B . 
G 5 HOH   71  271 11   HOH   HOH B . 
G 5 HOH   72  272 117  HOH   HOH B . 
G 5 HOH   73  273 84   HOH   HOH B . 
G 5 HOH   74  274 103  HOH   HOH B . 
G 5 HOH   75  275 114  HOH   HOH B . 
G 5 HOH   76  276 287  HOH   HOH B . 
G 5 HOH   77  277 175  HOH   HOH B . 
G 5 HOH   78  278 1106 HOH   HOH B . 
G 5 HOH   79  279 242  HOH   HOH B . 
G 5 HOH   80  280 147  HOH   HOH B . 
G 5 HOH   81  281 235  HOH   HOH B . 
G 5 HOH   82  282 77   HOH   HOH B . 
G 5 HOH   83  283 22   HOH   HOH B . 
G 5 HOH   84  284 43   HOH   HOH B . 
G 5 HOH   85  285 1066 HOH   HOH B . 
G 5 HOH   86  286 1285 HOH   HOH B . 
G 5 HOH   87  287 88   HOH   HOH B . 
G 5 HOH   88  288 302  HOH   HOH B . 
G 5 HOH   89  289 99   HOH   HOH B . 
G 5 HOH   90  290 13   HOH   HOH B . 
G 5 HOH   91  291 106  HOH   HOH B . 
G 5 HOH   92  292 89   HOH   HOH B . 
G 5 HOH   93  293 252  HOH   HOH B . 
G 5 HOH   94  294 38   HOH   HOH B . 
G 5 HOH   95  295 216  HOH   HOH B . 
G 5 HOH   96  296 297  HOH   HOH B . 
G 5 HOH   97  297 137  HOH   HOH B . 
G 5 HOH   98  298 1305 HOH   HOH B . 
G 5 HOH   99  299 960  HOH   HOH B . 
G 5 HOH   100 300 160  HOH   HOH B . 
G 5 HOH   101 301 112  HOH   HOH B . 
G 5 HOH   102 302 101  HOH   HOH B . 
G 5 HOH   103 303 316  HOH   HOH B . 
G 5 HOH   104 304 704  HOH   HOH B . 
G 5 HOH   105 305 32   HOH   HOH B . 
G 5 HOH   106 306 37   HOH   HOH B . 
G 5 HOH   107 307 118  HOH   HOH B . 
G 5 HOH   108 308 48   HOH   HOH B . 
G 5 HOH   109 309 142  HOH   HOH B . 
G 5 HOH   110 310 299  HOH   HOH B . 
G 5 HOH   111 311 311  HOH   HOH B . 
G 5 HOH   112 312 23   HOH   HOH B . 
G 5 HOH   113 313 91   HOH   HOH B . 
G 5 HOH   114 314 362  HOH   HOH B . 
G 5 HOH   115 315 215  HOH   HOH B . 
G 5 HOH   116 316 55   HOH   HOH B . 
G 5 HOH   117 317 635  HOH   HOH B . 
G 5 HOH   118 318 44   HOH   HOH B . 
G 5 HOH   119 319 170  HOH   HOH B . 
G 5 HOH   120 320 28   HOH   HOH B . 
G 5 HOH   121 321 177  HOH   HOH B . 
G 5 HOH   122 322 220  HOH   HOH B . 
G 5 HOH   123 323 182  HOH   HOH B . 
G 5 HOH   124 324 1291 HOH   HOH B . 
G 5 HOH   125 325 197  HOH   HOH B . 
G 5 HOH   126 326 387  HOH   HOH B . 
G 5 HOH   127 327 445  HOH   HOH B . 
G 5 HOH   128 328 100  HOH   HOH B . 
G 5 HOH   129 329 29   HOH   HOH B . 
G 5 HOH   130 330 717  HOH   HOH B . 
G 5 HOH   131 331 98   HOH   HOH B . 
G 5 HOH   132 332 341  HOH   HOH B . 
G 5 HOH   133 333 207  HOH   HOH B . 
G 5 HOH   134 334 161  HOH   HOH B . 
G 5 HOH   135 335 1274 HOH   HOH B . 
G 5 HOH   136 336 141  HOH   HOH B . 
G 5 HOH   137 337 234  HOH   HOH B . 
G 5 HOH   138 338 1294 HOH   HOH B . 
G 5 HOH   139 339 65   HOH   HOH B . 
G 5 HOH   140 340 1126 HOH   HOH B . 
G 5 HOH   141 341 334  HOH   HOH B . 
G 5 HOH   142 342 1293 HOH   HOH B . 
G 5 HOH   143 343 619  HOH   HOH B . 
G 5 HOH   144 344 339  HOH   HOH B . 
G 5 HOH   145 345 178  HOH   HOH B . 
G 5 HOH   146 346 87   HOH   HOH B . 
G 5 HOH   147 347 90   HOH   HOH B . 
G 5 HOH   148 348 463  HOH   HOH B . 
G 5 HOH   149 349 623  HOH   HOH B . 
G 5 HOH   150 350 1304 HOH   HOH B . 
G 5 HOH   151 351 191  HOH   HOH B . 
G 5 HOH   152 352 1280 HOH   HOH B . 
G 5 HOH   153 353 304  HOH   HOH B . 
G 5 HOH   154 354 1046 HOH   HOH B . 
G 5 HOH   155 355 335  HOH   HOH B . 
G 5 HOH   156 356 203  HOH   HOH B . 
G 5 HOH   157 357 1077 HOH   HOH B . 
G 5 HOH   158 358 290  HOH   HOH B . 
G 5 HOH   159 359 541  HOH   HOH B . 
G 5 HOH   160 360 479  HOH   HOH B . 
G 5 HOH   161 361 389  HOH   HOH B . 
G 5 HOH   162 362 718  HOH   HOH B . 
G 5 HOH   163 363 1072 HOH   HOH B . 
G 5 HOH   164 364 283  HOH   HOH B . 
G 5 HOH   165 365 291  HOH   HOH B . 
G 5 HOH   166 366 615  HOH   HOH B . 
G 5 HOH   167 367 1316 HOH   HOH B . 
G 5 HOH   168 368 373  HOH   HOH B . 
G 5 HOH   169 369 898  HOH   HOH B . 
G 5 HOH   170 370 340  HOH   HOH B . 
G 5 HOH   171 371 667  HOH   HOH B . 
G 5 HOH   172 372 1303 HOH   HOH B . 
G 5 HOH   173 373 190  HOH   HOH B . 
G 5 HOH   174 374 310  HOH   HOH B . 
G 5 HOH   175 375 431  HOH   HOH B . 
G 5 HOH   176 376 1000 HOH   HOH B . 
G 5 HOH   177 377 1173 HOH   HOH B . 
G 5 HOH   178 378 149  HOH   HOH B . 
G 5 HOH   179 379 183  HOH   HOH B . 
G 5 HOH   180 380 418  HOH   HOH B . 
G 5 HOH   181 381 1311 HOH   HOH B . 
G 5 HOH   182 382 1163 HOH   HOH B . 
G 5 HOH   183 383 424  HOH   HOH B . 
G 5 HOH   184 384 176  HOH   HOH B . 
G 5 HOH   185 385 248  HOH   HOH B . 
G 5 HOH   186 386 981  HOH   HOH B . 
G 5 HOH   187 387 491  HOH   HOH B . 
G 5 HOH   188 388 1298 HOH   HOH B . 
G 5 HOH   189 389 470  HOH   HOH B . 
G 5 HOH   190 390 265  HOH   HOH B . 
G 5 HOH   191 391 184  HOH   HOH B . 
G 5 HOH   192 392 360  HOH   HOH B . 
G 5 HOH   193 393 410  HOH   HOH B . 
G 5 HOH   194 394 355  HOH   HOH B . 
G 5 HOH   195 395 274  HOH   HOH B . 
G 5 HOH   196 396 314  HOH   HOH B . 
G 5 HOH   197 397 566  HOH   HOH B . 
G 5 HOH   198 398 157  HOH   HOH B . 
G 5 HOH   199 399 792  HOH   HOH B . 
G 5 HOH   200 400 321  HOH   HOH B . 
G 5 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HCS 
_cell.length_a           88.779 
_cell.length_b           88.779 
_cell.length_c           39.442 
_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                         7HCS 
_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          7HCS 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.56 
_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   2023-03-04 
_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                     7HCS 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.390 
_reflns.d_resolution_high            0.990 
_reflns.number_obs                   170513 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.800 
_reflns.pdbx_Rmerge_I_obs            0.064 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        10.100 
_reflns.B_iso_Wilson_estimate        11.910 
_reflns.pdbx_redundancy              6.200 
_reflns.pdbx_Rrim_I_all              0.070 
_reflns.pdbx_Rpim_I_all              0.027 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1058705 
_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 0.990 1.010  ? 28757 8083 ? 1.948 ? ? ? 3.600 ? 0.400  ? ? ? ? ? ? 96.500 2.277 1.137 0.306 
1 2 5.420 44.390 ? 7748  1132 ? 0.031 ? ? ? 6.800 ? 40.100 ? ? ? ? ? ? 99.900 0.033 0.012 0.999 
# 
_refine.entry_id                                 7HCS 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9900 
_refine.ls_d_res_low                             44.3900 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.5300 
_refine.ls_number_reflns_obs                     169917 
_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                          0.1493 
_refine.ls_R_factor_R_work                       0.1485 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1650 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  8195 
_refine.ls_number_reflns_R_work                  161722 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.8824 
_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                            0.1300 
_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                                72.670 
_refine.B_iso_min                                7.850 
_refine.pdbx_overall_phase_error                 19.0000 
_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                       0.9900 
_refine_hist.d_res_low                        44.3900 
_refine_hist.pdbx_number_atoms_ligand         41 
_refine_hist.number_atoms_solvent             434 
_refine_hist.number_atoms_total               3017 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           13.19 
_refine_hist.pdbx_B_iso_mean_solvent          30.28 
_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 
0.9900 1.0000  30 88.0000  4748 . 0.4519 0.4137 . 237 0.0000 4985 . 'X-RAY DIFFRACTION' 
1.0000 1.0100  30 99.0000  5352 . 0.4123 0.4110 . 276 0.0000 5628 . 'X-RAY DIFFRACTION' 
1.0100 1.0300  30 100.0000 5376 . 0.3567 0.3515 . 241 0.0000 5617 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5414 . 0.3166 0.3044 . 279 0.0000 5693 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5340 . 0.2835 0.2988 . 283 0.0000 5623 . 'X-RAY DIFFRACTION' 
1.0500 1.0700  30 100.0000 5400 . 0.2663 0.2767 . 324 0.0000 5724 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 5327 . 0.2455 0.2769 . 274 0.0000 5601 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 5420 . 0.2260 0.2368 . 248 0.0000 5668 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5367 . 0.2036 0.2061 . 288 0.0000 5655 . 'X-RAY DIFFRACTION' 
1.1200 1.1300  30 100.0000 5406 . 0.1785 0.1986 . 251 0.0000 5657 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 5443 . 0.1687 0.1834 . 258 0.0000 5701 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 5386 . 0.1521 0.1747 . 273 0.0000 5659 . 'X-RAY DIFFRACTION' 
1.1700 1.2000  30 100.0000 5402 . 0.1457 0.1769 . 275 0.0000 5677 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 100.0000 5358 . 0.1338 0.1642 . 295 0.0000 5653 . 'X-RAY DIFFRACTION' 
1.2200 1.2500  30 100.0000 5432 . 0.1340 0.1554 . 251 0.0000 5683 . 'X-RAY DIFFRACTION' 
1.2500 1.2800  30 100.0000 5417 . 0.1327 0.1706 . 263 0.0000 5680 . 'X-RAY DIFFRACTION' 
1.2800 1.3100  30 100.0000 5373 . 0.1302 0.1601 . 272 0.0000 5645 . 'X-RAY DIFFRACTION' 
1.3100 1.3400  30 100.0000 5384 . 0.1332 0.1555 . 287 0.0000 5671 . 'X-RAY DIFFRACTION' 
1.3400 1.3800  30 100.0000 5411 . 0.1337 0.1615 . 284 0.0000 5695 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 5442 . 0.1319 0.1734 . 258 0.0000 5700 . 'X-RAY DIFFRACTION' 
1.4300 1.4800  30 100.0000 5424 . 0.1261 0.1356 . 273 0.0000 5697 . 'X-RAY DIFFRACTION' 
1.4800 1.5400  30 100.0000 5384 . 0.1175 0.1332 . 285 0.0000 5669 . 'X-RAY DIFFRACTION' 
1.5400 1.6100  30 100.0000 5399 . 0.1176 0.1328 . 276 0.0000 5675 . 'X-RAY DIFFRACTION' 
1.6100 1.6900  30 100.0000 5434 . 0.1231 0.1388 . 266 0.0000 5700 . 'X-RAY DIFFRACTION' 
1.6900 1.8000  30 100.0000 5478 . 0.1317 0.1398 . 256 0.0000 5734 . 'X-RAY DIFFRACTION' 
1.8000 1.9400  30 100.0000 5407 . 0.1303 0.1369 . 299 0.0000 5706 . 'X-RAY DIFFRACTION' 
1.9400 2.1300  30 100.0000 5424 . 0.1347 0.1465 . 272 0.0000 5696 . 'X-RAY DIFFRACTION' 
2.1300 2.4400  30 100.0000 5444 . 0.1326 0.1432 . 300 0.0000 5744 . 'X-RAY DIFFRACTION' 
2.4400 3.0800  30 100.0000 5496 . 0.1458 0.1649 . 282 0.0000 5778 . 'X-RAY DIFFRACTION' 
3.0800 44.3900 30 100.0000 5634 . 0.1491 0.1715 . 269 0.0000 5903 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HCS 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0000609' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HCS 
_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 5 ? 
# 
_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 7HCS A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HCS 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 7HCS SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HCS MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HCS SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HCS 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 
2 1 B,G       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HCS 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86 ? ? 54.95 -132.74 
2 1 HIS B 86 ? ? 58.03 -127.36 
# 
_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 628 ? 5.90 .    
2 1 O ? A HOH 629 ? 5.98 .    
3 1 O B A HOH 630 ? 6.35 .    
4 1 O B A HOH 631 ? .    6.48 
5 1 O B A HOH 632 ? 6.76 .    
6 1 O ? A HOH 633 ? 7.47 .    
7 1 O ? B HOH 401 ? 6.35 .    
# 
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 
A1A58 N2   N  Y N 1   
A1A58 C3   C  N N 2   
A1A58 C6   C  Y N 3   
A1A58 C9   C  Y N 4   
A1A58 C1   C  N N 5   
A1A58 C10  C  Y N 6   
A1A58 C11  C  Y N 7   
A1A58 C2   C  N S 8   
A1A58 C4   C  N S 9   
A1A58 C5   C  N N 10  
A1A58 C7   C  Y N 11  
A1A58 C8   C  Y N 12  
A1A58 F1   F  N N 13  
A1A58 N1   N  N N 14  
A1A58 N3   N  Y N 15  
A1A58 N4   N  Y N 16  
A1A58 O1   O  N N 17  
A1A58 H7   H  N N 18  
A1A58 H6   H  N N 19  
A1A58 H5   H  N N 20  
A1A58 H4   H  N N 21  
A1A58 H11  H  N N 22  
A1A58 H12  H  N N 23  
A1A58 H1   H  N N 24  
A1A58 H2   H  N N 25  
A1A58 H9   H  N N 26  
A1A58 H8   H  N N 27  
A1A58 H10  H  N N 28  
A1A58 H13  H  N N 29  
A1A58 H3   H  N N 30  
ALA   N    N  N N 31  
ALA   CA   C  N S 32  
ALA   C    C  N N 33  
ALA   O    O  N N 34  
ALA   CB   C  N N 35  
ALA   OXT  O  N N 36  
ALA   H    H  N N 37  
ALA   H2   H  N N 38  
ALA   HA   H  N N 39  
ALA   HB1  H  N N 40  
ALA   HB2  H  N N 41  
ALA   HB3  H  N N 42  
ALA   HXT  H  N N 43  
ARG   N    N  N N 44  
ARG   CA   C  N S 45  
ARG   C    C  N N 46  
ARG   O    O  N N 47  
ARG   CB   C  N N 48  
ARG   CG   C  N N 49  
ARG   CD   C  N N 50  
ARG   NE   N  N N 51  
ARG   CZ   C  N N 52  
ARG   NH1  N  N N 53  
ARG   NH2  N  N N 54  
ARG   OXT  O  N N 55  
ARG   H    H  N N 56  
ARG   H2   H  N N 57  
ARG   HA   H  N N 58  
ARG   HB2  H  N N 59  
ARG   HB3  H  N N 60  
ARG   HG2  H  N N 61  
ARG   HG3  H  N N 62  
ARG   HD2  H  N N 63  
ARG   HD3  H  N N 64  
ARG   HE   H  N N 65  
ARG   HH11 H  N N 66  
ARG   HH12 H  N N 67  
ARG   HH21 H  N N 68  
ARG   HH22 H  N N 69  
ARG   HXT  H  N N 70  
ASN   N    N  N N 71  
ASN   CA   C  N S 72  
ASN   C    C  N N 73  
ASN   O    O  N N 74  
ASN   CB   C  N N 75  
ASN   CG   C  N N 76  
ASN   OD1  O  N N 77  
ASN   ND2  N  N N 78  
ASN   OXT  O  N N 79  
ASN   H    H  N N 80  
ASN   H2   H  N N 81  
ASN   HA   H  N N 82  
ASN   HB2  H  N N 83  
ASN   HB3  H  N N 84  
ASN   HD21 H  N N 85  
ASN   HD22 H  N N 86  
ASN   HXT  H  N N 87  
ASP   N    N  N N 88  
ASP   CA   C  N S 89  
ASP   C    C  N N 90  
ASP   O    O  N N 91  
ASP   CB   C  N N 92  
ASP   CG   C  N N 93  
ASP   OD1  O  N N 94  
ASP   OD2  O  N N 95  
ASP   OXT  O  N N 96  
ASP   H    H  N N 97  
ASP   H2   H  N N 98  
ASP   HA   H  N N 99  
ASP   HB2  H  N N 100 
ASP   HB3  H  N N 101 
ASP   HD2  H  N N 102 
ASP   HXT  H  N N 103 
CL    CL   CL N N 104 
CYS   N    N  N N 105 
CYS   CA   C  N R 106 
CYS   C    C  N N 107 
CYS   O    O  N N 108 
CYS   CB   C  N N 109 
CYS   SG   S  N N 110 
CYS   OXT  O  N N 111 
CYS   H    H  N N 112 
CYS   H2   H  N N 113 
CYS   HA   H  N N 114 
CYS   HB2  H  N N 115 
CYS   HB3  H  N N 116 
CYS   HG   H  N N 117 
CYS   HXT  H  N N 118 
DMS   S    S  N N 119 
DMS   O    O  N N 120 
DMS   C1   C  N N 121 
DMS   C2   C  N N 122 
DMS   H11  H  N N 123 
DMS   H12  H  N N 124 
DMS   H13  H  N N 125 
DMS   H21  H  N N 126 
DMS   H22  H  N N 127 
DMS   H23  H  N N 128 
GLN   N    N  N N 129 
GLN   CA   C  N S 130 
GLN   C    C  N N 131 
GLN   O    O  N N 132 
GLN   CB   C  N N 133 
GLN   CG   C  N N 134 
GLN   CD   C  N N 135 
GLN   OE1  O  N N 136 
GLN   NE2  N  N N 137 
GLN   OXT  O  N N 138 
GLN   H    H  N N 139 
GLN   H2   H  N N 140 
GLN   HA   H  N N 141 
GLN   HB2  H  N N 142 
GLN   HB3  H  N N 143 
GLN   HG2  H  N N 144 
GLN   HG3  H  N N 145 
GLN   HE21 H  N N 146 
GLN   HE22 H  N N 147 
GLN   HXT  H  N N 148 
GLU   N    N  N N 149 
GLU   CA   C  N S 150 
GLU   C    C  N N 151 
GLU   O    O  N N 152 
GLU   CB   C  N N 153 
GLU   CG   C  N N 154 
GLU   CD   C  N N 155 
GLU   OE1  O  N N 156 
GLU   OE2  O  N N 157 
GLU   OXT  O  N N 158 
GLU   H    H  N N 159 
GLU   H2   H  N N 160 
GLU   HA   H  N N 161 
GLU   HB2  H  N N 162 
GLU   HB3  H  N N 163 
GLU   HG2  H  N N 164 
GLU   HG3  H  N N 165 
GLU   HE2  H  N N 166 
GLU   HXT  H  N N 167 
GLY   N    N  N N 168 
GLY   CA   C  N N 169 
GLY   C    C  N N 170 
GLY   O    O  N N 171 
GLY   OXT  O  N N 172 
GLY   H    H  N N 173 
GLY   H2   H  N N 174 
GLY   HA2  H  N N 175 
GLY   HA3  H  N N 176 
GLY   HXT  H  N N 177 
HIS   N    N  N N 178 
HIS   CA   C  N S 179 
HIS   C    C  N N 180 
HIS   O    O  N N 181 
HIS   CB   C  N N 182 
HIS   CG   C  Y N 183 
HIS   ND1  N  Y N 184 
HIS   CD2  C  Y N 185 
HIS   CE1  C  Y N 186 
HIS   NE2  N  Y N 187 
HIS   OXT  O  N N 188 
HIS   H    H  N N 189 
HIS   H2   H  N N 190 
HIS   HA   H  N N 191 
HIS   HB2  H  N N 192 
HIS   HB3  H  N N 193 
HIS   HD1  H  N N 194 
HIS   HD2  H  N N 195 
HIS   HE1  H  N N 196 
HIS   HE2  H  N N 197 
HIS   HXT  H  N N 198 
HOH   O    O  N N 199 
HOH   H1   H  N N 200 
HOH   H2   H  N N 201 
ILE   N    N  N N 202 
ILE   CA   C  N S 203 
ILE   C    C  N N 204 
ILE   O    O  N N 205 
ILE   CB   C  N S 206 
ILE   CG1  C  N N 207 
ILE   CG2  C  N N 208 
ILE   CD1  C  N N 209 
ILE   OXT  O  N N 210 
ILE   H    H  N N 211 
ILE   H2   H  N N 212 
ILE   HA   H  N N 213 
ILE   HB   H  N N 214 
ILE   HG12 H  N N 215 
ILE   HG13 H  N N 216 
ILE   HG21 H  N N 217 
ILE   HG22 H  N N 218 
ILE   HG23 H  N N 219 
ILE   HD11 H  N N 220 
ILE   HD12 H  N N 221 
ILE   HD13 H  N N 222 
ILE   HXT  H  N N 223 
LEU   N    N  N N 224 
LEU   CA   C  N S 225 
LEU   C    C  N N 226 
LEU   O    O  N N 227 
LEU   CB   C  N N 228 
LEU   CG   C  N N 229 
LEU   CD1  C  N N 230 
LEU   CD2  C  N N 231 
LEU   OXT  O  N N 232 
LEU   H    H  N N 233 
LEU   H2   H  N N 234 
LEU   HA   H  N N 235 
LEU   HB2  H  N N 236 
LEU   HB3  H  N N 237 
LEU   HG   H  N N 238 
LEU   HD11 H  N N 239 
LEU   HD12 H  N N 240 
LEU   HD13 H  N N 241 
LEU   HD21 H  N N 242 
LEU   HD22 H  N N 243 
LEU   HD23 H  N N 244 
LEU   HXT  H  N N 245 
LYS   N    N  N N 246 
LYS   CA   C  N S 247 
LYS   C    C  N N 248 
LYS   O    O  N N 249 
LYS   CB   C  N N 250 
LYS   CG   C  N N 251 
LYS   CD   C  N N 252 
LYS   CE   C  N N 253 
LYS   NZ   N  N N 254 
LYS   OXT  O  N N 255 
LYS   H    H  N N 256 
LYS   H2   H  N N 257 
LYS   HA   H  N N 258 
LYS   HB2  H  N N 259 
LYS   HB3  H  N N 260 
LYS   HG2  H  N N 261 
LYS   HG3  H  N N 262 
LYS   HD2  H  N N 263 
LYS   HD3  H  N N 264 
LYS   HE2  H  N N 265 
LYS   HE3  H  N N 266 
LYS   HZ1  H  N N 267 
LYS   HZ2  H  N N 268 
LYS   HZ3  H  N N 269 
LYS   HXT  H  N N 270 
MET   N    N  N N 271 
MET   CA   C  N S 272 
MET   C    C  N N 273 
MET   O    O  N N 274 
MET   CB   C  N N 275 
MET   CG   C  N N 276 
MET   SD   S  N N 277 
MET   CE   C  N N 278 
MET   OXT  O  N N 279 
MET   H    H  N N 280 
MET   H2   H  N N 281 
MET   HA   H  N N 282 
MET   HB2  H  N N 283 
MET   HB3  H  N N 284 
MET   HG2  H  N N 285 
MET   HG3  H  N N 286 
MET   HE1  H  N N 287 
MET   HE2  H  N N 288 
MET   HE3  H  N N 289 
MET   HXT  H  N N 290 
PHE   N    N  N N 291 
PHE   CA   C  N S 292 
PHE   C    C  N N 293 
PHE   O    O  N N 294 
PHE   CB   C  N N 295 
PHE   CG   C  Y N 296 
PHE   CD1  C  Y N 297 
PHE   CD2  C  Y N 298 
PHE   CE1  C  Y N 299 
PHE   CE2  C  Y N 300 
PHE   CZ   C  Y N 301 
PHE   OXT  O  N N 302 
PHE   H    H  N N 303 
PHE   H2   H  N N 304 
PHE   HA   H  N N 305 
PHE   HB2  H  N N 306 
PHE   HB3  H  N N 307 
PHE   HD1  H  N N 308 
PHE   HD2  H  N N 309 
PHE   HE1  H  N N 310 
PHE   HE2  H  N N 311 
PHE   HZ   H  N N 312 
PHE   HXT  H  N N 313 
PRO   N    N  N N 314 
PRO   CA   C  N S 315 
PRO   C    C  N N 316 
PRO   O    O  N N 317 
PRO   CB   C  N N 318 
PRO   CG   C  N N 319 
PRO   CD   C  N N 320 
PRO   OXT  O  N N 321 
PRO   H    H  N N 322 
PRO   HA   H  N N 323 
PRO   HB2  H  N N 324 
PRO   HB3  H  N N 325 
PRO   HG2  H  N N 326 
PRO   HG3  H  N N 327 
PRO   HD2  H  N N 328 
PRO   HD3  H  N N 329 
PRO   HXT  H  N N 330 
SER   N    N  N N 331 
SER   CA   C  N S 332 
SER   C    C  N N 333 
SER   O    O  N N 334 
SER   CB   C  N N 335 
SER   OG   O  N N 336 
SER   OXT  O  N N 337 
SER   H    H  N N 338 
SER   H2   H  N N 339 
SER   HA   H  N N 340 
SER   HB2  H  N N 341 
SER   HB3  H  N N 342 
SER   HG   H  N N 343 
SER   HXT  H  N N 344 
THR   N    N  N N 345 
THR   CA   C  N S 346 
THR   C    C  N N 347 
THR   O    O  N N 348 
THR   CB   C  N R 349 
THR   OG1  O  N N 350 
THR   CG2  C  N N 351 
THR   OXT  O  N N 352 
THR   H    H  N N 353 
THR   H2   H  N N 354 
THR   HA   H  N N 355 
THR   HB   H  N N 356 
THR   HG1  H  N N 357 
THR   HG21 H  N N 358 
THR   HG22 H  N N 359 
THR   HG23 H  N N 360 
THR   HXT  H  N N 361 
TYR   N    N  N N 362 
TYR   CA   C  N S 363 
TYR   C    C  N N 364 
TYR   O    O  N N 365 
TYR   CB   C  N N 366 
TYR   CG   C  Y N 367 
TYR   CD1  C  Y N 368 
TYR   CD2  C  Y N 369 
TYR   CE1  C  Y N 370 
TYR   CE2  C  Y N 371 
TYR   CZ   C  Y N 372 
TYR   OH   O  N N 373 
TYR   OXT  O  N N 374 
TYR   H    H  N N 375 
TYR   H2   H  N N 376 
TYR   HA   H  N N 377 
TYR   HB2  H  N N 378 
TYR   HB3  H  N N 379 
TYR   HD1  H  N N 380 
TYR   HD2  H  N N 381 
TYR   HE1  H  N N 382 
TYR   HE2  H  N N 383 
TYR   HH   H  N N 384 
TYR   HXT  H  N N 385 
VAL   N    N  N N 386 
VAL   CA   C  N S 387 
VAL   C    C  N N 388 
VAL   O    O  N N 389 
VAL   CB   C  N N 390 
VAL   CG1  C  N N 391 
VAL   CG2  C  N N 392 
VAL   OXT  O  N N 393 
VAL   H    H  N N 394 
VAL   H2   H  N N 395 
VAL   HA   H  N N 396 
VAL   HB   H  N N 397 
VAL   HG11 H  N N 398 
VAL   HG12 H  N N 399 
VAL   HG13 H  N N 400 
VAL   HG21 H  N N 401 
VAL   HG22 H  N N 402 
VAL   HG23 H  N N 403 
VAL   HXT  H  N N 404 
# 
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 
A1A58 F1  C4   sing N N 1   
A1A58 C4  C3   sing N N 2   
A1A58 C4  C5   sing N N 3   
A1A58 C3  C2   sing N N 4   
A1A58 C5  N1   sing N N 5   
A1A58 C2  N1   sing N N 6   
A1A58 C2  C1   sing N N 7   
A1A58 N1  C6   sing N N 8   
A1A58 C1  O1   sing N N 9   
A1A58 C10 C9   sing Y N 10  
A1A58 C10 C11  doub Y N 11  
A1A58 C6  C9   doub Y N 12  
A1A58 C6  N2   sing Y N 13  
A1A58 C9  C8   sing Y N 14  
A1A58 C11 N4   sing Y N 15  
A1A58 N2  C7   doub Y N 16  
A1A58 C8  N4   sing Y N 17  
A1A58 C8  N3   doub Y N 18  
A1A58 C7  N3   sing Y N 19  
A1A58 C3  H7   sing N N 20  
A1A58 C3  H6   sing N N 21  
A1A58 C1  H5   sing N N 22  
A1A58 C1  H4   sing N N 23  
A1A58 C10 H11  sing N N 24  
A1A58 C11 H12  sing N N 25  
A1A58 C2  H1   sing N N 26  
A1A58 C4  H2   sing N N 27  
A1A58 C5  H9   sing N N 28  
A1A58 C5  H8   sing N N 29  
A1A58 C7  H10  sing N N 30  
A1A58 N4  H13  sing N N 31  
A1A58 O1  H3   sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
CYS   N   CA   sing N N 102 
CYS   N   H    sing N N 103 
CYS   N   H2   sing N N 104 
CYS   CA  C    sing N N 105 
CYS   CA  CB   sing N N 106 
CYS   CA  HA   sing N N 107 
CYS   C   O    doub N N 108 
CYS   C   OXT  sing N N 109 
CYS   CB  SG   sing N N 110 
CYS   CB  HB2  sing N N 111 
CYS   CB  HB3  sing N N 112 
CYS   SG  HG   sing N N 113 
CYS   OXT HXT  sing N N 114 
DMS   S   O    doub N N 115 
DMS   S   C1   sing N N 116 
DMS   S   C2   sing N N 117 
DMS   C1  H11  sing N N 118 
DMS   C1  H12  sing N N 119 
DMS   C1  H13  sing N N 120 
DMS   C2  H21  sing N N 121 
DMS   C2  H22  sing N N 122 
DMS   C2  H23  sing N N 123 
GLN   N   CA   sing N N 124 
GLN   N   H    sing N N 125 
GLN   N   H2   sing N N 126 
GLN   CA  C    sing N N 127 
GLN   CA  CB   sing N N 128 
GLN   CA  HA   sing N N 129 
GLN   C   O    doub N N 130 
GLN   C   OXT  sing N N 131 
GLN   CB  CG   sing N N 132 
GLN   CB  HB2  sing N N 133 
GLN   CB  HB3  sing N N 134 
GLN   CG  CD   sing N N 135 
GLN   CG  HG2  sing N N 136 
GLN   CG  HG3  sing N N 137 
GLN   CD  OE1  doub N N 138 
GLN   CD  NE2  sing N N 139 
GLN   NE2 HE21 sing N N 140 
GLN   NE2 HE22 sing N N 141 
GLN   OXT HXT  sing N N 142 
GLU   N   CA   sing N N 143 
GLU   N   H    sing N N 144 
GLU   N   H2   sing N N 145 
GLU   CA  C    sing N N 146 
GLU   CA  CB   sing N N 147 
GLU   CA  HA   sing N N 148 
GLU   C   O    doub N N 149 
GLU   C   OXT  sing N N 150 
GLU   CB  CG   sing N N 151 
GLU   CB  HB2  sing N N 152 
GLU   CB  HB3  sing N N 153 
GLU   CG  CD   sing N N 154 
GLU   CG  HG2  sing N N 155 
GLU   CG  HG3  sing N N 156 
GLU   CD  OE1  doub N N 157 
GLU   CD  OE2  sing N N 158 
GLU   OE2 HE2  sing N N 159 
GLU   OXT HXT  sing N N 160 
GLY   N   CA   sing N N 161 
GLY   N   H    sing N N 162 
GLY   N   H2   sing N N 163 
GLY   CA  C    sing N N 164 
GLY   CA  HA2  sing N N 165 
GLY   CA  HA3  sing N N 166 
GLY   C   O    doub N N 167 
GLY   C   OXT  sing N N 168 
GLY   OXT HXT  sing N N 169 
HIS   N   CA   sing N N 170 
HIS   N   H    sing N N 171 
HIS   N   H2   sing N N 172 
HIS   CA  C    sing N N 173 
HIS   CA  CB   sing N N 174 
HIS   CA  HA   sing N N 175 
HIS   C   O    doub N N 176 
HIS   C   OXT  sing N N 177 
HIS   CB  CG   sing N N 178 
HIS   CB  HB2  sing N N 179 
HIS   CB  HB3  sing N N 180 
HIS   CG  ND1  sing Y N 181 
HIS   CG  CD2  doub Y N 182 
HIS   ND1 CE1  doub Y N 183 
HIS   ND1 HD1  sing N N 184 
HIS   CD2 NE2  sing Y N 185 
HIS   CD2 HD2  sing N N 186 
HIS   CE1 NE2  sing Y N 187 
HIS   CE1 HE1  sing N N 188 
HIS   NE2 HE2  sing N N 189 
HIS   OXT HXT  sing N N 190 
HOH   O   H1   sing N N 191 
HOH   O   H2   sing N N 192 
ILE   N   CA   sing N N 193 
ILE   N   H    sing N N 194 
ILE   N   H2   sing N N 195 
ILE   CA  C    sing N N 196 
ILE   CA  CB   sing N N 197 
ILE   CA  HA   sing N N 198 
ILE   C   O    doub N N 199 
ILE   C   OXT  sing N N 200 
ILE   CB  CG1  sing N N 201 
ILE   CB  CG2  sing N N 202 
ILE   CB  HB   sing N N 203 
ILE   CG1 CD1  sing N N 204 
ILE   CG1 HG12 sing N N 205 
ILE   CG1 HG13 sing N N 206 
ILE   CG2 HG21 sing N N 207 
ILE   CG2 HG22 sing N N 208 
ILE   CG2 HG23 sing N N 209 
ILE   CD1 HD11 sing N N 210 
ILE   CD1 HD12 sing N N 211 
ILE   CD1 HD13 sing N N 212 
ILE   OXT HXT  sing N N 213 
LEU   N   CA   sing N N 214 
LEU   N   H    sing N N 215 
LEU   N   H2   sing N N 216 
LEU   CA  C    sing N N 217 
LEU   CA  CB   sing N N 218 
LEU   CA  HA   sing N N 219 
LEU   C   O    doub N N 220 
LEU   C   OXT  sing N N 221 
LEU   CB  CG   sing N N 222 
LEU   CB  HB2  sing N N 223 
LEU   CB  HB3  sing N N 224 
LEU   CG  CD1  sing N N 225 
LEU   CG  CD2  sing N N 226 
LEU   CG  HG   sing N N 227 
LEU   CD1 HD11 sing N N 228 
LEU   CD1 HD12 sing N N 229 
LEU   CD1 HD13 sing N N 230 
LEU   CD2 HD21 sing N N 231 
LEU   CD2 HD22 sing N N 232 
LEU   CD2 HD23 sing N N 233 
LEU   OXT HXT  sing N N 234 
LYS   N   CA   sing N N 235 
LYS   N   H    sing N N 236 
LYS   N   H2   sing N N 237 
LYS   CA  C    sing N N 238 
LYS   CA  CB   sing N N 239 
LYS   CA  HA   sing N N 240 
LYS   C   O    doub N N 241 
LYS   C   OXT  sing N N 242 
LYS   CB  CG   sing N N 243 
LYS   CB  HB2  sing N N 244 
LYS   CB  HB3  sing N N 245 
LYS   CG  CD   sing N N 246 
LYS   CG  HG2  sing N N 247 
LYS   CG  HG3  sing N N 248 
LYS   CD  CE   sing N N 249 
LYS   CD  HD2  sing N N 250 
LYS   CD  HD3  sing N N 251 
LYS   CE  NZ   sing N N 252 
LYS   CE  HE2  sing N N 253 
LYS   CE  HE3  sing N N 254 
LYS   NZ  HZ1  sing N N 255 
LYS   NZ  HZ2  sing N N 256 
LYS   NZ  HZ3  sing N N 257 
LYS   OXT HXT  sing N N 258 
MET   N   CA   sing N N 259 
MET   N   H    sing N N 260 
MET   N   H2   sing N N 261 
MET   CA  C    sing N N 262 
MET   CA  CB   sing N N 263 
MET   CA  HA   sing N N 264 
MET   C   O    doub N N 265 
MET   C   OXT  sing N N 266 
MET   CB  CG   sing N N 267 
MET   CB  HB2  sing N N 268 
MET   CB  HB3  sing N N 269 
MET   CG  SD   sing N N 270 
MET   CG  HG2  sing N N 271 
MET   CG  HG3  sing N N 272 
MET   SD  CE   sing N N 273 
MET   CE  HE1  sing N N 274 
MET   CE  HE2  sing N N 275 
MET   CE  HE3  sing N N 276 
MET   OXT HXT  sing N N 277 
PHE   N   CA   sing N N 278 
PHE   N   H    sing N N 279 
PHE   N   H2   sing N N 280 
PHE   CA  C    sing N N 281 
PHE   CA  CB   sing N N 282 
PHE   CA  HA   sing N N 283 
PHE   C   O    doub N N 284 
PHE   C   OXT  sing N N 285 
PHE   CB  CG   sing N N 286 
PHE   CB  HB2  sing N N 287 
PHE   CB  HB3  sing N N 288 
PHE   CG  CD1  doub Y N 289 
PHE   CG  CD2  sing Y N 290 
PHE   CD1 CE1  sing Y N 291 
PHE   CD1 HD1  sing N N 292 
PHE   CD2 CE2  doub Y N 293 
PHE   CD2 HD2  sing N N 294 
PHE   CE1 CZ   doub Y N 295 
PHE   CE1 HE1  sing N N 296 
PHE   CE2 CZ   sing Y N 297 
PHE   CE2 HE2  sing N N 298 
PHE   CZ  HZ   sing N N 299 
PHE   OXT HXT  sing N N 300 
PRO   N   CA   sing N N 301 
PRO   N   CD   sing N N 302 
PRO   N   H    sing N N 303 
PRO   CA  C    sing N N 304 
PRO   CA  CB   sing N N 305 
PRO   CA  HA   sing N N 306 
PRO   C   O    doub N N 307 
PRO   C   OXT  sing N N 308 
PRO   CB  CG   sing N N 309 
PRO   CB  HB2  sing N N 310 
PRO   CB  HB3  sing N N 311 
PRO   CG  CD   sing N N 312 
PRO   CG  HG2  sing N N 313 
PRO   CG  HG3  sing N N 314 
PRO   CD  HD2  sing N N 315 
PRO   CD  HD3  sing N N 316 
PRO   OXT HXT  sing N N 317 
SER   N   CA   sing N N 318 
SER   N   H    sing N N 319 
SER   N   H2   sing N N 320 
SER   CA  C    sing N N 321 
SER   CA  CB   sing N N 322 
SER   CA  HA   sing N N 323 
SER   C   O    doub N N 324 
SER   C   OXT  sing N N 325 
SER   CB  OG   sing N N 326 
SER   CB  HB2  sing N N 327 
SER   CB  HB3  sing N N 328 
SER   OG  HG   sing N N 329 
SER   OXT HXT  sing N N 330 
THR   N   CA   sing N N 331 
THR   N   H    sing N N 332 
THR   N   H2   sing N N 333 
THR   CA  C    sing N N 334 
THR   CA  CB   sing N N 335 
THR   CA  HA   sing N N 336 
THR   C   O    doub N N 337 
THR   C   OXT  sing N N 338 
THR   CB  OG1  sing N N 339 
THR   CB  CG2  sing N N 340 
THR   CB  HB   sing N N 341 
THR   OG1 HG1  sing N N 342 
THR   CG2 HG21 sing N N 343 
THR   CG2 HG22 sing N N 344 
THR   CG2 HG23 sing N N 345 
THR   OXT HXT  sing N N 346 
TYR   N   CA   sing N N 347 
TYR   N   H    sing N N 348 
TYR   N   H2   sing N N 349 
TYR   CA  C    sing N N 350 
TYR   CA  CB   sing N N 351 
TYR   CA  HA   sing N N 352 
TYR   C   O    doub N N 353 
TYR   C   OXT  sing N N 354 
TYR   CB  CG   sing N N 355 
TYR   CB  HB2  sing N N 356 
TYR   CB  HB3  sing N N 357 
TYR   CG  CD1  doub Y N 358 
TYR   CG  CD2  sing Y N 359 
TYR   CD1 CE1  sing Y N 360 
TYR   CD1 HD1  sing N N 361 
TYR   CD2 CE2  doub Y N 362 
TYR   CD2 HD2  sing N N 363 
TYR   CE1 CZ   doub Y N 364 
TYR   CE1 HE1  sing N N 365 
TYR   CE2 CZ   sing Y N 366 
TYR   CE2 HE2  sing N N 367 
TYR   CZ  OH   sing N N 368 
TYR   OH  HH   sing N N 369 
TYR   OXT HXT  sing N N 370 
VAL   N   CA   sing N N 371 
VAL   N   H    sing N N 372 
VAL   N   H2   sing N N 373 
VAL   CA  C    sing N N 374 
VAL   CA  CB   sing N N 375 
VAL   CA  HA   sing N N 376 
VAL   C   O    doub N N 377 
VAL   C   OXT  sing N N 378 
VAL   CB  CG1  sing N N 379 
VAL   CB  CG2  sing N N 380 
VAL   CB  HB   sing N N 381 
VAL   CG1 HG11 sing N N 382 
VAL   CG1 HG12 sing N N 383 
VAL   CG1 HG13 sing N N 384 
VAL   CG2 HG21 sing N N 385 
VAL   CG2 HG22 sing N N 386 
VAL   CG2 HG23 sing N N 387 
VAL   OXT HXT  sing N N 388 
# 
_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                    7HCS 
_atom_sites.fract_transf_matrix[1][1]   0.011264 
_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]   0.011264 
_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]   0.025354 
_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    A VAL   A 1 3   ? 19.780 -16.276 22.267  0.66 58.89 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.706 -16.240 22.370  0.34 58.13 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.806 -15.204 22.440  0.66 58.51 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.760 -15.147 22.556  0.34 57.81 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.452 -13.852 22.153  0.66 56.81 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.420 -13.814 22.223  0.34 56.39 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.576 -13.589 22.582  0.66 57.34 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.524 -13.528 22.685  0.34 56.86 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.171 -15.246 23.847  0.66 59.42 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.185 -15.140 23.987  0.34 58.54 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.142 -14.135 24.004  0.66 59.67 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.189 -14.000 24.155  0.34 58.75 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.534 -16.605 24.100  0.66 59.68 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.531 -16.476 24.305  0.34 58.75 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 18.093 -15.326 21.799  0.66 70.22 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 18.018 -15.268 21.946  0.34 69.37 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.862 -15.112 24.514  0.66 71.31 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.907 -15.003 24.620  0.34 70.26 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.638 -14.286 24.820  0.66 71.61 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.706 -14.124 24.987  0.34 70.51 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.601 -13.282 24.054  0.66 71.61 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.670 -13.158 24.175  0.34 70.51 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.544 -14.148 23.241  0.66 71.61 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.569 -14.011 23.409  0.34 70.51 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 17.078 -16.586 24.956  0.66 71.62 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 17.114 -16.424 25.179  0.34 70.50 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.899 -16.792 23.391  0.66 71.62 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.861 -16.667 23.630  0.34 70.50 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.228 -17.283 24.110  0.66 71.62 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.210 -17.169 24.303  0.34 70.50 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.739 -13.004 21.414  1.00 54.11 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.193 -11.657 21.088  1.00 48.71 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 18.071 -10.663 21.372  1.00 43.20 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.951 -11.041 21.728  1.00 43.25 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.708 -11.551 19.644  1.00 48.37 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.688 -11.999 18.622  1.00 47.86 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.533 -11.577 18.653  1.00 47.83 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 19.114 -12.861 17.704  1.00 47.70 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.969 -13.196 21.079  0.66 64.93 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.996 -13.219 21.036  0.34 64.93 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.933 -11.435 21.666  1.00 58.46 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 19.936 -10.624 19.457  1.00 58.05 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.495 -12.109 19.547  1.00 58.05 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.576 -13.145 17.096  1.00 57.25 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.931 -13.135 17.716  1.00 57.25 ?  4   ASN   A HD22 1 
ATOM   46   N  N    A SER   A 1 5   ? 18.354 -9.378  21.165  0.66 40.06 ?  5   SER   A N    1 
ATOM   47   N  N    B SER   A 1 5   ? 18.407 -9.380  21.255  0.34 40.35 ?  5   SER   A N    1 
ATOM   48   C  CA   A SER   A 1 5   ? 17.437 -8.309  21.542  0.66 36.70 ?  5   SER   A CA   1 
ATOM   49   C  CA   B SER   A 1 5   ? 17.504 -8.293  21.608  0.34 37.29 ?  5   SER   A CA   1 
ATOM   50   C  C    A SER   A 1 5   ? 16.581 -7.797  20.384  0.66 32.61 ?  5   SER   A C    1 
ATOM   51   C  C    B SER   A 1 5   ? 16.608 -7.864  20.455  0.34 33.56 ?  5   SER   A C    1 
ATOM   52   O  O    A SER   A 1 5   ? 15.958 -6.738  20.517  0.66 32.76 ?  5   SER   A O    1 
ATOM   53   O  O    B SER   A 1 5   ? 15.848 -6.902  20.606  0.34 33.57 ?  5   SER   A O    1 
ATOM   54   C  CB   A SER   A 1 5   ? 18.205 -7.146  22.172  0.66 37.60 ?  5   SER   A CB   1 
ATOM   55   C  CB   B SER   A 1 5   ? 18.299 -7.090  22.131  0.34 38.01 ?  5   SER   A CB   1 
ATOM   56   O  OG   A SER   A 1 5   ? 19.162 -6.621  21.269  0.66 37.97 ?  5   SER   A OG   1 
ATOM   57   O  OG   B SER   A 1 5   ? 19.223 -6.627  21.162  0.34 38.34 ?  5   SER   A OG   1 
ATOM   58   H  H    A SER   A 1 5   ? 19.080 -9.100  20.798  0.66 48.08 ?  5   SER   A H    1 
ATOM   59   H  H    B SER   A 1 5   ? 19.172 -9.111  20.965  0.34 48.43 ?  5   SER   A H    1 
ATOM   60   H  HA   A SER   A 1 5   ? 16.838 -8.654  22.223  0.66 44.04 ?  5   SER   A HA   1 
ATOM   61   H  HA   B SER   A 1 5   ? 16.928 -8.591  22.325  0.34 44.75 ?  5   SER   A HA   1 
ATOM   62   H  HB2  A SER   A 1 5   ? 17.575 -6.444  22.407  0.66 45.13 ?  5   SER   A HB2  1 
ATOM   63   H  HB2  B SER   A 1 5   ? 17.682 -6.372  22.347  0.34 45.62 ?  5   SER   A HB2  1 
ATOM   64   H  HB3  A SER   A 1 5   ? 18.659 -7.461  22.968  0.66 45.13 ?  5   SER   A HB3  1 
ATOM   65   H  HB3  B SER   A 1 5   ? 18.785 -7.356  22.930  0.34 45.62 ?  5   SER   A HB3  1 
ATOM   66   H  HG   A SER   A 1 5   ? 19.575 -5.983  21.628  0.66 45.58 ?  5   SER   A HG   1 
ATOM   67   H  HG   B SER   A 1 5   ? 19.651 -5.970  21.464  0.34 46.02 ?  5   SER   A HG   1 
ATOM   68   N  N    A PHE   A 1 6   ? 16.535 -8.506  19.259  0.66 27.92 ?  6   PHE   A N    1 
ATOM   69   N  N    B PHE   A 1 6   ? 16.677 -8.544  19.313  0.34 29.70 ?  6   PHE   A N    1 
ATOM   70   C  CA   A PHE   A 1 6   ? 15.637 -8.116  18.176  0.66 23.65 ?  6   PHE   A CA   1 
ATOM   71   C  CA   B PHE   A 1 6   ? 15.729 -8.287  18.239  0.34 26.04 ?  6   PHE   A CA   1 
ATOM   72   C  C    A PHE   A 1 6   ? 14.199 -8.476  18.541  0.66 23.60 ?  6   PHE   A C    1 
ATOM   73   C  C    B PHE   A 1 6   ? 14.340 -8.731  18.680  0.34 25.19 ?  6   PHE   A C    1 
ATOM   74   O  O    A PHE   A 1 6   ? 13.928 -9.570  19.040  0.66 24.78 ?  6   PHE   A O    1 
ATOM   75   O  O    B PHE   A 1 6   ? 14.161 -9.855  19.159  0.34 25.92 ?  6   PHE   A O    1 
ATOM   76   C  CB   A PHE   A 1 6   ? 16.034 -8.823  16.880  0.66 20.54 ?  6   PHE   A CB   1 
ATOM   77   C  CB   B PHE   A 1 6   ? 16.136 -9.062  16.987  0.34 23.52 ?  6   PHE   A CB   1 
ATOM   78   C  CG   A PHE   A 1 6   ? 17.296 -8.287  16.255  0.66 18.19 ?  6   PHE   A CG   1 
ATOM   79   C  CG   B PHE   A 1 6   ? 17.425 -8.595  16.366  0.34 21.46 ?  6   PHE   A CG   1 
ATOM   80   C  CD1  A PHE   A 1 6   ? 17.290 -7.083  15.571  0.66 16.98 ?  6   PHE   A CD1  1 
ATOM   81   C  CD1  B PHE   A 1 6   ? 17.463 -7.450  15.588  0.34 20.41 ?  6   PHE   A CD1  1 
ATOM   82   C  CD2  A PHE   A 1 6   ? 18.479 -8.998  16.337  0.66 18.64 ?  6   PHE   A CD2  1 
ATOM   83   C  CD2  B PHE   A 1 6   ? 18.594 -9.317  16.541  0.34 21.04 ?  6   PHE   A CD2  1 
ATOM   84   C  CE1  A PHE   A 1 6   ? 18.449 -6.591  14.990  0.66 16.98 ?  6   PHE   A CE1  1 
ATOM   85   C  CE1  B PHE   A 1 6   ? 18.647 -7.026  15.008  0.34 19.95 ?  6   PHE   A CE1  1 
ATOM   86   C  CE2  A PHE   A 1 6   ? 19.639 -8.517  15.760  0.66 18.50 ?  6   PHE   A CE2  1 
ATOM   87   C  CE2  B PHE   A 1 6   ? 19.780 -8.899  15.964  0.34 20.46 ?  6   PHE   A CE2  1 
ATOM   88   C  CZ   A PHE   A 1 6   ? 19.625 -7.311  15.084  0.66 17.42 ?  6   PHE   A CZ   1 
ATOM   89   C  CZ   B PHE   A 1 6   ? 19.806 -7.751  15.196  0.34 19.94 ?  6   PHE   A CZ   1 
ATOM   90   H  H    A PHE   A 1 6   ? 17.007 -9.208  19.097  0.66 33.51 ?  6   PHE   A H    1 
ATOM   91   H  H    B PHE   A 1 6   ? 17.259 -9.154  19.139  0.34 35.65 ?  6   PHE   A H    1 
ATOM   92   H  HA   A PHE   A 1 6   ? 15.690 -7.162  18.037  0.66 28.38 ?  6   PHE   A HA   1 
ATOM   93   H  HA   B PHE   A 1 6   ? 15.711 -7.339  18.034  0.34 31.26 ?  6   PHE   A HA   1 
ATOM   94   H  HB2  A PHE   A 1 6   ? 16.176 -9.765  17.065  0.66 24.65 ?  6   PHE   A HB2  1 
ATOM   95   H  HB2  B PHE   A 1 6   ? 16.242 -9.997  17.222  0.34 28.23 ?  6   PHE   A HB2  1 
ATOM   96   H  HB3  A PHE   A 1 6   ? 15.318 -8.720  16.234  0.66 24.65 ?  6   PHE   A HB3  1 
ATOM   97   H  HB3  B PHE   A 1 6   ? 15.437 -8.969  16.323  0.34 28.23 ?  6   PHE   A HB3  1 
ATOM   98   H  HD1  A PHE   A 1 6   ? 16.500 -6.592  15.504  0.66 20.38 ?  6   PHE   A HD1  1 
ATOM   99   H  HD1  B PHE   A 1 6   ? 16.686 -6.957  15.459  0.34 24.50 ?  6   PHE   A HD1  1 
ATOM   100  H  HD2  A PHE   A 1 6   ? 18.493 -9.807  16.791  0.66 22.38 ?  6   PHE   A HD2  1 
ATOM   101  H  HD2  B PHE   A 1 6   ? 18.584 -10.091 17.055  0.34 25.26 ?  6   PHE   A HD2  1 
ATOM   102  H  HE1  A PHE   A 1 6   ? 18.434 -5.774  14.535  0.66 20.38 ?  6   PHE   A HE1  1 
ATOM   103  H  HE1  B PHE   A 1 6   ? 18.664 -6.253  14.491  0.34 23.95 ?  6   PHE   A HE1  1 
ATOM   104  H  HE2  A PHE   A 1 6   ? 20.429 -9.000  15.827  0.66 22.20 ?  6   PHE   A HE2  1 
ATOM   105  H  HE2  B PHE   A 1 6   ? 20.560 -9.391  16.091  0.34 24.56 ?  6   PHE   A HE2  1 
ATOM   106  H  HZ   A PHE   A 1 6   ? 20.404 -6.978  14.696  0.66 20.91 ?  6   PHE   A HZ   1 
ATOM   107  H  HZ   B PHE   A 1 6   ? 20.604 -7.469  14.806  0.34 23.94 ?  6   PHE   A HZ   1 
ATOM   108  N  N    A SER   A 1 7   ? 13.268 -7.553  18.284  0.66 22.08 ?  7   SER   A N    1 
ATOM   109  N  N    B SER   A 1 7   ? 13.353 -7.851  18.518  0.34 23.51 ?  7   SER   A N    1 
ATOM   110  C  CA   A SER   A 1 7   ? 11.893 -7.695  18.754  0.66 22.48 ?  7   SER   A CA   1 
ATOM   111  C  CA   B SER   A 1 7   ? 11.987 -8.151  18.924  0.34 22.44 ?  7   SER   A CA   1 
ATOM   112  C  C    A SER   A 1 7   ? 10.891 -7.434  17.634  0.66 20.96 ?  7   SER   A C    1 
ATOM   113  C  C    B SER   A 1 7   ? 11.020 -7.642  17.865  0.34 21.11 ?  7   SER   A C    1 
ATOM   114  O  O    A SER   A 1 7   ? 11.092 -6.552  16.796  0.66 21.07 ?  7   SER   A O    1 
ATOM   115  O  O    B SER   A 1 7   ? 11.311 -6.687  17.142  0.34 21.15 ?  7   SER   A O    1 
ATOM   116  C  CB   A SER   A 1 7   ? 11.630 -6.731  19.917  0.66 24.29 ?  7   SER   A CB   1 
ATOM   117  C  CB   B SER   A 1 7   ? 11.645 -7.525  20.285  0.34 22.90 ?  7   SER   A CB   1 
ATOM   118  O  OG   A SER   A 1 7   ? 10.308 -6.860  20.404  0.66 25.63 ?  7   SER   A OG   1 
ATOM   119  O  OG   B SER   A 1 7   ? 11.446 -6.125  20.171  0.34 23.14 ?  7   SER   A OG   1 
ATOM   120  H  H    A SER   A 1 7   ? 13.410 -6.832  17.837  0.66 26.50 ?  7   SER   A H    1 
ATOM   121  H  H    B SER   A 1 7   ? 13.451 -7.073  18.165  0.34 28.22 ?  7   SER   A H    1 
ATOM   122  H  HA   A SER   A 1 7   ? 11.754 -8.598  19.075  0.66 26.99 ?  7   SER   A HA   1 
ATOM   123  H  HA   B SER   A 1 7   ? 11.876 -9.111  18.996  0.34 26.93 ?  7   SER   A HA   1 
ATOM   124  H  HB2  A SER   A 1 7   ? 12.253 -6.929  20.636  0.66 29.15 ?  7   SER   A HB2  1 
ATOM   125  H  HB2  B SER   A 1 7   ? 10.834 -7.939  20.626  0.34 27.49 ?  7   SER   A HB2  1 
ATOM   126  H  HB3  A SER   A 1 7   ? 11.759 -5.821  19.610  0.66 29.15 ?  7   SER   A HB3  1 
ATOM   127  H  HB3  B SER   A 1 7   ? 12.378 -7.685  20.901  0.34 27.49 ?  7   SER   A HB3  1 
ATOM   128  H  HG   A SER   A 1 7   ? 10.183 -6.334  21.047  0.66 30.76 ?  7   SER   A HG   1 
ATOM   129  H  HG   B SER   A 1 7   ? 11.247 -5.803  20.921  0.34 27.77 ?  7   SER   A HG   1 
ATOM   130  N  N    A GLY   A 1 8   ? 9.806  -8.212  17.625  0.66 19.84 ?  8   GLY   A N    1 
ATOM   131  N  N    B GLY   A 1 8   ? 9.866  -8.300  17.778  0.34 19.93 ?  8   GLY   A N    1 
ATOM   132  C  CA   A GLY   A 1 8   ? 8.714  -7.977  16.699  0.66 19.18 ?  8   GLY   A CA   1 
ATOM   133  C  CA   B GLY   A 1 8   ? 8.852  -7.928  16.814  0.34 18.86 ?  8   GLY   A CA   1 
ATOM   134  C  C    A GLY   A 1 8   ? 8.914  -8.493  15.293  0.66 18.08 ?  8   GLY   A C    1 
ATOM   135  C  C    B GLY   A 1 8   ? 9.039  -8.506  15.431  0.34 17.60 ?  8   GLY   A C    1 
ATOM   136  O  O    A GLY   A 1 8   ? 8.173  -8.090  14.390  0.66 18.97 ?  8   GLY   A O    1 
ATOM   137  O  O    B GLY   A 1 8   ? 8.291  -8.139  14.518  0.34 18.12 ?  8   GLY   A O    1 
ATOM   138  H  H    A GLY   A 1 8   ? 9.684  -8.882  18.149  0.66 23.82 ?  8   GLY   A H    1 
ATOM   139  H  H    B GLY   A 1 8   ? 9.653  -8.972  18.269  0.34 23.93 ?  8   GLY   A H    1 
ATOM   140  H  HA2  A GLY   A 1 8   ? 7.911  -8.390  17.057  0.66 23.02 ?  8   GLY   A HA2  1 
ATOM   141  H  HA2  B GLY   A 1 8   ? 7.987  -8.220  17.140  0.34 22.64 ?  8   GLY   A HA2  1 
ATOM   142  H  HA3  A GLY   A 1 8   ? 8.553  -7.022  16.643  0.66 23.02 ?  8   GLY   A HA3  1 
ATOM   143  H  HA3  B GLY   A 1 8   ? 8.832  -6.960  16.737  0.34 22.64 ?  8   GLY   A HA3  1 
ATOM   144  N  N    A TYR   A 1 9   ? 9.890  -9.370  15.069  0.66 16.98 ?  9   TYR   A N    1 
ATOM   145  N  N    B TYR   A 1 9   ? 10.008 -9.398  15.245  0.34 16.29 ?  9   TYR   A N    1 
ATOM   146  C  CA   A TYR   A 1 9   ? 10.157 -9.904  13.740  0.66 15.53 ?  9   TYR   A CA   1 
ATOM   147  C  CA   B TYR   A 1 9   ? 10.286 -9.961  13.933  0.34 15.00 ?  9   TYR   A CA   1 
ATOM   148  C  C    A TYR   A 1 9   ? 9.315  -11.144 13.467  0.66 14.95 ?  9   TYR   A C    1 
ATOM   149  C  C    B TYR   A 1 9   ? 9.382  -11.149 13.641  0.34 14.43 ?  9   TYR   A C    1 
ATOM   150  O  O    A TYR   A 1 9   ? 9.110  -11.984 14.350  0.66 16.26 ?  9   TYR   A O    1 
ATOM   151  O  O    B TYR   A 1 9   ? 8.901  -11.839 14.546  0.34 15.07 ?  9   TYR   A O    1 
ATOM   152  C  CB   A TYR   A 1 9   ? 11.640 -10.268 13.593  0.66 15.87 ?  9   TYR   A CB   1 
ATOM   153  C  CB   B TYR   A 1 9   ? 11.745 -10.413 13.843  0.34 14.20 ?  9   TYR   A CB   1 
ATOM   154  C  CG   A TYR   A 1 9   ? 12.540 -9.064  13.418  0.66 15.71 ?  9   TYR   A CG   1 
ATOM   155  C  CG   B TYR   A 1 9   ? 12.698 -9.259  13.703  0.34 13.21 ?  9   TYR   A CG   1 
ATOM   156  C  CD1  A TYR   A 1 9   ? 12.842 -8.242  14.494  0.66 16.12 ?  9   TYR   A CD1  1 
ATOM   157  C  CD1  B TYR   A 1 9   ? 13.031 -8.479  14.799  0.34 13.16 ?  9   TYR   A CD1  1 
ATOM   158  C  CD2  A TYR   A 1 9   ? 13.060 -8.737  12.175  0.66 15.38 ?  9   TYR   A CD2  1 
ATOM   159  C  CD2  B TYR   A 1 9   ? 13.239 -8.929  12.472  0.34 13.12 ?  9   TYR   A CD2  1 
ATOM   160  C  CE1  A TYR   A 1 9   ? 13.646 -7.127  14.341  0.66 16.14 ?  9   TYR   A CE1  1 
ATOM   161  C  CE1  B TYR   A 1 9   ? 13.884 -7.409  14.676  0.34 13.44 ?  9   TYR   A CE1  1 
ATOM   162  C  CE2  A TYR   A 1 9   ? 13.868 -7.626  12.011  0.66 15.59 ?  9   TYR   A CE2  1 
ATOM   163  C  CE2  B TYR   A 1 9   ? 14.093 -7.862  12.338  0.34 13.29 ?  9   TYR   A CE2  1 
ATOM   164  C  CZ   A TYR   A 1 9   ? 14.153 -6.826  13.094  0.66 15.99 ?  9   TYR   A CZ   1 
ATOM   165  C  CZ   B TYR   A 1 9   ? 14.416 -7.108  13.442  0.34 13.85 ?  9   TYR   A CZ   1 
ATOM   166  O  OH   A TYR   A 1 9   ? 14.946 -5.720  12.926  0.66 16.44 ?  9   TYR   A OH   1 
ATOM   167  O  OH   B TYR   A 1 9   ? 15.271 -6.045  13.311  0.34 14.81 ?  9   TYR   A OH   1 
ATOM   168  H  H    A TYR   A 1 9   ? 10.411 -9.674  15.678  0.66 20.39 ?  9   TYR   A H    1 
ATOM   169  H  H    B TYR   A 1 9   ? 10.520 -9.694  15.868  0.34 19.56 ?  9   TYR   A H    1 
ATOM   170  H  HA   A TYR   A 1 9   ? 9.939  -9.229  13.076  0.66 18.65 ?  9   TYR   A HA   1 
ATOM   171  H  HA   B TYR   A 1 9   ? 10.139 -9.287  13.252  0.34 18.01 ?  9   TYR   A HA   1 
ATOM   172  H  HB2  A TYR   A 1 9   ? 11.925 -10.749 14.385  0.66 19.05 ?  9   TYR   A HB2  1 
ATOM   173  H  HB2  B TYR   A 1 9   ? 11.982 -10.902 14.646  0.34 17.05 ?  9   TYR   A HB2  1 
ATOM   174  H  HB3  A TYR   A 1 9   ? 11.737 -10.831 12.809  0.66 19.05 ?  9   TYR   A HB3  1 
ATOM   175  H  HB3  B TYR   A 1 9   ? 11.851 -10.981 13.065  0.34 17.05 ?  9   TYR   A HB3  1 
ATOM   176  H  HD1  A TYR   A 1 9   ? 12.489 -8.444  15.334  0.66 19.35 ?  9   TYR   A HD1  1 
ATOM   177  H  HD1  B TYR   A 1 9   ? 12.667 -8.682  15.632  0.34 15.79 ?  9   TYR   A HD1  1 
ATOM   178  H  HD2  A TYR   A 1 9   ? 12.866 -9.272  11.441  0.66 18.46 ?  9   TYR   A HD2  1 
ATOM   179  H  HD2  B TYR   A 1 9   ? 13.026 -9.440  11.726  0.34 15.75 ?  9   TYR   A HD2  1 
ATOM   180  H  HE1  A TYR   A 1 9   ? 13.839 -6.588  15.075  0.66 19.38 ?  9   TYR   A HE1  1 
ATOM   181  H  HE1  B TYR   A 1 9   ? 14.100 -6.896  15.421  0.34 16.13 ?  9   TYR   A HE1  1 
ATOM   182  H  HE2  A TYR   A 1 9   ? 14.219 -7.416  11.175  0.66 18.71 ?  9   TYR   A HE2  1 
ATOM   183  H  HE2  B TYR   A 1 9   ? 14.459 -7.656  11.509  0.34 15.96 ?  9   TYR   A HE2  1 
ATOM   184  H  HH   A TYR   A 1 9   ? 15.056 -5.325  13.661  0.66 19.74 ?  9   TYR   A HH   1 
ATOM   185  H  HH   B TYR   A 1 9   ? 15.370 -5.674  14.056  0.34 17.78 ?  9   TYR   A HH   1 
ATOM   186  N  N    A LEU   A 1 10  ? 8.844  -11.254 12.229  0.66 13.96 ?  10  LEU   A N    1 
ATOM   187  N  N    B LEU   A 1 10  ? 9.166  -11.385 12.352  0.34 13.39 ?  10  LEU   A N    1 
ATOM   188  C  CA   A LEU   A 1 10  ? 8.271  -12.496 11.733  0.66 13.55 ?  10  LEU   A CA   1 
ATOM   189  C  CA   B LEU   A 1 10  ? 8.475  -12.568 11.864  0.34 13.07 ?  10  LEU   A CA   1 
ATOM   190  C  C    A LEU   A 1 10  ? 9.407  -13.422 11.310  0.66 13.17 ?  10  LEU   A C    1 
ATOM   191  C  C    B LEU   A 1 10  ? 9.520  -13.548 11.346  0.34 11.56 ?  10  LEU   A C    1 
ATOM   192  O  O    A LEU   A 1 10  ? 10.405 -12.979 10.731  0.66 13.36 ?  10  LEU   A O    1 
ATOM   193  O  O    B LEU   A 1 10  ? 10.261 -13.232 10.404  0.34 10.96 ?  10  LEU   A O    1 
ATOM   194  C  CB   A LEU   A 1 10  ? 7.379  -12.204 10.526  0.66 14.54 ?  10  LEU   A CB   1 
ATOM   195  C  CB   B LEU   A 1 10  ? 7.508  -12.189 10.746  0.34 14.02 ?  10  LEU   A CB   1 
ATOM   196  C  CG   A LEU   A 1 10  ? 6.684  -13.413 9.902   0.66 16.49 ?  10  LEU   A CG   1 
ATOM   197  C  CG   B LEU   A 1 10  ? 6.723  -13.344 10.126  0.34 15.29 ?  10  LEU   A CG   1 
ATOM   198  C  CD1  A LEU   A 1 10  ? 5.584  -13.914 10.817  0.66 17.66 ?  10  LEU   A CD1  1 
ATOM   199  C  CD1  B LEU   A 1 10  ? 5.753  -13.937 11.135  0.34 15.58 ?  10  LEU   A CD1  1 
ATOM   200  C  CD2  A LEU   A 1 10  ? 6.144  -13.092 8.515   0.66 17.55 ?  10  LEU   A CD2  1 
ATOM   201  C  CD2  B LEU   A 1 10  ? 6.000  -12.888 8.868   0.34 16.46 ?  10  LEU   A CD2  1 
ATOM   202  H  H    A LEU   A 1 10  ? 8.840  -10.611 11.648  0.66 16.75 ?  10  LEU   A H    1 
ATOM   203  H  H    B LEU   A 1 10  ? 9.424  -10.857 11.722  0.34 16.07 ?  10  LEU   A H    1 
ATOM   204  H  HA   A LEU   A 1 10  ? 7.734  -12.919 12.429  0.66 16.27 ?  10  LEU   A HA   1 
ATOM   205  H  HA   B LEU   A 1 10  ? 7.982  -12.986 12.587  0.34 15.69 ?  10  LEU   A HA   1 
ATOM   206  H  HB2  A LEU   A 1 10  ? 6.686  -11.578 10.793  0.66 17.46 ?  10  LEU   A HB2  1 
ATOM   207  H  HB2  B LEU   A 1 10  ? 6.868  -11.555 11.101  0.34 16.83 ?  10  LEU   A HB2  1 
ATOM   208  H  HB3  A LEU   A 1 10  ? 7.928  -11.797 9.836   0.66 17.46 ?  10  LEU   A HB3  1 
ATOM   209  H  HB3  B LEU   A 1 10  ? 8.019  -11.768 10.035  0.34 16.83 ?  10  LEU   A HB3  1 
ATOM   210  H  HG   A LEU   A 1 10  ? 7.331  -14.128 9.804   0.66 19.80 ?  10  LEU   A HG   1 
ATOM   211  H  HG   B LEU   A 1 10  ? 7.345  -14.043 9.871   0.34 18.35 ?  10  LEU   A HG   1 
ATOM   212  H  HD11 A LEU   A 1 10  ? 5.177  -14.701 10.421  0.66 21.20 ?  10  LEU   A HD11 1 
ATOM   213  H  HD11 B LEU   A 1 10  ? 5.223  -14.622 10.697  0.34 18.71 ?  10  LEU   A HD11 1 
ATOM   214  H  HD12 A LEU   A 1 10  ? 5.965  -14.140 11.681  0.66 21.20 ?  10  LEU   A HD12 1 
ATOM   215  H  HD12 B LEU   A 1 10  ? 6.254  -14.326 11.869  0.34 18.71 ?  10  LEU   A HD12 1 
ATOM   216  H  HD13 A LEU   A 1 10  ? 4.918  -13.217 10.924  0.66 21.20 ?  10  LEU   A HD13 1 
ATOM   217  H  HD13 B LEU   A 1 10  ? 5.173  -13.233 11.467  0.34 18.71 ?  10  LEU   A HD13 1 
ATOM   218  H  HD21 A LEU   A 1 10  ? 5.712  -13.883 8.159   0.66 21.07 ?  10  LEU   A HD21 1 
ATOM   219  H  HD21 B LEU   A 1 10  ? 5.512  -13.640 8.499   0.34 19.76 ?  10  LEU   A HD21 1 
ATOM   220  H  HD22 A LEU   A 1 10  ? 5.505  -12.368 8.588   0.66 21.07 ?  10  LEU   A HD22 1 
ATOM   221  H  HD22 B LEU   A 1 10  ? 5.389  -12.173 9.098   0.34 19.76 ?  10  LEU   A HD22 1 
ATOM   222  H  HD23 A LEU   A 1 10  ? 6.882  -12.830 7.945   0.66 21.07 ?  10  LEU   A HD23 1 
ATOM   223  H  HD23 B LEU   A 1 10  ? 6.656  -12.572 8.227   0.34 19.76 ?  10  LEU   A HD23 1 
ATOM   224  N  N    A LYS   A 1 11  ? 9.249  -14.712 11.595  0.66 12.99 ?  11  LYS   A N    1 
ATOM   225  N  N    B LYS   A 1 11  ? 9.593  -14.721 11.973  0.34 11.31 ?  11  LYS   A N    1 
ATOM   226  C  CA   A LYS   A 1 11  ? 10.268 -15.710 11.300  0.66 13.62 ?  11  LYS   A CA   1 
ATOM   227  C  CA   B LYS   A 1 11  ? 10.465 -15.777 11.483  0.34 11.52 ?  11  LYS   A CA   1 
ATOM   228  C  C    A LYS   A 1 11  ? 9.944  -16.354 9.957   0.66 13.68 ?  11  LYS   A C    1 
ATOM   229  C  C    B LYS   A 1 11  ? 9.971  -16.231 10.118  0.34 11.15 ?  11  LYS   A C    1 
ATOM   230  O  O    A LYS   A 1 11  ? 8.914  -17.020 9.825   0.66 15.13 ?  11  LYS   A O    1 
ATOM   231  O  O    B LYS   A 1 11  ? 8.803  -16.601 9.965   0.34 11.73 ?  11  LYS   A O    1 
ATOM   232  C  CB   A LYS   A 1 11  ? 10.285 -16.759 12.413  0.66 13.66 ?  11  LYS   A CB   1 
ATOM   233  C  CB   B LYS   A 1 11  ? 10.460 -16.947 12.468  0.34 11.71 ?  11  LYS   A CB   1 
ATOM   234  C  CG   A LYS   A 1 11  ? 11.294 -17.881 12.226  0.66 13.51 ?  11  LYS   A CG   1 
ATOM   235  C  CG   B LYS   A 1 11  ? 11.531 -18.004 12.222  0.34 12.01 ?  11  LYS   A CG   1 
ATOM   236  C  CD   A LYS   A 1 11  ? 11.428 -18.704 13.506  0.66 13.57 ?  11  LYS   A CD   1 
ATOM   237  C  CD   B LYS   A 1 11  ? 11.572 -18.993 13.381  0.34 12.59 ?  11  LYS   A CD   1 
ATOM   238  C  CE   A LYS   A 1 11  ? 12.381 -19.887 13.334  0.66 14.04 ?  11  LYS   A CE   1 
ATOM   239  C  CE   B LYS   A 1 11  ? 12.699 -20.005 13.242  0.34 12.59 ?  11  LYS   A CE   1 
ATOM   240  N  NZ   A LYS   A 1 11  ? 13.767 -19.472 12.979  0.66 14.31 ?  11  LYS   A NZ   1 
ATOM   241  N  NZ   B LYS   A 1 11  ? 14.038 -19.357 13.255  0.34 12.73 ?  11  LYS   A NZ   1 
ATOM   242  H  H    A LYS   A 1 11  ? 8.536  -15.040 11.958  0.66 15.59 ?  11  LYS   A H    1 
ATOM   243  H  H    B LYS   A 1 11  ? 9.154  -14.923 12.686  0.34 13.58 ?  11  LYS   A H    1 
ATOM   244  H  HA   A LYS   A 1 11  ? 11.139 -15.283 11.250  0.66 16.35 ?  11  LYS   A HA   1 
ATOM   245  H  HA   B LYS   A 1 11  ? 11.372 -15.447 11.397  0.34 13.84 ?  11  LYS   A HA   1 
ATOM   246  H  HB2  A LYS   A 1 11  ? 10.489 -16.312 13.250  0.66 16.40 ?  11  LYS   A HB2  1 
ATOM   247  H  HB2  B LYS   A 1 11  ? 10.595 -16.602 13.363  0.34 14.05 ?  11  LYS   A HB2  1 
ATOM   248  H  HB3  A LYS   A 1 11  ? 9.402  -17.158 12.467  0.66 16.40 ?  11  LYS   A HB3  1 
ATOM   249  H  HB3  B LYS   A 1 11  ? 9.599  -17.391 12.417  0.34 14.05 ?  11  LYS   A HB3  1 
ATOM   250  H  HG2  A LYS   A 1 11  ? 10.994 -18.468 11.515  0.66 16.22 ?  11  LYS   A HG2  1 
ATOM   251  H  HG2  B LYS   A 1 11  ? 11.327 -18.494 11.408  0.34 14.41 ?  11  LYS   A HG2  1 
ATOM   252  H  HG3  A LYS   A 1 11  ? 12.160 -17.504 12.013  0.66 16.22 ?  11  LYS   A HG3  1 
ATOM   253  H  HG3  B LYS   A 1 11  ? 12.400 -17.578 12.151  0.34 14.41 ?  11  LYS   A HG3  1 
ATOM   254  H  HD2  A LYS   A 1 11  ? 11.769 -18.137 14.215  0.66 16.28 ?  11  LYS   A HD2  1 
ATOM   255  H  HD2  B LYS   A 1 11  ? 11.704 -18.507 14.209  0.34 15.11 ?  11  LYS   A HD2  1 
ATOM   256  H  HD3  A LYS   A 1 11  ? 10.554 -19.053 13.753  0.66 16.28 ?  11  LYS   A HD3  1 
ATOM   257  H  HD3  B LYS   A 1 11  ? 10.734 -19.482 13.411  0.34 15.11 ?  11  LYS   A HD3  1 
ATOM   258  H  HE2  A LYS   A 1 11  ? 12.423 -20.382 14.168  0.66 16.85 ?  11  LYS   A HE2  1 
ATOM   259  H  HE2  B LYS   A 1 11  ? 12.660 -20.631 13.984  0.34 15.11 ?  11  LYS   A HE2  1 
ATOM   260  H  HE3  A LYS   A 1 11  ? 12.050 -20.460 12.626  0.66 16.85 ?  11  LYS   A HE3  1 
ATOM   261  H  HE3  B LYS   A 1 11  ? 12.601 -20.478 12.402  0.34 15.11 ?  11  LYS   A HE3  1 
ATOM   262  H  HZ1  A LYS   A 1 11  ? 14.294 -20.191 12.931  0.66 17.18 ?  11  LYS   A HZ1  1 
ATOM   263  H  HZ1  B LYS   A 1 11  ? 14.677 -19.977 13.200  0.34 15.28 ?  11  LYS   A HZ1  1 
ATOM   264  H  HZ2  A LYS   A 1 11  ? 13.768 -19.061 12.191  0.66 17.18 ?  11  LYS   A HZ2  1 
ATOM   265  H  HZ2  B LYS   A 1 11  ? 14.116 -18.803 12.564  0.34 15.28 ?  11  LYS   A HZ2  1 
ATOM   266  H  HZ3  A LYS   A 1 11  ? 14.088 -18.921 13.598  0.66 17.18 ?  11  LYS   A HZ3  1 
ATOM   267  H  HZ3  B LYS   A 1 11  ? 14.148 -18.898 14.009  0.34 15.28 ?  11  LYS   A HZ3  1 
ATOM   268  N  N    A LEU   A 1 12  ? 10.820 -16.169 8.963   0.66 13.10 ?  12  LEU   A N    1 
ATOM   269  N  N    B LEU   A 1 12  ? 10.848 -16.171 9.119   0.34 11.26 ?  12  LEU   A N    1 
ATOM   270  C  CA   A LEU   A 1 12  ? 10.585 -16.789 7.661   0.66 12.91 ?  12  LEU   A CA   1 
ATOM   271  C  CA   B LEU   A 1 12  ? 10.529 -16.657 7.781   0.34 12.00 ?  12  LEU   A CA   1 
ATOM   272  C  C    A LEU   A 1 12  ? 11.189 -18.183 7.561   0.66 12.54 ?  12  LEU   A C    1 
ATOM   273  C  C    B LEU   A 1 12  ? 11.091 -18.044 7.504   0.34 11.81 ?  12  LEU   A C    1 
ATOM   274  O  O    A LEU   A 1 12  ? 10.567 -19.087 6.991   0.66 13.43 ?  12  LEU   A O    1 
ATOM   275  O  O    B LEU   A 1 12  ? 10.430 -18.856 6.849   0.34 11.50 ?  12  LEU   A O    1 
ATOM   276  C  CB   A LEU   A 1 12  ? 11.132 -15.918 6.526   0.66 12.94 ?  12  LEU   A CB   1 
ATOM   277  C  CB   B LEU   A 1 12  ? 11.065 -15.695 6.717   0.34 12.97 ?  12  LEU   A CB   1 
ATOM   278  C  CG   A LEU   A 1 12  ? 10.473 -14.549 6.358   0.66 13.09 ?  12  LEU   A CG   1 
ATOM   279  C  CG   B LEU   A 1 12  ? 10.419 -14.313 6.640   0.34 13.23 ?  12  LEU   A CG   1 
ATOM   280  C  CD1  A LEU   A 1 12  ? 11.221 -13.744 5.312   0.66 14.09 ?  12  LEU   A CD1  1 
ATOM   281  C  CD1  B LEU   A 1 12  ? 10.983 -13.541 5.459   0.34 14.23 ?  12  LEU   A CD1  1 
ATOM   282  C  CD2  A LEU   A 1 12  ? 9.007  -14.691 5.978   0.66 13.60 ?  12  LEU   A CD2  1 
ATOM   283  C  CD2  B LEU   A 1 12  ? 8.917  -14.441 6.525   0.34 13.01 ?  12  LEU   A CD2  1 
ATOM   284  H  H    A LEU   A 1 12  ? 11.548 -15.702 9.012   0.66 15.72 ?  12  LEU   A H    1 
ATOM   285  H  H    B LEU   A 1 12  ? 11.637 -15.835 9.194   0.34 13.52 ?  12  LEU   A H    1 
ATOM   286  H  HA   A LEU   A 1 12  ? 9.631  -16.878 7.528   0.66 15.50 ?  12  LEU   A HA   1 
ATOM   287  H  HA   B LEU   A 1 12  ? 9.563  -16.698 7.693   0.34 14.40 ?  12  LEU   A HA   1 
ATOM   288  H  HB2  A LEU   A 1 12  ? 12.075 -15.763 6.679   0.66 15.53 ?  12  LEU   A HB2  1 
ATOM   289  H  HB2  B LEU   A 1 12  ? 12.010 -15.559 6.880   0.34 15.58 ?  12  LEU   A HB2  1 
ATOM   290  H  HB3  A LEU   A 1 12  ? 11.016 -16.395 5.687   0.66 15.53 ?  12  LEU   A HB3  1 
ATOM   291  H  HB3  B LEU   A 1 12  ? 10.944 -16.113 5.851   0.34 15.58 ?  12  LEU   A HB3  1 
ATOM   292  H  HG   A LEU   A 1 12  ? 10.519 -14.068 7.197   0.66 15.72 ?  12  LEU   A HG   1 
ATOM   293  H  HG   B LEU   A 1 12  ? 10.622 -13.816 7.449   0.34 15.88 ?  12  LEU   A HG   1 
ATOM   294  H  HD11 A LEU   A 1 12  ? 10.793 -12.878 5.212   0.66 16.92 ?  12  LEU   A HD11 1 
ATOM   295  H  HD11 B LEU   A 1 12  ? 10.569 -12.664 5.426   0.34 17.08 ?  12  LEU   A HD11 1 
ATOM   296  H  HD12 A LEU   A 1 12  ? 12.139 -13.627 5.602   0.66 16.92 ?  12  LEU   A HD12 1 
ATOM   297  H  HD12 B LEU   A 1 12  ? 11.942 -13.450 5.569   0.34 17.08 ?  12  LEU   A HD12 1 
ATOM   298  H  HD13 A LEU   A 1 12  ? 11.198 -14.222 4.468   0.66 16.92 ?  12  LEU   A HD13 1 
ATOM   299  H  HD13 B LEU   A 1 12  ? 10.789 -14.029 4.643   0.34 17.08 ?  12  LEU   A HD13 1 
ATOM   300  H  HD21 A LEU   A 1 12  ? 8.647  -13.817 5.763   0.66 16.33 ?  12  LEU   A HD21 1 
ATOM   301  H  HD21 B LEU   A 1 12  ? 8.546  -13.588 6.254   0.34 15.61 ?  12  LEU   A HD21 1 
ATOM   302  H  HD22 A LEU   A 1 12  ? 8.935  -15.277 5.206   0.66 16.33 ?  12  LEU   A HD22 1 
ATOM   303  H  HD22 B LEU   A 1 12  ? 8.711  -15.119 5.862   0.34 15.61 ?  12  LEU   A HD22 1 
ATOM   304  H  HD23 A LEU   A 1 12  ? 8.521  -15.075 6.726   0.66 16.33 ?  12  LEU   A HD23 1 
ATOM   305  H  HD23 B LEU   A 1 12  ? 8.556  -14.702 7.387   0.34 15.61 ?  12  LEU   A HD23 1 
ATOM   306  N  N    A THR   A 1 13  ? 12.403 -18.362 8.078   0.66 12.15 ?  13  THR   A N    1 
ATOM   307  N  N    B THR   A 1 13  ? 12.312 -18.314 7.959   0.34 12.41 ?  13  THR   A N    1 
ATOM   308  C  CA   A THR   A 1 13  ? 13.107 -19.636 8.020   0.66 12.05 ?  13  THR   A CA   1 
ATOM   309  C  CA   B THR   A 1 13  ? 12.966 -19.603 7.774   0.34 12.75 ?  13  THR   A CA   1 
ATOM   310  C  C    A THR   A 1 13  ? 13.861 -19.825 9.329   0.66 11.95 ?  13  THR   A C    1 
ATOM   311  C  C    B THR   A 1 13  ? 13.798 -19.890 9.019   0.34 12.81 ?  13  THR   A C    1 
ATOM   312  O  O    A THR   A 1 13  ? 13.749 -19.027 10.264  0.66 12.40 ?  13  THR   A O    1 
ATOM   313  O  O    B THR   A 1 13  ? 13.725 -19.170 10.020  0.34 12.97 ?  13  THR   A O    1 
ATOM   314  C  CB   A THR   A 1 13  ? 14.098 -19.694 6.850   0.66 12.85 ?  13  THR   A CB   1 
ATOM   315  C  CB   B THR   A 1 13  ? 13.863 -19.589 6.530   0.34 12.74 ?  13  THR   A CB   1 
ATOM   316  O  OG1  A THR   A 1 13  ? 15.170 -18.787 7.109   0.66 11.97 ?  13  THR   A OG1  1 
ATOM   317  O  OG1  B THR   A 1 13  ? 14.913 -18.636 6.726   0.34 13.00 ?  13  THR   A OG1  1 
ATOM   318  C  CG2  A THR   A 1 13  ? 13.447 -19.362 5.511   0.66 13.55 ?  13  THR   A CG2  1 
ATOM   319  C  CG2  B THR   A 1 13  ? 13.078 -19.233 5.274   0.34 13.34 ?  13  THR   A CG2  1 
ATOM   320  H  H    A THR   A 1 13  ? 12.845 -17.745 8.475   0.66 14.59 ?  13  THR   A H    1 
ATOM   321  H  H    B THR   A 1 13  ? 12.794 -17.744 8.381   0.34 14.90 ?  13  THR   A H    1 
ATOM   322  H  HA   A THR   A 1 13  ? 12.470 -20.360 7.921   0.66 14.47 ?  13  THR   A HA   1 
ATOM   323  H  HA   B THR   A 1 13  ? 12.295 -20.301 7.668   0.34 15.30 ?  13  THR   A HA   1 
ATOM   324  H  HB   A THR   A 1 13  ? 14.461 -20.591 6.788   0.66 15.43 ?  13  THR   A HB   1 
ATOM   325  H  HB   B THR   A 1 13  ? 14.252 -20.467 6.407   0.34 15.29 ?  13  THR   A HB   1 
ATOM   326  H  HG1  A THR   A 1 13  ? 15.835 -19.202 7.418   0.66 14.38 ?  13  THR   A HG1  1 
ATOM   327  H  HG1  B THR   A 1 13  ? 15.409 -18.614 6.052   0.34 15.60 ?  13  THR   A HG1  1 
ATOM   328  H  HG21 A THR   A 1 13  ? 14.093 -19.476 4.791   0.66 16.26 ?  13  THR   A HG21 1 
ATOM   329  H  HG21 B THR   A 1 13  ? 13.637 -19.365 4.490   0.34 16.02 ?  13  THR   A HG21 1 
ATOM   330  H  HG22 A THR   A 1 13  ? 12.698 -19.957 5.352   0.66 16.26 ?  13  THR   A HG22 1 
ATOM   331  H  HG22 B THR   A 1 13  ? 12.296 -19.801 5.199   0.34 16.02 ?  13  THR   A HG22 1 
ATOM   332  H  HG23 A THR   A 1 13  ? 13.134 -18.447 5.508   0.66 16.26 ?  13  THR   A HG23 1 
ATOM   333  H  HG23 B THR   A 1 13  ? 12.796 -18.307 5.307   0.34 16.02 ?  13  THR   A HG23 1 
ATOM   334  N  N    A ASP   A 1 14  ? 14.655 -20.894 9.378   0.66 12.64 ?  14  ASP   A N    1 
ATOM   335  N  N    B ASP   A 1 14  ? 14.619 -20.942 8.948   0.34 12.92 ?  14  ASP   A N    1 
ATOM   336  C  CA   A ASP   A 1 14  ? 15.500 -21.142 10.535  0.66 12.99 ?  14  ASP   A CA   1 
ATOM   337  C  CA   B ASP   A 1 14  ? 15.480 -21.284 10.075  0.34 13.02 ?  14  ASP   A CA   1 
ATOM   338  C  C    A ASP   A 1 14  ? 16.307 -19.904 10.930  0.66 12.36 ?  14  ASP   A C    1 
ATOM   339  C  C    B ASP   A 1 14  ? 16.373 -20.116 10.488  0.34 11.75 ?  14  ASP   A C    1 
ATOM   340  O  O    A ASP   A 1 14  ? 16.498 -19.635 12.122  0.66 13.42 ?  14  ASP   A O    1 
ATOM   341  O  O    B ASP   A 1 14  ? 16.693 -19.974 11.673  0.34 12.02 ?  14  ASP   A O    1 
ATOM   342  C  CB   A ASP   A 1 14  ? 16.446 -22.296 10.229  0.66 15.21 ?  14  ASP   A CB   1 
ATOM   343  C  CB   B ASP   A 1 14  ? 16.337 -22.502 9.725   0.34 14.80 ?  14  ASP   A CB   1 
ATOM   344  C  CG   A ASP   A 1 14  ? 17.352 -22.597 11.388  0.66 19.35 ?  14  ASP   A CG   1 
ATOM   345  C  CG   B ASP   A 1 14  ? 17.222 -22.942 10.878  0.34 16.98 ?  14  ASP   A CG   1 
ATOM   346  O  OD1  A ASP   A 1 14  ? 16.823 -22.996 12.448  0.66 20.95 ?  14  ASP   A OD1  1 
ATOM   347  O  OD1  B ASP   A 1 14  ? 16.678 -23.441 11.889  0.34 17.79 ?  14  ASP   A OD1  1 
ATOM   348  O  OD2  A ASP   A 1 14  ? 18.576 -22.400 11.248  0.66 22.02 -1 14  ASP   A OD2  1 
ATOM   349  O  OD2  B ASP   A 1 14  ? 18.456 -22.795 10.772  0.34 18.31 -1 14  ASP   A OD2  1 
ATOM   350  H  H    A ASP   A 1 14  ? 14.727 -21.473 8.756   0.66 15.18 ?  14  ASP   A H    1 
ATOM   351  H  H    B ASP   A 1 14  ? 14.696 -21.464 8.267   0.34 15.51 ?  14  ASP   A H    1 
ATOM   352  H  HA   A ASP   A 1 14  ? 14.945 -21.394 11.289  0.66 15.59 ?  14  ASP   A HA   1 
ATOM   353  H  HA   B ASP   A 1 14  ? 14.929 -21.525 10.837  0.34 15.62 ?  14  ASP   A HA   1 
ATOM   354  H  HB2  A ASP   A 1 14  ? 15.912 -23.084 10.007  0.66 18.26 ?  14  ASP   A HB2  1 
ATOM   355  H  HB2  B ASP   A 1 14  ? 15.756 -23.251 9.502   0.34 17.77 ?  14  ASP   A HB2  1 
ATOM   356  H  HB3  A ASP   A 1 14  ? 17.000 -22.058 9.467   0.66 18.26 ?  14  ASP   A HB3  1 
ATOM   357  H  HB3  B ASP   A 1 14  ? 16.900 -22.288 8.962   0.34 17.77 ?  14  ASP   A HB3  1 
ATOM   358  N  N    A ASN   A 1 15  ? 16.791 -19.137 9.946   0.66 12.29 ?  15  ASN   A N    1 
ATOM   359  N  N    B ASN   A 1 15  ? 16.785 -19.267 9.538   0.34 10.58 ?  15  ASN   A N    1 
ATOM   360  C  CA   A ASN   A 1 15  ? 17.763 -18.079 10.209  0.66 12.84 ?  15  ASN   A CA   1 
ATOM   361  C  CA   B ASN   A 1 15  ? 17.783 -18.239 9.822   0.34 10.70 ?  15  ASN   A CA   1 
ATOM   362  C  C    A ASN   A 1 15  ? 17.376 -16.698 9.697   0.66 12.64 ?  15  ASN   A C    1 
ATOM   363  C  C    B ASN   A 1 15  ? 17.429 -16.843 9.319   0.34 11.21 ?  15  ASN   A C    1 
ATOM   364  O  O    A ASN   A 1 15  ? 18.103 -15.741 9.989   0.66 12.98 ?  15  ASN   A O    1 
ATOM   365  O  O    B ASN   A 1 15  ? 18.261 -15.935 9.441   0.34 11.45 ?  15  ASN   A O    1 
ATOM   366  C  CB   A ASN   A 1 15  ? 19.139 -18.450 9.626   0.66 12.69 ?  15  ASN   A CB   1 
ATOM   367  C  CB   B ASN   A 1 15  ? 19.152 -18.650 9.258   0.34 10.31 ?  15  ASN   A CB   1 
ATOM   368  C  CG   A ASN   A 1 15  ? 19.118 -18.587 8.115   0.66 12.88 ?  15  ASN   A CG   1 
ATOM   369  C  CG   B ASN   A 1 15  ? 19.160 -18.696 7.743   0.34 10.96 ?  15  ASN   A CG   1 
ATOM   370  O  OD1  A ASN   A 1 15  ? 18.335 -19.367 7.564   0.66 12.84 ?  15  ASN   A OD1  1 
ATOM   371  O  OD1  B ASN   A 1 15  ? 18.547 -19.575 7.134   0.34 10.89 ?  15  ASN   A OD1  1 
ATOM   372  N  ND2  A ASN   A 1 15  ? 19.959 -17.807 7.433   0.66 13.62 ?  15  ASN   A ND2  1 
ATOM   373  N  ND2  B ASN   A 1 15  ? 19.849 -17.742 7.124   0.34 11.54 ?  15  ASN   A ND2  1 
ATOM   374  H  H    A ASN   A 1 15  ? 16.565 -19.201 9.126   0.66 14.75 ?  15  ASN   A H    1 
ATOM   375  H  H    B ASN   A 1 15  ? 16.498 -19.277 8.728   0.34 12.70 ?  15  ASN   A H    1 
ATOM   376  H  HA   A ASN   A 1 15  ? 17.880 -18.000 11.170  0.66 15.42 ?  15  ASN   A HA   1 
ATOM   377  H  HA   B ASN   A 1 15  ? 17.884 -18.179 10.782  0.34 12.84 ?  15  ASN   A HA   1 
ATOM   378  H  HB2  A ASN   A 1 15  ? 19.779 -17.751 9.856   0.66 15.24 ?  15  ASN   A HB2  1 
ATOM   379  H  HB2  B ASN   A 1 15  ? 19.820 -18.003 9.545   0.34 12.38 ?  15  ASN   A HB2  1 
ATOM   380  H  HB3  A ASN   A 1 15  ? 19.425 -19.293 10.003  0.66 15.24 ?  15  ASN   A HB3  1 
ATOM   381  H  HB3  B ASN   A 1 15  ? 19.390 -19.533 9.595   0.34 12.38 ?  15  ASN   A HB3  1 
ATOM   382  H  HD21 A ASN   A 1 15  ? 19.983 -17.848 6.571   0.66 16.35 ?  15  ASN   A HD21 1 
ATOM   383  H  HD21 B ASN   A 1 15  ? 19.881 -17.731 6.267   0.34 13.86 ?  15  ASN   A HD21 1 
ATOM   384  H  HD22 A ASN   A 1 15  ? 20.485 -17.270 7.849   0.66 16.35 ?  15  ASN   A HD22 1 
ATOM   385  H  HD22 B ASN   A 1 15  ? 20.258 -17.141 7.581   0.34 13.86 ?  15  ASN   A HD22 1 
ATOM   386  N  N    A VAL   A 1 16  ? 16.281 -16.552 8.951   0.66 12.87 ?  16  VAL   A N    1 
ATOM   387  N  N    B VAL   A 1 16  ? 16.235 -16.635 8.768   0.34 11.52 ?  16  VAL   A N    1 
ATOM   388  C  CA   A VAL   A 1 16  ? 15.881 -15.273 8.368   0.66 12.52 ?  16  VAL   A CA   1 
ATOM   389  C  CA   B VAL   A 1 16  ? 15.837 -15.344 8.213   0.34 11.75 ?  16  VAL   A CA   1 
ATOM   390  C  C    A VAL   A 1 16  ? 14.593 -14.790 9.022   0.66 12.54 ?  16  VAL   A C    1 
ATOM   391  C  C    B VAL   A 1 16  ? 14.620 -14.829 8.973   0.34 11.96 ?  16  VAL   A C    1 
ATOM   392  O  O    A VAL   A 1 16  ? 13.589 -15.516 9.068   0.66 12.93 ?  16  VAL   A O    1 
ATOM   393  O  O    B VAL   A 1 16  ? 13.633 -15.555 9.149   0.34 12.40 ?  16  VAL   A O    1 
ATOM   394  C  CB   A VAL   A 1 16  ? 15.727 -15.348 6.840   0.66 12.71 ?  16  VAL   A CB   1 
ATOM   395  C  CB   B VAL   A 1 16  ? 15.547 -15.441 6.704   0.34 12.18 ?  16  VAL   A CB   1 
ATOM   396  C  CG1  A VAL   A 1 16  ? 15.289 -13.991 6.279   0.66 13.66 ?  16  VAL   A CG1  1 
ATOM   397  C  CG1  B VAL   A 1 16  ? 15.103 -14.091 6.155   0.34 12.87 ?  16  VAL   A CG1  1 
ATOM   398  C  CG2  A VAL   A 1 16  ? 17.031 -15.778 6.190   0.66 13.84 ?  16  VAL   A CG2  1 
ATOM   399  C  CG2  B VAL   A 1 16  ? 16.775 -15.949 5.950   0.34 12.49 ?  16  VAL   A CG2  1 
ATOM   400  H  H    A VAL   A 1 16  ? 15.747 -17.196 8.772   0.66 15.45 ?  16  VAL   A H    1 
ATOM   401  H  H    B VAL   A 1 16  ? 15.632 -17.244 8.701   0.34 13.83 ?  16  VAL   A H    1 
ATOM   402  H  HA   A VAL   A 1 16  ? 16.572 -14.615 8.555   0.66 15.04 ?  16  VAL   A HA   1 
ATOM   403  H  HA   B VAL   A 1 16  ? 16.566 -14.714 8.339   0.34 14.10 ?  16  VAL   A HA   1 
ATOM   404  H  HB   A VAL   A 1 16  ? 15.051 -16.006 6.620   0.66 15.26 ?  16  VAL   A HB   1 
ATOM   405  H  HB   B VAL   A 1 16  ? 14.829 -16.075 6.565   0.34 14.62 ?  16  VAL   A HB   1 
ATOM   406  H  HG11 A VAL   A 1 16  ? 15.396 -14.002 5.315   0.66 16.40 ?  16  VAL   A HG11 1 
ATOM   407  H  HG11 B VAL   A 1 16  ? 15.091 -14.139 5.187   0.34 15.45 ?  16  VAL   A HG11 1 
ATOM   408  H  HG12 A VAL   A 1 16  ? 14.358 -13.844 6.505   0.66 16.40 ?  16  VAL   A HG12 1 
ATOM   409  H  HG12 B VAL   A 1 16  ? 14.215 -13.892 6.488   0.34 15.45 ?  16  VAL   A HG12 1 
ATOM   410  H  HG13 A VAL   A 1 16  ? 15.842 -13.297 6.666   0.66 16.40 ?  16  VAL   A HG13 1 
ATOM   411  H  HG13 B VAL   A 1 16  ? 15.730 -13.412 6.446   0.34 15.45 ?  16  VAL   A HG13 1 
ATOM   412  H  HG21 A VAL   A 1 16  ? 16.956 -15.666 5.229   0.66 16.62 ?  16  VAL   A HG21 1 
ATOM   413  H  HG21 B VAL   A 1 16  ? 16.613 -15.873 4.997   0.34 14.99 ?  16  VAL   A HG21 1 
ATOM   414  H  HG22 A VAL   A 1 16  ? 17.750 -15.228 6.532   0.66 16.62 ?  16  VAL   A HG22 1 
ATOM   415  H  HG22 B VAL   A 1 16  ? 17.545 -15.410 6.196   0.34 14.99 ?  16  VAL   A HG22 1 
ATOM   416  H  HG23 A VAL   A 1 16  ? 17.197 -16.708 6.404   0.66 16.62 ?  16  VAL   A HG23 1 
ATOM   417  H  HG23 B VAL   A 1 16  ? 16.934 -16.876 6.186   0.34 14.99 ?  16  VAL   A HG23 1 
ATOM   418  N  N    A TYR   A 1 17  ? 14.621 -13.532 9.460   0.66 12.29 ?  17  TYR   A N    1 
ATOM   419  N  N    B TYR   A 1 17  ? 14.690 -13.563 9.390   0.34 11.64 ?  17  TYR   A N    1 
ATOM   420  C  CA   A TYR   A 1 17  ? 13.544 -12.858 10.164  0.66 12.43 ?  17  TYR   A CA   1 
ATOM   421  C  CA   B TYR   A 1 17  ? 13.633 -12.873 10.113  0.34 11.54 ?  17  TYR   A CA   1 
ATOM   422  C  C    A TYR   A 1 17  ? 13.284 -11.522 9.477   0.66 12.68 ?  17  TYR   A C    1 
ATOM   423  C  C    B TYR   A 1 17  ? 13.351 -11.556 9.404   0.34 11.66 ?  17  TYR   A C    1 
ATOM   424  O  O    A TYR   A 1 17  ? 14.207 -10.931 8.912   0.66 13.00 ?  17  TYR   A O    1 
ATOM   425  O  O    B TYR   A 1 17  ? 14.212 -11.019 8.704   0.34 11.77 ?  17  TYR   A O    1 
ATOM   426  C  CB   A TYR   A 1 17  ? 13.988 -12.610 11.606  0.66 13.17 ?  17  TYR   A CB   1 
ATOM   427  C  CB   B TYR   A 1 17  ? 14.058 -12.585 11.559  0.34 11.99 ?  17  TYR   A CB   1 
ATOM   428  C  CG   A TYR   A 1 17  ? 14.236 -13.885 12.396  0.66 13.52 ?  17  TYR   A CG   1 
ATOM   429  C  CG   B TYR   A 1 17  ? 14.079 -13.811 12.434  0.34 12.38 ?  17  TYR   A CG   1 
ATOM   430  C  CD1  A TYR   A 1 17  ? 15.431 -14.598 12.287  0.66 14.17 ?  17  TYR   A CD1  1 
ATOM   431  C  CD1  B TYR   A 1 17  ? 15.155 -14.689 12.410  0.34 12.95 ?  17  TYR   A CD1  1 
ATOM   432  C  CD2  A TYR   A 1 17  ? 13.262 -14.386 13.249  0.66 13.78 ?  17  TYR   A CD2  1 
ATOM   433  C  CD2  B TYR   A 1 17  ? 13.016 -14.099 13.279  0.34 12.62 ?  17  TYR   A CD2  1 
ATOM   434  C  CE1  A TYR   A 1 17  ? 15.637 -15.778 13.011  0.66 14.29 ?  17  TYR   A CE1  1 
ATOM   435  C  CE1  B TYR   A 1 17  ? 15.172 -15.822 13.204  0.34 13.02 ?  17  TYR   A CE1  1 
ATOM   436  C  CE2  A TYR   A 1 17  ? 13.459 -15.554 13.973  0.66 14.04 ?  17  TYR   A CE2  1 
ATOM   437  C  CE2  B TYR   A 1 17  ? 13.021 -15.231 14.075  0.34 12.85 ?  17  TYR   A CE2  1 
ATOM   438  C  CZ   A TYR   A 1 17  ? 14.641 -16.247 13.850  0.66 13.71 ?  17  TYR   A CZ   1 
ATOM   439  C  CZ   B TYR   A 1 17  ? 14.103 -16.087 14.037  0.34 12.97 ?  17  TYR   A CZ   1 
ATOM   440  O  OH   A TYR   A 1 17  ? 14.824 -17.403 14.578  0.66 14.00 ?  17  TYR   A OH   1 
ATOM   441  O  OH   B TYR   A 1 17  ? 14.108 -17.210 14.831  0.34 13.36 ?  17  TYR   A OH   1 
ATOM   442  H  H    A TYR   A 1 17  ? 15.306 -13.019 9.343   0.66 14.75 ?  17  TYR   A H    1 
ATOM   443  H  H    B TYR   A 1 17  ? 15.372 -13.057 9.244   0.34 13.97 ?  17  TYR   A H    1 
ATOM   444  H  HA   A TYR   A 1 17  ? 12.740 -13.403 10.142  0.66 14.93 ?  17  TYR   A HA   1 
ATOM   445  H  HA   B TYR   A 1 17  ? 12.820 -13.403 10.121  0.34 13.85 ?  17  TYR   A HA   1 
ATOM   446  H  HB2  A TYR   A 1 17  ? 14.813 -12.099 11.588  0.66 15.81 ?  17  TYR   A HB2  1 
ATOM   447  H  HB2  B TYR   A 1 17  ? 14.952 -12.214 11.556  0.34 14.39 ?  17  TYR   A HB2  1 
ATOM   448  H  HB3  A TYR   A 1 17  ? 13.297 -12.106 12.055  0.66 15.81 ?  17  TYR   A HB3  1 
ATOM   449  H  HB3  B TYR   A 1 17  ? 13.439 -11.954 11.951  0.34 14.39 ?  17  TYR   A HB3  1 
ATOM   450  H  HD1  A TYR   A 1 17  ? 16.101 -14.296 11.719  0.66 17.01 ?  17  TYR   A HD1  1 
ATOM   451  H  HD1  B TYR   A 1 17  ? 15.874 -14.515 11.847  0.34 15.54 ?  17  TYR   A HD1  1 
ATOM   452  H  HD2  A TYR   A 1 17  ? 12.457 -13.934 13.338  0.66 16.55 ?  17  TYR   A HD2  1 
ATOM   453  H  HD2  B TYR   A 1 17  ? 12.285 -13.523 13.310  0.34 15.15 ?  17  TYR   A HD2  1 
ATOM   454  H  HE1  A TYR   A 1 17  ? 16.440 -16.251 12.933  0.66 17.15 ?  17  TYR   A HE1  1 
ATOM   455  H  HE1  B TYR   A 1 17  ? 15.900 -16.403 13.177  0.34 15.63 ?  17  TYR   A HE1  1 
ATOM   456  H  HE2  A TYR   A 1 17  ? 12.793 -15.873 14.543  0.66 16.85 ?  17  TYR   A HE2  1 
ATOM   457  H  HE2  B TYR   A 1 17  ? 12.305 -15.407 14.640  0.34 15.43 ?  17  TYR   A HE2  1 
ATOM   458  H  HH   A TYR   A 1 17  ? 15.583 -17.733 14.426  0.66 16.80 ?  17  TYR   A HH   1 
ATOM   459  H  HH   B TYR   A 1 17  ? 13.328 -17.372 15.097  0.34 16.04 ?  17  TYR   A HH   1 
ATOM   460  N  N    A ILE   A 1 18  ? 12.039 -11.024 9.524   0.66 12.49 ?  18  ILE   A N    1 
ATOM   461  N  N    B ILE   A 1 18  ? 12.138 -11.029 9.579   0.34 11.59 ?  18  ILE   A N    1 
ATOM   462  C  CA   A ILE   A 1 18  ? 11.655 -9.836  8.757   0.66 12.87 ?  18  ILE   A CA   1 
ATOM   463  C  CA   B ILE   A 1 18  ? 11.754 -9.779  8.927   0.34 11.50 ?  18  ILE   A CA   1 
ATOM   464  C  C    A ILE   A 1 18  ? 10.683 -8.963  9.545   0.66 13.21 ?  18  ILE   A C    1 
ATOM   465  C  C    B ILE   A 1 18  ? 10.853 -8.960  9.843   0.34 11.59 ?  18  ILE   A C    1 
ATOM   466  O  O    A ILE   A 1 18  ? 9.843  -9.458  10.302  0.66 13.70 ?  18  ILE   A O    1 
ATOM   467  O  O    B ILE   A 1 18  ? 10.002 -9.507  10.554  0.34 12.19 ?  18  ILE   A O    1 
ATOM   468  C  CB   A ILE   A 1 18  ? 11.099 -10.229 7.365   0.66 12.82 ?  18  ILE   A CB   1 
ATOM   469  C  CB   B ILE   A 1 18  ? 11.103 -10.057 7.556   0.34 11.31 ?  18  ILE   A CB   1 
ATOM   470  C  CG1  A ILE   A 1 18  ? 11.048 -9.025  6.425   0.66 12.76 ?  18  ILE   A CG1  1 
ATOM   471  C  CG1  B ILE   A 1 18  ? 10.952 -8.768  6.751   0.34 12.12 ?  18  ILE   A CG1  1 
ATOM   472  C  CG2  A ILE   A 1 18  ? 9.739  -10.934 7.483   0.66 13.32 ?  18  ILE   A CG2  1 
ATOM   473  C  CG2  B ILE   A 1 18  ? 9.774  -10.793 7.718   0.34 11.56 ?  18  ILE   A CG2  1 
ATOM   474  C  CD1  A ILE   A 1 18  ? 10.818 -9.413  4.983   0.66 14.84 ?  18  ILE   A CD1  1 
ATOM   475  C  CD1  B ILE   A 1 18  ? 10.637 -9.017  5.297   0.34 13.51 ?  18  ILE   A CD1  1 
ATOM   476  H  H    A ILE   A 1 18  ? 11.403 -11.360 9.997   0.66 14.99 ?  18  ILE   A H    1 
ATOM   477  H  H    B ILE   A 1 18  ? 11.512 -11.391 10.051  0.34 13.92 ?  18  ILE   A H    1 
ATOM   478  H  HA   A ILE   A 1 18  ? 12.453 -9.314  8.598   0.66 15.45 ?  18  ILE   A HA   1 
ATOM   479  H  HA   B ILE   A 1 18  ? 12.559 -9.262  8.768   0.34 13.81 ?  18  ILE   A HA   1 
ATOM   480  H  HB   A ILE   A 1 18  ? 11.713 -10.867 6.974   0.66 15.39 ?  18  ILE   A HB   1 
ATOM   481  H  HB   B ILE   A 1 18  ? 11.700 -10.636 7.064   0.34 13.58 ?  18  ILE   A HB   1 
ATOM   482  H  HG12 A ILE   A 1 18  ? 10.327 -8.438  6.692   0.66 15.32 ?  18  ILE   A HG12 1 
ATOM   483  H  HG12 B ILE   A 1 18  ? 10.237 -8.233  7.127   0.34 14.55 ?  18  ILE   A HG12 1 
ATOM   484  H  HG13 A ILE   A 1 18  ? 11.895 -8.554  6.468   0.66 15.32 ?  18  ILE   A HG13 1 
ATOM   485  H  HG13 B ILE   A 1 18  ? 11.782 -8.273  6.792   0.34 14.55 ?  18  ILE   A HG13 1 
ATOM   486  H  HG21 A ILE   A 1 18  ? 9.494  -11.300 6.615   0.66 15.99 ?  18  ILE   A HG21 1 
ATOM   487  H  HG21 B ILE   A 1 18  ? 9.461  -11.071 6.841   0.34 13.88 ?  18  ILE   A HG21 1 
ATOM   488  H  HG22 A ILE   A 1 18  ? 9.811  -11.651 8.131   0.66 15.99 ?  18  ILE   A HG22 1 
ATOM   489  H  HG22 B ILE   A 1 18  ? 9.911  -11.572 8.279   0.34 13.88 ?  18  ILE   A HG22 1 
ATOM   490  H  HG23 A ILE   A 1 18  ? 9.069  -10.295 7.769   0.66 15.99 ?  18  ILE   A HG23 1 
ATOM   491  H  HG23 B ILE   A 1 18  ? 9.127  -10.199 8.126   0.34 13.88 ?  18  ILE   A HG23 1 
ATOM   492  H  HD11 A ILE   A 1 18  ? 10.862 -8.615  4.431   0.66 17.81 ?  18  ILE   A HD11 1 
ATOM   493  H  HD11 B ILE   A 1 18  ? 10.614 -8.169  4.827   0.34 16.21 ?  18  ILE   A HD11 1 
ATOM   494  H  HD12 A ILE   A 1 18  ? 11.501 -10.042 4.711   0.66 17.81 ?  18  ILE   A HD12 1 
ATOM   495  H  HD12 B ILE   A 1 18  ? 11.330 -9.584  4.919   0.34 16.21 ?  18  ILE   A HD12 1 
ATOM   496  H  HD13 A ILE   A 1 18  ? 9.940  -9.819  4.903   0.66 17.81 ?  18  ILE   A HD13 1 
ATOM   497  H  HD13 B ILE   A 1 18  ? 9.777  -9.459  5.227   0.34 16.21 ?  18  ILE   A HD13 1 
ATOM   498  N  N    A LYS   A 1 19  ? 10.793 -7.646  9.344   0.66 12.93 ?  19  LYS   A N    1 
ATOM   499  N  N    B LYS   A 1 19  ? 11.047 -7.639  9.821   0.34 11.68 ?  19  LYS   A N    1 
ATOM   500  C  CA   A LYS   A 1 19  ? 9.981  -6.676  10.074  0.66 13.78 ?  19  LYS   A CA   1 
ATOM   501  C  CA   B LYS   A 1 19  ? 10.277 -6.715  10.642  0.34 12.26 ?  19  LYS   A CA   1 
ATOM   502  C  C    A LYS   A 1 19  ? 9.773  -5.434  9.218   0.66 13.47 ?  19  LYS   A C    1 
ATOM   503  C  C    B LYS   A 1 19  ? 9.954  -5.474  9.827   0.34 12.57 ?  19  LYS   A C    1 
ATOM   504  O  O    A LYS   A 1 19  ? 10.651 -5.048  8.445   0.66 13.10 ?  19  LYS   A O    1 
ATOM   505  O  O    B LYS   A 1 19  ? 10.792 -4.984  9.068   0.34 12.19 ?  19  LYS   A O    1 
ATOM   506  C  CB   A LYS   A 1 19  ? 10.673 -6.286  11.388  0.66 14.50 ?  19  LYS   A CB   1 
ATOM   507  C  CB   B LYS   A 1 19  ? 11.053 -6.316  11.906  0.34 13.00 ?  19  LYS   A CB   1 
ATOM   508  C  CG   A LYS   A 1 19  ? 9.906  -5.341  12.309  0.66 15.54 ?  19  LYS   A CG   1 
ATOM   509  C  CG   B LYS   A 1 19  ? 10.344 -5.351  12.846  0.34 13.80 ?  19  LYS   A CG   1 
ATOM   510  C  CD   A LYS   A 1 19  ? 10.783 -5.021  13.521  0.66 17.05 ?  19  LYS   A CD   1 
ATOM   511  C  CD   B LYS   A 1 19  ? 11.262 -4.998  14.010  0.34 14.38 ?  19  LYS   A CD   1 
ATOM   512  C  CE   A LYS   A 1 19  ? 10.107 -4.109  14.530  0.66 17.99 ?  19  LYS   A CE   1 
ATOM   513  C  CE   B LYS   A 1 19  ? 10.592 -4.084  15.017  0.34 14.97 ?  19  LYS   A CE   1 
ATOM   514  N  NZ   A LYS   A 1 19  ? 11.001 -3.839  15.694  0.66 18.20 ?  19  LYS   A NZ   1 
ATOM   515  N  NZ   B LYS   A 1 19  ? 11.463 -3.905  16.214  0.34 15.36 ?  19  LYS   A NZ   1 
ATOM   516  H  H    A LYS   A 1 19  ? 11.346 -7.286  8.786   0.66 15.53 ?  19  LYS   A H    1 
ATOM   517  H  H    B LYS   A 1 19  ? 11.642 -7.243  9.332   0.34 14.03 ?  19  LYS   A H    1 
ATOM   518  H  HA   A LYS   A 1 19  ? 9.118  -7.069  10.277  0.66 16.54 ?  19  LYS   A HA   1 
ATOM   519  H  HA   B LYS   A 1 19  ? 9.447  -7.127  10.908  0.34 14.71 ?  19  LYS   A HA   1 
ATOM   520  H  HB2  A LYS   A 1 19  ? 10.845 -7.094  11.891  0.66 17.41 ?  19  LYS   A HB2  1 
ATOM   521  H  HB2  B LYS   A 1 19  ? 11.237 -7.118  12.415  0.34 15.60 ?  19  LYS   A HB2  1 
ATOM   522  H  HB3  A LYS   A 1 19  ? 11.513 -5.854  11.171  0.66 17.41 ?  19  LYS   A HB3  1 
ATOM   523  H  HB3  B LYS   A 1 19  ? 11.889 -5.899  11.643  0.34 15.60 ?  19  LYS   A HB3  1 
ATOM   524  H  HG2  A LYS   A 1 19  ? 9.705  -4.512  11.846  0.66 18.66 ?  19  LYS   A HG2  1 
ATOM   525  H  HG2  B LYS   A 1 19  ? 10.120 -4.534  12.373  0.34 16.57 ?  19  LYS   A HG2  1 
ATOM   526  H  HG3  A LYS   A 1 19  ? 9.092  -5.768  12.620  0.66 18.66 ?  19  LYS   A HG3  1 
ATOM   527  H  HG3  B LYS   A 1 19  ? 9.543  -5.770  13.201  0.34 16.57 ?  19  LYS   A HG3  1 
ATOM   528  H  HD2  A LYS   A 1 19  ? 11.010 -5.850  13.974  0.66 20.47 ?  19  LYS   A HD2  1 
ATOM   529  H  HD2  B LYS   A 1 19  ? 11.520 -5.813  14.467  0.34 17.27 ?  19  LYS   A HD2  1 
ATOM   530  H  HD3  A LYS   A 1 19  ? 11.594 -4.581  13.218  0.66 20.47 ?  19  LYS   A HD3  1 
ATOM   531  H  HD3  B LYS   A 1 19  ? 12.048 -4.545  13.666  0.34 17.27 ?  19  LYS   A HD3  1 
ATOM   532  H  HE2  A LYS   A 1 19  ? 9.896  -3.262  14.108  0.66 21.60 ?  19  LYS   A HE2  1 
ATOM   533  H  HE2  B LYS   A 1 19  ? 10.440 -3.215  14.613  0.34 17.97 ?  19  LYS   A HE2  1 
ATOM   534  H  HE3  A LYS   A 1 19  ? 9.301  -4.533  14.860  0.66 21.60 ?  19  LYS   A HE3  1 
ATOM   535  H  HE3  B LYS   A 1 19  ? 9.753  -4.477  15.302  0.34 17.97 ?  19  LYS   A HE3  1 
ATOM   536  H  HZ1  A LYS   A 1 19  ? 10.585 -3.322  16.287  0.66 21.84 ?  19  LYS   A HZ1  1 
ATOM   537  H  HZ1  B LYS   A 1 19  ? 11.022 -3.459  16.845  0.34 18.44 ?  19  LYS   A HZ1  1 
ATOM   538  H  HZ2  A LYS   A 1 19  ? 11.229 -4.605  16.088  0.66 21.84 ?  19  LYS   A HZ2  1 
ATOM   539  H  HZ2  B LYS   A 1 19  ? 11.703 -4.699  16.535  0.34 18.44 ?  19  LYS   A HZ2  1 
ATOM   540  H  HZ3  A LYS   A 1 19  ? 11.742 -3.426  15.422  0.66 21.84 ?  19  LYS   A HZ3  1 
ATOM   541  H  HZ3  B LYS   A 1 19  ? 12.193 -3.448  15.993  0.34 18.44 ?  19  LYS   A HZ3  1 
ATOM   542  N  N    A ASN   A 1 20  ? 8.598  -4.814  9.353   0.66 14.51 ?  20  ASN   A N    1 
ATOM   543  N  N    B ASN   A 1 20  ? 8.732  -4.977  9.985   0.34 13.54 ?  20  ASN   A N    1 
ATOM   544  C  CA   A ASN   A 1 20  ? 8.358  -3.490  8.788   0.66 15.88 ?  20  ASN   A CA   1 
ATOM   545  C  CA   B ASN   A 1 20  ? 8.311  -3.728  9.364   0.34 14.60 ?  20  ASN   A CA   1 
ATOM   546  C  C    A ASN   A 1 20  ? 8.963  -2.479  9.751   0.66 17.00 ?  20  ASN   A C    1 
ATOM   547  C  C    B ASN   A 1 20  ? 8.890  -2.610  10.221  0.34 14.73 ?  20  ASN   A C    1 
ATOM   548  O  O    A ASN   A 1 20  ? 8.428  -2.244  10.838  0.66 18.55 ?  20  ASN   A O    1 
ATOM   549  O  O    B ASN   A 1 20  ? 8.382  -2.317  11.305  0.34 15.68 ?  20  ASN   A O    1 
ATOM   550  C  CB   A ASN   A 1 20  ? 6.860  -3.255  8.595   0.66 16.86 ?  20  ASN   A CB   1 
ATOM   551  C  CB   B ASN   A 1 20  ? 6.786  -3.686  9.315   0.34 15.53 ?  20  ASN   A CB   1 
ATOM   552  C  CG   A ASN   A 1 20  ? 6.519  -1.816  8.202   0.66 18.35 ?  20  ASN   A CG   1 
ATOM   553  C  CG   B ASN   A 1 20  ? 6.235  -2.446  8.623   0.34 16.51 ?  20  ASN   A CG   1 
ATOM   554  O  OD1  A ASN   A 1 20  ? 5.548  -1.245  8.702   0.66 20.23 ?  20  ASN   A OD1  1 
ATOM   555  O  OD1  B ASN   A 1 20  ? 5.101  -2.040  8.886   0.34 17.47 ?  20  ASN   A OD1  1 
ATOM   556  N  ND2  A ASN   A 1 20  ? 7.298  -1.237  7.298   0.66 19.14 ?  20  ASN   A ND2  1 
ATOM   557  N  ND2  B ASN   A 1 20  ? 7.019  -1.846  7.737   0.34 16.74 ?  20  ASN   A ND2  1 
ATOM   558  H  H    A ASN   A 1 20  ? 7.927  -5.144  9.773   0.66 17.42 ?  20  ASN   A H    1 
ATOM   559  H  H    B ASN   A 1 20  ? 8.121  -5.346  10.456  0.34 16.25 ?  20  ASN   A H    1 
ATOM   560  H  HA   A ASN   A 1 20  ? 8.797  -3.409  7.931   0.66 19.06 ?  20  ASN   A HA   1 
ATOM   561  H  HA   B ASN   A 1 20  ? 8.667  -3.670  8.465   0.34 17.52 ?  20  ASN   A HA   1 
ATOM   562  H  HB2  A ASN   A 1 20  ? 6.537  -3.835  7.889   0.66 20.24 ?  20  ASN   A HB2  1 
ATOM   563  H  HB2  B ASN   A 1 20  ? 6.468  -4.468  8.832   0.34 18.65 ?  20  ASN   A HB2  1 
ATOM   564  H  HB3  A ASN   A 1 20  ? 6.398  -3.457  9.424   0.66 20.24 ?  20  ASN   A HB3  1 
ATOM   565  H  HB3  B ASN   A 1 20  ? 6.440  -3.695  10.219  0.34 18.65 ?  20  ASN   A HB3  1 
ATOM   566  H  HD21 A ASN   A 1 20  ? 7.139  -0.427  7.051   0.66 22.97 ?  20  ASN   A HD21 1 
ATOM   567  H  HD21 B ASN   A 1 20  ? 6.737  -1.152  7.323   0.34 20.10 ?  20  ASN   A HD21 1 
ATOM   568  H  HD22 A ASN   A 1 20  ? 7.965  -1.664  6.969   0.66 22.97 ?  20  ASN   A HD22 1 
ATOM   569  H  HD22 B ASN   A 1 20  ? 7.808  -2.148  7.575   0.34 20.10 ?  20  ASN   A HD22 1 
ATOM   570  N  N    A ALA   A 1 21  ? 10.105 -1.913  9.381   0.66 16.99 ?  21  ALA   A N    1 
ATOM   571  N  N    B ALA   A 1 21  ? 9.990  -2.009  9.768   0.34 14.98 ?  21  ALA   A N    1 
ATOM   572  C  CA   A ALA   A 1 21  ? 10.804 -1.009  10.279  0.66 16.63 ?  21  ALA   A CA   1 
ATOM   573  C  CA   B ALA   A 1 21  ? 10.672 -1.038  10.611  0.34 15.71 ?  21  ALA   A CA   1 
ATOM   574  C  C    A ALA   A 1 21  ? 11.764 -0.156  9.475   0.66 16.04 ?  21  ALA   A C    1 
ATOM   575  C  C    B ALA   A 1 21  ? 11.591 -0.152  9.787   0.34 14.83 ?  21  ALA   A C    1 
ATOM   576  O  O    A ALA   A 1 21  ? 12.213 -0.552  8.395   0.66 16.04 ?  21  ALA   A O    1 
ATOM   577  O  O    B ALA   A 1 21  ? 11.974 -0.483  8.662   0.34 14.14 ?  21  ALA   A O    1 
ATOM   578  C  CB   A ALA   A 1 21  ? 11.567 -1.784  11.357  0.66 17.62 ?  21  ALA   A CB   1 
ATOM   579  C  CB   B ALA   A 1 21  ? 11.470 -1.725  11.722  0.34 17.15 ?  21  ALA   A CB   1 
ATOM   580  H  H    A ALA   A 1 21  ? 10.496 -2.036  8.625   0.66 20.39 ?  21  ALA   A H    1 
ATOM   581  H  H    B ALA   A 1 21  ? 10.354 -2.145  8.997   0.34 17.99 ?  21  ALA   A H    1 
ATOM   582  H  HA   A ALA   A 1 21  ? 10.160 -0.425  10.717  0.66 19.96 ?  21  ALA   A HA   1 
ATOM   583  H  HA   B ALA   A 1 21  ? 10.010 -0.465  11.026  0.34 18.86 ?  21  ALA   A HA   1 
ATOM   584  H  HB1  A ALA   A 1 21  ? 11.960 -1.153  11.977  0.66 21.15 ?  21  ALA   A HB1  1 
ATOM   585  H  HB1  B ALA   A 1 21  ? 11.888 -1.044  12.271  0.34 20.58 ?  21  ALA   A HB1  1 
ATOM   586  H  HB2  A ALA   A 1 21  ? 10.940 -2.361  11.832  0.66 21.15 ?  21  ALA   A HB2  1 
ATOM   587  H  HB2  B ALA   A 1 21  ? 10.863 -2.257  12.257  0.34 20.58 ?  21  ALA   A HB2  1 
ATOM   588  H  HB3  A ALA   A 1 21  ? 12.252 -2.320  10.937  0.66 21.15 ?  21  ALA   A HB3  1 
ATOM   589  H  HB3  B ALA   A 1 21  ? 12.145 -2.292  11.320  0.34 20.58 ?  21  ALA   A HB3  1 
ATOM   590  N  N    A ASP   A 1 22  ? 12.043 1.029   10.013  0.66 16.21 ?  22  ASP   A N    1 
ATOM   591  N  N    B ASP   A 1 22  ? 11.922 0.992   10.385  0.34 14.79 ?  22  ASP   A N    1 
ATOM   592  C  CA   A ASP   A 1 22  ? 13.097 1.898   9.514   0.66 16.35 ?  22  ASP   A CA   1 
ATOM   593  C  CA   B ASP   A 1 22  ? 12.921 1.919   9.873   0.34 14.67 ?  22  ASP   A CA   1 
ATOM   594  C  C    A ASP   A 1 22  ? 14.421 1.393   10.077  0.66 14.63 ?  22  ASP   A C    1 
ATOM   595  C  C    B ASP   A 1 22  ? 14.290 1.431   10.337  0.34 14.43 ?  22  ASP   A C    1 
ATOM   596  O  O    A ASP   A 1 22  ? 14.594 1.336   11.297  0.66 15.28 ?  22  ASP   A O    1 
ATOM   597  O  O    B ASP   A 1 22  ? 14.541 1.334   11.543  0.34 15.07 ?  22  ASP   A O    1 
ATOM   598  C  CB   A ASP   A 1 22  ? 12.816 3.325   9.987   0.66 19.53 ?  22  ASP   A CB   1 
ATOM   599  C  CB   B ASP   A 1 22  ? 12.610 3.296   10.459  0.34 15.33 ?  22  ASP   A CB   1 
ATOM   600  C  CG   A ASP   A 1 22  ? 13.866 4.330   9.515   0.66 21.78 ?  22  ASP   A CG   1 
ATOM   601  C  CG   B ASP   A 1 22  ? 13.493 4.398   9.913   0.34 15.06 ?  22  ASP   A CG   1 
ATOM   602  O  OD1  A ASP   A 1 22  ? 14.900 3.911   8.950   0.66 22.07 ?  22  ASP   A OD1  1 
ATOM   603  O  OD1  B ASP   A 1 22  ? 14.721 4.208   9.866   0.34 14.63 ?  22  ASP   A OD1  1 
ATOM   604  O  OD2  A ASP   A 1 22  ? 13.647 5.550   9.709   0.66 23.59 -1 22  ASP   A OD2  1 
ATOM   605  O  OD2  B ASP   A 1 22  ? 12.955 5.474   9.559   0.34 15.32 -1 22  ASP   A OD2  1 
ATOM   606  H  H    A ASP   A 1 22  ? 11.612 1.361   10.684  0.66 19.46 ?  22  ASP   A H    1 
ATOM   607  H  H    B ASP   A 1 22  ? 11.559 1.263   11.115  0.34 17.76 ?  22  ASP   A H    1 
ATOM   608  H  HA   A ASP   A 1 22  ? 13.123 1.876   8.546   0.66 19.63 ?  22  ASP   A HA   1 
ATOM   609  H  HA   B ASP   A 1 22  ? 12.890 1.958   8.901   0.34 17.61 ?  22  ASP   A HA   1 
ATOM   610  H  HB2  A ASP   A 1 22  ? 11.944 3.599   9.652   0.66 23.44 ?  22  ASP   A HB2  1 
ATOM   611  H  HB2  B ASP   A 1 22  ? 11.690 3.521   10.266  0.34 18.40 ?  22  ASP   A HB2  1 
ATOM   612  H  HB3  A ASP   A 1 22  ? 12.802 3.333   10.961  0.66 23.44 ?  22  ASP   A HB3  1 
ATOM   613  H  HB3  B ASP   A 1 22  ? 12.753 3.268   11.416  0.34 18.40 ?  22  ASP   A HB3  1 
ATOM   614  N  N    A ILE   A 1 23  ? 15.346 1.005   9.195   0.66 14.10 ?  23  ILE   A N    1 
ATOM   615  N  N    B ILE   A 1 23  ? 15.172 1.113   9.386   0.34 14.19 ?  23  ILE   A N    1 
ATOM   616  C  CA   A ILE   A 1 23  ? 16.597 0.400   9.657   0.66 13.42 ?  23  ILE   A CA   1 
ATOM   617  C  CA   B ILE   A 1 23  ? 16.431 0.451   9.722   0.34 13.89 ?  23  ILE   A CA   1 
ATOM   618  C  C    A ILE   A 1 23  ? 17.373 1.344   10.570  0.66 13.24 ?  23  ILE   A C    1 
ATOM   619  C  C    B ILE   A 1 23  ? 17.305 1.346   10.589  0.34 13.80 ?  23  ILE   A C    1 
ATOM   620  O  O    A ILE   A 1 23  ? 18.097 0.889   11.466  0.66 13.24 ?  23  ILE   A O    1 
ATOM   621  O  O    B ILE   A 1 23  ? 18.046 0.859   11.452  0.34 13.80 ?  23  ILE   A O    1 
ATOM   622  C  CB   A ILE   A 1 23  ? 17.443 -0.120  8.471   0.66 13.37 ?  23  ILE   A CB   1 
ATOM   623  C  CB   B ILE   A 1 23  ? 17.150 -0.032  8.444   0.34 13.83 ?  23  ILE   A CB   1 
ATOM   624  C  CG1  A ILE   A 1 23  ? 18.573 -1.031  8.968   0.66 13.54 ?  23  ILE   A CG1  1 
ATOM   625  C  CG1  B ILE   A 1 23  ? 18.297 -0.976  8.806   0.34 13.43 ?  23  ILE   A CG1  1 
ATOM   626  C  CG2  A ILE   A 1 23  ? 17.990 1.033   7.638   0.66 13.42 ?  23  ILE   A CG2  1 
ATOM   627  C  CG2  B ILE   A 1 23  ? 17.661 1.147   7.624   0.34 14.04 ?  23  ILE   A CG2  1 
ATOM   628  C  CD1  A ILE   A 1 23  ? 19.367 -1.698  7.846   0.66 13.67 ?  23  ILE   A CD1  1 
ATOM   629  C  CD1  B ILE   A 1 23  ? 18.882 -1.700  7.616   0.34 13.17 ?  23  ILE   A CD1  1 
ATOM   630  H  H    A ILE   A 1 23  ? 15.271 1.075   8.346   0.66 16.93 ?  23  ILE   A H    1 
ATOM   631  H  H    B ILE   A 1 23  ? 15.075 1.275   8.557   0.34 17.03 ?  23  ILE   A H    1 
ATOM   632  H  HA   A ILE   A 1 23  ? 16.371 -0.375  10.192  0.66 16.11 ?  23  ILE   A HA   1 
ATOM   633  H  HA   B ILE   A 1 23  ? 16.226 -0.337  10.238  0.34 16.68 ?  23  ILE   A HA   1 
ATOM   634  H  HB   A ILE   A 1 23  ? 16.867 -0.651  7.902   0.66 16.05 ?  23  ILE   A HB   1 
ATOM   635  H  HB   B ILE   A 1 23  ? 16.517 -0.524  7.899   0.34 16.60 ?  23  ILE   A HB   1 
ATOM   636  H  HG12 A ILE   A 1 23  ? 19.196 -0.507  9.494   0.66 16.26 ?  23  ILE   A HG12 1 
ATOM   637  H  HG12 B ILE   A 1 23  ? 19.009 -0.464  9.219   0.34 16.13 ?  23  ILE   A HG12 1 
ATOM   638  H  HG13 A ILE   A 1 23  ? 18.192 -1.736  9.516   0.66 16.26 ?  23  ILE   A HG13 1 
ATOM   639  H  HG13 B ILE   A 1 23  ? 17.968 -1.645  9.425   0.34 16.13 ?  23  ILE   A HG13 1 
ATOM   640  H  HG21 A ILE   A 1 23  ? 18.361 0.679   6.812   0.66 16.12 ?  23  ILE   A HG21 1 
ATOM   641  H  HG21 B ILE   A 1 23  ? 17.948 0.825   6.753   0.34 16.85 ?  23  ILE   A HG21 1 
ATOM   642  H  HG22 A ILE   A 1 23  ? 17.265 1.644   7.435   0.66 16.12 ?  23  ILE   A HG22 1 
ATOM   643  H  HG22 B ILE   A 1 23  ? 16.945 1.792   7.516   0.34 16.85 ?  23  ILE   A HG22 1 
ATOM   644  H  HG23 A ILE   A 1 23  ? 18.679 1.491   8.141   0.66 16.12 ?  23  ILE   A HG23 1 
ATOM   645  H  HG23 B ILE   A 1 23  ? 18.408 1.556   8.085   0.34 16.85 ?  23  ILE   A HG23 1 
ATOM   646  H  HD11 A ILE   A 1 23  ? 19.995 -2.327  8.233   0.66 16.41 ?  23  ILE   A HD11 1 
ATOM   647  H  HD11 B ILE   A 1 23  ? 19.556 -2.325  7.927   0.34 15.82 ?  23  ILE   A HD11 1 
ATOM   648  H  HD12 A ILE   A 1 23  ? 18.750 -2.165  7.260   0.66 16.41 ?  23  ILE   A HD12 1 
ATOM   649  H  HD12 B ILE   A 1 23  ? 18.173 -2.179  7.159   0.34 15.82 ?  23  ILE   A HD12 1 
ATOM   650  H  HD13 A ILE   A 1 23  ? 19.844 -1.016  7.348   0.66 16.41 ?  23  ILE   A HD13 1 
ATOM   651  H  HD13 B ILE   A 1 23  ? 19.284 -1.051  7.017   0.34 15.82 ?  23  ILE   A HD13 1 
ATOM   652  N  N    . VAL   A 1 24  ? 17.231 2.660   10.379  1.00 14.20 ?  24  VAL   A N    1 
ATOM   653  C  CA   . VAL   A 1 24  ? 17.929 3.607   11.244  1.00 15.42 ?  24  VAL   A CA   1 
ATOM   654  C  C    . VAL   A 1 24  ? 17.386 3.523   12.660  1.00 15.86 ?  24  VAL   A C    1 
ATOM   655  O  O    . VAL   A 1 24  ? 18.145 3.469   13.634  1.00 16.21 ?  24  VAL   A O    1 
ATOM   656  C  CB   . VAL   A 1 24  ? 17.805 5.032   10.680  1.00 16.61 ?  24  VAL   A CB   1 
ATOM   657  C  CG1  . VAL   A 1 24  ? 18.272 6.064   11.709  1.00 18.29 ?  24  VAL   A CG1  1 
ATOM   658  C  CG2  . VAL   A 1 24  ? 18.592 5.153   9.393   1.00 18.15 ?  24  VAL   A CG2  1 
ATOM   659  H  H    A VAL   A 1 24  ? 16.745 3.019   9.766   0.66 17.04 ?  24  VAL   A H    1 
ATOM   660  H  H    B VAL   A 1 24  ? 16.780 3.027   9.744   0.34 17.04 ?  24  VAL   A H    1 
ATOM   661  H  HA   . VAL   A 1 24  ? 18.869 3.377   11.268  1.00 18.51 ?  24  VAL   A HA   1 
ATOM   662  H  HB   . VAL   A 1 24  ? 16.875 5.213   10.474  1.00 19.94 ?  24  VAL   A HB   1 
ATOM   663  H  HG11 . VAL   A 1 24  ? 18.458 6.897   11.251  1.00 21.95 ?  24  VAL   A HG11 1 
ATOM   664  H  HG12 . VAL   A 1 24  ? 17.569 6.196   12.363  1.00 21.95 ?  24  VAL   A HG12 1 
ATOM   665  H  HG13 . VAL   A 1 24  ? 19.075 5.735   12.140  1.00 21.95 ?  24  VAL   A HG13 1 
ATOM   666  H  HG21 . VAL   A 1 24  ? 18.345 5.974   8.944   1.00 21.78 ?  24  VAL   A HG21 1 
ATOM   667  H  HG22 . VAL   A 1 24  ? 19.542 5.167   9.603   1.00 21.78 ?  24  VAL   A HG22 1 
ATOM   668  H  HG23 . VAL   A 1 24  ? 18.394 4.392   8.822   1.00 21.78 ?  24  VAL   A HG23 1 
ATOM   669  N  N    A GLU   A 1 25  ? 16.062 3.559   12.801  0.66 16.46 ?  25  GLU   A N    1 
ATOM   670  N  N    B GLU   A 1 25  ? 16.058 3.478   12.793  0.34 16.58 ?  25  GLU   A N    1 
ATOM   671  C  CA   A GLU   A 1 25  ? 15.469 3.494   14.132  0.66 17.84 ?  25  GLU   A CA   1 
ATOM   672  C  CA   B GLU   A 1 25  ? 15.448 3.345   14.111  0.34 17.75 ?  25  GLU   A CA   1 
ATOM   673  C  C    A GLU   A 1 25  ? 15.720 2.139   14.776  0.66 16.18 ?  25  GLU   A C    1 
ATOM   674  C  C    B GLU   A 1 25  ? 15.729 1.972   14.713  0.34 16.97 ?  25  GLU   A C    1 
ATOM   675  O  O    A GLU   A 1 25  ? 15.937 2.057   15.989  0.66 16.78 ?  25  GLU   A O    1 
ATOM   676  O  O    B GLU   A 1 25  ? 16.019 1.866   15.910  0.34 17.10 ?  25  GLU   A O    1 
ATOM   677  C  CB   A GLU   A 1 25  ? 13.976 3.818   14.060  0.66 20.67 ?  25  GLU   A CB   1 
ATOM   678  C  CB   B GLU   A 1 25  ? 13.946 3.625   14.022  0.34 19.62 ?  25  GLU   A CB   1 
ATOM   679  C  CG   A GLU   A 1 25  ? 13.703 5.273   13.699  0.66 24.03 ?  25  GLU   A CG   1 
ATOM   680  C  CG   B GLU   A 1 25  ? 13.618 5.034   13.541  0.34 22.02 ?  25  GLU   A CG   1 
ATOM   681  C  CD   A GLU   A 1 25  ? 14.494 6.246   14.558  0.66 27.22 ?  25  GLU   A CD   1 
ATOM   682  C  CD   B GLU   A 1 25  ? 14.215 6.099   14.432  0.34 24.14 ?  25  GLU   A CD   1 
ATOM   683  O  OE1  A GLU   A 1 25  ? 14.566 6.037   15.788  0.66 28.64 ?  25  GLU   A OE1  1 
ATOM   684  O  OE1  B GLU   A 1 25  ? 14.228 5.900   15.666  0.34 25.06 ?  25  GLU   A OE1  1 
ATOM   685  O  OE2  A GLU   A 1 25  ? 15.073 7.200   13.998  0.66 28.46 -1 25  GLU   A OE2  1 
ATOM   686  O  OE2  B GLU   A 1 25  ? 14.679 7.126   13.898  0.34 25.00 -1 25  GLU   A OE2  1 
ATOM   687  H  H    A GLU   A 1 25  ? 15.497 3.626   12.156  0.66 19.76 ?  25  GLU   A H    1 
ATOM   688  H  H    B GLU   A 1 25  ? 15.497 3.522   12.141  0.34 19.90 ?  25  GLU   A H    1 
ATOM   689  H  HA   A GLU   A 1 25  ? 15.896 4.153   14.695  0.66 21.42 ?  25  GLU   A HA   1 
ATOM   690  H  HA   B GLU   A 1 25  ? 15.836 4.004   14.703  0.34 21.31 ?  25  GLU   A HA   1 
ATOM   691  H  HB2  A GLU   A 1 25  ? 13.560 3.260   13.382  0.66 24.81 ?  25  GLU   A HB2  1 
ATOM   692  H  HB2  B GLU   A 1 25  ? 13.541 3.000   13.403  0.34 23.55 ?  25  GLU   A HB2  1 
ATOM   693  H  HB3  A GLU   A 1 25  ? 13.569 3.643   14.924  0.66 24.81 ?  25  GLU   A HB3  1 
ATOM   694  H  HB3  B GLU   A 1 25  ? 13.552 3.519   14.901  0.34 23.55 ?  25  GLU   A HB3  1 
ATOM   695  H  HG2  A GLU   A 1 25  ? 13.969 5.424   12.780  0.66 28.84 ?  25  GLU   A HG2  1 
ATOM   696  H  HG2  B GLU   A 1 25  ? 13.974 5.161   12.648  0.34 26.43 ?  25  GLU   A HG2  1 
ATOM   697  H  HG3  A GLU   A 1 25  ? 12.755 5.452   13.807  0.66 28.84 ?  25  GLU   A HG3  1 
ATOM   698  H  HG3  B GLU   A 1 25  ? 12.657 5.160   13.538  0.34 26.43 ?  25  GLU   A HG3  1 
ATOM   699  N  N    A GLU   A 1 26  ? 15.713 1.070   13.978  0.66 16.05 ?  26  GLU   A N    1 
ATOM   700  N  N    B GLU   A 1 26  ? 15.667 0.911   13.902  0.34 16.84 ?  26  GLU   A N    1 
ATOM   701  C  CA   A GLU   A 1 26  ? 16.027 -0.253  14.508  0.66 15.93 ?  26  GLU   A CA   1 
ATOM   702  C  CA   B GLU   A 1 26  ? 16.014 -0.417  14.405  0.34 16.94 ?  26  GLU   A CA   1 
ATOM   703  C  C    A GLU   A 1 26  ? 17.449 -0.296  15.054  0.66 14.56 ?  26  GLU   A C    1 
ATOM   704  C  C    B GLU   A 1 26  ? 17.454 -0.449  14.899  0.34 16.77 ?  26  GLU   A C    1 
ATOM   705  O  O    A GLU   A 1 26  ? 17.687 -0.773  16.169  0.66 14.79 ?  26  GLU   A O    1 
ATOM   706  O  O    B GLU   A 1 26  ? 17.761 -1.104  15.902  0.34 16.43 ?  26  GLU   A O    1 
ATOM   707  C  CB   A GLU   A 1 26  ? 15.862 -1.302  13.407  0.66 17.75 ?  26  GLU   A CB   1 
ATOM   708  C  CB   B GLU   A 1 26  ? 15.820 -1.475  13.314  0.34 17.20 ?  26  GLU   A CB   1 
ATOM   709  C  CG   A GLU   A 1 26  ? 14.452 -1.768  13.175  0.66 20.78 ?  26  GLU   A CG   1 
ATOM   710  C  CG   B GLU   A 1 26  ? 14.549 -2.329  13.405  0.34 17.48 ?  26  GLU   A CG   1 
ATOM   711  C  CD   A GLU   A 1 26  ? 13.871 -2.468  14.378  0.66 22.37 ?  26  GLU   A CD   1 
ATOM   712  C  CD   B GLU   A 1 26  ? 14.349 -3.009  14.755  0.34 16.49 ?  26  GLU   A CD   1 
ATOM   713  O  OE1  A GLU   A 1 26  ? 14.480 -3.444  14.861  0.66 23.49 ?  26  GLU   A OE1  1 
ATOM   714  O  OE1  B GLU   A 1 26  ? 13.801 -2.339  15.641  0.34 15.81 ?  26  GLU   A OE1  1 
ATOM   715  O  OE2  A GLU   A 1 26  ? 12.816 -2.015  14.850  0.66 22.77 -1 26  GLU   A OE2  1 
ATOM   716  O  OE2  B GLU   A 1 26  ? 14.694 -4.203  14.935  0.34 15.48 -1 26  GLU   A OE2  1 
ATOM   717  H  H    A GLU   A 1 26  ? 15.534 1.088   13.135  0.66 19.27 ?  26  GLU   A H    1 
ATOM   718  H  H    B GLU   A 1 26  ? 15.442 0.935   13.072  0.34 20.21 ?  26  GLU   A H    1 
ATOM   719  H  HA   A GLU   A 1 26  ? 15.413 -0.460  15.226  0.66 19.12 ?  26  GLU   A HA   1 
ATOM   720  H  HA   B GLU   A 1 26  ? 15.435 -0.634  15.150  0.34 20.34 ?  26  GLU   A HA   1 
ATOM   721  H  HB2  A GLU   A 1 26  ? 16.183 -0.930  12.571  0.66 21.30 ?  26  GLU   A HB2  1 
ATOM   722  H  HB2  B GLU   A 1 26  ? 15.804 -1.029  12.452  0.34 20.65 ?  26  GLU   A HB2  1 
ATOM   723  H  HB3  A GLU   A 1 26  ? 16.395 -2.079  13.642  0.66 21.30 ?  26  GLU   A HB3  1 
ATOM   724  H  HB3  B GLU   A 1 26  ? 16.577 -2.084  13.342  0.34 20.65 ?  26  GLU   A HB3  1 
ATOM   725  H  HG2  A GLU   A 1 26  ? 13.890 -1.004  13.000  0.66 24.94 ?  26  GLU   A HG2  1 
ATOM   726  H  HG2  B GLU   A 1 26  ? 13.781 -1.758  13.253  0.34 20.98 ?  26  GLU   A HG2  1 
ATOM   727  H  HG3  A GLU   A 1 26  ? 14.435 -2.382  12.423  0.66 24.94 ?  26  GLU   A HG3  1 
ATOM   728  H  HG3  B GLU   A 1 26  ? 14.586 -3.020  12.728  0.34 20.98 ?  26  GLU   A HG3  1 
ATOM   729  N  N    A ALA   A 1 27  ? 18.414 0.182   14.266  0.66 13.57 ?  27  ALA   A N    1 
ATOM   730  N  N    B ALA   A 1 27  ? 18.356 0.243   14.201  0.34 16.85 ?  27  ALA   A N    1 
ATOM   731  C  CA   A ALA   A 1 27  ? 19.806 0.149   14.703  0.66 13.47 ?  27  ALA   A CA   1 
ATOM   732  C  CA   B ALA   A 1 27  ? 19.753 0.260   14.619  0.34 17.28 ?  27  ALA   A CA   1 
ATOM   733  C  C    A ALA   A 1 27  ? 20.000 0.955   15.980  0.66 14.93 ?  27  ALA   A C    1 
ATOM   734  C  C    B ALA   A 1 27  ? 19.925 1.030   15.924  0.34 18.76 ?  27  ALA   A C    1 
ATOM   735  O  O    A ALA   A 1 27  ? 20.673 0.505   16.913  0.66 15.29 ?  27  ALA   A O    1 
ATOM   736  O  O    B ALA   A 1 27  ? 20.620 0.574   16.839  0.34 18.81 ?  27  ALA   A O    1 
ATOM   737  C  CB   A ALA   A 1 27  ? 20.722 0.661   13.590  0.66 13.00 ?  27  ALA   A CB   1 
ATOM   738  C  CB   B ALA   A 1 27  ? 20.626 0.855   13.513  0.34 16.80 ?  27  ALA   A CB   1 
ATOM   739  H  H    A ALA   A 1 27  ? 18.288 0.526   13.490  0.66 16.29 ?  27  ALA   A H    1 
ATOM   740  H  H    B ALA   A 1 27  ? 18.185 0.702   13.492  0.34 20.22 ?  27  ALA   A H    1 
ATOM   741  H  HA   A ALA   A 1 27  ? 20.052 -0.769  14.891  0.66 16.17 ?  27  ALA   A HA   1 
ATOM   742  H  HA   B ALA   A 1 27  ? 20.045 -0.651  14.769  0.34 20.74 ?  27  ALA   A HA   1 
ATOM   743  H  HB1  A ALA   A 1 27  ? 21.643 0.628   13.899  0.66 15.61 ?  27  ALA   A HB1  1 
ATOM   744  H  HB1  B ALA   A 1 27  ? 21.550 0.856   13.808  0.34 20.17 ?  27  ALA   A HB1  1 
ATOM   745  H  HB2  A ALA   A 1 27  ? 20.618 0.092   12.809  0.66 15.61 ?  27  ALA   A HB2  1 
ATOM   746  H  HB2  B ALA   A 1 27  ? 20.535 0.312   12.713  0.34 20.17 ?  27  ALA   A HB2  1 
ATOM   747  H  HB3  A ALA   A 1 27  ? 20.479 1.572   13.371  0.66 15.61 ?  27  ALA   A HB3  1 
ATOM   748  H  HB3  B ALA   A 1 27  ? 20.334 1.761   13.332  0.34 20.17 ?  27  ALA   A HB3  1 
ATOM   749  N  N    A LYS   A 1 28  ? 19.397 2.142   16.055  0.66 17.11 ?  28  LYS   A N    1 
ATOM   750  N  N    B LYS   A 1 28  ? 19.290 2.199   16.032  0.34 20.64 ?  28  LYS   A N    1 
ATOM   751  C  CA   A LYS   A 1 28  ? 19.542 2.954   17.259  0.66 20.75 ?  28  LYS   A CA   1 
ATOM   752  C  CA   B LYS   A 1 28  ? 19.426 2.995   17.248  0.34 23.04 ?  28  LYS   A CA   1 
ATOM   753  C  C    A LYS   A 1 28  ? 18.991 2.241   18.486  0.66 21.81 ?  28  LYS   A C    1 
ATOM   754  C  C    B LYS   A 1 28  ? 18.840 2.285   18.462  0.34 24.11 ?  28  LYS   A C    1 
ATOM   755  O  O    A LYS   A 1 28  ? 19.555 2.367   19.578  0.66 23.79 ?  28  LYS   A O    1 
ATOM   756  O  O    B LYS   A 1 28  ? 19.304 2.500   19.588  0.34 24.91 ?  28  LYS   A O    1 
ATOM   757  C  CB   A LYS   A 1 28  ? 18.893 4.326   17.064  0.66 23.38 ?  28  LYS   A CB   1 
ATOM   758  C  CB   B LYS   A 1 28  ? 18.779 4.368   17.060  0.34 24.64 ?  28  LYS   A CB   1 
ATOM   759  C  CG   A LYS   A 1 28  ? 19.739 5.266   16.219  0.66 25.78 ?  28  LYS   A CG   1 
ATOM   760  C  CG   B LYS   A 1 28  ? 19.547 5.270   16.109  0.34 26.20 ?  28  LYS   A CG   1 
ATOM   761  C  CD   A LYS   A 1 28  ? 19.243 6.700   16.275  0.66 28.52 ?  28  LYS   A CD   1 
ATOM   762  C  CD   B LYS   A 1 28  ? 19.123 6.724   16.227  0.34 28.03 ?  28  LYS   A CD   1 
ATOM   763  C  CE   A LYS   A 1 28  ? 17.952 6.868   15.505  0.66 30.35 ?  28  LYS   A CE   1 
ATOM   764  C  CE   B LYS   A 1 28  ? 17.759 6.962   15.611  0.34 29.30 ?  28  LYS   A CE   1 
ATOM   765  N  NZ   A LYS   A 1 28  ? 17.539 8.296   15.436  0.66 31.61 ?  28  LYS   A NZ   1 
ATOM   766  N  NZ   B LYS   A 1 28  ? 17.430 8.413   15.556  0.34 30.08 ?  28  LYS   A NZ   1 
ATOM   767  H  H    A LYS   A 1 28  ? 18.913 2.489   15.443  0.66 20.54 ?  28  LYS   A H    1 
ATOM   768  H  H    B LYS   A 1 28  ? 18.793 2.549   15.426  0.34 24.78 ?  28  LYS   A H    1 
ATOM   769  H  HA   A LYS   A 1 28  ? 20.484 3.103   17.425  0.66 24.90 ?  28  LYS   A HA   1 
ATOM   770  H  HA   B LYS   A 1 28  ? 20.369 3.138   17.419  0.34 27.66 ?  28  LYS   A HA   1 
ATOM   771  H  HB2  A LYS   A 1 28  ? 18.041 4.214   16.617  0.66 28.06 ?  28  LYS   A HB2  1 
ATOM   772  H  HB2  B LYS   A 1 28  ? 17.885 4.249   16.703  0.34 29.57 ?  28  LYS   A HB2  1 
ATOM   773  H  HB3  A LYS   A 1 28  ? 18.762 4.744   17.930  0.66 28.06 ?  28  LYS   A HB3  1 
ATOM   774  H  HB3  B LYS   A 1 28  ? 18.733 4.813   17.922  0.34 29.57 ?  28  LYS   A HB3  1 
ATOM   775  H  HG2  A LYS   A 1 28  ? 20.653 5.253   16.545  0.66 30.94 ?  28  LYS   A HG2  1 
ATOM   776  H  HG2  B LYS   A 1 28  ? 20.494 5.214   16.312  0.34 31.45 ?  28  LYS   A HG2  1 
ATOM   777  H  HG3  A LYS   A 1 28  ? 19.712 4.975   15.295  0.66 30.94 ?  28  LYS   A HG3  1 
ATOM   778  H  HG3  B LYS   A 1 28  ? 19.384 4.982   15.197  0.34 31.45 ?  28  LYS   A HG3  1 
ATOM   779  H  HD2  A LYS   A 1 28  ? 19.082 6.949   17.199  0.66 34.23 ?  28  LYS   A HD2  1 
ATOM   780  H  HD2  B LYS   A 1 28  ? 19.080 6.970   17.165  0.34 33.64 ?  28  LYS   A HD2  1 
ATOM   781  H  HD3  A LYS   A 1 28  ? 19.910 7.286   15.882  0.66 34.23 ?  28  LYS   A HD3  1 
ATOM   782  H  HD3  B LYS   A 1 28  ? 19.767 7.283   15.765  0.34 33.64 ?  28  LYS   A HD3  1 
ATOM   783  H  HE2  A LYS   A 1 28  ? 18.076 6.542   14.600  0.66 36.43 ?  28  LYS   A HE2  1 
ATOM   784  H  HE2  B LYS   A 1 28  ? 17.752 6.613   14.706  0.34 35.16 ?  28  LYS   A HE2  1 
ATOM   785  H  HE3  A LYS   A 1 28  ? 17.249 6.368   15.948  0.66 36.43 ?  28  LYS   A HE3  1 
ATOM   786  H  HE3  B LYS   A 1 28  ? 17.084 6.517   16.147  0.34 35.16 ?  28  LYS   A HE3  1 
ATOM   787  H  HZ1  A LYS   A 1 28  ? 16.780 8.371   14.980  0.66 37.94 ?  28  LYS   A HZ1  1 
ATOM   788  H  HZ1  B LYS   A 1 28  ? 16.628 8.530   15.191  0.34 36.11 ?  28  LYS   A HZ1  1 
ATOM   789  H  HZ2  A LYS   A 1 28  ? 17.417 8.617   16.257  0.66 37.94 ?  28  LYS   A HZ2  1 
ATOM   790  H  HZ2  B LYS   A 1 28  ? 17.428 8.755   16.378  0.34 36.11 ?  28  LYS   A HZ2  1 
ATOM   791  H  HZ3  A LYS   A 1 28  ? 18.170 8.775   15.029  0.66 37.94 ?  28  LYS   A HZ3  1 
ATOM   792  H  HZ3  B LYS   A 1 28  ? 18.036 8.843   15.065  0.34 36.11 ?  28  LYS   A HZ3  1 
ATOM   793  N  N    A LYS   A 1 29  ? 17.917 1.468   18.325  0.66 21.75 ?  29  LYS   A N    1 
ATOM   794  N  N    B LYS   A 1 29  ? 17.827 1.442   18.262  0.34 24.84 ?  29  LYS   A N    1 
ATOM   795  C  CA   A LYS   A 1 29  ? 17.323 0.763   19.456  0.66 23.45 ?  29  LYS   A CA   1 
ATOM   796  C  CA   B LYS   A 1 29  ? 17.212 0.734   19.380  0.34 25.85 ?  29  LYS   A CA   1 
ATOM   797  C  C    A LYS   A 1 29  ? 18.140 -0.466  19.838  0.66 22.42 ?  29  LYS   A C    1 
ATOM   798  C  C    B LYS   A 1 29  ? 18.035 -0.478  19.799  0.34 24.55 ?  29  LYS   A C    1 
ATOM   799  O  O    A LYS   A 1 29  ? 18.429 -0.687  21.021  0.66 23.55 ?  29  LYS   A O    1 
ATOM   800  O  O    B LYS   A 1 29  ? 18.254 -0.707  20.995  0.34 24.72 ?  29  LYS   A O    1 
ATOM   801  C  CB   A LYS   A 1 29  ? 15.891 0.350   19.111  0.66 26.41 ?  29  LYS   A CB   1 
ATOM   802  C  CB   B LYS   A 1 29  ? 15.796 0.297   18.998  0.34 28.25 ?  29  LYS   A CB   1 
ATOM   803  C  CG   A LYS   A 1 29  ? 15.159 -0.362  20.238  0.66 30.28 ?  29  LYS   A CG   1 
ATOM   804  C  CG   B LYS   A 1 29  ? 15.023 -0.373  20.124  0.34 30.79 ?  29  LYS   A CG   1 
ATOM   805  C  CD   A LYS   A 1 29  ? 14.859 0.592   21.382  0.66 33.71 ?  29  LYS   A CD   1 
ATOM   806  C  CD   B LYS   A 1 29  ? 14.709 0.609   21.240  0.34 33.05 ?  29  LYS   A CD   1 
ATOM   807  C  CE   A LYS   A 1 29  ? 13.996 -0.066  22.446  0.66 35.82 ?  29  LYS   A CE   1 
ATOM   808  C  CE   B LYS   A 1 29  ? 13.897 -0.045  22.343  0.34 34.55 ?  29  LYS   A CE   1 
ATOM   809  N  NZ   A LYS   A 1 29  ? 13.563 0.912   23.483  0.66 37.08 ?  29  LYS   A NZ   1 
ATOM   810  N  NZ   B LYS   A 1 29  ? 13.519 0.934   23.397  0.34 35.44 ?  29  LYS   A NZ   1 
ATOM   811  H  H    A LYS   A 1 29  ? 17.520 1.332   17.575  0.66 26.10 ?  29  LYS   A H    1 
ATOM   812  H  H    B LYS   A 1 29  ? 17.473 1.275   17.497  0.34 29.81 ?  29  LYS   A H    1 
ATOM   813  H  HA   A LYS   A 1 29  ? 17.291 1.353   20.224  0.66 28.14 ?  29  LYS   A HA   1 
ATOM   814  H  HA   B LYS   A 1 29  ? 17.151 1.334   20.138  0.34 31.02 ?  29  LYS   A HA   1 
ATOM   815  H  HB2  A LYS   A 1 29  ? 15.382 1.145   18.890  0.66 31.70 ?  29  LYS   A HB2  1 
ATOM   816  H  HB2  B LYS   A 1 29  ? 15.294 1.077   18.720  0.34 33.91 ?  29  LYS   A HB2  1 
ATOM   817  H  HB3  A LYS   A 1 29  ? 15.912 -0.250  18.350  0.66 31.70 ?  29  LYS   A HB3  1 
ATOM   818  H  HB3  B LYS   A 1 29  ? 15.853 -0.336  18.265  0.34 33.91 ?  29  LYS   A HB3  1 
ATOM   819  H  HG2  A LYS   A 1 29  ? 14.317 -0.708  19.904  0.66 36.34 ?  29  LYS   A HG2  1 
ATOM   820  H  HG2  B LYS   A 1 29  ? 14.184 -0.713  19.776  0.34 36.96 ?  29  LYS   A HG2  1 
ATOM   821  H  HG3  A LYS   A 1 29  ? 15.705 -1.089  20.581  0.66 36.34 ?  29  LYS   A HG3  1 
ATOM   822  H  HG3  B LYS   A 1 29  ? 15.548 -1.100  20.495  0.34 36.96 ?  29  LYS   A HG3  1 
ATOM   823  H  HD2  A LYS   A 1 29  ? 15.692 0.868   21.796  0.66 40.45 ?  29  LYS   A HD2  1 
ATOM   824  H  HD2  B LYS   A 1 29  ? 15.538 0.933   21.626  0.34 39.66 ?  29  LYS   A HD2  1 
ATOM   825  H  HD3  A LYS   A 1 29  ? 14.384 1.364   21.038  0.66 40.45 ?  29  LYS   A HD3  1 
ATOM   826  H  HD3  B LYS   A 1 29  ? 14.195 1.349   20.880  0.34 39.66 ?  29  LYS   A HD3  1 
ATOM   827  H  HE2  A LYS   A 1 29  ? 13.203 -0.438  22.029  0.66 42.99 ?  29  LYS   A HE2  1 
ATOM   828  H  HE2  B LYS   A 1 29  ? 13.083 -0.415  21.965  0.34 41.47 ?  29  LYS   A HE2  1 
ATOM   829  H  HE3  A LYS   A 1 29  ? 14.505 -0.767  22.883  0.66 42.99 ?  29  LYS   A HE3  1 
ATOM   830  H  HE3  B LYS   A 1 29  ? 14.425 -0.748  22.755  0.34 41.47 ?  29  LYS   A HE3  1 
ATOM   831  H  HZ1  A LYS   A 1 29  ? 13.060 0.505   24.094  0.66 44.50 ?  29  LYS   A HZ1  1 
ATOM   832  H  HZ1  B LYS   A 1 29  ? 13.045 0.529   24.032  0.34 42.53 ?  29  LYS   A HZ1  1 
ATOM   833  H  HZ2  A LYS   A 1 29  ? 14.275 1.265   23.884  0.66 44.50 ?  29  LYS   A HZ2  1 
ATOM   834  H  HZ2  B LYS   A 1 29  ? 14.251 1.285   23.762  0.34 42.53 ?  29  LYS   A HZ2  1 
ATOM   835  H  HZ3  A LYS   A 1 29  ? 13.089 1.565   23.106  0.66 44.50 ?  29  LYS   A HZ3  1 
ATOM   836  H  HZ3  B LYS   A 1 29  ? 13.030 1.588   23.043  0.34 42.53 ?  29  LYS   A HZ3  1 
ATOM   837  N  N    A VAL   A 1 30  ? 18.493 -1.288  18.852  0.66 20.92 ?  30  VAL   A N    1 
ATOM   838  N  N    B VAL   A 1 30  ? 18.486 -1.271  18.832  0.34 23.30 ?  30  VAL   A N    1 
ATOM   839  C  CA   A VAL   A 1 30  ? 19.140 -2.566  19.129  0.66 20.61 ?  30  VAL   A CA   1 
ATOM   840  C  CA   B VAL   A 1 30  ? 19.134 -2.546  19.127  0.34 22.38 ?  30  VAL   A CA   1 
ATOM   841  C  C    A VAL   A 1 30  ? 20.638 -2.392  19.353  0.66 19.65 ?  30  VAL   A C    1 
ATOM   842  C  C    B VAL   A 1 30  ? 20.632 -2.382  19.358  0.34 20.90 ?  30  VAL   A C    1 
ATOM   843  O  O    A VAL   A 1 30  ? 21.238 -3.100  20.168  0.66 19.98 ?  30  VAL   A O    1 
ATOM   844  O  O    B VAL   A 1 30  ? 21.216 -3.084  20.187  0.34 21.22 ?  30  VAL   A O    1 
ATOM   845  C  CB   A VAL   A 1 30  ? 18.844 -3.553  17.985  0.66 21.40 ?  30  VAL   A CB   1 
ATOM   846  C  CB   B VAL   A 1 30  ? 18.841 -3.538  17.984  0.34 22.90 ?  30  VAL   A CB   1 
ATOM   847  C  CG1  A VAL   A 1 30  ? 19.656 -4.831  18.152  0.66 21.50 ?  30  VAL   A CG1  1 
ATOM   848  C  CG1  B VAL   A 1 30  ? 19.581 -4.851  18.207  0.34 23.13 ?  30  VAL   A CG1  1 
ATOM   849  C  CG2  A VAL   A 1 30  ? 17.356 -3.868  17.921  0.66 22.36 ?  30  VAL   A CG2  1 
ATOM   850  C  CG2  B VAL   A 1 30  ? 17.344 -3.776  17.857  0.34 23.31 ?  30  VAL   A CG2  1 
ATOM   851  H  H    A VAL   A 1 30  ? 18.356 -1.137  18.016  0.66 25.12 ?  30  VAL   A H    1 
ATOM   852  H  H    B VAL   A 1 30  ? 18.420 -1.098  17.991  0.34 27.97 ?  30  VAL   A H    1 
ATOM   853  H  HA   A VAL   A 1 30  ? 18.756 -2.938  19.938  0.66 24.74 ?  30  VAL   A HA   1 
ATOM   854  H  HA   B VAL   A 1 30  ? 18.742 -2.909  19.936  0.34 26.86 ?  30  VAL   A HA   1 
ATOM   855  H  HB   A VAL   A 1 30  ? 19.100 -3.148  17.142  0.66 25.69 ?  30  VAL   A HB   1 
ATOM   856  H  HB   B VAL   A 1 30  ? 19.157 -3.158  17.149  0.34 27.49 ?  30  VAL   A HB   1 
ATOM   857  H  HG11 A VAL   A 1 30  ? 19.283 -5.519  17.578  0.66 25.80 ?  30  VAL   A HG11 1 
ATOM   858  H  HG11 B VAL   A 1 30  ? 19.218 -5.521  17.606  0.34 27.76 ?  30  VAL   A HG11 1 
ATOM   859  H  HG12 A VAL   A 1 30  ? 20.577 -4.659  17.902  0.66 25.80 ?  30  VAL   A HG12 1 
ATOM   860  H  HG12 B VAL   A 1 30  ? 20.524 -4.721  18.022  0.34 27.76 ?  30  VAL   A HG12 1 
ATOM   861  H  HG13 A VAL   A 1 30  ? 19.609 -5.116  19.078  0.66 25.80 ?  30  VAL   A HG13 1 
ATOM   862  H  HG13 B VAL   A 1 30  ? 19.457 -5.131  19.126  0.34 27.76 ?  30  VAL   A HG13 1 
ATOM   863  H  HG21 A VAL   A 1 30  ? 17.199 -4.510  17.210  0.66 26.84 ?  30  VAL   A HG21 1 
ATOM   864  H  HG21 B VAL   A 1 30  ? 17.188 -4.448  17.176  0.34 27.98 ?  30  VAL   A HG21 1 
ATOM   865  H  HG22 A VAL   A 1 30  ? 17.077 -4.243  18.771  0.66 26.84 ?  30  VAL   A HG22 1 
ATOM   866  H  HG22 B VAL   A 1 30  ? 17.000 -4.083  18.710  0.34 27.98 ?  30  VAL   A HG22 1 
ATOM   867  H  HG23 A VAL   A 1 30  ? 16.869 -3.050  17.743  0.66 26.84 ?  30  VAL   A HG23 1 
ATOM   868  H  HG23 B VAL   A 1 30  ? 16.912 -2.945  17.606  0.34 27.98 ?  30  VAL   A HG23 1 
ATOM   869  N  N    . LYS   A 1 31  ? 21.268 -1.466  18.638  1.00 19.73 ?  31  LYS   A N    1 
ATOM   870  C  CA   . LYS   A 1 31  ? 22.721 -1.340  18.612  1.00 20.45 ?  31  LYS   A CA   1 
ATOM   871  C  C    . LYS   A 1 31  ? 23.349 -2.698  18.285  1.00 17.92 ?  31  LYS   A C    1 
ATOM   872  O  O    . LYS   A 1 31  ? 24.121 -3.243  19.082  1.00 19.40 ?  31  LYS   A O    1 
ATOM   873  C  CB   . LYS   A 1 31  ? 23.286 -0.769  19.904  1.00 25.40 ?  31  LYS   A CB   1 
ATOM   874  C  CG   . LYS   A 1 31  ? 22.617 0.517   20.349  1.00 32.18 ?  31  LYS   A CG   1 
ATOM   875  C  CD   . LYS   A 1 31  ? 23.627 1.520   20.880  1.00 37.43 ?  31  LYS   A CD   1 
ATOM   876  C  CE   . LYS   A 1 31  ? 22.961 2.553   21.774  1.00 40.79 ?  31  LYS   A CE   1 
ATOM   877  N  NZ   . LYS   A 1 31  ? 21.816 3.234   21.111  1.00 42.72 ?  31  LYS   A NZ   1 
ATOM   878  H  H    A LYS   A 1 31  ? 20.865 -0.889  18.151  0.66 23.69 ?  31  LYS   A H    1 
ATOM   879  H  H    B LYS   A 1 31  ? 20.867 -0.893  18.144  0.34 23.69 ?  31  LYS   A H    1 
ATOM   880  H  HA   . LYS   A 1 31  ? 22.954 -0.729  17.904  1.00 24.54 ?  31  LYS   A HA   1 
ATOM   881  H  HB2  . LYS   A 1 31  ? 23.165 -1.431  20.589  1.00 30.49 ?  31  LYS   A HB2  1 
ATOM   882  H  HB3  . LYS   A 1 31  ? 24.234 -0.590  19.781  1.00 30.49 ?  31  LYS   A HB3  1 
ATOM   883  H  HG2  . LYS   A 1 31  ? 22.160 0.917   19.593  1.00 38.62 ?  31  LYS   A HG2  1 
ATOM   884  H  HG3  . LYS   A 1 31  ? 21.985 0.319   21.058  1.00 38.62 ?  31  LYS   A HG3  1 
ATOM   885  H  HD2  . LYS   A 1 31  ? 24.300 1.054   21.401  1.00 44.93 ?  31  LYS   A HD2  1 
ATOM   886  H  HD3  . LYS   A 1 31  ? 24.042 1.983   20.134  1.00 44.93 ?  31  LYS   A HD3  1 
ATOM   887  H  HE2  . LYS   A 1 31  ? 22.628 2.111   22.570  1.00 48.95 ?  31  LYS   A HE2  1 
ATOM   888  H  HE3  . LYS   A 1 31  ? 23.613 3.228   22.016  1.00 48.95 ?  31  LYS   A HE3  1 
ATOM   889  H  HZ1  . LYS   A 1 31  ? 21.472 3.849   21.655  1.00 51.27 ?  31  LYS   A HZ1  1 
ATOM   890  H  HZ2  . LYS   A 1 31  ? 22.089 3.631   20.363  1.00 51.27 ?  31  LYS   A HZ2  1 
ATOM   891  H  HZ3  . LYS   A 1 31  ? 21.183 2.641   20.909  1.00 51.27 ?  31  LYS   A HZ3  1 
ATOM   892  N  N    . PRO   A 1 32  ? 23.036 -3.257  17.122  1.00 15.68 ?  32  PRO   A N    1 
ATOM   893  C  CA   . PRO   A 1 32  ? 23.521 -4.594  16.781  1.00 16.24 ?  32  PRO   A CA   1 
ATOM   894  C  C    . PRO   A 1 32  ? 25.022 -4.600  16.575  1.00 16.21 ?  32  PRO   A C    1 
ATOM   895  O  O    . PRO   A 1 32  ? 25.656 -3.567  16.349  1.00 16.00 ?  32  PRO   A O    1 
ATOM   896  C  CB   . PRO   A 1 32  ? 22.800 -4.892  15.463  1.00 16.73 ?  32  PRO   A CB   1 
ATOM   897  C  CG   . PRO   A 1 32  ? 22.647 -3.534  14.840  1.00 15.27 ?  32  PRO   A CG   1 
ATOM   898  C  CD   . PRO   A 1 32  ? 22.305 -2.646  16.001  1.00 15.23 ?  32  PRO   A CD   1 
ATOM   899  H  HA   . PRO   A 1 32  ? 23.273 -5.243  17.454  1.00 19.50 ?  32  PRO   A HA   1 
ATOM   900  H  HB2  . PRO   A 1 32  ? 23.345 -5.477  14.906  1.00 20.08 ?  32  PRO   A HB2  1 
ATOM   901  H  HB3  . PRO   A 1 32  ? 21.934 -5.295  15.640  1.00 20.08 ?  32  PRO   A HB3  1 
ATOM   902  H  HG2  . PRO   A 1 32  ? 23.486 -3.270  14.424  1.00 18.33 ?  32  PRO   A HG2  1 
ATOM   903  H  HG3  . PRO   A 1 32  ? 21.931 -3.555  14.182  1.00 18.33 ?  32  PRO   A HG3  1 
ATOM   904  H  HD2  . PRO   A 1 32  ? 22.623 -1.746  15.826  1.00 18.28 ?  32  PRO   A HD2  1 
ATOM   905  H  HD3  . PRO   A 1 32  ? 21.351 -2.665  16.158  1.00 18.28 ?  32  PRO   A HD3  1 
ATOM   906  N  N    . THR   A 1 33  ? 25.587 -5.805  16.625  1.00 16.07 ?  33  THR   A N    1 
ATOM   907  C  CA   . THR   A 1 33  ? 26.999 -5.960  16.303  1.00 16.30 ?  33  THR   A CA   1 
ATOM   908  C  C    . THR   A 1 33  ? 27.289 -5.509  14.878  1.00 14.79 ?  33  THR   A C    1 
ATOM   909  O  O    . THR   A 1 33  ? 28.313 -4.859  14.622  1.00 15.20 ?  33  THR   A O    1 
ATOM   910  C  CB   . THR   A 1 33  ? 27.412 -7.415  16.518  1.00 18.13 ?  33  THR   A CB   1 
ATOM   911  O  OG1  . THR   A 1 33  ? 27.120 -7.789  17.868  1.00 19.80 ?  33  THR   A OG1  1 
ATOM   912  C  CG2  . THR   A 1 33  ? 28.902 -7.601  16.260  1.00 19.03 ?  33  THR   A CG2  1 
ATOM   913  H  H    . THR   A 1 33  ? 25.184 -6.534  16.834  1.00 19.30 ?  33  THR   A H    1 
ATOM   914  H  HA   . THR   A 1 33  ? 27.525 -5.414  16.906  1.00 19.56 ?  33  THR   A HA   1 
ATOM   915  H  HB   . THR   A 1 33  ? 26.923 -7.995  15.911  1.00 21.76 ?  33  THR   A HB   1 
ATOM   916  H  HG1  . THR   A 1 33  ? 27.557 -7.304  18.403  1.00 23.77 ?  33  THR   A HG1  1 
ATOM   917  H  HG21 . THR   A 1 33  ? 29.184 -8.484  16.550  1.00 22.85 ?  33  THR   A HG21 1 
ATOM   918  H  HG22 . THR   A 1 33  ? 29.091 -7.508  15.313  1.00 22.85 ?  33  THR   A HG22 1 
ATOM   919  H  HG23 . THR   A 1 33  ? 29.408 -6.935  16.751  1.00 22.85 ?  33  THR   A HG23 1 
ATOM   920  N  N    . VAL   A 1 34  ? 26.396 -5.831  13.939  1.00 13.69 ?  34  VAL   A N    1 
ATOM   921  C  CA   . VAL   A 1 34  ? 26.584 -5.492  12.532  1.00 12.68 ?  34  VAL   A CA   1 
ATOM   922  C  C    . VAL   A 1 34  ? 25.279 -4.941  11.971  1.00 12.05 ?  34  VAL   A C    1 
ATOM   923  O  O    . VAL   A 1 34  ? 24.242 -5.613  12.025  1.00 12.87 ?  34  VAL   A O    1 
ATOM   924  C  CB   . VAL   A 1 34  ? 27.043 -6.697  11.687  1.00 13.42 ?  34  VAL   A CB   1 
ATOM   925  C  CG1  . VAL   A 1 34  ? 27.221 -6.294  10.230  1.00 13.30 ?  34  VAL   A CG1  1 
ATOM   926  C  CG2  . VAL   A 1 34  ? 28.331 -7.308  12.240  1.00 14.40 ?  34  VAL   A CG2  1 
ATOM   927  H  H    . VAL   A 1 34  ? 25.669 -6.262  14.097  1.00 16.44 ?  34  VAL   A H    1 
ATOM   928  H  HA   . VAL   A 1 34  ? 27.260 -4.799  12.457  1.00 15.23 ?  34  VAL   A HA   1 
ATOM   929  H  HB   . VAL   A 1 34  ? 26.354 -7.379  11.721  1.00 16.11 ?  34  VAL   A HB   1 
ATOM   930  H  HG11 . VAL   A 1 34  ? 27.708 -6.995  9.767   1.00 15.97 ?  34  VAL   A HG11 1 
ATOM   931  H  HG12 . VAL   A 1 34  ? 26.351 -6.172  9.821   1.00 15.97 ?  34  VAL   A HG12 1 
ATOM   932  H  HG13 . VAL   A 1 34  ? 27.726 -5.465  10.191  1.00 15.97 ?  34  VAL   A HG13 1 
ATOM   933  H  HG21 . VAL   A 1 34  ? 28.604 -8.041  11.668  1.00 17.29 ?  34  VAL   A HG21 1 
ATOM   934  H  HG22 . VAL   A 1 34  ? 29.022 -6.626  12.255  1.00 17.29 ?  34  VAL   A HG22 1 
ATOM   935  H  HG23 . VAL   A 1 34  ? 28.168 -7.632  13.139  1.00 17.29 ?  34  VAL   A HG23 1 
ATOM   936  N  N    . VAL   A 1 35  ? 25.334 -3.734  11.412  1.00 11.26 ?  35  VAL   A N    1 
ATOM   937  C  CA   . VAL   A 1 35  ? 24.292 -3.225  10.529  1.00 11.04 ?  35  VAL   A CA   1 
ATOM   938  C  C    . VAL   A 1 35  ? 24.842 -3.219  9.108   1.00 10.51 ?  35  VAL   A C    1 
ATOM   939  O  O    . VAL   A 1 35  ? 25.988 -2.812  8.878   1.00 11.18 ?  35  VAL   A O    1 
ATOM   940  C  CB   . VAL   A 1 35  ? 23.759 -1.834  10.941  1.00 11.70 ?  35  VAL   A CB   1 
ATOM   941  C  CG1  . VAL   A 1 35  ? 24.814 -0.734  10.805  1.00 12.46 ?  35  VAL   A CG1  1 
ATOM   942  C  CG2  . VAL   A 1 35  ? 22.509 -1.480  10.128  1.00 12.66 ?  35  VAL   A CG2  1 
ATOM   943  H  H    . VAL   A 1 35  ? 25.978 -3.177  11.532  1.00 13.52 ?  35  VAL   A H    1 
ATOM   944  H  HA   . VAL   A 1 35  ? 23.537 -3.839  10.552  1.00 13.26 ?  35  VAL   A HA   1 
ATOM   945  H  HB   . VAL   A 1 35  ? 23.490 -1.866  11.870  1.00 14.04 ?  35  VAL   A HB   1 
ATOM   946  H  HG11 . VAL   A 1 35  ? 24.469 0.092   11.181  1.00 14.96 ?  35  VAL   A HG11 1 
ATOM   947  H  HG12 . VAL   A 1 35  ? 25.614 -1.003  11.288  1.00 14.96 ?  35  VAL   A HG12 1 
ATOM   948  H  HG13 . VAL   A 1 35  ? 25.028 -0.604  9.867   1.00 14.96 ?  35  VAL   A HG13 1 
ATOM   949  H  HG21 . VAL   A 1 35  ? 22.157 -0.631  10.437  1.00 15.20 ?  35  VAL   A HG21 1 
ATOM   950  H  HG22 . VAL   A 1 35  ? 22.750 -1.412  9.187   1.00 15.20 ?  35  VAL   A HG22 1 
ATOM   951  H  HG23 . VAL   A 1 35  ? 21.845 -2.176  10.246  1.00 15.20 ?  35  VAL   A HG23 1 
ATOM   952  N  N    . VAL   A 1 36  ? 24.030 -3.682  8.160   1.00 9.76  ?  36  VAL   A N    1 
ATOM   953  C  CA   . VAL   A 1 36  ? 24.401 -3.694  6.753   1.00 9.78  ?  36  VAL   A CA   1 
ATOM   954  C  C    . VAL   A 1 36  ? 23.941 -2.401  6.096   1.00 10.07 ?  36  VAL   A C    1 
ATOM   955  O  O    . VAL   A 1 36  ? 22.780 -1.996  6.239   1.00 10.37 ?  36  VAL   A O    1 
ATOM   956  C  CB   . VAL   A 1 36  ? 23.796 -4.911  6.033   1.00 9.88  ?  36  VAL   A CB   1 
ATOM   957  C  CG1  . VAL   A 1 36  ? 24.059 -4.837  4.551   1.00 10.48 ?  36  VAL   A CG1  1 
ATOM   958  C  CG2  . VAL   A 1 36  ? 24.341 -6.208  6.610   1.00 11.21 ?  36  VAL   A CG2  1 
ATOM   959  H  H    . VAL   A 1 36  ? 23.239 -4.008  8.312   1.00 11.72 ?  36  VAL   A H    1 
ATOM   960  H  HA   . VAL   A 1 36  ? 25.370 -3.755  6.682   1.00 11.74 ?  36  VAL   A HA   1 
ATOM   961  H  HB   . VAL   A 1 36  ? 22.837 -4.905  6.162   1.00 11.86 ?  36  VAL   A HB   1 
ATOM   962  H  HG11 . VAL   A 1 36  ? 23.919 -5.713  4.158   1.00 12.58 ?  36  VAL   A HG11 1 
ATOM   963  H  HG12 . VAL   A 1 36  ? 23.456 -4.194  4.147   1.00 12.58 ?  36  VAL   A HG12 1 
ATOM   964  H  HG13 . VAL   A 1 36  ? 24.982 -4.559  4.406   1.00 12.58 ?  36  VAL   A HG13 1 
ATOM   965  H  HG21 . VAL   A 1 36  ? 23.946 -6.958  6.132   1.00 13.45 ?  36  VAL   A HG21 1 
ATOM   966  H  HG22 . VAL   A 1 36  ? 25.304 -6.223  6.508   1.00 13.45 ?  36  VAL   A HG22 1 
ATOM   967  H  HG23 . VAL   A 1 36  ? 24.105 -6.260  7.550   1.00 13.45 ?  36  VAL   A HG23 1 
ATOM   968  N  N    . ASN   A 1 37  ? 24.848 -1.770  5.351   1.00 9.53  ?  37  ASN   A N    1 
ATOM   969  C  CA   . ASN   A 1 37  ? 24.509 -0.649  4.487   1.00 9.66  ?  37  ASN   A CA   1 
ATOM   970  C  C    . ASN   A 1 37  ? 24.378 -1.115  3.048   1.00 9.36  ?  37  ASN   A C    1 
ATOM   971  O  O    . ASN   A 1 37  ? 25.165 -1.945  2.570   1.00 9.92  ?  37  ASN   A O    1 
ATOM   972  C  CB   . ASN   A 1 37  ? 25.583 0.437   4.567   1.00 9.84  ?  37  ASN   A CB   1 
ATOM   973  C  CG   . ASN   A 1 37  ? 25.249 1.631   3.719   1.00 10.10 ?  37  ASN   A CG   1 
ATOM   974  O  OD1  . ASN   A 1 37  ? 24.073 1.960   3.547   1.00 10.78 ?  37  ASN   A OD1  1 
ATOM   975  N  ND2  . ASN   A 1 37  ? 26.274 2.300   3.192   1.00 10.24 ?  37  ASN   A ND2  1 
ATOM   976  H  H    . ASN   A 1 37  ? 25.688 -1.976  5.339   1.00 11.45 ?  37  ASN   A H    1 
ATOM   977  H  HA   . ASN   A 1 37  ? 23.666 -0.266  4.774   1.00 11.60 ?  37  ASN   A HA   1 
ATOM   978  H  HB2  . ASN   A 1 37  ? 25.669 0.733   5.491   1.00 11.82 ?  37  ASN   A HB2  1 
ATOM   979  H  HB3  . ASN   A 1 37  ? 26.430 0.070   4.261   1.00 11.82 ?  37  ASN   A HB3  1 
ATOM   980  H  HD21 . ASN   A 1 37  ? 26.130 2.985   2.698   1.00 12.30 ?  37  ASN   A HD21 1 
ATOM   981  H  HD22 . ASN   A 1 37  ? 27.077 2.039   3.336   1.00 12.30 ?  37  ASN   A HD22 1 
ATOM   982  N  N    A ALA   A 1 38  ? 23.360 -0.573  2.370   0.66 9.81  ?  38  ALA   A N    1 
ATOM   983  N  N    B ALA   A 1 38  ? 23.361 -0.603  2.354   0.34 10.12 ?  38  ALA   A N    1 
ATOM   984  C  CA   A ALA   A 1 38  ? 23.159 -0.704  0.928   0.66 9.77  ?  38  ALA   A CA   1 
ATOM   985  C  CA   B ALA   A 1 38  ? 23.197 -0.866  0.924   0.34 10.85 ?  38  ALA   A CA   1 
ATOM   986  C  C    A ALA   A 1 38  ? 24.079 0.290   0.219   0.66 9.61  ?  38  ALA   A C    1 
ATOM   987  C  C    B ALA   A 1 38  ? 24.011 0.173   0.154   0.34 10.68 ?  38  ALA   A C    1 
ATOM   988  O  O    A ALA   A 1 38  ? 23.679 1.390   -0.171  0.66 9.47  ?  38  ALA   A O    1 
ATOM   989  O  O    B ALA   A 1 38  ? 23.499 1.175   -0.350  0.34 10.57 ?  38  ALA   A O    1 
ATOM   990  C  CB   A ALA   A 1 38  ? 21.697 -0.442  0.578   0.66 10.65 ?  38  ALA   A CB   1 
ATOM   991  C  CB   B ALA   A 1 38  ? 21.724 -0.849  0.536   0.34 11.65 ?  38  ALA   A CB   1 
ATOM   992  H  H    A ALA   A 1 38  ? 22.756 -0.092  2.747   0.66 11.78 ?  38  ALA   A H    1 
ATOM   993  H  H    B ALA   A 1 38  ? 22.752 -0.097  2.692   0.34 12.15 ?  38  ALA   A H    1 
ATOM   994  H  HA   A ALA   A 1 38  ? 23.394 -1.600  0.645   0.66 11.73 ?  38  ALA   A HA   1 
ATOM   995  H  HA   B ALA   A 1 38  ? 23.555 -1.747  0.720   0.34 13.02 ?  38  ALA   A HA   1 
ATOM   996  H  HB1  A ALA   A 1 38  ? 21.571 -0.576  -0.373  0.66 12.79 ?  38  ALA   A HB1  1 
ATOM   997  H  HB1  B ALA   A 1 38  ? 21.657 -0.920  -0.428  0.34 13.99 ?  38  ALA   A HB1  1 
ATOM   998  H  HB2  A ALA   A 1 38  ? 21.139 -1.058  1.078   0.66 12.79 ?  38  ALA   A HB2  1 
ATOM   999  H  HB2  B ALA   A 1 38  ? 21.274 -1.600  0.957   0.34 13.99 ?  38  ALA   A HB2  1 
ATOM   1000 H  HB3  A ALA   A 1 38  ? 21.476 0.473   0.816   0.66 12.79 ?  38  ALA   A HB3  1 
ATOM   1001 H  HB3  B ALA   A 1 38  ? 21.332 -0.015  0.833   0.34 13.99 ?  38  ALA   A HB3  1 
ATOM   1002 N  N    A ALA   A 1 39  ? 25.338 -0.113  0.051   0.66 9.90  ?  39  ALA   A N    1 
ATOM   1003 N  N    B ALA   A 1 39  ? 25.311 -0.084  0.066   0.34 10.84 ?  39  ALA   A N    1 
ATOM   1004 C  CA   A ALA   A 1 39  ? 26.402 0.762   -0.412  0.66 9.35  ?  39  ALA   A CA   1 
ATOM   1005 C  CA   B ALA   A 1 39  ? 26.258 0.885   -0.459  0.34 10.70 ?  39  ALA   A CA   1 
ATOM   1006 C  C    A ALA   A 1 39  ? 26.532 0.733   -1.932  0.66 9.68  ?  39  ALA   A C    1 
ATOM   1007 C  C    B ALA   A 1 39  ? 26.427 0.729   -1.966  0.34 10.14 ?  39  ALA   A C    1 
ATOM   1008 O  O    A ALA   A 1 39  ? 26.028 -0.165  -2.616  0.66 10.43 ?  39  ALA   A O    1 
ATOM   1009 O  O    B ALA   A 1 39  ? 26.074 -0.295  -2.559  0.34 10.10 ?  39  ALA   A O    1 
ATOM   1010 C  CB   A ALA   A 1 39  ? 27.729 0.333   0.220   0.66 10.00 ?  39  ALA   A CB   1 
ATOM   1011 C  CB   B ALA   A 1 39  ? 27.613 0.711   0.225   0.34 11.58 ?  39  ALA   A CB   1 
ATOM   1012 H  H    A ALA   A 1 39  ? 25.606 -0.920  0.209   0.66 11.89 ?  39  ALA   A H    1 
ATOM   1013 H  H    B ALA   A 1 39  ? 25.671 -0.831  0.304   0.34 13.01 ?  39  ALA   A H    1 
ATOM   1014 H  HA   A ALA   A 1 39  ? 26.212 1.673   -0.136  0.66 11.23 ?  39  ALA   A HA   1 
ATOM   1015 H  HA   B ALA   A 1 39  ? 25.930 1.779   -0.272  0.34 12.85 ?  39  ALA   A HA   1 
ATOM   1016 H  HB1  A ALA   A 1 39  ? 28.431 0.923   -0.093  0.66 12.01 ?  39  ALA   A HB1  1 
ATOM   1017 H  HB1  B ALA   A 1 39  ? 28.231 1.366   -0.136  0.34 13.91 ?  39  ALA   A HB1  1 
ATOM   1018 H  HB2  A ALA   A 1 39  ? 27.651 0.395   1.187   0.66 12.01 ?  39  ALA   A HB2  1 
ATOM   1019 H  HB2  B ALA   A 1 39  ? 27.505 0.849   1.179   0.34 13.91 ?  39  ALA   A HB2  1 
ATOM   1020 H  HB3  A ALA   A 1 39  ? 27.919 -0.581  -0.038  0.66 12.01 ?  39  ALA   A HB3  1 
ATOM   1021 H  HB3  B ALA   A 1 39  ? 27.940 -0.185  0.054   0.34 13.91 ?  39  ALA   A HB3  1 
ATOM   1022 N  N    A ASN   A 1 40  ? 27.236 1.739   -2.455  0.66 9.71  ?  40  ASN   A N    1 
ATOM   1023 N  N    B ASN   A 1 40  ? 26.976 1.772   -2.582  0.34 9.93  ?  40  ASN   A N    1 
ATOM   1024 C  CA   A ASN   A 1 40  ? 27.783 1.695   -3.804  0.66 10.03 ?  40  ASN   A CA   1 
ATOM   1025 C  CA   B ASN   A 1 40  ? 27.470 1.703   -3.948  0.34 9.91  ?  40  ASN   A CA   1 
ATOM   1026 C  C    A ASN   A 1 40  ? 29.307 1.589   -3.739  0.66 9.56  ?  40  ASN   A C    1 
ATOM   1027 C  C    B ASN   A 1 40  ? 28.994 1.572   -3.929  0.34 9.70  ?  40  ASN   A C    1 
ATOM   1028 O  O    A ASN   A 1 40  ? 29.913 1.706   -2.672  0.66 10.06 ?  40  ASN   A O    1 
ATOM   1029 O  O    B ASN   A 1 40  ? 29.636 1.642   -2.880  0.34 9.37  ?  40  ASN   A O    1 
ATOM   1030 C  CB   A ASN   A 1 40  ? 27.294 2.872   -4.666  0.66 11.47 ?  40  ASN   A CB   1 
ATOM   1031 C  CB   B ASN   A 1 40  ? 27.020 2.928   -4.754  0.34 10.61 ?  40  ASN   A CB   1 
ATOM   1032 C  CG   A ASN   A 1 40  ? 27.638 4.226   -4.083  0.66 13.30 ?  40  ASN   A CG   1 
ATOM   1033 C  CG   B ASN   A 1 40  ? 27.449 4.237   -4.122  0.34 11.22 ?  40  ASN   A CG   1 
ATOM   1034 O  OD1  A ASN   A 1 40  ? 28.785 4.481   -3.713  0.66 14.03 ?  40  ASN   A OD1  1 
ATOM   1035 O  OD1  B ASN   A 1 40  ? 28.643 4.526   -4.019  0.34 10.91 ?  40  ASN   A OD1  1 
ATOM   1036 N  ND2  A ASN   A 1 40  ? 26.639 5.112   -4.009  0.66 13.67 ?  40  ASN   A ND2  1 
ATOM   1037 N  ND2  B ASN   A 1 40  ? 26.472 5.048   -3.714  0.34 11.79 ?  40  ASN   A ND2  1 
ATOM   1038 H  H    A ASN   A 1 40  ? 27.411 2.471   -2.038  0.66 11.66 ?  40  ASN   A H    1 
ATOM   1039 H  H    B ASN   A 1 40  ? 27.065 2.549   -2.219  0.34 11.93 ?  40  ASN   A H    1 
ATOM   1040 H  HA   A ASN   A 1 40  ? 27.467 0.888   -4.231  0.66 12.05 ?  40  ASN   A HA   1 
ATOM   1041 H  HA   B ASN   A 1 40  ? 27.091 0.912   -4.377  0.34 11.90 ?  40  ASN   A HA   1 
ATOM   1042 H  HB2  A ASN   A 1 40  ? 27.699 2.804   -5.550  0.66 13.77 ?  40  ASN   A HB2  1 
ATOM   1043 H  HB2  B ASN   A 1 40  ? 27.410 2.881   -5.636  0.34 12.74 ?  40  ASN   A HB2  1 
ATOM   1044 H  HB3  A ASN   A 1 40  ? 26.329 2.821   -4.748  0.66 13.77 ?  40  ASN   A HB3  1 
ATOM   1045 H  HB3  B ASN   A 1 40  ? 26.053 2.918   -4.819  0.34 12.74 ?  40  ASN   A HB3  1 
ATOM   1046 H  HD21 A ASN   A 1 40  ? 26.784 5.901   -3.696  0.66 16.41 ?  40  ASN   A HD21 1 
ATOM   1047 H  HD21 B ASN   A 1 40  ? 26.667 5.802   -3.347  0.34 14.15 ?  40  ASN   A HD21 1 
ATOM   1048 H  HD22 A ASN   A 1 40  ? 25.849 4.891   -4.265  0.66 16.41 ?  40  ASN   A HD22 1 
ATOM   1049 H  HD22 B ASN   A 1 40  ? 25.650 4.818   -3.813  0.34 14.15 ?  40  ASN   A HD22 1 
ATOM   1050 N  N    A VAL   A 1 41  ? 29.926 1.333   -4.894  0.66 9.69  ?  41  VAL   A N    1 
ATOM   1051 N  N    B VAL   A 1 41  ? 29.578 1.375   -5.112  0.34 9.94  ?  41  VAL   A N    1 
ATOM   1052 C  CA   A VAL   A 1 41  ? 31.351 1.013   -4.907  0.66 10.26 ?  41  VAL   A CA   1 
ATOM   1053 C  CA   B VAL   A 1 41  ? 31.007 1.077   -5.181  0.34 10.07 ?  41  VAL   A CA   1 
ATOM   1054 C  C    A VAL   A 1 41  ? 32.203 2.173   -4.436  0.66 10.22 ?  41  VAL   A C    1 
ATOM   1055 C  C    B VAL   A 1 41  ? 31.886 2.223   -4.691  0.34 9.84  ?  41  VAL   A C    1 
ATOM   1056 O  O    A VAL   A 1 41  ? 33.333 1.959   -3.982  0.66 10.98 ?  41  VAL   A O    1 
ATOM   1057 O  O    B VAL   A 1 41  ? 33.057 1.998   -4.364  0.34 10.09 ?  41  VAL   A O    1 
ATOM   1058 C  CB   A VAL   A 1 41  ? 31.848 0.516   -6.285  0.66 10.99 ?  41  VAL   A CB   1 
ATOM   1059 C  CB   B VAL   A 1 41  ? 31.424 0.647   -6.601  0.34 10.71 ?  41  VAL   A CB   1 
ATOM   1060 C  CG1  A VAL   A 1 41  ? 31.139 -0.771  -6.693  0.66 11.42 ?  41  VAL   A CG1  1 
ATOM   1061 C  CG1  B VAL   A 1 41  ? 30.720 -0.639  -6.998  0.34 11.67 ?  41  VAL   A CG1  1 
ATOM   1062 C  CG2  A VAL   A 1 41  ? 31.725 1.596   -7.358  0.66 11.17 ?  41  VAL   A CG2  1 
ATOM   1063 C  CG2  B VAL   A 1 41  ? 31.147 1.756   -7.610  0.34 10.78 ?  41  VAL   A CG2  1 
ATOM   1064 H  H    A VAL   A 1 41  ? 29.557 1.336   -5.665  0.66 11.63 ?  41  VAL   A H    1 
ATOM   1065 H  H    B VAL   A 1 41  ? 29.165 1.384   -5.868  0.34 11.93 ?  41  VAL   A H    1 
ATOM   1066 H  HA   A VAL   A 1 41  ? 31.508 0.290   -4.281  0.66 12.32 ?  41  VAL   A HA   1 
ATOM   1067 H  HA   B VAL   A 1 41  ? 31.171 0.320   -4.595  0.34 12.09 ?  41  VAL   A HA   1 
ATOM   1068 H  HB   A VAL   A 1 41  ? 32.795 0.306   -6.209  0.66 13.20 ?  41  VAL   A HB   1 
ATOM   1069 H  HB   B VAL   A 1 41  ? 32.379 0.474   -6.599  0.34 12.86 ?  41  VAL   A HB   1 
ATOM   1070 H  HG11 A VAL   A 1 41  ? 31.479 -1.064  -7.552  0.66 13.71 ?  41  VAL   A HG11 1 
ATOM   1071 H  HG11 B VAL   A 1 41  ? 30.916 -0.829  -7.927  0.34 14.01 ?  41  VAL   A HG11 1 
ATOM   1072 H  HG12 A VAL   A 1 41  ? 31.301 -1.449  -6.021  0.66 13.71 ?  41  VAL   A HG12 1 
ATOM   1073 H  HG12 B VAL   A 1 41  ? 31.044 -1.362  -6.436  0.34 14.01 ?  41  VAL   A HG12 1 
ATOM   1074 H  HG13 A VAL   A 1 41  ? 30.184 -0.594  -6.760  0.66 13.71 ?  41  VAL   A HG13 1 
ATOM   1075 H  HG13 B VAL   A 1 41  ? 29.766 -0.532  -6.876  0.34 14.01 ?  41  VAL   A HG13 1 
ATOM   1076 H  HG21 A VAL   A 1 41  ? 31.939 1.206   -8.224  0.66 13.41 ?  41  VAL   A HG21 1 
ATOM   1077 H  HG21 B VAL   A 1 41  ? 31.406 1.446   -8.492  0.34 12.95 ?  41  VAL   A HG21 1 
ATOM   1078 H  HG22 A VAL   A 1 41  ? 30.822 1.936   -7.362  0.66 13.41 ?  41  VAL   A HG22 1 
ATOM   1079 H  HG22 B VAL   A 1 41  ? 30.200 1.965   -7.600  0.34 12.95 ?  41  VAL   A HG22 1 
ATOM   1080 H  HG23 A VAL   A 1 41  ? 32.352 2.312   -7.161  0.66 13.41 ?  41  VAL   A HG23 1 
ATOM   1081 H  HG23 B VAL   A 1 41  ? 31.663 2.540   -7.370  0.34 12.95 ?  41  VAL   A HG23 1 
ATOM   1082 N  N    A TYR   A 1 42  ? 31.703 3.401   -4.554  0.66 10.48 ?  42  TYR   A N    1 
ATOM   1083 N  N    B TYR   A 1 42  ? 31.367 3.453   -4.658  0.34 9.97  ?  42  TYR   A N    1 
ATOM   1084 C  CA   A TYR   A 1 42  ? 32.426 4.590   -4.124  0.66 11.14 ?  42  TYR   A CA   1 
ATOM   1085 C  CA   B TYR   A 1 42  ? 32.147 4.624   -4.265  0.34 9.99  ?  42  TYR   A CA   1 
ATOM   1086 C  C    A TYR   A 1 42  ? 32.124 4.952   -2.683  0.66 10.94 ?  42  TYR   A C    1 
ATOM   1087 C  C    B TYR   A 1 42  ? 31.965 5.009   -2.801  0.34 10.31 ?  42  TYR   A C    1 
ATOM   1088 O  O    A TYR   A 1 42  ? 32.698 5.920   -2.162  0.66 11.65 ?  42  TYR   A O    1 
ATOM   1089 O  O    B TYR   A 1 42  ? 32.498 6.040   -2.373  0.34 10.52 ?  42  TYR   A O    1 
ATOM   1090 C  CB   A TYR   A 1 42  ? 32.108 5.780   -5.051  0.66 11.68 ?  42  TYR   A CB   1 
ATOM   1091 C  CB   B TYR   A 1 42  ? 31.789 5.821   -5.154  0.34 10.35 ?  42  TYR   A CB   1 
ATOM   1092 C  CG   A TYR   A 1 42  ? 32.281 5.458   -6.522  0.66 12.08 ?  42  TYR   A CG   1 
ATOM   1093 C  CG   B TYR   A 1 42  ? 31.919 5.534   -6.632  0.34 11.22 ?  42  TYR   A CG   1 
ATOM   1094 C  CD1  A TYR   A 1 42  ? 33.542 5.269   -7.067  0.66 12.84 ?  42  TYR   A CD1  1 
ATOM   1095 C  CD1  B TYR   A 1 42  ? 33.163 5.327   -7.212  0.34 11.41 ?  42  TYR   A CD1  1 
ATOM   1096 C  CD2  A TYR   A 1 42  ? 31.181 5.314   -7.363  0.66 13.25 ?  42  TYR   A CD2  1 
ATOM   1097 C  CD2  B TYR   A 1 42  ? 30.797 5.468   -7.448  0.34 12.45 ?  42  TYR   A CD2  1 
ATOM   1098 C  CE1  A TYR   A 1 42  ? 33.708 4.961   -8.406  0.66 13.47 ?  42  TYR   A CE1  1 
ATOM   1099 C  CE1  B TYR   A 1 42  ? 33.286 5.059   -8.563  0.34 11.52 ?  42  TYR   A CE1  1 
ATOM   1100 C  CE2  A TYR   A 1 42  ? 31.341 5.011   -8.707  0.66 14.01 ?  42  TYR   A CE2  1 
ATOM   1101 C  CE2  B TYR   A 1 42  ? 30.910 5.207   -8.802  0.34 12.79 ?  42  TYR   A CE2  1 
ATOM   1102 C  CZ   A TYR   A 1 42  ? 32.609 4.834   -9.222  0.66 13.96 ?  42  TYR   A CZ   1 
ATOM   1103 C  CZ   B TYR   A 1 42  ? 32.157 5.000   -9.355  0.34 12.46 ?  42  TYR   A CZ   1 
ATOM   1104 O  OH   A TYR   A 1 42  ? 32.781 4.530   -10.553 0.66 15.33 ?  42  TYR   A OH   1 
ATOM   1105 O  OH   B TYR   A 1 42  ? 32.277 4.744   -10.702 0.34 13.08 ?  42  TYR   A OH   1 
ATOM   1106 H  H    A TYR   A 1 42  ? 30.930 3.570   -4.883  0.66 12.58 ?  42  TYR   A H    1 
ATOM   1107 H  H    B TYR   A 1 42  ? 30.552 3.639   -4.882  0.34 11.97 ?  42  TYR   A H    1 
ATOM   1108 H  HA   A TYR   A 1 42  ? 33.378 4.421   -4.186  0.66 13.37 ?  42  TYR   A HA   1 
ATOM   1109 H  HA   B TYR   A 1 42  ? 33.084 4.426   -4.409  0.34 11.99 ?  42  TYR   A HA   1 
ATOM   1110 H  HB2  A TYR   A 1 42  ? 31.191 6.054   -4.914  0.66 14.02 ?  42  TYR   A HB2  1 
ATOM   1111 H  HB2  B TYR   A 1 42  ? 30.870 6.081   -4.982  0.34 12.43 ?  42  TYR   A HB2  1 
ATOM   1112 H  HB3  A TYR   A 1 42  ? 32.708 6.516   -4.839  0.66 14.02 ?  42  TYR   A HB3  1 
ATOM   1113 H  HB3  B TYR   A 1 42  ? 32.384 6.560   -4.942  0.34 12.43 ?  42  TYR   A HB3  1 
ATOM   1114 H  HD1  A TYR   A 1 42  ? 34.293 5.353   -6.525  0.66 15.41 ?  42  TYR   A HD1  1 
ATOM   1115 H  HD1  B TYR   A 1 42  ? 33.927 5.364   -6.682  0.34 13.69 ?  42  TYR   A HD1  1 
ATOM   1116 H  HD2  A TYR   A 1 42  ? 30.324 5.438   -7.021  0.66 15.91 ?  42  TYR   A HD2  1 
ATOM   1117 H  HD2  B TYR   A 1 42  ? 29.955 5.609   -7.080  0.34 14.95 ?  42  TYR   A HD2  1 
ATOM   1118 H  HE1  A TYR   A 1 42  ? 34.562 4.841   -8.759  0.66 16.18 ?  42  TYR   A HE1  1 
ATOM   1119 H  HE1  B TYR   A 1 42  ? 34.127 4.919   -8.937  0.34 13.83 ?  42  TYR   A HE1  1 
ATOM   1120 H  HE2  A TYR   A 1 42  ? 30.592 4.926   -9.259  0.66 16.82 ?  42  TYR   A HE2  1 
ATOM   1121 H  HE2  B TYR   A 1 42  ? 30.150 5.164   -9.337  0.34 15.36 ?  42  TYR   A HE2  1 
ATOM   1122 H  HH   A TYR   A 1 42  ? 33.596 4.398   -10.714 0.66 18.40 ?  42  TYR   A HH   1 
ATOM   1123 H  HH   B TYR   A 1 42  ? 31.518 4.729   -11.061 0.34 15.70 ?  42  TYR   A HH   1 
ATOM   1124 N  N    . LEU   A 1 43  ? 31.221 4.213   -2.035  1.00 10.77 ?  43  LEU   A N    1 
ATOM   1125 C  CA   . LEU   A 1 43  ? 30.784 4.548   -0.682  1.00 10.57 ?  43  LEU   A CA   1 
ATOM   1126 C  C    . LEU   A 1 43  ? 30.295 5.994   -0.588  1.00 10.86 ?  43  LEU   A C    1 
ATOM   1127 O  O    . LEU   A 1 43  ? 30.556 6.693   0.393   1.00 11.62 ?  43  LEU   A O    1 
ATOM   1128 C  CB   . LEU   A 1 43  ? 31.842 4.242   0.376   1.00 11.11 ?  43  LEU   A CB   1 
ATOM   1129 C  CG   . LEU   A 1 43  ? 32.335 2.794   0.455   1.00 11.34 ?  43  LEU   A CG   1 
ATOM   1130 C  CD1  . LEU   A 1 43  ? 33.387 2.684   1.540   1.00 12.17 ?  43  LEU   A CD1  1 
ATOM   1131 C  CD2  . LEU   A 1 43  ? 31.195 1.803   0.711   1.00 11.36 ?  43  LEU   A CD2  1 
ATOM   1132 H  H    A LEU   A 1 43  ? 30.842 3.506   -2.358  0.66 12.93 ?  43  LEU   A H    1 
ATOM   1133 H  H    B LEU   A 1 43  ? 30.930 3.442   -2.295  0.34 12.93 ?  43  LEU   A H    1 
ATOM   1134 H  HA   . LEU   A 1 43  ? 30.020 3.986   -0.475  1.00 12.69 ?  43  LEU   A HA   1 
ATOM   1135 H  HB2  . LEU   A 1 43  ? 32.613 4.798   0.208   1.00 13.33 ?  43  LEU   A HB2  1 
ATOM   1136 H  HB3  . LEU   A 1 43  ? 31.468 4.456   1.245   1.00 13.33 ?  43  LEU   A HB3  1 
ATOM   1137 H  HG   . LEU   A 1 43  ? 32.757 2.552   -0.387  1.00 13.61 ?  43  LEU   A HG   1 
ATOM   1138 H  HD11 . LEU   A 1 43  ? 33.701 1.769   1.588   1.00 14.61 ?  43  LEU   A HD11 1 
ATOM   1139 H  HD12 . LEU   A 1 43  ? 34.123 3.278   1.325   1.00 14.61 ?  43  LEU   A HD12 1 
ATOM   1140 H  HD13 . LEU   A 1 43  ? 32.989 2.944   2.387   1.00 14.61 ?  43  LEU   A HD13 1 
ATOM   1141 H  HD21 . LEU   A 1 43  ? 31.569 0.917   0.845   1.00 13.63 ?  43  LEU   A HD21 1 
ATOM   1142 H  HD22 . LEU   A 1 43  ? 30.714 2.081   1.507   1.00 13.63 ?  43  LEU   A HD22 1 
ATOM   1143 H  HD23 . LEU   A 1 43  ? 30.602 1.802   -0.053  1.00 13.63 ?  43  LEU   A HD23 1 
ATOM   1144 N  N    A LYS   A 1 44  ? 29.575 6.441   -1.616  0.66 10.38 ?  44  LYS   A N    1 
ATOM   1145 N  N    B LYS   A 1 44  ? 29.551 6.428   -1.607  0.34 11.61 ?  44  LYS   A N    1 
ATOM   1146 C  CA   A LYS   A 1 44  ? 28.937 7.758   -1.616  0.66 10.73 ?  44  LYS   A CA   1 
ATOM   1147 C  CA   B LYS   A 1 44  ? 28.877 7.727   -1.606  0.34 12.80 ?  44  LYS   A CA   1 
ATOM   1148 C  C    A LYS   A 1 44  ? 27.513 7.576   -1.110  0.66 9.74  ?  44  LYS   A C    1 
ATOM   1149 C  C    B LYS   A 1 44  ? 27.454 7.507   -1.111  0.34 12.03 ?  44  LYS   A C    1 
ATOM   1150 O  O    A LYS   A 1 44  ? 26.643 7.064   -1.820  0.66 10.84 ?  44  LYS   A O    1 
ATOM   1151 O  O    B LYS   A 1 44  ? 26.594 7.013   -1.846  0.34 12.17 ?  44  LYS   A O    1 
ATOM   1152 C  CB   A LYS   A 1 44  ? 28.984 8.384   -3.003  0.66 13.06 ?  44  LYS   A CB   1 
ATOM   1153 C  CB   B LYS   A 1 44  ? 28.897 8.349   -2.998  0.34 15.11 ?  44  LYS   A CB   1 
ATOM   1154 C  CG   A LYS   A 1 44  ? 30.369 8.838   -3.428  0.66 16.21 ?  44  LYS   A CG   1 
ATOM   1155 C  CG   B LYS   A 1 44  ? 30.252 8.890   -3.426  0.34 17.60 ?  44  LYS   A CG   1 
ATOM   1156 C  CD   A LYS   A 1 44  ? 31.036 9.732   -2.388  0.66 21.49 ?  44  LYS   A CD   1 
ATOM   1157 C  CD   B LYS   A 1 44  ? 30.835 9.845   -2.394  0.34 20.49 ?  44  LYS   A CD   1 
ATOM   1158 C  CE   A LYS   A 1 44  ? 32.339 10.305  -2.912  0.66 24.81 ?  44  LYS   A CE   1 
ATOM   1159 C  CE   B LYS   A 1 44  ? 32.124 10.464  -2.892  0.34 22.33 ?  44  LYS   A CE   1 
ATOM   1160 N  NZ   A LYS   A 1 44  ? 33.149 10.932  -1.836  0.66 26.66 ?  44  LYS   A NZ   1 
ATOM   1161 N  NZ   B LYS   A 1 44  ? 33.038 10.815  -1.772  0.34 23.40 ?  44  LYS   A NZ   1 
ATOM   1162 H  H    A LYS   A 1 44  ? 29.443 5.988   -2.336  0.66 12.46 ?  44  LYS   A H    1 
ATOM   1163 H  H    B LYS   A 1 44  ? 29.417 5.972   -2.324  0.34 13.94 ?  44  LYS   A H    1 
ATOM   1164 H  HA   A LYS   A 1 44  ? 29.396 8.332   -0.985  0.66 12.88 ?  44  LYS   A HA   1 
ATOM   1165 H  HA   B LYS   A 1 44  ? 29.314 8.318   -0.979  0.34 15.37 ?  44  LYS   A HA   1 
ATOM   1166 H  HB2  A LYS   A 1 44  ? 28.675 7.731   -3.650  0.66 15.68 ?  44  LYS   A HB2  1 
ATOM   1167 H  HB2  B LYS   A 1 44  ? 28.633 7.676   -3.646  0.34 18.14 ?  44  LYS   A HB2  1 
ATOM   1168 H  HB3  A LYS   A 1 44  ? 28.401 9.158   -3.012  0.66 15.68 ?  44  LYS   A HB3  1 
ATOM   1169 H  HB3  B LYS   A 1 44  ? 28.267 9.087   -3.021  0.34 18.14 ?  44  LYS   A HB3  1 
ATOM   1170 H  HG2  A LYS   A 1 44  ? 30.934 8.062   -3.563  0.66 19.46 ?  44  LYS   A HG2  1 
ATOM   1171 H  HG2  B LYS   A 1 44  ? 30.869 8.151   -3.539  0.34 21.12 ?  44  LYS   A HG2  1 
ATOM   1172 H  HG3  A LYS   A 1 44  ? 30.298 9.346   -4.254  0.66 19.46 ?  44  LYS   A HG3  1 
ATOM   1173 H  HG3  B LYS   A 1 44  ? 30.153 9.374   -4.262  0.34 21.12 ?  44  LYS   A HG3  1 
ATOM   1174 H  HD2  A LYS   A 1 44  ? 30.436 10.462  -2.163  0.66 25.79 ?  44  LYS   A HD2  1 
ATOM   1175 H  HD2  B LYS   A 1 44  ? 30.195 10.551  -2.213  0.34 24.59 ?  44  LYS   A HD2  1 
ATOM   1176 H  HD3  A LYS   A 1 44  ? 31.237 9.206   -1.596  0.66 25.79 ?  44  LYS   A HD3  1 
ATOM   1177 H  HD3  B LYS   A 1 44  ? 31.038 9.355   -1.580  0.34 24.59 ?  44  LYS   A HD3  1 
ATOM   1178 H  HE2  A LYS   A 1 44  ? 32.862 9.591   -3.308  0.66 29.78 ?  44  LYS   A HE2  1 
ATOM   1179 H  HE2  B LYS   A 1 44  ? 32.581 9.829   -3.466  0.34 26.80 ?  44  LYS   A HE2  1 
ATOM   1180 H  HE3  A LYS   A 1 44  ? 32.141 10.982  -3.577  0.66 29.78 ?  44  LYS   A HE3  1 
ATOM   1181 H  HE3  B LYS   A 1 44  ? 31.919 11.273  -3.382  0.34 26.80 ?  44  LYS   A HE3  1 
ATOM   1182 H  HZ1  A LYS   A 1 44  ? 33.904 11.258  -2.176  0.66 32.00 ?  44  LYS   A HZ1  1 
ATOM   1183 H  HZ1  B LYS   A 1 44  ? 33.785 11.177  -2.093  0.34 28.09 ?  44  LYS   A HZ1  1 
ATOM   1184 H  HZ2  A LYS   A 1 44  ? 32.691 11.597  -1.459  0.66 32.00 ?  44  LYS   A HZ2  1 
ATOM   1185 H  HZ2  B LYS   A 1 44  ? 32.643 11.402  -1.231  0.34 28.09 ?  44  LYS   A HZ2  1 
ATOM   1186 H  HZ3  A LYS   A 1 44  ? 33.347 10.329  -1.213  0.66 32.00 ?  44  LYS   A HZ3  1 
ATOM   1187 H  HZ3  B LYS   A 1 44  ? 33.246 10.086  -1.307  0.34 28.09 ?  44  LYS   A HZ3  1 
ATOM   1188 N  N    A HIS   A 1 45  ? 27.287 7.968   0.139   0.66 9.13  ?  45  HIS   A N    1 
ATOM   1189 N  N    B HIS   A 1 45  ? 27.208 7.865   0.146   0.34 11.78 ?  45  HIS   A N    1 
ATOM   1190 C  CA   A HIS   A 1 45  ? 26.061 7.611   0.854   0.66 9.55  ?  45  HIS   A CA   1 
ATOM   1191 C  CA   B HIS   A 1 45  ? 25.937 7.577   0.810   0.34 11.70 ?  45  HIS   A CA   1 
ATOM   1192 C  C    A HIS   A 1 45  ? 25.003 8.705   0.685   0.66 10.12 ?  45  HIS   A C    1 
ATOM   1193 C  C    B HIS   A 1 45  ? 25.012 8.775   0.643   0.34 11.94 ?  45  HIS   A C    1 
ATOM   1194 O  O    A HIS   A 1 45  ? 24.621 9.403   1.627   0.66 10.90 ?  45  HIS   A O    1 
ATOM   1195 O  O    B HIS   A 1 45  ? 24.983 9.687   1.472   0.34 12.12 ?  45  HIS   A O    1 
ATOM   1196 C  CB   A HIS   A 1 45  ? 26.373 7.368   2.321   0.66 9.63  ?  45  HIS   A CB   1 
ATOM   1197 C  CB   B HIS   A 1 45  ? 26.181 7.266   2.278   0.34 11.11 ?  45  HIS   A CB   1 
ATOM   1198 C  CG   A HIS   A 1 45  ? 27.481 6.391   2.547   0.66 9.84  ?  45  HIS   A CG   1 
ATOM   1199 C  CG   B HIS   A 1 45  ? 27.337 6.346   2.512   0.34 9.91  ?  45  HIS   A CG   1 
ATOM   1200 N  ND1  A HIS   A 1 45  ? 27.456 5.102   2.054   0.66 10.93 ?  45  HIS   A ND1  1 
ATOM   1201 N  ND1  B HIS   A 1 45  ? 27.384 5.063   2.007   0.34 9.45  ?  45  HIS   A ND1  1 
ATOM   1202 C  CD2  A HIS   A 1 45  ? 28.657 6.528   3.204   0.66 10.42 ?  45  HIS   A CD2  1 
ATOM   1203 C  CD2  B HIS   A 1 45  ? 28.495 6.531   3.189   0.34 9.98  ?  45  HIS   A CD2  1 
ATOM   1204 C  CE1  A HIS   A 1 45  ? 28.569 4.486   2.415   0.66 10.52 ?  45  HIS   A CE1  1 
ATOM   1205 C  CE1  B HIS   A 1 45  ? 28.519 4.496   2.374   0.34 9.24  ?  45  HIS   A CE1  1 
ATOM   1206 N  NE2  A HIS   A 1 45  ? 29.315 5.328   3.109   0.66 10.48 ?  45  HIS   A NE2  1 
ATOM   1207 N  NE2  B HIS   A 1 45  ? 29.212 5.365   3.090   0.34 9.71  ?  45  HIS   A NE2  1 
ATOM   1208 H  H    A HIS   A 1 45  ? 27.833 8.451   0.602   0.66 10.97 ?  45  HIS   A H    1 
ATOM   1209 H  H    B HIS   A 1 45  ? 27.775 8.278   0.647   0.34 14.14 ?  45  HIS   A H    1 
ATOM   1210 H  HA   A HIS   A 1 45  ? 25.708 6.790   0.485   0.66 11.47 ?  45  HIS   A HA   1 
ATOM   1211 H  HA   B HIS   A 1 45  ? 25.523 6.804   0.396   0.34 14.05 ?  45  HIS   A HA   1 
ATOM   1212 H  HB2  A HIS   A 1 45  ? 26.627 8.209   2.733   0.66 11.56 ?  45  HIS   A HB2  1 
ATOM   1213 H  HB2  B HIS   A 1 45  ? 26.360 8.095   2.750   0.34 13.34 ?  45  HIS   A HB2  1 
ATOM   1214 H  HB3  A HIS   A 1 45  ? 25.579 7.017   2.756   0.66 11.56 ?  45  HIS   A HB3  1 
ATOM   1215 H  HB3  B HIS   A 1 45  ? 25.391 6.842   2.642   0.34 13.34 ?  45  HIS   A HB3  1 
ATOM   1216 H  HD2  A HIS   A 1 45  ? 28.969 7.295   3.637   0.66 12.51 ?  45  HIS   A HD2  1 
ATOM   1217 H  HD2  B HIS   A 1 45  ? 28.760 7.304   3.637   0.34 11.99 ?  45  HIS   A HD2  1 
ATOM   1218 H  HE1  A HIS   A 1 45  ? 28.791 3.606   2.213   0.66 12.64 ?  45  HIS   A HE1  1 
ATOM   1219 H  HE1  B HIS   A 1 45  ? 28.788 3.630   2.166   0.34 11.09 ?  45  HIS   A HE1  1 
ATOM   1220 H  HE2  A HIS   A 1 45  ? 30.092 5.152   3.443   0.66 12.58 ?  45  HIS   A HE2  1 
ATOM   1221 H  HE2  B HIS   A 1 45  ? 29.989 5.222   3.436   0.34 11.66 ?  45  HIS   A HE2  1 
ATOM   1222 N  N    A GLY   A 1 46  ? 24.521 8.839   -0.549  0.66 10.73 ?  46  GLY   A N    1 
ATOM   1223 N  N    B GLY   A 1 46  ? 24.235 8.769   -0.437  0.34 12.19 ?  46  GLY   A N    1 
ATOM   1224 C  CA   A GLY   A 1 46  ? 23.718 9.997   -0.903  0.66 11.49 ?  46  GLY   A CA   1 
ATOM   1225 C  CA   B GLY   A 1 46  ? 23.405 9.911   -0.766  0.34 12.29 ?  46  GLY   A CA   1 
ATOM   1226 C  C    A GLY   A 1 46  ? 22.229 9.888   -0.641  0.66 11.39 ?  46  GLY   A C    1 
ATOM   1227 C  C    B GLY   A 1 46  ? 21.950 9.776   -0.364  0.34 11.63 ?  46  GLY   A C    1 
ATOM   1228 O  O    A GLY   A 1 46  ? 21.573 10.902  -0.367  0.66 11.88 ?  46  GLY   A O    1 
ATOM   1229 O  O    B GLY   A 1 46  ? 21.354 10.741  0.127   0.34 11.75 ?  46  GLY   A O    1 
ATOM   1230 H  H    A GLY   A 1 46  ? 24.640 8.269   -1.185  0.66 12.89 ?  46  GLY   A H    1 
ATOM   1231 H  H    B GLY   A 1 46  ? 24.178 8.113   -0.992  0.34 14.63 ?  46  GLY   A H    1 
ATOM   1232 H  HA2  A GLY   A 1 46  ? 24.053 10.761  -0.408  0.66 13.79 ?  46  GLY   A HA2  1 
ATOM   1233 H  HA2  B GLY   A 1 46  ? 23.760 10.698  -0.325  0.34 14.76 ?  46  GLY   A HA2  1 
ATOM   1234 H  HA3  A GLY   A 1 46  ? 23.838 10.175  -1.846  0.66 13.79 ?  46  GLY   A HA3  1 
ATOM   1235 H  HA3  B GLY   A 1 46  ? 23.449 10.061  -1.723  0.34 14.76 ?  46  GLY   A HA3  1 
ATOM   1236 N  N    A GLY   A 1 47  ? 21.674 8.686   -0.759  0.66 11.53 ?  47  GLY   A N    1 
ATOM   1237 N  N    B GLY   A 1 47  ? 21.362 8.597   -0.566  0.34 12.00 ?  47  GLY   A N    1 
ATOM   1238 C  CA   A GLY   A 1 47  ? 20.237 8.498   -0.679  0.66 11.78 ?  47  GLY   A CA   1 
ATOM   1239 C  CA   B GLY   A 1 47  ? 19.947 8.390   -0.329  0.34 12.21 ?  47  GLY   A CA   1 
ATOM   1240 C  C    A GLY   A 1 47  ? 19.908 7.057   -0.353  0.66 10.53 ?  47  GLY   A C    1 
ATOM   1241 C  C    B GLY   A 1 47  ? 19.654 6.951   0.044   0.34 11.42 ?  47  GLY   A C    1 
ATOM   1242 O  O    A GLY   A 1 47  ? 20.795 6.219   -0.177  0.66 10.74 ?  47  GLY   A O    1 
ATOM   1243 O  O    B GLY   A 1 47  ? 20.563 6.127   0.169   0.34 11.36 ?  47  GLY   A O    1 
ATOM   1244 H  H    A GLY   A 1 47  ? 22.115 7.957   -0.869  0.66 13.85 ?  47  GLY   A H    1 
ATOM   1245 H  H    B GLY   A 1 47  ? 21.775 7.892   -0.835  0.34 14.41 ?  47  GLY   A H    1 
ATOM   1246 H  HA2  A GLY   A 1 47  ? 19.862 9.073   0.008   0.66 14.14 ?  47  GLY   A HA2  1 
ATOM   1247 H  HA2  B GLY   A 1 47  ? 19.651 8.956   0.399   0.34 14.66 ?  47  GLY   A HA2  1 
ATOM   1248 H  HA3  A GLY   A 1 47  ? 19.833 8.724   -1.531  0.66 14.14 ?  47  GLY   A HA3  1 
ATOM   1249 H  HA3  B GLY   A 1 47  ? 19.444 8.625   -1.127  0.34 14.66 ?  47  GLY   A HA3  1 
ATOM   1250 N  N    A GLY   A 1 48  ? 18.613 6.761   -0.297  0.66 10.02 ?  48  GLY   A N    1 
ATOM   1251 N  N    B GLY   A 1 48  ? 18.367 6.647   0.222   0.34 11.34 ?  48  GLY   A N    1 
ATOM   1252 C  CA   A GLY   A 1 48  ? 18.198 5.415   0.062   0.66 10.03 ?  48  GLY   A CA   1 
ATOM   1253 C  CA   B GLY   A 1 48  ? 18.003 5.302   0.657   0.34 11.39 ?  48  GLY   A CA   1 
ATOM   1254 C  C    A GLY   A 1 48  ? 18.643 5.045   1.468   0.66 8.91  ?  48  GLY   A C    1 
ATOM   1255 C  C    B GLY   A 1 48  ? 18.554 5.013   2.047   0.34 11.68 ?  48  GLY   A C    1 
ATOM   1256 O  O    A GLY   A 1 48  ? 18.787 5.902   2.348   0.66 10.05 ?  48  GLY   A O    1 
ATOM   1257 O  O    B GLY   A 1 48  ? 18.767 5.921   2.859   0.34 11.75 ?  48  GLY   A O    1 
ATOM   1258 H  H    A GLY   A 1 48  ? 17.974 7.311   -0.460  0.66 12.03 ?  48  GLY   A H    1 
ATOM   1259 H  H    B GLY   A 1 48  ? 17.690 7.185   0.103   0.34 13.61 ?  48  GLY   A H    1 
ATOM   1260 H  HA2  A GLY   A 1 48  ? 17.238 5.347   0.011   0.66 12.04 ?  48  GLY   A HA2  1 
ATOM   1261 H  HA2  B GLY   A 1 48  ? 17.030 5.206   0.663   0.34 13.68 ?  48  GLY   A HA2  1 
ATOM   1262 H  HA3  A GLY   A 1 48  ? 18.592 4.780   -0.562  0.66 12.04 ?  48  GLY   A HA3  1 
ATOM   1263 H  HA3  B GLY   A 1 48  ? 18.363 4.649   0.034   0.34 13.68 ?  48  GLY   A HA3  1 
ATOM   1264 N  N    A VAL   A 1 49  ? 18.862 3.743   1.686   0.66 8.31  ?  49  VAL   A N    1 
ATOM   1265 N  N    B VAL   A 1 49  ? 18.781 3.725   2.339   0.34 11.47 ?  49  VAL   A N    1 
ATOM   1266 C  CA   A VAL   A 1 49  ? 19.348 3.264   2.980   0.66 8.48  ?  49  VAL   A CA   1 
ATOM   1267 C  CA   B VAL   A 1 49  ? 19.403 3.356   3.612   0.34 12.37 ?  49  VAL   A CA   1 
ATOM   1268 C  C    A VAL   A 1 49  ? 20.640 3.977   3.367   0.66 7.85  ?  49  VAL   A C    1 
ATOM   1269 C  C    B VAL   A 1 49  ? 20.762 4.026   3.757   0.34 12.27 ?  49  VAL   A C    1 
ATOM   1270 O  O    A VAL   A 1 49  ? 20.816 4.381   4.519   0.66 7.98  ?  49  VAL   A O    1 
ATOM   1271 O  O    B VAL   A 1 49  ? 21.126 4.481   4.848   0.34 12.85 ?  49  VAL   A O    1 
ATOM   1272 C  CB   A VAL   A 1 49  ? 19.521 1.732   2.962   0.66 8.94  ?  49  VAL   A CB   1 
ATOM   1273 C  CB   B VAL   A 1 49  ? 19.505 1.822   3.772   0.34 14.17 ?  49  VAL   A CB   1 
ATOM   1274 C  CG1  A VAL   A 1 49  ? 20.305 1.252   4.175   0.66 9.39  ?  49  VAL   A CG1  1 
ATOM   1275 C  CG1  B VAL   A 1 49  ? 20.470 1.453   4.888   0.34 14.36 ?  49  VAL   A CG1  1 
ATOM   1276 C  CG2  A VAL   A 1 49  ? 18.164 1.038   2.908   0.66 10.42 ?  49  VAL   A CG2  1 
ATOM   1277 C  CG2  B VAL   A 1 49  ? 18.138 1.207   4.033   0.34 15.42 ?  49  VAL   A CG2  1 
ATOM   1278 H  H    A VAL   A 1 49  ? 18.731 3.123   1.102   0.66 9.98  ?  49  VAL   A H    1 
ATOM   1279 H  H    B VAL   A 1 49  ? 18.574 3.064   1.840   0.34 13.77 ?  49  VAL   A H    1 
ATOM   1280 H  HA   A VAL   A 1 49  ? 18.684 3.473   3.655   0.66 10.18 ?  49  VAL   A HA   1 
ATOM   1281 H  HA   B VAL   A 1 49  ? 18.850 3.690   4.334   0.34 14.85 ?  49  VAL   A HA   1 
ATOM   1282 H  HB   A VAL   A 1 49  ? 20.013 1.481   2.161   0.66 10.73 ?  49  VAL   A HB   1 
ATOM   1283 H  HB   B VAL   A 1 49  ? 19.864 1.432   2.975   0.34 17.00 ?  49  VAL   A HB   1 
ATOM   1284 H  HG11 A VAL   A 1 49  ? 20.161 0.298   4.278   0.66 11.28 ?  49  VAL   A HG11 1 
ATOM   1285 H  HG11 B VAL   A 1 49  ? 20.396 0.502   5.062   0.34 17.23 ?  49  VAL   A HG11 1 
ATOM   1286 H  HG12 A VAL   A 1 49  ? 21.245 1.432   4.034   0.66 11.28 ?  49  VAL   A HG12 1 
ATOM   1287 H  HG12 B VAL   A 1 49  ? 21.380 1.661   4.614   0.34 17.23 ?  49  VAL   A HG12 1 
ATOM   1288 H  HG13 A VAL   A 1 49  ? 19.983 1.721   4.958   0.66 11.28 ?  49  VAL   A HG13 1 
ATOM   1289 H  HG13 B VAL   A 1 49  ? 20.236 1.951   5.683   0.34 17.23 ?  49  VAL   A HG13 1 
ATOM   1290 H  HG21 A VAL   A 1 49  ? 18.296 0.079   2.878   0.66 12.51 ?  49  VAL   A HG21 1 
ATOM   1291 H  HG21 B VAL   A 1 49  ? 18.253 0.289   4.328   0.34 18.51 ?  49  VAL   A HG21 1 
ATOM   1292 H  HG22 A VAL   A 1 49  ? 17.654 1.279   3.698   0.66 12.51 ?  49  VAL   A HG22 1 
ATOM   1293 H  HG22 B VAL   A 1 49  ? 17.686 1.720   4.723   0.34 18.51 ?  49  VAL   A HG22 1 
ATOM   1294 H  HG23 A VAL   A 1 49  ? 17.687 1.330   2.111   0.66 12.51 ?  49  VAL   A HG23 1 
ATOM   1295 H  HG23 B VAL   A 1 49  ? 17.628 1.233   3.214   0.34 18.51 ?  49  VAL   A HG23 1 
ATOM   1296 N  N    A ALA   A 1 50  ? 21.580 4.092   2.425   0.66 8.05  ?  50  ALA   A N    1 
ATOM   1297 N  N    B ALA   A 1 50  ? 21.541 4.075   2.671   0.34 12.24 ?  50  ALA   A N    1 
ATOM   1298 C  CA   A ALA   A 1 50  ? 22.890 4.648   2.760   0.66 8.84  ?  50  ALA   A CA   1 
ATOM   1299 C  CA   B ALA   A 1 50  ? 22.883 4.647   2.749   0.34 11.81 ?  50  ALA   A CA   1 
ATOM   1300 C  C    A ALA   A 1 50  ? 22.781 6.101   3.198   0.66 9.07  ?  50  ALA   A C    1 
ATOM   1301 C  C    B ALA   A 1 50  ? 22.826 6.112   3.157   0.34 10.76 ?  50  ALA   A C    1 
ATOM   1302 O  O    A ALA   A 1 50  ? 23.392 6.510   4.194   0.66 9.84  ?  50  ALA   A O    1 
ATOM   1303 O  O    B ALA   A 1 50  ? 23.504 6.535   4.101   0.34 10.92 ?  50  ALA   A O    1 
ATOM   1304 C  CB   A ALA   A 1 50  ? 23.840 4.526   1.572   0.66 8.38  ?  50  ALA   A CB   1 
ATOM   1305 C  CB   B ALA   A 1 50  ? 23.614 4.483   1.414   0.34 12.29 ?  50  ALA   A CB   1 
ATOM   1306 H  H    A ALA   A 1 50  ? 21.488 3.861   1.600   0.66 9.67  ?  50  ALA   A H    1 
ATOM   1307 H  H    B ALA   A 1 50  ? 21.317 3.796   1.882   0.34 14.70 ?  50  ALA   A H    1 
ATOM   1308 H  HA   A ALA   A 1 50  ? 23.265 4.149   3.499   0.66 10.62 ?  50  ALA   A HA   1 
ATOM   1309 H  HA   B ALA   A 1 50  ? 23.389 4.177   3.422   0.34 14.18 ?  50  ALA   A HA   1 
ATOM   1310 H  HB1  A ALA   A 1 50  ? 24.698 4.905   1.816   0.66 10.07 ?  50  ALA   A HB1  1 
ATOM   1311 H  HB1  B ALA   A 1 50  ? 24.503 4.871   1.490   0.34 14.75 ?  50  ALA   A HB1  1 
ATOM   1312 H  HB2  A ALA   A 1 50  ? 23.939 3.592   1.343   0.66 10.07 ?  50  ALA   A HB2  1 
ATOM   1313 H  HB2  B ALA   A 1 50  ? 23.685 3.539   1.205   0.34 14.75 ?  50  ALA   A HB2  1 
ATOM   1314 H  HB3  A ALA   A 1 50  ? 23.465 5.015   0.820   0.66 10.07 ?  50  ALA   A HB3  1 
ATOM   1315 H  HB3  B ALA   A 1 50  ? 23.116 4.940   0.718   0.34 14.75 ?  50  ALA   A HB3  1 
ATOM   1316 N  N    . GLY   A 1 51  ? 22.019 6.906   2.454   1.00 10.03 ?  51  GLY   A N    1 
ATOM   1317 C  CA   . GLY   A 1 51  ? 21.854 8.295   2.841   1.00 10.34 ?  51  GLY   A CA   1 
ATOM   1318 C  C    . GLY   A 1 51  ? 21.250 8.432   4.223   1.00 10.57 ?  51  GLY   A C    1 
ATOM   1319 O  O    . GLY   A 1 51  ? 21.629 9.324   4.989   1.00 11.21 ?  51  GLY   A O    1 
ATOM   1320 H  H    A GLY   A 1 51  ? 21.602 6.676   1.735   0.66 12.04 ?  51  GLY   A H    1 
ATOM   1321 H  H    B GLY   A 1 51  ? 21.563 6.667   1.763   0.34 12.04 ?  51  GLY   A H    1 
ATOM   1322 H  HA2  . GLY   A 1 51  ? 22.716 8.738   2.840   1.00 12.41 ?  51  GLY   A HA2  1 
ATOM   1323 H  HA3  . GLY   A 1 51  ? 21.275 8.745   2.205   1.00 12.41 ?  51  GLY   A HA3  1 
ATOM   1324 N  N    A ALA   A 1 52  ? 20.268 7.583   4.541   0.66 10.31 ?  52  ALA   A N    1 
ATOM   1325 N  N    B ALA   A 1 52  ? 20.334 7.520   4.574   0.34 10.71 ?  52  ALA   A N    1 
ATOM   1326 C  CA   A ALA   A 1 52  ? 19.615 7.642   5.843   0.66 11.18 ?  52  ALA   A CA   1 
ATOM   1327 C  CA   B ALA   A 1 52  ? 19.698 7.536   5.888   0.34 10.89 ?  52  ALA   A CA   1 
ATOM   1328 C  C    A ALA   A 1 52  ? 20.573 7.248   6.962   0.66 10.26 ?  52  ALA   A C    1 
ATOM   1329 C  C    B ALA   A 1 52  ? 20.672 7.119   6.986   0.34 10.63 ?  52  ALA   A C    1 
ATOM   1330 O  O    A ALA   A 1 52  ? 20.644 7.920   7.993   0.66 10.93 ?  52  ALA   A O    1 
ATOM   1331 O  O    B ALA   A 1 52  ? 20.762 7.776   8.028   0.34 11.03 ?  52  ALA   A O    1 
ATOM   1332 C  CB   A ALA   A 1 52  ? 18.373 6.750   5.845   0.66 12.47 ?  52  ALA   A CB   1 
ATOM   1333 C  CB   B ALA   A 1 52  ? 18.464 6.630   5.883   0.34 11.45 ?  52  ALA   A CB   1 
ATOM   1334 H  H    A ALA   A 1 52  ? 19.972 6.961   4.022   0.66 12.38 ?  52  ALA   A H    1 
ATOM   1335 H  H    B ALA   A 1 52  ? 20.073 6.873   4.066   0.34 12.85 ?  52  ALA   A H    1 
ATOM   1336 H  HA   A ALA   A 1 52  ? 19.327 8.551   6.004   0.66 13.42 ?  52  ALA   A HA   1 
ATOM   1337 H  HA   B ALA   A 1 52  ? 19.402 8.435   6.082   0.34 13.07 ?  52  ALA   A HA   1 
ATOM   1338 H  HB1  A ALA   A 1 52  ? 17.948 6.801   6.717   0.66 14.97 ?  52  ALA   A HB1  1 
ATOM   1339 H  HB1  B ALA   A 1 52  ? 18.043 6.661   6.759   0.34 13.75 ?  52  ALA   A HB1  1 
ATOM   1340 H  HB2  A ALA   A 1 52  ? 17.759 7.061   5.161   0.66 14.97 ?  52  ALA   A HB2  1 
ATOM   1341 H  HB2  B ALA   A 1 52  ? 17.840 6.948   5.210   0.34 13.75 ?  52  ALA   A HB2  1 
ATOM   1342 H  HB3  A ALA   A 1 52  ? 18.637 5.835   5.661   0.66 14.97 ?  52  ALA   A HB3  1 
ATOM   1343 H  HB3  B ALA   A 1 52  ? 18.733 5.721   5.680   0.34 13.75 ?  52  ALA   A HB3  1 
ATOM   1344 N  N    A LEU   A 1 53  ? 21.300 6.141   6.792   0.66 10.21 ?  53  LEU   A N    1 
ATOM   1345 N  N    B LEU   A 1 53  ? 21.393 6.011   6.788   0.34 10.49 ?  53  LEU   A N    1 
ATOM   1346 C  CA   A LEU   A 1 53  ? 22.266 5.734   7.812   0.66 10.53 ?  53  LEU   A CA   1 
ATOM   1347 C  CA   B LEU   A 1 53  ? 22.387 5.608   7.781   0.34 10.31 ?  53  LEU   A CA   1 
ATOM   1348 C  C    A LEU   A 1 53  ? 23.328 6.807   8.001   0.66 9.94  ?  53  LEU   A C    1 
ATOM   1349 C  C    B LEU   A 1 53  ? 23.415 6.707   7.988   0.34 9.86  ?  53  LEU   A C    1 
ATOM   1350 O  O    A LEU   A 1 53  ? 23.644 7.192   9.131   0.66 11.09 ?  53  LEU   A O    1 
ATOM   1351 O  O    B LEU   A 1 53  ? 23.790 7.014   9.124   0.34 10.00 ?  53  LEU   A O    1 
ATOM   1352 C  CB   A LEU   A 1 53  ? 22.909 4.393   7.440   0.66 10.30 ?  53  LEU   A CB   1 
ATOM   1353 C  CB   B LEU   A 1 53  ? 23.090 4.316   7.357   0.34 10.36 ?  53  LEU   A CB   1 
ATOM   1354 C  CG   A LEU   A 1 53  ? 22.019 3.137   7.445   0.66 10.45 ?  53  LEU   A CG   1 
ATOM   1355 C  CG   B LEU   A 1 53  ? 22.366 2.976   7.509   0.34 10.67 ?  53  LEU   A CG   1 
ATOM   1356 C  CD1  A LEU   A 1 53  ? 22.768 1.941   6.851   0.66 10.06 ?  53  LEU   A CD1  1 
ATOM   1357 C  CD1  B LEU   A 1 53  ? 23.280 1.849   7.045   0.34 11.51 ?  53  LEU   A CD1  1 
ATOM   1358 C  CD2  A LEU   A 1 53  ? 21.516 2.802   8.839   0.66 12.14 ?  53  LEU   A CD2  1 
ATOM   1359 C  CD2  B LEU   A 1 53  ? 21.911 2.733   8.934   0.34 10.44 ?  53  LEU   A CD2  1 
ATOM   1360 H  H    A LEU   A 1 53  ? 21.250 5.618   6.112   0.66 12.25 ?  53  LEU   A H    1 
ATOM   1361 H  H    B LEU   A 1 53  ? 21.331 5.490   6.104   0.34 12.59 ?  53  LEU   A H    1 
ATOM   1362 H  HA   A LEU   A 1 53  ? 21.804 5.623   8.654   0.66 12.65 ?  53  LEU   A HA   1 
ATOM   1363 H  HA   B LEU   A 1 53  ? 21.945 5.450   8.628   0.34 12.38 ?  53  LEU   A HA   1 
ATOM   1364 H  HB2  A LEU   A 1 53  ? 23.276 4.477   6.546   0.66 12.37 ?  53  LEU   A HB2  1 
ATOM   1365 H  HB2  B LEU   A 1 53  ? 23.319 4.401   6.420   0.34 12.44 ?  53  LEU   A HB2  1 
ATOM   1366 H  HB3  A LEU   A 1 53  ? 23.631 4.228   8.064   0.66 12.37 ?  53  LEU   A HB3  1 
ATOM   1367 H  HB3  B LEU   A 1 53  ? 23.908 4.245   7.874   0.34 12.44 ?  53  LEU   A HB3  1 
ATOM   1368 H  HG   A LEU   A 1 53  ? 21.246 3.304   6.880   0.66 12.54 ?  53  LEU   A HG   1 
ATOM   1369 H  HG   B LEU   A 1 53  ? 21.586 2.978   6.938   0.34 12.81 ?  53  LEU   A HG   1 
ATOM   1370 H  HD11 A LEU   A 1 53  ? 22.186 1.166   6.866   0.66 12.08 ?  53  LEU   A HD11 1 
ATOM   1371 H  HD11 B LEU   A 1 53  ? 22.817 1.003   7.142   0.34 13.82 ?  53  LEU   A HD11 1 
ATOM   1372 H  HD12 A LEU   A 1 53  ? 23.025 2.147   5.939   0.66 12.08 ?  53  LEU   A HD12 1 
ATOM   1373 H  HD12 B LEU   A 1 53  ? 23.516 1.993   6.115   0.34 13.82 ?  53  LEU   A HD12 1 
ATOM   1374 H  HD13 A LEU   A 1 53  ? 23.560 1.770   7.387   0.66 12.08 ?  53  LEU   A HD13 1 
ATOM   1375 H  HD13 B LEU   A 1 53  ? 24.085 1.849   7.591   0.34 13.82 ?  53  LEU   A HD13 1 
ATOM   1376 H  HD21 A LEU   A 1 53  ? 20.962 2.005   8.793   0.66 14.58 ?  53  LEU   A HD21 1 
ATOM   1377 H  HD21 B LEU   A 1 53  ? 21.525 1.844   8.995   0.34 12.53 ?  53  LEU   A HD21 1 
ATOM   1378 H  HD22 A LEU   A 1 53  ? 22.275 2.643   9.420   0.66 14.58 ?  53  LEU   A HD22 1 
ATOM   1379 H  HD22 B LEU   A 1 53  ? 22.674 2.804   9.525   0.34 12.53 ?  53  LEU   A HD22 1 
ATOM   1380 H  HD23 A LEU   A 1 53  ? 20.992 3.546   9.175   0.66 14.58 ?  53  LEU   A HD23 1 
ATOM   1381 H  HD23 B LEU   A 1 53  ? 21.243 3.398   9.168   0.34 12.53 ?  53  LEU   A HD23 1 
ATOM   1382 N  N    . ASN   A 1 54  ? 23.878 7.318   6.900   1.00 10.21 ?  54  ASN   A N    1 
ATOM   1383 C  CA   . ASN   A 1 54  ? 24.927 8.320   7.027   1.00 10.00 ?  54  ASN   A CA   1 
ATOM   1384 C  C    . ASN   A 1 54  ? 24.417 9.567   7.750   1.00 10.28 ?  54  ASN   A C    1 
ATOM   1385 O  O    . ASN   A 1 54  ? 25.110 10.122  8.612   1.00 11.00 ?  54  ASN   A O    1 
ATOM   1386 C  CB   . ASN   A 1 54  ? 25.487 8.682   5.664   1.00 10.17 ?  54  ASN   A CB   1 
ATOM   1387 C  CG   . ASN   A 1 54  ? 26.496 9.797   5.773   1.00 10.41 ?  54  ASN   A CG   1 
ATOM   1388 O  OD1  . ASN   A 1 54  ? 27.509 9.653   6.471   1.00 10.80 ?  54  ASN   A OD1  1 
ATOM   1389 N  ND2  . ASN   A 1 54  ? 26.231 10.921  5.123   1.00 11.23 ?  54  ASN   A ND2  1 
ATOM   1390 H  H    A ASN   A 1 54  ? 23.659 7.114   6.093   0.66 12.26 ?  54  ASN   A H    1 
ATOM   1391 H  H    B ASN   A 1 54  ? 23.597 7.184   6.097   0.34 12.26 ?  54  ASN   A H    1 
ATOM   1392 H  HA   . ASN   A 1 54  ? 25.644 7.951   7.555   1.00 12.00 ?  54  ASN   A HA   1 
ATOM   1393 H  HB2  . ASN   A 1 54  ? 25.927 7.901   5.287   1.00 12.21 ?  54  ASN   A HB2  1 
ATOM   1394 H  HB3  . ASN   A 1 54  ? 24.767 8.974   5.085   1.00 12.21 ?  54  ASN   A HB3  1 
ATOM   1395 H  HD21 . ASN   A 1 54  ? 26.781 11.580  5.167   1.00 13.49 ?  54  ASN   A HD21 1 
ATOM   1396 H  HD22 . ASN   A 1 54  ? 25.511 10.989  4.660   1.00 13.49 ?  54  ASN   A HD22 1 
ATOM   1397 N  N    . LYS   A 1 55  ? 23.203 10.023  7.414   1.00 10.59 ?  55  LYS   A N    1 
ATOM   1398 C  CA   . LYS   A 1 55  ? 22.629 11.180  8.091   1.00 11.24 ?  55  LYS   A CA   1 
ATOM   1399 C  C    . LYS   A 1 55  ? 22.538 10.939  9.590   1.00 11.57 ?  55  LYS   A C    1 
ATOM   1400 O  O    . LYS   A 1 55  ? 22.817 11.836  10.395  1.00 12.24 ?  55  LYS   A O    1 
ATOM   1401 C  CB   . LYS   A 1 55  ? 21.254 11.488  7.497   1.00 11.86 ?  55  LYS   A CB   1 
ATOM   1402 C  CG   . LYS   A 1 55  ? 20.528 12.656  8.153   1.00 13.57 ?  55  LYS   A CG   1 
ATOM   1403 C  CD   . LYS   A 1 55  ? 19.207 12.952  7.436   1.00 15.00 ?  55  LYS   A CD   1 
ATOM   1404 C  CE   . LYS   A 1 55  ? 18.396 14.051  8.107   1.00 17.60 ?  55  LYS   A CE   1 
ATOM   1405 N  NZ   . LYS   A 1 55  ? 17.071 14.245  7.440   1.00 18.24 ?  55  LYS   A NZ   1 
ATOM   1406 H  H    . LYS   A 1 55  ? 22.698 9.678   6.808   1.00 12.72 ?  55  LYS   A H    1 
ATOM   1407 H  HA   . LYS   A 1 55  ? 23.201 11.952  7.939   1.00 13.50 ?  55  LYS   A HA   1 
ATOM   1408 H  HB2  . LYS   A 1 55  ? 21.358 11.702  6.557   1.00 14.24 ?  55  LYS   A HB2  1 
ATOM   1409 H  HB3  . LYS   A 1 55  ? 20.692 10.703  7.593   1.00 14.24 ?  55  LYS   A HB3  1 
ATOM   1410 H  HG2  . LYS   A 1 55  ? 20.330 12.431  9.078   1.00 16.29 ?  55  LYS   A HG2  1 
ATOM   1411 H  HG3  . LYS   A 1 55  ? 21.088 13.445  8.111   1.00 16.29 ?  55  LYS   A HG3  1 
ATOM   1412 H  HD2  . LYS   A 1 55  ? 19.403 13.233  6.530   1.00 18.00 ?  55  LYS   A HD2  1 
ATOM   1413 H  HD3  . LYS   A 1 55  ? 18.671 12.144  7.426   1.00 18.00 ?  55  LYS   A HD3  1 
ATOM   1414 H  HE2  . LYS   A 1 55  ? 18.238 13.807  9.034   1.00 21.13 ?  55  LYS   A HE2  1 
ATOM   1415 H  HE3  . LYS   A 1 55  ? 18.889 14.883  8.059   1.00 21.13 ?  55  LYS   A HE3  1 
ATOM   1416 H  HZ1  . LYS   A 1 55  ? 16.555 14.771  7.940   1.00 21.89 ?  55  LYS   A HZ1  1 
ATOM   1417 H  HZ2  . LYS   A 1 55  ? 17.185 14.625  6.644   1.00 21.89 ?  55  LYS   A HZ2  1 
ATOM   1418 H  HZ3  . LYS   A 1 55  ? 16.665 13.460  7.333   1.00 21.89 ?  55  LYS   A HZ3  1 
ATOM   1419 N  N    . ALA   A 1 56  ? 22.157 9.725   9.988   1.00 11.62 ?  56  ALA   A N    1 
ATOM   1420 C  CA   . ALA   A 1 56  ? 22.030 9.411   11.401  1.00 12.23 ?  56  ALA   A CA   1 
ATOM   1421 C  C    . ALA   A 1 56  ? 23.371 9.437   12.127  1.00 12.02 ?  56  ALA   A C    1 
ATOM   1422 O  O    . ALA   A 1 56  ? 23.388 9.614   13.349  1.00 13.40 ?  56  ALA   A O    1 
ATOM   1423 C  CB   . ALA   A 1 56  ? 21.332 8.060   11.582  1.00 13.19 ?  56  ALA   A CB   1 
ATOM   1424 H  H    . ALA   A 1 56  ? 21.971 9.082   9.457   1.00 13.96 ?  56  ALA   A H    1 
ATOM   1425 H  HA   . ALA   A 1 56  ? 21.476 10.083  11.816  1.00 14.68 ?  56  ALA   A HA   1 
ATOM   1426 H  HB1  . ALA   A 1 56  ? 21.255 7.868   12.531  1.00 15.84 ?  56  ALA   A HB1  1 
ATOM   1427 H  HB2  . ALA   A 1 56  ? 20.444 8.114   11.187  1.00 15.84 ?  56  ALA   A HB2  1 
ATOM   1428 H  HB3  . ALA   A 1 56  ? 21.847 7.370   11.143  1.00 15.84 ?  56  ALA   A HB3  1 
ATOM   1429 N  N    . THR   A 1 57  ? 24.488 9.267   11.408  1.00 10.89 ?  57  THR   A N    1 
ATOM   1430 C  CA   . THR   A 1 57  ? 25.827 9.399   11.984  1.00 11.49 ?  57  THR   A CA   1 
ATOM   1431 C  C    . THR   A 1 57  ? 26.372 10.821  11.901  1.00 11.87 ?  57  THR   A C    1 
ATOM   1432 O  O    . THR   A 1 57  ? 27.557 11.039  12.183  1.00 12.38 ?  57  THR   A O    1 
ATOM   1433 C  CB   . THR   A 1 57  ? 26.848 8.450   11.321  1.00 11.54 ?  57  THR   A CB   1 
ATOM   1434 O  OG1  . THR   A 1 57  ? 27.229 8.936   10.021  1.00 11.37 ?  57  THR   A OG1  1 
ATOM   1435 C  CG2  . THR   A 1 57  ? 26.326 7.021   11.226  1.00 11.07 ?  57  THR   A CG2  1 
ATOM   1436 H  H    . THR   A 1 57  ? 24.498 9.053   10.571  1.00 13.08 ?  57  THR   A H    1 
ATOM   1437 H  HA   . THR   A 1 57  ? 25.781 9.151   12.926  1.00 13.80 ?  57  THR   A HA   1 
ATOM   1438 H  HB   . THR   A 1 57  ? 27.644 8.420   11.881  1.00 13.86 ?  57  THR   A HB   1 
ATOM   1439 H  HG1  . THR   A 1 57  ? 26.548 8.992   9.534   1.00 13.65 ?  57  THR   A HG1  1 
ATOM   1440 H  HG21 . THR   A 1 57  ? 26.973 6.457   10.771  1.00 13.29 ?  57  THR   A HG21 1 
ATOM   1441 H  HG22 . THR   A 1 57  ? 26.167 6.660   12.113  1.00 13.29 ?  57  THR   A HG22 1 
ATOM   1442 H  HG23 . THR   A 1 57  ? 25.493 7.001   10.729  1.00 13.29 ?  57  THR   A HG23 1 
ATOM   1443 N  N    . ASN   A 1 58  ? 25.551 11.789  11.499  1.00 12.07 ?  58  ASN   A N    1 
ATOM   1444 C  CA   . ASN   A 1 58  ? 26.011 13.171  11.395  1.00 13.14 ?  58  ASN   A CA   1 
ATOM   1445 C  C    . ASN   A 1 58  ? 27.149 13.301  10.381  1.00 11.71 ?  58  ASN   A C    1 
ATOM   1446 O  O    . ASN   A 1 58  ? 28.039 14.145  10.528  1.00 12.70 ?  58  ASN   A O    1 
ATOM   1447 C  CB   . ASN   A 1 58  ? 26.399 13.710  12.785  1.00 15.42 ?  58  ASN   A CB   1 
ATOM   1448 C  CG   . ASN   A 1 58  ? 26.808 15.168  12.781  1.00 19.04 ?  58  ASN   A CG   1 
ATOM   1449 O  OD1  . ASN   A 1 58  ? 26.161 15.999  12.150  1.00 20.69 ?  58  ASN   A OD1  1 
ATOM   1450 N  ND2  . ASN   A 1 58  ? 27.877 15.494  13.522  1.00 20.13 ?  58  ASN   A ND2  1 
ATOM   1451 H  H    . ASN   A 1 58  ? 24.731 11.662  11.268  1.00 14.49 ?  58  ASN   A H    1 
ATOM   1452 H  HA   . ASN   A 1 58  ? 25.271 13.705  11.072  1.00 15.77 ?  58  ASN   A HA   1 
ATOM   1453 H  HB2  . ASN   A 1 58  ? 25.634 13.617  13.381  1.00 18.51 ?  58  ASN   A HB2  1 
ATOM   1454 H  HB3  . ASN   A 1 58  ? 27.143 13.197  13.131  1.00 18.51 ?  58  ASN   A HB3  1 
ATOM   1455 H  HD21 . ASN   A 1 58  ? 28.148 16.309  13.559  1.00 24.16 ?  58  ASN   A HD21 1 
ATOM   1456 H  HD22 . ASN   A 1 58  ? 28.295 14.883  13.961  1.00 24.16 ?  58  ASN   A HD22 1 
ATOM   1457 N  N    . ASN   A 1 59  ? 27.126 12.477  9.333   1.00 10.95 ?  59  ASN   A N    1 
ATOM   1458 C  CA   . ASN   A 1 59  ? 28.107 12.455  8.241   1.00 10.67 ?  59  ASN   A CA   1 
ATOM   1459 C  C    . ASN   A 1 59  ? 29.425 11.783  8.638   1.00 10.80 ?  59  ASN   A C    1 
ATOM   1460 O  O    . ASN   A 1 59  ? 30.347 11.758  7.817   1.00 11.01 ?  59  ASN   A O    1 
ATOM   1461 C  CB   . ASN   A 1 59  ? 28.393 13.841  7.630   1.00 11.32 ?  59  ASN   A CB   1 
ATOM   1462 C  CG   . ASN   A 1 59  ? 28.752 13.774  6.158   1.00 11.34 ?  59  ASN   A CG   1 
ATOM   1463 O  OD1  . ASN   A 1 59  ? 28.048 13.151  5.363   1.00 11.90 ?  59  ASN   A OD1  1 
ATOM   1464 N  ND2  . ASN   A 1 59  ? 29.833 14.442  5.777   1.00 12.28 ?  59  ASN   A ND2  1 
ATOM   1465 H  H    . ASN   A 1 59  ? 26.520 11.873  9.222   1.00 13.15 ?  59  ASN   A H    1 
ATOM   1466 H  HA   . ASN   A 1 59  ? 27.734 11.922  7.525   1.00 12.81 ?  59  ASN   A HA   1 
ATOM   1467 H  HB2  . ASN   A 1 59  ? 27.605 14.402  7.717   1.00 13.59 ?  59  ASN   A HB2  1 
ATOM   1468 H  HB3  . ASN   A 1 59  ? 29.141 14.252  8.095   1.00 13.59 ?  59  ASN   A HB3  1 
ATOM   1469 H  HD21 . ASN   A 1 59  ? 30.074 14.442  4.950   1.00 14.74 ?  59  ASN   A HD21 1 
ATOM   1470 H  HD22 . ASN   A 1 59  ? 30.302 14.876  6.357   1.00 14.74 ?  59  ASN   A HD22 1 
ATOM   1471 N  N    . ALA   A 1 60  ? 29.553 11.246  9.850   1.00 10.36 ?  60  ALA   A N    1 
ATOM   1472 C  CA   . ALA   A 1 60  ? 30.799 10.574  10.210  1.00 10.85 ?  60  ALA   A CA   1 
ATOM   1473 C  C    . ALA   A 1 60  ? 31.034 9.338   9.345   1.00 11.18 ?  60  ALA   A C    1 
ATOM   1474 O  O    . ALA   A 1 60  ? 32.179 9.021   9.003   1.00 11.62 ?  60  ALA   A O    1 
ATOM   1475 C  CB   . ALA   A 1 60  ? 30.799 10.213  11.694  1.00 11.48 ?  60  ALA   A CB   1 
ATOM   1476 H  H    . ALA   A 1 60  ? 28.950 11.255  10.463  1.00 12.44 ?  60  ALA   A H    1 
ATOM   1477 H  HA   . ALA   A 1 60  ? 31.537 11.188  10.058  1.00 13.03 ?  60  ALA   A HA   1 
ATOM   1478 H  HB1  . ALA   A 1 60  ? 31.632 9.772   11.916  1.00 13.78 ?  60  ALA   A HB1  1 
ATOM   1479 H  HB2  . ALA   A 1 60  ? 30.706 11.027  12.221  1.00 13.78 ?  60  ALA   A HB2  1 
ATOM   1480 H  HB3  . ALA   A 1 60  ? 30.051 9.621   11.876  1.00 13.78 ?  60  ALA   A HB3  1 
ATOM   1481 N  N    . MET   A 1 61  ? 29.965 8.621   8.983   1.00 10.58 ?  61  MET   A N    1 
ATOM   1482 C  CA   . MET   A 1 61  ? 30.113 7.489   8.074   1.00 10.33 ?  61  MET   A CA   1 
ATOM   1483 C  C    . MET   A 1 61  ? 30.731 7.917   6.746   1.00 10.35 ?  61  MET   A C    1 
ATOM   1484 O  O    . MET   A 1 61  ? 31.622 7.241   6.223   1.00 10.77 ?  61  MET   A O    1 
ATOM   1485 C  CB   . MET   A 1 61  ? 28.753 6.824   7.858   1.00 10.37 ?  61  MET   A CB   1 
ATOM   1486 C  CG   . MET   A 1 61  ? 28.773 5.660   6.882   1.00 10.79 ?  61  MET   A CG   1 
ATOM   1487 S  SD   . MET   A 1 61  ? 27.138 4.904   6.671   1.00 11.67 ?  61  MET   A SD   1 
ATOM   1488 C  CE   . MET   A 1 61  ? 26.999 4.033   8.232   1.00 12.98 ?  61  MET   A CE   1 
ATOM   1489 H  H    . MET   A 1 61  ? 29.160 8.766   9.249   1.00 12.70 ?  61  MET   A H    1 
ATOM   1490 H  HA   . MET   A 1 61  ? 30.695 6.833   8.490   1.00 12.40 ?  61  MET   A HA   1 
ATOM   1491 H  HB2  . MET   A 1 61  ? 28.432 6.488   8.708   1.00 12.45 ?  61  MET   A HB2  1 
ATOM   1492 H  HB3  . MET   A 1 61  ? 28.135 7.485   7.511   1.00 12.45 ?  61  MET   A HB3  1 
ATOM   1493 H  HG2  . MET   A 1 61  ? 29.063 5.968   6.009   1.00 12.95 ?  61  MET   A HG2  1 
ATOM   1494 H  HG3  . MET   A 1 61  ? 29.375 4.973   7.209   1.00 12.95 ?  61  MET   A HG3  1 
ATOM   1495 H  HE1  . MET   A 1 61  ? 26.160 3.541   8.250   1.00 15.59 ?  61  MET   A HE1  1 
ATOM   1496 H  HE2  . MET   A 1 61  ? 27.743 3.417   8.318   1.00 15.59 ?  61  MET   A HE2  1 
ATOM   1497 H  HE3  . MET   A 1 61  ? 27.016 4.676   8.960   1.00 15.59 ?  61  MET   A HE3  1 
ATOM   1498 N  N    . GLN   A 1 62  ? 30.282 9.046   6.189   1.00 10.36 ?  62  GLN   A N    1 
ATOM   1499 C  CA   . GLN   A 1 62  ? 30.840 9.515   4.923   1.00 10.93 ?  62  GLN   A CA   1 
ATOM   1500 C  C    . GLN   A 1 62  ? 32.312 9.892   5.059   1.00 10.62 ?  62  GLN   A C    1 
ATOM   1501 O  O    . GLN   A 1 62  ? 33.119 9.580   4.175   1.00 11.17 ?  62  GLN   A O    1 
ATOM   1502 C  CB   . GLN   A 1 62  ? 30.034 10.701  4.387   1.00 10.64 ?  62  GLN   A CB   1 
ATOM   1503 C  CG   . GLN   A 1 62  ? 30.402 11.062  2.960   1.00 10.56 ?  62  GLN   A CG   1 
ATOM   1504 C  CD   . GLN   A 1 62  ? 30.069 9.929   2.016   1.00 11.01 ?  62  GLN   A CD   1 
ATOM   1505 O  OE1  . GLN   A 1 62  ? 28.890 9.608   1.822   1.00 11.78 ?  62  GLN   A OE1  1 
ATOM   1506 N  NE2  . GLN   A 1 62  ? 31.092 9.268   1.471   1.00 11.38 ?  62  GLN   A NE2  1 
ATOM   1507 H  H    . GLN   A 1 62  ? 29.672 9.545   6.524   1.00 12.44 ?  62  GLN   A H    1 
ATOM   1508 H  HA   . GLN   A 1 62  ? 30.785 8.793   4.279   1.00 13.12 ?  62  GLN   A HA   1 
ATOM   1509 H  HB2  . GLN   A 1 62  ? 29.092 10.476  4.411   1.00 12.77 ?  62  GLN   A HB2  1 
ATOM   1510 H  HB3  . GLN   A 1 62  ? 30.206 11.475  4.948   1.00 12.77 ?  62  GLN   A HB3  1 
ATOM   1511 H  HG2  . GLN   A 1 62  ? 29.894 11.839  2.689   1.00 12.68 ?  62  GLN   A HG2  1 
ATOM   1512 H  HG3  . GLN   A 1 62  ? 31.352 11.240  2.906   1.00 12.68 ?  62  GLN   A HG3  1 
ATOM   1513 H  HE21 . GLN   A 1 62  ? 31.903 9.503   1.644   1.00 13.66 ?  62  GLN   A HE21 1 
ATOM   1514 H  HE22 . GLN   A 1 62  ? 30.948 8.606   0.936   1.00 13.66 ?  62  GLN   A HE22 1 
ATOM   1515 N  N    . VAL   A 1 63  ? 32.675 10.583  6.142   1.00 10.88 ?  63  VAL   A N    1 
ATOM   1516 C  CA   . VAL   A 1 63  ? 34.065 10.984  6.346   1.00 11.82 ?  63  VAL   A CA   1 
ATOM   1517 C  C    . VAL   A 1 63  ? 34.963 9.752   6.416   1.00 11.21 ?  63  VAL   A C    1 
ATOM   1518 O  O    . VAL   A 1 63  ? 36.012 9.681   5.758   1.00 11.83 ?  63  VAL   A O    1 
ATOM   1519 C  CB   . VAL   A 1 63  ? 34.176 11.866  7.604   1.00 13.61 ?  63  VAL   A CB   1 
ATOM   1520 C  CG1  . VAL   A 1 63  ? 35.626 12.103  7.968   1.00 15.56 ?  63  VAL   A CG1  1 
ATOM   1521 C  CG2  . VAL   A 1 63  ? 33.440 13.188  7.383   1.00 14.03 ?  63  VAL   A CG2  1 
ATOM   1522 H  H    . VAL   A 1 63  ? 32.135 10.833  6.766   1.00 13.06 ?  63  VAL   A H    1 
ATOM   1523 H  HA   . VAL   A 1 63  ? 34.348 11.518  5.589   1.00 14.19 ?  63  VAL   A HA   1 
ATOM   1524 H  HB   . VAL   A 1 63  ? 33.749 11.412  8.349   1.00 16.34 ?  63  VAL   A HB   1 
ATOM   1525 H  HG11 . VAL   A 1 63  ? 35.674 12.844  8.592   1.00 18.68 ?  63  VAL   A HG11 1 
ATOM   1526 H  HG12 . VAL   A 1 63  ? 35.983 11.302  8.377   1.00 18.68 ?  63  VAL   A HG12 1 
ATOM   1527 H  HG13 . VAL   A 1 63  ? 36.118 12.318  7.161   1.00 18.68 ?  63  VAL   A HG13 1 
ATOM   1528 H  HG21 . VAL   A 1 63  ? 33.532 13.737  8.179   1.00 16.84 ?  63  VAL   A HG21 1 
ATOM   1529 H  HG22 . VAL   A 1 63  ? 33.826 13.641  6.620   1.00 16.84 ?  63  VAL   A HG22 1 
ATOM   1530 H  HG23 . VAL   A 1 63  ? 32.500 13.004  7.219   1.00 16.84 ?  63  VAL   A HG23 1 
ATOM   1531 N  N    . GLU   A 1 64  ? 34.546 8.751   7.197   1.00 11.47 ?  64  GLU   A N    1 
ATOM   1532 C  CA   . GLU   A 1 64  ? 35.310 7.514   7.296   1.00 10.92 ?  64  GLU   A CA   1 
ATOM   1533 C  C    . GLU   A 1 64  ? 35.401 6.826   5.942   1.00 10.69 ?  64  GLU   A C    1 
ATOM   1534 O  O    . GLU   A 1 64  ? 36.454 6.280   5.567   1.00 11.42 ?  64  GLU   A O    1 
ATOM   1535 C  CB   . GLU   A 1 64  ? 34.624 6.598   8.311   1.00 11.94 ?  64  GLU   A CB   1 
ATOM   1536 C  CG   . GLU   A 1 64  ? 35.284 5.247   8.476   1.00 12.25 ?  64  GLU   A CG   1 
ATOM   1537 C  CD   . GLU   A 1 64  ? 34.407 4.246   9.195   1.00 12.96 ?  64  GLU   A CD   1 
ATOM   1538 O  OE1  . GLU   A 1 64  ? 33.167 4.339   9.065   1.00 13.69 ?  64  GLU   A OE1  1 
ATOM   1539 O  OE2  . GLU   A 1 64  ? 34.963 3.358   9.882   1.00 13.14 -1 64  GLU   A OE2  1 
ATOM   1540 H  H    . GLU   A 1 64  ? 33.821 8.759   7.659   1.00 13.77 ?  64  GLU   A H    1 
ATOM   1541 H  HA   . GLU   A 1 64  ? 36.209 7.715   7.612   1.00 13.12 ?  64  GLU   A HA   1 
ATOM   1542 H  HB2  . GLU   A 1 64  ? 34.628 7.043   9.179   1.00 14.34 ?  64  GLU   A HB2  1 
ATOM   1543 H  HB3  . GLU   A 1 64  ? 33.708 6.460   8.024   1.00 14.34 ?  64  GLU   A HB3  1 
ATOM   1544 H  HG2  . GLU   A 1 64  ? 35.498 4.889   7.599   1.00 14.70 ?  64  GLU   A HG2  1 
ATOM   1545 H  HG3  . GLU   A 1 64  ? 36.094 5.365   8.990   1.00 14.70 ?  64  GLU   A HG3  1 
ATOM   1546 N  N    . SER   A 1 65  ? 34.279 6.812   5.211   1.00 10.58 ?  65  SER   A N    1 
ATOM   1547 C  CA   . SER   A 1 65  ? 34.227 6.146   3.916   1.00 10.26 ?  65  SER   A CA   1 
ATOM   1548 C  C    . SER   A 1 65  ? 35.150 6.809   2.904   1.00 10.85 ?  65  SER   A C    1 
ATOM   1549 O  O    . SER   A 1 65  ? 35.783 6.127   2.090   1.00 11.81 ?  65  SER   A O    1 
ATOM   1550 C  CB   . SER   A 1 65  ? 32.794 6.146   3.386   1.00 10.91 ?  65  SER   A CB   1 
ATOM   1551 O  OG   . SER   A 1 65  ? 31.941 5.331   4.185   1.00 11.02 ?  65  SER   A OG   1 
ATOM   1552 H  H    . SER   A 1 65  ? 33.543 7.181   5.454   1.00 12.70 ?  65  SER   A H    1 
ATOM   1553 H  HA   . SER   A 1 65  ? 34.511 5.226   4.025   1.00 12.32 ?  65  SER   A HA   1 
ATOM   1554 H  HB2  . SER   A 1 65  ? 32.454 7.049   3.395   1.00 13.10 ?  65  SER   A HB2  1 
ATOM   1555 H  HB3  . SER   A 1 65  ? 32.799 5.795   2.484   1.00 13.10 ?  65  SER   A HB3  1 
ATOM   1556 H  HG   . SER   A 1 65  ? 31.930 5.615   4.982   1.00 13.23 ?  65  SER   A HG   1 
ATOM   1557 N  N    . ASP   A 1 66  ? 35.216 8.142   2.915   1.00 11.42 ?  66  ASP   A N    1 
ATOM   1558 C  CA   . ASP   A 1 66  ? 36.069 8.835   1.955   1.00 12.05 ?  66  ASP   A CA   1 
ATOM   1559 C  C    . ASP   A 1 66  ? 37.536 8.491   2.193   1.00 12.21 ?  66  ASP   A C    1 
ATOM   1560 O  O    . ASP   A 1 66  ? 38.312 8.328   1.242   1.00 12.88 ?  66  ASP   A O    1 
ATOM   1561 C  CB   . ASP   A 1 66  ? 35.841 10.341  2.040   1.00 13.54 ?  66  ASP   A CB   1 
ATOM   1562 C  CG   . ASP   A 1 66  ? 34.507 10.793  1.426   1.00 14.69 ?  66  ASP   A CG   1 
ATOM   1563 O  OD1  . ASP   A 1 66  ? 33.795 9.987   0.791   1.00 15.04 ?  66  ASP   A OD1  1 
ATOM   1564 O  OD2  . ASP   A 1 66  ? 34.198 11.988  1.573   1.00 17.33 -1 66  ASP   A OD2  1 
ATOM   1565 H  H    . ASP   A 1 66  ? 34.773 8.660   3.450   1.00 13.71 ?  66  ASP   A H    1 
ATOM   1566 H  HA   . ASP   A 1 66  ? 35.831 8.542   1.062   1.00 14.47 ?  66  ASP   A HA   1 
ATOM   1567 H  HB2  . ASP   A 1 66  ? 35.840 10.606  2.973   1.00 16.26 ?  66  ASP   A HB2  1 
ATOM   1568 H  HB3  . ASP   A 1 66  ? 36.559 10.790  1.568   1.00 16.26 ?  66  ASP   A HB3  1 
ATOM   1569 N  N    . ASP   A 1 67  ? 37.931 8.365   3.459   1.00 12.16 ?  67  ASP   A N    1 
ATOM   1570 C  CA   . ASP   A 1 67  ? 39.290 7.925   3.763   1.00 13.08 ?  67  ASP   A CA   1 
ATOM   1571 C  C    . ASP   A 1 67  ? 39.517 6.492   3.295   1.00 13.26 ?  67  ASP   A C    1 
ATOM   1572 O  O    . ASP   A 1 67  ? 40.578 6.175   2.749   1.00 14.06 ?  67  ASP   A O    1 
ATOM   1573 C  CB   . ASP   A 1 67  ? 39.557 8.062   5.261   1.00 14.27 ?  67  ASP   A CB   1 
ATOM   1574 C  CG   . ASP   A 1 67  ? 40.851 7.405   5.682   1.00 15.61 ?  67  ASP   A CG   1 
ATOM   1575 O  OD1  . ASP   A 1 67  ? 41.915 8.055   5.564   1.00 18.59 ?  67  ASP   A OD1  1 
ATOM   1576 O  OD2  . ASP   A 1 67  ? 40.811 6.237   6.129   1.00 14.84 -1 67  ASP   A OD2  1 
ATOM   1577 H  H    . ASP   A 1 67  ? 37.444 8.531   4.147   1.00 14.60 ?  67  ASP   A H    1 
ATOM   1578 H  HA   . ASP   A 1 67  ? 39.918 8.494   3.294   1.00 15.71 ?  67  ASP   A HA   1 
ATOM   1579 H  HB2  . ASP   A 1 67  ? 39.609 9.003   5.484   1.00 17.13 ?  67  ASP   A HB2  1 
ATOM   1580 H  HB3  . ASP   A 1 67  ? 38.832 7.642   5.751   1.00 17.13 ?  67  ASP   A HB3  1 
ATOM   1581 N  N    . TYR   A 1 68  ? 38.528 5.612   3.484   1.00 12.54 ?  68  TYR   A N    1 
ATOM   1582 C  CA   . TYR   A 1 68  ? 38.663 4.232   3.017   1.00 12.24 ?  68  TYR   A CA   1 
ATOM   1583 C  C    . TYR   A 1 68  ? 38.889 4.182   1.506   1.00 12.21 ?  68  TYR   A C    1 
ATOM   1584 O  O    . TYR   A 1 68  ? 39.767 3.452   1.022   1.00 13.22 ?  68  TYR   A O    1 
ATOM   1585 C  CB   . TYR   A 1 68  ? 37.429 3.397   3.421   1.00 12.97 ?  68  TYR   A CB   1 
ATOM   1586 C  CG   . TYR   A 1 68  ? 37.459 2.012   2.799   1.00 14.54 ?  68  TYR   A CG   1 
ATOM   1587 C  CD1  . TYR   A 1 68  ? 36.994 1.815   1.507   1.00 15.62 ?  68  TYR   A CD1  1 
ATOM   1588 C  CD2  . TYR   A 1 68  ? 38.002 0.931   3.470   1.00 16.38 ?  68  TYR   A CD2  1 
ATOM   1589 C  CE1  . TYR   A 1 68  ? 37.056 0.606   0.895   1.00 17.61 ?  68  TYR   A CE1  1 
ATOM   1590 C  CE2  . TYR   A 1 68  ? 38.059 -0.330  2.856   1.00 17.01 ?  68  TYR   A CE2  1 
ATOM   1591 C  CZ   . TYR   A 1 68  ? 37.593 -0.461  1.564   1.00 17.37 ?  68  TYR   A CZ   1 
ATOM   1592 O  OH   . TYR   A 1 68  ? 37.664 -1.669  0.927   1.00 19.31 ?  68  TYR   A OH   1 
ATOM   1593 H  H    . TYR   A 1 68  ? 37.776 5.789   3.876   1.00 15.06 ?  68  TYR   A H    1 
ATOM   1594 H  HA   . TYR   A 1 68  ? 39.434 3.836   3.448   1.00 14.69 ?  68  TYR   A HA   1 
ATOM   1595 H  HB2  . TYR   A 1 68  ? 37.412 3.292   4.387   1.00 15.58 ?  68  TYR   A HB2  1 
ATOM   1596 H  HB3  . TYR   A 1 68  ? 36.622 3.845   3.121   1.00 15.58 ?  68  TYR   A HB3  1 
ATOM   1597 H  HD1  . TYR   A 1 68  ? 36.643 2.541   1.043   1.00 18.75 ?  68  TYR   A HD1  1 
ATOM   1598 H  HD2  . TYR   A 1 68  ? 38.339 1.035   4.330   1.00 19.66 ?  68  TYR   A HD2  1 
ATOM   1599 H  HE1  . TYR   A 1 68  ? 36.736 0.506   0.030   1.00 21.13 ?  68  TYR   A HE1  1 
ATOM   1600 H  HE2  . TYR   A 1 68  ? 38.434 -1.064  3.292   1.00 20.42 ?  68  TYR   A HE2  1 
ATOM   1601 H  HH   . TYR   A 1 68  ? 38.001 -2.245  1.439   1.00 23.17 ?  68  TYR   A HH   1 
ATOM   1602 N  N    . ILE   A 1 69  ? 38.097 4.942   0.741   1.00 11.74 ?  69  ILE   A N    1 
ATOM   1603 C  CA   . ILE   A 1 69  ? 38.231 4.922   -0.713  1.00 11.93 ?  69  ILE   A CA   1 
ATOM   1604 C  C    . ILE   A 1 69  ? 39.556 5.540   -1.147  1.00 12.12 ?  69  ILE   A C    1 
ATOM   1605 O  O    . ILE   A 1 69  ? 40.201 5.057   -2.084  1.00 12.67 ?  69  ILE   A O    1 
ATOM   1606 C  CB   . ILE   A 1 69  ? 37.028 5.627   -1.370  1.00 12.97 ?  69  ILE   A CB   1 
ATOM   1607 C  CG1  . ILE   A 1 69  ? 35.723 4.880   -1.089  1.00 13.37 ?  69  ILE   A CG1  1 
ATOM   1608 C  CG2  . ILE   A 1 69  ? 37.262 5.822   -2.869  1.00 14.14 ?  69  ILE   A CG2  1 
ATOM   1609 C  CD1  . ILE   A 1 69  ? 35.562 3.589   -1.865  1.00 14.54 ?  69  ILE   A CD1  1 
ATOM   1610 H  H    . ILE   A 1 69  ? 37.485 5.469   1.040   1.00 14.09 ?  69  ILE   A H    1 
ATOM   1611 H  HA   . ILE   A 1 69  ? 38.231 3.998   -1.006  1.00 14.32 ?  69  ILE   A HA   1 
ATOM   1612 H  HB   . ILE   A 1 69  ? 36.951 6.501   -0.973  1.00 15.57 ?  69  ILE   A HB   1 
ATOM   1613 H  HG12 . ILE   A 1 69  ? 35.687 4.659   -0.142  1.00 16.05 ?  69  ILE   A HG12 1 
ATOM   1614 H  HG13 . ILE   A 1 69  ? 34.978 5.457   -1.316  1.00 16.05 ?  69  ILE   A HG13 1 
ATOM   1615 H  HG21 . ILE   A 1 69  ? 36.414 6.020   -3.299  1.00 16.97 ?  69  ILE   A HG21 1 
ATOM   1616 H  HG22 . ILE   A 1 69  ? 37.875 6.565   -3.001  1.00 16.97 ?  69  ILE   A HG22 1 
ATOM   1617 H  HG23 . ILE   A 1 69  ? 37.640 5.012   -3.245  1.00 16.97 ?  69  ILE   A HG23 1 
ATOM   1618 H  HD11 . ILE   A 1 69  ? 34.768 3.130   -1.549  1.00 17.45 ?  69  ILE   A HD11 1 
ATOM   1619 H  HD12 . ILE   A 1 69  ? 35.467 3.798   -2.808  1.00 17.45 ?  69  ILE   A HD12 1 
ATOM   1620 H  HD13 . ILE   A 1 69  ? 36.342 3.033   -1.724  1.00 17.45 ?  69  ILE   A HD13 1 
ATOM   1621 N  N    . ALA   A 1 70  ? 39.969 6.623   -0.495  1.00 12.38 ?  70  ALA   A N    1 
ATOM   1622 C  CA   . ALA   A 1 70  ? 41.244 7.233   -0.853  1.00 13.55 ?  70  ALA   A CA   1 
ATOM   1623 C  C    . ALA   A 1 70  ? 42.398 6.251   -0.681  1.00 13.83 ?  70  ALA   A C    1 
ATOM   1624 O  O    . ALA   A 1 70  ? 43.373 6.298   -1.439  1.00 15.60 ?  70  ALA   A O    1 
ATOM   1625 C  CB   . ALA   A 1 70  ? 41.471 8.493   -0.018  1.00 14.02 ?  70  ALA   A CB   1 
ATOM   1626 H  H    . ALA   A 1 70  ? 39.540 7.016   0.134   1.00 14.87 ?  70  ALA   A H    1 
ATOM   1627 H  HA   . ALA   A 1 70  ? 41.216 7.498   -1.785  1.00 16.27 ?  70  ALA   A HA   1 
ATOM   1628 H  HB1  . ALA   A 1 70  ? 42.327 8.885   -0.268  1.00 16.83 ?  70  ALA   A HB1  1 
ATOM   1629 H  HB2  . ALA   A 1 70  ? 40.758 9.123   -0.193  1.00 16.83 ?  70  ALA   A HB2  1 
ATOM   1630 H  HB3  . ALA   A 1 70  ? 41.483 8.253   0.921   1.00 16.83 ?  70  ALA   A HB3  1 
ATOM   1631 N  N    . THR   A 1 71  ? 42.299 5.343   0.290   1.00 13.22 ?  71  THR   A N    1 
ATOM   1632 C  CA   . THR   A 1 71  ? 43.359 4.371   0.540   1.00 15.00 ?  71  THR   A CA   1 
ATOM   1633 C  C    . THR   A 1 71  ? 43.239 3.146   -0.356  1.00 15.09 ?  71  THR   A C    1 
ATOM   1634 O  O    . THR   A 1 71  ? 44.252 2.634   -0.853  1.00 16.98 ?  71  THR   A O    1 
ATOM   1635 C  CB   . THR   A 1 71  ? 43.303 3.936   2.002   1.00 17.32 ?  71  THR   A CB   1 
ATOM   1636 O  OG1  . THR   A 1 71  ? 43.557 5.066   2.840   1.00 18.98 ?  71  THR   A OG1  1 
ATOM   1637 C  CG2  . THR   A 1 71  ? 44.313 2.815   2.296   1.00 18.51 ?  71  THR   A CG2  1 
ATOM   1638 H  H    . THR   A 1 71  ? 41.618 5.257   0.809   1.00 15.88 ?  71  THR   A H    1 
ATOM   1639 H  HA   . THR   A 1 71  ? 44.218 4.782   0.372   1.00 18.01 ?  71  THR   A HA   1 
ATOM   1640 H  HB   . THR   A 1 71  ? 42.415 3.595   2.196   1.00 20.80 ?  71  THR   A HB   1 
ATOM   1641 H  HG1  . THR   A 1 71  ? 42.983 5.660   2.694   1.00 22.78 ?  71  THR   A HG1  1 
ATOM   1642 H  HG21 . THR   A 1 71  ? 44.441 2.730   3.254   1.00 22.22 ?  71  THR   A HG21 1 
ATOM   1643 H  HG22 . THR   A 1 71  ? 43.992 1.969   1.947   1.00 22.22 ?  71  THR   A HG22 1 
ATOM   1644 H  HG23 . THR   A 1 71  ? 45.169 3.022   1.885   1.00 22.22 ?  71  THR   A HG23 1 
ATOM   1645 N  N    . ASN   A 1 72  ? 42.016 2.650   -0.556  1.00 14.23 ?  72  ASN   A N    1 
ATOM   1646 C  CA   . ASN   A 1 72  ? 41.803 1.318   -1.108  1.00 13.88 ?  72  ASN   A CA   1 
ATOM   1647 C  C    . ASN   A 1 72  ? 41.178 1.304   -2.490  1.00 14.13 ?  72  ASN   A C    1 
ATOM   1648 O  O    . ASN   A 1 72  ? 41.190 0.251   -3.139  1.00 15.23 ?  72  ASN   A O    1 
ATOM   1649 C  CB   . ASN   A 1 72  ? 40.911 0.504   -0.161  1.00 15.26 ?  72  ASN   A CB   1 
ATOM   1650 C  CG   . ASN   A 1 72  ? 41.534 0.331   1.201   1.00 16.27 ?  72  ASN   A CG   1 
ATOM   1651 O  OD1  . ASN   A 1 72  ? 41.092 0.926   2.182   1.00 17.94 ?  72  ASN   A OD1  1 
ATOM   1652 N  ND2  . ASN   A 1 72  ? 42.581 -0.462  1.266   1.00 17.00 ?  72  ASN   A ND2  1 
ATOM   1653 H  H    . ASN   A 1 72  ? 41.284 3.074   -0.376  1.00 17.09 ?  72  ASN   A H    1 
ATOM   1654 H  HA   . ASN   A 1 72  ? 42.654 0.867   -1.170  1.00 16.67 ?  72  ASN   A HA   1 
ATOM   1655 H  HB2  . ASN   A 1 72  ? 40.062 0.959   -0.048  1.00 18.31 ?  72  ASN   A HB2  1 
ATOM   1656 H  HB3  . ASN   A 1 72  ? 40.770 -0.379  -0.535  1.00 18.31 ?  72  ASN   A HB3  1 
ATOM   1657 H  HD21 . ASN   A 1 72  ? 42.975 -0.588  2.022   1.00 20.41 ?  72  ASN   A HD21 1 
ATOM   1658 H  HD22 . ASN   A 1 72  ? 42.865 -0.855  0.561   1.00 20.41 ?  72  ASN   A HD22 1 
ATOM   1659 N  N    . GLY   A 1 73  ? 40.632 2.421   -2.955  1.00 13.84 ?  73  GLY   A N    1 
ATOM   1660 C  CA   . GLY   A 1 73  ? 39.896 2.438   -4.193  1.00 13.55 ?  73  GLY   A CA   1 
ATOM   1661 C  C    . GLY   A 1 73  ? 38.506 1.852   -4.013  1.00 12.81 ?  73  GLY   A C    1 
ATOM   1662 O  O    . GLY   A 1 73  ? 38.129 1.401   -2.927  1.00 13.61 ?  73  GLY   A O    1 
ATOM   1663 H  H    . GLY   A 1 73  ? 40.683 3.191   -2.570  1.00 16.61 ?  73  GLY   A H    1 
ATOM   1664 H  HA2  . GLY   A 1 73  ? 39.812 3.352   -4.509  1.00 16.27 ?  73  GLY   A HA2  1 
ATOM   1665 H  HA3  . GLY   A 1 73  ? 40.365 1.919   -4.863  1.00 16.27 ?  73  GLY   A HA3  1 
ATOM   1666 N  N    . PRO   A 1 74  ? 37.720 1.865   -5.087  1.00 13.42 ?  74  PRO   A N    1 
ATOM   1667 C  CA   . PRO   A 1 74  ? 36.325 1.425   -4.992  1.00 13.43 ?  74  PRO   A CA   1 
ATOM   1668 C  C    . PRO   A 1 74  ? 36.181 -0.061  -4.687  1.00 12.99 ?  74  PRO   A C    1 
ATOM   1669 O  O    . PRO   A 1 74  ? 37.049 -0.890  -4.983  1.00 13.78 ?  74  PRO   A O    1 
ATOM   1670 C  CB   . PRO   A 1 74  ? 35.759 1.740   -6.382  1.00 15.52 ?  74  PRO   A CB   1 
ATOM   1671 C  CG   . PRO   A 1 74  ? 36.704 2.730   -6.992  1.00 18.16 ?  74  PRO   A CG   1 
ATOM   1672 C  CD   . PRO   A 1 74  ? 38.043 2.385   -6.426  1.00 15.85 ?  74  PRO   A CD   1 
ATOM   1673 H  HA   . PRO   A 1 74  ? 35.847 1.940   -4.320  1.00 16.12 ?  74  PRO   A HA   1 
ATOM   1674 H  HB2  . PRO   A 1 74  ? 35.719 0.926   -6.907  1.00 18.63 ?  74  PRO   A HB2  1 
ATOM   1675 H  HB3  . PRO   A 1 74  ? 34.869 2.125   -6.288  1.00 18.63 ?  74  PRO   A HB3  1 
ATOM   1676 H  HG2  . PRO   A 1 74  ? 36.704 2.628   -7.955  1.00 21.79 ?  74  PRO   A HG2  1 
ATOM   1677 H  HG3  . PRO   A 1 74  ? 36.446 3.627   -6.737  1.00 21.79 ?  74  PRO   A HG3  1 
ATOM   1678 H  HD2  . PRO   A 1 74  ? 38.476 1.697   -6.958  1.00 19.02 ?  74  PRO   A HD2  1 
ATOM   1679 H  HD3  . PRO   A 1 74  ? 38.595 3.182   -6.363  1.00 19.02 ?  74  PRO   A HD3  1 
ATOM   1680 N  N    . LEU   A 1 75  ? 35.044 -0.388  -4.088  1.00 11.97 ?  75  LEU   A N    1 
ATOM   1681 C  CA   . LEU   A 1 75  ? 34.650 -1.778  -3.937  1.00 11.65 ?  75  LEU   A CA   1 
ATOM   1682 C  C    . LEU   A 1 75  ? 34.262 -2.356  -5.297  1.00 11.97 ?  75  LEU   A C    1 
ATOM   1683 O  O    . LEU   A 1 75  ? 34.126 -1.645  -6.295  1.00 13.63 ?  75  LEU   A O    1 
ATOM   1684 C  CB   . LEU   A 1 75  ? 33.465 -1.902  -2.979  1.00 11.77 ?  75  LEU   A CB   1 
ATOM   1685 C  CG   . LEU   A 1 75  ? 33.667 -1.512  -1.520  1.00 13.44 ?  75  LEU   A CG   1 
ATOM   1686 C  CD1  . LEU   A 1 75  ? 32.386 -1.744  -0.722  1.00 15.75 ?  75  LEU   A CD1  1 
ATOM   1687 C  CD2  . LEU   A 1 75  ? 34.817 -2.238  -0.880  1.00 16.91 ?  75  LEU   A CD2  1 
ATOM   1688 H  H    . LEU   A 1 75  ? 34.481 0.173   -3.762  1.00 14.38 ?  75  LEU   A H    1 
ATOM   1689 H  HA   . LEU   A 1 75  ? 35.391 -2.292  -3.585  1.00 13.99 ?  75  LEU   A HA   1 
ATOM   1690 H  HB2  . LEU   A 1 75  ? 32.746 -1.350  -3.317  1.00 14.14 ?  75  LEU   A HB2  1 
ATOM   1691 H  HB3  . LEU   A 1 75  ? 33.176 -2.832  -2.983  1.00 14.14 ?  75  LEU   A HB3  1 
ATOM   1692 H  HG   . LEU   A 1 75  ? 33.871 -0.568  -1.477  1.00 16.13 ?  75  LEU   A HG   1 
ATOM   1693 H  HD11 . LEU   A 1 75  ? 32.537 -1.490  0.204   1.00 18.91 ?  75  LEU   A HD11 1 
ATOM   1694 H  HD12 . LEU   A 1 75  ? 31.679 -1.200  -1.102  1.00 18.91 ?  75  LEU   A HD12 1 
ATOM   1695 H  HD13 . LEU   A 1 75  ? 32.146 -2.682  -0.770  1.00 18.91 ?  75  LEU   A HD13 1 
ATOM   1696 H  HD21 . LEU   A 1 75  ? 34.870 -1.991  0.057   1.00 20.30 ?  75  LEU   A HD21 1 
ATOM   1697 H  HD22 . LEU   A 1 75  ? 34.678 -3.194  -0.962  1.00 20.30 ?  75  LEU   A HD22 1 
ATOM   1698 H  HD23 . LEU   A 1 75  ? 35.643 -1.987  -1.330  1.00 20.30 ?  75  LEU   A HD23 1 
ATOM   1699 N  N    . LYS   A 1 76  ? 34.089 -3.677  -5.319  1.00 12.48 ?  76  LYS   A N    1 
ATOM   1700 C  CA   . LYS   A 1 76  ? 33.499 -4.391  -6.446  1.00 12.93 ?  76  LYS   A CA   1 
ATOM   1701 C  C    . LYS   A 1 76  ? 31.989 -4.481  -6.255  1.00 11.40 ?  76  LYS   A C    1 
ATOM   1702 O  O    . LYS   A 1 76  ? 31.507 -4.591  -5.131  1.00 11.53 ?  76  LYS   A O    1 
ATOM   1703 C  CB   . LYS   A 1 76  ? 34.046 -5.826  -6.497  1.00 14.91 ?  76  LYS   A CB   1 
ATOM   1704 C  CG   . LYS   A 1 76  ? 35.558 -5.933  -6.693  1.00 16.19 ?  76  LYS   A CG   1 
ATOM   1705 C  CD   . LYS   A 1 76  ? 36.069 -7.341  -6.466  1.00 17.50 ?  76  LYS   A CD   1 
ATOM   1706 C  CE   . LYS   A 1 76  ? 37.567 -7.418  -6.673  1.00 19.58 ?  76  LYS   A CE   1 
ATOM   1707 N  NZ   . LYS   A 1 76  ? 38.091 -8.778  -6.449  1.00 20.47 ?  76  LYS   A NZ   1 
ATOM   1708 H  H    . LYS   A 1 76  ? 34.312 -4.197  -4.669  1.00 14.98 ?  76  LYS   A H    1 
ATOM   1709 H  HA   . LYS   A 1 76  ? 33.698 -3.935  -7.279  1.00 15.53 ?  76  LYS   A HA   1 
ATOM   1710 H  HB2  . LYS   A 1 76  ? 33.829 -6.268  -5.663  1.00 17.90 ?  76  LYS   A HB2  1 
ATOM   1711 H  HB3  . LYS   A 1 76  ? 33.622 -6.289  -7.234  1.00 17.90 ?  76  LYS   A HB3  1 
ATOM   1712 H  HG2  . LYS   A 1 76  ? 35.778 -5.672  -7.603  1.00 19.43 ?  76  LYS   A HG2  1 
ATOM   1713 H  HG3  . LYS   A 1 76  ? 36.003 -5.343  -6.063  1.00 19.43 ?  76  LYS   A HG3  1 
ATOM   1714 H  HD2  . LYS   A 1 76  ? 35.867 -7.611  -5.555  1.00 21.00 ?  76  LYS   A HD2  1 
ATOM   1715 H  HD3  . LYS   A 1 76  ? 35.637 -7.942  -7.096  1.00 21.00 ?  76  LYS   A HD3  1 
ATOM   1716 H  HE2  . LYS   A 1 76  ? 37.772 -7.159  -7.584  1.00 23.50 ?  76  LYS   A HE2  1 
ATOM   1717 H  HE3  . LYS   A 1 76  ? 38.002 -6.820  -6.047  1.00 23.50 ?  76  LYS   A HE3  1 
ATOM   1718 H  HZ1  . LYS   A 1 76  ? 38.969 -8.797  -6.579  1.00 24.56 ?  76  LYS   A HZ1  1 
ATOM   1719 H  HZ2  . LYS   A 1 76  ? 37.914 -9.045  -5.617  1.00 24.56 ?  76  LYS   A HZ2  1 
ATOM   1720 H  HZ3  . LYS   A 1 76  ? 37.705 -9.354  -7.017  1.00 24.56 ?  76  LYS   A HZ3  1 
ATOM   1721 N  N    . VAL   A 1 77  ? 31.240 -4.461  -7.359  1.00 11.74 ?  77  VAL   A N    1 
ATOM   1722 C  CA   . VAL   A 1 77  ? 29.831 -4.841  -7.261  1.00 11.81 ?  77  VAL   A CA   1 
ATOM   1723 C  C    . VAL   A 1 77  ? 29.768 -6.293  -6.815  1.00 11.70 ?  77  VAL   A C    1 
ATOM   1724 O  O    . VAL   A 1 77  ? 30.414 -7.165  -7.409  1.00 12.12 ?  77  VAL   A O    1 
ATOM   1725 C  CB   . VAL   A 1 77  ? 29.106 -4.631  -8.596  1.00 13.18 ?  77  VAL   A CB   1 
ATOM   1726 C  CG1  . VAL   A 1 77  ? 27.647 -5.044  -8.467  1.00 14.21 ?  77  VAL   A CG1  1 
ATOM   1727 C  CG2  . VAL   A 1 77  ? 29.209 -3.179  -9.040  1.00 14.35 ?  77  VAL   A CG2  1 
ATOM   1728 H  H    . VAL   A 1 77  ? 31.517 -4.245  -8.142  1.00 14.10 ?  77  VAL   A H    1 
ATOM   1729 H  HA   . VAL   A 1 77  ? 29.400 -4.295  -6.589  1.00 14.18 ?  77  VAL   A HA   1 
ATOM   1730 H  HB   . VAL   A 1 77  ? 29.522 -5.183  -9.279  1.00 15.82 ?  77  VAL   A HB   1 
ATOM   1731 H  HG11 . VAL   A 1 77  ? 27.165 -4.731  -9.246  1.00 17.06 ?  77  VAL   A HG11 1 
ATOM   1732 H  HG12 . VAL   A 1 77  ? 27.597 -6.009  -8.408  1.00 17.06 ?  77  VAL   A HG12 1 
ATOM   1733 H  HG13 . VAL   A 1 77  ? 27.281 -4.640  -7.665  1.00 17.06 ?  77  VAL   A HG13 1 
ATOM   1734 H  HG21 . VAL   A 1 77  ? 28.695 -3.063  -9.853  1.00 17.22 ?  77  VAL   A HG21 1 
ATOM   1735 H  HG22 . VAL   A 1 77  ? 28.853 -2.613  -8.338  1.00 17.22 ?  77  VAL   A HG22 1 
ATOM   1736 H  HG23 . VAL   A 1 77  ? 30.140 -2.963  -9.201  1.00 17.22 ?  77  VAL   A HG23 1 
ATOM   1737 N  N    . GLY   A 1 78  ? 28.995 -6.562  -5.760  1.00 11.29 ?  78  GLY   A N    1 
ATOM   1738 C  CA   . GLY   A 1 78  ? 28.975 -7.856  -5.114  1.00 11.53 ?  78  GLY   A CA   1 
ATOM   1739 C  C    . GLY   A 1 78  ? 29.886 -7.946  -3.910  1.00 11.33 ?  78  GLY   A C    1 
ATOM   1740 O  O    . GLY   A 1 78  ? 29.828 -8.948  -3.182  1.00 11.46 ?  78  GLY   A O    1 
ATOM   1741 H  H    . GLY   A 1 78  ? 28.460 -5.989  -5.402  1.00 13.56 ?  78  GLY   A H    1 
ATOM   1742 H  HA2  . GLY   A 1 78  ? 28.073 -8.056  -4.827  1.00 13.85 ?  78  GLY   A HA2  1 
ATOM   1743 H  HA3  . GLY   A 1 78  ? 29.248 -8.536  -5.754  1.00 13.85 ?  78  GLY   A HA3  1 
ATOM   1744 N  N    . GLY   A 1 79  ? 30.740 -6.940  -3.698  1.00 11.18 ?  79  GLY   A N    1 
ATOM   1745 C  CA   . GLY   A 1 79  ? 31.711 -6.946  -2.627  1.00 11.05 ?  79  GLY   A CA   1 
ATOM   1746 C  C    . GLY   A 1 79  ? 31.254 -6.156  -1.410  1.00 10.90 ?  79  GLY   A C    1 
ATOM   1747 O  O    . GLY   A 1 79  ? 30.132 -5.650  -1.337  1.00 11.21 ?  79  GLY   A O    1 
ATOM   1748 H  H    . GLY   A 1 79  ? 30.780 -6.231  -4.185  1.00 13.43 ?  79  GLY   A H    1 
ATOM   1749 H  HA2  . GLY   A 1 79  ? 31.880 -7.867  -2.353  1.00 13.26 ?  79  GLY   A HA2  1 
ATOM   1750 H  HA3  . GLY   A 1 79  ? 32.545 -6.569  -2.941  1.00 13.26 ?  79  GLY   A HA3  1 
ATOM   1751 N  N    . SER   A 1 80  ? 32.156 -6.063  -0.435  1.00 11.30 ?  80  SER   A N    1 
ATOM   1752 C  CA   . SER   A 1 80  ? 31.835 -5.432  0.836   1.00 10.85 ?  80  SER   A CA   1 
ATOM   1753 C  C    . SER   A 1 80  ? 33.108 -4.976  1.531   1.00 10.66 ?  80  SER   A C    1 
ATOM   1754 O  O    . SER   A 1 80  ? 34.223 -5.401  1.197   1.00 12.37 ?  80  SER   A O    1 
ATOM   1755 C  CB   . SER   A 1 80  ? 31.077 -6.398  1.756   1.00 11.78 ?  80  SER   A CB   1 
ATOM   1756 O  OG   . SER   A 1 80  ? 31.915 -7.445  2.234   1.00 13.41 ?  80  SER   A OG   1 
ATOM   1757 H  H    . SER   A 1 80  ? 32.968 -6.344  -0.492  1.00 13.57 ?  80  SER   A H    1 
ATOM   1758 H  HA   . SER   A 1 80  ? 31.279 -4.658  0.664   1.00 13.03 ?  80  SER   A HA   1 
ATOM   1759 H  HB2  . SER   A 1 80  ? 30.733 -5.903  2.515   1.00 14.14 ?  80  SER   A HB2  1 
ATOM   1760 H  HB3  . SER   A 1 80  ? 30.339 -6.788  1.258   1.00 14.14 ?  80  SER   A HB3  1 
ATOM   1761 H  HG   . SER   A 1 80  ? 32.217 -7.885  1.580   1.00 16.09 ?  80  SER   A HG   1 
ATOM   1762 N  N    . CYS   A 1 81  ? 32.921 -4.128  2.540   1.00 10.43 ?  81  CYS   A N    1 
ATOM   1763 C  CA   . CYS   A 1 81  ? 33.972 -3.844  3.505   1.00 10.67 ?  81  CYS   A CA   1 
ATOM   1764 C  C    . CYS   A 1 81  ? 33.331 -3.611  4.866   1.00 10.83 ?  81  CYS   A C    1 
ATOM   1765 O  O    . CYS   A 1 81  ? 32.164 -3.206  4.958   1.00 11.84 ?  81  CYS   A O    1 
ATOM   1766 C  CB   . CYS   A 1 81  ? 34.835 -2.648  3.085   1.00 11.93 ?  81  CYS   A CB   1 
ATOM   1767 S  SG   . CYS   A 1 81  ? 33.934 -1.070  3.097   1.00 11.73 ?  81  CYS   A SG   1 
ATOM   1768 H  H    . CYS   A 1 81  ? 32.186 -3.701  2.689   1.00 12.53 ?  81  CYS   A H    1 
ATOM   1769 H  HA   . CYS   A 1 81  ? 34.555 -4.615  3.570   1.00 12.81 ?  81  CYS   A HA   1 
ATOM   1770 H  HB2  . CYS   A 1 81  ? 35.585 -2.570  3.696   1.00 14.33 ?  81  CYS   A HB2  1 
ATOM   1771 H  HB3  . CYS   A 1 81  ? 35.165 -2.796  2.182   1.00 14.33 ?  81  CYS   A HB3  1 
ATOM   1772 H  HG   . CYS   A 1 81  ? 34.681 -0.191  2.761   1.00 14.08 ?  81  CYS   A HG   1 
ATOM   1773 N  N    . VAL   A 1 82  ? 34.102 -3.871  5.919   1.00 11.05 ?  82  VAL   A N    1 
ATOM   1774 C  CA   . VAL   A 1 82  ? 33.682 -3.627  7.293   1.00 11.64 ?  82  VAL   A CA   1 
ATOM   1775 C  C    . VAL   A 1 82  ? 34.279 -2.307  7.760   1.00 11.63 ?  82  VAL   A C    1 
ATOM   1776 O  O    . VAL   A 1 82  ? 35.504 -2.131  7.745   1.00 12.61 ?  82  VAL   A O    1 
ATOM   1777 C  CB   . VAL   A 1 82  ? 34.101 -4.771  8.230   1.00 13.20 ?  82  VAL   A CB   1 
ATOM   1778 C  CG1  . VAL   A 1 82  ? 33.661 -4.474  9.658   1.00 14.50 ?  82  VAL   A CG1  1 
ATOM   1779 C  CG2  . VAL   A 1 82  ? 33.538 -6.100  7.754   1.00 14.26 ?  82  VAL   A CG2  1 
ATOM   1780 H  H    . VAL   A 1 82  ? 34.894 -4.215  5.858   1.00 13.27 ?  82  VAL   A H    1 
ATOM   1781 H  HA   . VAL   A 1 82  ? 32.715 -3.553  7.317   1.00 13.97 ?  82  VAL   A HA   1 
ATOM   1782 H  HB   . VAL   A 1 82  ? 35.068 -4.836  8.227   1.00 15.85 ?  82  VAL   A HB   1 
ATOM   1783 H  HG11 . VAL   A 1 82  ? 33.754 -5.278  10.192  1.00 17.41 ?  82  VAL   A HG11 1 
ATOM   1784 H  HG12 . VAL   A 1 82  ? 34.215 -3.768  10.028  1.00 17.41 ?  82  VAL   A HG12 1 
ATOM   1785 H  HG13 . VAL   A 1 82  ? 32.730 -4.191  9.653   1.00 17.41 ?  82  VAL   A HG13 1 
ATOM   1786 H  HG21 . VAL   A 1 82  ? 33.787 -6.793  8.389   1.00 17.12 ?  82  VAL   A HG21 1 
ATOM   1787 H  HG22 . VAL   A 1 82  ? 32.572 -6.035  7.701   1.00 17.12 ?  82  VAL   A HG22 1 
ATOM   1788 H  HG23 . VAL   A 1 82  ? 33.905 -6.307  6.881   1.00 17.12 ?  82  VAL   A HG23 1 
ATOM   1789 N  N    . LEU   A 1 83  ? 33.419 -1.386  8.181   1.00 11.37 ?  83  LEU   A N    1 
ATOM   1790 C  CA   . LEU   A 1 83  ? 33.830 -0.110  8.750   1.00 11.18 ?  83  LEU   A CA   1 
ATOM   1791 C  C    . LEU   A 1 83  ? 33.119 0.065   10.086  1.00 11.29 ?  83  LEU   A C    1 
ATOM   1792 O  O    . LEU   A 1 83  ? 32.407 -0.827  10.554  1.00 11.97 ?  83  LEU   A O    1 
ATOM   1793 C  CB   . LEU   A 1 83  ? 33.572 1.045   7.771   1.00 11.56 ?  83  LEU   A CB   1 
ATOM   1794 C  CG   . LEU   A 1 83  ? 34.472 1.036   6.527   1.00 12.56 ?  83  LEU   A CG   1 
ATOM   1795 C  CD1  . LEU   A 1 83  ? 34.038 2.087   5.516   1.00 13.08 ?  83  LEU   A CD1  1 
ATOM   1796 C  CD2  . LEU   A 1 83  ? 35.940 1.239   6.897   1.00 13.43 ?  83  LEU   A CD2  1 
ATOM   1797 H  H    . LEU   A 1 83  ? 32.565 -1.478  8.137   1.00 13.65 ?  83  LEU   A H    1 
ATOM   1798 H  HA   . LEU   A 1 83  ? 34.783 -0.133  8.923   1.00 13.42 ?  83  LEU   A HA   1 
ATOM   1799 H  HB2  . LEU   A 1 83  ? 32.651 1.001   7.463   1.00 13.88 ?  83  LEU   A HB2  1 
ATOM   1800 H  HB3  . LEU   A 1 83  ? 33.718 1.889   8.228   1.00 13.88 ?  83  LEU   A HB3  1 
ATOM   1801 H  HG   . LEU   A 1 83  ? 34.394 0.169   6.100   1.00 15.08 ?  83  LEU   A HG   1 
ATOM   1802 H  HD11 . LEU   A 1 83  ? 34.626 2.039   4.741   1.00 15.70 ?  83  LEU   A HD11 1 
ATOM   1803 H  HD12 . LEU   A 1 83  ? 33.124 1.906   5.243   1.00 15.70 ?  83  LEU   A HD12 1 
ATOM   1804 H  HD13 . LEU   A 1 83  ? 34.098 2.963   5.921   1.00 15.70 ?  83  LEU   A HD13 1 
ATOM   1805 H  HD21 . LEU   A 1 83  ? 36.454 1.398   6.089   1.00 16.12 ?  83  LEU   A HD21 1 
ATOM   1806 H  HD22 . LEU   A 1 83  ? 36.016 2.005   7.490   1.00 16.12 ?  83  LEU   A HD22 1 
ATOM   1807 H  HD23 . LEU   A 1 83  ? 36.270 0.444   7.345   1.00 16.12 ?  83  LEU   A HD23 1 
ATOM   1808 N  N    . SER   A 1 84  ? 33.323 1.214   10.719  1.00 11.85 ?  84  SER   A N    1 
ATOM   1809 C  CA   . SER   A 1 84  ? 32.684 1.471   11.999  1.00 11.85 ?  84  SER   A CA   1 
ATOM   1810 C  C    . SER   A 1 84  ? 31.167 1.552   11.851  1.00 11.90 ?  84  SER   A C    1 
ATOM   1811 O  O    . SER   A 1 84  ? 30.642 2.011   10.839  1.00 11.97 ?  84  SER   A O    1 
ATOM   1812 C  CB   . SER   A 1 84  ? 33.178 2.797   12.566  1.00 13.09 ?  84  SER   A CB   1 
ATOM   1813 O  OG   . SER   A 1 84  ? 32.542 3.085   13.793  1.00 13.81 ?  84  SER   A OG   1 
ATOM   1814 H  H    . SER   A 1 84  ? 33.818 1.857   10.424  1.00 14.23 ?  84  SER   A H    1 
ATOM   1815 H  HA   . SER   A 1 84  ? 32.903 0.756   12.616  1.00 14.23 ?  84  SER   A HA   1 
ATOM   1816 H  HB2  . SER   A 1 84  ? 34.137 2.741   12.701  1.00 15.71 ?  84  SER   A HB2  1 
ATOM   1817 H  HB3  . SER   A 1 84  ? 32.971 3.503   11.935  1.00 15.71 ?  84  SER   A HB3  1 
ATOM   1818 H  HG   . SER   A 1 84  ? 32.829 3.806   14.103  1.00 16.57 ?  84  SER   A HG   1 
ATOM   1819 N  N    . GLY   A 1 85  ? 30.460 1.131   12.895  1.00 12.45 ?  85  GLY   A N    1 
ATOM   1820 C  CA   . GLY   A 1 85  ? 29.035 1.367   12.975  1.00 13.13 ?  85  GLY   A CA   1 
ATOM   1821 C  C    . GLY   A 1 85  ? 28.665 2.678   13.628  1.00 12.62 ?  85  GLY   A C    1 
ATOM   1822 O  O    . GLY   A 1 85  ? 27.475 2.983   13.756  1.00 13.40 ?  85  GLY   A O    1 
ATOM   1823 H  H    . GLY   A 1 85  ? 30.789 0.704   13.568  1.00 14.95 ?  85  GLY   A H    1 
ATOM   1824 H  HA2  . GLY   A 1 85  ? 28.664 1.355   12.075  1.00 15.76 ?  85  GLY   A HA2  1 
ATOM   1825 H  HA3  . GLY   A 1 85  ? 28.623 0.657   13.479  1.00 15.76 ?  85  GLY   A HA3  1 
ATOM   1826 N  N    . HIS   A 1 86  ? 29.647 3.467   14.053  1.00 12.46 ?  86  HIS   A N    1 
ATOM   1827 C  CA   . HIS   A 1 86  ? 29.414 4.801   14.619  1.00 13.07 ?  86  HIS   A CA   1 
ATOM   1828 C  C    . HIS   A 1 86  ? 28.433 4.676   15.779  1.00 13.65 ?  86  HIS   A C    1 
ATOM   1829 O  O    . HIS   A 1 86  ? 28.632 3.813   16.649  1.00 15.07 ?  86  HIS   A O    1 
ATOM   1830 C  CB   . HIS   A 1 86  ? 29.025 5.775   13.514  1.00 13.31 ?  86  HIS   A CB   1 
ATOM   1831 C  CG   . HIS   A 1 86  ? 30.079 5.884   12.476  1.00 13.25 ?  86  HIS   A CG   1 
ATOM   1832 N  ND1  . HIS   A 1 86  ? 31.151 6.742   12.598  1.00 14.59 ?  86  HIS   A ND1  1 
ATOM   1833 C  CD2  . HIS   A 1 86  ? 30.282 5.178   11.342  1.00 12.80 ?  86  HIS   A CD2  1 
ATOM   1834 C  CE1  . HIS   A 1 86  ? 31.948 6.581   11.558  1.00 14.30 ?  86  HIS   A CE1  1 
ATOM   1835 N  NE2  . HIS   A 1 86  ? 31.450 5.633   10.787  1.00 13.69 ?  86  HIS   A NE2  1 
ATOM   1836 H  H    . HIS   A 1 86  ? 30.475 3.252   14.034  1.00 14.96 ?  86  HIS   A H    1 
ATOM   1837 H  HA   . HIS   A 1 86  ? 30.250 5.127   14.985  1.00 15.69 ?  86  HIS   A HA   1 
ATOM   1838 H  HB2  . HIS   A 1 86  ? 28.209 5.472   13.082  1.00 15.98 ?  86  HIS   A HB2  1 
ATOM   1839 H  HB3  . HIS   A 1 86  ? 28.887 6.663   13.890  1.00 15.98 ?  86  HIS   A HB3  1 
ATOM   1840 H  HD2  . HIS   A 1 86  ? 29.734 4.504   10.997  1.00 15.37 ?  86  HIS   A HD2  1 
ATOM   1841 H  HE1  . HIS   A 1 86  ? 32.731 7.055   11.386  1.00 17.16 ?  86  HIS   A HE1  1 
ATOM   1842 H  HE2  . HIS   A 1 86  ? 31.795 5.354   10.041  1.00 16.43 ?  86  HIS   A HE2  1 
ATOM   1843 N  N    . ASN   A 1 87  ? 27.409 5.517   15.845  1.00 14.58 ?  87  ASN   A N    1 
ATOM   1844 C  CA   . ASN   A 1 87  ? 26.417 5.500   16.903  1.00 15.98 ?  87  ASN   A CA   1 
ATOM   1845 C  C    . ASN   A 1 87  ? 25.303 4.495   16.656  1.00 16.79 ?  87  ASN   A C    1 
ATOM   1846 O  O    . ASN   A 1 87  ? 24.374 4.423   17.466  1.00 19.35 ?  87  ASN   A O    1 
ATOM   1847 C  CB   . ASN   A 1 87  ? 25.812 6.903   17.067  1.00 16.80 ?  87  ASN   A CB   1 
ATOM   1848 C  CG   . ASN   A 1 87  ? 25.298 7.485   15.753  1.00 17.40 ?  87  ASN   A CG   1 
ATOM   1849 O  OD1  . ASN   A 1 87  ? 25.940 7.376   14.714  1.00 17.73 ?  87  ASN   A OD1  1 
ATOM   1850 N  ND2  . ASN   A 1 87  ? 24.134 8.113   15.805  1.00 17.99 ?  87  ASN   A ND2  1 
ATOM   1851 H  H    . ASN   A 1 87  ? 27.266 6.136   15.263  1.00 17.50 ?  87  ASN   A H    1 
ATOM   1852 H  HA   . ASN   A 1 87  ? 26.850 5.261   17.741  1.00 19.19 ?  87  ASN   A HA   1 
ATOM   1853 H  HB2  . ASN   A 1 87  ? 25.067 6.852   17.690  1.00 20.16 ?  87  ASN   A HB2  1 
ATOM   1854 H  HB3  . ASN   A 1 87  ? 26.491 7.499   17.413  1.00 20.16 ?  87  ASN   A HB3  1 
ATOM   1855 H  HD21 . ASN   A 1 87  ? 23.803 8.457   15.092  1.00 21.59 ?  87  ASN   A HD21 1 
ATOM   1856 H  HD22 . ASN   A 1 87  ? 23.715 8.183   16.554  1.00 21.59 ?  87  ASN   A HD22 1 
ATOM   1857 N  N    . LEU   A 1 88  ? 25.373 3.718   15.577  1.00 15.72 ?  88  LEU   A N    1 
ATOM   1858 C  CA   . LEU   A 1 88  ? 24.269 2.853   15.183  1.00 15.63 ?  88  LEU   A CA   1 
ATOM   1859 C  C    . LEU   A 1 88  ? 24.489 1.380   15.497  1.00 15.14 ?  88  LEU   A C    1 
ATOM   1860 O  O    . LEU   A 1 88  ? 23.512 0.647   15.667  1.00 16.42 ?  88  LEU   A O    1 
ATOM   1861 C  CB   . LEU   A 1 88  ? 24.016 3.001   13.683  1.00 16.21 ?  88  LEU   A CB   1 
ATOM   1862 C  CG   . LEU   A 1 88  ? 23.708 4.421   13.202  1.00 17.45 ?  88  LEU   A CG   1 
ATOM   1863 C  CD1  . LEU   A 1 88  ? 23.509 4.427   11.699  1.00 17.76 ?  88  LEU   A CD1  1 
ATOM   1864 C  CD2  . LEU   A 1 88  ? 22.484 5.001   13.919  1.00 19.01 ?  88  LEU   A CD2  1 
ATOM   1865 H  H    . LEU   A 1 88  ? 26.058 3.674   15.056  1.00 18.87 ?  88  LEU   A H    1 
ATOM   1866 H  HA   . LEU   A 1 88  ? 23.470 3.138   15.651  1.00 18.76 ?  88  LEU   A HA   1 
ATOM   1867 H  HB2  . LEU   A 1 88  ? 24.800 2.700   13.205  1.00 19.45 ?  88  LEU   A HB2  1 
ATOM   1868 H  HB3  . LEU   A 1 88  ? 23.256 2.448   13.445  1.00 19.45 ?  88  LEU   A HB3  1 
ATOM   1869 H  HG   . LEU   A 1 88  ? 24.466 4.991   13.401  1.00 20.95 ?  88  LEU   A HG   1 
ATOM   1870 H  HD11 . LEU   A 1 88  ? 23.405 5.344   11.397  1.00 21.32 ?  88  LEU   A HD11 1 
ATOM   1871 H  HD12 . LEU   A 1 88  ? 24.281 4.024   11.275  1.00 21.32 ?  88  LEU   A HD12 1 
ATOM   1872 H  HD13 . LEU   A 1 88  ? 22.710 3.918   11.485  1.00 21.32 ?  88  LEU   A HD13 1 
ATOM   1873 H  HD21 . LEU   A 1 88  ? 22.247 5.845   13.504  1.00 22.82 ?  88  LEU   A HD21 1 
ATOM   1874 H  HD22 . LEU   A 1 88  ? 21.750 4.375   13.847  1.00 22.82 ?  88  LEU   A HD22 1 
ATOM   1875 H  HD23 . LEU   A 1 88  ? 22.708 5.145   14.853  1.00 22.82 ?  88  LEU   A HD23 1 
ATOM   1876 N  N    . ALA   A 1 89  ? 25.738 0.934   15.567  1.00 14.33 ?  89  ALA   A N    1 
ATOM   1877 C  CA   . ALA   A 1 89  ? 26.090 -0.477  15.655  1.00 14.13 ?  89  ALA   A CA   1 
ATOM   1878 C  C    . ALA   A 1 89  ? 27.574 -0.529  15.980  1.00 14.43 ?  89  ALA   A C    1 
ATOM   1879 O  O    . ALA   A 1 89  ? 28.278 0.472   15.863  1.00 15.40 ?  89  ALA   A O    1 
ATOM   1880 C  CB   . ALA   A 1 89  ? 25.830 -1.179  14.323  1.00 13.37 ?  89  ALA   A CB   1 
ATOM   1881 H  H    . ALA   A 1 89  ? 26.423 1.451   15.561  1.00 17.20 ?  89  ALA   A H    1 
ATOM   1882 H  HA   . ALA   A 1 89  ? 25.586 -0.913  16.361  1.00 16.96 ?  89  ALA   A HA   1 
ATOM   1883 H  HB1  . ALA   A 1 89  ? 26.084 -2.113  14.401  1.00 16.05 ?  89  ALA   A HB1  1 
ATOM   1884 H  HB2  . ALA   A 1 89  ? 24.883 -1.114  14.108  1.00 16.05 ?  89  ALA   A HB2  1 
ATOM   1885 H  HB3  . ALA   A 1 89  ? 26.354 -0.751  13.629  1.00 16.05 ?  89  ALA   A HB3  1 
ATOM   1886 N  N    . LYS   A 1 90  ? 28.062 -1.705  16.365  1.00 14.88 ?  90  LYS   A N    1 
ATOM   1887 C  CA   . LYS   A 1 90  ? 29.507 -1.841  16.519  1.00 15.36 ?  90  LYS   A CA   1 
ATOM   1888 C  C    . LYS   A 1 90  ? 30.209 -1.653  15.177  1.00 14.29 ?  90  LYS   A C    1 
ATOM   1889 O  O    . LYS   A 1 90  ? 31.143 -0.843  15.051  1.00 15.90 ?  90  LYS   A O    1 
ATOM   1890 C  CB   . LYS   A 1 90  ? 29.859 -3.189  17.145  1.00 17.74 ?  90  LYS   A CB   1 
ATOM   1891 C  CG   . LYS   A 1 90  ? 31.347 -3.343  17.422  1.00 22.22 ?  90  LYS   A CG   1 
ATOM   1892 C  CD   . LYS   A 1 90  ? 31.609 -4.550  18.308  1.00 27.57 ?  90  LYS   A CD   1 
ATOM   1893 C  CE   . LYS   A 1 90  ? 33.027 -4.556  18.864  1.00 31.84 ?  90  LYS   A CE   1 
ATOM   1894 N  NZ   . LYS   A 1 90  ? 34.035 -5.014  17.869  1.00 34.85 ?  90  LYS   A NZ   1 
ATOM   1895 H  H    . LYS   A 1 90  ? 27.598 -2.408  16.535  1.00 17.86 ?  90  LYS   A H    1 
ATOM   1896 H  HA   . LYS   A 1 90  ? 29.823 -1.145  17.110  1.00 18.44 ?  90  LYS   A HA   1 
ATOM   1897 H  HB2  . LYS   A 1 90  ? 29.386 -3.274  17.991  1.00 21.29 ?  90  LYS   A HB2  1 
ATOM   1898 H  HB3  . LYS   A 1 90  ? 29.589 -3.900  16.545  1.00 21.29 ?  90  LYS   A HB3  1 
ATOM   1899 H  HG2  . LYS   A 1 90  ? 31.820 -3.470  16.584  1.00 26.67 ?  90  LYS   A HG2  1 
ATOM   1900 H  HG3  . LYS   A 1 90  ? 31.675 -2.552  17.878  1.00 26.67 ?  90  LYS   A HG3  1 
ATOM   1901 H  HD2  . LYS   A 1 90  ? 30.992 -4.538  19.057  1.00 33.09 ?  90  LYS   A HD2  1 
ATOM   1902 H  HD3  . LYS   A 1 90  ? 31.486 -5.361  17.789  1.00 33.09 ?  90  LYS   A HD3  1 
ATOM   1903 H  HE2  . LYS   A 1 90  ? 33.263 -3.656  19.137  1.00 38.21 ?  90  LYS   A HE2  1 
ATOM   1904 H  HE3  . LYS   A 1 90  ? 33.065 -5.154  19.627  1.00 38.21 ?  90  LYS   A HE3  1 
ATOM   1905 H  HZ1  . LYS   A 1 90  ? 34.843 -5.034  18.243  1.00 41.83 ?  90  LYS   A HZ1  1 
ATOM   1906 H  HZ2  . LYS   A 1 90  ? 33.829 -5.831  17.582  1.00 41.83 ?  90  LYS   A HZ2  1 
ATOM   1907 H  HZ3  . LYS   A 1 90  ? 34.051 -4.458  17.176  1.00 41.83 ?  90  LYS   A HZ3  1 
ATOM   1908 N  N    . HIS   A 1 91  ? 29.743 -2.371  14.156  1.00 12.65 ?  91  HIS   A N    1 
ATOM   1909 C  CA   . HIS   A 1 91  ? 30.312 -2.358  12.823  1.00 12.41 ?  91  HIS   A CA   1 
ATOM   1910 C  C    . HIS   A 1 91  ? 29.223 -2.088  11.801  1.00 11.33 ?  91  HIS   A C    1 
ATOM   1911 O  O    . HIS   A 1 91  ? 28.052 -2.449  11.996  1.00 12.20 ?  91  HIS   A O    1 
ATOM   1912 C  CB   . HIS   A 1 91  ? 30.918 -3.726  12.454  1.00 15.12 ?  91  HIS   A CB   1 
ATOM   1913 C  CG   . HIS   A 1 91  ? 31.903 -4.247  13.452  1.00 18.60 ?  91  HIS   A CG   1 
ATOM   1914 N  ND1  . HIS   A 1 91  ? 33.184 -3.751  13.566  1.00 20.56 ?  91  HIS   A ND1  1 
ATOM   1915 C  CD2  . HIS   A 1 91  ? 31.801 -5.235  14.372  1.00 20.67 ?  91  HIS   A CD2  1 
ATOM   1916 C  CE1  . HIS   A 1 91  ? 33.826 -4.405  14.518  1.00 21.67 ?  91  HIS   A CE1  1 
ATOM   1917 N  NE2  . HIS   A 1 91  ? 33.007 -5.311  15.025  1.00 21.95 ?  91  HIS   A NE2  1 
ATOM   1918 H  H    . HIS   A 1 91  ? 29.062 -2.909  14.223  1.00 15.19 ?  91  HIS   A H    1 
ATOM   1919 H  HA   . HIS   A 1 91  ? 30.995 -1.683  12.753  1.00 14.90 ?  91  HIS   A HA   1 
ATOM   1920 H  HB2  . HIS   A 1 91  ? 30.203 -4.381  12.382  1.00 18.15 ?  91  HIS   A HB2  1 
ATOM   1921 H  HB3  . HIS   A 1 91  ? 31.374 -3.649  11.601  1.00 18.15 ?  91  HIS   A HB3  1 
ATOM   1922 H  HD1  . HIS   A 1 91  ? 33.514 -3.114  13.087  1.00 24.68 ?  91  HIS   A HD1  1 
ATOM   1923 H  HD2  . HIS   A 1 91  ? 31.058 -5.763  14.537  1.00 24.81 ?  91  HIS   A HD2  1 
ATOM   1924 H  HE1  . HIS   A 1 91  ? 34.706 -4.249  14.783  1.00 26.00 ?  91  HIS   A HE1  1 
ATOM   1925 N  N    . CYS   A 1 92  ? 29.624 -1.493  10.683  1.00 11.25 ?  92  CYS   A N    1 
ATOM   1926 C  CA   . CYS   A 1 92  ? 28.785 -1.423  9.495   1.00 11.01 ?  92  CYS   A CA   1 
ATOM   1927 C  C    . CYS   A 1 92  ? 29.436 -2.246  8.391   1.00 10.74 ?  92  CYS   A C    1 
ATOM   1928 O  O    . CYS   A 1 92  ? 30.595 -1.996  8.026   1.00 11.46 ?  92  CYS   A O    1 
ATOM   1929 C  CB   . CYS   A 1 92  ? 28.569 0.019   9.027   1.00 11.59 ?  92  CYS   A CB   1 
ATOM   1930 S  SG   . CYS   A 1 92  ? 27.558 0.118   7.523   1.00 11.00 ?  92  CYS   A SG   1 
ATOM   1931 H  H    . CYS   A 1 92  ? 30.386 -1.104  10.591  1.00 13.51 ?  92  CYS   A H    1 
ATOM   1932 H  HA   . CYS   A 1 92  ? 27.914 -1.802  9.694   1.00 13.22 ?  92  CYS   A HA   1 
ATOM   1933 H  HB2  . CYS   A 1 92  ? 28.116 0.521   9.727   1.00 13.91 ?  92  CYS   A HB2  1 
ATOM   1934 H  HB3  . CYS   A 1 92  ? 29.427 0.425   8.833   1.00 13.91 ?  92  CYS   A HB3  1 
ATOM   1935 H  HG   . CYS   A 1 92  ? 27.414 1.269   7.229   1.00 13.20 ?  92  CYS   A HG   1 
ATOM   1936 N  N    . LEU   A 1 93  ? 28.699 -3.237  7.886   1.00 10.61 ?  93  LEU   A N    1 
ATOM   1937 C  CA   . LEU   A 1 93  ? 29.101 -3.996  6.704   1.00 10.33 ?  93  LEU   A CA   1 
ATOM   1938 C  C    . LEU   A 1 93  ? 28.503 -3.301  5.486   1.00 9.92  ?  93  LEU   A C    1 
ATOM   1939 O  O    . LEU   A 1 93  ? 27.288 -3.373  5.254   1.00 10.13 ?  93  LEU   A O    1 
ATOM   1940 C  CB   . LEU   A 1 93  ? 28.634 -5.447  6.810   1.00 10.79 ?  93  LEU   A CB   1 
ATOM   1941 C  CG   . LEU   A 1 93  ? 29.023 -6.341  5.637   1.00 11.03 ?  93  LEU   A CG   1 
ATOM   1942 C  CD1  . LEU   A 1 93  ? 30.528 -6.580  5.631   1.00 12.13 ?  93  LEU   A CD1  1 
ATOM   1943 C  CD2  . LEU   A 1 93  ? 28.269 -7.665  5.684   1.00 12.31 ?  93  LEU   A CD2  1 
ATOM   1944 H  H    . LEU   A 1 93  ? 27.948 -3.491  8.226   1.00 12.73 ?  93  LEU   A H    1 
ATOM   1945 H  HA   . LEU   A 1 93  ? 30.064 -3.981  6.633   1.00 12.40 ?  93  LEU   A HA   1 
ATOM   1946 H  HB2  . LEU   A 1 93  ? 29.016 -5.833  7.618   1.00 12.95 ?  93  LEU   A HB2  1 
ATOM   1947 H  HB3  . LEU   A 1 93  ? 27.666 -5.455  6.879   1.00 12.95 ?  93  LEU   A HB3  1 
ATOM   1948 H  HG   . LEU   A 1 93  ? 28.795 -5.896  4.812   1.00 13.25 ?  93  LEU   A HG   1 
ATOM   1949 H  HD11 . LEU   A 1 93  ? 30.753 -7.196  4.918   1.00 14.56 ?  93  LEU   A HD11 1 
ATOM   1950 H  HD12 . LEU   A 1 93  ? 30.988 -5.735  5.497   1.00 14.56 ?  93  LEU   A HD12 1 
ATOM   1951 H  HD13 . LEU   A 1 93  ? 30.795 -6.962  6.489   1.00 14.56 ?  93  LEU   A HD13 1 
ATOM   1952 H  HD21 . LEU   A 1 93  ? 28.549 -8.211  4.929   1.00 14.77 ?  93  LEU   A HD21 1 
ATOM   1953 H  HD22 . LEU   A 1 93  ? 28.482 -8.122  6.514   1.00 14.77 ?  93  LEU   A HD22 1 
ATOM   1954 H  HD23 . LEU   A 1 93  ? 27.321 -7.490  5.633   1.00 14.77 ?  93  LEU   A HD23 1 
ATOM   1955 N  N    . HIS   A 1 94  ? 29.351 -2.605  4.730   1.00 9.96  ?  94  HIS   A N    1 
ATOM   1956 C  CA   . HIS   A 1 94  ? 28.922 -1.939  3.506   1.00 9.59  ?  94  HIS   A CA   1 
ATOM   1957 C  C    . HIS   A 1 94  ? 28.932 -2.970  2.392   1.00 9.91  ?  94  HIS   A C    1 
ATOM   1958 O  O    . HIS   A 1 94  ? 30.005 -3.478  2.043   1.00 11.30 ?  94  HIS   A O    1 
ATOM   1959 C  CB   . HIS   A 1 94  ? 29.871 -0.785  3.168   1.00 10.12 ?  94  HIS   A CB   1 
ATOM   1960 C  CG   . HIS   A 1 94  ? 29.861 0.307   4.179   1.00 9.82  ?  94  HIS   A CG   1 
ATOM   1961 N  ND1  . HIS   A 1 94  ? 28.977 1.366   4.124   1.00 10.45 ?  94  HIS   A ND1  1 
ATOM   1962 C  CD2  . HIS   A 1 94  ? 30.607 0.483   5.293   1.00 10.55 ?  94  HIS   A CD2  1 
ATOM   1963 C  CE1  . HIS   A 1 94  ? 29.196 2.154   5.162   1.00 10.59 ?  94  HIS   A CE1  1 
ATOM   1964 N  NE2  . HIS   A 1 94  ? 30.176 1.640   5.887   1.00 10.36 ?  94  HIS   A NE2  1 
ATOM   1965 H  H    . HIS   A 1 94  ? 30.187 -2.499  4.911   1.00 11.96 ?  94  HIS   A H    1 
ATOM   1966 H  HA   . HIS   A 1 94  ? 28.017 -1.594  3.616   1.00 11.51 ?  94  HIS   A HA   1 
ATOM   1967 H  HB2  . HIS   A 1 94  ? 30.768 -1.129  3.110   1.00 12.15 ?  94  HIS   A HB2  1 
ATOM   1968 H  HB3  . HIS   A 1 94  ? 29.599 -0.403  2.319   1.00 12.15 ?  94  HIS   A HB3  1 
ATOM   1969 H  HD2  . HIS   A 1 94  ? 31.288 -0.068  5.596   1.00 12.67 ?  94  HIS   A HD2  1 
ATOM   1970 H  HE1  . HIS   A 1 94  ? 28.732 2.938   5.355   1.00 12.71 ?  94  HIS   A HE1  1 
ATOM   1971 H  HE2  . HIS   A 1 94  ? 30.500 1.989   6.608   1.00 12.43 ?  94  HIS   A HE2  1 
ATOM   1972 N  N    . VAL   A 1 95  ? 27.762 -3.283  1.836   1.00 9.60  ?  95  VAL   A N    1 
ATOM   1973 C  CA   . VAL   A 1 95  ? 27.624 -4.323  0.820   1.00 9.31  ?  95  VAL   A CA   1 
ATOM   1974 C  C    . VAL   A 1 95  ? 27.073 -3.694  -0.446  1.00 9.59  ?  95  VAL   A C    1 
ATOM   1975 O  O    . VAL   A 1 95  ? 26.064 -2.979  -0.393  1.00 10.34 ?  95  VAL   A O    1 
ATOM   1976 C  CB   . VAL   A 1 95  ? 26.700 -5.469  1.280   1.00 10.24 ?  95  VAL   A CB   1 
ATOM   1977 C  CG1  . VAL   A 1 95  ? 26.600 -6.524  0.186   1.00 11.15 ?  95  VAL   A CG1  1 
ATOM   1978 C  CG2  . VAL   A 1 95  ? 27.200 -6.072  2.578   1.00 10.66 ?  95  VAL   A CG2  1 
ATOM   1979 H  H    . VAL   A 1 95  ? 27.018 -2.901  2.039   1.00 11.53 ?  95  VAL   A H    1 
ATOM   1980 H  HA   . VAL   A 1 95  ? 28.497 -4.697  0.623   1.00 11.17 ?  95  VAL   A HA   1 
ATOM   1981 H  HB   . VAL   A 1 95  ? 25.815 -5.118  1.436   1.00 12.30 ?  95  VAL   A HB   1 
ATOM   1982 H  HG11 . VAL   A 1 95  ? 26.204 -7.334  0.556   1.00 13.39 ?  95  VAL   A HG11 1 
ATOM   1983 H  HG12 . VAL   A 1 95  ? 26.042 -6.192  -0.535  1.00 13.39 ?  95  VAL   A HG12 1 
ATOM   1984 H  HG13 . VAL   A 1 95  ? 27.489 -6.727  -0.152  1.00 13.39 ?  95  VAL   A HG13 1 
ATOM   1985 H  HG21 . VAL   A 1 95  ? 26.637 -6.830  2.806   1.00 12.80 ?  95  VAL   A HG21 1 
ATOM   1986 H  HG22 . VAL   A 1 95  ? 28.115 -6.356  2.465   1.00 12.80 ?  95  VAL   A HG22 1 
ATOM   1987 H  HG23 . VAL   A 1 95  ? 27.140 -5.398  3.275   1.00 12.80 ?  95  VAL   A HG23 1 
ATOM   1988 N  N    . VAL   A 1 96  ? 27.700 -3.984  -1.583  1.00 9.41  ?  96  VAL   A N    1 
ATOM   1989 C  CA   . VAL   A 1 96  ? 27.291 -3.432  -2.867  1.00 10.46 ?  96  VAL   A CA   1 
ATOM   1990 C  C    . VAL   A 1 96  ? 26.485 -4.487  -3.619  1.00 10.77 ?  96  VAL   A C    1 
ATOM   1991 O  O    . VAL   A 1 96  ? 27.046 -5.427  -4.192  1.00 11.35 ?  96  VAL   A O    1 
ATOM   1992 C  CB   . VAL   A 1 96  ? 28.487 -2.961  -3.693  1.00 10.61 ?  96  VAL   A CB   1 
ATOM   1993 C  CG1  . VAL   A 1 96  ? 27.988 -2.332  -4.979  1.00 11.01 ?  96  VAL   A CG1  1 
ATOM   1994 C  CG2  . VAL   A 1 96  ? 29.348 -1.982  -2.905  1.00 11.31 ?  96  VAL   A CG2  1 
ATOM   1995 H  H    . VAL   A 1 96  ? 28.390 -4.502  -1.634  1.00 11.30 ?  96  VAL   A H    1 
ATOM   1996 H  HA   . VAL   A 1 96  ? 26.714 -2.666  -2.710  1.00 12.55 ?  96  VAL   A HA   1 
ATOM   1997 H  HB   . VAL   A 1 96  ? 29.030 -3.725  -3.928  1.00 12.74 ?  96  VAL   A HB   1 
ATOM   1998 H  HG11 . VAL   A 1 96  ? 28.727 -1.875  -5.411  1.00 13.21 ?  96  VAL   A HG11 1 
ATOM   1999 H  HG12 . VAL   A 1 96  ? 27.642 -3.023  -5.563  1.00 13.21 ?  96  VAL   A HG12 1 
ATOM   2000 H  HG13 . VAL   A 1 96  ? 27.287 -1.692  -4.770  1.00 13.21 ?  96  VAL   A HG13 1 
ATOM   2001 H  HG21 . VAL   A 1 96  ? 30.050 -1.643  -3.477  1.00 13.58 ?  96  VAL   A HG21 1 
ATOM   2002 H  HG22 . VAL   A 1 96  ? 28.789 -1.247  -2.596  1.00 13.58 ?  96  VAL   A HG22 1 
ATOM   2003 H  HG23 . VAL   A 1 96  ? 29.731 -2.443  -2.142  1.00 13.58 ?  96  VAL   A HG23 1 
ATOM   2004 N  N    . GLY   A 1 97  ? 25.165 -4.332  -3.644  1.00 10.41 ?  97  GLY   A N    1 
ATOM   2005 C  CA   . GLY   A 1 97  ? 24.344 -5.098  -4.550  1.00 10.89 ?  97  GLY   A CA   1 
ATOM   2006 C  C    . GLY   A 1 97  ? 24.353 -4.453  -5.923  1.00 11.48 ?  97  GLY   A C    1 
ATOM   2007 O  O    . GLY   A 1 97  ? 24.646 -3.259  -6.072  1.00 12.19 ?  97  GLY   A O    1 
ATOM   2008 H  H    . GLY   A 1 97  ? 24.719 -3.787  -3.137  1.00 12.50 ?  97  GLY   A H    1 
ATOM   2009 H  HA2  . GLY   A 1 97  ? 24.695 -6.001  -4.601  1.00 13.08 ?  97  GLY   A HA2  1 
ATOM   2010 H  HA3  . GLY   A 1 97  ? 23.430 -5.135  -4.222  1.00 13.08 ?  97  GLY   A HA3  1 
ATOM   2011 N  N    A PRO   A 1 98  ? 23.997 -5.200  -6.961  0.66 11.56 ?  98  PRO   A N    1 
ATOM   2012 N  N    B PRO   A 1 98  ? 24.081 -5.256  -6.953  0.34 11.77 ?  98  PRO   A N    1 
ATOM   2013 C  CA   A PRO   A 1 98  ? 23.872 -4.580  -8.286  0.66 12.52 ?  98  PRO   A CA   1 
ATOM   2014 C  CA   B PRO   A 1 98  ? 24.061 -4.729  -8.320  0.34 12.56 ?  98  PRO   A CA   1 
ATOM   2015 C  C    A PRO   A 1 98  ? 22.762 -3.533  -8.305  0.66 12.20 ?  98  PRO   A C    1 
ATOM   2016 C  C    B PRO   A 1 98  ? 22.933 -3.731  -8.509  0.34 12.89 ?  98  PRO   A C    1 
ATOM   2017 O  O    A PRO   A 1 98  ? 21.697 -3.714  -7.711  0.66 12.45 ?  98  PRO   A O    1 
ATOM   2018 O  O    B PRO   A 1 98  ? 21.840 -3.879  -7.958  0.34 13.48 ?  98  PRO   A O    1 
ATOM   2019 C  CB   A PRO   A 1 98  ? 23.545 -5.767  -9.200  0.66 12.61 ?  98  PRO   A CB   1 
ATOM   2020 C  CB   B PRO   A 1 98  ? 23.837 -5.981  -9.178  0.34 12.28 ?  98  PRO   A CB   1 
ATOM   2021 C  CG   A PRO   A 1 98  ? 22.902 -6.777  -8.291  0.66 12.50 ?  98  PRO   A CG   1 
ATOM   2022 C  CG   B PRO   A 1 98  ? 23.162 -6.951  -8.259  0.34 12.44 ?  98  PRO   A CG   1 
ATOM   2023 C  CD   A PRO   A 1 98  ? 23.627 -6.627  -6.972  0.66 11.79 ?  98  PRO   A CD   1 
ATOM   2024 C  CD   B PRO   A 1 98  ? 23.789 -6.700  -6.916  0.34 11.81 ?  98  PRO   A CD   1 
ATOM   2025 H  HA   A PRO   A 1 98  ? 24.714 -4.179  -8.552  0.66 15.02 ?  98  PRO   A HA   1 
ATOM   2026 H  HA   B PRO   A 1 98  ? 24.914 -4.320  -8.545  0.34 15.08 ?  98  PRO   A HA   1 
ATOM   2027 H  HB2  A PRO   A 1 98  ? 22.928 -5.483  -9.890  0.66 15.14 ?  98  PRO   A HB2  1 
ATOM   2028 H  HB2  B PRO   A 1 98  ? 23.267 -5.761  -9.931  0.34 14.74 ?  98  PRO   A HB2  1 
ATOM   2029 H  HB3  A PRO   A 1 98  ? 24.362 -6.119  -9.586  0.66 15.14 ?  98  PRO   A HB3  1 
ATOM   2030 H  HB3  B PRO   A 1 98  ? 24.690 -6.330  -9.481  0.34 14.74 ?  98  PRO   A HB3  1 
ATOM   2031 H  HG2  A PRO   A 1 98  ? 21.961 -6.576  -8.191  0.66 15.01 ?  98  PRO   A HG2  1 
ATOM   2032 H  HG2  B PRO   A 1 98  ? 22.208 -6.767  -8.234  0.34 14.93 ?  98  PRO   A HG2  1 
ATOM   2033 H  HG3  A PRO   A 1 98  ? 23.030 -7.668  -8.653  0.66 15.01 ?  98  PRO   A HG3  1 
ATOM   2034 H  HG3  B PRO   A 1 98  ? 23.329 -7.857  -8.558  0.34 14.93 ?  98  PRO   A HG3  1 
ATOM   2035 H  HD2  A PRO   A 1 98  ? 23.027 -6.832  -6.231  0.66 14.15 ?  98  PRO   A HD2  1 
ATOM   2036 H  HD2  B PRO   A 1 98  ? 23.159 -6.904  -6.204  0.34 14.18 ?  98  PRO   A HD2  1 
ATOM   2037 H  HD3  A PRO   A 1 98  ? 24.418 -7.191  -6.948  0.66 14.15 ?  98  PRO   A HD3  1 
ATOM   2038 H  HD3  B PRO   A 1 98  ? 24.607 -7.217  -6.821  0.34 14.18 ?  98  PRO   A HD3  1 
ATOM   2039 N  N    A ASN   A 1 99  ? 23.030 -2.419  -8.988  0.66 12.93 ?  99  ASN   A N    1 
ATOM   2040 N  N    B ASN   A 1 99  ? 23.210 -2.708  -9.301  0.34 12.74 ?  99  ASN   A N    1 
ATOM   2041 C  CA   A ASN   A 1 99  ? 22.052 -1.352  -9.187  0.66 13.64 ?  99  ASN   A CA   1 
ATOM   2042 C  CA   B ASN   A 1 99  ? 22.243 -1.663  -9.602  0.34 13.27 ?  99  ASN   A CA   1 
ATOM   2043 C  C    A ASN   A 1 99  ? 21.484 -1.504  -10.593 0.66 14.86 ?  99  ASN   A C    1 
ATOM   2044 C  C    B ASN   A 1 99  ? 21.635 -1.970  -10.966 0.34 14.14 ?  99  ASN   A C    1 
ATOM   2045 O  O    A ASN   A 1 99  ? 22.174 -1.236  -11.583 0.66 16.15 ?  99  ASN   A O    1 
ATOM   2046 O  O    B ASN   A 1 99  ? 22.313 -1.874  -11.995 0.34 13.55 ?  99  ASN   A O    1 
ATOM   2047 C  CB   A ASN   A 1 99  ? 22.700 0.020   -8.998  0.66 13.52 ?  99  ASN   A CB   1 
ATOM   2048 C  CB   B ASN   A 1 99  ? 22.927 -0.302  -9.592  0.34 14.21 ?  99  ASN   A CB   1 
ATOM   2049 C  CG   A ASN   A 1 99  ? 21.684 1.165   -8.990  0.66 13.86 ?  99  ASN   A CG   1 
ATOM   2050 C  CG   B ASN   A 1 99  ? 21.962 0.828   -9.814  0.34 14.80 ?  99  ASN   A CG   1 
ATOM   2051 O  OD1  A ASN   A 1 99  ? 20.686 1.129   -9.708  0.66 14.44 ?  99  ASN   A OD1  1 
ATOM   2052 O  OD1  B ASN   A 1 99  ? 21.053 0.718   -10.628 0.34 14.13 ?  99  ASN   A OD1  1 
ATOM   2053 N  ND2  A ASN   A 1 99  ? 21.956 2.197   -8.195  0.66 14.09 ?  99  ASN   A ND2  1 
ATOM   2054 N  ND2  B ASN   A 1 99  ? 22.140 1.919   -9.079  0.34 15.88 ?  99  ASN   A ND2  1 
ATOM   2055 H  H    A ASN   A 1 99  ? 23.794 -2.255  -9.342  0.66 15.52 ?  99  ASN   A H    1 
ATOM   2056 H  H    B ASN   A 1 99  ? 23.974 -2.593  -9.675  0.34 15.29 ?  99  ASN   A H    1 
ATOM   2057 H  HA   A ASN   A 1 99  ? 21.329 -1.449  -8.542  0.66 16.37 ?  99  ASN   A HA   1 
ATOM   2058 H  HA   B ASN   A 1 99  ? 21.538 -1.668  -8.931  0.34 15.93 ?  99  ASN   A HA   1 
ATOM   2059 H  HB2  A ASN   A 1 99  ? 23.175 0.032   -8.158  0.66 16.23 ?  99  ASN   A HB2  1 
ATOM   2060 H  HB2  B ASN   A 1 99  ? 23.359 -0.168  -8.735  0.34 17.06 ?  99  ASN   A HB2  1 
ATOM   2061 H  HB3  A ASN   A 1 99  ? 23.317 0.172   -9.734  0.66 16.23 ?  99  ASN   A HB3  1 
ATOM   2062 H  HB3  B ASN   A 1 99  ? 23.582 -0.283  -10.303 0.34 17.06 ?  99  ASN   A HB3  1 
ATOM   2063 H  HD21 A ASN   A 1 99  ? 21.419 2.866   -8.156  0.66 16.92 ?  99  ASN   A HD21 1 
ATOM   2064 H  HD21 B ASN   A 1 99  ? 21.612 2.587   -9.168  0.34 19.06 ?  99  ASN   A HD21 1 
ATOM   2065 H  HD22 A ASN   A 1 99  ? 22.671 2.188   -7.718  0.66 16.92 ?  99  ASN   A HD22 1 
ATOM   2066 H  HD22 B ASN   A 1 99  ? 22.785 1.954   -8.509  0.34 19.06 ?  99  ASN   A HD22 1 
ATOM   2067 N  N    A VAL   A 1 100 ? 20.226 -1.954  -10.671 0.66 16.01 ?  100 VAL   A N    1 
ATOM   2068 N  N    B VAL   A 1 100 ? 20.350 -2.334  -10.966 0.34 15.94 ?  100 VAL   A N    1 
ATOM   2069 C  CA   A VAL   A 1 100 ? 19.583 -2.197  -11.960 0.66 17.61 ?  100 VAL   A CA   1 
ATOM   2070 C  CA   B VAL   A 1 100 ? 19.683 -2.734  -12.201 0.34 18.13 ?  100 VAL   A CA   1 
ATOM   2071 C  C    A VAL   A 1 100 ? 19.485 -0.910  -12.763 0.66 17.94 ?  100 VAL   A C    1 
ATOM   2072 C  C    B VAL   A 1 100 ? 19.604 -1.570  -13.172 0.34 18.87 ?  100 VAL   A C    1 
ATOM   2073 O  O    A VAL   A 1 100 ? 19.544 -0.931  -13.998 0.66 18.89 ?  100 VAL   A O    1 
ATOM   2074 O  O    B VAL   A 1 100 ? 19.654 -1.763  -14.393 0.34 19.18 ?  100 VAL   A O    1 
ATOM   2075 C  CB   A VAL   A 1 100 ? 18.209 -2.876  -11.758 0.66 19.64 ?  100 VAL   A CB   1 
ATOM   2076 C  CB   B VAL   A 1 100 ? 18.287 -3.308  -11.891 0.34 19.39 ?  100 VAL   A CB   1 
ATOM   2077 C  CG1  A VAL   A 1 100 ? 17.457 -2.998  -13.079 0.66 20.36 ?  100 VAL   A CG1  1 
ATOM   2078 C  CG1  B VAL   A 1 100 ? 17.587 -3.718  -13.177 0.34 19.60 ?  100 VAL   A CG1  1 
ATOM   2079 C  CG2  A VAL   A 1 100 ? 18.391 -4.252  -11.133 0.66 20.08 ?  100 VAL   A CG2  1 
ATOM   2080 C  CG2  B VAL   A 1 100 ? 18.404 -4.480  -10.939 0.34 19.92 ?  100 VAL   A CG2  1 
ATOM   2081 H  H    A VAL   A 1 100 ? 19.724 -2.134  -9.988  0.66 19.22 ?  100 VAL   A H    1 
ATOM   2082 H  H    B VAL   A 1 100 ? 19.847 -2.350  -10.265 0.34 19.13 ?  100 VAL   A H    1 
ATOM   2083 H  HA   A VAL   A 1 100 ? 20.132 -2.816  -12.465 0.66 21.14 ?  100 VAL   A HA   1 
ATOM   2084 H  HA   B VAL   A 1 100 ? 20.203 -3.436  -12.619 0.34 21.77 ?  100 VAL   A HA   1 
ATOM   2085 H  HB   A VAL   A 1 100 ? 17.671 -2.344  -11.154 0.66 23.57 ?  100 VAL   A HB   1 
ATOM   2086 H  HB   B VAL   A 1 100 ? 17.753 -2.619  -11.462 0.34 23.27 ?  100 VAL   A HB   1 
ATOM   2087 H  HG11 A VAL   A 1 100 ? 16.706 -3.604  -12.960 0.66 24.43 ?  100 VAL   A HG11 1 
ATOM   2088 H  HG11 B VAL   A 1 100 ? 16.797 -4.233  -12.953 0.34 23.53 ?  100 VAL   A HG11 1 
ATOM   2089 H  HG12 A VAL   A 1 100 ? 17.135 -2.124  -13.343 0.66 24.43 ?  100 VAL   A HG12 1 
ATOM   2090 H  HG12 B VAL   A 1 100 ? 17.332 -2.922  -13.671 0.34 23.53 ?  100 VAL   A HG12 1 
ATOM   2091 H  HG13 A VAL   A 1 100 ? 18.058 -3.351  -13.754 0.66 24.43 ?  100 VAL   A HG13 1 
ATOM   2092 H  HG13 B VAL   A 1 100 ? 18.193 -4.257  -13.709 0.34 23.53 ?  100 VAL   A HG13 1 
ATOM   2093 H  HG21 A VAL   A 1 100 ? 17.523 -4.677  -11.037 0.66 24.10 ?  100 VAL   A HG21 1 
ATOM   2094 H  HG21 B VAL   A 1 100 ? 17.532 -4.889  -10.840 0.34 23.90 ?  100 VAL   A HG21 1 
ATOM   2095 H  HG22 A VAL   A 1 100 ? 18.957 -4.791  -11.710 0.66 24.10 ?  100 VAL   A HG22 1 
ATOM   2096 H  HG22 B VAL   A 1 100 ? 19.033 -5.119  -11.308 0.34 23.90 ?  100 VAL   A HG22 1 
ATOM   2097 H  HG23 A VAL   A 1 100 ? 18.807 -4.153  -10.263 0.66 24.10 ?  100 VAL   A HG23 1 
ATOM   2098 H  HG23 B VAL   A 1 100 ? 18.721 -4.159  -10.081 0.34 23.90 ?  100 VAL   A HG23 1 
ATOM   2099 N  N    A ASN   A 1 101 ? 19.343 0.227   -12.089 0.66 18.39 ?  101 ASN   A N    1 
ATOM   2100 N  N    B ASN   A 1 101 ? 19.459 -0.348  -12.655 0.34 19.51 ?  101 ASN   A N    1 
ATOM   2101 C  CA   A ASN   A 1 101 ? 19.281 1.496   -12.805 0.66 19.79 ?  101 ASN   A CA   1 
ATOM   2102 C  CA   B ASN   A 1 101 ? 19.399 0.818   -13.529 0.34 20.30 ?  101 ASN   A CA   1 
ATOM   2103 C  C    A ASN   A 1 101 ? 20.634 1.929   -13.368 0.66 21.92 ?  101 ASN   A C    1 
ATOM   2104 C  C    B ASN   A 1 101 ? 20.744 1.106   -14.181 0.34 20.84 ?  101 ASN   A C    1 
ATOM   2105 O  O    A ASN   A 1 101 ? 20.698 2.957   -14.057 0.66 24.02 ?  101 ASN   A O    1 
ATOM   2106 O  O    B ASN   A 1 101 ? 20.789 1.721   -15.253 0.34 20.37 ?  101 ASN   A O    1 
ATOM   2107 C  CB   A ASN   A 1 101 ? 18.667 2.563   -11.902 0.66 18.92 ?  101 ASN   A CB   1 
ATOM   2108 C  CB   B ASN   A 1 101 ? 18.911 2.034   -12.745 0.34 20.68 ?  101 ASN   A CB   1 
ATOM   2109 C  CG   A ASN   A 1 101 ? 17.330 2.127   -11.324 0.66 18.11 ?  101 ASN   A CG   1 
ATOM   2110 C  CG   B ASN   A 1 101 ? 17.601 1.780   -12.032 0.34 21.32 ?  101 ASN   A CG   1 
ATOM   2111 O  OD1  A ASN   A 1 101 ? 16.451 1.637   -12.045 0.66 17.67 ?  101 ASN   A OD1  1 
ATOM   2112 O  OD1  B ASN   A 1 101 ? 16.805 0.940   -12.450 0.34 21.79 ?  101 ASN   A OD1  1 
ATOM   2113 N  ND2  A ASN   A 1 101 ? 17.168 2.304   -10.019 0.66 17.38 ?  101 ASN   A ND2  1 
ATOM   2114 N  ND2  B ASN   A 1 101 ? 17.370 2.507   -10.947 0.34 21.85 ?  101 ASN   A ND2  1 
ATOM   2115 H  H    A ASN   A 1 101 ? 19.271 0.289   -11.236 0.66 22.07 ?  101 ASN   A H    1 
ATOM   2116 H  H    B ASN   A 1 101 ? 19.380 -0.177  -11.815 0.34 23.42 ?  101 ASN   A H    1 
ATOM   2117 H  HA   A ASN   A 1 101 ? 18.687 1.386   -13.562 0.66 23.75 ?  101 ASN   A HA   1 
ATOM   2118 H  HA   B ASN   A 1 101 ? 18.766 0.646   -14.236 0.34 24.37 ?  101 ASN   A HA   1 
ATOM   2119 H  HB2  A ASN   A 1 101 ? 19.268 2.748   -11.168 0.66 22.71 ?  101 ASN   A HB2  1 
ATOM   2120 H  HB2  B ASN   A 1 101 ? 19.573 2.263   -12.079 0.34 24.82 ?  101 ASN   A HB2  1 
ATOM   2121 H  HB3  A ASN   A 1 101 ? 18.521 3.372   -12.424 0.66 22.71 ?  101 ASN   A HB3  1 
ATOM   2122 H  HB3  B ASN   A 1 101 ? 18.779 2.774   -13.358 0.34 24.82 ?  101 ASN   A HB3  1 
ATOM   2123 H  HD21 A ASN   A 1 101 ? 16.427 2.074   -9.641  0.66 20.87 ?  101 ASN   A HD21 1 
ATOM   2124 H  HD21 B ASN   A 1 101 ? 16.638 2.406   -10.508 0.34 26.22 ?  101 ASN   A HD21 1 
ATOM   2125 H  HD22 A ASN   A 1 101 ? 17.799 2.647   -9.547  0.66 20.87 ?  101 ASN   A HD22 1 
ATOM   2126 H  HD22 B ASN   A 1 101 ? 17.948 3.090   -10.691 0.34 26.22 ?  101 ASN   A HD22 1 
ATOM   2127 N  N    A LYS   A 1 102 ? 21.700 1.166   -13.108 0.66 23.38 ?  102 LYS   A N    1 
ATOM   2128 N  N    B LYS   A 1 102 ? 21.841 0.684   -13.553 0.34 22.47 ?  102 LYS   A N    1 
ATOM   2129 C  CA   A LYS   A 1 102 ? 22.983 1.337   -13.778 0.66 24.88 ?  102 LYS   A CA   1 
ATOM   2130 C  CA   B LYS   A 1 102 ? 23.173 0.796   -14.136 0.34 23.48 ?  102 LYS   A CA   1 
ATOM   2131 C  C    A LYS   A 1 102 ? 23.280 0.216   -14.765 0.66 25.35 ?  102 LYS   A C    1 
ATOM   2132 C  C    B LYS   A 1 102 ? 23.489 -0.355  -15.086 0.34 23.51 ?  102 LYS   A C    1 
ATOM   2133 O  O    A LYS   A 1 102 ? 24.354 0.219   -15.376 0.66 26.03 ?  102 LYS   A O    1 
ATOM   2134 O  O    B LYS   A 1 102 ? 24.631 -0.471  -15.544 0.34 23.68 ?  102 LYS   A O    1 
ATOM   2135 C  CB   A LYS   A 1 102 ? 24.121 1.418   -12.752 0.66 26.26 ?  102 LYS   A CB   1 
ATOM   2136 C  CB   B LYS   A 1 102 ? 24.237 0.833   -13.033 0.34 24.70 ?  102 LYS   A CB   1 
ATOM   2137 C  CG   A LYS   A 1 102 ? 23.981 2.538   -11.740 0.66 27.37 ?  102 LYS   A CG   1 
ATOM   2138 C  CG   B LYS   A 1 102 ? 24.336 2.145   -12.264 0.34 25.83 ?  102 LYS   A CG   1 
ATOM   2139 C  CD   A LYS   A 1 102 ? 25.147 2.540   -10.761 0.66 28.83 ?  102 LYS   A CD   1 
ATOM   2140 C  CD   B LYS   A 1 102 ? 25.287 2.003   -11.076 0.34 27.36 ?  102 LYS   A CD   1 
ATOM   2141 C  CE   A LYS   A 1 102 ? 25.027 3.668   -9.747  0.66 30.03 ?  102 LYS   A CE   1 
ATOM   2142 C  CE   B LYS   A 1 102 ? 25.633 3.344   -10.452 0.34 28.59 ?  102 LYS   A CE   1 
ATOM   2143 N  NZ   A LYS   A 1 102 ? 26.125 3.631   -8.736  0.66 30.70 ?  102 LYS   A NZ   1 
ATOM   2144 N  NZ   B LYS   A 1 102 ? 26.395 3.180   -9.178  0.34 29.19 ?  102 LYS   A NZ   1 
ATOM   2145 H  H    A LYS   A 1 102 ? 21.702 0.520   -12.537 0.66 28.06 ?  102 LYS   A H    1 
ATOM   2146 H  H    B LYS   A 1 102 ? 21.838 0.314   -12.776 0.34 26.97 ?  102 LYS   A H    1 
ATOM   2147 H  HA   A LYS   A 1 102 ? 22.973 2.167   -14.273 0.66 29.86 ?  102 LYS   A HA   1 
ATOM   2148 H  HA   B LYS   A 1 102 ? 23.228 1.635   -14.625 0.34 28.19 ?  102 LYS   A HA   1 
ATOM   2149 H  HB2  A LYS   A 1 102 ? 24.158 0.582   -12.261 0.66 31.52 ?  102 LYS   A HB2  1 
ATOM   2150 H  HB2  B LYS   A 1 102 ? 24.041 0.133   -12.393 0.34 29.65 ?  102 LYS   A HB2  1 
ATOM   2151 H  HB3  A LYS   A 1 102 ? 24.958 1.554   -13.225 0.66 31.52 ?  102 LYS   A HB3  1 
ATOM   2152 H  HB3  B LYS   A 1 102 ? 25.104 0.670   -13.436 0.34 29.65 ?  102 LYS   A HB3  1 
ATOM   2153 H  HG2  A LYS   A 1 102 ? 23.969 3.389   -12.205 0.66 32.85 ?  102 LYS   A HG2  1 
ATOM   2154 H  HG2  B LYS   A 1 102 ? 24.681 2.839   -12.849 0.34 31.00 ?  102 LYS   A HG2  1 
ATOM   2155 H  HG3  A LYS   A 1 102 ? 23.159 2.415   -11.239 0.66 32.85 ?  102 LYS   A HG3  1 
ATOM   2156 H  HG3  B LYS   A 1 102 ? 23.461 2.391   -11.927 0.34 31.00 ?  102 LYS   A HG3  1 
ATOM   2157 H  HD2  A LYS   A 1 102 ? 25.160 1.698   -10.279 0.66 34.60 ?  102 LYS   A HD2  1 
ATOM   2158 H  HD2  B LYS   A 1 102 ? 24.868 1.456   -10.393 0.34 32.84 ?  102 LYS   A HD2  1 
ATOM   2159 H  HD3  A LYS   A 1 102 ? 25.976 2.658   -11.252 0.66 34.60 ?  102 LYS   A HD3  1 
ATOM   2160 H  HD3  B LYS   A 1 102 ? 26.110 1.586   -11.376 0.34 32.84 ?  102 LYS   A HD3  1 
ATOM   2161 H  HE2  A LYS   A 1 102 ? 25.071 4.519   -10.213 0.66 36.05 ?  102 LYS   A HE2  1 
ATOM   2162 H  HE2  B LYS   A 1 102 ? 26.183 3.851   -11.070 0.34 34.32 ?  102 LYS   A HE2  1 
ATOM   2163 H  HE3  A LYS   A 1 102 ? 24.180 3.587   -9.281  0.66 36.05 ?  102 LYS   A HE3  1 
ATOM   2164 H  HE3  B LYS   A 1 102 ? 24.816 3.827   -10.256 0.34 34.32 ?  102 LYS   A HE3  1 
ATOM   2165 H  HZ1  A LYS   A 1 102 ? 26.028 4.301   -8.159  0.66 36.85 ?  102 LYS   A HZ1  1 
ATOM   2166 H  HZ1  B LYS   A 1 102 ? 26.586 3.977   -8.833  0.34 35.03 ?  102 LYS   A HZ1  1 
ATOM   2167 H  HZ2  A LYS   A 1 102 ? 26.102 2.860   -8.292  0.66 36.85 ?  102 LYS   A HZ2  1 
ATOM   2168 H  HZ2  B LYS   A 1 102 ? 25.909 2.719   -8.591  0.34 35.03 ?  102 LYS   A HZ2  1 
ATOM   2169 H  HZ3  A LYS   A 1 102 ? 26.913 3.709   -9.141  0.66 36.85 ?  102 LYS   A HZ3  1 
ATOM   2170 H  HZ3  B LYS   A 1 102 ? 27.154 2.741   -9.332  0.34 35.03 ?  102 LYS   A HZ3  1 
ATOM   2171 N  N    A GLY   A 1 103 ? 22.370 -0.741  -14.932 0.66 25.90 ?  103 GLY   A N    1 
ATOM   2172 N  N    B GLY   A 1 103 ? 22.515 -1.215  -15.377 0.34 23.43 ?  103 GLY   A N    1 
ATOM   2173 C  CA   A GLY   A 1 103 ? 22.590 -1.848  -15.844 0.66 26.00 ?  103 GLY   A CA   1 
ATOM   2174 C  CA   B GLY   A 1 103 ? 22.760 -2.353  -16.241 0.34 23.37 ?  103 GLY   A CA   1 
ATOM   2175 C  C    A GLY   A 1 103 ? 23.444 -2.971  -15.300 0.66 26.08 ?  103 GLY   A C    1 
ATOM   2176 C  C    B GLY   A 1 103 ? 23.570 -3.469  -15.617 0.34 22.63 ?  103 GLY   A C    1 
ATOM   2177 O  O    A GLY   A 1 103 ? 24.001 -3.744  -16.086 0.66 27.72 ?  103 GLY   A O    1 
ATOM   2178 O  O    B GLY   A 1 103 ? 24.074 -4.337  -16.336 0.34 23.10 ?  103 GLY   A O    1 
ATOM   2179 H  H    A GLY   A 1 103 ? 21.612 -0.766  -14.530 0.66 31.09 ?  103 GLY   A H    1 
ATOM   2180 H  H    B GLY   A 1 103 ? 21.707 -1.144  -15.093 0.34 28.12 ?  103 GLY   A H    1 
ATOM   2181 H  HA2  A GLY   A 1 103 ? 21.729 -2.215  -16.107 0.66 31.20 ?  103 GLY   A HA2  1 
ATOM   2182 H  HA2  B GLY   A 1 103 ? 21.913 -2.722  -16.531 0.34 28.05 ?  103 GLY   A HA2  1 
ATOM   2183 H  HA3  A GLY   A 1 103 ? 23.025 -1.512  -16.645 0.66 31.20 ?  103 GLY   A HA3  1 
ATOM   2184 H  HA3  B GLY   A 1 103 ? 23.234 -2.032  -17.023 0.34 28.05 ?  103 GLY   A HA3  1 
ATOM   2185 N  N    A GLU   A 1 104 ? 23.569 -3.091  -13.982 0.66 23.66 ?  104 GLU   A N    1 
ATOM   2186 N  N    B GLU   A 1 104 ? 23.694 -3.486  -14.296 0.34 21.02 ?  104 GLU   A N    1 
ATOM   2187 C  CA   A GLU   A 1 104 ? 24.452 -4.087  -13.390 0.66 22.45 ?  104 GLU   A CA   1 
ATOM   2188 C  CA   B GLU   A 1 104 ? 24.585 -4.428  -13.639 0.34 19.48 ?  104 GLU   A CA   1 
ATOM   2189 C  C    A GLU   A 1 104 ? 23.774 -5.452  -13.287 0.66 23.22 ?  104 GLU   A C    1 
ATOM   2190 C  C    B GLU   A 1 104 ? 23.917 -5.794  -13.485 0.34 18.73 ?  104 GLU   A C    1 
ATOM   2191 O  O    A GLU   A 1 104 ? 22.558 -5.561  -13.098 0.66 23.75 ?  104 GLU   A O    1 
ATOM   2192 O  O    B GLU   A 1 104 ? 22.690 -5.922  -13.454 0.34 18.61 ?  104 GLU   A O    1 
ATOM   2193 C  CB   A GLU   A 1 104 ? 24.959 -3.593  -12.032 0.66 20.71 ?  104 GLU   A CB   1 
ATOM   2194 C  CB   B GLU   A 1 104 ? 25.045 -3.870  -12.292 0.34 19.02 ?  104 GLU   A CB   1 
ATOM   2195 C  CG   A GLU   A 1 104 ? 25.921 -2.414  -12.198 0.66 19.99 ?  104 GLU   A CG   1 
ATOM   2196 C  CG   B GLU   A 1 104 ? 25.842 -2.578  -12.443 0.34 19.65 ?  104 GLU   A CG   1 
ATOM   2197 C  CD   A GLU   A 1 104 ? 26.233 -1.632  -10.932 0.66 19.24 ?  104 GLU   A CD   1 
ATOM   2198 C  CD   B GLU   A 1 104 ? 26.240 -1.937  -11.127 0.34 20.02 ?  104 GLU   A CD   1 
ATOM   2199 O  OE1  A GLU   A 1 104 ? 25.650 -1.897  -9.865  0.66 17.58 ?  104 GLU   A OE1  1 
ATOM   2200 O  OE1  B GLU   A 1 104 ? 25.781 -2.392  -10.060 0.34 20.43 ?  104 GLU   A OE1  1 
ATOM   2201 O  OE2  A GLU   A 1 104 ? 27.084 -0.717  -11.032 0.66 20.18 -1 104 GLU   A OE2  1 
ATOM   2202 O  OE2  B GLU   A 1 104 ? 27.021 -0.961  -11.169 0.34 20.29 -1 104 GLU   A OE2  1 
ATOM   2203 H  H    A GLU   A 1 104 ? 23.161 -2.595  -13.413 0.66 28.40 ?  104 GLU   A H    1 
ATOM   2204 H  H    B GLU   A 1 104 ? 23.264 -2.965  -13.767 0.34 25.24 ?  104 GLU   A H    1 
ATOM   2205 H  HA   A GLU   A 1 104 ? 25.223 -4.188  -13.968 0.66 26.95 ?  104 GLU   A HA   1 
ATOM   2206 H  HA   B GLU   A 1 104 ? 25.372 -4.541  -14.194 0.34 23.38 ?  104 GLU   A HA   1 
ATOM   2207 H  HB2  A GLU   A 1 104 ? 24.206 -3.304  -11.494 0.66 24.86 ?  104 GLU   A HB2  1 
ATOM   2208 H  HB2  B GLU   A 1 104 ? 24.267 -3.685  -11.745 0.34 22.83 ?  104 GLU   A HB2  1 
ATOM   2209 H  HB3  A GLU   A 1 104 ? 25.432 -4.315  -11.589 0.66 24.86 ?  104 GLU   A HB3  1 
ATOM   2210 H  HB3  B GLU   A 1 104 ? 25.612 -4.527  -11.861 0.34 22.83 ?  104 GLU   A HB3  1 
ATOM   2211 H  HG2  A GLU   A 1 104 ? 26.762 -2.747  -12.545 0.66 23.99 ?  104 GLU   A HG2  1 
ATOM   2212 H  HG2  B GLU   A 1 104 ? 26.657 -2.770  -12.931 0.34 23.59 ?  104 GLU   A HG2  1 
ATOM   2213 H  HG3  A GLU   A 1 104 ? 25.535 -1.786  -12.828 0.66 23.99 ?  104 GLU   A HG3  1 
ATOM   2214 H  HG3  B GLU   A 1 104 ? 25.306 -1.937  -12.937 0.34 23.59 ?  104 GLU   A HG3  1 
ATOM   2215 N  N    A ASP   A 1 105 ? 24.589 -6.500  -13.407 0.66 23.66 ?  105 ASP   A N    1 
ATOM   2216 N  N    B ASP   A 1 105 ? 24.757 -6.820  -13.377 0.34 18.84 ?  105 ASP   A N    1 
ATOM   2217 C  CA   A ASP   A 1 105 ? 24.097 -7.866  -13.548 0.66 24.57 ?  105 ASP   A CA   1 
ATOM   2218 C  CA   B ASP   A 1 105 ? 24.327 -8.215  -13.454 0.34 19.36 ?  105 ASP   A CA   1 
ATOM   2219 C  C    A ASP   A 1 105 ? 23.439 -8.339  -12.256 0.66 22.53 ?  105 ASP   A C    1 
ATOM   2220 C  C    B ASP   A 1 105 ? 23.564 -8.594  -12.189 0.34 18.72 ?  105 ASP   A C    1 
ATOM   2221 O  O    A ASP   A 1 105 ? 24.086 -8.398  -11.208 0.66 20.88 ?  105 ASP   A O    1 
ATOM   2222 O  O    B ASP   A 1 105 ? 24.141 -8.648  -11.100 0.34 17.53 ?  105 ASP   A O    1 
ATOM   2223 C  CB   A ASP   A 1 105 ? 25.270 -8.776  -13.903 0.66 27.37 ?  105 ASP   A CB   1 
ATOM   2224 C  CB   B ASP   A 1 105 ? 25.569 -9.088  -13.619 0.34 20.61 ?  105 ASP   A CB   1 
ATOM   2225 C  CG   A ASP   A 1 105 ? 24.852 -10.213 -14.105 0.66 30.01 ?  105 ASP   A CG   1 
ATOM   2226 C  CG   B ASP   A 1 105 ? 25.241 -10.535 -13.909 0.34 21.65 ?  105 ASP   A CG   1 
ATOM   2227 O  OD1  A ASP   A 1 105 ? 23.632 -10.471 -14.170 0.66 30.47 ?  105 ASP   A OD1  1 
ATOM   2228 O  OD1  B ASP   A 1 105 ? 24.043 -10.877 -13.971 0.34 21.46 ?  105 ASP   A OD1  1 
ATOM   2229 O  OD2  A ASP   A 1 105 ? 25.746 -11.083 -14.199 0.66 31.84 -1 105 ASP   A OD2  1 
ATOM   2230 O  OD2  B ASP   A 1 105 ? 26.194 -11.332 -14.069 0.34 22.39 -1 105 ASP   A OD2  1 
ATOM   2231 H  H    A ASP   A 1 105 ? 25.446 -6.440  -13.403 0.66 28.39 ?  105 ASP   A H    1 
ATOM   2232 H  H    B ASP   A 1 105 ? 25.601 -6.726  -13.250 0.34 22.62 ?  105 ASP   A H    1 
ATOM   2233 H  HA   A ASP   A 1 105 ? 23.443 -7.909  -14.261 0.66 29.50 ?  105 ASP   A HA   1 
ATOM   2234 H  HA   B ASP   A 1 105 ? 23.746 -8.337  -14.219 0.34 23.24 ?  105 ASP   A HA   1 
ATOM   2235 H  HB2  A ASP   A 1 105 ? 25.676 -8.462  -14.727 0.66 32.85 ?  105 ASP   A HB2  1 
ATOM   2236 H  HB2  B ASP   A 1 105 ? 26.107 -8.730  -14.343 0.34 24.74 ?  105 ASP   A HB2  1 
ATOM   2237 H  HB3  A ASP   A 1 105 ? 25.922 -8.750  -13.184 0.66 32.85 ?  105 ASP   A HB3  1 
ATOM   2238 H  HB3  B ASP   A 1 105 ? 26.072 -9.077  -12.794 0.34 24.74 ?  105 ASP   A HB3  1 
ATOM   2239 N  N    A ILE   A 1 106 ? 22.158 -8.709  -12.339 0.66 22.24 ?  106 ILE   A N    1 
ATOM   2240 N  N    B ILE   A 1 106 ? 22.264 -8.872  -12.329 0.34 19.77 ?  106 ILE   A N    1 
ATOM   2241 C  CA   A ILE   A 1 106 ? 21.413 -9.113  -11.152 0.66 21.49 ?  106 ILE   A CA   1 
ATOM   2242 C  CA   B ILE   A 1 106 ? 21.464 -9.266  -11.175 0.34 20.65 ?  106 ILE   A CA   1 
ATOM   2243 C  C    A ILE   A 1 106 ? 21.954 -10.403 -10.549 0.66 19.90 ?  106 ILE   A C    1 
ATOM   2244 C  C    B ILE   A 1 106 ? 21.991 -10.548 -10.549 0.34 20.75 ?  106 ILE   A C    1 
ATOM   2245 O  O    A ILE   A 1 106 ? 21.734 -10.663 -9.360  0.66 19.18 ?  106 ILE   A O    1 
ATOM   2246 O  O    B ILE   A 1 106 ? 21.766 -10.791 -9.358  0.34 20.58 ?  106 ILE   A O    1 
ATOM   2247 C  CB   A ILE   A 1 106 ? 19.906 -9.196  -11.474 0.66 23.57 ?  106 ILE   A CB   1 
ATOM   2248 C  CB   B ILE   A 1 106 ? 19.966 -9.372  -11.544 0.34 22.02 ?  106 ILE   A CB   1 
ATOM   2249 C  CG1  A ILE   A 1 106 ? 19.071 -9.268  -10.192 0.66 24.27 ?  106 ILE   A CG1  1 
ATOM   2250 C  CG1  B ILE   A 1 106 ? 19.095 -9.415  -10.285 0.34 22.49 ?  106 ILE   A CG1  1 
ATOM   2251 C  CG2  A ILE   A 1 106 ? 19.613 -10.392 -12.365 0.66 24.61 ?  106 ILE   A CG2  1 
ATOM   2252 C  CG2  B ILE   A 1 106 ? 19.705 -10.610 -12.373 0.34 22.56 ?  106 ILE   A CG2  1 
ATOM   2253 C  CD1  A ILE   A 1 106 ? 19.169 -8.029  -9.323  0.66 24.54 ?  106 ILE   A CD1  1 
ATOM   2254 C  CD1  B ILE   A 1 106 ? 19.175 -8.166  -9.433  0.34 22.66 ?  106 ILE   A CD1  1 
ATOM   2255 H  H    A ILE   A 1 106 ? 21.706 -8.731  -13.068 0.66 26.70 ?  106 ILE   A H    1 
ATOM   2256 H  H    B ILE   A 1 106 ? 21.831 -8.836  -13.069 0.34 23.73 ?  106 ILE   A H    1 
ATOM   2257 H  HA   A ILE   A 1 106 ? 21.529 -8.424  -10.484 0.66 25.79 ?  106 ILE   A HA   1 
ATOM   2258 H  HA   B ILE   A 1 106 ? 21.549 -8.577  -10.504 0.34 24.79 ?  106 ILE   A HA   1 
ATOM   2259 H  HB   A ILE   A 1 106 ? 19.657 -8.393  -11.955 0.66 28.29 ?  106 ILE   A HB   1 
ATOM   2260 H  HB   B ILE   A 1 106 ? 19.720 -8.591  -12.064 0.34 26.44 ?  106 ILE   A HB   1 
ATOM   2261 H  HG12 A ILE   A 1 106 ? 18.139 -9.381  -10.435 0.66 29.13 ?  106 ILE   A HG12 1 
ATOM   2262 H  HG12 B ILE   A 1 106 ? 18.169 -9.528  -10.550 0.34 27.00 ?  106 ILE   A HG12 1 
ATOM   2263 H  HG13 A ILE   A 1 106 ? 19.367 -10.024 -9.664  0.66 29.13 ?  106 ILE   A HG13 1 
ATOM   2264 H  HG13 B ILE   A 1 106 ? 19.373 -10.163 -9.736  0.34 27.00 ?  106 ILE   A HG13 1 
ATOM   2265 H  HG21 A ILE   A 1 106 ? 18.709 -10.314 -12.705 0.66 29.53 ?  106 ILE   A HG21 1 
ATOM   2266 H  HG21 B ILE   A 1 106 ? 18.834 -10.526 -12.791 0.34 27.08 ?  106 ILE   A HG21 1 
ATOM   2267 H  HG22 A ILE   A 1 106 ? 20.245 -10.396 -13.100 0.66 29.53 ?  106 ILE   A HG22 1 
ATOM   2268 H  HG22 B ILE   A 1 106 ? 20.394 -10.683 -13.048 0.34 27.08 ?  106 ILE   A HG22 1 
ATOM   2269 H  HG23 A ILE   A 1 106 ? 19.704 -11.204 -11.844 0.66 29.53 ?  106 ILE   A HG23 1 
ATOM   2270 H  HG23 B ILE   A 1 106 ? 19.721 -11.386 -11.792 0.34 27.08 ?  106 ILE   A HG23 1 
ATOM   2271 H  HD11 A ILE   A 1 106 ? 18.459 -8.049  -8.664  0.66 29.45 ?  106 ILE   A HD11 1 
ATOM   2272 H  HD11 B ILE   A 1 106 ? 18.431 -8.161  -8.812  0.34 27.20 ?  106 ILE   A HD11 1 
ATOM   2273 H  HD12 A ILE   A 1 106 ? 20.032 -8.021  -8.877  0.66 29.45 ?  106 ILE   A HD12 1 
ATOM   2274 H  HD12 B ILE   A 1 106 ? 20.013 -8.169  -8.943  0.34 27.20 ?  106 ILE   A HD12 1 
ATOM   2275 H  HD13 A ILE   A 1 106 ? 19.079 -7.241  -9.883  0.66 29.45 ?  106 ILE   A HD13 1 
ATOM   2276 H  HD13 B ILE   A 1 106 ? 19.130 -7.387  -10.009 0.34 27.20 ?  106 ILE   A HD13 1 
ATOM   2277 N  N    A GLN   A 1 107 ? 22.682 -11.207 -11.334 0.66 20.82 ?  107 GLN   A N    1 
ATOM   2278 N  N    B GLN   A 1 107 ? 22.702 -11.374 -11.323 0.34 21.53 ?  107 GLN   A N    1 
ATOM   2279 C  CA   A GLN   A 1 107 ? 23.285 -12.425 -10.800 0.66 23.22 ?  107 GLN   A CA   1 
ATOM   2280 C  CA   B GLN   A 1 107 ? 23.355 -12.545 -10.754 0.34 23.04 ?  107 GLN   A CA   1 
ATOM   2281 C  C    A GLN   A 1 107 ? 24.253 -12.113 -9.665  0.66 20.61 ?  107 GLN   A C    1 
ATOM   2282 C  C    B GLN   A 1 107 ? 24.364 -12.162 -9.679  0.34 20.50 ?  107 GLN   A C    1 
ATOM   2283 O  O    A GLN   A 1 107 ? 24.458 -12.943 -8.773  0.66 21.70 ?  107 GLN   A O    1 
ATOM   2284 O  O    B GLN   A 1 107 ? 24.722 -13.008 -8.851  0.34 21.40 ?  107 GLN   A O    1 
ATOM   2285 C  CB   A GLN   A 1 107 ? 23.990 -13.190 -11.927 0.66 28.24 ?  107 GLN   A CB   1 
ATOM   2286 C  CB   B GLN   A 1 107 ? 24.038 -13.359 -11.857 0.34 26.93 ?  107 GLN   A CB   1 
ATOM   2287 C  CG   A GLN   A 1 107 ? 23.117 -13.408 -13.162 0.66 33.63 ?  107 GLN   A CG   1 
ATOM   2288 C  CG   B GLN   A 1 107 ? 23.137 -13.680 -13.045 0.34 30.75 ?  107 GLN   A CG   1 
ATOM   2289 C  CD   A GLN   A 1 107 ? 21.835 -14.154 -12.848 0.66 38.14 ?  107 GLN   A CD   1 
ATOM   2290 C  CD   B GLN   A 1 107 ? 21.858 -14.383 -12.639 0.34 34.04 ?  107 GLN   A CD   1 
ATOM   2291 O  OE1  A GLN   A 1 107 ? 21.858 -15.213 -12.218 0.66 39.80 ?  107 GLN   A OE1  1 
ATOM   2292 O  OE1  B GLN   A 1 107 ? 21.863 -15.260 -11.774 0.34 35.18 ?  107 GLN   A OE1  1 
ATOM   2293 N  NE2  A GLN   A 1 107 ? 20.706 -13.602 -13.281 0.66 39.50 ?  107 GLN   A NE2  1 
ATOM   2294 N  NE2  B GLN   A 1 107 ? 20.749 -13.996 -13.261 0.34 35.13 ?  107 GLN   A NE2  1 
ATOM   2295 H  H    A GLN   A 1 107 ? 22.851 -11.060 -12.164 0.66 24.99 ?  107 GLN   A H    1 
ATOM   2296 H  H    B GLN   A 1 107 ? 22.817 -11.276 -12.170 0.34 25.84 ?  107 GLN   A H    1 
ATOM   2297 H  HA   A GLN   A 1 107 ? 22.592 -12.995 -10.448 0.66 27.87 ?  107 GLN   A HA   1 
ATOM   2298 H  HA   B GLN   A 1 107 ? 22.685 -13.111 -10.345 0.34 27.66 ?  107 GLN   A HA   1 
ATOM   2299 H  HB2  A GLN   A 1 107 ? 24.776 -12.696 -12.207 0.66 33.89 ?  107 GLN   A HB2  1 
ATOM   2300 H  HB2  B GLN   A 1 107 ? 24.798 -12.859 -12.193 0.34 32.33 ?  107 GLN   A HB2  1 
ATOM   2301 H  HB3  A GLN   A 1 107 ? 24.253 -14.066 -11.601 0.66 33.89 ?  107 GLN   A HB3  1 
ATOM   2302 H  HB3  B GLN   A 1 107 ? 24.341 -14.203 -11.484 0.34 32.33 ?  107 GLN   A HB3  1 
ATOM   2303 H  HG2  A GLN   A 1 107 ? 22.877 -12.548 -13.542 0.66 40.36 ?  107 GLN   A HG2  1 
ATOM   2304 H  HG2  B GLN   A 1 107 ? 22.895 -12.857 -13.496 0.34 36.91 ?  107 GLN   A HG2  1 
ATOM   2305 H  HG3  A GLN   A 1 107 ? 23.616 -13.925 -13.814 0.66 40.36 ?  107 GLN   A HG3  1 
ATOM   2306 H  HG3  B GLN   A 1 107 ? 23.616 -14.261 -13.657 0.34 36.91 ?  107 GLN   A HG3  1 
ATOM   2307 H  HE21 A GLN   A 1 107 ? 20.726 -12.861 -13.717 0.66 47.40 ?  107 GLN   A HE21 1 
ATOM   2308 H  HE21 B GLN   A 1 107 ? 20.783 -13.377 -13.859 0.34 42.16 ?  107 GLN   A HE21 1 
ATOM   2309 H  HE22 A GLN   A 1 107 ? 19.952 -13.989 -13.127 0.66 47.40 ?  107 GLN   A HE22 1 
ATOM   2310 H  HE22 B GLN   A 1 107 ? 19.996 -14.363 -13.067 0.34 42.16 ?  107 GLN   A HE22 1 
ATOM   2311 N  N    . LEU   A 1 108 ? 24.828 -10.909 -9.662  1.00 17.56 ?  108 LEU   A N    1 
ATOM   2312 C  CA   . LEU   A 1 108 ? 25.735 -10.479 -8.607  1.00 15.05 ?  108 LEU   A CA   1 
ATOM   2313 C  C    . LEU   A 1 108 ? 25.025 -10.290 -7.274  1.00 13.14 ?  108 LEU   A C    1 
ATOM   2314 O  O    . LEU   A 1 108 ? 25.698 -10.129 -6.253  1.00 13.60 ?  108 LEU   A O    1 
ATOM   2315 C  CB   . LEU   A 1 108 ? 26.455 -9.191  -9.018  1.00 14.80 ?  108 LEU   A CB   1 
ATOM   2316 C  CG   . LEU   A 1 108 ? 27.446 -9.378  -10.170 1.00 16.75 ?  108 LEU   A CG   1 
ATOM   2317 C  CD1  . LEU   A 1 108 ? 27.949 -8.048  -10.707 1.00 17.91 ?  108 LEU   A CD1  1 
ATOM   2318 C  CD2  . LEU   A 1 108 ? 28.627 -10.234 -9.732  1.00 18.61 ?  108 LEU   A CD2  1 
ATOM   2319 H  H    A LEU   A 1 108 ? 24.702 -10.319 -10.270 0.66 21.07 ?  108 LEU   A H    1 
ATOM   2320 H  H    B LEU   A 1 108 ? 24.642 -10.310 -10.245 0.34 21.07 ?  108 LEU   A H    1 
ATOM   2321 H  HA   . LEU   A 1 108 ? 26.407 -11.165 -8.480  1.00 18.06 ?  108 LEU   A HA   1 
ATOM   2322 H  HB2  . LEU   A 1 108 ? 25.797 -8.537  -9.299  1.00 17.76 ?  108 LEU   A HB2  1 
ATOM   2323 H  HB3  . LEU   A 1 108 ? 26.951 -8.853  -8.259  1.00 17.76 ?  108 LEU   A HB3  1 
ATOM   2324 H  HG   . LEU   A 1 108 ? 27.001 -9.838  -10.900 1.00 20.11 ?  108 LEU   A HG   1 
ATOM   2325 H  HD11 . LEU   A 1 108 ? 28.561 -8.212  -11.445 1.00 21.50 ?  108 LEU   A HD11 1 
ATOM   2326 H  HD12 . LEU   A 1 108 ? 27.195 -7.523  -11.017 1.00 21.50 ?  108 LEU   A HD12 1 
ATOM   2327 H  HD13 . LEU   A 1 108 ? 28.413 -7.575  -9.998  1.00 21.50 ?  108 LEU   A HD13 1 
ATOM   2328 H  HD21 . LEU   A 1 108 ? 29.319 -10.187 -10.408 1.00 22.34 ?  108 LEU   A HD21 1 
ATOM   2329 H  HD22 . LEU   A 1 108 ? 28.962 -9.892  -8.888  1.00 22.34 ?  108 LEU   A HD22 1 
ATOM   2330 H  HD23 . LEU   A 1 108 ? 28.328 -11.149 -9.624  1.00 22.34 ?  108 LEU   A HD23 1 
ATOM   2331 N  N    . LEU   A 1 109 ? 23.690 -10.341 -7.248  1.00 13.03 ?  109 LEU   A N    1 
ATOM   2332 C  CA   . LEU   A 1 109 ? 22.986 -10.213 -5.980  1.00 12.15 ?  109 LEU   A CA   1 
ATOM   2333 C  C    . LEU   A 1 109 ? 23.323 -11.366 -5.043  1.00 11.44 ?  109 LEU   A C    1 
ATOM   2334 O  O    . LEU   A 1 109 ? 23.461 -11.175 -3.830  1.00 11.87 ?  109 LEU   A O    1 
ATOM   2335 C  CB   . LEU   A 1 109 ? 21.484 -10.124 -6.239  1.00 13.15 ?  109 LEU   A CB   1 
ATOM   2336 C  CG   . LEU   A 1 109 ? 20.586 -9.865  -5.038  1.00 13.21 ?  109 LEU   A CG   1 
ATOM   2337 C  CD1  . LEU   A 1 109 ? 21.022 -8.606  -4.313  1.00 13.63 ?  109 LEU   A CD1  1 
ATOM   2338 C  CD2  . LEU   A 1 109 ? 19.139 -9.736  -5.489  1.00 14.05 ?  109 LEU   A CD2  1 
ATOM   2339 H  H    . LEU   A 1 109 ? 23.187 -10.459 -7.936  1.00 15.64 ?  109 LEU   A H    1 
ATOM   2340 H  HA   . LEU   A 1 109 ? 23.272 -9.391  -5.556  1.00 14.59 ?  109 LEU   A HA   1 
ATOM   2341 H  HB2  . LEU   A 1 109 ? 21.333 -9.396  -6.867  1.00 15.79 ?  109 LEU   A HB2  1 
ATOM   2342 H  HB3  . LEU   A 1 109 ? 21.195 -10.954 -6.639  1.00 15.79 ?  109 LEU   A HB3  1 
ATOM   2343 H  HG   . LEU   A 1 109 ? 20.642 -10.610 -4.423  1.00 15.85 ?  109 LEU   A HG   1 
ATOM   2344 H  HD11 . LEU   A 1 109 ? 20.343 -8.357  -3.668  1.00 16.36 ?  109 LEU   A HD11 1 
ATOM   2345 H  HD12 . LEU   A 1 109 ? 21.862 -8.778  -3.862  1.00 16.36 ?  109 LEU   A HD12 1 
ATOM   2346 H  HD13 . LEU   A 1 109 ? 21.135 -7.892  -4.963  1.00 16.36 ?  109 LEU   A HD13 1 
ATOM   2347 H  HD21 . LEU   A 1 109 ? 18.592 -9.460  -4.733  1.00 16.87 ?  109 LEU   A HD21 1 
ATOM   2348 H  HD22 . LEU   A 1 109 ? 19.080 -9.072  -6.194  1.00 16.87 ?  109 LEU   A HD22 1 
ATOM   2349 H  HD23 . LEU   A 1 109 ? 18.828 -10.595 -5.820  1.00 16.87 ?  109 LEU   A HD23 1 
ATOM   2350 N  N    . LYS   A 1 110 ? 23.466 -12.577 -5.583  1.00 11.41 ?  110 LYS   A N    1 
ATOM   2351 C  CA   . LYS   A 1 110 ? 23.850 -13.700 -4.731  1.00 11.57 ?  110 LYS   A CA   1 
ATOM   2352 C  C    . LYS   A 1 110 ? 25.233 -13.474 -4.123  1.00 10.90 ?  110 LYS   A C    1 
ATOM   2353 O  O    . LYS   A 1 110 ? 25.430 -13.681 -2.922  1.00 11.03 ?  110 LYS   A O    1 
ATOM   2354 C  CB   . LYS   A 1 110 ? 23.779 -15.021 -5.500  1.00 12.61 ?  110 LYS   A CB   1 
ATOM   2355 C  CG   . LYS   A 1 110 ? 23.964 -16.236 -4.590  1.00 12.63 ?  110 LYS   A CG   1 
ATOM   2356 C  CD   . LYS   A 1 110 ? 23.736 -17.553 -5.315  1.00 13.64 ?  110 LYS   A CD   1 
ATOM   2357 C  CE   . LYS   A 1 110 ? 23.847 -18.740 -4.382  1.00 14.26 ?  110 LYS   A CE   1 
ATOM   2358 N  NZ   . LYS   A 1 110 ? 22.671 -18.878 -3.488  1.00 14.47 ?  110 LYS   A NZ   1 
ATOM   2359 H  H    . LYS   A 1 110 ? 23.348 -12.773 -6.409  1.00 13.70 ?  110 LYS   A H    1 
ATOM   2360 H  HA   . LYS   A 1 110 ? 23.212 -13.760 -3.998  1.00 13.89 ?  110 LYS   A HA   1 
ATOM   2361 H  HB2  . LYS   A 1 110 ? 22.910 -15.096 -5.928  1.00 15.14 ?  110 LYS   A HB2  1 
ATOM   2362 H  HB3  . LYS   A 1 110 ? 24.481 -15.039 -6.166  1.00 15.14 ?  110 LYS   A HB3  1 
ATOM   2363 H  HG2  . LYS   A 1 110 ? 24.863 -16.239 -4.236  1.00 15.16 ?  110 LYS   A HG2  1 
ATOM   2364 H  HG3  . LYS   A 1 110 ? 23.320 -16.185 -3.860  1.00 15.16 ?  110 LYS   A HG3  1 
ATOM   2365 H  HD2  . LYS   A 1 110 ? 22.848 -17.554 -5.702  1.00 16.38 ?  110 LYS   A HD2  1 
ATOM   2366 H  HD3  . LYS   A 1 110 ? 24.406 -17.648 -6.008  1.00 16.38 ?  110 LYS   A HD3  1 
ATOM   2367 H  HE2  . LYS   A 1 110 ? 23.923 -19.551 -4.907  1.00 17.12 ?  110 LYS   A HE2  1 
ATOM   2368 H  HE3  . LYS   A 1 110 ? 24.635 -18.632 -3.822  1.00 17.12 ?  110 LYS   A HE3  1 
ATOM   2369 H  HZ1  . LYS   A 1 110 ? 22.766 -19.581 -2.957  1.00 17.37 ?  110 LYS   A HZ1  1 
ATOM   2370 H  HZ2  . LYS   A 1 110 ? 22.578 -18.145 -2.988  1.00 17.37 ?  110 LYS   A HZ2  1 
ATOM   2371 H  HZ3  . LYS   A 1 110 ? 21.929 -18.982 -3.976  1.00 17.37 ?  110 LYS   A HZ3  1 
ATOM   2372 N  N    . SER   A 1 111 ? 26.196 -13.031 -4.937  1.00 11.11 ?  111 SER   A N    1 
ATOM   2373 C  CA   . SER   A 1 111 ? 27.526 -12.734 -4.415  1.00 11.34 ?  111 SER   A CA   1 
ATOM   2374 C  C    . SER   A 1 111 ? 27.464 -11.686 -3.308  1.00 11.01 ?  111 SER   A C    1 
ATOM   2375 O  O    . SER   A 1 111 ? 28.170 -11.792 -2.299  1.00 11.56 ?  111 SER   A O    1 
ATOM   2376 C  CB   . SER   A 1 111 ? 28.420 -12.247 -5.554  1.00 12.38 ?  111 SER   A CB   1 
ATOM   2377 O  OG   . SER   A 1 111 ? 28.482 -13.215 -6.587  1.00 14.47 ?  111 SER   A OG   1 
ATOM   2378 H  H    . SER   A 1 111 ? 26.096 -12.901 -5.780  1.00 13.34 ?  111 SER   A H    1 
ATOM   2379 H  HA   . SER   A 1 111 ? 27.914 -13.546 -4.050  1.00 13.61 ?  111 SER   A HA   1 
ATOM   2380 H  HB2  . SER   A 1 111 ? 28.047 -11.430 -5.922  1.00 14.87 ?  111 SER   A HB2  1 
ATOM   2381 H  HB3  . SER   A 1 111 ? 29.310 -12.076 -5.206  1.00 14.87 ?  111 SER   A HB3  1 
ATOM   2382 H  HG   . SER   A 1 111 ? 29.001 -12.939 -7.203  1.00 17.37 ?  111 SER   A HG   1 
ATOM   2383 N  N    . ALA   A 1 112 ? 26.620 -10.666 -3.485  1.00 11.05 ?  112 ALA   A N    1 
ATOM   2384 C  CA   . ALA   A 1 112 ? 26.480 -9.630  -2.468  1.00 10.64 ?  112 ALA   A CA   1 
ATOM   2385 C  C    . ALA   A 1 112 ? 25.999 -10.226 -1.150  1.00 10.66 ?  112 ALA   A C    1 
ATOM   2386 O  O    . ALA   A 1 112 ? 26.545 -9.923  -0.082  1.00 11.18 ?  112 ALA   A O    1 
ATOM   2387 C  CB   . ALA   A 1 112 ? 25.527 -8.539  -2.959  1.00 11.10 ?  112 ALA   A CB   1 
ATOM   2388 H  H    . ALA   A 1 112 ? 26.131 -10.548 -4.179  1.00 13.27 ?  112 ALA   A H    1 
ATOM   2389 H  HA   . ALA   A 1 112 ? 27.346 -9.216  -2.310  1.00 12.78 ?  112 ALA   A HA   1 
ATOM   2390 H  HB1  . ALA   A 1 112 ? 25.466 -7.840  -2.280  1.00 13.33 ?  112 ALA   A HB1  1 
ATOM   2391 H  HB2  . ALA   A 1 112 ? 25.870 -8.161  -3.783  1.00 13.33 ?  112 ALA   A HB2  1 
ATOM   2392 H  HB3  . ALA   A 1 112 ? 24.651 -8.924  -3.109  1.00 13.33 ?  112 ALA   A HB3  1 
ATOM   2393 N  N    . TYR   A 1 113 ? 24.965 -11.079 -1.203  1.00 10.90 ?  113 TYR   A N    1 
ATOM   2394 C  CA   . TYR   A 1 113 ? 24.453 -11.678 0.022   1.00 10.41 ?  113 TYR   A CA   1 
ATOM   2395 C  C    . TYR   A 1 113 ? 25.459 -12.625 0.671   1.00 9.92  ?  113 TYR   A C    1 
ATOM   2396 O  O    . TYR   A 1 113 ? 25.424 -12.810 1.891   1.00 10.43 ?  113 TYR   A O    1 
ATOM   2397 C  CB   . TYR   A 1 113 ? 23.144 -12.420 -0.253  1.00 10.96 ?  113 TYR   A CB   1 
ATOM   2398 C  CG   . TYR   A 1 113 ? 21.920 -11.533 -0.163  1.00 10.99 ?  113 TYR   A CG   1 
ATOM   2399 C  CD1  . TYR   A 1 113 ? 21.562 -10.944 1.040   1.00 10.90 ?  113 TYR   A CD1  1 
ATOM   2400 C  CD2  . TYR   A 1 113 ? 21.114 -11.309 -1.268  1.00 11.17 ?  113 TYR   A CD2  1 
ATOM   2401 C  CE1  . TYR   A 1 113 ? 20.432 -10.154 1.141   1.00 11.23 ?  113 TYR   A CE1  1 
ATOM   2402 C  CE2  . TYR   A 1 113 ? 19.966 -10.506 -1.174  1.00 11.11 ?  113 TYR   A CE2  1 
ATOM   2403 C  CZ   . TYR   A 1 113 ? 19.638 -9.947  0.033   1.00 11.20 ?  113 TYR   A CZ   1 
ATOM   2404 O  OH   . TYR   A 1 113 ? 18.514 -9.151  0.153   1.00 11.96 ?  113 TYR   A OH   1 
ATOM   2405 H  H    . TYR   A 1 113 ? 24.564 -11.319 -1.923  1.00 13.08 ?  113 TYR   A H    1 
ATOM   2406 H  HA   . TYR   A 1 113 ? 24.270 -10.974 0.658   1.00 12.49 ?  113 TYR   A HA   1 
ATOM   2407 H  HB2  . TYR   A 1 113 ? 23.178 -12.787 -1.152  1.00 13.16 ?  113 TYR   A HB2  1 
ATOM   2408 H  HB3  . TYR   A 1 113 ? 23.048 -13.136 0.391   1.00 13.16 ?  113 TYR   A HB3  1 
ATOM   2409 H  HD1  . TYR   A 1 113 ? 22.092 -11.092 1.795   1.00 13.09 ?  113 TYR   A HD1  1 
ATOM   2410 H  HD2  . TYR   A 1 113 ? 21.329 -11.703 -2.080  1.00 13.41 ?  113 TYR   A HD2  1 
ATOM   2411 H  HE1  . TYR   A 1 113 ? 20.209 -9.766  1.961   1.00 13.48 ?  113 TYR   A HE1  1 
ATOM   2412 H  HE2  . TYR   A 1 113 ? 19.423 -10.362 -1.916  1.00 13.34 ?  113 TYR   A HE2  1 
ATOM   2413 H  HH   . TYR   A 1 113 ? 18.115 -9.103  -0.584  1.00 14.36 ?  113 TYR   A HH   1 
ATOM   2414 N  N    . GLU   A 1 114 ? 26.362 -13.233 -0.115  1.00 10.40 ?  114 GLU   A N    1 
ATOM   2415 C  CA   . GLU   A 1 114 ? 27.355 -14.133 0.477   1.00 10.68 ?  114 GLU   A CA   1 
ATOM   2416 C  C    . GLU   A 1 114 ? 28.206 -13.422 1.525   1.00 10.66 ?  114 GLU   A C    1 
ATOM   2417 O  O    . GLU   A 1 114 ? 28.682 -14.059 2.476   1.00 11.05 ?  114 GLU   A O    1 
ATOM   2418 C  CB   . GLU   A 1 114 ? 28.229 -14.770 -0.612  1.00 11.07 ?  114 GLU   A CB   1 
ATOM   2419 C  CG   . GLU   A 1 114 ? 27.466 -15.833 -1.391  1.00 11.11 ?  114 GLU   A CG   1 
ATOM   2420 C  CD   . GLU   A 1 114 ? 28.174 -16.344 -2.639  1.00 11.91 ?  114 GLU   A CD   1 
ATOM   2421 O  OE1  . GLU   A 1 114 ? 29.132 -15.713 -3.137  1.00 12.14 ?  114 GLU   A OE1  1 
ATOM   2422 O  OE2  . GLU   A 1 114 ? 27.736 -17.403 -3.141  1.00 12.84 -1 114 GLU   A OE2  1 
ATOM   2423 H  H    . GLU   A 1 114 ? 26.421 -13.134 -0.971  1.00 12.49 ?  114 GLU   A H    1 
ATOM   2424 H  HA   . GLU   A 1 114 ? 26.883 -14.850 0.921   1.00 12.82 ?  114 GLU   A HA   1 
ATOM   2425 H  HB2  . GLU   A 1 114 ? 28.515 -14.083 -1.239  1.00 13.29 ?  114 GLU   A HB2  1 
ATOM   2426 H  HB3  . GLU   A 1 114 ? 29.000 -15.188 -0.202  1.00 13.29 ?  114 GLU   A HB3  1 
ATOM   2427 H  HG2  . GLU   A 1 114 ? 27.322 -16.595 -0.813  1.00 13.34 ?  114 GLU   A HG2  1 
ATOM   2428 H  HG3  . GLU   A 1 114 ? 26.616 -15.464 -1.671  1.00 13.34 ?  114 GLU   A HG3  1 
ATOM   2429 N  N    . ASN   A 1 115 ? 28.388 -12.105 1.391   1.00 10.59 ?  115 ASN   A N    1 
ATOM   2430 C  CA   . ASN   A 1 115 ? 29.152 -11.373 2.396   1.00 11.19 ?  115 ASN   A CA   1 
ATOM   2431 C  C    . ASN   A 1 115 ? 28.535 -11.504 3.784   1.00 10.44 ?  115 ASN   A C    1 
ATOM   2432 O  O    . ASN   A 1 115 ? 29.248 -11.434 4.794   1.00 11.22 ?  115 ASN   A O    1 
ATOM   2433 C  CB   . ASN   A 1 115 ? 29.253 -9.892  2.015   1.00 11.12 ?  115 ASN   A CB   1 
ATOM   2434 C  CG   . ASN   A 1 115 ? 30.052 -9.676  0.757   1.00 11.84 ?  115 ASN   A CG   1 
ATOM   2435 O  OD1  . ASN   A 1 115 ? 31.270 -9.796  0.762   1.00 14.84 ?  115 ASN   A OD1  1 
ATOM   2436 N  ND2  . ASN   A 1 115 ? 29.373 -9.369  -0.333  1.00 11.28 ?  115 ASN   A ND2  1 
ATOM   2437 H  H    . ASN   A 1 115 ? 28.084 -11.623 0.747   1.00 12.71 ?  115 ASN   A H    1 
ATOM   2438 H  HA   . ASN   A 1 115 ? 30.047 -11.733 2.440   1.00 13.43 ?  115 ASN   A HA   1 
ATOM   2439 H  HB2  . ASN   A 1 115 ? 28.355 -9.541  1.884   1.00 13.35 ?  115 ASN   A HB2  1 
ATOM   2440 H  HB3  . ASN   A 1 115 ? 29.687 -9.413  2.742   1.00 13.35 ?  115 ASN   A HB3  1 
ATOM   2441 H  HD21 . ASN   A 1 115 ? 29.790 -9.238  -1.073  1.00 13.55 ?  115 ASN   A HD21 1 
ATOM   2442 H  HD22 . ASN   A 1 115 ? 28.516 -9.308  -0.305  1.00 13.55 ?  115 ASN   A HD22 1 
ATOM   2443 N  N    . PHE   A 1 116 ? 27.206 -11.673 3.863   1.00 10.56 ?  116 PHE   A N    1 
ATOM   2444 C  CA   . PHE   A 1 116 ? 26.563 -11.776 5.170   1.00 10.86 ?  116 PHE   A CA   1 
ATOM   2445 C  C    . PHE   A 1 116 ? 27.042 -13.006 5.935   1.00 10.86 ?  116 PHE   A C    1 
ATOM   2446 O  O    . PHE   A 1 116 ? 26.964 -13.031 7.164   1.00 11.40 ?  116 PHE   A O    1 
ATOM   2447 C  CB   . PHE   A 1 116 ? 25.033 -11.906 5.045   1.00 11.20 ?  116 PHE   A CB   1 
ATOM   2448 C  CG   . PHE   A 1 116 ? 24.275 -10.662 4.570   1.00 10.84 ?  116 PHE   A CG   1 
ATOM   2449 C  CD1  . PHE   A 1 116 ? 24.849 -9.638  3.820   1.00 11.28 ?  116 PHE   A CD1  1 
ATOM   2450 C  CD2  . PHE   A 1 116 ? 22.918 -10.562 4.886   1.00 11.49 ?  116 PHE   A CD2  1 
ATOM   2451 C  CE1  . PHE   A 1 116 ? 24.073 -8.554  3.393   1.00 11.42 ?  116 PHE   A CE1  1 
ATOM   2452 C  CE2  . PHE   A 1 116 ? 22.147 -9.489  4.473   1.00 11.17 ?  116 PHE   A CE2  1 
ATOM   2453 C  CZ   . PHE   A 1 116 ? 22.711 -8.491  3.723   1.00 11.04 ?  116 PHE   A CZ   1 
ATOM   2454 H  H    . PHE   A 1 116 ? 26.668 -11.725 3.190   1.00 12.68 ?  116 PHE   A H    1 
ATOM   2455 H  HA   . PHE   A 1 116 ? 26.757 -10.984 5.694   1.00 13.03 ?  116 PHE   A HA   1 
ATOM   2456 H  HB2  . PHE   A 1 116 ? 24.838 -12.620 4.416   1.00 13.45 ?  116 PHE   A HB2  1 
ATOM   2457 H  HB3  . PHE   A 1 116 ? 24.676 -12.149 5.918   1.00 13.45 ?  116 PHE   A HB3  1 
ATOM   2458 H  HD1  . PHE   A 1 116 ? 25.743 -9.693  3.588   1.00 13.54 ?  116 PHE   A HD1  1 
ATOM   2459 H  HD2  . PHE   A 1 116 ? 22.512 -11.246 5.385   1.00 13.79 ?  116 PHE   A HD2  1 
ATOM   2460 H  HE1  . PHE   A 1 116 ? 24.460 -7.876  2.892   1.00 13.71 ?  116 PHE   A HE1  1 
ATOM   2461 H  HE2  . PHE   A 1 116 ? 21.243 -9.456  4.701   1.00 13.41 ?  116 PHE   A HE2  1 
ATOM   2462 H  HZ   . PHE   A 1 116 ? 22.198 -7.763  3.455   1.00 13.26 ?  116 PHE   A HZ   1 
ATOM   2463 N  N    . ASN   A 1 117 ? 27.478 -14.053 5.230   1.00 10.97 ?  117 ASN   A N    1 
ATOM   2464 C  CA   . ASN   A 1 117 ? 27.853 -15.301 5.889   1.00 11.25 ?  117 ASN   A CA   1 
ATOM   2465 C  C    . ASN   A 1 117 ? 29.115 -15.180 6.721   1.00 11.65 ?  117 ASN   A C    1 
ATOM   2466 O  O    . ASN   A 1 117 ? 29.418 -16.097 7.494   1.00 12.86 ?  117 ASN   A O    1 
ATOM   2467 C  CB   . ASN   A 1 117 ? 27.975 -16.418 4.858   1.00 11.67 ?  117 ASN   A CB   1 
ATOM   2468 C  CG   . ASN   A 1 117 ? 26.626 -16.813 4.317   1.00 11.65 ?  117 ASN   A CG   1 
ATOM   2469 O  OD1  . ASN   A 1 117 ? 25.654 -16.841 5.067   1.00 12.55 ?  117 ASN   A OD1  1 
ATOM   2470 N  ND2  . ASN   A 1 117 ? 26.541 -17.076 3.026   1.00 11.62 ?  117 ASN   A ND2  1 
ATOM   2471 H  H    . ASN   A 1 117 ? 27.553 -14.059 4.373   1.00 13.17 ?  117 ASN   A H    1 
ATOM   2472 H  HA   . ASN   A 1 117 ? 27.135 -15.538 6.493   1.00 13.51 ?  117 ASN   A HA   1 
ATOM   2473 H  HB2  . ASN   A 1 117 ? 28.527 -16.113 4.119   1.00 14.01 ?  117 ASN   A HB2  1 
ATOM   2474 H  HB3  . ASN   A 1 117 ? 28.375 -17.192 5.280   1.00 14.01 ?  117 ASN   A HB3  1 
ATOM   2475 H  HD21 . ASN   A 1 117 ? 25.791 -17.298 2.680   1.00 13.95 ?  117 ASN   A HD21 1 
ATOM   2476 H  HD22 . ASN   A 1 117 ? 27.248 -17.026 2.533   1.00 13.95 ?  117 ASN   A HD22 1 
ATOM   2477 N  N    . GLN   A 1 118 ? 29.843 -14.073 6.597   1.00 11.82 ?  118 GLN   A N    1 
ATOM   2478 C  CA   . GLN   A 1 118 ? 31.020 -13.837 7.421   1.00 12.65 ?  118 GLN   A CA   1 
ATOM   2479 C  C    . GLN   A 1 118 ? 30.675 -13.265 8.790   1.00 12.36 ?  118 GLN   A C    1 
ATOM   2480 O  O    . GLN   A 1 118 ? 31.590 -12.982 9.574   1.00 13.87 ?  118 GLN   A O    1 
ATOM   2481 C  CB   . GLN   A 1 118 ? 32.007 -12.925 6.687   1.00 12.95 ?  118 GLN   A CB   1 
ATOM   2482 C  CG   . GLN   A 1 118 ? 32.481 -13.508 5.363   1.00 12.80 ?  118 GLN   A CG   1 
ATOM   2483 C  CD   . GLN   A 1 118 ? 33.319 -14.768 5.541   1.00 12.79 ?  118 GLN   A CD   1 
ATOM   2484 O  OE1  . GLN   A 1 118 ? 34.187 -14.827 6.417   1.00 13.66 ?  118 GLN   A OE1  1 
ATOM   2485 N  NE2  . GLN   A 1 118 ? 33.077 -15.768 4.694   1.00 13.37 ?  118 GLN   A NE2  1 
ATOM   2486 H  H    . GLN   A 1 118 ? 29.670 -13.424 6.047   1.00 14.19 ?  118 GLN   A H    1 
ATOM   2487 H  HA   . GLN   A 1 118 ? 31.460 -14.690 7.562   1.00 15.19 ?  118 GLN   A HA   1 
ATOM   2488 H  HB2  . GLN   A 1 118 ? 31.578 -12.074 6.510   1.00 15.55 ?  118 GLN   A HB2  1 
ATOM   2489 H  HB3  . GLN   A 1 118 ? 32.788 -12.790 7.251   1.00 15.55 ?  118 GLN   A HB3  1 
ATOM   2490 H  HG2  . GLN   A 1 118 ? 31.706 -13.731 4.819   1.00 15.37 ?  118 GLN   A HG2  1 
ATOM   2491 H  HG3  . GLN   A 1 118 ? 33.024 -12.848 4.902   1.00 15.37 ?  118 GLN   A HG3  1 
ATOM   2492 H  HE21 . GLN   A 1 118 ? 32.463 -15.686 4.091   1.00 16.05 ?  118 GLN   A HE21 1 
ATOM   2493 H  HE22 . GLN   A 1 118 ? 33.520 -16.499 4.752   1.00 16.05 ?  118 GLN   A HE22 1 
ATOM   2494 N  N    . HIS   A 1 119 ? 29.386 -13.108 9.102   1.00 11.76 ?  119 HIS   A N    1 
ATOM   2495 C  CA   . HIS   A 1 119 ? 28.942 -12.498 10.352  1.00 12.52 ?  119 HIS   A CA   1 
ATOM   2496 C  C    . HIS   A 1 119 ? 27.810 -13.321 10.936  1.00 12.63 ?  119 HIS   A C    1 
ATOM   2497 O  O    . HIS   A 1 119 ? 26.860 -13.655 10.225  1.00 13.46 ?  119 HIS   A O    1 
ATOM   2498 C  CB   . HIS   A 1 119 ? 28.479 -11.066 10.081  1.00 13.30 ?  119 HIS   A CB   1 
ATOM   2499 C  CG   . HIS   A 1 119 ? 29.549 -10.256 9.452   1.00 14.22 ?  119 HIS   A CG   1 
ATOM   2500 N  ND1  . HIS   A 1 119 ? 30.536 -9.651  10.193  1.00 16.44 ?  119 HIS   A ND1  1 
ATOM   2501 C  CD2  . HIS   A 1 119 ? 29.873 -10.066 8.153   1.00 15.45 ?  119 HIS   A CD2  1 
ATOM   2502 C  CE1  . HIS   A 1 119 ? 31.392 -9.067  9.375   1.00 16.87 ?  119 HIS   A CE1  1 
ATOM   2503 N  NE2  . HIS   A 1 119 ? 31.024 -9.318  8.132   1.00 16.96 ?  119 HIS   A NE2  1 
ATOM   2504 H  H    . HIS   A 1 119 ? 28.736 -13.370 8.597   1.00 14.11 ?  119 HIS   A H    1 
ATOM   2505 H  HA   . HIS   A 1 119 ? 29.676 -12.486 10.985  1.00 15.04 ?  119 HIS   A HA   1 
ATOM   2506 H  HB2  . HIS   A 1 119 ? 27.716 -11.094 9.482   1.00 15.97 ?  119 HIS   A HB2  1 
ATOM   2507 H  HB3  . HIS   A 1 119 ? 28.234 -10.657 10.922  1.00 15.97 ?  119 HIS   A HB3  1 
ATOM   2508 H  HD1  . HIS   A 1 119 ? 30.575 -9.640  11.051  1.00 19.74 ?  119 HIS   A HD1  1 
ATOM   2509 H  HD2  . HIS   A 1 119 ? 29.402 -10.378 7.412   1.00 18.55 ?  119 HIS   A HD2  1 
ATOM   2510 H  HE1  . HIS   A 1 119 ? 32.132 -8.569  9.633   1.00 20.26 ?  119 HIS   A HE1  1 
ATOM   2511 N  N    . GLU   A 1 120 ? 27.908 -13.631 12.232  1.00 13.62 ?  120 GLU   A N    1 
ATOM   2512 C  CA   . GLU   A 1 120 ? 26.966 -14.566 12.843  1.00 15.55 ?  120 GLU   A CA   1 
ATOM   2513 C  C    . GLU   A 1 120 ? 25.544 -14.012 12.884  1.00 14.17 ?  120 GLU   A C    1 
ATOM   2514 O  O    . GLU   A 1 120 ? 24.571 -14.776 12.761  1.00 14.42 ?  120 GLU   A O    1 
ATOM   2515 C  CB   . GLU   A 1 120 ? 27.435 -14.933 14.251  1.00 19.78 ?  120 GLU   A CB   1 
ATOM   2516 C  CG   . GLU   A 1 120 ? 28.621 -15.882 14.279  1.00 27.56 ?  120 GLU   A CG   1 
ATOM   2517 C  CD   . GLU   A 1 120 ? 28.732 -16.636 15.588  1.00 34.49 ?  120 GLU   A CD   1 
ATOM   2518 O  OE1  . GLU   A 1 120 ? 28.317 -16.086 16.632  1.00 35.72 ?  120 GLU   A OE1  1 
ATOM   2519 O  OE2  . GLU   A 1 120 ? 29.231 -17.782 15.574  1.00 37.97 -1 120 GLU   A OE2  1 
ATOM   2520 H  H    . GLU   A 1 120 ? 28.508 -13.322 12.770  1.00 16.35 ?  120 GLU   A H    1 
ATOM   2521 H  HA   . GLU   A 1 120 ? 26.952 -15.381 12.322  1.00 18.66 ?  120 GLU   A HA   1 
ATOM   2522 H  HB2  . GLU   A 1 120 ? 27.699 -14.127 14.721  1.00 23.75 ?  120 GLU   A HB2  1 
ATOM   2523 H  HB3  . GLU   A 1 120 ? 26.705 -15.364 14.726  1.00 23.75 ?  120 GLU   A HB3  1 
ATOM   2524 H  HG2  . GLU   A 1 120 ? 28.534 -16.524 13.556  1.00 33.08 ?  120 GLU   A HG2  1 
ATOM   2525 H  HG3  . GLU   A 1 120 ? 29.440 -15.377 14.181  1.00 33.08 ?  120 GLU   A HG3  1 
ATOM   2526 N  N    . VAL   A 1 121 ? 25.401 -12.703 13.103  1.00 13.53 ?  121 VAL   A N    1 
ATOM   2527 C  CA   . VAL   A 1 121 ? 24.103 -12.046 13.226  1.00 13.18 ?  121 VAL   A CA   1 
ATOM   2528 C  C    . VAL   A 1 121 ? 24.209 -10.660 12.601  1.00 12.50 ?  121 VAL   A C    1 
ATOM   2529 O  O    . VAL   A 1 121 ? 25.180 -9.937  12.845  1.00 13.53 ?  121 VAL   A O    1 
ATOM   2530 C  CB   . VAL   A 1 121 ? 23.666 -11.918 14.703  1.00 16.78 ?  121 VAL   A CB   1 
ATOM   2531 C  CG1  . VAL   A 1 121 ? 22.272 -11.307 14.794  1.00 17.57 ?  121 VAL   A CG1  1 
ATOM   2532 C  CG2  . VAL   A 1 121 ? 23.695 -13.254 15.426  1.00 19.43 ?  121 VAL   A CG2  1 
ATOM   2533 H  H    . VAL   A 1 121 ? 26.063 -12.160 13.188  1.00 16.24 ?  121 VAL   A H    1 
ATOM   2534 H  HA   . VAL   A 1 121 ? 23.433 -12.564 12.752  1.00 15.82 ?  121 VAL   A HA   1 
ATOM   2535 H  HB   . VAL   A 1 121 ? 24.276 -11.324 15.163  1.00 20.14 ?  121 VAL   A HB   1 
ATOM   2536 H  HG11 . VAL   A 1 121 ? 21.954 -11.373 15.710  1.00 21.09 ?  121 VAL   A HG11 1 
ATOM   2537 H  HG12 . VAL   A 1 121 ? 22.315 -10.375 14.529  1.00 21.09 ?  121 VAL   A HG12 1 
ATOM   2538 H  HG13 . VAL   A 1 121 ? 21.673 -11.793 14.204  1.00 21.09 ?  121 VAL   A HG13 1 
ATOM   2539 H  HG21 . VAL   A 1 121 ? 23.341 -13.138 16.328  1.00 23.33 ?  121 VAL   A HG21 1 
ATOM   2540 H  HG22 . VAL   A 1 121 ? 23.146 -13.893 14.943  1.00 23.33 ?  121 VAL   A HG22 1 
ATOM   2541 H  HG23 . VAL   A 1 121 ? 24.608 -13.572 15.474  1.00 23.33 ?  121 VAL   A HG23 1 
ATOM   2542 N  N    . LEU   A 1 122 ? 23.191 -10.269 11.828  1.00 11.81 ?  122 LEU   A N    1 
ATOM   2543 C  CA   . LEU   A 1 122 ? 23.195 -8.970  11.159  1.00 12.00 ?  122 LEU   A CA   1 
ATOM   2544 C  C    . LEU   A 1 122 ? 21.797 -8.382  11.111  1.00 11.86 ?  122 LEU   A C    1 
ATOM   2545 O  O    . LEU   A 1 122 ? 20.807 -9.104  10.967  1.00 12.88 ?  122 LEU   A O    1 
ATOM   2546 C  CB   . LEU   A 1 122 ? 23.615 -9.057  9.690   1.00 13.17 ?  122 LEU   A CB   1 
ATOM   2547 C  CG   . LEU   A 1 122 ? 24.821 -9.903  9.315   1.00 13.39 ?  122 LEU   A CG   1 
ATOM   2548 C  CD1  . LEU   A 1 122 ? 24.410 -11.352 9.084   1.00 14.11 ?  122 LEU   A CD1  1 
ATOM   2549 C  CD2  . LEU   A 1 122 ? 25.492 -9.327  8.083   1.00 12.72 ?  122 LEU   A CD2  1 
ATOM   2550 H  H    . LEU   A 1 122 ? 22.481 -10.745 11.677  1.00 14.18 ?  122 LEU   A H    1 
ATOM   2551 H  HA   . LEU   A 1 122 ? 23.782 -8.361  11.627  1.00 14.40 ?  122 LEU   A HA   1 
ATOM   2552 H  HB2  . LEU   A 1 122 ? 22.873 -9.409  9.184   1.00 15.81 ?  122 LEU   A HB2  1 
ATOM   2553 H  HB3  . LEU   A 1 122 ? 23.813 -8.159  9.386   1.00 15.81 ?  122 LEU   A HB3  1 
ATOM   2554 H  HG   . LEU   A 1 122 ? 25.474 -9.888  10.037  1.00 16.07 ?  122 LEU   A HG   1 
ATOM   2555 H  HD11 . LEU   A 1 122 ? 25.185 -11.866 8.808   1.00 16.94 ?  122 LEU   A HD11 1 
ATOM   2556 H  HD12 . LEU   A 1 122 ? 24.053 -11.714 9.910   1.00 16.94 ?  122 LEU   A HD12 1 
ATOM   2557 H  HD13 . LEU   A 1 122 ? 23.732 -11.380 8.391   1.00 16.94 ?  122 LEU   A HD13 1 
ATOM   2558 H  HD21 . LEU   A 1 122 ? 26.236 -9.898  7.820   1.00 15.27 ?  122 LEU   A HD21 1 
ATOM   2559 H  HD22 . LEU   A 1 122 ? 24.846 -9.279  7.361   1.00 15.27 ?  122 LEU   A HD22 1 
ATOM   2560 H  HD23 . LEU   A 1 122 ? 25.825 -8.436  8.287   1.00 15.27 ?  122 LEU   A HD23 1 
ATOM   2561 N  N    A LEU   A 1 123 ? 21.731 -7.055  11.222  0.66 11.57 ?  123 LEU   A N    1 
ATOM   2562 N  N    B LEU   A 1 123 ? 21.738 -7.054  11.226  0.34 11.73 ?  123 LEU   A N    1 
ATOM   2563 C  CA   A LEU   A 1 123 ? 20.561 -6.266  10.849  0.66 10.89 ?  123 LEU   A CA   1 
ATOM   2564 C  CA   B LEU   A 1 123 ? 20.561 -6.262  10.885  0.34 11.69 ?  123 LEU   A CA   1 
ATOM   2565 C  C    A LEU   A 1 123 ? 20.796 -5.749  9.436   0.66 10.28 ?  123 LEU   A C    1 
ATOM   2566 C  C    B LEU   A 1 123 ? 20.778 -5.713  9.482   0.34 11.19 ?  123 LEU   A C    1 
ATOM   2567 O  O    A LEU   A 1 123 ? 21.886 -5.243  9.148   0.66 10.79 ?  123 LEU   A O    1 
ATOM   2568 O  O    B LEU   A 1 123 ? 21.731 -4.959  9.259   0.34 10.93 ?  123 LEU   A O    1 
ATOM   2569 C  CB   A LEU   A 1 123 ? 20.419 -5.076  11.801  0.66 11.33 ?  123 LEU   A CB   1 
ATOM   2570 C  CB   B LEU   A 1 123 ? 20.400 -5.106  11.873  0.34 12.12 ?  123 LEU   A CB   1 
ATOM   2571 C  CG   A LEU   A 1 123 ? 19.369 -4.015  11.460  0.66 12.72 ?  123 LEU   A CG   1 
ATOM   2572 C  CG   B LEU   A 1 123 ? 19.391 -4.022  11.475  0.34 12.53 ?  123 LEU   A CG   1 
ATOM   2573 C  CD1  A LEU   A 1 123 ? 17.969 -4.616  11.474  0.66 13.72 ?  123 LEU   A CD1  1 
ATOM   2574 C  CD1  B LEU   A 1 123 ? 17.980 -4.595  11.418  0.34 12.73 ?  123 LEU   A CD1  1 
ATOM   2575 C  CD2  A LEU   A 1 123 ? 19.468 -2.840  12.433  0.66 13.10 ?  123 LEU   A CD2  1 
ATOM   2576 C  CD2  B LEU   A 1 123 ? 19.457 -2.829  12.425  0.34 12.75 ?  123 LEU   A CD2  1 
ATOM   2577 H  H    A LEU   A 1 123 ? 22.381 -6.573  11.521  0.66 13.89 ?  123 LEU   A H    1 
ATOM   2578 H  H    B LEU   A 1 123 ? 22.396 -6.571  11.509  0.34 14.08 ?  123 LEU   A H    1 
ATOM   2579 H  HA   A LEU   A 1 123 ? 19.757 -6.811  10.877  0.66 13.07 ?  123 LEU   A HA   1 
ATOM   2580 H  HA   B LEU   A 1 123 ? 19.765 -6.813  10.896  0.34 14.03 ?  123 LEU   A HA   1 
ATOM   2581 H  HB2  A LEU   A 1 123 ? 20.193 -5.419  12.680  0.66 13.60 ?  123 LEU   A HB2  1 
ATOM   2582 H  HB2  B LEU   A 1 123 ? 20.112 -5.472  12.724  0.34 14.55 ?  123 LEU   A HB2  1 
ATOM   2583 H  HB3  A LEU   A 1 123 ? 21.272 -4.623  11.845  0.66 13.60 ?  123 LEU   A HB3  1 
ATOM   2584 H  HB3  B LEU   A 1 123 ? 21.261 -4.674  11.982  0.34 14.55 ?  123 LEU   A HB3  1 
ATOM   2585 H  HG   A LEU   A 1 123 ? 19.534 -3.670  10.567  0.66 15.27 ?  123 LEU   A HG   1 
ATOM   2586 H  HG   B LEU   A 1 123 ? 19.607 -3.691  10.590  0.34 15.04 ?  123 LEU   A HG   1 
ATOM   2587 H  HD11 A LEU   A 1 123 ? 17.322 -3.920  11.287  0.66 16.48 ?  123 LEU   A HD11 1 
ATOM   2588 H  HD11 B LEU   A 1 123 ? 17.358 -3.884  11.205  0.34 15.28 ?  123 LEU   A HD11 1 
ATOM   2589 H  HD12 A LEU   A 1 123 ? 17.918 -5.308  10.797  0.66 16.48 ?  123 LEU   A HD12 1 
ATOM   2590 H  HD12 B LEU   A 1 123 ? 17.947 -5.282  10.733  0.34 15.28 ?  123 LEU   A HD12 1 
ATOM   2591 H  HD13 A LEU   A 1 123 ? 17.802 -4.998  12.351  0.66 16.48 ?  123 LEU   A HD13 1 
ATOM   2592 H  HD13 B LEU   A 1 123 ? 17.762 -4.980  12.282  0.34 15.28 ?  123 LEU   A HD13 1 
ATOM   2593 H  HD21 A LEU   A 1 123 ? 18.795 -2.179  12.203  0.66 15.72 ?  123 LEU   A HD21 1 
ATOM   2594 H  HD21 B LEU   A 1 123 ? 18.806 -2.166  12.144  0.34 15.31 ?  123 LEU   A HD21 1 
ATOM   2595 H  HD22 A LEU   A 1 123 ? 19.313 -3.167  13.335  0.66 15.72 ?  123 LEU   A HD22 1 
ATOM   2596 H  HD22 B LEU   A 1 123 ? 19.254 -3.131  13.324  0.34 15.31 ?  123 LEU   A HD22 1 
ATOM   2597 H  HD23 A LEU   A 1 123 ? 20.352 -2.452  12.369  0.66 15.72 ?  123 LEU   A HD23 1 
ATOM   2598 H  HD23 B LEU   A 1 123 ? 20.349 -2.451  12.395  0.34 15.31 ?  123 LEU   A HD23 1 
ATOM   2599 N  N    A ALA   A 1 124 ? 19.799 -5.855  8.556   0.66 9.51  ?  124 ALA   A N    1 
ATOM   2600 N  N    B ALA   A 1 124 ? 19.900 -6.067  8.544   0.34 11.14 ?  124 ALA   A N    1 
ATOM   2601 C  CA   A ALA   A 1 124 ? 20.074 -5.572  7.154   0.66 8.99  ?  124 ALA   A CA   1 
ATOM   2602 C  CA   B ALA   A 1 124 ? 20.193 -5.829  7.138   0.34 11.42 ?  124 ALA   A CA   1 
ATOM   2603 C  C    A ALA   A 1 124 ? 18.822 -5.105  6.425   0.66 9.17  ?  124 ALA   A C    1 
ATOM   2604 C  C    B ALA   A 1 124 ? 18.977 -5.354  6.356   0.34 10.64 ?  124 ALA   A C    1 
ATOM   2605 O  O    A ALA   A 1 124 ? 17.696 -5.448  6.815   0.66 10.14 ?  124 ALA   A O    1 
ATOM   2606 O  O    B ALA   A 1 124 ? 17.836 -5.692  6.695   0.34 11.09 ?  124 ALA   A O    1 
ATOM   2607 C  CB   A ALA   A 1 124 ? 20.638 -6.805  6.441   0.66 9.56  ?  124 ALA   A CB   1 
ATOM   2608 C  CB   B ALA   A 1 124 ? 20.747 -7.099  6.471   0.34 12.15 ?  124 ALA   A CB   1 
ATOM   2609 H  H    A ALA   A 1 124 ? 18.983 -6.076  8.740   0.66 11.42 ?  124 ALA   A H    1 
ATOM   2610 H  H    B ALA   A 1 124 ? 19.137 -6.439  8.692   0.34 13.37 ?  124 ALA   A H    1 
ATOM   2611 H  HA   A ALA   A 1 124 ? 20.741 -4.867  7.112   0.66 10.79 ?  124 ALA   A HA   1 
ATOM   2612 H  HA   B ALA   A 1 124 ? 20.874 -5.148  7.083   0.34 13.72 ?  124 ALA   A HA   1 
ATOM   2613 H  HB1  A ALA   A 1 124 ? 20.815 -6.578  5.514   0.66 11.47 ?  124 ALA   A HB1  1 
ATOM   2614 H  HB1  B ALA   A 1 124 ? 20.936 -6.914  5.538   0.34 14.59 ?  124 ALA   A HB1  1 
ATOM   2615 H  HB2  A ALA   A 1 124 ? 21.463 -7.073  6.878   0.66 11.47 ?  124 ALA   A HB2  1 
ATOM   2616 H  HB2  B ALA   A 1 124 ? 21.565 -7.363  6.926   0.34 14.59 ?  124 ALA   A HB2  1 
ATOM   2617 H  HB3  A ALA   A 1 124 ? 19.989 -7.521  6.490   0.66 11.47 ?  124 ALA   A HB3  1 
ATOM   2618 H  HB3  B ALA   A 1 124 ? 20.089 -7.808  6.541   0.34 14.59 ?  124 ALA   A HB3  1 
ATOM   2619 N  N    A PRO   A 1 125 ? 18.990 -4.350  5.342   0.66 9.91  ?  125 PRO   A N    1 
ATOM   2620 N  N    B PRO   A 1 125 ? 19.198 -4.580  5.297   0.34 9.42  ?  125 PRO   A N    1 
ATOM   2621 C  CA   A PRO   A 1 125 ? 17.915 -4.139  4.373   0.66 10.54 ?  125 PRO   A CA   1 
ATOM   2622 C  CA   B PRO   A 1 125 ? 18.134 -4.258  4.348   0.34 9.22  ?  125 PRO   A CA   1 
ATOM   2623 C  C    A PRO   A 1 125 ? 17.996 -5.224  3.302   0.66 10.72 ?  125 PRO   A C    1 
ATOM   2624 C  C    B PRO   A 1 125 ? 18.117 -5.291  3.225   0.34 10.21 ?  125 PRO   A C    1 
ATOM   2625 O  O    A PRO   A 1 125 ? 18.970 -5.976  3.221   0.66 11.20 ?  125 PRO   A O    1 
ATOM   2626 O  O    B PRO   A 1 125 ? 19.051 -6.076  3.052   0.34 10.52 ?  125 PRO   A O    1 
ATOM   2627 C  CB   A PRO   A 1 125 ? 18.314 -2.787  3.765   0.66 10.84 ?  125 PRO   A CB   1 
ATOM   2628 C  CB   B PRO   A 1 125 ? 18.614 -2.910  3.795   0.34 8.84  ?  125 PRO   A CB   1 
ATOM   2629 C  CG   A PRO   A 1 125 ? 19.814 -2.912  3.656   0.66 11.48 ?  125 PRO   A CG   1 
ATOM   2630 C  CG   B PRO   A 1 125 ? 20.102 -3.091  3.714   0.34 9.06  ?  125 PRO   A CG   1 
ATOM   2631 C  CD   A PRO   A 1 125 ? 20.230 -3.668  4.919   0.66 10.94 ?  125 PRO   A CD   1 
ATOM   2632 C  CD   B PRO   A 1 125 ? 20.475 -3.954  4.906   0.34 9.19  ?  125 PRO   A CD   1 
ATOM   2633 H  HA   A PRO   A 1 125 ? 17.037 -4.108  4.787   0.66 12.65 ?  125 PRO   A HA   1 
ATOM   2634 H  HA   B PRO   A 1 125 ? 17.265 -4.177  4.777   0.34 11.07 ?  125 PRO   A HA   1 
ATOM   2635 H  HB2  A PRO   A 1 125 ? 17.900 -2.677  2.894   0.66 13.02 ?  125 PRO   A HB2  1 
ATOM   2636 H  HB2  B PRO   A 1 125 ? 18.233 -2.756  2.917   0.34 10.61 ?  125 PRO   A HB2  1 
ATOM   2637 H  HB3  A PRO   A 1 125 ? 18.060 -2.066  4.367   0.66 13.02 ?  125 PRO   A HB3  1 
ATOM   2638 H  HB3  B PRO   A 1 125 ? 18.382 -2.197  4.409   0.34 10.61 ?  125 PRO   A HB3  1 
ATOM   2639 H  HG2  A PRO   A 1 125 ? 20.046 -3.417  2.860   0.66 13.79 ?  125 PRO   A HG2  1 
ATOM   2640 H  HG2  B PRO   A 1 125 ? 20.332 -3.537  2.884   0.34 10.87 ?  125 PRO   A HG2  1 
ATOM   2641 H  HG3  A PRO   A 1 125 ? 20.217 -2.029  3.632   0.66 13.79 ?  125 PRO   A HG3  1 
ATOM   2642 H  HG3  B PRO   A 1 125 ? 20.539 -2.226  3.769   0.34 10.87 ?  125 PRO   A HG3  1 
ATOM   2643 H  HD2  A PRO   A 1 125 ? 20.926 -4.312  4.715   0.66 13.13 ?  125 PRO   A HD2  1 
ATOM   2644 H  HD2  B PRO   A 1 125 ? 21.121 -4.632  4.646   0.34 11.04 ?  125 PRO   A HD2  1 
ATOM   2645 H  HD3  A PRO   A 1 125 ? 20.519 -3.043  5.606   0.66 13.13 ?  125 PRO   A HD3  1 
ATOM   2646 H  HD3  B PRO   A 1 125 ? 20.813 -3.404  5.631   0.34 11.04 ?  125 PRO   A HD3  1 
ATOM   2647 N  N    A LEU   A 1 126 ? 16.959 -5.289  2.465   0.66 10.75 ?  126 LEU   A N    1 
ATOM   2648 N  N    B LEU   A 1 126 ? 17.035 -5.270  2.452   0.34 10.73 ?  126 LEU   A N    1 
ATOM   2649 C  CA   A LEU   A 1 126 ? 17.023 -6.140  1.282   0.66 11.24 ?  126 LEU   A CA   1 
ATOM   2650 C  CA   B LEU   A 1 126 ? 17.000 -6.032  1.210   0.34 10.99 ?  126 LEU   A CA   1 
ATOM   2651 C  C    A LEU   A 1 126 ? 17.952 -5.528  0.241   0.66 11.49 ?  126 LEU   A C    1 
ATOM   2652 C  C    B LEU   A 1 126 ? 17.925 -5.385  0.188   0.34 10.99 ?  126 LEU   A C    1 
ATOM   2653 O  O    A LEU   A 1 126 ? 17.720 -4.415  -0.239  0.66 12.71 ?  126 LEU   A O    1 
ATOM   2654 O  O    B LEU   A 1 126 ? 17.716 -4.234  -0.208  0.34 11.95 ?  126 LEU   A O    1 
ATOM   2655 C  CB   A LEU   A 1 126 ? 15.636 -6.350  0.689   0.66 12.16 ?  126 LEU   A CB   1 
ATOM   2656 C  CB   B LEU   A 1 126 ? 15.578 -6.076  0.668   0.34 11.56 ?  126 LEU   A CB   1 
ATOM   2657 C  CG   A LEU   A 1 126 ? 14.720 -7.316  1.444   0.66 13.45 ?  126 LEU   A CG   1 
ATOM   2658 C  CG   B LEU   A 1 126 ? 14.623 -6.977  1.444   0.34 11.79 ?  126 LEU   A CG   1 
ATOM   2659 C  CD1  A LEU   A 1 126 ? 13.298 -7.173  0.943   0.66 14.50 ?  126 LEU   A CD1  1 
ATOM   2660 C  CD1  B LEU   A 1 126 ? 13.223 -6.820  0.897   0.34 11.87 ?  126 LEU   A CD1  1 
ATOM   2661 C  CD2  A LEU   A 1 126 ? 15.206 -8.754  1.292   0.66 13.67 ?  126 LEU   A CD2  1 
ATOM   2662 C  CD2  B LEU   A 1 126 ? 15.076 -8.432  1.370   0.34 12.09 ?  126 LEU   A CD2  1 
ATOM   2663 H  H    A LEU   A 1 126 ? 16.221 -4.854  2.554   0.66 12.91 ?  126 LEU   A H    1 
ATOM   2664 H  H    B LEU   A 1 126 ? 16.314 -4.833  2.626   0.34 12.88 ?  126 LEU   A H    1 
ATOM   2665 H  HA   A LEU   A 1 126 ? 17.379 -7.004  1.529   0.66 13.50 ?  126 LEU   A HA   1 
ATOM   2666 H  HA   B LEU   A 1 126 ? 17.301 -6.940  1.375   0.34 13.19 ?  126 LEU   A HA   1 
ATOM   2667 H  HB2  A LEU   A 1 126 ? 15.183 -5.493  0.657   0.66 14.60 ?  126 LEU   A HB2  1 
ATOM   2668 H  HB2  B LEU   A 1 126 ? 15.211 -5.177  0.688   0.34 13.88 ?  126 LEU   A HB2  1 
ATOM   2669 H  HB3  A LEU   A 1 126 ? 15.736 -6.694  -0.214  0.66 14.60 ?  126 LEU   A HB3  1 
ATOM   2670 H  HB3  B LEU   A 1 126 ? 15.604 -6.396  -0.247  0.34 13.88 ?  126 LEU   A HB3  1 
ATOM   2671 H  HG   A LEU   A 1 126 ? 14.735 -7.095  2.388   0.66 16.15 ?  126 LEU   A HG   1 
ATOM   2672 H  HG   B LEU   A 1 126 ? 14.618 -6.708  2.376   0.34 14.15 ?  126 LEU   A HG   1 
ATOM   2673 H  HD11 A LEU   A 1 126 ? 12.732 -7.799  1.421   0.66 17.40 ?  126 LEU   A HD11 1 
ATOM   2674 H  HD11 B LEU   A 1 126 ? 12.625 -7.396  1.396   0.34 14.25 ?  126 LEU   A HD11 1 
ATOM   2675 H  HD12 A LEU   A 1 126 ? 13.000 -6.265  1.102   0.66 17.40 ?  126 LEU   A HD12 1 
ATOM   2676 H  HD12 B LEU   A 1 126 ? 12.951 -5.895  0.990   0.34 14.25 ?  126 LEU   A HD12 1 
ATOM   2677 H  HD13 A LEU   A 1 126 ? 13.279 -7.368  -0.007  0.66 17.40 ?  126 LEU   A HD13 1 
ATOM   2678 H  HD13 B LEU   A 1 126 ? 13.223 -7.074  -0.040  0.34 14.25 ?  126 LEU   A HD13 1 
ATOM   2679 H  HD21 A LEU   A 1 126 ? 14.566 -9.349  1.706   0.66 16.41 ?  126 LEU   A HD21 1 
ATOM   2680 H  HD21 B LEU   A 1 126 ? 14.357 -9.002  1.674   0.34 14.52 ?  126 LEU   A HD21 1 
ATOM   2681 H  HD22 A LEU   A 1 126 ? 15.290 -8.959  0.347   0.66 16.41 ?  126 LEU   A HD22 1 
ATOM   2682 H  HD22 B LEU   A 1 126 ? 15.304 -8.643  0.450   0.34 14.52 ?  126 LEU   A HD22 1 
ATOM   2683 H  HD23 A LEU   A 1 126 ? 16.072 -8.843  1.725   0.66 16.41 ?  126 LEU   A HD23 1 
ATOM   2684 H  HD23 B LEU   A 1 126 ? 15.857 -8.549  1.936   0.34 14.52 ?  126 LEU   A HD23 1 
ATOM   2685 N  N    A LEU   A 1 127 ? 19.001 -6.266  -0.115  0.66 11.67 ?  127 LEU   A N    1 
ATOM   2686 N  N    B LEU   A 1 127 ? 18.941 -6.122  -0.251  0.34 10.67 ?  127 LEU   A N    1 
ATOM   2687 C  CA   A LEU   A 1 127 ? 19.971 -5.777  -1.085  0.66 11.49 ?  127 LEU   A CA   1 
ATOM   2688 C  CA   B LEU   A 1 127 ? 19.931 -5.553  -1.150  0.34 10.36 ?  127 LEU   A CA   1 
ATOM   2689 C  C    A LEU   A 1 127 ? 19.324 -5.556  -2.445  0.66 10.28 ?  127 LEU   A C    1 
ATOM   2690 C  C    B LEU   A 1 127 ? 19.375 -5.426  -2.561  0.34 11.04 ?  127 LEU   A C    1 
ATOM   2691 O  O    A LEU   A 1 127 ? 18.493 -6.346  -2.904  0.66 11.05 ?  127 LEU   A O    1 
ATOM   2692 O  O    B LEU   A 1 127 ? 18.511 -6.198  -2.990  0.34 11.63 ?  127 LEU   A O    1 
ATOM   2693 C  CB   A LEU   A 1 127 ? 21.119 -6.780  -1.220  0.66 11.95 ?  127 LEU   A CB   1 
ATOM   2694 C  CB   B LEU   A 1 127 ? 21.194 -6.411  -1.175  0.34 10.47 ?  127 LEU   A CB   1 
ATOM   2695 C  CG   A LEU   A 1 127 ? 21.949 -7.023  0.037   0.66 12.22 ?  127 LEU   A CG   1 
ATOM   2696 C  CG   B LEU   A 1 127 ? 21.962 -6.518  0.145   0.34 10.77 ?  127 LEU   A CG   1 
ATOM   2697 C  CD1  A LEU   A 1 127 ? 23.056 -8.018  -0.260  0.66 12.38 ?  127 LEU   A CD1  1 
ATOM   2698 C  CD1  B LEU   A 1 127 ? 23.138 -7.461  -0.005  0.34 11.04 ?  127 LEU   A CD1  1 
ATOM   2699 C  CD2  A LEU   A 1 127 ? 22.527 -5.724  0.563   0.66 12.55 ?  127 LEU   A CD2  1 
ATOM   2700 C  CD2  B LEU   A 1 127 ? 22.435 -5.147  0.608   0.34 11.50 ?  127 LEU   A CD2  1 
ATOM   2701 H  H    A LEU   A 1 127 ? 19.173 -7.051  0.192   0.66 14.01 ?  127 LEU   A H    1 
ATOM   2702 H  H    B LEU   A 1 127 ? 19.072 -6.950  -0.047  0.34 12.81 ?  127 LEU   A H    1 
ATOM   2703 H  HA   A LEU   A 1 127 ? 20.339 -4.936  -0.780  0.66 13.79 ?  127 LEU   A HA   1 
ATOM   2704 H  HA   B LEU   A 1 127 ? 20.163 -4.669  -0.839  0.34 12.44 ?  127 LEU   A HA   1 
ATOM   2705 H  HB2  A LEU   A 1 127 ? 20.749 -7.636  -1.494  0.66 14.34 ?  127 LEU   A HB2  1 
ATOM   2706 H  HB2  B LEU   A 1 127 ? 20.945 -7.309  -1.443  0.34 12.57 ?  127 LEU   A HB2  1 
ATOM   2707 H  HB3  A LEU   A 1 127 ? 21.727 -6.461  -1.906  0.66 14.34 ?  127 LEU   A HB3  1 
ATOM   2708 H  HB3  B LEU   A 1 127 ? 21.798 -6.035  -1.835  0.34 12.57 ?  127 LEU   A HB3  1 
ATOM   2709 H  HG   A LEU   A 1 127 ? 21.376 -7.406  0.725   0.66 14.67 ?  127 LEU   A HG   1 
ATOM   2710 H  HG   B LEU   A 1 127 ? 21.369 -6.875  0.826   0.34 12.94 ?  127 LEU   A HG   1 
ATOM   2711 H  HD11 A LEU   A 1 127 ? 23.540 -8.207  0.561   0.66 14.86 ?  127 LEU   A HD11 1 
ATOM   2712 H  HD11 B LEU   A 1 127 ? 23.637 -7.473  0.826   0.34 13.25 ?  127 LEU   A HD11 1 
ATOM   2713 H  HD12 A LEU   A 1 127 ? 22.665 -8.838  -0.606  0.66 14.86 ?  127 LEU   A HD12 1 
ATOM   2714 H  HD12 B LEU   A 1 127 ? 22.804 -8.349  -0.205  0.34 13.25 ?  127 LEU   A HD12 1 
ATOM   2715 H  HD13 A LEU   A 1 127 ? 23.655 -7.635  -0.917  0.66 14.86 ?  127 LEU   A HD13 1 
ATOM   2716 H  HD13 B LEU   A 1 127 ? 23.702 -7.146  -0.726  0.34 13.25 ?  127 LEU   A HD13 1 
ATOM   2717 H  HD21 A LEU   A 1 127 ? 23.182 -5.924  1.247   0.66 15.07 ?  127 LEU   A HD21 1 
ATOM   2718 H  HD21 B LEU   A 1 127 ? 23.024 -5.258  1.369   0.34 13.81 ?  127 LEU   A HD21 1 
ATOM   2719 H  HD22 A LEU   A 1 127 ? 22.951 -5.251  -0.174  0.66 15.07 ?  127 LEU   A HD22 1 
ATOM   2720 H  HD22 B LEU   A 1 127 ? 22.912 -4.717  -0.120  0.34 13.81 ?  127 LEU   A HD22 1 
ATOM   2721 H  HD23 A LEU   A 1 127 ? 21.811 -5.185  0.932   0.66 15.07 ?  127 LEU   A HD23 1 
ATOM   2722 H  HD23 B LEU   A 1 127 ? 21.666 -4.612  0.859   0.34 13.81 ?  127 LEU   A HD23 1 
ATOM   2723 N  N    A SER   A 1 128 ? 19.731 -4.468  -3.089  0.66 10.39 ?  128 SER   A N    1 
ATOM   2724 N  N    B SER   A 1 128 ? 19.883 -4.428  -3.282  0.34 11.31 ?  128 SER   A N    1 
ATOM   2725 C  CA   A SER   A 1 128 ? 19.310 -4.043  -4.418  0.66 10.42 ?  128 SER   A CA   1 
ATOM   2726 C  CA   B SER   A 1 128 ? 19.542 -4.148  -4.668  0.34 11.55 ?  128 SER   A CA   1 
ATOM   2727 C  C    A SER   A 1 128 ? 17.847 -3.605  -4.489  0.66 10.11 ?  128 SER   A C    1 
ATOM   2728 C  C    B SER   A 1 128 ? 18.122 -3.626  -4.819  0.34 12.12 ?  128 SER   A C    1 
ATOM   2729 O  O    A SER   A 1 128 ? 17.367 -3.280  -5.578  0.66 11.57 ?  128 SER   A O    1 
ATOM   2730 O  O    B SER   A 1 128 ? 17.691 -3.356  -5.947  0.34 12.37 ?  128 SER   A O    1 
ATOM   2731 C  CB   A SER   A 1 128 ? 19.661 -5.049  -5.522  0.66 10.86 ?  128 SER   A CB   1 
ATOM   2732 C  CB   B SER   A 1 128 ? 19.780 -5.357  -5.580  0.34 11.53 ?  128 SER   A CB   1 
ATOM   2733 O  OG   A SER   A 1 128 ? 21.072 -5.261  -5.588  0.66 11.33 ?  128 SER   A OG   1 
ATOM   2734 O  OG   B SER   A 1 128 ? 21.168 -5.576  -5.771  0.34 11.06 ?  128 SER   A OG   1 
ATOM   2735 H  H    A SER   A 1 128 ? 20.310 -3.923  -2.746  0.66 12.48 ?  128 SER   A H    1 
ATOM   2736 H  H    B SER   A 1 128 ? 20.455 -3.863  -2.968  0.34 13.58 ?  128 SER   A H    1 
ATOM   2737 H  HA   A SER   A 1 128 ? 19.829 -3.255  -4.615  0.66 12.51 ?  128 SER   A HA   1 
ATOM   2738 H  HA   B SER   A 1 128 ? 20.118 -3.438  -4.983  0.34 13.86 ?  128 SER   A HA   1 
ATOM   2739 H  HB2  A SER   A 1 128 ? 19.223 -5.891  -5.341  0.66 13.04 ?  128 SER   A HB2  1 
ATOM   2740 H  HB2  B SER   A 1 128 ? 19.379 -6.141  -5.168  0.34 13.84 ?  128 SER   A HB2  1 
ATOM   2741 H  HB3  A SER   A 1 128 ? 19.357 -4.691  -6.375  0.66 13.04 ?  128 SER   A HB3  1 
ATOM   2742 H  HB3  B SER   A 1 128 ? 19.381 -5.186  -6.438  0.34 13.84 ?  128 SER   A HB3  1 
ATOM   2743 H  HG   A SER   A 1 128 ? 21.465 -4.533  -5.746  0.66 13.60 ?  128 SER   A HG   1 
ATOM   2744 H  HG   B SER   A 1 128 ? 21.519 -4.873  -6.068  0.34 13.28 ?  128 SER   A HG   1 
ATOM   2745 N  N    A ALA   A 1 129 ? 17.142 -3.551  -3.359  0.66 10.39 ?  129 ALA   A N    1 
ATOM   2746 N  N    B ALA   A 1 129 ? 17.400 -3.434  -3.720  0.34 12.95 ?  129 ALA   A N    1 
ATOM   2747 C  CA   A ALA   A 1 129 ? 15.781 -3.030  -3.332  0.66 11.16 ?  129 ALA   A CA   1 
ATOM   2748 C  CA   B ALA   A 1 129 ? 16.016 -3.001  -3.750  0.34 13.62 ?  129 ALA   A CA   1 
ATOM   2749 C  C    A ALA   A 1 129 ? 15.818 -1.500  -3.420  0.66 11.71 ?  129 ALA   A C    1 
ATOM   2750 C  C    B ALA   A 1 129 ? 15.923 -1.501  -3.463  0.34 13.46 ?  129 ALA   A C    1 
ATOM   2751 O  O    A ALA   A 1 129 ? 16.870 -0.882  -3.618  0.66 12.01 ?  129 ALA   A O    1 
ATOM   2752 O  O    B ALA   A 1 129 ? 16.935 -0.797  -3.359  0.34 13.54 ?  129 ALA   A O    1 
ATOM   2753 C  CB   A ALA   A 1 129 ? 15.030 -3.558  -2.108  0.66 11.37 ?  129 ALA   A CB   1 
ATOM   2754 C  CB   B ALA   A 1 129 ? 15.194 -3.865  -2.795  0.34 13.94 ?  129 ALA   A CB   1 
ATOM   2755 H  H    A ALA   A 1 129 ? 17.435 -3.804  -2.584  0.66 12.47 ?  129 ALA   A H    1 
ATOM   2756 H  H    B ALA   A 1 129 ? 17.716 -3.545  -2.918  0.34 15.54 ?  129 ALA   A H    1 
ATOM   2757 H  HA   A ALA   A 1 129 ? 15.319 -3.356  -4.116  0.66 13.40 ?  129 ALA   A HA   1 
ATOM   2758 H  HA   B ALA   A 1 129 ? 15.676 -3.134  -4.636  0.34 16.36 ?  129 ALA   A HA   1 
ATOM   2759 H  HB1  A ALA   A 1 129 ? 14.126 -3.204  -2.117  0.66 13.65 ?  129 ALA   A HB1  1 
ATOM   2760 H  HB1  B ALA   A 1 129 ? 14.260 -3.655  -2.922  0.34 16.73 ?  129 ALA   A HB1  1 
ATOM   2761 H  HB2  A ALA   A 1 129 ? 15.005 -4.528  -2.147  0.66 13.65 ?  129 ALA   A HB2  1 
ATOM   2762 H  HB2  B ALA   A 1 129 ? 15.358 -4.797  -3.011  0.34 16.73 ?  129 ALA   A HB2  1 
ATOM   2763 H  HB3  A ALA   A 1 129 ? 15.490 -3.272  -1.304  0.66 13.65 ?  129 ALA   A HB3  1 
ATOM   2764 H  HB3  B ALA   A 1 129 ? 15.466 -3.684  -1.883  0.34 16.73 ?  129 ALA   A HB3  1 
ATOM   2765 N  N    A GLY   A 1 130 ? 14.650 -0.875  -3.294  0.66 13.35 ?  130 GLY   A N    1 
ATOM   2766 N  N    B GLY   A 1 130 ? 14.696 -0.998  -3.352  0.34 13.75 ?  130 GLY   A N    1 
ATOM   2767 C  CA   A GLY   A 1 130 ? 14.578 0.577   -3.330  0.66 14.18 ?  130 GLY   A CA   1 
ATOM   2768 C  CA   B GLY   A 1 130 ? 14.511 0.435   -3.191  0.34 13.58 ?  130 GLY   A CA   1 
ATOM   2769 C  C    A GLY   A 1 130 ? 15.214 1.149   -4.579  0.66 13.72 ?  130 GLY   A C    1 
ATOM   2770 C  C    B GLY   A 1 130 ? 15.071 1.161   -4.400  0.34 13.03 ?  130 GLY   A C    1 
ATOM   2771 O  O    A GLY   A 1 130 ? 14.988 0.674   -5.698  0.66 13.91 ?  130 GLY   A O    1 
ATOM   2772 O  O    B GLY   A 1 130 ? 14.800 0.800   -5.550  0.34 12.89 ?  130 GLY   A O    1 
ATOM   2773 H  H    A GLY   A 1 130 ? 13.892 -1.266  -3.185  0.66 16.02 ?  130 GLY   A H    1 
ATOM   2774 H  H    B GLY   A 1 130 ? 13.969 -1.457  -3.372  0.34 16.51 ?  130 GLY   A H    1 
ATOM   2775 H  HA2  A GLY   A 1 130 ? 13.647 0.853   -3.300  0.66 17.03 ?  130 GLY   A HA2  1 
ATOM   2776 H  HA2  B GLY   A 1 130 ? 13.562 0.640   -3.097  0.34 16.31 ?  130 GLY   A HA2  1 
ATOM   2777 H  HA3  A GLY   A 1 130 ? 15.034 0.944   -2.560  0.66 17.03 ?  130 GLY   A HA3  1 
ATOM   2778 H  HA3  B GLY   A 1 130 ? 14.973 0.743   -2.395  0.34 16.31 ?  130 GLY   A HA3  1 
ATOM   2779 N  N    A ILE   A 1 131 ? 16.028 2.193   -4.388  0.66 12.98 ?  131 ILE   A N    1 
ATOM   2780 N  N    B ILE   A 1 131 ? 15.880 2.195   -4.144  0.34 13.13 ?  131 ILE   A N    1 
ATOM   2781 C  CA   A ILE   A 1 131 ? 16.595 2.944   -5.506  0.66 12.81 ?  131 ILE   A CA   1 
ATOM   2782 C  CA   B ILE   A 1 131 ? 16.446 3.008   -5.219  0.34 13.23 ?  131 ILE   A CA   1 
ATOM   2783 C  C    A ILE   A 1 131 ? 17.626 2.162   -6.304  0.66 12.32 ?  131 ILE   A C    1 
ATOM   2784 C  C    B ILE   A 1 131 ? 17.421 2.250   -6.112  0.34 12.86 ?  131 ILE   A C    1 
ATOM   2785 O  O    A ILE   A 1 131 ? 18.061 2.645   -7.357  0.66 13.18 ?  131 ILE   A O    1 
ATOM   2786 O  O    B ILE   A 1 131 ? 17.783 2.762   -7.178  0.34 13.03 ?  131 ILE   A O    1 
ATOM   2787 C  CB   A ILE   A 1 131 ? 17.157 4.314   -5.064  0.66 13.84 ?  131 ILE   A CB   1 
ATOM   2788 C  CB   B ILE   A 1 131 ? 17.108 4.300   -4.685  0.34 13.74 ?  131 ILE   A CB   1 
ATOM   2789 C  CG1  A ILE   A 1 131 ? 18.412 4.149   -4.196  0.66 14.28 ?  131 ILE   A CG1  1 
ATOM   2790 C  CG1  B ILE   A 1 131 ? 18.295 3.984   -3.766  0.34 14.61 ?  131 ILE   A CG1  1 
ATOM   2791 C  CG2  A ILE   A 1 131 ? 16.078 5.122   -4.342  0.66 13.90 ?  131 ILE   A CG2  1 
ATOM   2792 C  CG2  B ILE   A 1 131 ? 16.089 5.168   -3.966  0.34 14.25 ?  131 ILE   A CG2  1 
ATOM   2793 C  CD1  A ILE   A 1 131 ? 19.056 5.473   -3.792  0.66 14.59 ?  131 ILE   A CD1  1 
ATOM   2794 C  CD1  B ILE   A 1 131 ? 18.919 5.220   -3.115  0.34 15.38 ?  131 ILE   A CD1  1 
ATOM   2795 H  H    A ILE   A 1 131 ? 16.262 2.484   -3.616  0.66 15.58 ?  131 ILE   A H    1 
ATOM   2796 H  H    B ILE   A 1 131 ? 16.097 2.450   -3.354  0.34 15.77 ?  131 ILE   A H    1 
ATOM   2797 H  HA   A ILE   A 1 131 ? 15.878 3.125   -6.123  0.66 15.38 ?  131 ILE   A HA   1 
ATOM   2798 H  HA   B ILE   A 1 131 ? 15.710 3.293   -5.783  0.34 15.88 ?  131 ILE   A HA   1 
ATOM   2799 H  HB   A ILE   A 1 131 ? 17.407 4.800   -5.864  0.66 16.61 ?  131 ILE   A HB   1 
ATOM   2800 H  HB   B ILE   A 1 131 ? 17.440 4.798   -5.446  0.34 16.50 ?  131 ILE   A HB   1 
ATOM   2801 H  HG12 A ILE   A 1 131 ? 18.173 3.673   -3.388  0.66 17.14 ?  131 ILE   A HG12 1 
ATOM   2802 H  HG12 B ILE   A 1 131 ? 17.995 3.397   -3.057  0.34 17.54 ?  131 ILE   A HG12 1 
ATOM   2803 H  HG13 A ILE   A 1 131 ? 19.076 3.643   -4.693  0.66 17.14 ?  131 ILE   A HG13 1 
ATOM   2804 H  HG13 B ILE   A 1 131 ? 18.986 3.547   -4.287  0.34 17.54 ?  131 ILE   A HG13 1 
ATOM   2805 H  HG21 A ILE   A 1 131 ? 16.395 6.025   -4.208  0.66 16.68 ?  131 ILE   A HG21 1 
ATOM   2806 H  HG21 B ILE   A 1 131 ? 16.456 6.058   -3.855  0.34 17.11 ?  131 ILE   A HG21 1 
ATOM   2807 H  HG22 A ILE   A 1 131 ? 15.274 5.129   -4.886  0.66 16.68 ?  131 ILE   A HG22 1 
ATOM   2808 H  HG22 B ILE   A 1 131 ? 15.281 5.207   -4.499  0.34 17.11 ?  131 ILE   A HG22 1 
ATOM   2809 H  HG23 A ILE   A 1 131 ? 15.891 4.702   -3.486  0.66 16.68 ?  131 ILE   A HG23 1 
ATOM   2810 H  HG23 B ILE   A 1 131 ? 15.897 4.774   -3.101  0.34 17.11 ?  131 ILE   A HG23 1 
ATOM   2811 H  HD11 A ILE   A 1 131 ? 19.900 5.292   -3.348  0.66 17.52 ?  131 ILE   A HD11 1 
ATOM   2812 H  HD11 B ILE   A 1 131 ? 19.758 4.969   -2.697  0.34 18.46 ?  131 ILE   A HD11 1 
ATOM   2813 H  HD12 A ILE   A 1 131 ? 19.210 6.009   -4.586  0.66 17.52 ?  131 ILE   A HD12 1 
ATOM   2814 H  HD12 B ILE   A 1 131 ? 19.078 5.892   -3.796  0.34 18.46 ?  131 ILE   A HD12 1 
ATOM   2815 H  HD13 A ILE   A 1 131 ? 18.461 5.945   -3.187  0.66 17.52 ?  131 ILE   A HD13 1 
ATOM   2816 H  HD13 B ILE   A 1 131 ? 18.309 5.570   -2.444  0.34 18.46 ?  131 ILE   A HD13 1 
ATOM   2817 N  N    A PHE   A 1 132 ? 18.017 0.962   -5.853  0.66 12.13 ?  132 PHE   A N    1 
ATOM   2818 N  N    B PHE   A 1 132 ? 17.861 1.049   -5.721  0.34 12.91 ?  132 PHE   A N    1 
ATOM   2819 C  CA   A PHE   A 1 132 ? 18.847 0.086   -6.677  0.66 12.44 ?  132 PHE   A CA   1 
ATOM   2820 C  CA   B PHE   A 1 132 ? 18.797 0.293   -6.552  0.34 13.17 ?  132 PHE   A CA   1 
ATOM   2821 C  C    A PHE   A 1 132 ? 18.036 -0.671  -7.728  0.66 13.06 ?  132 PHE   A C    1 
ATOM   2822 C  C    B PHE   A 1 132 ? 18.133 -0.430  -7.723  0.34 13.71 ?  132 PHE   A C    1 
ATOM   2823 O  O    A PHE   A 1 132 ? 18.627 -1.327  -8.590  0.66 13.29 ?  132 PHE   A O    1 
ATOM   2824 O  O    B PHE   A 1 132 ? 18.848 -0.900  -8.616  0.34 14.50 ?  132 PHE   A O    1 
ATOM   2825 C  CB   A PHE   A 1 132 ? 19.658 -0.901  -5.820  0.66 11.84 ?  132 PHE   A CB   1 
ATOM   2826 C  CB   B PHE   A 1 132 ? 19.622 -0.692  -5.712  0.34 12.74 ?  132 PHE   A CB   1 
ATOM   2827 C  CG   A PHE   A 1 132 ? 20.864 -0.293  -5.125  0.66 11.92 ?  132 PHE   A CG   1 
ATOM   2828 C  CG   B PHE   A 1 132 ? 20.886 -0.098  -5.134  0.34 12.83 ?  132 PHE   A CG   1 
ATOM   2829 C  CD1  A PHE   A 1 132 ? 20.718 0.727   -4.199  0.66 12.35 ?  132 PHE   A CD1  1 
ATOM   2830 C  CD1  B PHE   A 1 132 ? 20.830 0.968   -4.254  0.34 13.28 ?  132 PHE   A CD1  1 
ATOM   2831 C  CD2  A PHE   A 1 132 ? 22.141 -0.791  -5.365  0.66 12.81 ?  132 PHE   A CD2  1 
ATOM   2832 C  CD2  B PHE   A 1 132 ? 22.130 -0.623  -5.461  0.34 13.52 ?  132 PHE   A CD2  1 
ATOM   2833 C  CE1  A PHE   A 1 132 ? 21.825 1.263   -3.551  0.66 12.32 ?  132 PHE   A CE1  1 
ATOM   2834 C  CE1  B PHE   A 1 132 ? 21.988 1.510   -3.718  0.34 13.80 ?  132 PHE   A CE1  1 
ATOM   2835 C  CE2  A PHE   A 1 132 ? 23.248 -0.263  -4.716  0.66 12.57 ?  132 PHE   A CE2  1 
ATOM   2836 C  CE2  B PHE   A 1 132 ? 23.292 -0.088  -4.925  0.34 14.22 ?  132 PHE   A CE2  1 
ATOM   2837 C  CZ   A PHE   A 1 132 ? 23.089 0.768   -3.807  0.66 12.21 ?  132 PHE   A CZ   1 
ATOM   2838 C  CZ   B PHE   A 1 132 ? 23.219 0.979   -4.052  0.34 14.37 ?  132 PHE   A CZ   1 
ATOM   2839 H  H    A PHE   A 1 132 ? 17.823 0.635   -5.073  0.66 14.56 ?  132 PHE   A H    1 
ATOM   2840 H  H    B PHE   A 1 132 ? 17.648 0.665   -4.980  0.34 15.50 ?  132 PHE   A H    1 
ATOM   2841 H  HA   A PHE   A 1 132 ? 19.487 0.637   -7.145  0.66 14.94 ?  132 PHE   A HA   1 
ATOM   2842 H  HA   B PHE   A 1 132 ? 19.423 0.926   -6.932  0.34 15.81 ?  132 PHE   A HA   1 
ATOM   2843 H  HB2  A PHE   A 1 132 ? 19.083 -1.264  -5.131  0.66 14.22 ?  132 PHE   A HB2  1 
ATOM   2844 H  HB2  B PHE   A 1 132 ? 19.082 -1.006  -4.973  0.34 15.30 ?  132 PHE   A HB2  1 
ATOM   2845 H  HB3  A PHE   A 1 132 ? 19.981 -1.624  -6.389  0.66 14.22 ?  132 PHE   A HB3  1 
ATOM   2846 H  HB3  B PHE   A 1 132 ? 19.879 -1.441  -6.274  0.34 15.30 ?  132 PHE   A HB3  1 
ATOM   2847 H  HD1  A PHE   A 1 132 ? 19.873 1.061   -4.018  0.66 14.83 ?  132 PHE   A HD1  1 
ATOM   2848 H  HD1  B PHE   A 1 132 ? 20.007 1.329   -4.025  0.34 15.94 ?  132 PHE   A HD1  1 
ATOM   2849 H  HD2  A PHE   A 1 132 ? 22.259 -1.486  -5.979  0.66 15.37 ?  132 PHE   A HD2  1 
ATOM   2850 H  HD2  B PHE   A 1 132 ? 22.188 -1.343  -6.049  0.34 16.24 ?  132 PHE   A HD2  1 
ATOM   2851 H  HE1  A PHE   A 1 132 ? 21.714 1.952   -2.938  0.66 14.79 ?  132 PHE   A HE1  1 
ATOM   2852 H  HE1  B PHE   A 1 132 ? 21.936 2.228   -3.129  0.34 16.56 ?  132 PHE   A HE1  1 
ATOM   2853 H  HE2  A PHE   A 1 132 ? 24.100 -0.596  -4.900  0.66 15.09 ?  132 PHE   A HE2  1 
ATOM   2854 H  HE2  B PHE   A 1 132 ? 24.122 -0.447  -5.155  0.34 17.07 ?  132 PHE   A HE2  1 
ATOM   2855 H  HZ   A PHE   A 1 132 ? 23.830 1.129   -3.377  0.66 14.66 ?  132 PHE   A HZ   1 
ATOM   2856 H  HZ   B PHE   A 1 132 ? 23.998 1.342   -3.693  0.34 17.25 ?  132 PHE   A HZ   1 
ATOM   2857 N  N    A GLY   A 1 133 ? 16.705 -0.619  -7.669  0.66 13.46 ?  133 GLY   A N    1 
ATOM   2858 N  N    B GLY   A 1 133 ? 16.803 -0.544  -7.755  0.34 13.55 ?  133 GLY   A N    1 
ATOM   2859 C  CA   A GLY   A 1 133 ? 15.868 -0.984  -8.801  0.66 13.89 ?  133 GLY   A CA   1 
ATOM   2860 C  CA   B GLY   A 1 133 ? 16.088 -0.915  -8.963  0.34 13.49 ?  133 GLY   A CA   1 
ATOM   2861 C  C    A GLY   A 1 133 ? 15.600 -2.456  -9.037  0.66 13.99 ?  133 GLY   A C    1 
ATOM   2862 C  C    B GLY   A 1 133 ? 15.544 -2.330  -9.018  0.34 13.33 ?  133 GLY   A C    1 
ATOM   2863 O  O    A GLY   A 1 133 ? 15.026 -2.790  -10.080 0.66 14.61 ?  133 GLY   A O    1 
ATOM   2864 O  O    B GLY   A 1 133 ? 14.627 -2.586  -9.812  0.34 13.44 ?  133 GLY   A O    1 
ATOM   2865 H  H    A GLY   A 1 133 ? 16.258 -0.378  -6.973  0.66 16.16 ?  133 GLY   A H    1 
ATOM   2866 H  H    B GLY   A 1 133 ? 16.288 -0.404  -7.076  0.34 16.27 ?  133 GLY   A H    1 
ATOM   2867 H  HA2  A GLY   A 1 133 ? 15.009 -0.546  -8.703  0.66 16.68 ?  133 GLY   A HA2  1 
ATOM   2868 H  HA2  B GLY   A 1 133 ? 15.335 -0.321  -9.072  0.34 16.20 ?  133 GLY   A HA2  1 
ATOM   2869 H  HA3  A GLY   A 1 133 ? 16.281 -0.645  -9.608  0.66 16.68 ?  133 GLY   A HA3  1 
ATOM   2870 H  HA3  B GLY   A 1 133 ? 16.677 -0.792  -9.724  0.34 16.20 ?  133 GLY   A HA3  1 
ATOM   2871 N  N    A ALA   A 1 134 ? 15.997 -3.349  -8.132  0.66 13.59 ?  134 ALA   A N    1 
ATOM   2872 N  N    B ALA   A 1 134 ? 16.074 -3.260  -8.229  0.34 13.04 ?  134 ALA   A N    1 
ATOM   2873 C  CA   A ALA   A 1 134 ? 15.674 -4.758  -8.303  0.66 14.10 ?  134 ALA   A CA   1 
ATOM   2874 C  CA   B ALA   A 1 134 ? 15.637 -4.642  -8.358  0.34 13.18 ?  134 ALA   A CA   1 
ATOM   2875 C  C    A ALA   A 1 134 ? 14.309 -5.075  -7.688  0.66 14.28 ?  134 ALA   A C    1 
ATOM   2876 C  C    B ALA   A 1 134 ? 14.330 -4.882  -7.605  0.34 12.95 ?  134 ALA   A C    1 
ATOM   2877 O  O    A ALA   A 1 134 ? 13.741 -4.294  -6.921  0.66 15.45 ?  134 ALA   A O    1 
ATOM   2878 O  O    B ALA   A 1 134 ? 13.920 -4.102  -6.740  0.34 13.64 ?  134 ALA   A O    1 
ATOM   2879 C  CB   A ALA   A 1 134 ? 16.761 -5.646  -7.693  0.66 14.90 ?  134 ALA   A CB   1 
ATOM   2880 C  CB   B ALA   A 1 134 ? 16.703 -5.605  -7.843  0.34 13.88 ?  134 ALA   A CB   1 
ATOM   2881 H  H    A ALA   A 1 134 ? 16.461 -3.168  -7.425  0.66 16.31 ?  134 ALA   A H    1 
ATOM   2882 H  H    B ALA   A 1 134 ? 16.674 -3.119  -7.629  0.34 15.66 ?  134 ALA   A H    1 
ATOM   2883 H  HA   A ALA   A 1 134 ? 15.630 -4.956  -9.251  0.66 16.92 ?  134 ALA   A HA   1 
ATOM   2884 H  HA   B ALA   A 1 134 ? 15.484 -4.833  -9.297  0.34 15.83 ?  134 ALA   A HA   1 
ATOM   2885 H  HB1  A ALA   A 1 134 ? 16.522 -6.577  -7.833  0.66 17.88 ?  134 ALA   A HB1  1 
ATOM   2886 H  HB1  B ALA   A 1 134 ? 16.386 -6.514  -7.965  0.34 16.66 ?  134 ALA   A HB1  1 
ATOM   2887 H  HB2  A ALA   A 1 134 ? 17.607 -5.455  -8.131  0.66 17.88 ?  134 ALA   A HB2  1 
ATOM   2888 H  HB2  B ALA   A 1 134 ? 17.518 -5.467  -8.348  0.34 16.66 ?  134 ALA   A HB2  1 
ATOM   2889 H  HB3  A ALA   A 1 134 ? 16.829 -5.459  -6.746  0.66 17.88 ?  134 ALA   A HB3  1 
ATOM   2890 H  HB3  B ALA   A 1 134 ? 16.857 -5.429  -6.904  0.34 16.66 ?  134 ALA   A HB3  1 
ATOM   2891 N  N    A ASP   A 1 135 ? 13.782 -6.241  -8.048  0.66 14.66 ?  135 ASP   A N    1 
ATOM   2892 N  N    B ASP   A 1 135 ? 13.684 -5.992  -7.945  0.34 13.25 ?  135 ASP   A N    1 
ATOM   2893 C  CA   A ASP   A 1 135 ? 12.524 -6.730  -7.487  0.66 15.45 ?  135 ASP   A CA   1 
ATOM   2894 C  CA   B ASP   A 1 135 ? 12.432 -6.382  -7.309  0.34 13.67 ?  135 ASP   A CA   1 
ATOM   2895 C  C    A ASP   A 1 135 ? 12.758 -7.168  -6.048  0.66 15.20 ?  135 ASP   A C    1 
ATOM   2896 C  C    B ASP   A 1 135 ? 12.718 -6.886  -5.899  0.34 13.43 ?  135 ASP   A C    1 
ATOM   2897 O  O    A ASP   A 1 135 ? 13.540 -8.100  -5.818  0.66 15.10 ?  135 ASP   A O    1 
ATOM   2898 O  O    B ASP   A 1 135 ? 13.432 -7.886  -5.745  0.34 13.59 ?  135 ASP   A O    1 
ATOM   2899 C  CB   A ASP   A 1 135 ? 12.052 -7.920  -8.323  0.66 17.29 ?  135 ASP   A CB   1 
ATOM   2900 C  CB   B ASP   A 1 135 ? 11.782 -7.489  -8.133  0.34 14.63 ?  135 ASP   A CB   1 
ATOM   2901 C  CG   A ASP   A 1 135 ? 10.798 -8.590  -7.767  0.66 19.53 ?  135 ASP   A CG   1 
ATOM   2902 C  CG   B ASP   A 1 135 ? 10.413 -7.891  -7.603  0.34 15.79 ?  135 ASP   A CG   1 
ATOM   2903 O  OD1  A ASP   A 1 135 ? 10.220 -8.089  -6.782  0.66 19.21 ?  135 ASP   A OD1  1 
ATOM   2904 O  OD1  B ASP   A 1 135 ? 10.036 -7.444  -6.496  0.34 15.99 ?  135 ASP   A OD1  1 
ATOM   2905 O  OD2  A ASP   A 1 135 ? 10.394 -9.631  -8.330  0.66 22.32 -1 135 ASP   A OD2  1 
ATOM   2906 O  OD2  B ASP   A 1 135 ? 9.708  -8.651  -8.300  0.34 16.87 -1 135 ASP   A OD2  1 
ATOM   2907 H  H    A ASP   A 1 135 ? 14.134 -6.770  -8.625  0.66 17.60 ?  135 ASP   A H    1 
ATOM   2908 H  H    B ASP   A 1 135 ? 13.951 -6.544  -8.544  0.34 15.91 ?  135 ASP   A H    1 
ATOM   2909 H  HA   A ASP   A 1 135 ? 11.852 -6.028  -7.525  0.66 18.54 ?  135 ASP   A HA   1 
ATOM   2910 H  HA   B ASP   A 1 135 ? 11.823 -5.626  -7.282  0.34 16.41 ?  135 ASP   A HA   1 
ATOM   2911 H  HB2  A ASP   A 1 135 ? 11.858 -7.616  -9.221  0.66 20.75 ?  135 ASP   A HB2  1 
ATOM   2912 H  HB2  B ASP   A 1 135 ? 11.679 -7.179  -9.048  0.34 17.56 ?  135 ASP   A HB2  1 
ATOM   2913 H  HB3  A ASP   A 1 135 ? 12.756 -8.585  -8.340  0.66 20.75 ?  135 ASP   A HB3  1 
ATOM   2914 H  HB3  B ASP   A 1 135 ? 12.358 -8.271  -8.115  0.34 17.56 ?  135 ASP   A HB3  1 
ATOM   2915 N  N    A PRO   A 1 136 ? 12.127 -6.534  -5.056  0.66 15.11 ?  136 PRO   A N    1 
ATOM   2916 N  N    B PRO   A 1 136 ? 12.201 -6.236  -4.853  0.34 13.33 ?  136 PRO   A N    1 
ATOM   2917 C  CA   A PRO   A 1 136 ? 12.376 -6.935  -3.660  0.66 15.19 ?  136 PRO   A CA   1 
ATOM   2918 C  CA   B PRO   A 1 136 ? 12.471 -6.713  -3.485  0.34 13.57 ?  136 PRO   A CA   1 
ATOM   2919 C  C    A PRO   A 1 136 ? 11.958 -8.360  -3.347  0.66 14.18 ?  136 PRO   A C    1 
ATOM   2920 C  C    B PRO   A 1 136 ? 11.978 -8.127  -3.207  0.34 13.12 ?  136 PRO   A C    1 
ATOM   2921 O  O    A PRO   A 1 136 ? 12.576 -9.001  -2.489  0.66 13.68 ?  136 PRO   A O    1 
ATOM   2922 O  O    B PRO   A 1 136 ? 12.505 -8.782  -2.299  0.34 12.72 ?  136 PRO   A O    1 
ATOM   2923 C  CB   A PRO   A 1 136 ? 11.574 -5.910  -2.847  0.66 16.40 ?  136 PRO   A CB   1 
ATOM   2924 C  CB   B PRO   A 1 136 ? 11.775 -5.668  -2.598  0.34 14.11 ?  136 PRO   A CB   1 
ATOM   2925 C  CG   A PRO   A 1 136 ? 10.530 -5.400  -3.793  0.66 17.17 ?  136 PRO   A CG   1 
ATOM   2926 C  CG   B PRO   A 1 136 ? 10.807 -4.972  -3.503  0.34 14.62 ?  136 PRO   A CG   1 
ATOM   2927 C  CD   A PRO   A 1 136 ? 11.153 -5.432  -5.154  0.66 16.13 ?  136 PRO   A CD   1 
ATOM   2928 C  CD   B PRO   A 1 136 ? 11.411 -4.993  -4.860  0.34 13.71 ?  136 PRO   A CD   1 
ATOM   2929 H  HA   A PRO   A 1 136 ? 13.320 -6.835  -3.449  0.66 18.24 ?  136 PRO   A HA   1 
ATOM   2930 H  HA   B PRO   A 1 136 ? 13.423 -6.676  -3.307  0.34 16.30 ?  136 PRO   A HA   1 
ATOM   2931 H  HB2  A PRO   A 1 136 ? 11.164 -6.350  -2.085  0.66 19.69 ?  136 PRO   A HB2  1 
ATOM   2932 H  HB2  B PRO   A 1 136 ? 11.308 -6.106  -1.872  0.34 16.94 ?  136 PRO   A HB2  1 
ATOM   2933 H  HB3  A PRO   A 1 136 ? 12.161 -5.195  -2.556  0.66 19.69 ?  136 PRO   A HB3  1 
ATOM   2934 H  HB3  B PRO   A 1 136 ? 12.431 -5.038  -2.255  0.34 16.94 ?  136 PRO   A HB3  1 
ATOM   2935 H  HG2  A PRO   A 1 136 ? 9.755  -5.977  -3.762  0.66 20.61 ?  136 PRO   A HG2  1 
ATOM   2936 H  HG2  B PRO   A 1 136 ? 9.969  -5.457  -3.514  0.34 17.56 ?  136 PRO   A HG2  1 
ATOM   2937 H  HG3  A PRO   A 1 136 ? 10.295 -4.492  -3.553  0.66 20.61 ?  136 PRO   A HG3  1 
ATOM   2938 H  HG3  B PRO   A 1 136 ? 10.673 -4.060  -3.204  0.34 17.56 ?  136 PRO   A HG3  1 
ATOM   2939 H  HD2  A PRO   A 1 136 ? 10.479 -5.639  -5.826  0.66 19.36 ?  136 PRO   A HD2  1 
ATOM   2940 H  HD2  B PRO   A 1 136 ? 10.712 -5.034  -5.534  0.34 16.45 ?  136 PRO   A HD2  1 
ATOM   2941 H  HD3  A PRO   A 1 136 ? 11.599 -4.594  -5.348  0.66 19.36 ?  136 PRO   A HD3  1 
ATOM   2942 H  HD3  B PRO   A 1 136 ? 11.986 -4.221  -4.992  0.34 16.45 ?  136 PRO   A HD3  1 
ATOM   2943 N  N    A ILE   A 1 137 ? 10.906 -8.869  -3.991  0.66 14.46 ?  137 ILE   A N    1 
ATOM   2944 N  N    B ILE   A 1 137 ? 10.983 -8.618  -3.950  0.34 13.61 ?  137 ILE   A N    1 
ATOM   2945 C  CA   A ILE   A 1 137 ? 10.535 -10.270 -3.804  0.66 14.66 ?  137 ILE   A CA   1 
ATOM   2946 C  CA   B ILE   A 1 137 ? 10.546 -10.005 -3.786  0.34 14.57 ?  137 ILE   A CA   1 
ATOM   2947 C  C    A ILE   A 1 137 ? 11.688 -11.176 -4.218  0.66 13.95 ?  137 ILE   A C    1 
ATOM   2948 C  C    B ILE   A 1 137 ? 11.680 -10.955 -4.154  0.34 14.72 ?  137 ILE   A C    1 
ATOM   2949 O  O    A ILE   A 1 137 ? 12.006 -12.163 -3.540  0.66 13.57 ?  137 ILE   A O    1 
ATOM   2950 O  O    B ILE   A 1 137 ? 11.981 -11.912 -3.428  0.34 15.12 ?  137 ILE   A O    1 
ATOM   2951 C  CB   A ILE   A 1 137 ? 9.240  -10.592 -4.575  0.66 16.06 ?  137 ILE   A CB   1 
ATOM   2952 C  CB   B ILE   A 1 137 ? 9.292  -10.278 -4.637  0.34 15.57 ?  137 ILE   A CB   1 
ATOM   2953 C  CG1  A ILE   A 1 137 ? 8.061  -9.786  -4.010  0.66 18.11 ?  137 ILE   A CG1  1 
ATOM   2954 C  CG1  B ILE   A 1 137 ? 8.182  -9.271  -4.331  0.34 16.66 ?  137 ILE   A CG1  1 
ATOM   2955 C  CG2  A ILE   A 1 137 ? 8.950  -12.094 -4.535  0.66 16.27 ?  137 ILE   A CG2  1 
ATOM   2956 C  CG2  B ILE   A 1 137 ? 8.800  -11.710 -4.417  0.34 15.91 ?  137 ILE   A CG2  1 
ATOM   2957 C  CD1  A ILE   A 1 137 ? 6.774  -9.937  -4.793  0.66 19.46 ?  137 ILE   A CD1  1 
ATOM   2958 C  CD1  B ILE   A 1 137 ? 6.977  -9.448  -5.215  0.34 17.59 ?  137 ILE   A CD1  1 
ATOM   2959 H  H    A ILE   A 1 137 ? 10.397 -8.430  -4.528  0.66 17.36 ?  137 ILE   A H    1 
ATOM   2960 H  H    B ILE   A 1 137 ? 10.550 -8.169  -4.542  0.34 16.34 ?  137 ILE   A H    1 
ATOM   2961 H  HA   A ILE   A 1 137 ? 10.367 -10.429 -2.866  0.66 17.60 ?  137 ILE   A HA   1 
ATOM   2962 H  HA   B ILE   A 1 137 ? 10.314 -10.154 -2.855  0.34 17.49 ?  137 ILE   A HA   1 
ATOM   2963 H  HB   A ILE   A 1 137 ? 9.362  -10.334 -5.499  0.66 19.28 ?  137 ILE   A HB   1 
ATOM   2964 H  HB   B ILE   A 1 137 ? 9.534  -10.182 -5.569  0.34 18.69 ?  137 ILE   A HB   1 
ATOM   2965 H  HG12 A ILE   A 1 137 ? 7.893  -10.071 -3.100  0.66 21.74 ?  137 ILE   A HG12 1 
ATOM   2966 H  HG12 B ILE   A 1 137 ? 7.899  -9.380  -3.411  0.34 20.00 ?  137 ILE   A HG12 1 
ATOM   2967 H  HG13 A ILE   A 1 137 ? 8.301  -8.842  -4.016  0.66 21.74 ?  137 ILE   A HG13 1 
ATOM   2968 H  HG13 B ILE   A 1 137 ? 8.517  -8.371  -4.471  0.34 20.00 ?  137 ILE   A HG13 1 
ATOM   2969 H  HG21 A ILE   A 1 137 ? 8.118  -12.275 -4.998  0.66 19.53 ?  137 ILE   A HG21 1 
ATOM   2970 H  HG21 B ILE   A 1 137 ? 8.003  -11.862 -4.949  0.34 19.10 ?  137 ILE   A HG21 1 
ATOM   2971 H  HG22 A ILE   A 1 137 ? 9.666  -12.569 -4.977  0.66 19.53 ?  137 ILE   A HG22 1 
ATOM   2972 H  HG22 B ILE   A 1 137 ? 9.494  -12.329 -4.690  0.34 19.10 ?  137 ILE   A HG22 1 
ATOM   2973 H  HG23 A ILE   A 1 137 ? 8.881  -12.374 -3.611  0.66 19.53 ?  137 ILE   A HG23 1 
ATOM   2974 H  HG23 B ILE   A 1 137 ? 8.598  -11.832 -3.477  0.34 19.10 ?  137 ILE   A HG23 1 
ATOM   2975 H  HD11 A ILE   A 1 137 ? 6.059  -9.563  -4.262  0.66 23.36 ?  137 ILE   A HD11 1 
ATOM   2976 H  HD11 B ILE   A 1 137 ? 6.682  -8.580  -5.519  0.34 21.12 ?  137 ILE   A HD11 1 
ATOM   2977 H  HD12 A ILE   A 1 137 ? 6.852  -9.459  -5.635  0.66 23.36 ?  137 ILE   A HD12 1 
ATOM   2978 H  HD12 B ILE   A 1 137 ? 7.225  -9.998  -5.977  0.34 21.12 ?  137 ILE   A HD12 1 
ATOM   2979 H  HD13 A ILE   A 1 137 ? 6.592  -10.874 -4.959  0.66 23.36 ?  137 ILE   A HD13 1 
ATOM   2980 H  HD13 B ILE   A 1 137 ? 6.276  -9.886  -4.708  0.34 21.12 ?  137 ILE   A HD13 1 
ATOM   2981 N  N    A HIS   A 1 138 ? 12.326 -10.857 -5.345  0.66 14.22 ?  138 HIS   A N    1 
ATOM   2982 N  N    B HIS   A 1 138 ? 12.313 -10.711 -5.303  0.34 14.76 ?  138 HIS   A N    1 
ATOM   2983 C  CA   A HIS   A 1 138 ? 13.505 -11.603 -5.764  0.66 13.95 ?  138 HIS   A CA   1 
ATOM   2984 C  CA   B HIS   A 1 138 ? 13.433 -11.541 -5.732  0.34 14.42 ?  138 HIS   A CA   1 
ATOM   2985 C  C    A HIS   A 1 138 ? 14.644 -11.453 -4.760  0.66 13.29 ?  138 HIS   A C    1 
ATOM   2986 C  C    B HIS   A 1 138 ? 14.597 -11.442 -4.755  0.34 13.59 ?  138 HIS   A C    1 
ATOM   2987 O  O    A HIS   A 1 138 ? 15.317 -12.435 -4.423  0.66 13.81 ?  138 HIS   A O    1 
ATOM   2988 O  O    B HIS   A 1 138 ? 15.239 -12.449 -4.434  0.34 13.96 ?  138 HIS   A O    1 
ATOM   2989 C  CB   A HIS   A 1 138 ? 13.932 -11.144 -7.155  0.66 14.73 ?  138 HIS   A CB   1 
ATOM   2990 C  CB   B HIS   A 1 138 ? 13.861 -11.119 -7.137  0.34 14.86 ?  138 HIS   A CB   1 
ATOM   2991 C  CG   A HIS   A 1 138 ? 15.195 -11.784 -7.627  0.66 16.33 ?  138 HIS   A CG   1 
ATOM   2992 C  CG   B HIS   A 1 138 ? 15.109 -11.791 -7.616  0.34 15.67 ?  138 HIS   A CG   1 
ATOM   2993 N  ND1  A HIS   A 1 138 ? 15.305 -13.141 -7.849  0.66 17.60 ?  138 HIS   A ND1  1 
ATOM   2994 N  ND1  B HIS   A 1 138 ? 15.172 -13.141 -7.889  0.34 16.37 ?  138 HIS   A ND1  1 
ATOM   2995 C  CD2  A HIS   A 1 138 ? 16.410 -11.256 -7.902  0.66 16.87 ?  138 HIS   A CD2  1 
ATOM   2996 C  CD2  B HIS   A 1 138 ? 16.343 -11.297 -7.872  0.34 15.92 ?  138 HIS   A CD2  1 
ATOM   2997 C  CE1  A HIS   A 1 138 ? 16.534 -13.417 -8.249  0.66 17.92 ?  138 HIS   A CE1  1 
ATOM   2998 C  CE1  B HIS   A 1 138 ? 16.392 -13.448 -8.292  0.34 16.68 ?  138 HIS   A CE1  1 
ATOM   2999 N  NE2  A HIS   A 1 138 ? 17.225 -12.292 -8.287  0.66 17.42 ?  138 HIS   A NE2  1 
ATOM   3000 N  NE2  B HIS   A 1 138 ? 17.122 -12.348 -8.290  0.34 16.28 ?  138 HIS   A NE2  1 
ATOM   3001 H  H    A HIS   A 1 138 ? 12.091 -10.222 -5.882  0.66 17.07 ?  138 HIS   A H    1 
ATOM   3002 H  H    B HIS   A 1 138 ? 12.110 -10.073 -5.845  0.34 17.71 ?  138 HIS   A H    1 
ATOM   3003 H  HA   A HIS   A 1 138 ? 13.274 -12.542 -5.823  0.66 16.74 ?  138 HIS   A HA   1 
ATOM   3004 H  HA   B HIS   A 1 138 ? 13.144 -12.464 -5.769  0.34 17.31 ?  138 HIS   A HA   1 
ATOM   3005 H  HB2  A HIS   A 1 138 ? 13.226 -11.368 -7.790  0.66 17.69 ?  138 HIS   A HB2  1 
ATOM   3006 H  HB2  B HIS   A 1 138 ? 13.148 -11.339 -7.761  0.34 17.83 ?  138 HIS   A HB2  1 
ATOM   3007 H  HB3  A HIS   A 1 138 ? 14.067 -10.185 -7.144  0.66 17.69 ?  138 HIS   A HB3  1 
ATOM   3008 H  HB3  B HIS   A 1 138 ? 14.017 -10.162 -7.145  0.34 17.83 ?  138 HIS   A HB3  1 
ATOM   3009 H  HD1  A HIS   A 1 138 ? 14.670 -13.715 -7.748  0.66 21.12 ?  138 HIS   A HD1  1 
ATOM   3010 H  HD1  B HIS   A 1 138 ? 14.520 -13.695 -7.811  0.34 19.65 ?  138 HIS   A HD1  1 
ATOM   3011 H  HD2  A HIS   A 1 138 ? 16.642 -10.358 -7.841  0.66 20.25 ?  138 HIS   A HD2  1 
ATOM   3012 H  HD2  B HIS   A 1 138 ? 16.611 -10.411 -7.781  0.34 19.11 ?  138 HIS   A HD2  1 
ATOM   3013 H  HE1  A HIS   A 1 138 ? 16.856 -14.260 -8.465  0.66 21.51 ?  138 HIS   A HE1  1 
ATOM   3014 H  HE1  B HIS   A 1 138 ? 16.687 -14.296 -8.536  0.34 20.02 ?  138 HIS   A HE1  1 
ATOM   3015 N  N    . SER   A 1 139 ? 14.877 -10.234 -4.266  1.00 12.91 ?  139 SER   A N    1 
ATOM   3016 C  CA   . SER   A 1 139 ? 15.957 -10.048 -3.306  1.00 12.58 ?  139 SER   A CA   1 
ATOM   3017 C  C    . SER   A 1 139 ? 15.740 -10.895 -2.056  1.00 12.18 ?  139 SER   A C    1 
ATOM   3018 O  O    . SER   A 1 139 ? 16.688 -11.491 -1.533  1.00 12.65 ?  139 SER   A O    1 
ATOM   3019 C  CB   . SER   A 1 139 ? 16.085 -8.573  -2.942  1.00 12.80 ?  139 SER   A CB   1 
ATOM   3020 O  OG   . SER   A 1 139 ? 17.176 -8.407  -2.057  1.00 13.23 ?  139 SER   A OG   1 
ATOM   3021 H  H    A SER   A 1 139 ? 14.438 -9.522  -4.465  0.66 15.50 ?  139 SER   A H    1 
ATOM   3022 H  H    B SER   A 1 139 ? 14.453 -9.514  -4.469  0.34 15.50 ?  139 SER   A H    1 
ATOM   3023 H  HA   . SER   A 1 139 ? 16.791 -10.328 -3.714  1.00 15.10 ?  139 SER   A HA   1 
ATOM   3024 H  HB2  . SER   A 1 139 ? 16.237 -8.054  -3.749  1.00 15.37 ?  139 SER   A HB2  1 
ATOM   3025 H  HB3  . SER   A 1 139 ? 15.271 -8.277  -2.503  1.00 15.37 ?  139 SER   A HB3  1 
ATOM   3026 H  HG   . SER   A 1 139 ? 17.261 -7.593  -1.854  1.00 15.88 ?  139 SER   A HG   1 
ATOM   3027 N  N    . LEU   A 1 140 ? 14.502 -10.963 -1.562  1.00 12.55 ?  140 LEU   A N    1 
ATOM   3028 C  CA   . LEU   A 1 140 ? 14.229 -11.785 -0.386  1.00 11.81 ?  140 LEU   A CA   1 
ATOM   3029 C  C    . LEU   A 1 140 ? 14.495 -13.258 -0.671  1.00 12.29 ?  140 LEU   A C    1 
ATOM   3030 O  O    . LEU   A 1 140 ? 15.048 -13.973 0.174   1.00 12.73 ?  140 LEU   A O    1 
ATOM   3031 C  CB   . LEU   A 1 140 ? 12.789 -11.564 0.079   1.00 12.27 ?  140 LEU   A CB   1 
ATOM   3032 C  CG   . LEU   A 1 140 ? 12.327 -12.431 1.252   1.00 13.12 ?  140 LEU   A CG   1 
ATOM   3033 C  CD1  . LEU   A 1 140 ? 13.226 -12.264 2.467   1.00 13.95 ?  140 LEU   A CD1  1 
ATOM   3034 C  CD2  . LEU   A 1 140 ? 10.872 -12.113 1.614   1.00 13.84 ?  140 LEU   A CD2  1 
ATOM   3035 H  H    . LEU   A 1 140 ? 13.820 -10.551 -1.885  1.00 15.07 ?  140 LEU   A H    1 
ATOM   3036 H  HA   . LEU   A 1 140 ? 14.817 -11.509 0.329   1.00 14.18 ?  140 LEU   A HA   1 
ATOM   3037 H  HB2  . LEU   A 1 140 ? 12.693 -10.640 0.348   1.00 14.73 ?  140 LEU   A HB2  1 
ATOM   3038 H  HB3  . LEU   A 1 140 ? 12.196 -11.749 -0.666  1.00 14.73 ?  140 LEU   A HB3  1 
ATOM   3039 H  HG   . LEU   A 1 140 ? 12.361 -13.365 0.987   1.00 15.75 ?  140 LEU   A HG   1 
ATOM   3040 H  HD11 . LEU   A 1 140 ? 12.849 -12.761 3.209   1.00 16.75 ?  140 LEU   A HD11 1 
ATOM   3041 H  HD12 . LEU   A 1 140 ? 14.110 -12.612 2.255   1.00 16.75 ?  140 LEU   A HD12 1 
ATOM   3042 H  HD13 . LEU   A 1 140 ? 13.285 -11.325 2.690   1.00 16.75 ?  140 LEU   A HD13 1 
ATOM   3043 H  HD21 . LEU   A 1 140 ? 10.591 -12.688 2.344   1.00 16.61 ?  140 LEU   A HD21 1 
ATOM   3044 H  HD22 . LEU   A 1 140 ? 10.810 -11.182 1.889   1.00 16.61 ?  140 LEU   A HD22 1 
ATOM   3045 H  HD23 . LEU   A 1 140 ? 10.309 -12.265 0.839   1.00 16.61 ?  140 LEU   A HD23 1 
ATOM   3046 N  N    A ARG   A 1 141 ? 14.096 -13.722 -1.858  0.66 12.78 ?  141 ARG   A N    1 
ATOM   3047 N  N    B ARG   A 1 141 ? 14.118 -13.741 -1.858  0.34 12.25 ?  141 ARG   A N    1 
ATOM   3048 C  CA   A ARG   A 1 141 ? 14.344 -15.102 -2.257  0.66 14.20 ?  141 ARG   A CA   1 
ATOM   3049 C  CA   B ARG   A 1 141 ? 14.360 -15.150 -2.158  0.34 12.84 ?  141 ARG   A CA   1 
ATOM   3050 C  C    A ARG   A 1 141 ? 15.837 -15.413 -2.232  0.66 13.33 ?  141 ARG   A C    1 
ATOM   3051 C  C    B ARG   A 1 141 ? 15.852 -15.440 -2.277  0.34 12.80 ?  141 ARG   A C    1 
ATOM   3052 O  O    A ARG   A 1 141 ? 16.270 -16.408 -1.635  0.66 12.88 ?  141 ARG   A O    1 
ATOM   3053 O  O    B ARG   A 1 141 ? 16.319 -16.504 -1.850  0.34 12.73 ?  141 ARG   A O    1 
ATOM   3054 C  CB   A ARG   A 1 141 ? 13.767 -15.312 -3.659  0.66 16.24 ?  141 ARG   A CB   1 
ATOM   3055 C  CB   B ARG   A 1 141 ? 13.620 -15.572 -3.427  0.34 13.36 ?  141 ARG   A CB   1 
ATOM   3056 C  CG   A ARG   A 1 141 ? 13.774 -16.743 -4.154  0.66 18.84 ?  141 ARG   A CG   1 
ATOM   3057 C  CG   B ARG   A 1 141 ? 13.759 -17.062 -3.750  0.34 13.93 ?  141 ARG   A CG   1 
ATOM   3058 C  CD   A ARG   A 1 141 ? 12.727 -17.564 -3.438  0.66 20.34 ?  141 ARG   A CD   1 
ATOM   3059 C  CD   B ARG   A 1 141 ? 13.183 -17.932 -2.643  0.34 14.25 ?  141 ARG   A CD   1 
ATOM   3060 N  NE   A ARG   A 1 141 ? 13.312 -18.379 -2.382  0.66 21.04 ?  141 ARG   A NE   1 
ATOM   3061 N  NE   B ARG   A 1 141 ? 11.763 -17.665 -2.445  0.34 14.66 ?  141 ARG   A NE   1 
ATOM   3062 C  CZ   A ARG   A 1 141 ? 12.616 -18.928 -1.396  0.66 21.13 ?  141 ARG   A CZ   1 
ATOM   3063 C  CZ   B ARG   A 1 141 ? 11.018 -18.202 -1.488  0.34 14.76 ?  141 ARG   A CZ   1 
ATOM   3064 N  NH1  A ARG   A 1 141 ? 11.321 -18.696 -1.251  0.66 21.27 ?  141 ARG   A NH1  1 
ATOM   3065 N  NH1  B ARG   A 1 141 ? 11.524 -19.059 -0.615  0.34 14.64 ?  141 ARG   A NH1  1 
ATOM   3066 N  NH2  A ARG   A 1 141 ? 13.234 -19.724 -0.531  0.66 21.10 ?  141 ARG   A NH2  1 
ATOM   3067 N  NH2  B ARG   A 1 141 ? 9.733  -17.868 -1.403  0.34 15.08 ?  141 ARG   A NH2  1 
ATOM   3068 H  H    A ARG   A 1 141 ? 13.679 -13.254 -2.449  0.66 15.34 ?  141 ARG   A H    1 
ATOM   3069 H  H    B ARG   A 1 141 ? 13.734 -13.292 -2.485  0.34 14.71 ?  141 ARG   A H    1 
ATOM   3070 H  HA   A ARG   A 1 141 ? 13.895 -15.702 -1.645  0.66 17.04 ?  141 ARG   A HA   1 
ATOM   3071 H  HA   B ARG   A 1 141 ? 14.020 -15.678 -1.425  0.34 15.41 ?  141 ARG   A HA   1 
ATOM   3072 H  HB2  A ARG   A 1 141 ? 12.843 -15.006 -3.662  0.66 19.49 ?  141 ARG   A HB2  1 
ATOM   3073 H  HB2  B ARG   A 1 141 ? 12.673 -15.381 -3.317  0.34 16.03 ?  141 ARG   A HB2  1 
ATOM   3074 H  HB3  A ARG   A 1 141 ? 14.280 -14.789 -4.288  0.66 19.49 ?  141 ARG   A HB3  1 
ATOM   3075 H  HB3  B ARG   A 1 141 ? 13.968 -15.070 -4.180  0.34 16.03 ?  141 ARG   A HB3  1 
ATOM   3076 H  HG2  A ARG   A 1 141 ? 13.573 -16.763 -5.103  0.66 22.62 ?  141 ARG   A HG2  1 
ATOM   3077 H  HG2  B ARG   A 1 141 ? 13.278 -17.256 -4.572  0.34 16.72 ?  141 ARG   A HG2  1 
ATOM   3078 H  HG3  A ARG   A 1 141 ? 14.640 -17.146 -3.985  0.66 22.62 ?  141 ARG   A HG3  1 
ATOM   3079 H  HG3  B ARG   A 1 141 ? 14.699 -17.283 -3.859  0.34 16.72 ?  141 ARG   A HG3  1 
ATOM   3080 H  HD2  A ARG   A 1 141 ? 12.076 -16.972 -3.029  0.66 24.41 ?  141 ARG   A HD2  1 
ATOM   3081 H  HD2  B ARG   A 1 141 ? 13.281 -18.862 -2.887  0.34 17.10 ?  141 ARG   A HD2  1 
ATOM   3082 H  HD3  A ARG   A 1 141 ? 12.286 -18.152 -4.074  0.66 24.41 ?  141 ARG   A HD3  1 
ATOM   3083 H  HD3  B ARG   A 1 141 ? 13.646 -17.755 -1.809  0.34 17.10 ?  141 ARG   A HD3  1 
ATOM   3084 H  HE   A ARG   A 1 141 ? 14.138 -18.604 -2.462  0.66 25.25 ?  141 ARG   A HE   1 
ATOM   3085 H  HE   B ARG   A 1 141 ? 11.374 -17.134 -3.002  0.34 17.59 ?  141 ARG   A HE   1 
ATOM   3086 H  HH11 A ARG   A 1 141 ? 10.906 -18.191 -1.807  0.66 25.53 ?  141 ARG   A HH11 1 
ATOM   3087 H  HH11 B ARG   A 1 141 ? 12.351 -19.283 -0.662  0.34 17.58 ?  141 ARG   A HH11 1 
ATOM   3088 H  HH12 A ARG   A 1 141 ? 10.891 -19.060 -0.599  0.66 25.53 ?  141 ARG   A HH12 1 
ATOM   3089 H  HH12 B ARG   A 1 141 ? 11.020 -19.395 -0.006  0.34 17.58 ?  141 ARG   A HH12 1 
ATOM   3090 H  HH21 A ARG   A 1 141 ? 14.076 -19.881 -0.616  0.66 25.33 ?  141 ARG   A HH21 1 
ATOM   3091 H  HH21 B ARG   A 1 141 ? 9.394  -17.311 -1.966  0.34 18.10 ?  141 ARG   A HH21 1 
ATOM   3092 H  HH22 A ARG   A 1 141 ? 12.796 -20.078 0.120   0.66 25.33 ?  141 ARG   A HH22 1 
ATOM   3093 H  HH22 B ARG   A 1 141 ? 9.239  -18.210 -0.788  0.34 18.10 ?  141 ARG   A HH22 1 
ATOM   3094 N  N    A VAL   A 1 142 ? 16.642 -14.567 -2.880  0.66 12.42 ?  142 VAL   A N    1 
ATOM   3095 N  N    B VAL   A 1 142 ? 16.615 -14.512 -2.857  0.34 12.56 ?  142 VAL   A N    1 
ATOM   3096 C  CA   A VAL   A 1 142 ? 18.084 -14.790 -2.892  0.66 12.17 ?  142 VAL   A CA   1 
ATOM   3097 C  CA   B VAL   A 1 142 ? 18.063 -14.691 -2.921  0.34 12.54 ?  142 VAL   A CA   1 
ATOM   3098 C  C    A VAL   A 1 142 ? 18.639 -14.756 -1.475  0.66 11.30 ?  142 VAL   A C    1 
ATOM   3099 C  C    B VAL   A 1 142 ? 18.651 -14.709 -1.517  0.34 11.80 ?  142 VAL   A C    1 
ATOM   3100 O  O    A VAL   A 1 142 ? 19.497 -15.570 -1.112  0.66 12.00 ?  142 VAL   A O    1 
ATOM   3101 O  O    B VAL   A 1 142 ? 19.531 -15.520 -1.202  0.34 12.16 ?  142 VAL   A O    1 
ATOM   3102 C  CB   A VAL   A 1 142 ? 18.794 -13.784 -3.819  0.66 12.31 ?  142 VAL   A CB   1 
ATOM   3103 C  CB   B VAL   A 1 142 ? 18.705 -13.601 -3.801  0.34 12.77 ?  142 VAL   A CB   1 
ATOM   3104 C  CG1  A VAL   A 1 142 ? 20.300 -13.997 -3.765  0.66 12.19 ?  142 VAL   A CG1  1 
ATOM   3105 C  CG1  B VAL   A 1 142 ? 20.214 -13.754 -3.814  0.34 13.03 ?  142 VAL   A CG1  1 
ATOM   3106 C  CG2  A VAL   A 1 142 ? 18.298 -13.928 -5.251  0.66 13.62 ?  142 VAL   A CG2  1 
ATOM   3107 C  CG2  B VAL   A 1 142 ? 18.161 -13.668 -5.218  0.34 13.16 ?  142 VAL   A CG2  1 
ATOM   3108 H  H    A VAL   A 1 142 ? 16.384 -13.868 -3.314  0.66 14.92 ?  142 VAL   A H    1 
ATOM   3109 H  H    B VAL   A 1 142 ? 16.325 -13.781 -3.212  0.34 15.08 ?  142 VAL   A H    1 
ATOM   3110 H  HA   A VAL   A 1 142 ? 18.259 -15.670 -3.249  0.66 14.61 ?  142 VAL   A HA   1 
ATOM   3111 H  HA   B VAL   A 1 142 ? 18.252 -15.544 -3.336  0.34 15.06 ?  142 VAL   A HA   1 
ATOM   3112 H  HB   A VAL   A 1 142 ? 18.608 -12.876 -3.523  0.66 14.78 ?  142 VAL   A HB   1 
ATOM   3113 H  HB   B VAL   A 1 142 ? 18.493 -12.724 -3.437  0.34 15.33 ?  142 VAL   A HB   1 
ATOM   3114 H  HG11 A VAL   A 1 142 ? 20.715 -13.523 -4.507  0.66 14.64 ?  142 VAL   A HG11 1 
ATOM   3115 H  HG11 B VAL   A 1 142 ? 20.582 -13.174 -4.499  0.34 15.65 ?  142 VAL   A HG11 1 
ATOM   3116 H  HG12 A VAL   A 1 142 ? 20.643 -13.645 -2.926  0.66 14.64 ?  142 VAL   A HG12 1 
ATOM   3117 H  HG12 B VAL   A 1 142 ? 20.566 -13.504 -2.946  0.34 15.65 ?  142 VAL   A HG12 1 
ATOM   3118 H  HG13 A VAL   A 1 142 ? 20.489 -14.943 -3.832  0.66 14.64 ?  142 VAL   A HG13 1 
ATOM   3119 H  HG13 B VAL   A 1 142 ? 20.431 -14.677 -4.010  0.34 15.65 ?  142 VAL   A HG13 1 
ATOM   3120 H  HG21 A VAL   A 1 142 ? 18.783 -13.307 -5.820  0.66 16.35 ?  142 VAL   A HG21 1 
ATOM   3121 H  HG21 B VAL   A 1 142 ? 18.536 -12.938 -5.735  0.34 15.80 ?  142 VAL   A HG21 1 
ATOM   3122 H  HG22 A VAL   A 1 142 ? 18.453 -14.837 -5.547  0.66 16.35 ?  142 VAL   A HG22 1 
ATOM   3123 H  HG22 B VAL   A 1 142 ? 18.419 -14.517 -5.610  0.34 15.80 ?  142 VAL   A HG22 1 
ATOM   3124 H  HG23 A VAL   A 1 142 ? 17.350 -13.726 -5.276  0.66 16.35 ?  142 VAL   A HG23 1 
ATOM   3125 H  HG23 B VAL   A 1 142 ? 17.196 -13.595 -5.193  0.34 15.80 ?  142 VAL   A HG23 1 
ATOM   3126 N  N    . CYS   A 1 143 ? 18.177 -13.810 -0.655  1.00 11.45 ?  143 CYS   A N    1 
ATOM   3127 C  CA   . CYS   A 1 143 ? 18.640 -13.762 0.726   1.00 11.69 ?  143 CYS   A CA   1 
ATOM   3128 C  C    . CYS   A 1 143 ? 18.409 -15.101 1.419   1.00 11.86 ?  143 CYS   A C    1 
ATOM   3129 O  O    . CYS   A 1 143 ? 19.328 -15.690 1.997   1.00 12.05 ?  143 CYS   A O    1 
ATOM   3130 C  CB   . CYS   A 1 143 ? 17.913 -12.643 1.470   1.00 12.42 ?  143 CYS   A CB   1 
ATOM   3131 S  SG   . CYS   A 1 143 ? 18.397 -12.480 3.196   1.00 12.77 ?  143 CYS   A SG   1 
ATOM   3132 H  H    A CYS   A 1 143 ? 17.598 -13.211 -0.866  0.66 13.75 ?  143 CYS   A H    1 
ATOM   3133 H  H    B CYS   A 1 143 ? 17.583 -13.220 -0.848  0.34 13.75 ?  143 CYS   A H    1 
ATOM   3134 H  HA   . CYS   A 1 143 ? 19.590 -13.577 0.739   1.00 14.04 ?  143 CYS   A HA   1 
ATOM   3135 H  HB2  . CYS   A 1 143 ? 18.093 -11.804 1.024   1.00 14.91 ?  143 CYS   A HB2  1 
ATOM   3136 H  HB3  . CYS   A 1 143 ? 16.963 -12.826 1.447   1.00 14.91 ?  143 CYS   A HB3  1 
ATOM   3137 H  HG   . CYS   A 1 143 ? 17.815 -11.552 3.673   1.00 15.34 ?  143 CYS   A HG   1 
ATOM   3138 N  N    . VAL   A 1 144 ? 17.179 -15.610 1.354   1.00 12.24 ?  144 VAL   A N    1 
ATOM   3139 C  CA   . VAL   A 1 144 ? 16.834 -16.854 2.040   1.00 13.47 ?  144 VAL   A CA   1 
ATOM   3140 C  C    . VAL   A 1 144 ? 17.660 -18.019 1.516   1.00 13.26 ?  144 VAL   A C    1 
ATOM   3141 O  O    . VAL   A 1 144 ? 18.023 -18.929 2.273   1.00 14.09 ?  144 VAL   A O    1 
ATOM   3142 C  CB   . VAL   A 1 144 ? 15.320 -17.105 1.902   1.00 16.34 ?  144 VAL   A CB   1 
ATOM   3143 C  CG1  . VAL   A 1 144 ? 14.960 -18.543 2.226   1.00 18.47 ?  144 VAL   A CG1  1 
ATOM   3144 C  CG2  . VAL   A 1 144 ? 14.565 -16.118 2.785   1.00 16.51 ?  144 VAL   A CG2  1 
ATOM   3145 H  H    . VAL   A 1 144 ? 16.523 -15.251 0.921   1.00 14.69 ?  144 VAL   A H    1 
ATOM   3146 H  HA   . VAL   A 1 144 ? 17.024 -16.754 2.982   1.00 16.17 ?  144 VAL   A HA   1 
ATOM   3147 H  HB   . VAL   A 1 144 ? 15.053 -16.931 0.982   1.00 19.61 ?  144 VAL   A HB   1 
ATOM   3148 H  HG11 . VAL   A 1 144 ? 14.002 -18.601 2.376   1.00 22.17 ?  144 VAL   A HG11 1 
ATOM   3149 H  HG12 . VAL   A 1 144 ? 15.209 -19.109 1.480   1.00 22.17 ?  144 VAL   A HG12 1 
ATOM   3150 H  HG13 . VAL   A 1 144 ? 15.435 -18.813 3.026   1.00 22.17 ?  144 VAL   A HG13 1 
ATOM   3151 H  HG21 . VAL   A 1 144 ? 13.609 -16.220 2.642   1.00 19.82 ?  144 VAL   A HG21 1 
ATOM   3152 H  HG22 . VAL   A 1 144 ? 14.778 -16.291 3.715   1.00 19.82 ?  144 VAL   A HG22 1 
ATOM   3153 H  HG23 . VAL   A 1 144 ? 14.830 -15.209 2.552   1.00 19.82 ?  144 VAL   A HG23 1 
ATOM   3154 N  N    . ASP   A 1 145 ? 17.933 -18.038 0.216   1.00 13.48 ?  145 ASP   A N    1 
ATOM   3155 C  CA   . ASP   A 1 145 ? 18.647 -19.141 -0.416  1.00 13.71 ?  145 ASP   A CA   1 
ATOM   3156 C  C    . ASP   A 1 145 ? 20.166 -18.987 -0.366  1.00 14.02 ?  145 ASP   A C    1 
ATOM   3157 O  O    . ASP   A 1 145 ? 20.877 -19.876 -0.853  1.00 16.08 ?  145 ASP   A O    1 
ATOM   3158 C  CB   . ASP   A 1 145 ? 18.206 -19.268 -1.877  1.00 15.29 ?  145 ASP   A CB   1 
ATOM   3159 C  CG   . ASP   A 1 145 ? 16.771 -19.744 -2.021  1.00 17.38 ?  145 ASP   A CG   1 
ATOM   3160 O  OD1  . ASP   A 1 145 ? 16.201 -20.283 -1.046  1.00 18.70 ?  145 ASP   A OD1  1 
ATOM   3161 O  OD2  . ASP   A 1 145 ? 16.224 -19.574 -3.127  1.00 19.19 -1 145 ASP   A OD2  1 
ATOM   3162 H  H    . ASP   A 1 145 ? 17.692 -17.422 -0.336  1.00 16.19 ?  145 ASP   A H    1 
ATOM   3163 H  HA   . ASP   A 1 145 ? 18.416 -19.966 0.035   1.00 16.46 ?  145 ASP   A HA   1 
ATOM   3164 H  HB2  . ASP   A 1 145 ? 18.284 -18.399 -2.306  1.00 18.35 ?  145 ASP   A HB2  1 
ATOM   3165 H  HB3  . ASP   A 1 145 ? 18.781 -19.909 -2.323  1.00 18.35 ?  145 ASP   A HB3  1 
ATOM   3166 N  N    . THR   A 1 146 ? 20.685 -17.896 0.199   1.00 12.29 ?  146 THR   A N    1 
ATOM   3167 C  CA   . THR   A 1 146 ? 22.121 -17.628 0.207   1.00 12.00 ?  146 THR   A CA   1 
ATOM   3168 C  C    . THR   A 1 146 ? 22.677 -17.449 1.607   1.00 11.99 ?  146 THR   A C    1 
ATOM   3169 O  O    . THR   A 1 146 ? 23.755 -17.981 1.914   1.00 13.00 ?  146 THR   A O    1 
ATOM   3170 C  CB   . THR   A 1 146 ? 22.435 -16.377 -0.631  1.00 12.22 ?  146 THR   A CB   1 
ATOM   3171 O  OG1  . THR   A 1 146 ? 21.920 -16.548 -1.951  1.00 12.57 ?  146 THR   A OG1  1 
ATOM   3172 C  CG2  . THR   A 1 146 ? 23.941 -16.129 -0.699  1.00 13.00 ?  146 THR   A CG2  1 
ATOM   3173 H  H    . THR   A 1 146 ? 20.218 -17.283 0.588   1.00 14.75 ?  146 THR   A H    1 
ATOM   3174 H  HA   . THR   A 1 146 ? 22.585 -18.372 -0.194  1.00 14.41 ?  146 THR   A HA   1 
ATOM   3175 H  HB   . THR   A 1 146 ? 22.025 -15.598 -0.224  1.00 14.67 ?  146 THR   A HB   1 
ATOM   3176 H  HG1  . THR   A 1 146 ? 21.088 -16.634 -1.922  1.00 15.09 ?  146 THR   A HG1  1 
ATOM   3177 H  HG21 . THR   A 1 146 ? 24.138 -15.470 -1.384  1.00 15.61 ?  146 THR   A HG21 1 
ATOM   3178 H  HG22 . THR   A 1 146 ? 24.263 -15.796 0.155   1.00 15.61 ?  146 THR   A HG22 1 
ATOM   3179 H  HG23 . THR   A 1 146 ? 24.403 -16.952 -0.912  1.00 15.61 ?  146 THR   A HG23 1 
ATOM   3180 N  N    . VAL   A 1 147 ? 22.002 -16.670 2.444   1.00 11.45 ?  147 VAL   A N    1 
ATOM   3181 C  CA   . VAL   A 1 147 ? 22.490 -16.368 3.781   1.00 11.66 ?  147 VAL   A CA   1 
ATOM   3182 C  C    . VAL   A 1 147 ? 22.180 -17.537 4.704   1.00 12.38 ?  147 VAL   A C    1 
ATOM   3183 O  O    . VAL   A 1 147 ? 21.038 -18.019 4.762   1.00 13.00 ?  147 VAL   A O    1 
ATOM   3184 C  CB   . VAL   A 1 147 ? 21.866 -15.062 4.300   1.00 11.92 ?  147 VAL   A CB   1 
ATOM   3185 C  CG1  . VAL   A 1 147 ? 22.398 -14.756 5.679   1.00 13.20 ?  147 VAL   A CG1  1 
ATOM   3186 C  CG2  . VAL   A 1 147 ? 22.127 -13.910 3.330   1.00 11.88 ?  147 VAL   A CG2  1 
ATOM   3187 H  H    . VAL   A 1 147 ? 21.242 -16.296 2.261   1.00 13.74 ?  147 VAL   A H    1 
ATOM   3188 H  HA   . VAL   A 1 147 ? 23.451 -16.250 3.748   1.00 14.00 ?  147 VAL   A HA   1 
ATOM   3189 H  HB   . VAL   A 1 147 ? 20.908 -15.179 4.374   1.00 14.31 ?  147 VAL   A HB   1 
ATOM   3190 H  HG11 . VAL   A 1 147 ? 22.166 -13.846 5.913   1.00 15.85 ?  147 VAL   A HG11 1 
ATOM   3191 H  HG12 . VAL   A 1 147 ? 21.997 -15.372 6.317   1.00 15.85 ?  147 VAL   A HG12 1 
ATOM   3192 H  HG13 . VAL   A 1 147 ? 23.361 -14.864 5.679   1.00 15.85 ?  147 VAL   A HG13 1 
ATOM   3193 H  HG21 . VAL   A 1 147 ? 21.792 -13.088 3.725   1.00 14.26 ?  147 VAL   A HG21 1 
ATOM   3194 H  HG22 . VAL   A 1 147 ? 23.076 -13.841 3.169   1.00 14.26 ?  147 VAL   A HG22 1 
ATOM   3195 H  HG23 . VAL   A 1 147 ? 21.657 -14.090 2.500   1.00 14.26 ?  147 VAL   A HG23 1 
ATOM   3196 N  N    . ARG   A 1 148 ? 23.206 -17.995 5.424   1.00 12.70 ?  148 ARG   A N    1 
ATOM   3197 C  CA   . ARG   A 1 148 ? 23.080 -19.076 6.388   1.00 12.52 ?  148 ARG   A CA   1 
ATOM   3198 C  C    . ARG   A 1 148 ? 23.216 -18.605 7.824   1.00 13.27 ?  148 ARG   A C    1 
ATOM   3199 O  O    . ARG   A 1 148 ? 22.816 -19.332 8.746   1.00 14.73 ?  148 ARG   A O    1 
ATOM   3200 C  CB   . ARG   A 1 148 ? 24.127 -20.164 6.110   1.00 13.36 ?  148 ARG   A CB   1 
ATOM   3201 C  CG   . ARG   A 1 148 ? 23.971 -20.796 4.743   1.00 14.62 ?  148 ARG   A CG   1 
ATOM   3202 C  CD   . ARG   A 1 148 ? 25.055 -21.833 4.451   1.00 15.79 ?  148 ARG   A CD   1 
ATOM   3203 N  NE   . ARG   A 1 148 ? 26.394 -21.258 4.476   1.00 15.51 ?  148 ARG   A NE   1 
ATOM   3204 C  CZ   . ARG   A 1 148 ? 26.906 -20.520 3.500   1.00 14.60 ?  148 ARG   A CZ   1 
ATOM   3205 N  NH1  . ARG   A 1 148 ? 26.236 -20.294 2.381   1.00 14.99 ?  148 ARG   A NH1  1 
ATOM   3206 N  NH2  . ARG   A 1 148 ? 28.120 -19.990 3.653   1.00 14.82 ?  148 ARG   A NH2  1 
ATOM   3207 H  H    . ARG   A 1 148 ? 24.006 -17.680 5.359   1.00 15.25 ?  148 ARG   A H    1 
ATOM   3208 H  HA   . ARG   A 1 148 ? 22.206 -19.476 6.293   1.00 15.03 ?  148 ARG   A HA   1 
ATOM   3209 H  HB2  . ARG   A 1 148 ? 25.012 -19.781 6.161   1.00 16.04 ?  148 ARG   A HB2  1 
ATOM   3210 H  HB3  . ARG   A 1 148 ? 24.030 -20.870 6.772   1.00 16.04 ?  148 ARG   A HB3  1 
ATOM   3211 H  HG2  . ARG   A 1 148 ? 23.106 -21.233 4.700   1.00 17.56 ?  148 ARG   A HG2  1 
ATOM   3212 H  HG3  . ARG   A 1 148 ? 24.024 -20.097 4.074   1.00 17.56 ?  148 ARG   A HG3  1 
ATOM   3213 H  HD2  . ARG   A 1 148 ? 25.014 -22.531 5.122   1.00 18.95 ?  148 ARG   A HD2  1 
ATOM   3214 H  HD3  . ARG   A 1 148 ? 24.899 -22.209 3.570   1.00 18.95 ?  148 ARG   A HD3  1 
ATOM   3215 H  HE   . ARG   A 1 148 ? 26.886 -21.410 5.162   1.00 18.62 ?  148 ARG   A HE   1 
ATOM   3216 H  HH11 . ARG   A 1 148 ? 25.451 -20.621 2.271   1.00 18.00 ?  148 ARG   A HH11 1 
ATOM   3217 H  HH12 . ARG   A 1 148 ? 26.586 -19.804 1.762   1.00 18.00 ?  148 ARG   A HH12 1 
ATOM   3218 H  HH21 . ARG   A 1 148 ? 28.561 -20.129 4.376   1.00 17.80 ?  148 ARG   A HH21 1 
ATOM   3219 H  HH22 . ARG   A 1 148 ? 28.462 -19.505 3.028   1.00 17.80 ?  148 ARG   A HH22 1 
ATOM   3220 N  N    . THR   A 1 149 ? 23.763 -17.411 8.029   1.00 13.01 ?  149 THR   A N    1 
ATOM   3221 C  CA   . THR   A 1 149 ? 23.842 -16.815 9.344   1.00 13.12 ?  149 THR   A CA   1 
ATOM   3222 C  C    . THR   A 1 149 ? 22.511 -16.127 9.653   1.00 12.41 ?  149 THR   A C    1 
ATOM   3223 O  O    . THR   A 1 149 ? 21.569 -16.135 8.847   1.00 13.16 ?  149 THR   A O    1 
ATOM   3224 C  CB   . THR   A 1 149 ? 25.035 -15.871 9.394   1.00 13.43 ?  149 THR   A CB   1 
ATOM   3225 O  OG1  . THR   A 1 149 ? 24.897 -14.928 8.326   1.00 13.53 ?  149 THR   A OG1  1 
ATOM   3226 C  CG2  . THR   A 1 149 ? 26.342 -16.659 9.251   1.00 13.91 ?  149 THR   A CG2  1 
ATOM   3227 H  H    . THR   A 1 149 ? 24.106 -16.921 7.408   1.00 15.62 ?  149 THR   A H    1 
ATOM   3228 H  HA   . THR   A 1 149 ? 23.976 -17.516 10.001  1.00 15.75 ?  149 THR   A HA   1 
ATOM   3229 H  HB   . THR   A 1 149 ? 25.039 -15.410 10.245  1.00 16.13 ?  149 THR   A HB   1 
ATOM   3230 H  HG1  . THR   A 1 149 ? 25.543 -14.390 8.335   1.00 16.24 ?  149 THR   A HG1  1 
ATOM   3231 H  HG21 . THR   A 1 149 ? 27.100 -16.059 9.311   1.00 16.69 ?  149 THR   A HG21 1 
ATOM   3232 H  HG22 . THR   A 1 149 ? 26.412 -17.325 9.955   1.00 16.69 ?  149 THR   A HG22 1 
ATOM   3233 H  HG23 . THR   A 1 149 ? 26.369 -17.113 8.391   1.00 16.69 ?  149 THR   A HG23 1 
ATOM   3234 N  N    . ASN   A 1 150 ? 22.396 -15.580 10.856  1.00 12.73 ?  150 ASN   A N    1 
ATOM   3235 C  CA   . ASN   A 1 150 ? 21.115 -15.076 11.347  1.00 13.41 ?  150 ASN   A CA   1 
ATOM   3236 C  C    . ASN   A 1 150 ? 20.925 -13.637 10.888  1.00 12.90 ?  150 ASN   A C    1 
ATOM   3237 O  O    . ASN   A 1 150 ? 21.659 -12.737 11.310  1.00 14.38 ?  150 ASN   A O    1 
ATOM   3238 C  CB   . ASN   A 1 150 ? 21.052 -15.193 12.863  1.00 16.16 ?  150 ASN   A CB   1 
ATOM   3239 C  CG   . ASN   A 1 150 ? 20.943 -16.627 13.315  1.00 20.39 ?  150 ASN   A CG   1 
ATOM   3240 O  OD1  . ASN   A 1 150 ? 20.332 -17.449 12.635  1.00 21.57 ?  150 ASN   A OD1  1 
ATOM   3241 N  ND2  . ASN   A 1 150 ? 21.550 -16.945 14.453  1.00 23.15 ?  150 ASN   A ND2  1 
ATOM   3242 H  H    . ASN   A 1 150 ? 23.050 -15.482 11.411  1.00 15.28 ?  150 ASN   A H    1 
ATOM   3243 H  HA   . ASN   A 1 150 ? 20.399 -15.610 10.973  1.00 16.10 ?  150 ASN   A HA   1 
ATOM   3244 H  HB2  . ASN   A 1 150 ? 21.857 -14.820 13.250  1.00 19.39 ?  150 ASN   A HB2  1 
ATOM   3245 H  HB3  . ASN   A 1 150 ? 20.271 -14.718 13.190  1.00 19.39 ?  150 ASN   A HB3  1 
ATOM   3246 H  HD21 . ASN   A 1 150 ? 21.518 -17.754 14.753  1.00 27.79 ?  150 ASN   A HD21 1 
ATOM   3247 H  HD22 . ASN   A 1 150 ? 21.972 -16.343 14.900  1.00 27.79 ?  150 ASN   A HD22 1 
ATOM   3248 N  N    . VAL   A 1 151 ? 19.942 -13.413 10.026  1.00 12.62 ?  151 VAL   A N    1 
ATOM   3249 C  CA   . VAL   A 1 151 ? 19.726 -12.106 9.428   1.00 12.50 ?  151 VAL   A CA   1 
ATOM   3250 C  C    . VAL   A 1 151 ? 18.339 -11.593 9.793   1.00 12.05 ?  151 VAL   A C    1 
ATOM   3251 O  O    . VAL   A 1 151 ? 17.332 -12.304 9.646   1.00 13.61 ?  151 VAL   A O    1 
ATOM   3252 C  CB   . VAL   A 1 151 ? 20.010 -12.094 7.910   1.00 13.80 ?  151 VAL   A CB   1 
ATOM   3253 C  CG1  . VAL   A 1 151 ? 19.166 -13.105 7.164   1.00 14.93 ?  151 VAL   A CG1  1 
ATOM   3254 C  CG2  . VAL   A 1 151 ? 19.825 -10.689 7.339   1.00 14.00 ?  151 VAL   A CG2  1 
ATOM   3255 H  H    . VAL   A 1 151 ? 19.382 -14.011 9.769   1.00 15.16 ?  151 VAL   A H    1 
ATOM   3256 H  HA   . VAL   A 1 151 ? 20.365 -11.490 9.823   1.00 15.01 ?  151 VAL   A HA   1 
ATOM   3257 H  HB   . VAL   A 1 151 ? 20.942 -12.342 7.773   1.00 16.57 ?  151 VAL   A HB   1 
ATOM   3258 H  HG11 . VAL   A 1 151 ? 19.358 -13.044 6.214   1.00 17.92 ?  151 VAL   A HG11 1 
ATOM   3259 H  HG12 . VAL   A 1 151 ? 19.380 -13.998 7.484   1.00 17.92 ?  151 VAL   A HG12 1 
ATOM   3260 H  HG13 . VAL   A 1 151 ? 18.227 -12.916 7.322   1.00 17.92 ?  151 VAL   A HG13 1 
ATOM   3261 H  HG21 . VAL   A 1 151 ? 20.146 -10.680 6.422   1.00 16.81 ?  151 VAL   A HG21 1 
ATOM   3262 H  HG22 . VAL   A 1 151 ? 18.886 -10.459 7.364   1.00 16.81 ?  151 VAL   A HG22 1 
ATOM   3263 H  HG23 . VAL   A 1 151 ? 20.339 -10.063 7.872   1.00 16.81 ?  151 VAL   A HG23 1 
ATOM   3264 N  N    . TYR   A 1 152 ? 18.318 -10.353 10.284  1.00 11.95 ?  152 TYR   A N    1 
ATOM   3265 C  CA   . TYR   A 1 152 ? 17.126 -9.621  10.684  1.00 11.70 ?  152 TYR   A CA   1 
ATOM   3266 C  C    . TYR   A 1 152 ? 16.928 -8.517  9.656   1.00 11.54 ?  152 TYR   A C    1 
ATOM   3267 O  O    . TYR   A 1 152 ? 17.705 -7.551  9.612   1.00 12.03 ?  152 TYR   A O    1 
ATOM   3268 C  CB   . TYR   A 1 152 ? 17.335 -9.078  12.098  1.00 12.15 ?  152 TYR   A CB   1 
ATOM   3269 C  CG   . TYR   A 1 152 ? 17.294 -10.211 13.099  1.00 13.63 ?  152 TYR   A CG   1 
ATOM   3270 C  CD1  . TYR   A 1 152 ? 18.427 -10.965 13.383  1.00 15.46 ?  152 TYR   A CD1  1 
ATOM   3271 C  CD2  . TYR   A 1 152 ? 16.108 -10.564 13.721  1.00 14.00 ?  152 TYR   A CD2  1 
ATOM   3272 C  CE1  . TYR   A 1 152 ? 18.385 -12.025 14.268  1.00 17.10 ?  152 TYR   A CE1  1 
ATOM   3273 C  CE2  . TYR   A 1 152 ? 16.054 -11.624 14.613  1.00 15.48 ?  152 TYR   A CE2  1 
ATOM   3274 C  CZ   . TYR   A 1 152 ? 17.198 -12.345 14.883  1.00 17.20 ?  152 TYR   A CZ   1 
ATOM   3275 O  OH   . TYR   A 1 152 ? 17.155 -13.408 15.765  1.00 19.52 ?  152 TYR   A OH   1 
ATOM   3276 H  H    . TYR   A 1 152 ? 19.038 -9.884  10.394  1.00 14.35 ?  152 TYR   A H    1 
ATOM   3277 H  HA   . TYR   A 1 152 ? 16.359 -10.215 10.682  1.00 14.05 ?  152 TYR   A HA   1 
ATOM   3278 H  HB2  . TYR   A 1 152 ? 18.208 -8.658  12.155  1.00 14.58 ?  152 TYR   A HB2  1 
ATOM   3279 H  HB3  . TYR   A 1 152 ? 16.642 -8.443  12.316  1.00 14.58 ?  152 TYR   A HB3  1 
ATOM   3280 H  HD1  . TYR   A 1 152 ? 19.230 -10.747 12.966  1.00 18.56 ?  152 TYR   A HD1  1 
ATOM   3281 H  HD2  . TYR   A 1 152 ? 15.334 -10.079 13.539  1.00 16.81 ?  152 TYR   A HD2  1 
ATOM   3282 H  HE1  . TYR   A 1 152 ? 19.154 -12.514 14.454  1.00 20.53 ?  152 TYR   A HE1  1 
ATOM   3283 H  HE2  . TYR   A 1 152 ? 15.250 -11.843 15.027  1.00 18.58 ?  152 TYR   A HE2  1 
ATOM   3284 H  HH   . TYR   A 1 152 ? 16.373 -13.495 16.070  1.00 23.43 ?  152 TYR   A HH   1 
ATOM   3285 N  N    . LEU   A 1 153 ? 15.922 -8.686  8.804   1.00 11.49 ?  153 LEU   A N    1 
ATOM   3286 C  CA   . LEU   A 1 153 ? 15.661 -7.774  7.700   1.00 11.78 ?  153 LEU   A CA   1 
ATOM   3287 C  C    . LEU   A 1 153 ? 14.661 -6.709  8.111   1.00 12.29 ?  153 LEU   A C    1 
ATOM   3288 O  O    . LEU   A 1 153 ? 13.582 -7.024  8.629   1.00 13.73 ?  153 LEU   A O    1 
ATOM   3289 C  CB   . LEU   A 1 153 ? 15.083 -8.538  6.508   1.00 12.09 ?  153 LEU   A CB   1 
ATOM   3290 C  CG   . LEU   A 1 153 ? 16.013 -9.553  5.848   1.00 12.19 ?  153 LEU   A CG   1 
ATOM   3291 C  CD1  . LEU   A 1 153 ? 15.211 -10.430 4.897   1.00 12.89 ?  153 LEU   A CD1  1 
ATOM   3292 C  CD2  . LEU   A 1 153 ? 17.154 -8.836  5.117   1.00 12.57 ?  153 LEU   A CD2  1 
ATOM   3293 H  H    . LEU   A 1 153 ? 15.358 -9.343  8.851   1.00 13.80 ?  153 LEU   A H    1 
ATOM   3294 H  HA   . LEU   A 1 153 ? 16.489 -7.352  7.442   1.00 14.15 ?  153 LEU   A HA   1 
ATOM   3295 H  HB2  . LEU   A 1 153 ? 14.295 -9.010  6.808   1.00 14.52 ?  153 LEU   A HB2  1 
ATOM   3296 H  HB3  . LEU   A 1 153 ? 14.835 -7.885  5.833   1.00 14.52 ?  153 LEU   A HB3  1 
ATOM   3297 H  HG   . LEU   A 1 153 ? 16.402 -10.117 6.535   1.00 14.63 ?  153 LEU   A HG   1 
ATOM   3298 H  HD11 . LEU   A 1 153 ? 15.794 -11.116 4.539   1.00 15.48 ?  153 LEU   A HD11 1 
ATOM   3299 H  HD12 . LEU   A 1 153 ? 14.481 -10.836 5.386   1.00 15.48 ?  153 LEU   A HD12 1 
ATOM   3300 H  HD13 . LEU   A 1 153 ? 14.865 -9.878  4.179   1.00 15.48 ?  153 LEU   A HD13 1 
ATOM   3301 H  HD21 . LEU   A 1 153 ? 17.705 -9.500  4.677   1.00 15.09 ?  153 LEU   A HD21 1 
ATOM   3302 H  HD22 . LEU   A 1 153 ? 16.774 -8.231  4.463   1.00 15.09 ?  153 LEU   A HD22 1 
ATOM   3303 H  HD23 . LEU   A 1 153 ? 17.681 -8.340  5.762   1.00 15.09 ?  153 LEU   A HD23 1 
ATOM   3304 N  N    A ALA   A 1 154 ? 15.007 -5.452  7.851   0.66 12.14 ?  154 ALA   A N    1 
ATOM   3305 N  N    B ALA   A 1 154 ? 15.020 -5.452  7.876   0.34 11.97 ?  154 ALA   A N    1 
ATOM   3306 C  CA   A ALA   A 1 154 ? 14.126 -4.313  8.085   0.66 12.97 ?  154 ALA   A CA   1 
ATOM   3307 C  CA   B ALA   A 1 154 ? 14.135 -4.322  8.113   0.34 12.24 ?  154 ALA   A CA   1 
ATOM   3308 C  C    A ALA   A 1 154 ? 13.634 -3.789  6.741   0.66 13.23 ?  154 ALA   A C    1 
ATOM   3309 C  C    B ALA   A 1 154 ? 13.564 -3.860  6.781   0.34 12.33 ?  154 ALA   A C    1 
ATOM   3310 O  O    A ALA   A 1 154 ? 14.444 -3.400  5.891   0.66 13.37 ?  154 ALA   A O    1 
ATOM   3311 O  O    B ALA   A 1 154 ? 14.304 -3.712  5.802   0.34 12.38 ?  154 ALA   A O    1 
ATOM   3312 C  CB   A ALA   A 1 154 ? 14.868 -3.204  8.833   0.66 13.35 ?  154 ALA   A CB   1 
ATOM   3313 C  CB   B ALA   A 1 154 ? 14.894 -3.169  8.773   0.34 12.35 ?  154 ALA   A CB   1 
ATOM   3314 H  H    A ALA   A 1 154 ? 15.769 -5.228  7.520   0.66 14.57 ?  154 ALA   A H    1 
ATOM   3315 H  H    B ALA   A 1 154 ? 15.788 -5.225  7.562   0.34 14.38 ?  154 ALA   A H    1 
ATOM   3316 H  HA   A ALA   A 1 154 ? 13.362 -4.586  8.615   0.66 15.57 ?  154 ALA   A HA   1 
ATOM   3317 H  HA   B ALA   A 1 154 ? 13.403 -4.585  8.692   0.34 14.70 ?  154 ALA   A HA   1 
ATOM   3318 H  HB1  A ALA   A 1 154 ? 14.263 -2.458  8.976   0.66 16.03 ?  154 ALA   A HB1  1 
ATOM   3319 H  HB1  B ALA   A 1 154 ? 14.283 -2.429  8.919   0.34 14.83 ?  154 ALA   A HB1  1 
ATOM   3320 H  HB2  A ALA   A 1 154 ? 15.177 -3.547  9.686   0.66 16.03 ?  154 ALA   A HB2  1 
ATOM   3321 H  HB2  B ALA   A 1 154 ? 15.253 -3.473  9.621   0.34 14.83 ?  154 ALA   A HB2  1 
ATOM   3322 H  HB3  A ALA   A 1 154 ? 15.626 -2.914  8.299   0.66 16.03 ?  154 ALA   A HB3  1 
ATOM   3323 H  HB3  B ALA   A 1 154 ? 15.616 -2.890  8.188   0.34 14.83 ?  154 ALA   A HB3  1 
ATOM   3324 N  N    A VAL   A 1 155 ? 12.313 -3.759  6.564   0.66 13.31 ?  155 VAL   A N    1 
ATOM   3325 N  N    B VAL   A 1 155 ? 12.252 -3.637  6.748   0.34 12.61 ?  155 VAL   A N    1 
ATOM   3326 C  CA   A VAL   A 1 155 ? 11.669 -3.268  5.347   0.66 14.13 ?  155 VAL   A CA   1 
ATOM   3327 C  CA   B VAL   A 1 155 ? 11.562 -3.122  5.570   0.34 12.99 ?  155 VAL   A CA   1 
ATOM   3328 C  C    A VAL   A 1 155 ? 10.922 -1.984  5.692   0.66 15.37 ?  155 VAL   A C    1 
ATOM   3329 C  C    B VAL   A 1 155 ? 10.591 -2.059  6.059   0.34 13.33 ?  155 VAL   A C    1 
ATOM   3330 O  O    A VAL   A 1 155 ? 9.991  -1.999  6.505   0.66 15.69 ?  155 VAL   A O    1 
ATOM   3331 O  O    B VAL   A 1 155 ? 9.641  -2.372  6.786   0.34 13.53 ?  155 VAL   A O    1 
ATOM   3332 C  CB   A VAL   A 1 155 ? 10.723 -4.322  4.749   0.66 14.08 ?  155 VAL   A CB   1 
ATOM   3333 C  CB   B VAL   A 1 155 ? 10.818 -4.217  4.792   0.34 13.03 ?  155 VAL   A CB   1 
ATOM   3334 C  CG1  A VAL   A 1 155 ? 9.970  -3.753  3.556   0.66 15.42 ?  155 VAL   A CG1  1 
ATOM   3335 C  CG1  B VAL   A 1 155 ? 10.106 -3.620  3.590   0.34 13.64 ?  155 VAL   A CG1  1 
ATOM   3336 C  CG2  A VAL   A 1 155 ? 11.505 -5.565  4.343   0.66 14.34 ?  155 VAL   A CG2  1 
ATOM   3337 C  CG2  B VAL   A 1 155 ? 11.787 -5.303  4.354   0.34 13.34 ?  155 VAL   A CG2  1 
ATOM   3338 H  H    A VAL   A 1 155 ? 11.753 -4.033  7.158   0.66 15.98 ?  155 VAL   A H    1 
ATOM   3339 H  H    B VAL   A 1 155 ? 11.726 -3.776  7.416   0.34 15.14 ?  155 VAL   A H    1 
ATOM   3340 H  HA   A VAL   A 1 155 ? 12.347 -3.059  4.688   0.66 16.97 ?  155 VAL   A HA   1 
ATOM   3341 H  HA   B VAL   A 1 155 ? 12.200 -2.698  4.982   0.34 15.59 ?  155 VAL   A HA   1 
ATOM   3342 H  HB   A VAL   A 1 155 ? 10.074 -4.585  5.423   0.66 16.90 ?  155 VAL   A HB   1 
ATOM   3343 H  HB   B VAL   A 1 155 ? 10.152 -4.620  5.371   0.34 15.64 ?  155 VAL   A HB   1 
ATOM   3344 H  HG11 A VAL   A 1 155 ? 9.552  -4.482  3.072   0.66 18.51 ?  155 VAL   A HG11 1 
ATOM   3345 H  HG11 B VAL   A 1 155 ? 9.806  -4.341  3.016   0.34 16.37 ?  155 VAL   A HG11 1 
ATOM   3346 H  HG12 A VAL   A 1 155 ? 9.290  -3.137  3.874   0.66 18.51 ?  155 VAL   A HG12 1 
ATOM   3347 H  HG12 B VAL   A 1 155 ? 9.344  -3.103  3.895   0.34 16.37 ?  155 VAL   A HG12 1 
ATOM   3348 H  HG13 A VAL   A 1 155 ? 10.596 -3.289  2.980   0.66 18.51 ?  155 VAL   A HG13 1 
ATOM   3349 H  HG13 B VAL   A 1 155 ? 10.724 -3.049  3.109   0.34 16.37 ?  155 VAL   A HG13 1 
ATOM   3350 H  HG21 A VAL   A 1 155 ? 10.898 -6.209  3.949   0.66 17.22 ?  155 VAL   A HG21 1 
ATOM   3351 H  HG21 B VAL   A 1 155 ? 11.296 -5.986  3.873   0.34 16.01 ?  155 VAL   A HG21 1 
ATOM   3352 H  HG22 A VAL   A 1 155 ? 12.185 -5.313  3.696   0.66 17.22 ?  155 VAL   A HG22 1 
ATOM   3353 H  HG22 B VAL   A 1 155 ? 12.460 -4.911  3.776   0.34 16.01 ?  155 VAL   A HG22 1 
ATOM   3354 H  HG23 A VAL   A 1 155 ? 11.928 -5.947  5.130   0.66 17.22 ?  155 VAL   A HG23 1 
ATOM   3355 H  HG23 B VAL   A 1 155 ? 12.209 -5.689  5.138   0.34 16.01 ?  155 VAL   A HG23 1 
ATOM   3356 N  N    A PHE   A 1 156 ? 11.319 -0.874  5.061   0.66 16.38 ?  156 PHE   A N    1 
ATOM   3357 N  N    B PHE   A 1 156 ? 10.826 -0.803  5.672   0.34 13.34 ?  156 PHE   A N    1 
ATOM   3358 C  CA   A PHE   A 1 156 ? 10.776 0.437   5.423   0.66 18.07 ?  156 PHE   A CA   1 
ATOM   3359 C  CA   B PHE   A 1 156 ? 9.995  0.281   6.183   0.34 13.47 ?  156 PHE   A CA   1 
ATOM   3360 C  C    A PHE   A 1 156 ? 9.305  0.583   5.041   0.66 18.46 ?  156 PHE   A C    1 
ATOM   3361 C  C    B PHE   A 1 156 ? 8.628  0.331   5.507   0.34 14.48 ?  156 PHE   A C    1 
ATOM   3362 O  O    A PHE   A 1 156 ? 8.510  1.134   5.813   0.66 19.69 ?  156 PHE   A O    1 
ATOM   3363 O  O    B PHE   A 1 156 ? 7.609  0.528   6.181   0.34 14.84 ?  156 PHE   A O    1 
ATOM   3364 C  CB   A PHE   A 1 156 ? 11.610 1.535   4.760   0.66 19.42 ?  156 PHE   A CB   1 
ATOM   3365 C  CB   B PHE   A 1 156 ? 10.692 1.631   6.029   0.34 14.09 ?  156 PHE   A CB   1 
ATOM   3366 C  CG   A PHE   A 1 156 ? 11.167 2.934   5.107   0.66 21.16 ?  156 PHE   A CG   1 
ATOM   3367 C  CG   B PHE   A 1 156 ? 9.825  2.780   6.436   0.34 14.70 ?  156 PHE   A CG   1 
ATOM   3368 C  CD1  A PHE   A 1 156 ? 11.137 3.354   6.428   0.66 22.35 ?  156 PHE   A CD1  1 
ATOM   3369 C  CD1  B PHE   A 1 156 ? 9.695  3.119   7.770   0.34 15.20 ?  156 PHE   A CD1  1 
ATOM   3370 C  CD2  A PHE   A 1 156 ? 10.799 3.831   4.116   0.66 22.38 ?  156 PHE   A CD2  1 
ATOM   3371 C  CD2  B PHE   A 1 156 ? 9.104  3.493   5.492   0.34 15.07 ?  156 PHE   A CD2  1 
ATOM   3372 C  CE1  A PHE   A 1 156 ? 10.737 4.637   6.755   0.66 23.58 ?  156 PHE   A CE1  1 
ATOM   3373 C  CE1  B PHE   A 1 156 ? 8.883  4.168   8.156   0.34 15.59 ?  156 PHE   A CE1  1 
ATOM   3374 C  CE2  A PHE   A 1 156 ? 10.399 5.119   4.436   0.66 23.48 ?  156 PHE   A CE2  1 
ATOM   3375 C  CE2  B PHE   A 1 156 ? 8.290  4.544   5.869   0.34 15.11 ?  156 PHE   A CE2  1 
ATOM   3376 C  CZ   A PHE   A 1 156 ? 10.372 5.522   5.757   0.66 24.01 ?  156 PHE   A CZ   1 
ATOM   3377 C  CZ   B PHE   A 1 156 ? 8.175  4.878   7.205   0.34 15.62 ?  156 PHE   A CZ   1 
ATOM   3378 H  H    A PHE   A 1 156 ? 11.902 -0.854  4.429   0.66 19.66 ?  156 PHE   A H    1 
ATOM   3379 H  H    B PHE   A 1 156 ? 11.446 -0.557  5.128   0.34 16.01 ?  156 PHE   A H    1 
ATOM   3380 H  HA   A PHE   A 1 156 ? 10.846 0.553   6.381   0.66 21.69 ?  156 PHE   A HA   1 
ATOM   3381 H  HA   B PHE   A 1 156 ? 9.846  0.140   7.127   0.34 16.17 ?  156 PHE   A HA   1 
ATOM   3382 H  HB2  A PHE   A 1 156 ? 12.534 1.440   5.040   0.66 23.31 ?  156 PHE   A HB2  1 
ATOM   3383 H  HB2  B PHE   A 1 156 ? 11.485 1.642   6.589   0.34 16.91 ?  156 PHE   A HB2  1 
ATOM   3384 H  HB3  A PHE   A 1 156 ? 11.549 1.439   3.796   0.66 23.31 ?  156 PHE   A HB3  1 
ATOM   3385 H  HB3  B PHE   A 1 156 ? 10.942 1.759   5.100   0.34 16.91 ?  156 PHE   A HB3  1 
ATOM   3386 H  HD1  A PHE   A 1 156 ? 11.385 2.758   7.103   0.66 26.82 ?  156 PHE   A HD1  1 
ATOM   3387 H  HD1  B PHE   A 1 156 ? 10.166 2.646   8.414   0.34 18.24 ?  156 PHE   A HD1  1 
ATOM   3388 H  HD2  A PHE   A 1 156 ? 10.819 3.562   3.226   0.66 26.87 ?  156 PHE   A HD2  1 
ATOM   3389 H  HD2  B PHE   A 1 156 ? 9.183  3.278   4.590   0.34 18.09 ?  156 PHE   A HD2  1 
ATOM   3390 H  HE1  A PHE   A 1 156 ? 10.721 4.901   7.648   0.66 28.30 ?  156 PHE   A HE1  1 
ATOM   3391 H  HE1  B PHE   A 1 156 ? 8.805  4.396   9.054   0.34 18.71 ?  156 PHE   A HE1  1 
ATOM   3392 H  HE2  A PHE   A 1 156 ? 10.154 5.707   3.765   0.66 28.18 ?  156 PHE   A HE2  1 
ATOM   3393 H  HE2  B PHE   A 1 156 ? 7.821  5.028   5.224   0.34 18.13 ?  156 PHE   A HE2  1 
ATOM   3394 H  HZ   A PHE   A 1 156 ? 10.103 6.381   5.978   0.66 28.82 ?  156 PHE   A HZ   1 
ATOM   3395 H  HZ   B PHE   A 1 156 ? 7.630  5.591   7.459   0.34 18.75 ?  156 PHE   A HZ   1 
ATOM   3396 N  N    A ASP   A 1 157 ? 8.927  0.114   3.856   0.66 18.47 ?  157 ASP   A N    1 
ATOM   3397 N  N    B ASP   A 1 157 ? 8.586  0.195   4.183   0.34 14.90 ?  157 ASP   A N    1 
ATOM   3398 C  CA   A ASP   A 1 157 ? 7.598  0.353   3.305   0.66 19.11 ?  157 ASP   A CA   1 
ATOM   3399 C  CA   B ASP   A 1 157 ? 7.327  0.309   3.454   0.34 15.84 ?  157 ASP   A CA   1 
ATOM   3400 C  C    A ASP   A 1 157 ? 6.618  -0.709  3.803   0.66 19.05 ?  157 ASP   A C    1 
ATOM   3401 C  C    B ASP   A 1 157 ? 6.378  -0.810  3.862   0.34 16.58 ?  157 ASP   A C    1 
ATOM   3402 O  O    A ASP   A 1 157 ? 6.806  -1.902  3.538   0.66 18.63 ?  157 ASP   A O    1 
ATOM   3403 O  O    B ASP   A 1 157 ? 6.683  -1.995  3.686   0.34 16.59 ?  157 ASP   A O    1 
ATOM   3404 C  CB   A ASP   A 1 157 ? 7.686  0.318   1.782   0.66 20.32 ?  157 ASP   A CB   1 
ATOM   3405 C  CB   B ASP   A 1 157 ? 7.588  0.261   1.948   0.34 16.37 ?  157 ASP   A CB   1 
ATOM   3406 C  CG   A ASP   A 1 157 ? 6.414  0.787   1.119   0.66 22.39 ?  157 ASP   A CG   1 
ATOM   3407 C  CG   B ASP   A 1 157 ? 6.310  0.310   1.133   0.34 17.48 ?  157 ASP   A CG   1 
ATOM   3408 O  OD1  A ASP   A 1 157 ? 6.170  2.007   1.097   0.66 24.11 ?  157 ASP   A OD1  1 
ATOM   3409 O  OD1  B ASP   A 1 157 ? 5.241  0.573   1.718   0.34 18.40 ?  157 ASP   A OD1  1 
ATOM   3410 O  OD2  A ASP   A 1 157 ? 5.647  -0.067  0.629   0.66 22.42 -1 157 ASP   A OD2  1 
ATOM   3411 O  OD2  B ASP   A 1 157 ? 6.371  0.065   -0.091  0.34 18.13 -1 157 ASP   A OD2  1 
ATOM   3412 H  H    A ASP   A 1 157 ? 9.438  -0.349  3.340   0.66 22.17 ?  157 ASP   A H    1 
ATOM   3413 H  H    B ASP   A 1 157 ? 9.271  0.039   3.688   0.34 17.89 ?  157 ASP   A H    1 
ATOM   3414 H  HA   A ASP   A 1 157 ? 7.281  1.228   3.578   0.66 22.94 ?  157 ASP   A HA   1 
ATOM   3415 H  HA   B ASP   A 1 157 ? 6.908  1.158   3.662   0.34 19.02 ?  157 ASP   A HA   1 
ATOM   3416 H  HB2  A ASP   A 1 157 ? 8.437  0.874   1.500   0.66 24.39 ?  157 ASP   A HB2  1 
ATOM   3417 H  HB2  B ASP   A 1 157 ? 8.157  1.009   1.700   0.34 19.65 ?  157 ASP   A HB2  1 
ATOM   3418 H  HB3  A ASP   A 1 157 ? 7.841  -0.598  1.497   0.66 24.39 ?  157 ASP   A HB3  1 
ATOM   3419 H  HB3  B ASP   A 1 157 ? 8.021  -0.574  1.724   0.34 19.65 ?  157 ASP   A HB3  1 
ATOM   3420 N  N    A LYS   A 1 158 ? 5.565  -0.276  4.508   0.66 20.24 ?  158 LYS   A N    1 
ATOM   3421 N  N    B LYS   A 1 158 ? 5.218  -0.426  4.397   0.34 17.74 ?  158 LYS   A N    1 
ATOM   3422 C  CA   A LYS   A 1 158 ? 4.619  -1.226  5.096   0.66 21.21 ?  158 LYS   A CA   1 
ATOM   3423 C  CA   B LYS   A 1 158 ? 4.266  -1.409  4.907   0.34 18.96 ?  158 LYS   A CA   1 
ATOM   3424 C  C    A LYS   A 1 158 ? 3.894  -2.029  4.020   0.66 20.94 ?  158 LYS   A C    1 
ATOM   3425 C  C    B LYS   A 1 158 ? 3.682  -2.258  3.780   0.34 18.95 ?  158 LYS   A C    1 
ATOM   3426 O  O    A LYS   A 1 158 ? 3.697  -3.241  4.167   0.66 20.79 ?  158 LYS   A O    1 
ATOM   3427 O  O    B LYS   A 1 158 ? 3.596  -3.486  3.897   0.34 18.59 ?  158 LYS   A O    1 
ATOM   3428 C  CB   A LYS   A 1 158 ? 3.623  -0.490  6.001   0.66 22.27 ?  158 LYS   A CB   1 
ATOM   3429 C  CB   B LYS   A 1 158 ? 3.165  -0.686  5.684   0.34 20.31 ?  158 LYS   A CB   1 
ATOM   3430 C  CG   A LYS   A 1 158 ? 2.435  -1.334  6.484   0.66 23.90 ?  158 LYS   A CG   1 
ATOM   3431 C  CG   B LYS   A 1 158 ? 2.521  -1.502  6.794   0.34 21.69 ?  158 LYS   A CG   1 
ATOM   3432 C  CD   A LYS   A 1 158 ? 2.869  -2.555  7.303   0.66 24.46 ?  158 LYS   A CD   1 
ATOM   3433 C  CD   B LYS   A 1 158 ? 1.421  -2.399  6.261   0.34 22.48 ?  158 LYS   A CD   1 
ATOM   3434 C  CE   A LYS   A 1 158 ? 1.666  -3.244  7.941   0.66 25.21 ?  158 LYS   A CE   1 
ATOM   3435 C  CE   B LYS   A 1 158 ? 0.598  -2.997  7.388   0.34 22.82 ?  158 LYS   A CE   1 
ATOM   3436 N  NZ   A LYS   A 1 158 ? 1.987  -4.590  8.503   0.66 25.34 ?  158 LYS   A NZ   1 
ATOM   3437 N  NZ   B LYS   A 1 158 ? 1.151  -4.285  7.891   0.34 23.38 ?  158 LYS   A NZ   1 
ATOM   3438 H  H    A LYS   A 1 158 ? 5.386  0.551   4.658   0.66 24.29 ?  158 LYS   A H    1 
ATOM   3439 H  H    B LYS   A 1 158 ? 4.967  0.392   4.485   0.34 21.30 ?  158 LYS   A H    1 
ATOM   3440 H  HA   A LYS   A 1 158 ? 5.111  -1.849  5.654   0.66 25.46 ?  158 LYS   A HA   1 
ATOM   3441 H  HA   B LYS   A 1 158 ? 4.726  -2.003  5.520   0.34 22.76 ?  158 LYS   A HA   1 
ATOM   3442 H  HB2  A LYS   A 1 158 ? 4.096  -0.172  6.790   0.66 26.73 ?  158 LYS   A HB2  1 
ATOM   3443 H  HB2  B LYS   A 1 158 ? 3.545  0.108   6.089   0.34 24.38 ?  158 LYS   A HB2  1 
ATOM   3444 H  HB3  A LYS   A 1 158 ? 3.265  0.270   5.514   0.66 26.73 ?  158 LYS   A HB3  1 
ATOM   3445 H  HB3  B LYS   A 1 158 ? 2.465  -0.432  5.063   0.34 24.38 ?  158 LYS   A HB3  1 
ATOM   3446 H  HG2  A LYS   A 1 158 ? 1.873  -0.784  7.049   0.66 28.69 ?  158 LYS   A HG2  1 
ATOM   3447 H  HG2  B LYS   A 1 158 ? 3.193  -2.062  7.214   0.34 26.04 ?  158 LYS   A HG2  1 
ATOM   3448 H  HG3  A LYS   A 1 158 ? 1.928  -1.645  5.719   0.66 28.69 ?  158 LYS   A HG3  1 
ATOM   3449 H  HG3  B LYS   A 1 158 ? 2.133  -0.898  7.448   0.34 26.04 ?  158 LYS   A HG3  1 
ATOM   3450 H  HD2  A LYS   A 1 158 ? 3.310  -3.192  6.720   0.66 29.35 ?  158 LYS   A HD2  1 
ATOM   3451 H  HD2  B LYS   A 1 158 ? 0.828  -1.880  5.695   0.34 26.98 ?  158 LYS   A HD2  1 
ATOM   3452 H  HD3  A LYS   A 1 158 ? 3.473  -2.270  8.007   0.66 29.35 ?  158 LYS   A HD3  1 
ATOM   3453 H  HD3  B LYS   A 1 158 ? 1.817  -3.126  5.756   0.34 26.98 ?  158 LYS   A HD3  1 
ATOM   3454 H  HE2  A LYS   A 1 158 ? 1.319  -2.688  8.655   0.66 30.26 ?  158 LYS   A HE2  1 
ATOM   3455 H  HE2  B LYS   A 1 158 ? 0.578  -2.370  8.130   0.34 27.39 ?  158 LYS   A HE2  1 
ATOM   3456 H  HE3  A LYS   A 1 158 ? 0.983  -3.358  7.270   0.66 30.26 ?  158 LYS   A HE3  1 
ATOM   3457 H  HE3  B LYS   A 1 158 ? -0.301 -3.157  7.067   0.34 27.39 ?  158 LYS   A HE3  1 
ATOM   3458 H  HZ1  A LYS   A 1 158 ? 1.255  -4.958  8.849   0.66 30.42 ?  158 LYS   A HZ1  1 
ATOM   3459 H  HZ1  B LYS   A 1 158 ? 0.677  -4.566  8.589   0.34 28.07 ?  158 LYS   A HZ1  1 
ATOM   3460 H  HZ2  A LYS   A 1 158 ? 2.297  -5.117  7.856   0.66 30.42 ?  158 LYS   A HZ2  1 
ATOM   3461 H  HZ2  B LYS   A 1 158 ? 1.115  -4.902  7.250   0.34 28.07 ?  158 LYS   A HZ2  1 
ATOM   3462 H  HZ3  A LYS   A 1 158 ? 2.605  -4.519  9.139   0.66 30.42 ?  158 LYS   A HZ3  1 
ATOM   3463 H  HZ3  B LYS   A 1 158 ? 1.998  -4.177  8.141   0.34 28.07 ?  158 LYS   A HZ3  1 
ATOM   3464 N  N    A ASN   A 1 159 ? 3.489  -1.374  2.930   0.66 21.55 ?  159 ASN   A N    1 
ATOM   3465 N  N    B ASN   A 1 159 ? 3.279  -1.624  2.676   0.34 19.85 ?  159 ASN   A N    1 
ATOM   3466 C  CA   A ASN   A 1 159 ? 2.829  -2.101  1.850   0.66 22.01 ?  159 ASN   A CA   1 
ATOM   3467 C  CA   B ASN   A 1 159 ? 2.661  -2.370  1.583   0.34 20.78 ?  159 ASN   A CA   1 
ATOM   3468 C  C    A ASN   A 1 159 ? 3.748  -3.170  1.261   0.66 20.07 ?  159 ASN   A C    1 
ATOM   3469 C  C    B ASN   A 1 159 ? 3.640  -3.367  0.972   0.34 19.31 ?  159 ASN   A C    1 
ATOM   3470 O  O    A ASN   A 1 159 ? 3.314  -4.295  0.992   0.66 19.90 ?  159 ASN   A O    1 
ATOM   3471 O  O    B ASN   A 1 159 ? 3.265  -4.498  0.643   0.34 19.49 ?  159 ASN   A O    1 
ATOM   3472 C  CB   A ASN   A 1 159 ? 2.342  -1.118  0.782   0.66 24.68 ?  159 ASN   A CB   1 
ATOM   3473 C  CB   B ASN   A 1 159 ? 2.125  -1.399  0.528   0.34 23.34 ?  159 ASN   A CB   1 
ATOM   3474 C  CG   A ASN   A 1 159 ? 1.198  -0.250  1.275   0.66 27.24 ?  159 ASN   A CG   1 
ATOM   3475 C  CG   B ASN   A 1 159 ? 1.140  -0.397  1.108   0.34 25.55 ?  159 ASN   A CG   1 
ATOM   3476 O  OD1  A ASN   A 1 159 ? 0.349  -0.711  2.033   0.66 27.82 ?  159 ASN   A OD1  1 
ATOM   3477 O  OD1  B ASN   A 1 159 ? -0.037 -0.706  1.293   0.34 26.23 ?  159 ASN   A OD1  1 
ATOM   3478 N  ND2  A ASN   A 1 159 ? 1.175  1.010   0.853   0.66 28.24 ?  159 ASN   A ND2  1 
ATOM   3479 N  ND2  B ASN   A 1 159 ? 1.620  0.807   1.403   0.34 26.38 ?  159 ASN   A ND2  1 
ATOM   3480 H  H    A ASN   A 1 159 ? 3.587  -0.532  2.799   0.66 25.87 ?  159 ASN   A H    1 
ATOM   3481 H  H    B ASN   A 1 159 ? 3.352  -0.782  2.536   0.34 23.82 ?  159 ASN   A H    1 
ATOM   3482 H  HA   A ASN   A 1 159 ? 2.050  -2.550  2.215   0.66 26.42 ?  159 ASN   A HA   1 
ATOM   3483 H  HA   B ASN   A 1 159 ? 1.911  -2.875  1.929   0.34 24.95 ?  159 ASN   A HA   1 
ATOM   3484 H  HB2  A ASN   A 1 159 ? 3.073  -0.538  0.529   0.66 29.63 ?  159 ASN   A HB2  1 
ATOM   3485 H  HB2  B ASN   A 1 159 ? 2.867  -0.903  0.147   0.34 28.01 ?  159 ASN   A HB2  1 
ATOM   3486 H  HB3  A ASN   A 1 159 ? 2.029  -1.621  0.015   0.66 29.63 ?  159 ASN   A HB3  1 
ATOM   3487 H  HB3  B ASN   A 1 159 ? 1.667  -1.899  -0.164  0.34 28.01 ?  159 ASN   A HB3  1 
ATOM   3488 H  HD21 A ASN   A 1 159 ? 0.553  1.539   1.106   0.66 33.90 ?  159 ASN   A HD21 1 
ATOM   3489 H  HD21 B ASN   A 1 159 ? 1.101  1.410   1.737   0.34 31.67 ?  159 ASN   A HD21 1 
ATOM   3490 H  HD22 A ASN   A 1 159 ? 1.793  1.298   0.334   0.66 33.90 ?  159 ASN   A HD22 1 
ATOM   3491 H  HD22 B ASN   A 1 159 ? 2.448  0.990   1.258   0.34 31.67 ?  159 ASN   A HD22 1 
ATOM   3492 N  N    A LEU   A 1 160 ? 5.029  -2.847  1.080   0.66 18.98 ?  160 LEU   A N    1 
ATOM   3493 N  N    B LEU   A 1 160 ? 4.904  -2.969  0.824   0.34 18.21 ?  160 LEU   A N    1 
ATOM   3494 C  CA   A LEU   A 1 160 ? 5.972  -3.839  0.568   0.66 18.17 ?  160 LEU   A CA   1 
ATOM   3495 C  CA   B LEU   A 1 160 ? 5.918  -3.893  0.332   0.34 17.80 ?  160 LEU   A CA   1 
ATOM   3496 C  C    A LEU   A 1 160 ? 6.184  -4.969  1.568   0.66 17.26 ?  160 LEU   A C    1 
ATOM   3497 C  C    B LEU   A 1 160 ? 6.161  -5.013  1.335   0.34 16.93 ?  160 LEU   A C    1 
ATOM   3498 O  O    A LEU   A 1 160 ? 6.225  -6.146  1.188   0.66 18.19 ?  160 LEU   A O    1 
ATOM   3499 O  O    B LEU   A 1 160 ? 6.222  -6.193  0.964   0.34 17.17 ?  160 LEU   A O    1 
ATOM   3500 C  CB   A LEU   A 1 160 ? 7.304  -3.175  0.229   0.66 18.09 ?  160 LEU   A CB   1 
ATOM   3501 C  CB   B LEU   A 1 160 ? 7.214  -3.136  0.050   0.34 18.11 ?  160 LEU   A CB   1 
ATOM   3502 C  CG   A LEU   A 1 160 ? 8.406  -4.160  -0.167  0.66 18.26 ?  160 LEU   A CG   1 
ATOM   3503 C  CG   B LEU   A 1 160 ? 8.391  -4.024  -0.343  0.34 18.47 ?  160 LEU   A CG   1 
ATOM   3504 C  CD1  A LEU   A 1 160 ? 7.999  -4.900  -1.426  0.66 19.39 ?  160 LEU   A CD1  1 
ATOM   3505 C  CD1  B LEU   A 1 160 ? 8.004  -4.881  -1.531  0.34 18.91 ?  160 LEU   A CD1  1 
ATOM   3506 C  CD2  A LEU   A 1 160 ? 9.733  -3.453  -0.357  0.66 17.70 ?  160 LEU   A CD2  1 
ATOM   3507 C  CD2  B LEU   A 1 160 ? 9.610  -3.176  -0.655  0.34 18.45 ?  160 LEU   A CD2  1 
ATOM   3508 H  H    A LEU   A 1 160 ? 5.373  -2.082  1.260   0.66 22.79 ?  160 LEU   A H    1 
ATOM   3509 H  H    B LEU   A 1 160 ? 5.198  -2.185  1.002   0.34 21.85 ?  160 LEU   A H    1 
ATOM   3510 H  HA   A LEU   A 1 160 ? 5.609  -4.222  -0.244  0.66 21.81 ?  160 LEU   A HA   1 
ATOM   3511 H  HA   B LEU   A 1 160 ? 5.609  -4.290  -0.497  0.34 21.36 ?  160 LEU   A HA   1 
ATOM   3512 H  HB2  A LEU   A 1 160 ? 7.167  -2.561  -0.513  0.66 21.72 ?  160 LEU   A HB2  1 
ATOM   3513 H  HB2  B LEU   A 1 160 ? 7.059  -2.514  -0.680  0.34 21.73 ?  160 LEU   A HB2  1 
ATOM   3514 H  HB3  A LEU   A 1 160 ? 7.612  -2.687  1.007   0.66 21.72 ?  160 LEU   A HB3  1 
ATOM   3515 H  HB3  B LEU   A 1 160 ? 7.469  -2.645  0.847   0.34 21.73 ?  160 LEU   A HB3  1 
ATOM   3516 H  HG   A LEU   A 1 160 ? 8.521  -4.815  0.539   0.66 21.92 ?  160 LEU   A HG   1 
ATOM   3517 H  HG   B LEU   A 1 160 ? 8.616  -4.612  0.396   0.34 22.17 ?  160 LEU   A HG   1 
ATOM   3518 H  HD11 A LEU   A 1 160 ? 8.741  -5.442  -1.721  0.66 23.27 ?  160 LEU   A HD11 1 
ATOM   3519 H  HD11 B LEU   A 1 160 ? 8.761  -5.423  -1.778  0.34 22.70 ?  160 LEU   A HD11 1 
ATOM   3520 H  HD12 A LEU   A 1 160 ? 7.232  -5.464  -1.230  0.66 23.27 ?  160 LEU   A HD12 1 
ATOM   3521 H  HD12 B LEU   A 1 160 ? 7.262  -5.458  -1.287  0.34 22.70 ?  160 LEU   A HD12 1 
ATOM   3522 H  HD13 A LEU   A 1 160 ? 7.764  -4.251  -2.109  0.66 23.27 ?  160 LEU   A HD13 1 
ATOM   3523 H  HD13 B LEU   A 1 160 ? 7.746  -4.302  -2.267  0.34 22.70 ?  160 LEU   A HD13 1 
ATOM   3524 H  HD21 A LEU   A 1 160 ? 10.403 -4.109  -0.605  0.66 21.24 ?  160 LEU   A HD21 1 
ATOM   3525 H  HD21 B LEU   A 1 160 ? 10.349 -3.759  -0.886  0.34 22.15 ?  160 LEU   A HD21 1 
ATOM   3526 H  HD22 A LEU   A 1 160 ? 9.640  -2.792  -1.060  0.66 21.24 ?  160 LEU   A HD22 1 
ATOM   3527 H  HD22 B LEU   A 1 160 ? 9.403  -2.590  -1.399  0.34 22.15 ?  160 LEU   A HD22 1 
ATOM   3528 H  HD23 A LEU   A 1 160 ? 9.982  -3.022  0.475   0.66 21.24 ?  160 LEU   A HD23 1 
ATOM   3529 H  HD23 B LEU   A 1 160 ? 9.835  -2.649  0.129   0.34 22.15 ?  160 LEU   A HD23 1 
ATOM   3530 N  N    A TYR   A 1 161 ? 6.328  -4.629  2.849   0.66 17.02 ?  161 TYR   A N    1 
ATOM   3531 N  N    B TYR   A 1 161 ? 6.304  -4.659  2.614   0.34 16.28 ?  161 TYR   A N    1 
ATOM   3532 C  CA   A TYR   A 1 161 ? 6.465  -5.650  3.880   0.66 16.49 ?  161 TYR   A CA   1 
ATOM   3533 C  CA   B TYR   A 1 161 ? 6.453  -5.674  3.650   0.34 15.73 ?  161 TYR   A CA   1 
ATOM   3534 C  C    A TYR   A 1 161 ? 5.331  -6.670  3.802   0.66 16.93 ?  161 TYR   A C    1 
ATOM   3535 C  C    B TYR   A 1 161 ? 5.301  -6.671  3.601   0.34 15.85 ?  161 TYR   A C    1 
ATOM   3536 O  O    A TYR   A 1 161 ? 5.565  -7.883  3.829   0.66 17.10 ?  161 TYR   A O    1 
ATOM   3537 O  O    B TYR   A 1 161 ? 5.513  -7.888  3.627   0.34 15.31 ?  161 TYR   A O    1 
ATOM   3538 C  CB   A TYR   A 1 161 ? 6.523  -4.997  5.263   0.66 16.58 ?  161 TYR   A CB   1 
ATOM   3539 C  CB   B TYR   A 1 161 ? 6.550  -5.014  5.031   0.34 15.61 ?  161 TYR   A CB   1 
ATOM   3540 C  CG   A TYR   A 1 161 ? 6.424  -6.004  6.377   0.66 16.07 ?  161 TYR   A CG   1 
ATOM   3541 C  CG   B TYR   A 1 161 ? 6.535  -6.020  6.159   0.34 15.44 ?  161 TYR   A CG   1 
ATOM   3542 C  CD1  A TYR   A 1 161 ? 7.548  -6.689  6.816   0.66 16.23 ?  161 TYR   A CD1  1 
ATOM   3543 C  CD1  B TYR   A 1 161 ? 7.709  -6.620  6.593   0.34 15.30 ?  161 TYR   A CD1  1 
ATOM   3544 C  CD2  A TYR   A 1 161 ? 5.203  -6.290  6.976   0.66 16.35 ?  161 TYR   A CD2  1 
ATOM   3545 C  CD2  B TYR   A 1 161 ? 5.344  -6.389  6.774   0.34 15.68 ?  161 TYR   A CD2  1 
ATOM   3546 C  CE1  A TYR   A 1 161 ? 7.461  -7.631  7.821   0.66 16.69 ?  161 TYR   A CE1  1 
ATOM   3547 C  CE1  B TYR   A 1 161 ? 7.698  -7.556  7.612   0.34 15.52 ?  161 TYR   A CE1  1 
ATOM   3548 C  CE2  A TYR   A 1 161 ? 5.108  -7.229  7.983   0.66 16.56 ?  161 TYR   A CE2  1 
ATOM   3549 C  CE2  B TYR   A 1 161 ? 5.325  -7.323  7.793   0.34 15.48 ?  161 TYR   A CE2  1 
ATOM   3550 C  CZ   A TYR   A 1 161 ? 6.240  -7.903  8.402   0.66 17.28 ?  161 TYR   A CZ   1 
ATOM   3551 C  CZ   B TYR   A 1 161 ? 6.506  -7.905  8.208   0.34 15.59 ?  161 TYR   A CZ   1 
ATOM   3552 O  OH   A TYR   A 1 161 ? 6.162  -8.847  9.406   0.66 18.65 ?  161 TYR   A OH   1 
ATOM   3553 O  OH   B TYR   A 1 161 ? 6.501  -8.840  9.220   0.34 15.56 ?  161 TYR   A OH   1 
ATOM   3554 H  H    A TYR   A 1 161 ? 6.343  -3.824  3.143   0.66 20.43 ?  161 TYR   A H    1 
ATOM   3555 H  H    B TYR   A 1 161 ? 6.311  -3.850  2.901   0.34 19.54 ?  161 TYR   A H    1 
ATOM   3556 H  HA   A TYR   A 1 161 ? 7.292  -6.128  3.742   0.66 19.80 ?  161 TYR   A HA   1 
ATOM   3557 H  HA   B TYR   A 1 161 ? 7.275  -6.164  3.499   0.34 18.88 ?  161 TYR   A HA   1 
ATOM   3558 H  HB2  A TYR   A 1 161 ? 7.366  -4.529  5.354   0.66 19.91 ?  161 TYR   A HB2  1 
ATOM   3559 H  HB2  B TYR   A 1 161 ? 7.381  -4.515  5.087   0.34 18.74 ?  161 TYR   A HB2  1 
ATOM   3560 H  HB3  A TYR   A 1 161 ? 5.784  -4.375  5.354   0.66 19.91 ?  161 TYR   A HB3  1 
ATOM   3561 H  HB3  B TYR   A 1 161 ? 5.796  -4.417  5.153   0.34 18.74 ?  161 TYR   A HB3  1 
ATOM   3562 H  HD1  A TYR   A 1 161 ? 8.373  -6.512  6.423   0.66 19.49 ?  161 TYR   A HD1  1 
ATOM   3563 H  HD1  B TYR   A 1 161 ? 8.516  -6.388  6.191   0.34 18.37 ?  161 TYR   A HD1  1 
ATOM   3564 H  HD2  A TYR   A 1 161 ? 4.436  -5.845  6.694   0.66 19.63 ?  161 TYR   A HD2  1 
ATOM   3565 H  HD2  B TYR   A 1 161 ? 4.546  -6.003  6.497   0.34 18.82 ?  161 TYR   A HD2  1 
ATOM   3566 H  HE1  A TYR   A 1 161 ? 8.226  -8.079  8.104   0.66 20.04 ?  161 TYR   A HE1  1 
ATOM   3567 H  HE1  B TYR   A 1 161 ? 8.492  -7.949  7.898   0.34 18.63 ?  161 TYR   A HE1  1 
ATOM   3568 H  HE2  A TYR   A 1 161 ? 4.283  -7.413  8.377   0.66 19.88 ?  161 TYR   A HE2  1 
ATOM   3569 H  HE2  B TYR   A 1 161 ? 4.521  -7.559  8.198   0.34 18.59 ?  161 TYR   A HE2  1 
ATOM   3570 H  HH   A TYR   A 1 161 ? 5.367  -8.912  9.672   0.66 22.39 ?  161 TYR   A HH   1 
ATOM   3571 H  HH   B TYR   A 1 161 ? 7.277  -9.113  9.372   0.34 18.68 ?  161 TYR   A HH   1 
ATOM   3572 N  N    A ASP   A 1 162 ? 4.087  -6.193  3.701   0.66 17.51 ?  162 ASP   A N    1 
ATOM   3573 N  N    B ASP   A 1 162 ? 4.066  -6.169  3.514   0.34 16.59 ?  162 ASP   A N    1 
ATOM   3574 C  CA   A ASP   A 1 162 ? 2.949  -7.111  3.653   0.66 18.44 ?  162 ASP   A CA   1 
ATOM   3575 C  CA   B ASP   A 1 162 ? 2.911  -7.063  3.464   0.34 17.48 ?  162 ASP   A CA   1 
ATOM   3576 C  C    A ASP   A 1 162 ? 2.990  -7.988  2.404   0.66 18.50 ?  162 ASP   A C    1 
ATOM   3577 C  C    B ASP   A 1 162 ? 2.968  -7.970  2.240   0.34 18.47 ?  162 ASP   A C    1 
ATOM   3578 O  O    A ASP   A 1 162 ? 2.621  -9.167  2.454   0.66 18.87 ?  162 ASP   A O    1 
ATOM   3579 O  O    B ASP   A 1 162 ? 2.582  -9.143  2.305   0.34 18.60 ?  162 ASP   A O    1 
ATOM   3580 C  CB   A ASP   A 1 162 ? 1.624  -6.342  3.733   0.66 19.53 ?  162 ASP   A CB   1 
ATOM   3581 C  CB   B ASP   A 1 162 ? 1.610  -6.257  3.468   0.34 17.93 ?  162 ASP   A CB   1 
ATOM   3582 C  CG   A ASP   A 1 162 ? 1.386  -5.706  5.094   0.66 21.28 ?  162 ASP   A CG   1 
ATOM   3583 C  CG   B ASP   A 1 162 ? 1.242  -5.727  4.841   0.34 18.52 ?  162 ASP   A CG   1 
ATOM   3584 O  OD1  A ASP   A 1 162 ? 2.009  -6.137  6.084   0.66 21.76 ?  162 ASP   A OD1  1 
ATOM   3585 O  OD1  B ASP   A 1 162 ? 2.005  -5.946  5.802   0.34 18.77 ?  162 ASP   A OD1  1 
ATOM   3586 O  OD2  A ASP   A 1 162 ? 0.547  -4.778  5.174   0.66 22.81 -1 162 ASP   A OD2  1 
ATOM   3587 O  OD2  B ASP   A 1 162 ? 0.167  -5.097  4.959   0.34 18.54 -1 162 ASP   A OD2  1 
ATOM   3588 H  H    A ASP   A 1 162 ? 3.874  -5.364  3.666   0.66 21.02 ?  162 ASP   A H    1 
ATOM   3589 H  H    B ASP   A 1 162 ? 3.875  -5.331  3.478   0.34 19.92 ?  162 ASP   A H    1 
ATOM   3590 H  HA   A ASP   A 1 162 ? 2.986  -7.705  4.418   0.66 22.13 ?  162 ASP   A HA   1 
ATOM   3591 H  HA   B ASP   A 1 162 ? 2.917  -7.627  4.250   0.34 20.98 ?  162 ASP   A HA   1 
ATOM   3592 H  HB2  A ASP   A 1 162 ? 1.627  -5.630  3.082   0.66 23.44 ?  162 ASP   A HB2  1 
ATOM   3593 H  HB2  B ASP   A 1 162 ? 1.700  -5.506  2.864   0.34 21.53 ?  162 ASP   A HB2  1 
ATOM   3594 H  HB3  A ASP   A 1 162 ? 0.887  -6.954  3.556   0.66 23.44 ?  162 ASP   A HB3  1 
ATOM   3595 H  HB3  B ASP   A 1 162 ? 0.883  -6.830  3.184   0.34 21.53 ?  162 ASP   A HB3  1 
ATOM   3596 N  N    A LYS   A 1 163 ? 3.436  -7.434  1.274   0.66 19.54 ?  163 LYS   A N    1 
ATOM   3597 N  N    B LYS   A 1 163 ? 3.443  -7.439  1.112   0.34 19.85 ?  163 LYS   A N    1 
ATOM   3598 C  CA   A LYS   A 1 163 ? 3.512  -8.219  0.044   0.66 20.15 ?  163 LYS   A CA   1 
ATOM   3599 C  CA   B LYS   A 1 163 ? 3.566  -8.237  -0.104  0.34 20.85 ?  163 LYS   A CA   1 
ATOM   3600 C  C    A LYS   A 1 163 ? 4.611  -9.276  0.120   0.66 19.03 ?  163 LYS   A C    1 
ATOM   3601 C  C    B LYS   A 1 163 ? 4.659  -9.291  0.038   0.34 19.73 ?  163 LYS   A C    1 
ATOM   3602 O  O    A LYS   A 1 163 ? 4.449  -10.389 -0.394  0.66 19.88 ?  163 LYS   A O    1 
ATOM   3603 O  O    B LYS   A 1 163 ? 4.478  -10.443 -0.374  0.34 20.24 ?  163 LYS   A O    1 
ATOM   3604 C  CB   A LYS   A 1 163 ? 3.733  -7.289  -1.148  0.66 23.46 ?  163 LYS   A CB   1 
ATOM   3605 C  CB   B LYS   A 1 163 ? 3.861  -7.297  -1.270  0.34 23.45 ?  163 LYS   A CB   1 
ATOM   3606 C  CG   A LYS   A 1 163 ? 3.783  -7.985  -2.494  0.66 26.99 ?  163 LYS   A CG   1 
ATOM   3607 C  CG   B LYS   A 1 163 ? 3.848  -7.910  -2.650  0.34 25.89 ?  163 LYS   A CG   1 
ATOM   3608 C  CD   A LYS   A 1 163 ? 4.149  -7.003  -3.594  0.66 30.87 ?  163 LYS   A CD   1 
ATOM   3609 C  CD   B LYS   A 1 163 ? 4.062  -6.800  -3.668  0.34 28.27 ?  163 LYS   A CD   1 
ATOM   3610 C  CE   A LYS   A 1 163 ? 4.023  -7.633  -4.971  0.66 33.78 ?  163 LYS   A CE   1 
ATOM   3611 C  CE   B LYS   A 1 163 ? 4.227  -7.324  -5.077  0.34 29.97 ?  163 LYS   A CE   1 
ATOM   3612 N  NZ   A LYS   A 1 163 ? 4.668  -6.802  -6.025  0.66 35.39 ?  163 LYS   A NZ   1 
ATOM   3613 N  NZ   B LYS   A 1 163 ? 5.204  -6.492  -5.835  0.34 30.94 ?  163 LYS   A NZ   1 
ATOM   3614 H  H    A LYS   A 1 163 ? 3.705  -6.622  1.197   0.66 23.46 ?  163 LYS   A H    1 
ATOM   3615 H  H    B LYS   A 1 163 ? 3.697  -6.624  1.023   0.34 23.83 ?  163 LYS   A H    1 
ATOM   3616 H  HA   A LYS   A 1 163 ? 2.670  -8.677  -0.089  0.66 24.19 ?  163 LYS   A HA   1 
ATOM   3617 H  HA   B LYS   A 1 163 ? 2.726  -8.690  -0.280  0.34 25.03 ?  163 LYS   A HA   1 
ATOM   3618 H  HB2  A LYS   A 1 163 ? 3.005  -6.647  -1.178  0.66 28.15 ?  163 LYS   A HB2  1 
ATOM   3619 H  HB2  B LYS   A 1 163 ? 3.197  -6.591  -1.265  0.34 28.14 ?  163 LYS   A HB2  1 
ATOM   3620 H  HB3  A LYS   A 1 163 ? 4.574  -6.822  -1.028  0.66 28.15 ?  163 LYS   A HB3  1 
ATOM   3621 H  HB3  B LYS   A 1 163 ? 4.741  -6.913  -1.136  0.34 28.14 ?  163 LYS   A HB3  1 
ATOM   3622 H  HG2  A LYS   A 1 163 ? 4.455  -8.683  -2.475  0.66 32.40 ?  163 LYS   A HG2  1 
ATOM   3623 H  HG2  B LYS   A 1 163 ? 4.569  -8.555  -2.732  0.34 31.07 ?  163 LYS   A HG2  1 
ATOM   3624 H  HG3  A LYS   A 1 163 ? 2.910  -8.360  -2.695  0.66 32.40 ?  163 LYS   A HG3  1 
ATOM   3625 H  HG3  B LYS   A 1 163 ? 2.989  -8.330  -2.817  0.34 31.07 ?  163 LYS   A HG3  1 
ATOM   3626 H  HD2  A LYS   A 1 163 ? 3.548  -6.240  -3.555  0.66 37.05 ?  163 LYS   A HD2  1 
ATOM   3627 H  HD2  B LYS   A 1 163 ? 3.292  -6.208  -3.655  0.34 33.93 ?  163 LYS   A HD2  1 
ATOM   3628 H  HD3  A LYS   A 1 163 ? 5.066  -6.712  -3.473  0.66 37.05 ?  163 LYS   A HD3  1 
ATOM   3629 H  HD3  B LYS   A 1 163 ? 4.863  -6.307  -3.434  0.34 33.93 ?  163 LYS   A HD3  1 
ATOM   3630 H  HE2  A LYS   A 1 163 ? 4.441  -8.506  -4.969  0.66 40.55 ?  163 LYS   A HE2  1 
ATOM   3631 H  HE2  B LYS   A 1 163 ? 4.549  -8.237  -5.046  0.34 35.97 ?  163 LYS   A HE2  1 
ATOM   3632 H  HE3  A LYS   A 1 163 ? 3.085  -7.719  -5.191  0.66 40.55 ?  163 LYS   A HE3  1 
ATOM   3633 H  HE3  B LYS   A 1 163 ? 3.372  -7.284  -5.535  0.34 35.97 ?  163 LYS   A HE3  1 
ATOM   3634 H  HZ1  A LYS   A 1 163 ? 4.581  -7.197  -6.818  0.66 42.48 ?  163 LYS   A HZ1  1 
ATOM   3635 H  HZ1  B LYS   A 1 163 ? 5.303  -6.812  -6.658  0.34 37.13 ?  163 LYS   A HZ1  1 
ATOM   3636 H  HZ2  A LYS   A 1 163 ? 4.282  -6.001  -6.057  0.66 42.48 ?  163 LYS   A HZ2  1 
ATOM   3637 H  HZ2  B LYS   A 1 163 ? 4.914  -5.651  -5.884  0.34 37.13 ?  163 LYS   A HZ2  1 
ATOM   3638 H  HZ3  A LYS   A 1 163 ? 5.534  -6.699  -5.846  0.66 42.48 ?  163 LYS   A HZ3  1 
ATOM   3639 H  HZ3  B LYS   A 1 163 ? 5.994  -6.500  -5.424  0.34 37.13 ?  163 LYS   A HZ3  1 
ATOM   3640 N  N    A LEU   A 1 164 ? 5.742  -8.941  0.746   0.66 17.13 ?  164 LEU   A N    1 
ATOM   3641 N  N    B LEU   A 1 164 ? 5.799  -8.914  0.621   0.34 18.36 ?  164 LEU   A N    1 
ATOM   3642 C  CA   A LEU   A 1 164 ? 6.838  -9.899  0.880   0.66 16.22 ?  164 LEU   A CA   1 
ATOM   3643 C  CA   B LEU   A 1 164 ? 6.871  -9.874  0.873   0.34 17.28 ?  164 LEU   A CA   1 
ATOM   3644 C  C    A LEU   A 1 164 ? 6.426  -11.089 1.733   0.66 16.00 ?  164 LEU   A C    1 
ATOM   3645 C  C    B LEU   A 1 164 ? 6.383  -10.998 1.774   0.34 16.97 ?  164 LEU   A C    1 
ATOM   3646 O  O    A LEU   A 1 164 ? 6.772  -12.236 1.428   0.66 16.92 ?  164 LEU   A O    1 
ATOM   3647 O  O    B LEU   A 1 164 ? 6.640  -12.179 1.512   0.34 17.41 ?  164 LEU   A O    1 
ATOM   3648 C  CB   A LEU   A 1 164 ? 8.046  -9.208  1.513   0.66 16.41 ?  164 LEU   A CB   1 
ATOM   3649 C  CB   B LEU   A 1 164 ? 8.056  -9.160  1.525   0.34 16.98 ?  164 LEU   A CB   1 
ATOM   3650 C  CG   A LEU   A 1 164 ? 8.738  -8.144  0.655   0.66 16.68 ?  164 LEU   A CG   1 
ATOM   3651 C  CG   B LEU   A 1 164 ? 8.880  -8.206  0.660   0.34 16.64 ?  164 LEU   A CG   1 
ATOM   3652 C  CD1  A LEU   A 1 164 ? 9.679  -7.268  1.481   0.66 16.47 ?  164 LEU   A CD1  1 
ATOM   3653 C  CD1  B LEU   A 1 164 ? 9.668  -7.239  1.534   0.34 16.60 ?  164 LEU   A CD1  1 
ATOM   3654 C  CD2  A LEU   A 1 164 ? 9.488  -8.795  -0.494  0.66 16.84 ?  164 LEU   A CD2  1 
ATOM   3655 C  CD2  B LEU   A 1 164 ? 9.811  -8.989  -0.249  0.34 16.46 ?  164 LEU   A CD2  1 
ATOM   3656 H  H    A LEU   A 1 164 ? 5.905  -8.174  1.090   0.66 20.56 ?  164 LEU   A H    1 
ATOM   3657 H  H    B LEU   A 1 164 ? 5.972  -8.119  0.885   0.34 22.03 ?  164 LEU   A H    1 
ATOM   3658 H  HA   A LEU   A 1 164 ? 7.098  -10.231 0.007   0.66 19.47 ?  164 LEU   A HA   1 
ATOM   3659 H  HA   B LEU   A 1 164 ? 7.169  -10.265 0.037   0.34 20.75 ?  164 LEU   A HA   1 
ATOM   3660 H  HB2  A LEU   A 1 164 ? 7.759  -8.778  2.332   0.66 19.69 ?  164 LEU   A HB2  1 
ATOM   3661 H  HB2  B LEU   A 1 164 ? 7.720  -8.643  2.271   0.34 20.38 ?  164 LEU   A HB2  1 
ATOM   3662 H  HB3  A LEU   A 1 164 ? 8.713  -9.885  1.724   0.66 19.69 ?  164 LEU   A HB3  1 
ATOM   3663 H  HB3  B LEU   A 1 164 ? 8.669  -9.836  1.857   0.34 20.38 ?  164 LEU   A HB3  1 
ATOM   3664 H  HG   A LEU   A 1 164 ? 8.061  -7.566  0.274   0.66 20.02 ?  164 LEU   A HG   1 
ATOM   3665 H  HG   B LEU   A 1 164 ? 8.280  -7.687  0.103   0.34 19.98 ?  164 LEU   A HG   1 
ATOM   3666 H  HD11 A LEU   A 1 164 ? 10.093 -6.610  0.899   0.66 19.77 ?  164 LEU   A HD11 1 
ATOM   3667 H  HD11 B LEU   A 1 164 ? 10.196 -6.657  0.967   0.34 19.92 ?  164 LEU   A HD11 1 
ATOM   3668 H  HD12 A LEU   A 1 164 ? 9.168  -6.819  2.174   0.66 19.77 ?  164 LEU   A HD12 1 
ATOM   3669 H  HD12 B LEU   A 1 164 ? 9.047  -6.711  2.062   0.34 19.92 ?  164 LEU   A HD12 1 
ATOM   3670 H  HD13 A LEU   A 1 164 ? 10.362 -7.826  1.885   0.66 19.77 ?  164 LEU   A HD13 1 
ATOM   3671 H  HD13 B LEU   A 1 164 ? 10.251 -7.746  2.122   0.34 19.92 ?  164 LEU   A HD13 1 
ATOM   3672 H  HD21 A LEU   A 1 164 ? 9.963  -8.107  -0.991  0.66 20.22 ?  164 LEU   A HD21 1 
ATOM   3673 H  HD21 B LEU   A 1 164 ? 10.308 -8.366  -0.803  0.34 19.76 ?  164 LEU   A HD21 1 
ATOM   3674 H  HD22 A LEU   A 1 164 ? 10.119 -9.438  -0.138  0.66 20.22 ?  164 LEU   A HD22 1 
ATOM   3675 H  HD22 B LEU   A 1 164 ? 10.423 -9.508  0.296   0.34 19.76 ?  164 LEU   A HD22 1 
ATOM   3676 H  HD23 A LEU   A 1 164 ? 8.852  -9.239  -1.076  0.66 20.22 ?  164 LEU   A HD23 1 
ATOM   3677 H  HD23 B LEU   A 1 164 ? 9.282  -9.580  -0.808  0.34 19.76 ?  164 LEU   A HD23 1 
ATOM   3678 N  N    A VAL   A 1 165 ? 5.702  -10.828 2.818   0.66 16.04 ?  165 VAL   A N    1 
ATOM   3679 N  N    B VAL   A 1 165 ? 5.686  -10.646 2.853   0.34 16.71 ?  165 VAL   A N    1 
ATOM   3680 C  CA   A VAL   A 1 165 ? 5.259  -11.898 3.703   0.66 15.90 ?  165 VAL   A CA   1 
ATOM   3681 C  CA   B VAL   A 1 165 ? 5.134  -11.664 3.739   0.34 16.63 ?  165 VAL   A CA   1 
ATOM   3682 C  C    A VAL   A 1 165 ? 4.225  -12.771 3.004   0.66 16.01 ?  165 VAL   A C    1 
ATOM   3683 C  C    B VAL   A 1 165 ? 4.046  -12.458 3.023   0.34 16.62 ?  165 VAL   A C    1 
ATOM   3684 O  O    A VAL   A 1 165 ? 4.346  -14.000 2.969   0.66 15.52 ?  165 VAL   A O    1 
ATOM   3685 O  O    B VAL   A 1 165 ? 4.042  -13.694 3.042   0.34 16.66 ?  165 VAL   A O    1 
ATOM   3686 C  CB   A VAL   A 1 165 ? 4.703  -11.294 5.006   0.66 16.67 ?  165 VAL   A CB   1 
ATOM   3687 C  CB   B VAL   A 1 165 ? 4.625  -11.025 5.045   0.34 16.86 ?  165 VAL   A CB   1 
ATOM   3688 C  CG1  A VAL   A 1 165 ? 3.946  -12.349 5.811   0.66 16.98 ?  165 VAL   A CG1  1 
ATOM   3689 C  CG1  B VAL   A 1 165 ? 3.932  -12.066 5.914   0.34 17.11 ?  165 VAL   A CG1  1 
ATOM   3690 C  CG2  A VAL   A 1 165 ? 5.823  -10.657 5.824   0.66 17.30 ?  165 VAL   A CG2  1 
ATOM   3691 C  CG2  B VAL   A 1 165 ? 5.778  -10.375 5.801   0.34 17.34 ?  165 VAL   A CG2  1 
ATOM   3692 H  H    A VAL   A 1 165 ? 5.451  -10.051 3.063   0.66 19.26 ?  165 VAL   A H    1 
ATOM   3693 H  H    B VAL   A 1 165 ? 5.526  -9.833  3.094   0.34 20.06 ?  165 VAL   A H    1 
ATOM   3694 H  HA   A VAL   A 1 165 ? 6.012  -12.465 3.933   0.66 19.09 ?  165 VAL   A HA   1 
ATOM   3695 H  HA   B VAL   A 1 165 ? 5.842  -12.279 3.981   0.34 19.97 ?  165 VAL   A HA   1 
ATOM   3696 H  HB   A VAL   A 1 165 ? 4.071  -10.599 4.777   0.66 20.01 ?  165 VAL   A HB   1 
ATOM   3697 H  HB   B VAL   A 1 165 ? 3.980  -10.332 4.833   0.34 20.24 ?  165 VAL   A HB   1 
ATOM   3698 H  HG11 A VAL   A 1 165 ? 3.856  -12.039 6.725   0.66 20.38 ?  165 VAL   A HG11 1 
ATOM   3699 H  HG11 B VAL   A 1 165 ? 3.822  -11.708 6.809   0.34 20.54 ?  165 VAL   A HG11 1 
ATOM   3700 H  HG12 A VAL   A 1 165 ? 3.065  -12.475 5.420   0.66 20.38 ?  165 VAL   A HG12 1 
ATOM   3701 H  HG12 B VAL   A 1 165 ? 3.064  -12.271 5.533   0.34 20.54 ?  165 VAL   A HG12 1 
ATOM   3702 H  HG13 A VAL   A 1 165 ? 4.442  -13.180 5.790   0.66 20.38 ?  165 VAL   A HG13 1 
ATOM   3703 H  HG13 B VAL   A 1 165 ? 4.480  -12.866 5.944   0.34 20.54 ?  165 VAL   A HG13 1 
ATOM   3704 H  HG21 A VAL   A 1 165 ? 5.448  -10.285 6.638   0.66 20.77 ?  165 VAL   A HG21 1 
ATOM   3705 H  HG21 B VAL   A 1 165 ? 5.442  -10.001 6.631   0.34 20.82 ?  165 VAL   A HG21 1 
ATOM   3706 H  HG22 A VAL   A 1 165 ? 6.482  -11.333 6.042   0.66 20.77 ?  165 VAL   A HG22 1 
ATOM   3707 H  HG22 B VAL   A 1 165 ? 6.451  -11.048 5.991   0.34 20.82 ?  165 VAL   A HG22 1 
ATOM   3708 H  HG23 A VAL   A 1 165 ? 6.233  -9.952  5.297   0.66 20.77 ?  165 VAL   A HG23 1 
ATOM   3709 H  HG23 B VAL   A 1 165 ? 6.161  -9.671  5.254   0.34 20.82 ?  165 VAL   A HG23 1 
ATOM   3710 N  N    A SER   A 1 166 ? 3.195  -12.147 2.431   0.66 16.86 ?  166 SER   A N    1 
ATOM   3711 N  N    B SER   A 1 166 ? 3.116  -11.758 2.364   0.34 16.77 ?  166 SER   A N    1 
ATOM   3712 C  CA   A SER   A 1 166 ? 2.072  -12.909 1.896   0.66 18.30 ?  166 SER   A CA   1 
ATOM   3713 C  CA   B SER   A 1 166 ? 1.967  -12.424 1.753   0.34 17.61 ?  166 SER   A CA   1 
ATOM   3714 C  C    A SER   A 1 166 ? 2.467  -13.722 0.676   0.66 19.28 ?  166 SER   A C    1 
ATOM   3715 C  C    B SER   A 1 166 ? 2.374  -13.449 0.702   0.34 18.45 ?  166 SER   A C    1 
ATOM   3716 O  O    A SER   A 1 166 ? 1.868  -14.774 0.419   0.66 21.20 ?  166 SER   A O    1 
ATOM   3717 O  O    B SER   A 1 166 ? 1.629  -14.402 0.452   0.34 18.87 ?  166 SER   A O    1 
ATOM   3718 C  CB   A SER   A 1 166 ? 0.918  -11.969 1.539   0.66 20.08 ?  166 SER   A CB   1 
ATOM   3719 C  CB   B SER   A 1 166 ? 1.033  -11.393 1.115   0.34 17.67 ?  166 SER   A CB   1 
ATOM   3720 O  OG   A SER   A 1 166 ? 0.523  -11.207 2.665   0.66 23.14 ?  166 SER   A OG   1 
ATOM   3721 O  OG   B SER   A 1 166 ? 0.170  -10.810 2.079   0.34 18.71 ?  166 SER   A OG   1 
ATOM   3722 H  H    A SER   A 1 166 ? 3.119  -11.307 2.342   0.66 20.24 ?  166 SER   A H    1 
ATOM   3723 H  H    B SER   A 1 166 ? 3.121  -10.903 2.270   0.34 20.13 ?  166 SER   A H    1 
ATOM   3724 H  HA   A SER   A 1 166 ? 1.743  -13.533 2.563   0.66 21.97 ?  166 SER   A HA   1 
ATOM   3725 H  HA   B SER   A 1 166 ? 1.470  -12.884 2.446   0.34 21.14 ?  166 SER   A HA   1 
ATOM   3726 H  HB2  A SER   A 1 166 ? 1.201  -11.369 0.831   0.66 24.10 ?  166 SER   A HB2  1 
ATOM   3727 H  HB2  B SER   A 1 166 ? 1.568  -10.702 0.696   0.34 21.21 ?  166 SER   A HB2  1 
ATOM   3728 H  HB3  A SER   A 1 166 ? 0.153  -12.491 1.236   0.66 24.10 ?  166 SER   A HB3  1 
ATOM   3729 H  HB3  B SER   A 1 166 ? 0.491  -11.841 0.442   0.34 21.21 ?  166 SER   A HB3  1 
ATOM   3730 H  HG   A SER   A 1 166 ? 1.161  -10.729 2.926   0.66 27.78 ?  166 SER   A HG   1 
ATOM   3731 H  HG   B SER   A 1 166 ? -0.344 -10.265 1.701   0.34 22.46 ?  166 SER   A HG   1 
ATOM   3732 N  N    A SER   A 1 167 ? 3.450  -13.251 -0.089  0.66 18.78 ?  167 SER   A N    1 
ATOM   3733 N  N    B SER   A 1 167 ? 3.528  -13.267 0.064   0.34 19.02 ?  167 SER   A N    1 
ATOM   3734 C  CA   A SER   A 1 167 ? 3.926  -13.963 -1.265  0.66 18.94 ?  167 SER   A CA   1 
ATOM   3735 C  CA   B SER   A 1 167 ? 3.940  -14.130 -1.037  0.34 19.81 ?  167 SER   A CA   1 
ATOM   3736 C  C    A SER   A 1 167 ? 5.085  -14.895 -0.953  0.66 18.66 ?  167 SER   A C    1 
ATOM   3737 C  C    B SER   A 1 167 ? 5.277  -14.786 -0.732  0.34 20.43 ?  167 SER   A C    1 
ATOM   3738 O  O    A SER   A 1 167 ? 5.565  -15.582 -1.859  0.66 18.20 ?  167 SER   A O    1 
ATOM   3739 O  O    B SER   A 1 167 ? 6.255  -14.580 -1.458  0.34 22.00 ?  167 SER   A O    1 
ATOM   3740 C  CB   A SER   A 1 167 ? 4.353  -12.968 -2.354  0.66 19.17 ?  167 SER   A CB   1 
ATOM   3741 C  CB   B SER   A 1 167 ? 4.018  -13.323 -2.338  0.34 19.91 ?  167 SER   A CB   1 
ATOM   3742 O  OG   A SER   A 1 167 ? 5.466  -12.187 -1.935  0.66 19.45 ?  167 SER   A OG   1 
ATOM   3743 O  OG   B SER   A 1 167 ? 5.187  -12.519 -2.380  0.34 19.80 ?  167 SER   A OG   1 
ATOM   3744 H  H    A SER   A 1 167 ? 3.853  -12.505 0.053   0.66 22.54 ?  167 SER   A H    1 
ATOM   3745 H  H    B SER   A 1 167 ? 4.086  -12.653 0.252   0.34 22.83 ?  167 SER   A H    1 
ATOM   3746 H  HA   A SER   A 1 167 ? 3.201  -14.499 -1.624  0.66 22.74 ?  167 SER   A HA   1 
ATOM   3747 H  HA   B SER   A 1 167 ? 3.309  -14.850 -1.160  0.34 23.78 ?  167 SER   A HA   1 
ATOM   3748 H  HB2  A SER   A 1 167 ? 4.597  -13.465 -3.152  0.66 23.01 ?  167 SER   A HB2  1 
ATOM   3749 H  HB2  B SER   A 1 167 ? 4.020  -13.931 -3.093  0.34 23.90 ?  167 SER   A HB2  1 
ATOM   3750 H  HB3  A SER   A 1 167 ? 3.601  -12.382 -2.555  0.66 23.01 ?  167 SER   A HB3  1 
ATOM   3751 H  HB3  B SER   A 1 167 ? 3.241  -12.740 -2.391  0.34 23.90 ?  167 SER   A HB3  1 
ATOM   3752 H  HG   A SER   A 1 167 ? 5.251  -11.746 -1.250  0.66 23.35 ?  167 SER   A HG   1 
ATOM   3753 H  HG   B SER   A 1 167 ? 5.870  -12.999 -2.486  0.34 23.77 ?  167 SER   A HG   1 
ATOM   3754 N  N    A PHE   A 1 168 ? 5.550  -14.939 0.293   0.66 17.75 ?  168 PHE   A N    1 
ATOM   3755 N  N    B PHE   A 1 168 ? 5.322  -15.596 0.324   0.34 18.89 ?  168 PHE   A N    1 
ATOM   3756 C  CA   A PHE   A 1 168 ? 6.739  -15.725 0.591   0.66 18.31 ?  168 PHE   A CA   1 
ATOM   3757 C  CA   B PHE   A 1 168 ? 6.564  -16.243 0.732   0.34 17.83 ?  168 PHE   A CA   1 
ATOM   3758 C  C    A PHE   A 1 168 ? 6.432  -17.209 0.475   0.66 20.77 ?  168 PHE   A C    1 
ATOM   3759 C  C    B PHE   A 1 168 ? 6.503  -17.762 0.671   0.34 18.25 ?  168 PHE   A C    1 
ATOM   3760 O  O    A PHE   A 1 168 ? 5.465  -17.705 1.061   0.66 21.96 ?  168 PHE   A O    1 
ATOM   3761 O  O    B PHE   A 1 168 ? 7.433  -18.384 0.141   0.34 17.43 ?  168 PHE   A O    1 
ATOM   3762 C  CB   A PHE   A 1 168 ? 7.281  -15.428 1.986   0.66 17.51 ?  168 PHE   A CB   1 
ATOM   3763 C  CB   B PHE   A 1 168 ? 7.024  -15.786 2.127   0.34 17.56 ?  168 PHE   A CB   1 
ATOM   3764 C  CG   A PHE   A 1 168 ? 8.550  -16.185 2.291   0.66 16.85 ?  168 PHE   A CG   1 
ATOM   3765 C  CG   B PHE   A 1 168 ? 8.374  -16.323 2.502   0.34 17.56 ?  168 PHE   A CG   1 
ATOM   3766 C  CD1  A PHE   A 1 168 ? 9.724  -15.858 1.640   0.66 17.01 ?  168 PHE   A CD1  1 
ATOM   3767 C  CD1  B PHE   A 1 168 ? 9.520  -15.799 1.929   0.34 17.60 ?  168 PHE   A CD1  1 
ATOM   3768 C  CD2  A PHE   A 1 168 ? 8.565  -17.239 3.192   0.66 16.02 ?  168 PHE   A CD2  1 
ATOM   3769 C  CD2  B PHE   A 1 168 ? 8.500  -17.371 3.397   0.34 17.58 ?  168 PHE   A CD2  1 
ATOM   3770 C  CE1  A PHE   A 1 168 ? 10.891 -16.548 1.893   0.66 16.51 ?  168 PHE   A CE1  1 
ATOM   3771 C  CE1  B PHE   A 1 168 ? 10.766 -16.297 2.255   0.34 17.63 ?  168 PHE   A CE1  1 
ATOM   3772 C  CE2  A PHE   A 1 168 ? 9.737  -17.937 3.448   0.66 15.97 ?  168 PHE   A CE2  1 
ATOM   3773 C  CE2  B PHE   A 1 168 ? 9.744  -17.872 3.728   0.34 17.66 ?  168 PHE   A CE2  1 
ATOM   3774 C  CZ   A PHE   A 1 168 ? 10.900 -17.587 2.796   0.66 16.27 ?  168 PHE   A CZ   1 
ATOM   3775 C  CZ   B PHE   A 1 168 ? 10.878 -17.335 3.155   0.34 17.72 ?  168 PHE   A CZ   1 
ATOM   3776 H  H    A PHE   A 1 168 ? 5.210  -14.526 0.964   0.66 21.30 ?  168 PHE   A H    1 
ATOM   3777 H  H    B PHE   A 1 168 ? 4.634  -15.795 0.800   0.34 22.68 ?  168 PHE   A H    1 
ATOM   3778 H  HA   A PHE   A 1 168 ? 7.434  -15.507 -0.053  0.66 21.97 ?  168 PHE   A HA   1 
ATOM   3779 H  HA   B PHE   A 1 168 ? 7.256  -15.975 0.118   0.34 21.40 ?  168 PHE   A HA   1 
ATOM   3780 H  HB2  A PHE   A 1 168 ? 7.474  -14.478 2.056   0.66 21.01 ?  168 PHE   A HB2  1 
ATOM   3781 H  HB2  B PHE   A 1 168 ? 7.075  -14.816 2.143   0.34 21.08 ?  168 PHE   A HB2  1 
ATOM   3782 H  HB3  A PHE   A 1 168 ? 6.614  -15.678 2.643   0.66 21.01 ?  168 PHE   A HB3  1 
ATOM   3783 H  HB3  B PHE   A 1 168 ? 6.387  -16.093 2.792   0.34 21.08 ?  168 PHE   A HB3  1 
ATOM   3784 H  HD1  A PHE   A 1 168 ? 9.731  -15.156 1.031   0.66 20.42 ?  168 PHE   A HD1  1 
ATOM   3785 H  HD1  B PHE   A 1 168 ? 9.451  -15.098 1.320   0.34 21.13 ?  168 PHE   A HD1  1 
ATOM   3786 H  HD2  A PHE   A 1 168 ? 7.780  -17.477 3.633   0.66 19.23 ?  168 PHE   A HD2  1 
ATOM   3787 H  HD2  B PHE   A 1 168 ? 7.738  -17.735 3.784   0.34 21.10 ?  168 PHE   A HD2  1 
ATOM   3788 H  HE1  A PHE   A 1 168 ? 11.677 -16.311 1.454   0.66 19.82 ?  168 PHE   A HE1  1 
ATOM   3789 H  HE1  B PHE   A 1 168 ? 11.531 -15.934 1.867   0.34 21.16 ?  168 PHE   A HE1  1 
ATOM   3790 H  HE2  A PHE   A 1 168 ? 9.737  -18.640 4.059   0.66 19.17 ?  168 PHE   A HE2  1 
ATOM   3791 H  HE2  B PHE   A 1 168 ? 9.815  -18.573 4.334   0.34 21.20 ?  168 PHE   A HE2  1 
ATOM   3792 H  HZ   A PHE   A 1 168 ? 11.689 -18.052 2.966   0.66 19.53 ?  168 PHE   A HZ   1 
ATOM   3793 H  HZ   B PHE   A 1 168 ? 11.716 -17.672 3.376   0.34 21.27 ?  168 PHE   A HZ   1 
ATOM   3794 N  N    A LEU   A 1 169 ? 7.274  -17.917 -0.269  0.66 22.95 ?  169 LEU   A N    1 
ATOM   3795 N  N    B LEU   A 1 169 ? 5.457  -18.382 1.216   0.34 20.23 ?  169 LEU   A N    1 
ATOM   3796 C  CA   A LEU   A 1 169 ? 7.107  -19.350 -0.427  0.66 25.89 ?  169 LEU   A CA   1 
ATOM   3797 C  CA   B LEU   A 1 169 ? 5.351  -19.844 1.211   0.34 22.42 ?  169 LEU   A CA   1 
ATOM   3798 C  C    A LEU   A 1 169 ? 7.967  -20.066 0.600   0.66 26.73 ?  169 LEU   A C    1 
ATOM   3799 C  C    B LEU   A 1 169 ? 4.988  -20.395 -0.160  0.34 23.28 ?  169 LEU   A C    1 
ATOM   3800 O  O    A LEU   A 1 169 ? 7.456  -20.485 1.639   0.66 27.34 ?  169 LEU   A O    1 
ATOM   3801 O  O    B LEU   A 1 169 ? 4.161  -19.825 -0.869  0.34 23.73 ?  169 LEU   A O    1 
ATOM   3802 C  CB   A LEU   A 1 169 ? 7.464  -19.783 -1.852  0.66 27.42 ?  169 LEU   A CB   1 
ATOM   3803 C  CB   B LEU   A 1 169 ? 4.287  -20.301 2.206   0.34 23.57 ?  169 LEU   A CB   1 
ATOM   3804 C  CG   A LEU   A 1 169 ? 7.112  -21.224 -2.234  0.66 28.58 ?  169 LEU   A CG   1 
ATOM   3805 C  CG   B LEU   A 1 169 ? 4.456  -21.638 2.938   0.34 24.53 ?  169 LEU   A CG   1 
ATOM   3806 C  CD1  A LEU   A 1 169 ? 5.685  -21.561 -1.833  0.66 29.09 ?  169 LEU   A CD1  1 
ATOM   3807 C  CD1  B LEU   A 1 169 ? 5.097  -22.720 2.074   0.34 24.79 ?  169 LEU   A CD1  1 
ATOM   3808 C  CD2  A LEU   A 1 169 ? 7.305  -21.443 -3.729  0.66 28.69 ?  169 LEU   A CD2  1 
ATOM   3809 C  CD2  B LEU   A 1 169 ? 5.244  -21.420 4.216   0.34 24.87 ?  169 LEU   A CD2  1 
ATOM   3810 O  OXT  A LEU   A 1 169 ? 9.175  -20.224 0.431   0.66 26.28 -1 169 LEU   A OXT  1 
ATOM   3811 O  OXT  B LEU   A 1 169 ? 5.491  -21.440 -0.573  0.34 23.85 -1 169 LEU   A OXT  1 
ATOM   3812 H  H    A LEU   A 1 169 ? 7.951  -17.592 -0.690  0.66 27.55 ?  169 LEU   A H    1 
ATOM   3813 H  H    B LEU   A 1 169 ? 4.798  -17.978 1.610   0.34 24.29 ?  169 LEU   A H    1 
ATOM   3814 H  HA   A LEU   A 1 169 ? 6.186  -19.580 -0.253  0.66 31.08 ?  169 LEU   A HA   1 
ATOM   3815 H  HA   B LEU   A 1 169 ? 6.205  -20.222 1.460   0.34 26.91 ?  169 LEU   A HA   1 
ATOM   3816 H  HB2  A LEU   A 1 169 ? 6.995  -19.202 -2.470  0.66 32.91 ?  169 LEU   A HB2  1 
ATOM   3817 H  HB2  B LEU   A 1 169 ? 4.233  -19.632 2.892   0.34 28.29 ?  169 LEU   A HB2  1 
ATOM   3818 H  HB3  A LEU   A 1 169 ? 8.420  -19.681 -1.975  0.66 32.91 ?  169 LEU   A HB3  1 
ATOM   3819 H  HB3  B LEU   A 1 169 ? 3.438  -20.330 1.737   0.34 28.29 ?  169 LEU   A HB3  1 
ATOM   3820 H  HG   A LEU   A 1 169 ? 7.706  -21.833 -1.767  0.66 34.30 ?  169 LEU   A HG   1 
ATOM   3821 H  HG   B LEU   A 1 169 ? 3.577  -21.957 3.193   0.34 29.44 ?  169 LEU   A HG   1 
ATOM   3822 H  HD11 A LEU   A 1 169 ? 5.412  -22.375 -2.282  0.66 34.92 ?  169 LEU   A HD11 1 
ATOM   3823 H  HD11 B LEU   A 1 169 ? 5.084  -23.561 2.562   0.34 29.76 ?  169 LEU   A HD11 1 
ATOM   3824 H  HD12 A LEU   A 1 169 ? 5.648  -21.687 -0.871  0.66 34.92 ?  169 LEU   A HD12 1 
ATOM   3825 H  HD12 B LEU   A 1 169 ? 4.591  -22.809 1.252   0.34 29.76 ?  169 LEU   A HD12 1 
ATOM   3826 H  HD13 A LEU   A 1 169 ? 5.103  -20.829 -2.094  0.66 34.92 ?  169 LEU   A HD13 1 
ATOM   3827 H  HD13 B LEU   A 1 169 ? 6.012  -22.469 1.875   0.34 29.76 ?  169 LEU   A HD13 1 
ATOM   3828 H  HD21 A LEU   A 1 169 ? 7.085  -22.363 -3.946  0.66 34.43 ?  169 LEU   A HD21 1 
ATOM   3829 H  HD21 B LEU   A 1 169 ? 5.534  -22.279 4.558   0.34 29.85 ?  169 LEU   A HD21 1 
ATOM   3830 H  HD22 A LEU   A 1 169 ? 6.718  -20.841 -4.214  0.66 34.43 ?  169 LEU   A HD22 1 
ATOM   3831 H  HD22 B LEU   A 1 169 ? 6.011  -20.862 4.019   0.34 29.85 ?  169 LEU   A HD22 1 
ATOM   3832 H  HD23 A LEU   A 1 169 ? 8.229  -21.260 -3.959  0.66 34.43 ?  169 LEU   A HD23 1 
ATOM   3833 H  HD23 B LEU   A 1 169 ? 4.672  -20.979 4.864   0.34 29.85 ?  169 LEU   A HD23 1 
ATOM   3834 N  N    A SER   B 1 1   ? 50.788 -9.211  -23.743 0.66 28.29 ?  1   SER   B N    1 
ATOM   3835 N  N    B SER   B 1 1   ? 50.851 -9.328  -23.821 0.34 25.80 ?  1   SER   B N    1 
ATOM   3836 C  CA   A SER   B 1 1   ? 51.304 -10.269 -22.851 0.66 27.98 ?  1   SER   B CA   1 
ATOM   3837 C  CA   B SER   B 1 1   ? 51.290 -10.257 -22.757 0.34 25.91 ?  1   SER   B CA   1 
ATOM   3838 C  C    A SER   B 1 1   ? 50.240 -11.324 -22.577 0.66 26.40 ?  1   SER   B C    1 
ATOM   3839 C  C    B SER   B 1 1   ? 50.229 -11.315 -22.483 0.34 25.60 ?  1   SER   B C    1 
ATOM   3840 O  O    A SER   B 1 1   ? 49.038 -11.128 -22.827 0.66 25.83 ?  1   SER   B O    1 
ATOM   3841 O  O    B SER   B 1 1   ? 49.041 -11.123 -22.763 0.34 25.24 ?  1   SER   B O    1 
ATOM   3842 C  CB   A SER   B 1 1   ? 51.794 -9.676  -21.532 0.66 29.13 ?  1   SER   B CB   1 
ATOM   3843 C  CB   B SER   B 1 1   ? 51.601 -9.496  -21.472 0.34 26.13 ?  1   SER   B CB   1 
ATOM   3844 O  OG   A SER   B 1 1   ? 50.706 -9.376  -20.680 0.66 31.10 ?  1   SER   B OG   1 
ATOM   3845 O  OG   B SER   B 1 1   ? 50.575 -9.684  -20.515 0.34 26.81 ?  1   SER   B OG   1 
ATOM   3846 H  H1   A SER   B 1 1   ? 50.687 -9.545  -24.560 0.66 33.96 ?  1   SER   B H1   1 
ATOM   3847 H  H1   B SER   B 1 1   ? 51.484 -8.719  -23.950 0.34 30.97 ?  1   SER   B H1   1 
ATOM   3848 H  H2   A SER   B 1 1   ? 50.008 -8.927  -23.433 0.66 33.96 ?  1   SER   B H2   1 
ATOM   3849 H  H2   B SER   B 1 1   ? 50.718 -9.788  -24.570 0.34 30.97 ?  1   SER   B H2   1 
ATOM   3850 H  H3   A SER   B 1 1   ? 51.371 -8.541  -23.761 0.66 33.96 ?  1   SER   B H3   1 
ATOM   3851 H  H3   B SER   B 1 1   ? 50.098 -8.935  -23.570 0.34 30.97 ?  1   SER   B H3   1 
ATOM   3852 H  HA   A SER   B 1 1   ? 52.053 -10.694 -23.292 0.66 33.58 ?  1   SER   B HA   1 
ATOM   3853 H  HA   B SER   B 1 1   ? 52.096 -10.695 -23.058 0.34 31.10 ?  1   SER   B HA   1 
ATOM   3854 H  HB2  A SER   B 1 1   ? 52.368 -10.325 -21.099 0.66 34.96 ?  1   SER   B HB2  1 
ATOM   3855 H  HB2  B SER   B 1 1   ? 52.436 -9.829  -21.113 0.34 31.36 ?  1   SER   B HB2  1 
ATOM   3856 H  HB3  A SER   B 1 1   ? 52.286 -8.862  -21.715 0.66 34.96 ?  1   SER   B HB3  1 
ATOM   3857 H  HB3  B SER   B 1 1   ? 51.679 -8.550  -21.675 0.34 31.36 ?  1   SER   B HB3  1 
ATOM   3858 H  HG   A SER   B 1 1   ? 50.986 -8.988  -19.989 0.66 37.32 ?  1   SER   B HG   1 
ATOM   3859 H  HG   B SER   B 1 1   ? 50.695 -9.163  -19.867 0.34 32.18 ?  1   SER   B HG   1 
ATOM   3860 N  N    A MET   B 1 2   ? 50.704 -12.449 -22.051 0.66 25.53 ?  2   MET   B N    1 
ATOM   3861 N  N    B MET   B 1 2   ? 50.677 -12.431 -21.922 0.34 25.52 ?  2   MET   B N    1 
ATOM   3862 C  CA   A MET   B 1 2   ? 49.894 -13.646 -21.877 0.66 25.98 ?  2   MET   B CA   1 
ATOM   3863 C  CA   B MET   B 1 2   ? 49.854 -13.618 -21.730 0.34 25.68 ?  2   MET   B CA   1 
ATOM   3864 C  C    A MET   B 1 2   ? 49.647 -13.851 -20.390 0.66 23.71 ?  2   MET   B C    1 
ATOM   3865 C  C    B MET   B 1 2   ? 49.579 -13.783 -20.242 0.34 24.04 ?  2   MET   B C    1 
ATOM   3866 O  O    A MET   B 1 2   ? 50.581 -14.119 -19.630 0.66 23.64 ?  2   MET   B O    1 
ATOM   3867 O  O    B MET   B 1 2   ? 50.488 -14.102 -19.468 0.34 24.22 ?  2   MET   B O    1 
ATOM   3868 C  CB   A MET   B 1 2   ? 50.630 -14.837 -22.475 0.66 30.00 ?  2   MET   B CB   1 
ATOM   3869 C  CB   B MET   B 1 2   ? 50.600 -14.824 -22.280 0.34 27.93 ?  2   MET   B CB   1 
ATOM   3870 C  CG   A MET   B 1 2   ? 49.799 -16.102 -22.605 0.66 33.87 ?  2   MET   B CG   1 
ATOM   3871 C  CG   B MET   B 1 2   ? 49.722 -15.981 -22.733 0.34 29.95 ?  2   MET   B CG   1 
ATOM   3872 S  SD   A MET   B 1 2   ? 50.641 -17.337 -23.612 0.66 37.55 ?  2   MET   B SD   1 
ATOM   3873 S  SD   B MET   B 1 2   ? 50.638 -17.124 -23.771 0.34 31.87 ?  2   MET   B SD   1 
ATOM   3874 C  CE   A MET   B 1 2   ? 51.177 -16.298 -24.964 0.66 37.73 ?  2   MET   B CE   1 
ATOM   3875 C  CE   B MET   B 1 2   ? 51.700 -15.981 -24.634 0.34 32.12 ?  2   MET   B CE   1 
ATOM   3876 H  H    A MET   B 1 2   ? 51.515 -12.550 -21.784 0.66 30.64 ?  2   MET   B H    1 
ATOM   3877 H  H    B MET   B 1 2   ? 51.487 -12.532 -21.646 0.34 30.64 ?  2   MET   B H    1 
ATOM   3878 H  HA   A MET   B 1 2   ? 49.049 -13.547 -22.338 0.66 31.18 ?  2   MET   B HA   1 
ATOM   3879 H  HA   B MET   B 1 2   ? 49.025 -13.531 -22.227 0.34 30.82 ?  2   MET   B HA   1 
ATOM   3880 H  HB2  A MET   B 1 2   ? 50.928 -14.557 -23.349 0.66 36.01 ?  2   MET   B HB2  1 
ATOM   3881 H  HB2  B MET   B 1 2   ? 51.098 -14.470 -23.024 0.34 33.52 ?  2   MET   B HB2  1 
ATOM   3882 H  HB3  A MET   B 1 2   ? 51.394 -15.056 -21.924 0.66 36.01 ?  2   MET   B HB3  1 
ATOM   3883 H  HB3  B MET   B 1 2   ? 51.211 -15.179 -21.619 0.34 33.52 ?  2   MET   B HB3  1 
ATOM   3884 H  HG2  A MET   B 1 2   ? 49.646 -16.477 -21.719 0.66 40.65 ?  2   MET   B HG2  1 
ATOM   3885 H  HG2  B MET   B 1 2   ? 49.404 -16.468 -21.954 0.34 35.95 ?  2   MET   B HG2  1 
ATOM   3886 H  HG3  A MET   B 1 2   ? 48.954 -15.897 -23.033 0.66 40.65 ?  2   MET   B HG3  1 
ATOM   3887 H  HG3  B MET   B 1 2   ? 48.975 -15.654 -23.250 0.34 35.95 ?  2   MET   B HG3  1 
ATOM   3888 H  HE1  A MET   B 1 2   ? 51.338 -16.852 -25.729 0.66 45.28 ?  2   MET   B HE1  1 
ATOM   3889 H  HE1  B MET   B 1 2   ? 52.082 -16.454 -25.359 0.34 38.55 ?  2   MET   B HE1  1 
ATOM   3890 H  HE2  A MET   B 1 2   ? 50.472 -15.654 -25.158 0.66 45.28 ?  2   MET   B HE2  1 
ATOM   3891 H  HE2  B MET   B 1 2   ? 51.169 -15.229 -24.960 0.34 38.55 ?  2   MET   B HE2  1 
ATOM   3892 H  HE3  A MET   B 1 2   ? 51.991 -15.825 -24.713 0.66 45.28 ?  2   MET   B HE3  1 
ATOM   3893 H  HE3  B MET   B 1 2   ? 52.408 -15.665 -24.039 0.34 38.55 ?  2   MET   B HE3  1 
ATOM   3894 N  N    A VAL   B 1 3   ? 48.391 -13.717 -19.978 0.66 21.78 ?  3   VAL   B N    1 
ATOM   3895 N  N    B VAL   B 1 3   ? 48.333 -13.558 -19.847 0.34 22.36 ?  3   VAL   B N    1 
ATOM   3896 C  CA   A VAL   B 1 3   ? 47.981 -13.951 -18.602 0.66 20.56 ?  3   VAL   B CA   1 
ATOM   3897 C  CA   B VAL   B 1 3   ? 47.893 -13.798 -18.480 0.34 20.76 ?  3   VAL   B CA   1 
ATOM   3898 C  C    A VAL   B 1 3   ? 46.749 -14.845 -18.621 0.66 18.90 ?  3   VAL   B C    1 
ATOM   3899 C  C    B VAL   B 1 3   ? 46.638 -14.655 -18.510 0.34 18.84 ?  3   VAL   B C    1 
ATOM   3900 O  O    A VAL   B 1 3   ? 46.049 -14.958 -19.629 0.66 18.90 ?  3   VAL   B O    1 
ATOM   3901 O  O    B VAL   B 1 3   ? 45.812 -14.555 -19.422 0.34 18.64 ?  3   VAL   B O    1 
ATOM   3902 C  CB   A VAL   B 1 3   ? 47.689 -12.636 -17.845 0.66 22.29 ?  3   VAL   B CB   1 
ATOM   3903 C  CB   B VAL   B 1 3   ? 47.627 -12.494 -17.699 0.34 21.60 ?  3   VAL   B CB   1 
ATOM   3904 C  CG1  A VAL   B 1 3   ? 48.943 -11.764 -17.770 0.66 23.00 ?  3   VAL   B CG1  1 
ATOM   3905 C  CG1  B VAL   B 1 3   ? 48.889 -11.649 -17.612 0.34 21.88 ?  3   VAL   B CG1  1 
ATOM   3906 C  CG2  A VAL   B 1 3   ? 46.543 -11.886 -18.508 0.66 22.69 ?  3   VAL   B CG2  1 
ATOM   3907 C  CG2  B VAL   B 1 3   ? 46.484 -11.718 -18.334 0.34 21.79 ?  3   VAL   B CG2  1 
ATOM   3908 H  H    A VAL   B 1 3   ? 47.743 -13.495 -20.496 0.66 26.14 ?  3   VAL   B H    1 
ATOM   3909 H  H    B VAL   B 1 3   ? 47.719 -13.260 -20.370 0.34 26.84 ?  3   VAL   B H    1 
ATOM   3910 H  HA   A VAL   B 1 3   ? 48.690 -14.420 -18.132 0.66 24.68 ?  3   VAL   B HA   1 
ATOM   3911 H  HA   B VAL   B 1 3   ? 48.586 -14.293 -18.016 0.34 24.92 ?  3   VAL   B HA   1 
ATOM   3912 H  HB   A VAL   B 1 3   ? 47.421 -12.853 -16.938 0.66 26.75 ?  3   VAL   B HB   1 
ATOM   3913 H  HB   B VAL   B 1 3   ? 47.362 -12.730 -16.797 0.34 25.92 ?  3   VAL   B HB   1 
ATOM   3914 H  HG11 A VAL   B 1 3   ? 48.733 -10.955 -17.278 0.66 27.61 ?  3   VAL   B HG11 1 
ATOM   3915 H  HG11 B VAL   B 1 3   ? 48.694 -10.849 -17.100 0.34 26.27 ?  3   VAL   B HG11 1 
ATOM   3916 H  HG12 A VAL   B 1 3   ? 49.643 -12.258 -17.315 0.66 27.61 ?  3   VAL   B HG12 1 
ATOM   3917 H  HG12 B VAL   B 1 3   ? 49.583 -12.164 -17.172 0.34 26.27 ?  3   VAL   B HG12 1 
ATOM   3918 H  HG13 A VAL   B 1 3   ? 49.226 -11.542 -18.670 0.66 27.61 ?  3   VAL   B HG13 1 
ATOM   3919 H  HG13 B VAL   B 1 3   ? 49.171 -11.410 -18.508 0.34 26.27 ?  3   VAL   B HG13 1 
ATOM   3920 H  HG21 A VAL   B 1 3   ? 46.478 -11.003 -18.118 0.66 27.23 ?  3   VAL   B HG21 1 
ATOM   3921 H  HG21 B VAL   B 1 3   ? 46.452 -10.833 -17.944 0.34 26.16 ?  3   VAL   B HG21 1 
ATOM   3922 H  HG22 A VAL   B 1 3   ? 46.713 -11.820 -19.459 0.66 27.23 ?  3   VAL   B HG22 1 
ATOM   3923 H  HG22 B VAL   B 1 3   ? 46.636 -11.656 -19.290 0.34 26.16 ?  3   VAL   B HG22 1 
ATOM   3924 H  HG23 A VAL   B 1 3   ? 45.714 -12.374 -18.355 0.66 27.23 ?  3   VAL   B HG23 1 
ATOM   3925 H  HG23 B VAL   B 1 3   ? 45.649 -12.186 -18.163 0.34 26.16 ?  3   VAL   B HG23 1 
ATOM   3926 N  N    . ASN   B 1 4   ? 46.491 -15.491 -17.485 1.00 17.48 ?  4   ASN   B N    1 
ATOM   3927 C  CA   . ASN   B 1 4   ? 45.357 -16.403 -17.369 1.00 15.96 ?  4   ASN   B CA   1 
ATOM   3928 C  C    . ASN   B 1 4   ? 45.307 -17.367 -18.553 1.00 15.92 ?  4   ASN   B C    1 
ATOM   3929 O  O    . ASN   B 1 4   ? 44.249 -17.618 -19.124 1.00 16.30 ?  4   ASN   B O    1 
ATOM   3930 C  CB   . ASN   B 1 4   ? 44.035 -15.646 -17.209 1.00 15.30 ?  4   ASN   B CB   1 
ATOM   3931 C  CG   . ASN   B 1 4   ? 43.981 -14.839 -15.927 1.00 14.54 ?  4   ASN   B CG   1 
ATOM   3932 O  OD1  . ASN   B 1 4   ? 44.274 -15.349 -14.848 1.00 14.11 ?  4   ASN   B OD1  1 
ATOM   3933 N  ND2  . ASN   B 1 4   ? 43.634 -13.559 -16.042 1.00 15.92 ?  4   ASN   B ND2  1 
ATOM   3934 H  H    A ASN   B 1 4   ? 46.959 -15.419 -16.771 0.66 20.98 ?  4   ASN   B H    1 
ATOM   3935 H  H    B ASN   B 1 4   ? 47.043 -15.543 -16.831 0.34 20.98 ?  4   ASN   B H    1 
ATOM   3936 H  HA   . ASN   B 1 4   ? 45.481 -16.936 -16.568 1.00 19.15 ?  4   ASN   B HA   1 
ATOM   3937 H  HB2  . ASN   B 1 4   ? 43.925 -15.036 -17.953 1.00 18.37 ?  4   ASN   B HB2  1 
ATOM   3938 H  HB3  . ASN   B 1 4   ? 43.305 -16.285 -17.192 1.00 18.37 ?  4   ASN   B HB3  1 
ATOM   3939 H  HD21 . ASN   B 1 4   ? 43.593 -13.058 -15.340 1.00 19.11 ?  4   ASN   B HD21 1 
ATOM   3940 H  HD22 . ASN   B 1 4   ? 43.443 -13.231 -16.811 1.00 19.11 ?  4   ASN   B HD22 1 
ATOM   3941 N  N    . SER   B 1 5   ? 46.467 -17.895 -18.938 1.00 16.90 ?  5   SER   B N    1 
ATOM   3942 C  CA   . SER   B 1 5   ? 46.556 -18.798 -20.084 1.00 18.75 ?  5   SER   B CA   1 
ATOM   3943 C  C    . SER   B 1 5   ? 46.497 -20.240 -19.593 1.00 20.56 ?  5   SER   B C    1 
ATOM   3944 O  O    . SER   B 1 5   ? 47.463 -20.992 -19.649 1.00 23.52 ?  5   SER   B O    1 
ATOM   3945 C  CB   . SER   B 1 5   ? 47.828 -18.527 -20.884 1.00 20.09 ?  5   SER   B CB   1 
ATOM   3946 O  OG   . SER   B 1 5   ? 48.996 -18.740 -20.104 1.00 22.89 ?  5   SER   B OG   1 
ATOM   3947 H  H    . SER   B 1 5   ? 47.224 -17.738 -18.556 1.00 20.28 ?  5   SER   B H    1 
ATOM   3948 H  HA   . SER   B 1 5   ? 45.801 -18.649 -20.668 1.00 22.50 ?  5   SER   B HA   1 
ATOM   3949 H  HB2  . SER   B 1 5   ? 47.847 -19.122 -21.654 1.00 24.12 ?  5   SER   B HB2  1 
ATOM   3950 H  HB3  . SER   B 1 5   ? 47.803 -17.607 -21.183 1.00 24.12 ?  5   SER   B HB3  1 
ATOM   3951 H  HG   . SER   B 1 5   ? 49.024 -19.542 -19.852 1.00 27.48 ?  5   SER   B HG   1 
ATOM   3952 N  N    . PHE   B 1 6   ? 45.323 -20.603 -19.089 1.00 20.53 ?  6   PHE   B N    1 
ATOM   3953 C  CA   . PHE   B 1 6   ? 45.094 -21.961 -18.622 1.00 20.37 ?  6   PHE   B CA   1 
ATOM   3954 C  C    . PHE   B 1 6   ? 44.982 -22.898 -19.815 1.00 24.07 ?  6   PHE   B C    1 
ATOM   3955 O  O    . PHE   B 1 6   ? 44.335 -22.576 -20.815 1.00 25.95 ?  6   PHE   B O    1 
ATOM   3956 C  CB   . PHE   B 1 6   ? 43.812 -22.009 -17.793 1.00 18.66 ?  6   PHE   B CB   1 
ATOM   3957 C  CG   . PHE   B 1 6   ? 43.861 -21.161 -16.548 1.00 16.52 ?  6   PHE   B CG   1 
ATOM   3958 C  CD1  . PHE   B 1 6   ? 44.363 -21.678 -15.369 1.00 15.16 ?  6   PHE   B CD1  1 
ATOM   3959 C  CD2  . PHE   B 1 6   ? 43.390 -19.853 -16.556 1.00 16.03 ?  6   PHE   B CD2  1 
ATOM   3960 C  CE1  . PHE   B 1 6   ? 44.403 -20.910 -14.218 1.00 15.18 ?  6   PHE   B CE1  1 
ATOM   3961 C  CE2  . PHE   B 1 6   ? 43.431 -19.073 -15.411 1.00 16.42 ?  6   PHE   B CE2  1 
ATOM   3962 C  CZ   . PHE   B 1 6   ? 43.940 -19.597 -14.243 1.00 15.42 ?  6   PHE   B CZ   1 
ATOM   3963 H  H    . PHE   B 1 6   ? 44.643 -20.085 -19.017 1.00 24.64 ?  6   PHE   B H    1 
ATOM   3964 H  HA   . PHE   B 1 6   ? 45.835 -22.250 -18.070 1.00 24.45 ?  6   PHE   B HA   1 
ATOM   3965 H  HB2  . PHE   B 1 6   ? 43.072 -21.694 -18.337 1.00 22.40 ?  6   PHE   B HB2  1 
ATOM   3966 H  HB3  . PHE   B 1 6   ? 43.648 -22.926 -17.519 1.00 22.40 ?  6   PHE   B HB3  1 
ATOM   3967 H  HD1  . PHE   B 1 6   ? 44.683 -22.552 -15.350 1.00 18.19 ?  6   PHE   B HD1  1 
ATOM   3968 H  HD2  . PHE   B 1 6   ? 43.044 -19.497 -17.342 1.00 19.25 ?  6   PHE   B HD2  1 
ATOM   3969 H  HE1  . PHE   B 1 6   ? 44.756 -21.265 -13.431 1.00 18.22 ?  6   PHE   B HE1  1 
ATOM   3970 H  HE2  . PHE   B 1 6   ? 43.112 -18.198 -15.429 1.00 19.72 ?  6   PHE   B HE2  1 
ATOM   3971 H  HZ   . PHE   B 1 6   ? 43.969 -19.083 -13.469 1.00 18.51 ?  6   PHE   B HZ   1 
ATOM   3972 N  N    A SER   B 1 7   ? 45.628 -24.059 -19.703 0.66 24.75 ?  7   SER   B N    1 
ATOM   3973 N  N    B SER   B 1 7   ? 45.618 -24.064 -19.712 0.34 24.73 ?  7   SER   B N    1 
ATOM   3974 C  CA   A SER   B 1 7   ? 45.724 -25.020 -20.791 0.66 27.16 ?  7   SER   B CA   1 
ATOM   3975 C  CA   B SER   B 1 7   ? 45.623 -25.014 -20.814 0.34 26.06 ?  7   SER   B CA   1 
ATOM   3976 C  C    A SER   B 1 7   ? 45.659 -26.433 -20.232 0.66 26.78 ?  7   SER   B C    1 
ATOM   3977 C  C    B SER   B 1 7   ? 45.623 -26.434 -20.268 0.34 26.03 ?  7   SER   B C    1 
ATOM   3978 O  O    A SER   B 1 7   ? 46.264 -26.730 -19.198 0.66 27.47 ?  7   SER   B O    1 
ATOM   3979 O  O    B SER   B 1 7   ? 46.269 -26.720 -19.256 0.34 26.52 ?  7   SER   B O    1 
ATOM   3980 C  CB   A SER   B 1 7   ? 47.041 -24.836 -21.562 0.66 29.18 ?  7   SER   B CB   1 
ATOM   3981 C  CB   B SER   B 1 7   ? 46.842 -24.804 -21.720 0.34 26.99 ?  7   SER   B CB   1 
ATOM   3982 O  OG   A SER   B 1 7   ? 47.174 -25.797 -22.595 0.66 30.80 ?  7   SER   B OG   1 
ATOM   3983 O  OG   B SER   B 1 7   ? 46.672 -25.462 -22.963 0.34 27.68 ?  7   SER   B OG   1 
ATOM   3984 H  H    A SER   B 1 7   ? 46.033 -24.316 -18.987 0.66 29.70 ?  7   SER   B H    1 
ATOM   3985 H  H    B SER   B 1 7   ? 46.057 -24.324 -19.017 0.34 29.68 ?  7   SER   B H    1 
ATOM   3986 H  HA   A SER   B 1 7   ? 44.988 -24.898 -21.406 0.66 32.59 ?  7   SER   B HA   1 
ATOM   3987 H  HA   B SER   B 1 7   ? 44.825 -24.897 -21.346 0.34 31.28 ?  7   SER   B HA   1 
ATOM   3988 H  HB2  A SER   B 1 7   ? 47.055 -23.946 -21.954 0.66 35.02 ?  7   SER   B HB2  1 
ATOM   3989 H  HB2  B SER   B 1 7   ? 46.955 -23.853 -21.881 0.34 32.40 ?  7   SER   B HB2  1 
ATOM   3990 H  HB3  A SER   B 1 7   ? 47.786 -24.934 -20.947 0.66 35.02 ?  7   SER   B HB3  1 
ATOM   3991 H  HB3  B SER   B 1 7   ? 47.632 -25.158 -21.279 0.34 32.40 ?  7   SER   B HB3  1 
ATOM   3992 H  HG   A SER   B 1 7   ? 47.896 -25.676 -23.009 0.66 36.96 ?  7   SER   B HG   1 
ATOM   3993 H  HG   B SER   B 1 7   ? 47.349 -25.339 -23.447 0.34 33.22 ?  7   SER   B HG   1 
ATOM   3994 N  N    A GLY   B 1 8   ? 44.921 -27.299 -20.922 0.66 26.66 ?  8   GLY   B N    1 
ATOM   3995 N  N    B GLY   B 1 8   ? 44.896 -27.317 -20.950 0.34 25.86 ?  8   GLY   B N    1 
ATOM   3996 C  CA   A GLY   B 1 8   ? 44.890 -28.702 -20.569 0.66 25.66 ?  8   GLY   B CA   1 
ATOM   3997 C  CA   B GLY   B 1 8   ? 44.876 -28.716 -20.583 0.34 25.14 ?  8   GLY   B CA   1 
ATOM   3998 C  C    A GLY   B 1 8   ? 43.980 -29.052 -19.420 0.66 24.57 ?  8   GLY   B C    1 
ATOM   3999 C  C    B GLY   B 1 8   ? 43.961 -29.066 -19.436 0.34 24.26 ?  8   GLY   B C    1 
ATOM   4000 O  O    A GLY   B 1 8   ? 44.156 -30.112 -18.808 0.66 26.09 ?  8   GLY   B O    1 
ATOM   4001 O  O    B GLY   B 1 8   ? 44.119 -30.137 -18.840 0.34 25.15 ?  8   GLY   B O    1 
ATOM   4002 H  H    A GLY   B 1 8   ? 44.430 -27.091 -21.592 0.66 31.99 ?  8   GLY   B H    1 
ATOM   4003 H  H    B GLY   B 1 8   ? 44.409 -27.123 -21.631 0.34 31.04 ?  8   GLY   B H    1 
ATOM   4004 H  HA2  A GLY   B 1 8   ? 44.603 -29.213 -21.341 0.66 30.80 ?  8   GLY   B HA2  1 
ATOM   4005 H  HA2  B GLY   B 1 8   ? 44.601 -29.238 -21.352 0.34 30.18 ?  8   GLY   B HA2  1 
ATOM   4006 H  HA3  A GLY   B 1 8   ? 45.784 -28.990 -20.333 0.66 30.80 ?  8   GLY   B HA3  1 
ATOM   4007 H  HA3  B GLY   B 1 8   ? 45.772 -28.991 -20.337 0.34 30.18 ?  8   GLY   B HA3  1 
ATOM   4008 N  N    . TYR   B 1 9   ? 43.000 -28.207 -19.109 1.00 22.80 ?  9   TYR   B N    1 
ATOM   4009 C  CA   . TYR   B 1 9   ? 42.070 -28.488 -18.028 1.00 19.49 ?  9   TYR   B CA   1 
ATOM   4010 C  C    . TYR   B 1 9   ? 40.880 -29.285 -18.527 1.00 19.16 ?  9   TYR   B C    1 
ATOM   4011 O  O    . TYR   B 1 9   ? 40.434 -29.137 -19.670 1.00 21.24 ?  9   TYR   B O    1 
ATOM   4012 C  CB   . TYR   B 1 9   ? 41.568 -27.207 -17.363 1.00 18.53 ?  9   TYR   B CB   1 
ATOM   4013 C  CG   . TYR   B 1 9   ? 42.606 -26.583 -16.460 1.00 17.83 ?  9   TYR   B CG   1 
ATOM   4014 C  CD1  . TYR   B 1 9   ? 43.690 -25.907 -16.996 1.00 18.42 ?  9   TYR   B CD1  1 
ATOM   4015 C  CD2  . TYR   B 1 9   ? 42.523 -26.693 -15.081 1.00 17.00 ?  9   TYR   B CD2  1 
ATOM   4016 C  CE1  . TYR   B 1 9   ? 44.662 -25.350 -16.183 1.00 18.59 ?  9   TYR   B CE1  1 
ATOM   4017 C  CE2  . TYR   B 1 9   ? 43.485 -26.138 -14.255 1.00 17.83 ?  9   TYR   B CE2  1 
ATOM   4018 C  CZ   . TYR   B 1 9   ? 44.555 -25.466 -14.812 1.00 18.56 ?  9   TYR   B CZ   1 
ATOM   4019 O  OH   . TYR   B 1 9   ? 45.520 -24.917 -13.997 1.00 19.32 ?  9   TYR   B OH   1 
ATOM   4020 H  H    A TYR   B 1 9   ? 42.846 -27.467 -19.519 0.66 27.37 ?  9   TYR   B H    1 
ATOM   4021 H  H    B TYR   B 1 9   ? 42.858 -27.458 -19.506 0.34 27.37 ?  9   TYR   B H    1 
ATOM   4022 H  HA   . TYR   B 1 9   ? 42.514 -29.017 -17.352 1.00 23.40 ?  9   TYR   B HA   1 
ATOM   4023 H  HB2  . TYR   B 1 9   ? 41.318 -26.559 -18.044 1.00 22.24 ?  9   TYR   B HB2  1 
ATOM   4024 H  HB3  . TYR   B 1 9   ? 40.798 -27.432 -16.821 1.00 22.24 ?  9   TYR   B HB3  1 
ATOM   4025 H  HD1  . TYR   B 1 9   ? 43.763 -25.830 -17.923 1.00 22.11 ?  9   TYR   B HD1  1 
ATOM   4026 H  HD2  . TYR   B 1 9   ? 41.800 -27.152 -14.704 1.00 20.41 ?  9   TYR   B HD2  1 
ATOM   4027 H  HE1  . TYR   B 1 9   ? 45.378 -24.902 -16.563 1.00 22.32 ?  9   TYR   B HE1  1 
ATOM   4028 H  HE2  . TYR   B 1 9   ? 43.408 -26.228 -13.334 1.00 21.41 ?  9   TYR   B HE2  1 
ATOM   4029 H  HH   . TYR   B 1 9   ? 46.105 -24.546 -14.469 1.00 23.19 ?  9   TYR   B HH   1 
ATOM   4030 N  N    . LEU   B 1 10  ? 40.382 -30.149 -17.651 1.00 17.35 ?  10  LEU   B N    1 
ATOM   4031 C  CA   . LEU   B 1 10  ? 39.176 -30.917 -17.898 1.00 17.75 ?  10  LEU   B CA   1 
ATOM   4032 C  C    . LEU   B 1 10  ? 37.995 -30.147 -17.328 1.00 17.75 ?  10  LEU   B C    1 
ATOM   4033 O  O    . LEU   B 1 10  ? 38.019 -29.730 -16.167 1.00 17.23 ?  10  LEU   B O    1 
ATOM   4034 C  CB   . LEU   B 1 10  ? 39.285 -32.278 -17.212 1.00 19.11 ?  10  LEU   B CB   1 
ATOM   4035 C  CG   . LEU   B 1 10  ? 38.135 -33.241 -17.502 1.00 20.89 ?  10  LEU   B CG   1 
ATOM   4036 C  CD1  . LEU   B 1 10  ? 38.245 -33.772 -18.925 1.00 22.41 ?  10  LEU   B CD1  1 
ATOM   4037 C  CD2  . LEU   B 1 10  ? 38.092 -34.372 -16.489 1.00 21.94 ?  10  LEU   B CD2  1 
ATOM   4038 H  H    . LEU   B 1 10  ? 40.733 -30.309 -16.879 1.00 20.83 ?  10  LEU   B H    1 
ATOM   4039 H  HA   . LEU   B 1 10  ? 39.045 -31.051 -18.848 1.00 21.31 ?  10  LEU   B HA   1 
ATOM   4040 H  HB2  . LEU   B 1 10  ? 40.107 -32.707 -17.502 1.00 22.94 ?  10  LEU   B HB2  1 
ATOM   4041 H  HB3  . LEU   B 1 10  ? 39.316 -32.141 -16.250 1.00 22.94 ?  10  LEU   B HB3  1 
ATOM   4042 H  HG   . LEU   B 1 10  ? 37.299 -32.754 -17.434 1.00 25.08 ?  10  LEU   B HG   1 
ATOM   4043 H  HD11 . LEU   B 1 10  ? 37.538 -34.420 -19.073 1.00 26.90 ?  10  LEU   B HD11 1 
ATOM   4044 H  HD12 . LEU   B 1 10  ? 38.150 -33.033 -19.547 1.00 26.90 ?  10  LEU   B HD12 1 
ATOM   4045 H  HD13 . LEU   B 1 10  ? 39.110 -34.193 -19.039 1.00 26.90 ?  10  LEU   B HD13 1 
ATOM   4046 H  HD21 . LEU   B 1 10  ? 37.352 -34.958 -16.708 1.00 26.33 ?  10  LEU   B HD21 1 
ATOM   4047 H  HD22 . LEU   B 1 10  ? 38.928 -34.857 -16.526 1.00 26.33 ?  10  LEU   B HD22 1 
ATOM   4048 H  HD23 . LEU   B 1 10  ? 37.965 -33.993 -15.604 1.00 26.33 ?  10  LEU   B HD23 1 
ATOM   4049 N  N    . LYS   B 1 11  ? 36.963 -29.975 -18.142 1.00 18.86 ?  11  LYS   B N    1 
ATOM   4050 C  CA   . LYS   B 1 11  ? 35.767 -29.263 -17.724 1.00 21.32 ?  11  LYS   B CA   1 
ATOM   4051 C  C    . LYS   B 1 11  ? 34.908 -30.188 -16.867 1.00 20.03 ?  11  LYS   B C    1 
ATOM   4052 O  O    . LYS   B 1 11  ? 34.539 -31.288 -17.302 1.00 21.78 ?  11  LYS   B O    1 
ATOM   4053 C  CB   . LYS   B 1 11  ? 35.004 -28.812 -18.969 1.00 25.48 ?  11  LYS   B CB   1 
ATOM   4054 C  CG   . LYS   B 1 11  ? 33.889 -27.817 -18.718 1.00 29.11 ?  11  LYS   B CG   1 
ATOM   4055 C  CD   . LYS   B 1 11  ? 33.156 -27.495 -20.015 1.00 31.97 ?  11  LYS   B CD   1 
ATOM   4056 C  CE   . LYS   B 1 11  ? 32.145 -26.377 -19.831 1.00 34.15 ?  11  LYS   B CE   1 
ATOM   4057 N  NZ   . LYS   B 1 11  ? 32.801 -25.052 -19.652 1.00 35.34 ?  11  LYS   B NZ   1 
ATOM   4058 H  H    . LYS   B 1 11  ? 36.924 -30.276 -18.947 1.00 22.64 ?  11  LYS   B H    1 
ATOM   4059 H  HA   . LYS   B 1 11  ? 36.011 -28.482 -17.203 1.00 25.58 ?  11  LYS   B HA   1 
ATOM   4060 H  HB2  . LYS   B 1 11  ? 35.633 -28.395 -19.580 1.00 30.58 ?  11  LYS   B HB2  1 
ATOM   4061 H  HB3  . LYS   B 1 11  ? 34.611 -29.591 -19.390 1.00 30.58 ?  11  LYS   B HB3  1 
ATOM   4062 H  HG2  . LYS   B 1 11  ? 33.252 -28.197 -18.094 1.00 34.94 ?  11  LYS   B HG2  1 
ATOM   4063 H  HG3  . LYS   B 1 11  ? 34.262 -26.995 -18.365 1.00 34.94 ?  11  LYS   B HG3  1 
ATOM   4064 H  HD2  . LYS   B 1 11  ? 33.801 -27.213 -20.684 1.00 38.37 ?  11  LYS   B HD2  1 
ATOM   4065 H  HD3  . LYS   B 1 11  ? 32.683 -28.285 -20.320 1.00 38.37 ?  11  LYS   B HD3  1 
ATOM   4066 H  HE2  . LYS   B 1 11  ? 31.576 -26.328 -20.616 1.00 40.99 ?  11  LYS   B HE2  1 
ATOM   4067 H  HE3  . LYS   B 1 11  ? 31.611 -26.563 -19.043 1.00 40.99 ?  11  LYS   B HE3  1 
ATOM   4068 H  HZ1  . LYS   B 1 11  ? 32.184 -24.418 -19.549 1.00 42.41 ?  11  LYS   B HZ1  1 
ATOM   4069 H  HZ2  . LYS   B 1 11  ? 33.325 -25.066 -18.933 1.00 42.41 ?  11  LYS   B HZ2  1 
ATOM   4070 H  HZ3  . LYS   B 1 11  ? 33.296 -24.859 -20.367 1.00 42.41 ?  11  LYS   B HZ3  1 
ATOM   4071 N  N    . LEU   B 1 12  ? 34.595 -29.749 -15.649 1.00 17.64 ?  12  LEU   B N    1 
ATOM   4072 C  CA   . LEU   B 1 12  ? 33.636 -30.447 -14.800 1.00 17.02 ?  12  LEU   B CA   1 
ATOM   4073 C  C    . LEU   B 1 12  ? 32.250 -29.830 -14.881 1.00 17.26 ?  12  LEU   B C    1 
ATOM   4074 O  O    . LEU   B 1 12  ? 31.261 -30.545 -15.045 1.00 18.31 ?  12  LEU   B O    1 
ATOM   4075 C  CB   . LEU   B 1 12  ? 34.108 -30.473 -13.343 1.00 16.59 ?  12  LEU   B CB   1 
ATOM   4076 C  CG   . LEU   B 1 12  ? 35.446 -31.162 -13.083 1.00 16.73 ?  12  LEU   B CG   1 
ATOM   4077 C  CD1  . LEU   B 1 12  ? 35.775 -31.135 -11.602 1.00 16.70 ?  12  LEU   B CD1  1 
ATOM   4078 C  CD2  . LEU   B 1 12  ? 35.444 -32.592 -13.614 1.00 17.75 ?  12  LEU   B CD2  1 
ATOM   4079 H  H    . LEU   B 1 12  ? 34.924 -29.038 -15.287 1.00 21.18 ?  12  LEU   B H    1 
ATOM   4080 H  HA   . LEU   B 1 12  ? 33.558 -31.362 -15.104 1.00 20.43 ?  12  LEU   B HA   1 
ATOM   4081 H  HB2  . LEU   B 1 12  ? 34.186 -29.559 -13.031 1.00 19.91 ?  12  LEU   B HB2  1 
ATOM   4082 H  HB3  . LEU   B 1 12  ? 33.438 -30.937 -12.814 1.00 19.91 ?  12  LEU   B HB3  1 
ATOM   4083 H  HG   . LEU   B 1 12  ? 36.143 -30.672 -13.548 1.00 20.08 ?  12  LEU   B HG   1 
ATOM   4084 H  HD11 . LEU   B 1 12  ? 36.631 -31.576 -11.461 1.00 20.05 ?  12  LEU   B HD11 1 
ATOM   4085 H  HD12 . LEU   B 1 12  ? 35.826 -30.215 -11.302 1.00 20.05 ?  12  LEU   B HD12 1 
ATOM   4086 H  HD13 . LEU   B 1 12  ? 35.080 -31.605 -11.114 1.00 20.05 ?  12  LEU   B HD13 1 
ATOM   4087 H  HD21 . LEU   B 1 12  ? 36.246 -33.044 -13.310 1.00 21.30 ?  12  LEU   B HD21 1 
ATOM   4088 H  HD22 . LEU   B 1 12  ? 34.658 -33.053 -13.282 1.00 21.30 ?  12  LEU   B HD22 1 
ATOM   4089 H  HD23 . LEU   B 1 12  ? 35.427 -32.570 -14.585 1.00 21.30 ?  12  LEU   B HD23 1 
ATOM   4090 N  N    . THR   B 1 13  ? 32.166 -28.511 -14.764 1.00 17.05 ?  13  THR   B N    1 
ATOM   4091 C  CA   . THR   B 1 13  ? 30.939 -27.760 -14.962 1.00 17.04 ?  13  THR   B CA   1 
ATOM   4092 C  C    . THR   B 1 13  ? 31.278 -26.565 -15.848 1.00 19.52 ?  13  THR   B C    1 
ATOM   4093 O  O    . THR   B 1 13  ? 32.423 -26.384 -16.276 1.00 20.46 ?  13  THR   B O    1 
ATOM   4094 C  CB   . THR   B 1 13  ? 30.353 -27.282 -13.629 1.00 16.70 ?  13  THR   B CB   1 
ATOM   4095 O  OG1  . THR   B 1 13  ? 31.216 -26.280 -13.076 1.00 16.19 ?  13  THR   B OG1  1 
ATOM   4096 C  CG2  . THR   B 1 13  ? 30.222 -28.439 -12.645 1.00 17.51 ?  13  THR   B CG2  1 
ATOM   4097 H  H    . THR   B 1 13  ? 32.838 -28.009 -14.564 1.00 20.46 ?  13  THR   B H    1 
ATOM   4098 H  HA   . THR   B 1 13  ? 30.282 -28.311 -15.410 1.00 20.46 ?  13  THR   B HA   1 
ATOM   4099 H  HB   . THR   B 1 13  ? 29.464 -26.907 -13.779 1.00 20.04 ?  13  THR   B HB   1 
ATOM   4100 H  HG1  . THR   B 1 13  ? 30.939 -25.513 -13.295 1.00 19.44 ?  13  THR   B HG1  1 
ATOM   4101 H  HG21 . THR   B 1 13  ? 29.736 -28.154 -11.855 1.00 21.02 ?  13  THR   B HG21 1 
ATOM   4102 H  HG22 . THR   B 1 13  ? 29.742 -29.175 -13.058 1.00 21.02 ?  13  THR   B HG22 1 
ATOM   4103 H  HG23 . THR   B 1 13  ? 31.102 -28.748 -12.379 1.00 21.02 ?  13  THR   B HG23 1 
ATOM   4104 N  N    A ASP   B 1 14  ? 30.272 -25.736 -16.121 0.66 20.72 ?  14  ASP   B N    1 
ATOM   4105 N  N    B ASP   B 1 14  ? 30.275 -25.723 -16.108 0.34 20.39 ?  14  ASP   B N    1 
ATOM   4106 C  CA   A ASP   B 1 14  ? 30.504 -24.579 -16.977 0.66 22.40 ?  14  ASP   B CA   1 
ATOM   4107 C  CA   B ASP   B 1 14  ? 30.484 -24.568 -16.976 0.34 21.48 ?  14  ASP   B CA   1 
ATOM   4108 C  C    A ASP   B 1 14  ? 31.620 -23.692 -16.438 0.66 20.51 ?  14  ASP   B C    1 
ATOM   4109 C  C    B ASP   B 1 14  ? 31.489 -23.573 -16.410 0.34 19.80 ?  14  ASP   B C    1 
ATOM   4110 O  O    A ASP   B 1 14  ? 32.336 -23.056 -17.223 0.66 21.40 ?  14  ASP   B O    1 
ATOM   4111 O  O    B ASP   B 1 14  ? 31.953 -22.699 -17.150 0.34 20.11 ?  14  ASP   B O    1 
ATOM   4112 C  CB   A ASP   B 1 14  ? 29.209 -23.785 -17.153 0.66 26.03 ?  14  ASP   B CB   1 
ATOM   4113 C  CB   B ASP   B 1 14  ? 29.164 -23.843 -17.228 0.34 24.21 ?  14  ASP   B CB   1 
ATOM   4114 C  CG   A ASP   B 1 14  ? 28.219 -24.475 -18.064 0.66 29.29 ?  14  ASP   B CG   1 
ATOM   4115 C  CG   B ASP   B 1 14  ? 28.274 -24.580 -18.209 0.34 26.60 ?  14  ASP   B CG   1 
ATOM   4116 O  OD1  A ASP   B 1 14  ? 28.591 -25.467 -18.730 0.66 30.36 ?  14  ASP   B OD1  1 
ATOM   4117 O  OD1  B ASP   B 1 14  ? 28.815 -25.267 -19.102 0.34 27.46 ?  14  ASP   B OD1  1 
ATOM   4118 O  OD2  A ASP   B 1 14  ? 27.059 -24.021 -18.107 0.66 30.66 -1 14  ASP   B OD2  1 
ATOM   4119 O  OD2  B ASP   B 1 14  ? 27.037 -24.477 -18.089 0.34 27.36 -1 14  ASP   B OD2  1 
ATOM   4120 H  H    A ASP   B 1 14  ? 29.471 -25.811 -15.821 0.66 24.87 ?  14  ASP   B H    1 
ATOM   4121 H  H    B ASP   B 1 14  ? 29.477 -25.796 -15.798 0.34 24.48 ?  14  ASP   B H    1 
ATOM   4122 H  HA   A ASP   B 1 14  ? 30.785 -24.884 -17.848 0.66 26.89 ?  14  ASP   B HA   1 
ATOM   4123 H  HA   B ASP   B 1 14  ? 30.820 -24.879 -17.831 0.34 25.78 ?  14  ASP   B HA   1 
ATOM   4124 H  HB2  A ASP   B 1 14  ? 28.774 -23.680 -16.297 0.66 31.25 ?  14  ASP   B HB2  1 
ATOM   4125 H  HB2  B ASP   B 1 14  ? 28.686 -23.760 -16.388 0.34 29.06 ?  14  ASP   B HB2  1 
ATOM   4126 H  HB3  A ASP   B 1 14  ? 29.411 -22.921 -17.540 0.66 31.25 ?  14  ASP   B HB3  1 
ATOM   4127 H  HB3  B ASP   B 1 14  ? 29.358 -22.957 -17.584 0.34 29.06 ?  14  ASP   B HB3  1 
ATOM   4128 N  N    . ASN   B 1 15  ? 31.810 -23.657 -15.115 1.00 18.15 ?  15  ASN   B N    1 
ATOM   4129 C  CA   . ASN   B 1 15  ? 32.776 -22.745 -14.509 1.00 15.62 ?  15  ASN   B CA   1 
ATOM   4130 C  C    . ASN   B 1 15  ? 33.873 -23.408 -13.684 1.00 14.08 ?  15  ASN   B C    1 
ATOM   4131 O  O    . ASN   B 1 15  ? 34.741 -22.689 -13.177 1.00 14.41 ?  15  ASN   B O    1 
ATOM   4132 C  CB   . ASN   B 1 15  ? 32.070 -21.691 -13.640 1.00 16.06 ?  15  ASN   B CB   1 
ATOM   4133 C  CG   . ASN   B 1 15  ? 31.449 -22.290 -12.398 1.00 15.33 ?  15  ASN   B CG   1 
ATOM   4134 O  OD1  . ASN   B 1 15  ? 30.500 -23.080 -12.483 1.00 17.10 ?  15  ASN   B OD1  1 
ATOM   4135 N  ND2  . ASN   B 1 15  ? 31.981 -21.948 -11.242 1.00 14.36 ?  15  ASN   B ND2  1 
ATOM   4136 H  H    A ASN   B 1 15  ? 31.392 -24.154 -14.550 0.66 21.79 ?  15  ASN   B H    1 
ATOM   4137 H  H    B ASN   B 1 15  ? 31.452 -24.208 -14.562 0.34 21.79 ?  15  ASN   B H    1 
ATOM   4138 H  HA   . ASN   B 1 15  ? 33.221 -22.257 -15.214 1.00 18.75 ?  15  ASN   B HA   1 
ATOM   4139 H  HB2  . ASN   B 1 15  ? 32.718 -21.016 -13.366 1.00 19.28 ?  15  ASN   B HB2  1 
ATOM   4140 H  HB3  . ASN   B 1 15  ? 31.361 -21.267 -14.156 1.00 19.28 ?  15  ASN   B HB3  1 
ATOM   4141 H  HD21 . ASN   B 1 15  ? 31.664 -22.261 -10.507 1.00 17.23 ?  15  ASN   B HD21 1 
ATOM   4142 H  HD22 . ASN   B 1 15  ? 32.648 -21.394 -11.213 1.00 17.23 ?  15  ASN   B HD22 1 
ATOM   4143 N  N    . VAL   B 1 16  ? 33.864 -24.727 -13.512 1.00 14.01 ?  16  VAL   B N    1 
ATOM   4144 C  CA   . VAL   B 1 16  ? 34.872 -25.422 -12.716 1.00 13.77 ?  16  VAL   B CA   1 
ATOM   4145 C  C    . VAL   B 1 16  ? 35.655 -26.356 -13.623 1.00 13.82 ?  16  VAL   B C    1 
ATOM   4146 O  O    . VAL   B 1 16  ? 35.071 -27.236 -14.275 1.00 14.88 ?  16  VAL   B O    1 
ATOM   4147 C  CB   . VAL   B 1 16  ? 34.256 -26.196 -11.540 1.00 13.74 ?  16  VAL   B CB   1 
ATOM   4148 C  CG1  . VAL   B 1 16  ? 35.355 -26.926 -10.755 1.00 14.36 ?  16  VAL   B CG1  1 
ATOM   4149 C  CG2  . VAL   B 1 16  ? 33.460 -25.261 -10.637 1.00 14.64 ?  16  VAL   B CG2  1 
ATOM   4150 H  H    . VAL   B 1 16  ? 33.264 -25.248 -13.846 1.00 16.82 ?  16  VAL   B H    1 
ATOM   4151 H  HA   . VAL   B 1 16  ? 35.489 -24.768 -12.347 1.00 16.53 ?  16  VAL   B HA   1 
ATOM   4152 H  HB   . VAL   B 1 16  ? 33.647 -26.864 -11.887 1.00 16.49 ?  16  VAL   B HB   1 
ATOM   4153 H  HG11 . VAL   B 1 16  ? 34.987 -27.228 -9.909  1.00 17.24 ?  16  VAL   B HG11 1 
ATOM   4154 H  HG12 . VAL   B 1 16  ? 35.665 -27.682 -11.270 1.00 17.24 ?  16  VAL   B HG12 1 
ATOM   4155 H  HG13 . VAL   B 1 16  ? 36.086 -26.308 -10.591 1.00 17.24 ?  16  VAL   B HG13 1 
ATOM   4156 H  HG21 . VAL   B 1 16  ? 33.132 -25.762 -9.873  1.00 17.57 ?  16  VAL   B HG21 1 
ATOM   4157 H  HG22 . VAL   B 1 16  ? 34.035 -24.541 -10.339 1.00 17.57 ?  16  VAL   B HG22 1 
ATOM   4158 H  HG23 . VAL   B 1 16  ? 32.711 -24.900 -11.140 1.00 17.57 ?  16  VAL   B HG23 1 
ATOM   4159 N  N    . TYR   B 1 17  ? 36.977 -26.183 -13.624 1.00 14.20 ?  17  TYR   B N    1 
ATOM   4160 C  CA   . TYR   B 1 17  ? 37.910 -26.946 -14.434 1.00 14.51 ?  17  TYR   B CA   1 
ATOM   4161 C  C    . TYR   B 1 17  ? 38.968 -27.555 -13.525 1.00 13.52 ?  17  TYR   B C    1 
ATOM   4162 O  O    . TYR   B 1 17  ? 39.255 -27.025 -12.446 1.00 14.28 ?  17  TYR   B O    1 
ATOM   4163 C  CB   . TYR   B 1 17  ? 38.617 -26.035 -15.447 1.00 18.20 ?  17  TYR   B CB   1 
ATOM   4164 C  CG   . TYR   B 1 17  ? 37.689 -25.252 -16.345 1.00 21.86 ?  17  TYR   B CG   1 
ATOM   4165 C  CD1  . TYR   B 1 17  ? 37.149 -24.037 -15.939 1.00 23.77 ?  17  TYR   B CD1  1 
ATOM   4166 C  CD2  . TYR   B 1 17  ? 37.358 -25.727 -17.606 1.00 24.23 ?  17  TYR   B CD2  1 
ATOM   4167 C  CE1  . TYR   B 1 17  ? 36.302 -23.317 -16.763 1.00 25.66 ?  17  TYR   B CE1  1 
ATOM   4168 C  CE2  . TYR   B 1 17  ? 36.515 -25.015 -18.438 1.00 26.13 ?  17  TYR   B CE2  1 
ATOM   4169 C  CZ   . TYR   B 1 17  ? 35.987 -23.812 -18.009 1.00 27.08 ?  17  TYR   B CZ   1 
ATOM   4170 O  OH   . TYR   B 1 17  ? 35.149 -23.100 -18.833 1.00 28.60 ?  17  TYR   B OH   1 
ATOM   4171 H  H    . TYR   B 1 17  ? 37.374 -25.588 -13.138 1.00 17.05 ?  17  TYR   B H    1 
ATOM   4172 H  HA   . TYR   B 1 17  ? 37.439 -27.653 -14.909 1.00 17.42 ?  17  TYR   B HA   1 
ATOM   4173 H  HB2  . TYR   B 1 17  ? 39.175 -25.404 -14.972 1.00 21.85 ?  17  TYR   B HB2  1 
ATOM   4174 H  HB3  . TYR   B 1 17  ? 39.160 -26.590 -16.023 1.00 21.85 ?  17  TYR   B HB3  1 
ATOM   4175 H  HD1  . TYR   B 1 17  ? 37.364 -23.701 -15.100 1.00 28.53 ?  17  TYR   B HD1  1 
ATOM   4176 H  HD2  . TYR   B 1 17  ? 37.704 -26.536 -17.901 1.00 29.09 ?  17  TYR   B HD2  1 
ATOM   4177 H  HE1  . TYR   B 1 17  ? 35.950 -22.504 -16.478 1.00 30.80 ?  17  TYR   B HE1  1 
ATOM   4178 H  HE2  . TYR   B 1 17  ? 36.293 -25.346 -19.282 1.00 31.36 ?  17  TYR   B HE2  1 
ATOM   4179 H  HH   . TYR   B 1 17  ? 35.035 -23.510 -19.558 1.00 34.32 ?  17  TYR   B HH   1 
ATOM   4180 N  N    . ILE   B 1 18  ? 39.574 -28.659 -13.968 1.00 13.71 ?  18  ILE   B N    1 
ATOM   4181 C  CA   . ILE   B 1 18  ? 40.512 -29.387 -13.121 1.00 13.96 ?  18  ILE   B CA   1 
ATOM   4182 C  C    . ILE   B 1 18  ? 41.666 -29.936 -13.953 1.00 14.64 ?  18  ILE   B C    1 
ATOM   4183 O  O    . ILE   B 1 18  ? 41.497 -30.323 -15.114 1.00 15.56 ?  18  ILE   B O    1 
ATOM   4184 C  CB   . ILE   B 1 18  ? 39.767 -30.493 -12.324 1.00 14.31 ?  18  ILE   B CB   1 
ATOM   4185 C  CG1  . ILE   B 1 18  ? 40.611 -31.037 -11.169 1.00 14.72 ?  18  ILE   B CG1  1 
ATOM   4186 C  CG2  . ILE   B 1 18  ? 39.282 -31.626 -13.241 1.00 14.43 ?  18  ILE   B CG2  1 
ATOM   4187 C  CD1  . ILE   B 1 18  ? 39.798 -31.868 -10.185 1.00 16.55 ?  18  ILE   B CD1  1 
ATOM   4188 H  H    . ILE   B 1 18  ? 39.459 -29.001 -14.750 1.00 16.46 ?  18  ILE   B H    1 
ATOM   4189 H  HA   . ILE   B 1 18  ? 40.879 -28.771 -12.469 1.00 16.75 ?  18  ILE   B HA   1 
ATOM   4190 H  HB   . ILE   B 1 18  ? 38.973 -30.093 -11.929 1.00 17.18 ?  18  ILE   B HB   1 
ATOM   4191 H  HG12 . ILE   B 1 18  ? 41.313 -31.596 -11.521 1.00 17.67 ?  18  ILE   B HG12 1 
ATOM   4192 H  HG13 . ILE   B 1 18  ? 40.990 -30.289 -10.677 1.00 17.67 ?  18  ILE   B HG13 1 
ATOM   4193 H  HG21 . ILE   B 1 18  ? 38.683 -32.208 -12.742 1.00 17.32 ?  18  ILE   B HG21 1 
ATOM   4194 H  HG22 . ILE   B 1 18  ? 38.812 -31.240 -13.994 1.00 17.32 ?  18  ILE   B HG22 1 
ATOM   4195 H  HG23 . ILE   B 1 18  ? 40.049 -32.132 -13.551 1.00 17.32 ?  18  ILE   B HG23 1 
ATOM   4196 H  HD11 . ILE   B 1 18  ? 40.363 -32.117 -9.436  1.00 19.86 ?  18  ILE   B HD11 1 
ATOM   4197 H  HD12 . ILE   B 1 18  ? 39.045 -31.342 -9.868  1.00 19.86 ?  18  ILE   B HD12 1 
ATOM   4198 H  HD13 . ILE   B 1 18  ? 39.476 -32.666 -10.634 1.00 19.86 ?  18  ILE   B HD13 1 
ATOM   4199 N  N    . LYS   B 1 19  ? 42.851 -29.978 -13.343 1.00 15.07 ?  19  LYS   B N    1 
ATOM   4200 C  CA   . LYS   B 1 19  ? 44.052 -30.453 -14.013 1.00 16.06 ?  19  LYS   B CA   1 
ATOM   4201 C  C    . LYS   B 1 19  ? 44.961 -31.126 -12.997 1.00 15.83 ?  19  LYS   B C    1 
ATOM   4202 O  O    . LYS   B 1 19  ? 45.047 -30.698 -11.843 1.00 15.31 ?  19  LYS   B O    1 
ATOM   4203 C  CB   . LYS   B 1 19  ? 44.814 -29.290 -14.660 1.00 17.57 ?  19  LYS   B CB   1 
ATOM   4204 C  CG   . LYS   B 1 19  ? 45.997 -29.697 -15.527 1.00 20.24 ?  19  LYS   B CG   1 
ATOM   4205 C  CD   . LYS   B 1 19  ? 46.705 -28.464 -16.072 1.00 22.69 ?  19  LYS   B CD   1 
ATOM   4206 C  CE   . LYS   B 1 19  ? 47.892 -28.826 -16.944 1.00 25.39 ?  19  LYS   B CE   1 
ATOM   4207 N  NZ   . LYS   B 1 19  ? 48.595 -27.616 -17.453 1.00 26.88 ?  19  LYS   B NZ   1 
ATOM   4208 H  H    . LYS   B 1 19  ? 42.975 -29.726 -12.529 1.00 18.09 ?  19  LYS   B H    1 
ATOM   4209 H  HA   . LYS   B 1 19  ? 43.804 -31.094 -14.701 1.00 19.28 ?  19  LYS   B HA   1 
ATOM   4210 H  HB2  . LYS   B 1 19  ? 44.199 -28.793 -15.220 1.00 21.09 ?  19  LYS   B HB2  1 
ATOM   4211 H  HB3  . LYS   B 1 19  ? 45.147 -28.714 -13.952 1.00 21.09 ?  19  LYS   B HB3  1 
ATOM   4212 H  HG2  . LYS   B 1 19  ? 46.624 -30.208 -14.995 1.00 24.29 ?  19  LYS   B HG2  1 
ATOM   4213 H  HG3  . LYS   B 1 19  ? 45.674 -30.227 -16.275 1.00 24.29 ?  19  LYS   B HG3  1 
ATOM   4214 H  HD2  . LYS   B 1 19  ? 46.079 -27.947 -16.605 1.00 27.23 ?  19  LYS   B HD2  1 
ATOM   4215 H  HD3  . LYS   B 1 19  ? 47.026 -27.929 -15.327 1.00 27.23 ?  19  LYS   B HD3  1 
ATOM   4216 H  HE2  . LYS   B 1 19  ? 48.522 -29.349 -16.424 1.00 30.47 ?  19  LYS   B HE2  1 
ATOM   4217 H  HE3  . LYS   B 1 19  ? 47.581 -29.341 -17.706 1.00 30.47 ?  19  LYS   B HE3  1 
ATOM   4218 H  HZ1  . LYS   B 1 19  ? 49.268 -27.855 -17.985 1.00 32.26 ?  19  LYS   B HZ1  1 
ATOM   4219 H  HZ2  . LYS   B 1 19  ? 48.030 -27.106 -17.916 1.00 32.26 ?  19  LYS   B HZ2  1 
ATOM   4220 H  HZ3  . LYS   B 1 19  ? 48.920 -27.143 -16.773 1.00 32.26 ?  19  LYS   B HZ3  1 
ATOM   4221 N  N    . ASN   B 1 20  ? 45.633 -32.189 -13.433 1.00 16.76 ?  20  ASN   B N    1 
ATOM   4222 C  CA   . ASN   B 1 20  ? 46.676 -32.819 -12.632 1.00 17.96 ?  20  ASN   B CA   1 
ATOM   4223 C  C    . ASN   B 1 20  ? 47.949 -31.998 -12.808 1.00 18.58 ?  20  ASN   B C    1 
ATOM   4224 O  O    . ASN   B 1 20  ? 48.590 -32.059 -13.864 1.00 20.84 ?  20  ASN   B O    1 
ATOM   4225 C  CB   . ASN   B 1 20  ? 46.860 -34.264 -13.093 1.00 19.87 ?  20  ASN   B CB   1 
ATOM   4226 C  CG   . ASN   B 1 20  ? 48.016 -34.977 -12.400 1.00 21.82 ?  20  ASN   B CG   1 
ATOM   4227 O  OD1  . ASN   B 1 20  ? 48.693 -35.811 -13.012 1.00 23.94 ?  20  ASN   B OD1  1 
ATOM   4228 N  ND2  . ASN   B 1 20  ? 48.242 -34.671 -11.129 1.00 21.43 ?  20  ASN   B ND2  1 
ATOM   4229 H  H    . ASN   B 1 20  ? 45.492 -32.565 -14.194 1.00 20.12 ?  20  ASN   B H    1 
ATOM   4230 H  HA   . ASN   B 1 20  ? 46.406 -32.816 -11.697 1.00 21.56 ?  20  ASN   B HA   1 
ATOM   4231 H  HB2  . ASN   B 1 20  ? 46.044 -34.762 -12.908 1.00 23.85 ?  20  ASN   B HB2  1 
ATOM   4232 H  HB3  . ASN   B 1 20  ? 47.032 -34.266 -14.048 1.00 23.85 ?  20  ASN   B HB3  1 
ATOM   4233 H  HD21 . ASN   B 1 20  ? 48.884 -35.046 -10.704 1.00 25.72 ?  20  ASN   B HD21 1 
ATOM   4234 H  HD22 . ASN   B 1 20  ? 47.747 -34.086 -10.727 1.00 25.72 ?  20  ASN   B HD22 1 
ATOM   4235 N  N    . ALA   B 1 21  ? 48.309 -31.219 -11.788 1.00 17.79 ?  21  ALA   B N    1 
ATOM   4236 C  CA   . ALA   B 1 21  ? 49.419 -30.289 -11.933 1.00 18.46 ?  21  ALA   B CA   1 
ATOM   4237 C  C    . ALA   B 1 21  ? 49.889 -29.796 -10.571 1.00 17.30 ?  21  ALA   B C    1 
ATOM   4238 O  O    . ALA   B 1 21  ? 49.150 -29.821 -9.583  1.00 17.21 ?  21  ALA   B O    1 
ATOM   4239 C  CB   . ALA   B 1 21  ? 49.015 -29.111 -12.816 1.00 19.78 ?  21  ALA   B CB   1 
ATOM   4240 H  H    . ALA   B 1 21  ? 47.928 -31.217 -11.012 1.00 21.35 ?  21  ALA   B H    1 
ATOM   4241 H  HA   . ALA   B 1 21  ? 50.156 -30.755 -12.360 1.00 22.15 ?  21  ALA   B HA   1 
ATOM   4242 H  HB1  . ALA   B 1 21  ? 49.806 -28.595 -13.003 1.00 23.74 ?  21  ALA   B HB1  1 
ATOM   4243 H  HB2  . ALA   B 1 21  ? 48.638 -29.460 -13.639 1.00 23.74 ?  21  ALA   B HB2  1 
ATOM   4244 H  HB3  . ALA   B 1 21  ? 48.356 -28.583 -12.346 1.00 23.74 ?  21  ALA   B HB3  1 
ATOM   4245 N  N    . ASP   B 1 22  ? 51.152 -29.358 -10.552 1.00 16.82 ?  22  ASP   B N    1 
ATOM   4246 C  CA   . ASP   B 1 22  ? 51.776 -28.676 -9.423  1.00 15.81 ?  22  ASP   B CA   1 
ATOM   4247 C  C    . ASP   B 1 22  ? 51.371 -27.204 -9.486  1.00 14.61 ?  22  ASP   B C    1 
ATOM   4248 O  O    . ASP   B 1 22  ? 51.680 -26.521 -10.466 1.00 14.75 ?  22  ASP   B O    1 
ATOM   4249 C  CB   . ASP   B 1 22  ? 53.291 -28.856 -9.597  1.00 17.05 ?  22  ASP   B CB   1 
ATOM   4250 C  CG   . ASP   B 1 22  ? 54.133 -28.101 -8.575  1.00 18.70 ?  22  ASP   B CG   1 
ATOM   4251 O  OD1  . ASP   B 1 22  ? 53.769 -26.994 -8.156  1.00 18.78 ?  22  ASP   B OD1  1 
ATOM   4252 O  OD2  . ASP   B 1 22  ? 55.214 -28.620 -8.215  1.00 21.42 -1 22  ASP   B OD2  1 
ATOM   4253 H  H    . ASP   B 1 22  ? 51.691 -29.457 -11.220 1.00 20.19 ?  22  ASP   B H    1 
ATOM   4254 H  HA   . ASP   B 1 22  ? 51.490 -29.072 -8.581  1.00 18.97 ?  22  ASP   B HA   1 
ATOM   4255 H  HB2  . ASP   B 1 22  ? 53.510 -29.793 -9.521  1.00 20.47 ?  22  ASP   B HB2  1 
ATOM   4256 H  HB3  . ASP   B 1 22  ? 53.540 -28.526 -10.476 1.00 20.47 ?  22  ASP   B HB3  1 
ATOM   4257 N  N    . ILE   B 1 23  ? 50.666 -26.717 -8.455  1.00 14.03 ?  23  ILE   B N    1 
ATOM   4258 C  CA   . ILE   B 1 23  ? 50.076 -25.374 -8.508  1.00 13.35 ?  23  ILE   B CA   1 
ATOM   4259 C  C    . ILE   B 1 23  ? 51.135 -24.287 -8.633  1.00 12.63 ?  23  ILE   B C    1 
ATOM   4260 O  O    . ILE   B 1 23  ? 50.874 -23.235 -9.225  1.00 12.33 ?  23  ILE   B O    1 
ATOM   4261 C  CB   . ILE   B 1 23  ? 49.144 -25.143 -7.303  1.00 13.52 ?  23  ILE   B CB   1 
ATOM   4262 C  CG1  . ILE   B 1 23  ? 48.319 -23.869 -7.485  1.00 13.96 ?  23  ILE   B CG1  1 
ATOM   4263 C  CG2  . ILE   B 1 23  ? 49.923 -25.117 -6.004  1.00 14.09 ?  23  ILE   B CG2  1 
ATOM   4264 C  CD1  . ILE   B 1 23  ? 47.198 -23.728 -6.471  1.00 14.80 ?  23  ILE   B CD1  1 
ATOM   4265 H  H    . ILE   B 1 23  ? 50.517 -27.144 -7.726  1.00 16.84 ?  23  ILE   B H    1 
ATOM   4266 H  HA   . ILE   B 1 23  ? 49.526 -25.323 -9.305  1.00 16.03 ?  23  ILE   B HA   1 
ATOM   4267 H  HB   . ILE   B 1 23  ? 48.527 -25.890 -7.265  1.00 16.23 ?  23  ILE   B HB   1 
ATOM   4268 H  HG12 . ILE   B 1 23  ? 48.907 -23.101 -7.394  1.00 16.76 ?  23  ILE   B HG12 1 
ATOM   4269 H  HG13 . ILE   B 1 23  ? 47.925 -23.875 -8.374  1.00 16.76 ?  23  ILE   B HG13 1 
ATOM   4270 H  HG21 . ILE   B 1 23  ? 49.297 -25.131 -5.264  1.00 16.91 ?  23  ILE   B HG21 1 
ATOM   4271 H  HG22 . ILE   B 1 23  ? 50.499 -25.896 -5.966  1.00 16.91 ?  23  ILE   B HG22 1 
ATOM   4272 H  HG23 . ILE   B 1 23  ? 50.457 -24.308 -5.973  1.00 16.91 ?  23  ILE   B HG23 1 
ATOM   4273 H  HD11 . ILE   B 1 23  ? 46.670 -22.946 -6.693  1.00 17.76 ?  23  ILE   B HD11 1 
ATOM   4274 H  HD12 . ILE   B 1 23  ? 46.642 -24.523 -6.507  1.00 17.76 ?  23  ILE   B HD12 1 
ATOM   4275 H  HD13 . ILE   B 1 23  ? 47.582 -23.631 -5.588  1.00 17.76 ?  23  ILE   B HD13 1 
ATOM   4276 N  N    . VAL   B 1 24  ? 52.330 -24.504 -8.078  1.00 13.25 ?  24  VAL   B N    1 
ATOM   4277 C  CA   . VAL   B 1 24  ? 53.408 -23.523 -8.233  1.00 13.46 ?  24  VAL   B CA   1 
ATOM   4278 C  C    . VAL   B 1 24  ? 53.863 -23.465 -9.685  1.00 13.84 ?  24  VAL   B C    1 
ATOM   4279 O  O    . VAL   B 1 24  ? 53.990 -22.383 -10.273 1.00 14.43 ?  24  VAL   B O    1 
ATOM   4280 C  CB   . VAL   B 1 24  ? 54.586 -23.844 -7.290  1.00 14.34 ?  24  VAL   B CB   1 
ATOM   4281 C  CG1  . VAL   B 1 24  ? 55.803 -22.962 -7.615  1.00 15.44 ?  24  VAL   B CG1  1 
ATOM   4282 C  CG2  . VAL   B 1 24  ? 54.173 -23.680 -5.845  1.00 15.65 ?  24  VAL   B CG2  1 
ATOM   4283 H  H    . VAL   B 1 24  ? 52.539 -25.193 -7.616  1.00 15.91 ?  24  VAL   B H    1 
ATOM   4284 H  HA   . VAL   B 1 24  ? 53.070 -22.643 -7.996  1.00 16.16 ?  24  VAL   B HA   1 
ATOM   4285 H  HB   . VAL   B 1 24  ? 54.845 -24.767 -7.419  1.00 17.22 ?  24  VAL   B HB   1 
ATOM   4286 H  HG11 . VAL   B 1 24  ? 56.395 -22.949 -6.846  1.00 18.54 ?  24  VAL   B HG11 1 
ATOM   4287 H  HG12 . VAL   B 1 24  ? 56.267 -23.338 -8.380  1.00 18.54 ?  24  VAL   B HG12 1 
ATOM   4288 H  HG13 . VAL   B 1 24  ? 55.502 -22.063 -7.815  1.00 18.54 ?  24  VAL   B HG13 1 
ATOM   4289 H  HG21 . VAL   B 1 24  ? 54.895 -23.976 -5.274  1.00 18.78 ?  24  VAL   B HG21 1 
ATOM   4290 H  HG22 . VAL   B 1 24  ? 53.980 -22.742 -5.677  1.00 18.78 ?  24  VAL   B HG22 1 
ATOM   4291 H  HG23 . VAL   B 1 24  ? 53.378 -24.213 -5.681  1.00 18.78 ?  24  VAL   B HG23 1 
ATOM   4292 N  N    . GLU   B 1 25  ? 54.139 -24.631 -10.278 1.00 14.62 ?  25  GLU   B N    1 
ATOM   4293 C  CA   . GLU   B 1 25  ? 54.526 -24.659 -11.683 1.00 16.05 ?  25  GLU   B CA   1 
ATOM   4294 C  C    . GLU   B 1 25  ? 53.414 -24.114 -12.566 1.00 15.03 ?  25  GLU   B C    1 
ATOM   4295 O  O    . GLU   B 1 25  ? 53.677 -23.394 -13.538 1.00 16.24 ?  25  GLU   B O    1 
ATOM   4296 C  CB   . GLU   B 1 25  ? 54.922 -26.079 -12.081 1.00 20.69 ?  25  GLU   B CB   1 
ATOM   4297 C  CG   . GLU   B 1 25  ? 56.230 -26.524 -11.431 1.00 26.62 ?  25  GLU   B CG   1 
ATOM   4298 C  CD   . GLU   B 1 25  ? 57.340 -25.485 -11.533 1.00 31.56 ?  25  GLU   B CD   1 
ATOM   4299 O  OE1  . GLU   B 1 25  ? 57.713 -25.115 -12.667 1.00 33.53 ?  25  GLU   B OE1  1 
ATOM   4300 O  OE2  . GLU   B 1 25  ? 57.832 -25.023 -10.475 1.00 33.43 -1 25  GLU   B OE2  1 
ATOM   4301 H  H    . GLU   B 1 25  ? 54.108 -25.396 -9.893  1.00 17.55 ?  25  GLU   B H    1 
ATOM   4302 H  HA   . GLU   B 1 25  ? 55.283 -24.074 -11.809 1.00 19.27 ?  25  GLU   B HA   1 
ATOM   4303 H  HB2  . GLU   B 1 25  ? 54.226 -26.697 -11.799 1.00 24.84 ?  25  GLU   B HB2  1 
ATOM   4304 H  HB3  . GLU   B 1 25  ? 55.031 -26.122 -13.044 1.00 24.84 ?  25  GLU   B HB3  1 
ATOM   4305 H  HG2  . GLU   B 1 25  ? 56.081 -26.678 -10.491 1.00 31.95 ?  25  GLU   B HG2  1 
ATOM   4306 H  HG3  . GLU   B 1 25  ? 56.539 -27.333 -11.865 1.00 31.95 ?  25  GLU   B HG3  1 
ATOM   4307 N  N    A GLU   B 1 26  ? 52.161 -24.434 -12.239 0.66 14.65 ?  26  GLU   B N    1 
ATOM   4308 N  N    B GLU   B 1 26  ? 52.160 -24.436 -12.238 0.34 14.73 ?  26  GLU   B N    1 
ATOM   4309 C  CA   A GLU   B 1 26  ? 51.037 -23.910 -13.008 0.66 15.13 ?  26  GLU   B CA   1 
ATOM   4310 C  CA   B GLU   B 1 26  ? 51.033 -23.914 -13.006 0.34 14.86 ?  26  GLU   B CA   1 
ATOM   4311 C  C    A GLU   B 1 26  ? 50.978 -22.393 -12.923 0.66 14.07 ?  26  GLU   B C    1 
ATOM   4312 C  C    B GLU   B 1 26  ? 50.969 -22.396 -12.921 0.34 13.95 ?  26  GLU   B C    1 
ATOM   4313 O  O    A GLU   B 1 26  ? 50.780 -21.713 -13.935 0.66 15.25 ?  26  GLU   B O    1 
ATOM   4314 O  O    B GLU   B 1 26  ? 50.772 -21.715 -13.934 0.34 14.63 ?  26  GLU   B O    1 
ATOM   4315 C  CB   A GLU   B 1 26  ? 49.724 -24.502 -12.496 0.66 17.19 ?  26  GLU   B CB   1 
ATOM   4316 C  CB   B GLU   B 1 26  ? 49.722 -24.522 -12.502 0.34 16.10 ?  26  GLU   B CB   1 
ATOM   4317 C  CG   A GLU   B 1 26  ? 49.333 -25.820 -13.123 0.66 20.45 ?  26  GLU   B CG   1 
ATOM   4318 C  CG   B GLU   B 1 26  ? 49.236 -25.729 -13.286 0.34 17.96 ?  26  GLU   B CG   1 
ATOM   4319 C  CD   A GLU   B 1 26  ? 49.094 -25.725 -14.626 0.66 21.49 ?  26  GLU   B CD   1 
ATOM   4320 C  CD   B GLU   B 1 26  ? 48.889 -25.395 -14.734 0.34 17.86 ?  26  GLU   B CD   1 
ATOM   4321 O  OE1  A GLU   B 1 26  ? 48.233 -24.936 -15.069 0.66 21.18 ?  26  GLU   B OE1  1 
ATOM   4322 O  OE1  B GLU   B 1 26  ? 47.758 -24.920 -15.001 0.34 18.44 ?  26  GLU   B OE1  1 
ATOM   4323 O  OE2  A GLU   B 1 26  ? 49.775 -26.450 -15.366 0.66 22.72 -1 26  GLU   B OE2  1 
ATOM   4324 O  OE2  B GLU   B 1 26  ? 49.755 -25.611 -15.602 0.34 17.67 -1 26  GLU   B OE2  1 
ATOM   4325 H  H    A GLU   B 1 26  ? 51.935 -24.948 -11.582 0.66 17.58 ?  26  GLU   B H    1 
ATOM   4326 H  H    B GLU   B 1 26  ? 51.937 -24.949 -11.581 0.34 17.68 ?  26  GLU   B H    1 
ATOM   4327 H  HA   A GLU   B 1 26  ? 51.144 -24.160 -13.937 0.66 18.16 ?  26  GLU   B HA   1 
ATOM   4328 H  HA   B GLU   B 1 26  ? 51.146 -24.159 -13.936 0.34 17.83 ?  26  GLU   B HA   1 
ATOM   4329 H  HB2  A GLU   B 1 26  ? 49.800 -24.644 -11.537 0.66 20.64 ?  26  GLU   B HB2  1 
ATOM   4330 H  HB2  B GLU   B 1 26  ? 49.839 -24.797 -11.580 0.34 19.32 ?  26  GLU   B HB2  1 
ATOM   4331 H  HB3  A GLU   B 1 26  ? 49.010 -23.868 -12.671 0.66 20.64 ?  26  GLU   B HB3  1 
ATOM   4332 H  HB3  B GLU   B 1 26  ? 49.028 -23.845 -12.554 0.34 19.32 ?  26  GLU   B HB3  1 
ATOM   4333 H  HG2  A GLU   B 1 26  ? 50.052 -26.445 -12.973 0.66 24.55 ?  26  GLU   B HG2  1 
ATOM   4334 H  HG2  B GLU   B 1 26  ? 49.931 -26.408 -13.260 0.34 21.56 ?  26  GLU   B HG2  1 
ATOM   4335 H  HG3  A GLU   B 1 26  ? 48.517 -26.130 -12.706 0.66 24.55 ?  26  GLU   B HG3  1 
ATOM   4336 H  HG3  B GLU   B 1 26  ? 48.427 -26.064 -12.877 0.34 21.56 ?  26  GLU   B HG3  1 
ATOM   4337 N  N    . ALA   B 1 27  ? 51.116 -21.848 -11.712 1.00 13.09 ?  27  ALA   B N    1 
ATOM   4338 C  CA   . ALA   B 1 27  ? 51.089 -20.398 -11.556 1.00 13.70 ?  27  ALA   B CA   1 
ATOM   4339 C  C    . ALA   B 1 27  ? 52.157 -19.735 -12.416 1.00 14.57 ?  27  ALA   B C    1 
ATOM   4340 O  O    . ALA   B 1 27  ? 51.898 -18.724 -13.086 1.00 15.29 ?  27  ALA   B O    1 
ATOM   4341 C  CB   . ALA   B 1 27  ? 51.257 -20.028 -10.083 1.00 13.53 ?  27  ALA   B CB   1 
ATOM   4342 H  H    A ALA   B 1 27  ? 51.225 -22.289 -10.980 0.66 15.72 ?  27  ALA   B H    1 
ATOM   4343 H  H    B ALA   B 1 27  ? 51.232 -22.288 -10.981 0.34 15.72 ?  27  ALA   B H    1 
ATOM   4344 H  HA   . ALA   B 1 27  ? 50.227 -20.067 -11.846 1.00 16.45 ?  27  ALA   B HA   1 
ATOM   4345 H  HB1  . ALA   B 1 27  ? 51.231 -19.062 -9.994  1.00 16.24 ?  27  ALA   B HB1  1 
ATOM   4346 H  HB2  . ALA   B 1 27  ? 50.532 -20.424 -9.572  1.00 16.24 ?  27  ALA   B HB2  1 
ATOM   4347 H  HB3  . ALA   B 1 27  ? 52.108 -20.366 -9.765  1.00 16.24 ?  27  ALA   B HB3  1 
ATOM   4348 N  N    . LYS   B 1 28  ? 53.368 -20.291 -12.421 1.00 16.31 ?  28  LYS   B N    1 
ATOM   4349 C  CA   . LYS   B 1 28  ? 54.444 -19.667 -13.181 1.00 18.03 ?  28  LYS   B CA   1 
ATOM   4350 C  C    . LYS   B 1 28  ? 54.196 -19.750 -14.681 1.00 18.47 ?  28  LYS   B C    1 
ATOM   4351 O  O    . LYS   B 1 28  ? 54.588 -18.839 -15.418 1.00 20.19 ?  28  LYS   B O    1 
ATOM   4352 C  CB   . LYS   B 1 28  ? 55.802 -20.258 -12.789 1.00 21.61 ?  28  LYS   B CB   1 
ATOM   4353 C  CG   . LYS   B 1 28  ? 56.210 -19.907 -11.359 1.00 24.56 ?  28  LYS   B CG   1 
ATOM   4354 C  CD   . LYS   B 1 28  ? 57.633 -20.334 -11.024 1.00 29.01 ?  28  LYS   B CD   1 
ATOM   4355 C  CE   . LYS   B 1 28  ? 57.709 -21.800 -10.672 1.00 32.80 ?  28  LYS   B CE   1 
ATOM   4356 N  NZ   . LYS   B 1 28  ? 59.072 -22.170 -10.192 1.00 34.27 ?  28  LYS   B NZ   1 
ATOM   4357 H  H    . LYS   B 1 28  ? 53.589 -21.010 -12.005 1.00 19.58 ?  28  LYS   B H    1 
ATOM   4358 H  HA   . LYS   B 1 28  ? 54.470 -18.728 -12.960 1.00 21.65 ?  28  LYS   B HA   1 
ATOM   4359 H  HB2  . LYS   B 1 28  ? 55.764 -21.223 -12.859 1.00 25.93 ?  28  LYS   B HB2  1 
ATOM   4360 H  HB3  . LYS   B 1 28  ? 56.485 -19.908 -13.385 1.00 25.93 ?  28  LYS   B HB3  1 
ATOM   4361 H  HG2  . LYS   B 1 28  ? 56.145 -18.944 -11.242 1.00 29.47 ?  28  LYS   B HG2  1 
ATOM   4362 H  HG3  . LYS   B 1 28  ? 55.606 -20.353 -10.744 1.00 29.47 ?  28  LYS   B HG3  1 
ATOM   4363 H  HD2  . LYS   B 1 28  ? 58.199 -20.174 -11.794 1.00 34.82 ?  28  LYS   B HD2  1 
ATOM   4364 H  HD3  . LYS   B 1 28  ? 57.945 -19.819 -10.264 1.00 34.82 ?  28  LYS   B HD3  1 
ATOM   4365 H  HE2  . LYS   B 1 28  ? 57.073 -21.993 -9.964  1.00 39.37 ?  28  LYS   B HE2  1 
ATOM   4366 H  HE3  . LYS   B 1 28  ? 57.507 -22.331 -11.458 1.00 39.37 ?  28  LYS   B HE3  1 
ATOM   4367 H  HZ1  . LYS   B 1 28  ? 59.098 -23.036 -9.988  1.00 41.13 ?  28  LYS   B HZ1  1 
ATOM   4368 H  HZ2  . LYS   B 1 28  ? 59.673 -22.003 -10.826 1.00 41.13 ?  28  LYS   B HZ2  1 
ATOM   4369 H  HZ3  . LYS   B 1 28  ? 59.278 -21.697 -9.466  1.00 41.13 ?  28  LYS   B HZ3  1 
ATOM   4370 N  N    . LYS   B 1 29  ? 53.502 -20.792 -15.144 1.00 19.73 ?  29  LYS   B N    1 
ATOM   4371 C  CA   . LYS   B 1 29  ? 53.220 -20.933 -16.569 1.00 22.61 ?  29  LYS   B CA   1 
ATOM   4372 C  C    . LYS   B 1 29  ? 51.973 -20.167 -17.008 1.00 21.72 ?  29  LYS   B C    1 
ATOM   4373 O  O    . LYS   B 1 29  ? 51.979 -19.535 -18.070 1.00 23.36 ?  29  LYS   B O    1 
ATOM   4374 C  CB   . LYS   B 1 29  ? 53.079 -22.414 -16.933 1.00 26.87 ?  29  LYS   B CB   1 
ATOM   4375 C  CG   . LYS   B 1 29  ? 52.889 -22.671 -18.418 1.00 31.10 ?  29  LYS   B CG   1 
ATOM   4376 C  CD   . LYS   B 1 29  ? 53.131 -24.135 -18.766 1.00 34.40 ?  29  LYS   B CD   1 
ATOM   4377 C  CE   . LYS   B 1 29  ? 52.061 -25.043 -18.182 1.00 36.66 ?  29  LYS   B CE   1 
ATOM   4378 N  NZ   . LYS   B 1 29  ? 52.310 -26.473 -18.521 1.00 38.12 ?  29  LYS   B NZ   1 
ATOM   4379 H  H    . LYS   B 1 29  ? 53.182 -21.431 -14.653 1.00 23.68 ?  29  LYS   B H    1 
ATOM   4380 H  HA   . LYS   B 1 29  ? 53.973 -20.583 -17.068 1.00 27.14 ?  29  LYS   B HA   1 
ATOM   4381 H  HB2  . LYS   B 1 29  ? 53.886 -22.882 -16.658 1.00 32.25 ?  29  LYS   B HB2  1 
ATOM   4382 H  HB3  . LYS   B 1 29  ? 52.313 -22.781 -16.471 1.00 32.25 ?  29  LYS   B HB3  1 
ATOM   4383 H  HG2  . LYS   B 1 29  ? 51.979 -22.445 -18.666 1.00 37.32 ?  29  LYS   B HG2  1 
ATOM   4384 H  HG3  . LYS   B 1 29  ? 53.518 -22.130 -18.921 1.00 37.32 ?  29  LYS   B HG3  1 
ATOM   4385 H  HD2  . LYS   B 1 29  ? 53.122 -24.239 -19.730 1.00 41.28 ?  29  LYS   B HD2  1 
ATOM   4386 H  HD3  . LYS   B 1 29  ? 53.989 -24.411 -18.408 1.00 41.28 ?  29  LYS   B HD3  1 
ATOM   4387 H  HE2  . LYS   B 1 29  ? 52.058 -24.956 -17.216 1.00 44.00 ?  29  LYS   B HE2  1 
ATOM   4388 H  HE3  . LYS   B 1 29  ? 51.196 -24.791 -18.544 1.00 44.00 ?  29  LYS   B HE3  1 
ATOM   4389 H  HZ1  . LYS   B 1 29  ? 51.672 -26.985 -18.170 1.00 45.75 ?  29  LYS   B HZ1  1 
ATOM   4390 H  HZ2  . LYS   B 1 29  ? 52.313 -26.581 -19.405 1.00 45.75 ?  29  LYS   B HZ2  1 
ATOM   4391 H  HZ3  . LYS   B 1 29  ? 53.098 -26.730 -18.196 1.00 45.75 ?  29  LYS   B HZ3  1 
ATOM   4392 N  N    . VAL   B 1 30  ? 50.904 -20.219 -16.206 1.00 19.92 ?  30  VAL   B N    1 
ATOM   4393 C  CA   . VAL   B 1 30  ? 49.616 -19.631 -16.583 1.00 20.16 ?  30  VAL   B CA   1 
ATOM   4394 C  C    . VAL   B 1 30  ? 49.609 -18.120 -16.414 1.00 18.22 ?  30  VAL   B C    1 
ATOM   4395 O  O    . VAL   B 1 30  ? 48.853 -17.412 -17.097 1.00 19.12 ?  30  VAL   B O    1 
ATOM   4396 C  CB   . VAL   B 1 30  ? 48.509 -20.273 -15.725 1.00 22.24 ?  30  VAL   B CB   1 
ATOM   4397 C  CG1  . VAL   B 1 30  ? 47.222 -19.459 -15.775 1.00 22.56 ?  30  VAL   B CG1  1 
ATOM   4398 C  CG2  . VAL   B 1 30  ? 48.270 -21.714 -16.157 1.00 23.51 ?  30  VAL   B CG2  1 
ATOM   4399 H  H    . VAL   B 1 30  ? 50.898 -20.611 -15.432 1.00 23.91 ?  30  VAL   B H    1 
ATOM   4400 H  HA   . VAL   B 1 30  ? 49.435 -19.852 -17.510 1.00 24.19 ?  30  VAL   B HA   1 
ATOM   4401 H  HB   . VAL   B 1 30  ? 48.802 -20.300 -14.800 1.00 26.70 ?  30  VAL   B HB   1 
ATOM   4402 H  HG11 . VAL   B 1 30  ? 46.484 -20.037 -15.524 1.00 27.08 ?  30  VAL   B HG11 1 
ATOM   4403 H  HG12 . VAL   B 1 30  ? 47.287 -18.723 -15.150 1.00 27.08 ?  30  VAL   B HG12 1 
ATOM   4404 H  HG13 . VAL   B 1 30  ? 47.088 -19.135 -16.675 1.00 27.08 ?  30  VAL   B HG13 1 
ATOM   4405 H  HG21 . VAL   B 1 30  ? 47.576 -22.106 -15.599 1.00 28.21 ?  30  VAL   B HG21 1 
ATOM   4406 H  HG22 . VAL   B 1 30  ? 47.985 -21.724 -17.086 1.00 28.21 ?  30  VAL   B HG22 1 
ATOM   4407 H  HG23 . VAL   B 1 30  ? 49.092 -22.218 -16.059 1.00 28.21 ?  30  VAL   B HG23 1 
ATOM   4408 N  N    . LYS   B 1 31  ? 50.417 -17.614 -15.492 1.00 17.84 ?  31  LYS   B N    1 
ATOM   4409 C  CA   . LYS   B 1 31  ? 50.420 -16.205 -15.123 1.00 18.25 ?  31  LYS   B CA   1 
ATOM   4410 C  C    . LYS   B 1 31  ? 49.021 -15.717 -14.730 1.00 16.20 ?  31  LYS   B C    1 
ATOM   4411 O  O    . LYS   B 1 31  ? 48.479 -14.798 -15.353 1.00 17.24 ?  31  LYS   B O    1 
ATOM   4412 C  CB   . LYS   B 1 31  ? 51.032 -15.353 -16.228 1.00 21.73 ?  31  LYS   B CB   1 
ATOM   4413 C  CG   . LYS   B 1 31  ? 52.459 -15.797 -16.584 1.00 25.00 ?  31  LYS   B CG   1 
ATOM   4414 C  CD   . LYS   B 1 31  ? 53.057 -14.969 -17.703 1.00 28.60 ?  31  LYS   B CD   1 
ATOM   4415 C  CE   . LYS   B 1 31  ? 54.548 -15.209 -17.823 1.00 31.41 ?  31  LYS   B CE   1 
ATOM   4416 N  NZ   . LYS   B 1 31  ? 55.265 -14.791 -16.584 1.00 33.02 ?  31  LYS   B NZ   1 
ATOM   4417 H  H    . LYS   B 1 31  ? 51.000 -18.088 -15.070 1.00 21.42 ?  31  LYS   B H    1 
ATOM   4418 H  HA   . LYS   B 1 31  ? 50.978 -16.115 -14.351 1.00 21.91 ?  31  LYS   B HA   1 
ATOM   4419 H  HB2  . LYS   B 1 31  ? 50.492 -15.421 -17.032 1.00 26.08 ?  31  LYS   B HB2  1 
ATOM   4420 H  HB3  . LYS   B 1 31  ? 51.073 -14.434 -15.928 1.00 26.08 ?  31  LYS   B HB3  1 
ATOM   4421 H  HG2  . LYS   B 1 31  ? 53.021 -15.708 -15.798 1.00 30.00 ?  31  LYS   B HG2  1 
ATOM   4422 H  HG3  . LYS   B 1 31  ? 52.441 -16.727 -16.872 1.00 30.00 ?  31  LYS   B HG3  1 
ATOM   4423 H  HD2  . LYS   B 1 31  ? 52.636 -15.219 -18.539 1.00 34.32 ?  31  LYS   B HD2  1 
ATOM   4424 H  HD3  . LYS   B 1 31  ? 52.909 -14.032 -17.513 1.00 34.32 ?  31  LYS   B HD3  1 
ATOM   4425 H  HE2  . LYS   B 1 31  ? 54.714 -16.155 -17.966 1.00 37.70 ?  31  LYS   B HE2  1 
ATOM   4426 H  HE3  . LYS   B 1 31  ? 54.896 -14.692 -18.566 1.00 37.70 ?  31  LYS   B HE3  1 
ATOM   4427 H  HZ1  . LYS   B 1 31  ? 56.144 -14.814 -16.719 1.00 39.63 ?  31  LYS   B HZ1  1 
ATOM   4428 H  HZ2  . LYS   B 1 31  ? 55.028 -13.962 -16.362 1.00 39.63 ?  31  LYS   B HZ2  1 
ATOM   4429 H  HZ3  . LYS   B 1 31  ? 55.061 -15.339 -15.913 1.00 39.63 ?  31  LYS   B HZ3  1 
ATOM   4430 N  N    . PRO   B 1 32  ? 48.419 -16.307 -13.691 1.00 14.21 ?  32  PRO   B N    1 
ATOM   4431 C  CA   . PRO   B 1 32  ? 47.041 -15.948 -13.332 1.00 13.14 ?  32  PRO   B CA   1 
ATOM   4432 C  C    . PRO   B 1 32  ? 46.966 -14.607 -12.622 1.00 13.29 ?  32  PRO   B C    1 
ATOM   4433 O  O    . PRO   B 1 32  ? 47.900 -14.190 -11.929 1.00 15.08 ?  32  PRO   B O    1 
ATOM   4434 C  CB   . PRO   B 1 32  ? 46.638 -17.064 -12.362 1.00 13.48 ?  32  PRO   B CB   1 
ATOM   4435 C  CG   . PRO   B 1 32  ? 47.933 -17.393 -11.675 1.00 13.65 ?  32  PRO   B CG   1 
ATOM   4436 C  CD   . PRO   B 1 32  ? 48.988 -17.297 -12.752 1.00 14.65 ?  32  PRO   B CD   1 
ATOM   4437 H  HA   . PRO   B 1 32  ? 46.456 -15.961 -14.116 1.00 15.77 ?  32  PRO   B HA   1 
ATOM   4438 H  HB2  . PRO   B 1 32  ? 45.979 -16.732 -11.731 1.00 16.18 ?  32  PRO   B HB2  1 
ATOM   4439 H  HB3  . PRO   B 1 32  ? 46.297 -17.831 -12.851 1.00 16.18 ?  32  PRO   B HB3  1 
ATOM   4440 H  HG2  . PRO   B 1 32  ? 48.103 -16.743 -10.973 1.00 16.39 ?  32  PRO   B HG2  1 
ATOM   4441 H  HG3  . PRO   B 1 32  ? 47.895 -18.289 -11.312 1.00 16.39 ?  32  PRO   B HG3  1 
ATOM   4442 H  HD2  . PRO   B 1 32  ? 49.820 -16.963 -12.384 1.00 17.59 ?  32  PRO   B HD2  1 
ATOM   4443 H  HD3  . PRO   B 1 32  ? 49.105 -18.155 -13.186 1.00 17.59 ?  32  PRO   B HD3  1 
ATOM   4444 N  N    . THR   B 1 33  ? 45.809 -13.953 -12.770 1.00 13.17 ?  33  THR   B N    1 
ATOM   4445 C  CA   . THR   B 1 33  ? 45.525 -12.773 -11.961 1.00 13.62 ?  33  THR   B CA   1 
ATOM   4446 C  C    . THR   B 1 33  ? 45.483 -13.122 -10.480 1.00 13.01 ?  33  THR   B C    1 
ATOM   4447 O  O    . THR   B 1 33  ? 45.964 -12.345 -9.641  1.00 14.02 ?  33  THR   B O    1 
ATOM   4448 C  CB   . THR   B 1 33  ? 44.208 -12.125 -12.395 1.00 13.91 ?  33  THR   B CB   1 
ATOM   4449 O  OG1  . THR   B 1 33  ? 44.236 -11.883 -13.802 1.00 14.14 ?  33  THR   B OG1  1 
ATOM   4450 C  CG2  . THR   B 1 33  ? 43.982 -10.816 -11.659 1.00 14.62 ?  33  THR   B CG2  1 
ATOM   4451 H  H    . THR   B 1 33  ? 45.180 -14.176 -13.321 1.00 15.82 ?  33  THR   B H    1 
ATOM   4452 H  HA   . THR   B 1 33  ? 46.232 -12.131 -12.094 1.00 16.35 ?  33  THR   B HA   1 
ATOM   4453 H  HB   . THR   B 1 33  ? 43.469 -12.725 -12.189 1.00 16.70 ?  33  THR   B HB   1 
ATOM   4454 H  HG1  . THR   B 1 33  ? 43.515 -11.511 -14.046 1.00 16.98 ?  33  THR   B HG1  1 
ATOM   4455 H  HG21 . THR   B 1 33  ? 43.219 -10.352 -12.032 1.00 17.56 ?  33  THR   B HG21 1 
ATOM   4456 H  HG22 . THR   B 1 33  ? 43.816 -10.986 -10.717 1.00 17.56 ?  33  THR   B HG22 1 
ATOM   4457 H  HG23 . THR   B 1 33  ? 44.767 -10.251 -11.742 1.00 17.56 ?  33  THR   B HG23 1 
ATOM   4458 N  N    . VAL   B 1 34  ? 44.925 -14.292 -10.137 1.00 11.93 ?  34  VAL   B N    1 
ATOM   4459 C  CA   . VAL   B 1 34  ? 44.729 -14.691 -8.745  1.00 11.53 ?  34  VAL   B CA   1 
ATOM   4460 C  C    . VAL   B 1 34  ? 45.154 -16.141 -8.581  1.00 10.71 ?  34  VAL   B C    1 
ATOM   4461 O  O    . VAL   B 1 34  ? 44.635 -17.026 -9.272  1.00 11.60 ?  34  VAL   B O    1 
ATOM   4462 C  CB   . VAL   B 1 34  ? 43.267 -14.535 -8.281  1.00 12.79 ?  34  VAL   B CB   1 
ATOM   4463 C  CG1  . VAL   B 1 34  ? 43.124 -14.974 -6.820  1.00 13.29 ?  34  VAL   B CG1  1 
ATOM   4464 C  CG2  . VAL   B 1 34  ? 42.764 -13.107 -8.493  1.00 13.92 ?  34  VAL   B CG2  1 
ATOM   4465 H  H    . VAL   B 1 34  ? 44.658 -14.886 -10.701 1.00 14.32 ?  34  VAL   B H    1 
ATOM   4466 H  HA   . VAL   B 1 34  ? 45.288 -14.148 -8.167  1.00 13.84 ?  34  VAL   B HA   1 
ATOM   4467 H  HB   . VAL   B 1 34  ? 42.710 -15.125 -8.814  1.00 15.35 ?  34  VAL   B HB   1 
ATOM   4468 H  HG11 . VAL   B 1 34  ? 42.273 -14.655 -6.477  1.00 15.95 ?  34  VAL   B HG11 1 
ATOM   4469 H  HG12 . VAL   B 1 34  ? 43.157 -15.941 -6.769  1.00 15.95 ?  34  VAL   B HG12 1 
ATOM   4470 H  HG13 . VAL   B 1 34  ? 43.850 -14.588 -6.302  1.00 15.95 ?  34  VAL   B HG13 1 
ATOM   4471 H  HG21 . VAL   B 1 34  ? 41.854 -13.043 -8.168  1.00 16.71 ?  34  VAL   B HG21 1 
ATOM   4472 H  HG22 . VAL   B 1 34  ? 43.337 -12.497 -8.010  1.00 16.71 ?  34  VAL   B HG22 1 
ATOM   4473 H  HG23 . VAL   B 1 34  ? 42.790 -12.907 -9.444  1.00 16.71 ?  34  VAL   B HG23 1 
ATOM   4474 N  N    . VAL   B 1 35  ? 46.063 -16.395 -7.647  1.00 10.38 ?  35  VAL   B N    1 
ATOM   4475 C  CA   . VAL   B 1 35  ? 46.298 -17.738 -7.133  1.00 10.01 ?  35  VAL   B CA   1 
ATOM   4476 C  C    . VAL   B 1 35  ? 45.761 -17.796 -5.713  1.00 9.51  ?  35  VAL   B C    1 
ATOM   4477 O  O    . VAL   B 1 35  ? 45.971 -16.870 -4.922  1.00 10.26 ?  35  VAL   B O    1 
ATOM   4478 C  CB   . VAL   B 1 35  ? 47.780 -18.173 -7.214  1.00 11.31 ?  35  VAL   B CB   1 
ATOM   4479 C  CG1  . VAL   B 1 35  ? 48.677 -17.340 -6.292  1.00 12.23 ?  35  VAL   B CG1  1 
ATOM   4480 C  CG2  . VAL   B 1 35  ? 47.910 -19.664 -6.893  1.00 12.02 ?  35  VAL   B CG2  1 
ATOM   4481 H  H    . VAL   B 1 35  ? 46.567 -15.798 -7.291  1.00 12.46 ?  35  VAL   B H    1 
ATOM   4482 H  HA   . VAL   B 1 35  ? 45.780 -18.368 -7.660  1.00 12.02 ?  35  VAL   B HA   1 
ATOM   4483 H  HB   . VAL   B 1 35  ? 48.088 -18.048 -8.126  1.00 13.58 ?  35  VAL   B HB   1 
ATOM   4484 H  HG11 . VAL   B 1 35  ? 49.601 -17.566 -6.472  1.00 14.69 ?  35  VAL   B HG11 1 
ATOM   4485 H  HG12 . VAL   B 1 35  ? 48.517 -16.405 -6.463  1.00 14.69 ?  35  VAL   B HG12 1 
ATOM   4486 H  HG13 . VAL   B 1 35  ? 48.459 -17.556 -5.369  1.00 14.69 ?  35  VAL   B HG13 1 
ATOM   4487 H  HG21 . VAL   B 1 35  ? 48.831 -19.939 -7.005  1.00 14.44 ?  35  VAL   B HG21 1 
ATOM   4488 H  HG22 . VAL   B 1 35  ? 47.631 -19.819 -5.972  1.00 14.44 ?  35  VAL   B HG22 1 
ATOM   4489 H  HG23 . VAL   B 1 35  ? 47.338 -20.176 -7.492  1.00 14.44 ?  35  VAL   B HG23 1 
ATOM   4490 N  N    . VAL   B 1 36  ? 45.034 -18.876 -5.398  1.00 9.66  ?  36  VAL   B N    1 
ATOM   4491 C  CA   . VAL   B 1 36  ? 44.488 -19.080 -4.067  1.00 9.73  ?  36  VAL   B CA   1 
ATOM   4492 C  C    . VAL   B 1 36  ? 45.498 -19.837 -3.215  1.00 8.86  ?  36  VAL   B C    1 
ATOM   4493 O  O    . VAL   B 1 36  ? 46.043 -20.865 -3.639  1.00 10.55 ?  36  VAL   B O    1 
ATOM   4494 C  CB   . VAL   B 1 36  ? 43.154 -19.843 -4.135  1.00 10.11 ?  36  VAL   B CB   1 
ATOM   4495 C  CG1  . VAL   B 1 36  ? 42.660 -20.190 -2.728  1.00 10.86 ?  36  VAL   B CG1  1 
ATOM   4496 C  CG2  . VAL   B 1 36  ? 42.120 -19.014 -4.884  1.00 10.81 ?  36  VAL   B CG2  1 
ATOM   4497 H  H    . VAL   B 1 36  ? 44.853 -19.512 -5.949  1.00 11.59 ?  36  VAL   B H    1 
ATOM   4498 H  HA   . VAL   B 1 36  ? 44.323 -18.220 -3.650  1.00 11.68 ?  36  VAL   B HA   1 
ATOM   4499 H  HB   . VAL   B 1 36  ? 43.288 -20.673 -4.620  1.00 12.13 ?  36  VAL   B HB   1 
ATOM   4500 H  HG11 . VAL   B 1 36  ? 41.719 -20.421 -2.775  1.00 13.04 ?  36  VAL   B HG11 1 
ATOM   4501 H  HG12 . VAL   B 1 36  ? 43.169 -20.932 -2.381  1.00 13.04 ?  36  VAL   B HG12 1 
ATOM   4502 H  HG13 . VAL   B 1 36  ? 42.773 -19.408 -2.156  1.00 13.04 ?  36  VAL   B HG13 1 
ATOM   4503 H  HG21 . VAL   B 1 36  ? 41.279 -19.496 -4.902  1.00 12.98 ?  36  VAL   B HG21 1 
ATOM   4504 H  HG22 . VAL   B 1 36  ? 42.007 -18.164 -4.436  1.00 12.98 ?  36  VAL   B HG22 1 
ATOM   4505 H  HG23 . VAL   B 1 36  ? 42.431 -18.867 -5.796  1.00 12.98 ?  36  VAL   B HG23 1 
ATOM   4506 N  N    . ASN   B 1 37  ? 45.708 -19.351 -1.996  1.00 9.65  ?  37  ASN   B N    1 
ATOM   4507 C  CA   . ASN   B 1 37  ? 46.473 -20.069 -0.987  1.00 9.96  ?  37  ASN   B CA   1 
ATOM   4508 C  C    . ASN   B 1 37  ? 45.533 -20.745 0.008   1.00 10.00 ?  37  ASN   B C    1 
ATOM   4509 O  O    . ASN   B 1 37  ? 44.519 -20.176 0.425   1.00 10.46 ?  37  ASN   B O    1 
ATOM   4510 C  CB   . ASN   B 1 37  ? 47.416 -19.123 -0.238  1.00 10.15 ?  37  ASN   B CB   1 
ATOM   4511 C  CG   . ASN   B 1 37  ? 48.265 -19.841 0.786   1.00 10.49 ?  37  ASN   B CG   1 
ATOM   4512 O  OD1  . ASN   B 1 37  ? 48.605 -21.016 0.606   1.00 11.18 ?  37  ASN   B OD1  1 
ATOM   4513 N  ND2  . ASN   B 1 37  ? 48.618 -19.146 1.863   1.00 10.80 ?  37  ASN   B ND2  1 
ATOM   4514 H  H    . ASN   B 1 37  ? 45.420 -18.586 -1.719  1.00 11.59 ?  37  ASN   B H    1 
ATOM   4515 H  HA   . ASN   B 1 37  ? 47.004 -20.762 -1.407  1.00 11.96 ?  37  ASN   B HA   1 
ATOM   4516 H  HB2  . ASN   B 1 37  ? 48.015 -18.711 -0.876  1.00 12.18 ?  37  ASN   B HB2  1 
ATOM   4517 H  HB3  . ASN   B 1 37  ? 46.898 -18.453 0.225   1.00 12.18 ?  37  ASN   B HB3  1 
ATOM   4518 H  HD21 . ASN   B 1 37  ? 49.095 -19.516 2.475   1.00 12.97 ?  37  ASN   B HD21 1 
ATOM   4519 H  HD22 . ASN   B 1 37  ? 48.356 -18.340 1.955   1.00 12.97 ?  37  ASN   B HD22 1 
ATOM   4520 N  N    . ALA   B 1 38  ? 45.887 -21.977 0.382   1.00 10.25 ?  38  ALA   B N    1 
ATOM   4521 C  CA   . ALA   B 1 38  ? 45.242 -22.722 1.465   1.00 10.90 ?  38  ALA   B CA   1 
ATOM   4522 C  C    . ALA   B 1 38  ? 45.828 -22.236 2.790   1.00 10.61 ?  38  ALA   B C    1 
ATOM   4523 O  O    . ALA   B 1 38  ? 46.729 -22.844 3.379   1.00 11.68 ?  38  ALA   B O    1 
ATOM   4524 C  CB   . ALA   B 1 38  ? 45.474 -24.217 1.281   1.00 12.08 ?  38  ALA   B CB   1 
ATOM   4525 H  H    . ALA   B 1 38  ? 46.534 -22.408 0.024   1.00 12.31 ?  38  ALA   B H    1 
ATOM   4526 H  HA   . ALA   B 1 38  ? 44.287 -22.548 1.464   1.00 13.09 ?  38  ALA   B HA   1 
ATOM   4527 H  HB1  . ALA   B 1 38  ? 45.032 -24.697 2.009   1.00 14.50 ?  38  ALA   B HB1  1 
ATOM   4528 H  HB2  . ALA   B 1 38  ? 45.094 -24.493 0.434   1.00 14.50 ?  38  ALA   B HB2  1 
ATOM   4529 H  HB3  . ALA   B 1 38  ? 46.422 -24.398 1.300   1.00 14.50 ?  38  ALA   B HB3  1 
ATOM   4530 N  N    . ALA   B 1 39  ? 45.309 -21.092 3.249   1.00 10.45 ?  39  ALA   B N    1 
ATOM   4531 C  CA   . ALA   B 1 39  ? 45.857 -20.355 4.377   1.00 11.07 ?  39  ALA   B CA   1 
ATOM   4532 C  C    . ALA   B 1 39  ? 45.240 -20.802 5.701   1.00 11.14 ?  39  ALA   B C    1 
ATOM   4533 O  O    . ALA   B 1 39  ? 44.209 -21.482 5.753   1.00 11.76 ?  39  ALA   B O    1 
ATOM   4534 C  CB   . ALA   B 1 39  ? 45.616 -18.856 4.185   1.00 11.44 ?  39  ALA   B CB   1 
ATOM   4535 H  H    . ALA   B 1 39  ? 44.609 -20.720 2.912   1.00 12.54 ?  39  ALA   B H    1 
ATOM   4536 H  HA   . ALA   B 1 39  ? 46.813 -20.502 4.419   1.00 13.29 ?  39  ALA   B HA   1 
ATOM   4537 H  HB1  . ALA   B 1 39  ? 45.988 -18.375 4.940   1.00 13.73 ?  39  ALA   B HB1  1 
ATOM   4538 H  HB2  . ALA   B 1 39  ? 46.046 -18.567 3.364   1.00 13.73 ?  39  ALA   B HB2  1 
ATOM   4539 H  HB3  . ALA   B 1 39  ? 44.659 -18.693 4.129   1.00 13.73 ?  39  ALA   B HB3  1 
ATOM   4540 N  N    . ASN   B 1 40  ? 45.889 -20.388 6.784   1.00 11.79 ?  40  ASN   B N    1 
ATOM   4541 C  CA   . ASN   B 1 40  ? 45.329 -20.430 8.126   1.00 12.72 ?  40  ASN   B CA   1 
ATOM   4542 C  C    . ASN   B 1 40  ? 45.150 -19.002 8.651   1.00 11.79 ?  40  ASN   B C    1 
ATOM   4543 O  O    . ASN   B 1 40  ? 45.560 -18.023 8.020   1.00 11.89 ?  40  ASN   B O    1 
ATOM   4544 C  CB   . ASN   B 1 40  ? 46.185 -21.303 9.057   1.00 13.69 ?  40  ASN   B CB   1 
ATOM   4545 C  CG   . ASN   B 1 40  ? 47.641 -20.893 9.073   1.00 14.35 ?  40  ASN   B CG   1 
ATOM   4546 O  OD1  . ASN   B 1 40  ? 47.954 -19.709 9.153   1.00 16.29 ?  40  ASN   B OD1  1 
ATOM   4547 N  ND2  . ASN   B 1 40  ? 48.541 -21.865 9.004   1.00 14.62 ?  40  ASN   B ND2  1 
ATOM   4548 H  H    . ASN   B 1 40  ? 46.687 -20.065 6.762   1.00 14.16 ?  40  ASN   B H    1 
ATOM   4549 H  HA   . ASN   B 1 40  ? 44.449 -20.830 8.083   1.00 15.27 ?  40  ASN   B HA   1 
ATOM   4550 H  HB2  . ASN   B 1 40  ? 45.842 -21.230 9.964   1.00 16.44 ?  40  ASN   B HB2  1 
ATOM   4551 H  HB3  . ASN   B 1 40  ? 46.137 -22.224 8.759   1.00 16.44 ?  40  ASN   B HB3  1 
ATOM   4552 H  HD21 . ASN   B 1 40  ? 49.380 -21.679 9.013   1.00 17.55 ?  40  ASN   B HD21 1 
ATOM   4553 H  HD22 . ASN   B 1 40  ? 48.283 -22.684 8.943   1.00 17.55 ?  40  ASN   B HD22 1 
ATOM   4554 N  N    . VAL   B 1 41  ? 44.496 -18.873 9.808   1.00 12.31 ?  41  VAL   B N    1 
ATOM   4555 C  CA   . VAL   B 1 41  ? 44.040 -17.550 10.253  1.00 12.97 ?  41  VAL   B CA   1 
ATOM   4556 C  C    . VAL   B 1 41  ? 45.192 -16.596 10.543  1.00 12.63 ?  41  VAL   B C    1 
ATOM   4557 O  O    . VAL   B 1 41  ? 45.013 -15.375 10.463  1.00 13.20 ?  41  VAL   B O    1 
ATOM   4558 C  CB   . VAL   B 1 41  ? 43.068 -17.628 11.447  1.00 14.51 ?  41  VAL   B CB   1 
ATOM   4559 C  CG1  . VAL   B 1 41  ? 41.763 -18.309 11.046  1.00 15.12 ?  41  VAL   B CG1  1 
ATOM   4560 C  CG2  . VAL   B 1 41  ? 43.723 -18.308 12.641  1.00 15.88 ?  41  VAL   B CG2  1 
ATOM   4561 H  H    . VAL   B 1 41  ? 44.306 -19.516 10.339  1.00 14.78 ?  41  VAL   B H    1 
ATOM   4562 H  HA   . VAL   B 1 41  ? 43.537 -17.157 9.522   1.00 15.57 ?  41  VAL   B HA   1 
ATOM   4563 H  HB   . VAL   B 1 41  ? 42.846 -16.724 11.721  1.00 17.42 ?  41  VAL   B HB   1 
ATOM   4564 H  HG11 . VAL   B 1 41  ? 41.162 -18.318 11.810  1.00 18.15 ?  41  VAL   B HG11 1 
ATOM   4565 H  HG12 . VAL   B 1 41  ? 41.359 -17.815 10.316  1.00 18.15 ?  41  VAL   B HG12 1 
ATOM   4566 H  HG13 . VAL   B 1 41  ? 41.953 -19.218 10.767  1.00 18.15 ?  41  VAL   B HG13 1 
ATOM   4567 H  HG21 . VAL   B 1 41  ? 43.088 -18.342 13.373  1.00 19.06 ?  41  VAL   B HG21 1 
ATOM   4568 H  HG22 . VAL   B 1 41  ? 43.981 -19.210 12.388  1.00 19.06 ?  41  VAL   B HG22 1 
ATOM   4569 H  HG23 . VAL   B 1 41  ? 44.506 -17.802 12.904  1.00 19.06 ?  41  VAL   B HG23 1 
ATOM   4570 N  N    . TYR   B 1 42  ? 46.365 -17.108 10.920  1.00 13.23 ?  42  TYR   B N    1 
ATOM   4571 C  CA   . TYR   B 1 42  ? 47.517 -16.254 11.182  1.00 13.55 ?  42  TYR   B CA   1 
ATOM   4572 C  C    . TYR   B 1 42  ? 48.473 -16.180 10.001  1.00 13.02 ?  42  TYR   B C    1 
ATOM   4573 O  O    . TYR   B 1 42  ? 49.564 -15.619 10.136  1.00 13.86 ?  42  TYR   B O    1 
ATOM   4574 C  CB   . TYR   B 1 42  ? 48.227 -16.655 12.479  1.00 15.47 ?  42  TYR   B CB   1 
ATOM   4575 C  CG   . TYR   B 1 42  ? 47.630 -15.972 13.702  1.00 15.79 ?  42  TYR   B CG   1 
ATOM   4576 C  CD1  . TYR   B 1 42  ? 47.852 -14.619 13.934  1.00 14.90 ?  42  TYR   B CD1  1 
ATOM   4577 C  CD2  . TYR   B 1 42  ? 46.835 -16.664 14.607  1.00 17.46 ?  42  TYR   B CD2  1 
ATOM   4578 C  CE1  . TYR   B 1 42  ? 47.319 -13.979 15.030  1.00 15.63 ?  42  TYR   B CE1  1 
ATOM   4579 C  CE2  . TYR   B 1 42  ? 46.290 -16.026 15.715  1.00 17.78 ?  42  TYR   B CE2  1 
ATOM   4580 C  CZ   . TYR   B 1 42  ? 46.538 -14.678 15.922  1.00 17.52 ?  42  TYR   B CZ   1 
ATOM   4581 O  OH   . TYR   B 1 42  ? 46.014 -14.019 17.018  1.00 20.43 ?  42  TYR   B OH   1 
ATOM   4582 H  H    . TYR   B 1 42  ? 46.511 -17.955 11.028  1.00 15.88 ?  42  TYR   B H    1 
ATOM   4583 H  HA   . TYR   B 1 42  ? 47.184 -15.357 11.317  1.00 16.27 ?  42  TYR   B HA   1 
ATOM   4584 H  HB2  . TYR   B 1 42  ? 48.149 -17.612 12.603  1.00 18.57 ?  42  TYR   B HB2  1 
ATOM   4585 H  HB3  . TYR   B 1 42  ? 49.160 -16.400 12.418  1.00 18.57 ?  42  TYR   B HB3  1 
ATOM   4586 H  HD1  . TYR   B 1 42  ? 48.384 -14.136 13.335  1.00 17.89 ?  42  TYR   B HD1  1 
ATOM   4587 H  HD2  . TYR   B 1 42  ? 46.666 -17.569 14.465  1.00 20.96 ?  42  TYR   B HD2  1 
ATOM   4588 H  HE1  . TYR   B 1 42  ? 47.487 -13.073 15.167  1.00 18.76 ?  42  TYR   B HE1  1 
ATOM   4589 H  HE2  . TYR   B 1 42  ? 45.761 -16.503 16.310  1.00 21.34 ?  42  TYR   B HE2  1 
ATOM   4590 H  HH   . TYR   B 1 42  ? 46.251 -13.216 16.998  1.00 24.52 ?  42  TYR   B HH   1 
ATOM   4591 N  N    . LEU   B 1 43  ? 48.077 -16.707 8.847   1.00 11.78 ?  43  LEU   B N    1 
ATOM   4592 C  CA   . LEU   B 1 43  ? 48.889 -16.643 7.636   1.00 11.19 ?  43  LEU   B CA   1 
ATOM   4593 C  C    . LEU   B 1 43  ? 50.304 -17.148 7.894   1.00 11.64 ?  43  LEU   B C    1 
ATOM   4594 O  O    . LEU   B 1 43  ? 51.283 -16.552 7.440   1.00 12.81 ?  43  LEU   B O    1 
ATOM   4595 C  CB   . LEU   B 1 43  ? 48.910 -15.241 7.023   1.00 11.67 ?  43  LEU   B CB   1 
ATOM   4596 C  CG   . LEU   B 1 43  ? 47.551 -14.626 6.664   1.00 12.01 ?  43  LEU   B CG   1 
ATOM   4597 C  CD1  . LEU   B 1 43  ? 47.750 -13.234 6.094   1.00 13.32 ?  43  LEU   B CD1  1 
ATOM   4598 C  CD2  . LEU   B 1 43  ? 46.783 -15.510 5.695   1.00 12.50 ?  43  LEU   B CD2  1 
ATOM   4599 H  H    . LEU   B 1 43  ? 47.333 -17.128 8.736   1.00 14.15 ?  43  LEU   B H    1 
ATOM   4600 H  HA   . LEU   B 1 43  ? 48.491 -17.235 6.974   1.00 13.43 ?  43  LEU   B HA   1 
ATOM   4601 H  HB2  . LEU   B 1 43  ? 49.341 -14.643 7.649   1.00 14.01 ?  43  LEU   B HB2  1 
ATOM   4602 H  HB3  . LEU   B 1 43  ? 49.431 -15.279 6.203   1.00 14.01 ?  43  LEU   B HB3  1 
ATOM   4603 H  HG   . LEU   B 1 43  ? 47.024 -14.544 7.470   1.00 14.41 ?  43  LEU   B HG   1 
ATOM   4604 H  HD11 . LEU   B 1 43  ? 46.883 -12.854 5.873   1.00 16.00 ?  43  LEU   B HD11 1 
ATOM   4605 H  HD12 . LEU   B 1 43  ? 48.188 -12.679 6.762   1.00 16.00 ?  43  LEU   B HD12 1 
ATOM   4606 H  HD13 . LEU   B 1 43  ? 48.299 -13.287 5.298   1.00 16.00 ?  43  LEU   B HD13 1 
ATOM   4607 H  HD21 . LEU   B 1 43  ? 45.976 -15.045 5.412   1.00 15.01 ?  43  LEU   B HD21 1 
ATOM   4608 H  HD22 . LEU   B 1 43  ? 47.338 -15.700 4.923   1.00 15.01 ?  43  LEU   B HD22 1 
ATOM   4609 H  HD23 . LEU   B 1 43  ? 46.542 -16.338 6.141   1.00 15.01 ?  43  LEU   B HD23 1 
ATOM   4610 N  N    . LYS   B 1 44  ? 50.407 -18.270 8.608   1.00 11.85 ?  44  LYS   B N    1 
ATOM   4611 C  CA   . LYS   B 1 44  ? 51.677 -18.943 8.844   1.00 12.57 ?  44  LYS   B CA   1 
ATOM   4612 C  C    . LYS   B 1 44  ? 51.788 -20.061 7.816   1.00 12.07 ?  44  LYS   B C    1 
ATOM   4613 O  O    . LYS   B 1 44  ? 51.095 -21.077 7.910   1.00 13.64 ?  44  LYS   B O    1 
ATOM   4614 C  CB   . LYS   B 1 44  ? 51.736 -19.459 10.279  1.00 14.45 ?  44  LYS   B CB   1 
ATOM   4615 C  CG   . LYS   B 1 44  ? 51.913 -18.345 11.306  1.00 16.80 ?  44  LYS   B CG   1 
ATOM   4616 C  CD   . LYS   B 1 44  ? 53.098 -17.462 10.914  1.00 20.02 ?  44  LYS   B CD   1 
ATOM   4617 C  CE   . LYS   B 1 44  ? 53.626 -16.628 12.052  1.00 22.76 ?  44  LYS   B CE   1 
ATOM   4618 N  NZ   . LYS   B 1 44  ? 54.762 -15.766 11.646  1.00 23.97 ?  44  LYS   B NZ   1 
ATOM   4619 H  H    . LYS   B 1 44  ? 49.736 -18.663 8.979   1.00 14.23 ?  44  LYS   B H    1 
ATOM   4620 H  HA   . LYS   B 1 44  ? 52.406 -18.325 8.681   1.00 15.09 ?  44  LYS   B HA   1 
ATOM   4621 H  HB2  . LYS   B 1 44  ? 50.901 -19.919 10.480  1.00 17.34 ?  44  LYS   B HB2  1 
ATOM   4622 H  HB3  . LYS   B 1 44  ? 52.479 -20.070 10.365  1.00 17.34 ?  44  LYS   B HB3  1 
ATOM   4623 H  HG2  . LYS   B 1 44  ? 51.113 -17.801 11.337  1.00 20.17 ?  44  LYS   B HG2  1 
ATOM   4624 H  HG3  . LYS   B 1 44  ? 52.094 -18.738 12.176  1.00 20.17 ?  44  LYS   B HG3  1 
ATOM   4625 H  HD2  . LYS   B 1 44  ? 53.815 -18.031 10.584  1.00 24.03 ?  44  LYS   B HD2  1 
ATOM   4626 H  HD3  . LYS   B 1 44  ? 52.811 -16.855 10.212  1.00 24.03 ?  44  LYS   B HD3  1 
ATOM   4627 H  HE2  . LYS   B 1 44  ? 52.919 -16.039 12.333  1.00 27.32 ?  44  LYS   B HE2  1 
ATOM   4628 H  HE3  . LYS   B 1 44  ? 53.909 -17.209 12.781  1.00 27.32 ?  44  LYS   B HE3  1 
ATOM   4629 H  HZ1  . LYS   B 1 44  ? 55.044 -15.288 12.341  1.00 28.77 ?  44  LYS   B HZ1  1 
ATOM   4630 H  HZ2  . LYS   B 1 44  ? 55.432 -16.262 11.341  1.00 28.77 ?  44  LYS   B HZ2  1 
ATOM   4631 H  HZ3  . LYS   B 1 44  ? 54.499 -15.207 11.000  1.00 28.77 ?  44  LYS   B HZ3  1 
ATOM   4632 N  N    . HIS   B 1 45  ? 52.631 -19.845 6.811   1.00 12.03 ?  45  HIS   B N    1 
ATOM   4633 C  CA   . HIS   B 1 45  ? 52.647 -20.681 5.612   1.00 11.96 ?  45  HIS   B CA   1 
ATOM   4634 C  C    . HIS   B 1 45  ? 53.672 -21.797 5.770   1.00 14.17 ?  45  HIS   B C    1 
ATOM   4635 O  O    . HIS   B 1 45  ? 54.744 -21.790 5.171   1.00 17.02 ?  45  HIS   B O    1 
ATOM   4636 C  CB   . HIS   B 1 45  ? 52.956 -19.830 4.391   1.00 12.09 ?  45  HIS   B CB   1 
ATOM   4637 C  CG   . HIS   B 1 45  ? 52.091 -18.624 4.283   1.00 11.81 ?  45  HIS   B CG   1 
ATOM   4638 N  ND1  . HIS   B 1 45  ? 50.712 -18.694 4.265   1.00 12.04 ?  45  HIS   B ND1  1 
ATOM   4639 C  CD2  . HIS   B 1 45  ? 52.412 -17.312 4.206   1.00 12.69 ?  45  HIS   B CD2  1 
ATOM   4640 C  CE1  . HIS   B 1 45  ? 50.230 -17.470 4.158   1.00 11.76 ?  45  HIS   B CE1  1 
ATOM   4641 N  NE2  . HIS   B 1 45  ? 51.236 -16.614 4.127   1.00 12.54 ?  45  HIS   B NE2  1 
ATOM   4642 H  H    . HIS   B 1 45  ? 53.201 -19.200 6.791   1.00 14.45 ?  45  HIS   B H    1 
ATOM   4643 H  HA   . HIS   B 1 45  ? 51.769 -21.083 5.490   1.00 14.36 ?  45  HIS   B HA   1 
ATOM   4644 H  HB2  . HIS   B 1 45  ? 53.878 -19.543 4.435   1.00 14.52 ?  45  HIS   B HB2  1 
ATOM   4645 H  HB3  . HIS   B 1 45  ? 52.819 -20.374 3.592   1.00 14.52 ?  45  HIS   B HB3  1 
ATOM   4646 H  HD2  . HIS   B 1 45  ? 53.272 -16.954 4.201   1.00 15.24 ?  45  HIS   B HD2  1 
ATOM   4647 H  HE1  . HIS   B 1 45  ? 49.329 -17.249 4.120   1.00 14.12 ?  45  HIS   B HE1  1 
ATOM   4648 H  HE2  . HIS   B 1 45  ? 51.164 -15.760 4.067   1.00 15.05 ?  45  HIS   B HE2  1 
ATOM   4649 N  N    A GLY   B 1 46  ? 53.307 -22.791 6.574   0.66 15.07 ?  46  GLY   B N    1 
ATOM   4650 N  N    B GLY   B 1 46  ? 53.315 -22.778 6.590   0.34 15.10 ?  46  GLY   B N    1 
ATOM   4651 C  CA   A GLY   B 1 46  ? 54.239 -23.847 6.932   0.66 17.02 ?  46  GLY   B CA   1 
ATOM   4652 C  CA   B GLY   B 1 46  ? 54.244 -23.844 6.910   0.34 16.52 ?  46  GLY   B CA   1 
ATOM   4653 C  C    A GLY   B 1 46  ? 54.270 -25.072 6.037   0.66 19.02 ?  46  GLY   B C    1 
ATOM   4654 C  C    B GLY   B 1 46  ? 54.251 -25.001 5.931   0.34 18.09 ?  46  GLY   B C    1 
ATOM   4655 O  O    A GLY   B 1 46  ? 55.343 -25.502 5.601   0.66 21.49 ?  46  GLY   B O    1 
ATOM   4656 O  O    B GLY   B 1 46  ? 55.276 -25.290 5.306   0.34 19.04 ?  46  GLY   B O    1 
ATOM   4657 H  H    A GLY   B 1 46  ? 52.528 -22.860 6.943   0.66 18.08 ?  46  GLY   B H    1 
ATOM   4658 H  H    B GLY   B 1 46  ? 52.547 -22.843 6.978   0.34 18.12 ?  46  GLY   B H    1 
ATOM   4659 H  HA2  A GLY   B 1 46  ? 55.131 -23.470 6.957   0.66 20.43 ?  46  GLY   B HA2  1 
ATOM   4660 H  HA2  B GLY   B 1 46  ? 55.141 -23.476 6.944   0.34 19.83 ?  46  GLY   B HA2  1 
ATOM   4661 H  HA3  A GLY   B 1 46  ? 54.022 -24.157 7.824   0.66 20.43 ?  46  GLY   B HA3  1 
ATOM   4662 H  HA3  B GLY   B 1 46  ? 54.030 -24.192 7.789   0.34 19.83 ?  46  GLY   B HA3  1 
ATOM   4663 N  N    . GLY   B 1 47  ? 53.111 -25.673 5.782   1.00 18.52 ?  47  GLY   B N    1 
ATOM   4664 C  CA   . GLY   B 1 47  ? 53.045 -26.935 5.076   1.00 15.97 ?  47  GLY   B CA   1 
ATOM   4665 C  C    . GLY   B 1 47  ? 52.134 -26.901 3.865   1.00 13.73 ?  47  GLY   B C    1 
ATOM   4666 O  O    . GLY   B 1 47  ? 51.483 -25.895 3.576   1.00 14.18 ?  47  GLY   B O    1 
ATOM   4667 H  H    A GLY   B 1 47  ? 52.343 -25.380 6.038   0.66 22.23 ?  47  GLY   B H    1 
ATOM   4668 H  H    B GLY   B 1 47  ? 52.351 -25.410 6.091   0.34 22.23 ?  47  GLY   B H    1 
ATOM   4669 H  HA2  . GLY   B 1 47  ? 53.929 -27.191 4.776   1.00 19.18 ?  47  GLY   B HA2  1 
ATOM   4670 H  HA3  . GLY   B 1 47  ? 52.720 -27.620 5.681   1.00 19.18 ?  47  GLY   B HA3  1 
ATOM   4671 N  N    . GLY   B 1 48  ? 52.078 -28.041 3.177   1.00 12.56 ?  48  GLY   B N    1 
ATOM   4672 C  CA   . GLY   B 1 48  ? 51.144 -28.178 2.078   1.00 13.14 ?  48  GLY   B CA   1 
ATOM   4673 C  C    . GLY   B 1 48  ? 51.283 -27.060 1.069   1.00 12.35 ?  48  GLY   B C    1 
ATOM   4674 O  O    . GLY   B 1 48  ? 52.392 -26.604 0.756   1.00 12.77 ?  48  GLY   B O    1 
ATOM   4675 H  H    . GLY   B 1 48  ? 52.565 -28.731 3.324   1.00 15.08 ?  48  GLY   B H    1 
ATOM   4676 H  HA2  . GLY   B 1 48  ? 51.294 -29.024 1.626   1.00 15.78 ?  48  GLY   B HA2  1 
ATOM   4677 H  HA3  . GLY   B 1 48  ? 50.235 -28.169 2.417   1.00 15.78 ?  48  GLY   B HA3  1 
ATOM   4678 N  N    . VAL   B 1 49  ? 50.138 -26.626 0.535   1.00 12.10 ?  49  VAL   B N    1 
ATOM   4679 C  CA   . VAL   B 1 49  ? 50.127 -25.598 -0.503  1.00 12.03 ?  49  VAL   B CA   1 
ATOM   4680 C  C    . VAL   B 1 49  ? 50.785 -24.313 -0.011  1.00 11.39 ?  49  VAL   B C    1 
ATOM   4681 O  O    . VAL   B 1 49  ? 51.579 -23.697 -0.729  1.00 11.96 ?  49  VAL   B O    1 
ATOM   4682 C  CB   . VAL   B 1 49  ? 48.687 -25.345 -0.989  1.00 13.18 ?  49  VAL   B CB   1 
ATOM   4683 C  CG1  . VAL   B 1 49  ? 48.623 -24.101 -1.872  1.00 13.36 ?  49  VAL   B CG1  1 
ATOM   4684 C  CG2  . VAL   B 1 49  ? 48.149 -26.558 -1.731  1.00 14.50 ?  49  VAL   B CG2  1 
ATOM   4685 H  H    . VAL   B 1 49  ? 49.354 -26.909 0.750   1.00 14.52 ?  49  VAL   B H    1 
ATOM   4686 H  HA   . VAL   B 1 49  ? 50.640 -25.915 -1.265  1.00 14.44 ?  49  VAL   B HA   1 
ATOM   4687 H  HB   . VAL   B 1 49  ? 48.119 -25.191 -0.223  1.00 15.82 ?  49  VAL   B HB   1 
ATOM   4688 H  HG11 . VAL   B 1 49  ? 47.791 -24.114 -2.376  1.00 16.04 ?  49  VAL   B HG11 1 
ATOM   4689 H  HG12 . VAL   B 1 49  ? 48.652 -23.309 -1.312  1.00 16.04 ?  49  VAL   B HG12 1 
ATOM   4690 H  HG13 . VAL   B 1 49  ? 49.375 -24.104 -2.485  1.00 16.04 ?  49  VAL   B HG13 1 
ATOM   4691 H  HG21 . VAL   B 1 49  ? 47.245 -26.373 -2.027  1.00 17.41 ?  49  VAL   B HG21 1 
ATOM   4692 H  HG22 . VAL   B 1 49  ? 48.719 -26.736 -2.498  1.00 17.41 ?  49  VAL   B HG22 1 
ATOM   4693 H  HG23 . VAL   B 1 49  ? 48.155 -27.319 -1.131  1.00 17.41 ?  49  VAL   B HG23 1 
ATOM   4694 N  N    . ALA   B 1 50  ? 50.455 -23.879 1.209   1.00 11.12 ?  50  ALA   B N    1 
ATOM   4695 C  CA   . ALA   B 1 50  ? 50.973 -22.600 1.689   1.00 10.83 ?  50  ALA   B CA   1 
ATOM   4696 C  C    . ALA   B 1 50  ? 52.491 -22.633 1.795   1.00 11.20 ?  50  ALA   B C    1 
ATOM   4697 O  O    . ALA   B 1 50  ? 53.172 -21.661 1.434   1.00 11.32 ?  50  ALA   B O    1 
ATOM   4698 C  CB   . ALA   B 1 50  ? 50.353 -22.251 3.039   1.00 11.58 ?  50  ALA   B CB   1 
ATOM   4699 H  H    . ALA   B 1 50  ? 49.950 -24.299 1.764   1.00 13.36 ?  50  ALA   B H    1 
ATOM   4700 H  HA   . ALA   B 1 50  ? 50.742 -21.906 1.062   1.00 13.00 ?  50  ALA   B HA   1 
ATOM   4701 H  HB1  . ALA   B 1 50  ? 50.708 -21.401 3.342   1.00 13.90 ?  50  ALA   B HB1  1 
ATOM   4702 H  HB2  . ALA   B 1 50  ? 49.391 -22.191 2.938   1.00 13.90 ?  50  ALA   B HB2  1 
ATOM   4703 H  HB3  . ALA   B 1 50  ? 50.573 -22.947 3.682   1.00 13.90 ?  50  ALA   B HB3  1 
ATOM   4704 N  N    . GLY   B 1 51  ? 53.042 -23.733 2.306   1.00 11.78 ?  51  GLY   B N    1 
ATOM   4705 C  CA   . GLY   B 1 51  ? 54.487 -23.840 2.377   1.00 12.97 ?  51  GLY   B CA   1 
ATOM   4706 C  C    . GLY   B 1 51  ? 55.131 -23.784 1.006   1.00 12.25 ?  51  GLY   B C    1 
ATOM   4707 O  O    . GLY   B 1 51  ? 56.177 -23.153 0.823   1.00 13.14 ?  51  GLY   B O    1 
ATOM   4708 H  H    . GLY   B 1 51  ? 52.609 -24.419 2.608   1.00 14.14 ?  51  GLY   B H    1 
ATOM   4709 H  HA2  . GLY   B 1 51  ? 54.837 -23.113 2.913   1.00 15.57 ?  51  GLY   B HA2  1 
ATOM   4710 H  HA3  . GLY   B 1 51  ? 54.730 -24.680 2.801   1.00 15.57 ?  51  GLY   B HA3  1 
ATOM   4711 N  N    . ALA   B 1 52  ? 54.518 -24.440 0.023   1.00 12.01 ?  52  ALA   B N    1 
ATOM   4712 C  CA   . ALA   B 1 52  ? 55.078 -24.447 -1.321  1.00 12.46 ?  52  ALA   B CA   1 
ATOM   4713 C  C    . ALA   B 1 52  ? 55.010 -23.067 -1.964  1.00 11.85 ?  52  ALA   B C    1 
ATOM   4714 O  O    . ALA   B 1 52  ? 55.987 -22.619 -2.589  1.00 12.36 ?  52  ALA   B O    1 
ATOM   4715 C  CB   . ALA   B 1 52  ? 54.360 -25.481 -2.184  1.00 13.34 ?  52  ALA   B CB   1 
ATOM   4716 H  H    . ALA   B 1 52  ? 53.776 -24.875 0.106   1.00 14.42 ?  52  ALA   B H    1 
ATOM   4717 H  HA   . ALA   B 1 52  ? 56.011 -24.698 -1.263  1.00 14.96 ?  52  ALA   B HA   1 
ATOM   4718 H  HB1  . ALA   B 1 52  ? 54.753 -25.468 -3.072  1.00 16.01 ?  52  ALA   B HB1  1 
ATOM   4719 H  HB2  . ALA   B 1 52  ? 54.475 -26.354 -1.782  1.00 16.01 ?  52  ALA   B HB2  1 
ATOM   4720 H  HB3  . ALA   B 1 52  ? 53.422 -25.253 -2.231  1.00 16.01 ?  52  ALA   B HB3  1 
ATOM   4721 N  N    . LEU   B 1 53  ? 53.859 -22.388 -1.852  1.00 11.42 ?  53  LEU   B N    1 
ATOM   4722 C  CA   . LEU   B 1 53  ? 53.755 -21.048 -2.424  1.00 11.40 ?  53  LEU   B CA   1 
ATOM   4723 C  C    . LEU   B 1 53  ? 54.766 -20.111 -1.775  1.00 11.31 ?  53  LEU   B C    1 
ATOM   4724 O  O    . LEU   B 1 53  ? 55.476 -19.365 -2.461  1.00 12.33 ?  53  LEU   B O    1 
ATOM   4725 C  CB   . LEU   B 1 53  ? 52.335 -20.499 -2.257  1.00 12.09 ?  53  LEU   B CB   1 
ATOM   4726 C  CG   . LEU   B 1 53  ? 51.200 -21.234 -2.980  1.00 12.58 ?  53  LEU   B CG   1 
ATOM   4727 C  CD1  . LEU   B 1 53  ? 49.862 -20.603 -2.655  1.00 13.87 ?  53  LEU   B CD1  1 
ATOM   4728 C  CD2  . LEU   B 1 53  ? 51.416 -21.255 -4.482  1.00 14.03 ?  53  LEU   B CD2  1 
ATOM   4729 H  H    . LEU   B 1 53  ? 53.151 -22.672 -1.457  1.00 13.71 ?  53  LEU   B H    1 
ATOM   4730 H  HA   . LEU   B 1 53  ? 53.957 -21.097 -3.375  1.00 13.68 ?  53  LEU   B HA   1 
ATOM   4731 H  HB2  . LEU   B 1 53  ? 52.124 -20.511 -1.313  1.00 14.52 ?  53  LEU   B HB2  1 
ATOM   4732 H  HB3  . LEU   B 1 53  ? 52.330 -19.590 -2.580  1.00 14.52 ?  53  LEU   B HB3  1 
ATOM   4733 H  HG   . LEU   B 1 53  ? 51.169 -22.153 -2.667  1.00 15.11 ?  53  LEU   B HG   1 
ATOM   4734 H  HD11 . LEU   B 1 53  ? 49.159 -21.088 -3.118  1.00 16.65 ?  53  LEU   B HD11 1 
ATOM   4735 H  HD12 . LEU   B 1 53  ? 49.711 -20.652 -1.693  1.00 16.65 ?  53  LEU   B HD12 1 
ATOM   4736 H  HD13 . LEU   B 1 53  ? 49.868 -19.678 -2.939  1.00 16.65 ?  53  LEU   B HD13 1 
ATOM   4737 H  HD21 . LEU   B 1 53  ? 50.671 -21.708 -4.904  1.00 16.84 ?  53  LEU   B HD21 1 
ATOM   4738 H  HD22 . LEU   B 1 53  ? 51.476 -20.343 -4.804  1.00 16.84 ?  53  LEU   B HD22 1 
ATOM   4739 H  HD23 . LEU   B 1 53  ? 52.242 -21.728 -4.674  1.00 16.84 ?  53  LEU   B HD23 1 
ATOM   4740 N  N    . ASN   B 1 54  ? 54.854 -20.139 -0.447  1.00 11.08 ?  54  ASN   B N    1 
ATOM   4741 C  CA   . ASN   B 1 54  ? 55.774 -19.229 0.225   1.00 11.65 ?  54  ASN   B CA   1 
ATOM   4742 C  C    . ASN   B 1 54  ? 57.217 -19.508 -0.179  1.00 12.54 ?  54  ASN   B C    1 
ATOM   4743 O  O    . ASN   B 1 54  ? 57.988 -18.571 -0.420  1.00 12.98 ?  54  ASN   B O    1 
ATOM   4744 C  CB   . ASN   B 1 54  ? 55.617 -19.307 1.735   1.00 12.68 ?  54  ASN   B CB   1 
ATOM   4745 C  CG   . ASN   B 1 54  ? 56.591 -18.388 2.444   1.00 12.54 ?  54  ASN   B CG   1 
ATOM   4746 O  OD1  . ASN   B 1 54  ? 56.604 -17.180 2.202   1.00 12.99 ?  54  ASN   B OD1  1 
ATOM   4747 N  ND2  . ASN   B 1 54  ? 57.444 -18.957 3.283   1.00 14.25 ?  54  ASN   B ND2  1 
ATOM   4748 H  H    . ASN   B 1 54  ? 54.409 -20.663 0.075   1.00 13.31 ?  54  ASN   B H    1 
ATOM   4749 H  HA   . ASN   B 1 54  ? 55.563 -18.324 -0.051  1.00 13.98 ?  54  ASN   B HA   1 
ATOM   4750 H  HB2  . ASN   B 1 54  ? 54.715 -19.034 1.974   1.00 15.22 ?  54  ASN   B HB2  1 
ATOM   4751 H  HB3  . ASN   B 1 54  ? 55.784 -20.212 2.029   1.00 15.22 ?  54  ASN   B HB3  1 
ATOM   4752 H  HD21 . ASN   B 1 54  ? 58.023 -18.475 3.698   1.00 17.10 ?  54  ASN   B HD21 1 
ATOM   4753 H  HD22 . ASN   B 1 54  ? 57.422 -19.807 3.412   1.00 17.10 ?  54  ASN   B HD22 1 
ATOM   4754 N  N    . LYS   B 1 55  ? 57.603 -20.786 -0.239  1.00 13.32 ?  55  LYS   B N    1 
ATOM   4755 C  CA   . LYS   B 1 55  ? 58.958 -21.133 -0.663  1.00 13.96 ?  55  LYS   B CA   1 
ATOM   4756 C  C    . LYS   B 1 55  ? 59.247 -20.591 -2.056  1.00 13.57 ?  55  LYS   B C    1 
ATOM   4757 O  O    . LYS   B 1 55  ? 60.348 -20.089 -2.317  1.00 14.53 ?  55  LYS   B O    1 
ATOM   4758 C  CB   . LYS   B 1 55  ? 59.143 -22.650 -0.619  1.00 16.03 ?  55  LYS   B CB   1 
ATOM   4759 C  CG   . LYS   B 1 55  ? 60.527 -23.112 -1.032  1.00 20.50 ?  55  LYS   B CG   1 
ATOM   4760 C  CD   . LYS   B 1 55  ? 60.695 -24.611 -0.865  1.00 23.88 ?  55  LYS   B CD   1 
ATOM   4761 C  CE   . LYS   B 1 55  ? 60.642 -25.033 0.602   1.00 26.64 ?  55  LYS   B CE   1 
ATOM   4762 N  NZ   . LYS   B 1 55  ? 61.051 -26.446 0.793   1.00 28.36 ?  55  LYS   B NZ   1 
ATOM   4763 H  H    . LYS   B 1 55  ? 57.107 -21.458 -0.036  1.00 15.99 ?  55  LYS   B H    1 
ATOM   4764 H  HA   . LYS   B 1 55  ? 59.595 -20.734 -0.050  1.00 16.75 ?  55  LYS   B HA   1 
ATOM   4765 H  HB2  . LYS   B 1 55  ? 58.982 -22.948 0.289   1.00 19.24 ?  55  LYS   B HB2  1 
ATOM   4766 H  HB3  . LYS   B 1 55  ? 58.501 -23.059 -1.219  1.00 19.24 ?  55  LYS   B HB3  1 
ATOM   4767 H  HG2  . LYS   B 1 55  ? 60.671 -22.891 -1.966  1.00 24.60 ?  55  LYS   B HG2  1 
ATOM   4768 H  HG3  . LYS   B 1 55  ? 61.188 -22.666 -0.479  1.00 24.60 ?  55  LYS   B HG3  1 
ATOM   4769 H  HD2  . LYS   B 1 55  ? 59.980 -25.068 -1.337  1.00 28.66 ?  55  LYS   B HD2  1 
ATOM   4770 H  HD3  . LYS   B 1 55  ? 61.556 -24.878 -1.224  1.00 28.66 ?  55  LYS   B HD3  1 
ATOM   4771 H  HE2  . LYS   B 1 55  ? 61.240 -24.463 1.114   1.00 31.98 ?  55  LYS   B HE2  1 
ATOM   4772 H  HE3  . LYS   B 1 55  ? 59.731 -24.930 0.926   1.00 31.98 ?  55  LYS   B HE3  1 
ATOM   4773 H  HZ1  . LYS   B 1 55  ? 60.999 -26.659 1.655   1.00 34.03 ?  55  LYS   B HZ1  1 
ATOM   4774 H  HZ2  . LYS   B 1 55  ? 60.513 -26.980 0.328   1.00 34.03 ?  55  LYS   B HZ2  1 
ATOM   4775 H  HZ3  . LYS   B 1 55  ? 61.886 -26.558 0.514   1.00 34.03 ?  55  LYS   B HZ3  1 
ATOM   4776 N  N    . ALA   B 1 56  ? 58.269 -20.671 -2.965  1.00 13.25 ?  56  ALA   B N    1 
ATOM   4777 C  CA   . ALA   B 1 56  ? 58.481 -20.168 -4.318  1.00 14.04 ?  56  ALA   B CA   1 
ATOM   4778 C  C    . ALA   B 1 56  ? 58.769 -18.673 -4.314  1.00 14.22 ?  56  ALA   B C    1 
ATOM   4779 O  O    . ALA   B 1 56  ? 59.507 -18.181 -5.180  1.00 14.96 ?  56  ALA   B O    1 
ATOM   4780 C  CB   . ALA   B 1 56  ? 57.273 -20.489 -5.204  1.00 14.77 ?  56  ALA   B CB   1 
ATOM   4781 H  H    . ALA   B 1 56  ? 57.481 -20.995 -2.820  1.00 15.91 ?  56  ALA   B H    1 
ATOM   4782 H  HA   . ALA   B 1 56  ? 59.249 -20.607 -4.694  1.00 16.86 ?  56  ALA   B HA   1 
ATOM   4783 H  HB1  . ALA   B 1 56  ? 57.440 -20.148 -6.099  1.00 17.73 ?  56  ALA   B HB1  1 
ATOM   4784 H  HB2  . ALA   B 1 56  ? 57.155 -21.451 -5.235  1.00 17.73 ?  56  ALA   B HB2  1 
ATOM   4785 H  HB3  . ALA   B 1 56  ? 56.481 -20.070 -4.834  1.00 17.73 ?  56  ALA   B HB3  1 
ATOM   4786 N  N    . THR   B 1 57  ? 58.199 -17.938 -3.357  1.00 13.72 ?  57  THR   B N    1 
ATOM   4787 C  CA   . THR   B 1 57  ? 58.443 -16.504 -3.225  1.00 13.31 ?  57  THR   B CA   1 
ATOM   4788 C  C    . THR   B 1 57  ? 59.700 -16.184 -2.422  1.00 14.47 ?  57  THR   B C    1 
ATOM   4789 O  O    . THR   B 1 57  ? 59.937 -15.013 -2.109  1.00 15.00 ?  57  THR   B O    1 
ATOM   4790 C  CB   . THR   B 1 57  ? 57.242 -15.775 -2.583  1.00 12.53 ?  57  THR   B CB   1 
ATOM   4791 O  OG1  . THR   B 1 57  ? 57.223 -15.986 -1.165  1.00 12.86 ?  57  THR   B OG1  1 
ATOM   4792 C  CG2  . THR   B 1 57  ? 55.919 -16.195 -3.208  1.00 12.87 ?  57  THR   B CG2  1 
ATOM   4793 H  H    . THR   B 1 57  ? 57.646 -18.243 -2.768  1.00 16.47 ?  57  THR   B H    1 
ATOM   4794 H  HA   . THR   B 1 57  ? 58.561 -16.127 -4.112  1.00 15.98 ?  57  THR   B HA   1 
ATOM   4795 H  HB   . THR   B 1 57  ? 57.344 -14.819 -2.744  1.00 15.04 ?  57  THR   B HB   1 
ATOM   4796 H  HG1  . THR   B 1 57  ? 57.157 -16.808 -1.001  1.00 15.44 ?  57  THR   B HG1  1 
ATOM   4797 H  HG21 . THR   B 1 57  ? 55.200 -15.639 -2.875  1.00 15.45 ?  57  THR   B HG21 1 
ATOM   4798 H  HG22 . THR   B 1 57  ? 55.966 -16.107 -4.174  1.00 15.45 ?  57  THR   B HG22 1 
ATOM   4799 H  HG23 . THR   B 1 57  ? 55.730 -17.120 -2.988  1.00 15.45 ?  57  THR   B HG23 1 
ATOM   4800 N  N    . ASN   B 1 58  ? 60.493 -17.190 -2.067  1.00 15.40 ?  58  ASN   B N    1 
ATOM   4801 C  CA   . ASN   B 1 58  ? 61.693 -16.978 -1.261  1.00 18.14 ?  58  ASN   B CA   1 
ATOM   4802 C  C    . ASN   B 1 58  ? 61.358 -16.265 0.049   1.00 15.72 ?  58  ASN   B C    1 
ATOM   4803 O  O    . ASN   B 1 58  ? 62.095 -15.387 0.511   1.00 16.42 ?  58  ASN   B O    1 
ATOM   4804 C  CB   . ASN   B 1 58  ? 62.771 -16.223 -2.041  1.00 26.84 ?  58  ASN   B CB   1 
ATOM   4805 C  CG   . ASN   B 1 58  ? 64.148 -16.370 -1.423  1.00 37.27 ?  58  ASN   B CG   1 
ATOM   4806 O  OD1  . ASN   B 1 58  ? 64.436 -17.358 -0.748  1.00 39.93 ?  58  ASN   B OD1  1 
ATOM   4807 N  ND2  . ASN   B 1 58  ? 65.007 -15.384 -1.652  1.00 43.02 ?  58  ASN   B ND2  1 
ATOM   4808 H  H    . ASN   B 1 58  ? 60.359 -18.014 -2.278  1.00 18.49 ?  58  ASN   B H    1 
ATOM   4809 H  HA   . ASN   B 1 58  ? 62.059 -17.848 -1.036  1.00 21.78 ?  58  ASN   B HA   1 
ATOM   4810 H  HB2  . ASN   B 1 58  ? 62.809 -16.571 -2.946  1.00 32.22 ?  58  ASN   B HB2  1 
ATOM   4811 H  HB3  . ASN   B 1 58  ? 62.550 -15.280 -2.056  1.00 32.22 ?  58  ASN   B HB3  1 
ATOM   4812 H  HD21 . ASN   B 1 58  ? 65.801 -15.421 -1.324  1.00 51.63 ?  58  ASN   B HD21 1 
ATOM   4813 H  HD22 . ASN   B 1 58  ? 64.768 -14.709 -2.127  1.00 51.63 ?  58  ASN   B HD22 1 
ATOM   4814 N  N    . ASN   B 1 59  ? 60.238 -16.652 0.657   1.00 14.81 ?  59  ASN   B N    1 
ATOM   4815 C  CA   . ASN   B 1 59  ? 59.766 -16.182 1.959   1.00 14.53 ?  59  ASN   B CA   1 
ATOM   4816 C  C    . ASN   B 1 59  ? 59.168 -14.775 1.900   1.00 14.03 ?  59  ASN   B C    1 
ATOM   4817 O  O    . ASN   B 1 59  ? 58.743 -14.265 2.939   1.00 13.90 ?  59  ASN   B O    1 
ATOM   4818 C  CB   . ASN   B 1 59  ? 60.840 -16.249 3.060   1.00 15.67 ?  59  ASN   B CB   1 
ATOM   4819 C  CG   . ASN   B 1 59  ? 60.256 -16.419 4.441   1.00 16.76 ?  59  ASN   B CG   1 
ATOM   4820 O  OD1  . ASN   B 1 59  ? 59.426 -17.302 4.676   1.00 17.11 ?  59  ASN   B OD1  1 
ATOM   4821 N  ND2  . ASN   B 1 59  ? 60.681 -15.573 5.369   1.00 17.10 ?  59  ASN   B ND2  1 
ATOM   4822 H  H    . ASN   B 1 59  ? 59.699 -17.231 0.314   1.00 17.78 ?  59  ASN   B H    1 
ATOM   4823 H  HA   . ASN   B 1 59  ? 59.056 -16.777 2.244   1.00 17.45 ?  59  ASN   B HA   1 
ATOM   4824 H  HB2  . ASN   B 1 59  ? 61.423 -17.009 2.899   1.00 18.81 ?  59  ASN   B HB2  1 
ATOM   4825 H  HB3  . ASN   B 1 59  ? 61.354 -15.430 3.062   1.00 18.81 ?  59  ASN   B HB3  1 
ATOM   4826 H  HD21 . ASN   B 1 59  ? 60.378 -15.624 6.173   1.00 20.52 ?  59  ASN   B HD21 1 
ATOM   4827 H  HD22 . ASN   B 1 59  ? 61.260 -14.971 5.167   1.00 20.52 ?  59  ASN   B HD22 1 
ATOM   4828 N  N    . ALA   B 1 60  ? 59.103 -14.137 0.729   1.00 13.82 ?  60  ALA   B N    1 
ATOM   4829 C  CA   . ALA   B 1 60  ? 58.517 -12.799 0.659   1.00 13.74 ?  60  ALA   B CA   1 
ATOM   4830 C  C    . ALA   B 1 60  ? 57.048 -12.814 1.063   1.00 12.79 ?  60  ALA   B C    1 
ATOM   4831 O  O    . ALA   B 1 60  ? 56.551 -11.860 1.676   1.00 13.48 ?  60  ALA   B O    1 
ATOM   4832 C  CB   . ALA   B 1 60  ? 58.683 -12.225 -0.746  1.00 14.43 ?  60  ALA   B CB   1 
ATOM   4833 H  H    . ALA   B 1 60  ? 59.389 -14.454 -0.016  1.00 16.59 ?  60  ALA   B H    1 
ATOM   4834 H  HA   . ALA   B 1 60  ? 58.987 -12.222 1.275   1.00 16.49 ?  60  ALA   B HA   1 
ATOM   4835 H  HB1  . ALA   B 1 60  ? 58.290 -11.341 -0.772  1.00 17.32 ?  60  ALA   B HB1  1 
ATOM   4836 H  HB2  . ALA   B 1 60  ? 59.632 -12.172 -0.954  1.00 17.32 ?  60  ALA   B HB2  1 
ATOM   4837 H  HB3  . ALA   B 1 60  ? 58.240 -12.807 -1.382  1.00 17.32 ?  60  ALA   B HB3  1 
ATOM   4838 N  N    . MET   B 1 61  ? 56.330 -13.882 0.710   1.00 12.32 ?  61  MET   B N    1 
ATOM   4839 C  CA   . MET   B 1 61  ? 54.935 -14.004 1.110   1.00 11.71 ?  61  MET   B CA   1 
ATOM   4840 C  C    . MET   B 1 61  ? 54.800 -14.008 2.632   1.00 11.77 ?  61  MET   B C    1 
ATOM   4841 O  O    . MET   B 1 61  ? 53.896 -13.363 3.182   1.00 11.90 ?  61  MET   B O    1 
ATOM   4842 C  CB   . MET   B 1 61  ? 54.351 -15.270 0.477   1.00 11.59 ?  61  MET   B CB   1 
ATOM   4843 C  CG   . MET   B 1 61  ? 52.912 -15.568 0.883   1.00 11.67 ?  61  MET   B CG   1 
ATOM   4844 S  SD   . MET   B 1 61  ? 52.265 -17.068 0.137   1.00 12.13 ?  61  MET   B SD   1 
ATOM   4845 C  CE   . MET   B 1 61  ? 52.010 -16.507 -1.534  1.00 13.48 ?  61  MET   B CE   1 
ATOM   4846 H  H    . MET   B 1 61  ? 56.627 -14.546 0.242   1.00 14.79 ?  61  MET   B H    1 
ATOM   4847 H  HA   . MET   B 1 61  ? 54.443 -13.247 0.752   1.00 14.05 ?  61  MET   B HA   1 
ATOM   4848 H  HB2  . MET   B 1 61  ? 54.373 -15.175 -0.490  1.00 13.91 ?  61  MET   B HB2  1 
ATOM   4849 H  HB3  . MET   B 1 61  ? 54.898 -16.029 0.740   1.00 13.91 ?  61  MET   B HB3  1 
ATOM   4850 H  HG2  . MET   B 1 61  ? 52.872 -15.676 1.845   1.00 14.01 ?  61  MET   B HG2  1 
ATOM   4851 H  HG3  . MET   B 1 61  ? 52.350 -14.830 0.606   1.00 14.01 ?  61  MET   B HG3  1 
ATOM   4852 H  HE1  . MET   B 1 61  ? 51.631 -17.230 -2.056  1.00 16.18 ?  61  MET   B HE1  1 
ATOM   4853 H  HE2  . MET   B 1 61  ? 51.402 -15.751 -1.523  1.00 16.18 ?  61  MET   B HE2  1 
ATOM   4854 H  HE3  . MET   B 1 61  ? 52.864 -16.238 -1.910  1.00 16.18 ?  61  MET   B HE3  1 
ATOM   4855 N  N    . GLN   B 1 62  ? 55.678 -14.731 3.335   1.00 11.91 ?  62  GLN   B N    1 
ATOM   4856 C  CA   . GLN   B 1 62  ? 55.573 -14.787 4.792   1.00 12.43 ?  62  GLN   B CA   1 
ATOM   4857 C  C    . GLN   B 1 62  ? 55.861 -13.431 5.424   1.00 12.59 ?  62  GLN   B C    1 
ATOM   4858 O  O    . GLN   B 1 62  ? 55.181 -13.028 6.375   1.00 12.90 ?  62  GLN   B O    1 
ATOM   4859 C  CB   . GLN   B 1 62  ? 56.526 -15.841 5.355   1.00 12.57 ?  62  GLN   B CB   1 
ATOM   4860 C  CG   . GLN   B 1 62  ? 56.309 -16.113 6.834   1.00 12.88 ?  62  GLN   B CG   1 
ATOM   4861 C  CD   . GLN   B 1 62  ? 54.935 -16.706 7.078   1.00 12.65 ?  62  GLN   B CD   1 
ATOM   4862 O  OE1  . GLN   B 1 62  ? 54.675 -17.848 6.703   1.00 12.83 ?  62  GLN   B OE1  1 
ATOM   4863 N  NE2  . GLN   B 1 62  ? 54.031 -15.922 7.661   1.00 12.92 ?  62  GLN   B NE2  1 
ATOM   4864 H  H    . GLN   B 1 62  ? 56.318 -15.188 2.997   1.00 14.30 ?  62  GLN   B H    1 
ATOM   4865 H  HA   . GLN   B 1 62  ? 54.667 -15.039 5.030   1.00 14.92 ?  62  GLN   B HA   1 
ATOM   4866 H  HB2  . GLN   B 1 62  ? 56.399 -16.673 4.872   1.00 15.08 ?  62  GLN   B HB2  1 
ATOM   4867 H  HB3  . GLN   B 1 62  ? 57.440 -15.531 5.239   1.00 15.08 ?  62  GLN   B HB3  1 
ATOM   4868 H  HG2  . GLN   B 1 62  ? 56.975 -16.754 7.139   1.00 15.46 ?  62  GLN   B HG2  1 
ATOM   4869 H  HG3  . GLN   B 1 62  ? 56.381 -15.290 7.331   1.00 15.46 ?  62  GLN   B HG3  1 
ATOM   4870 H  HE21 . GLN   B 1 62  ? 54.241 -15.125 7.895   1.00 15.52 ?  62  GLN   B HE21 1 
ATOM   4871 H  HE22 . GLN   B 1 62  ? 53.237 -16.222 7.809   1.00 15.52 ?  62  GLN   B HE22 1 
ATOM   4872 N  N    . VAL   B 1 63  ? 56.875 -12.717 4.925   1.00 12.96 ?  63  VAL   B N    1 
ATOM   4873 C  CA   . VAL   B 1 63  ? 57.188 -11.400 5.474   1.00 13.92 ?  63  VAL   B CA   1 
ATOM   4874 C  C    . VAL   B 1 63  ? 55.996 -10.465 5.298   1.00 13.06 ?  63  VAL   B C    1 
ATOM   4875 O  O    . VAL   B 1 63  ? 55.583 -9.764  6.232   1.00 13.72 ?  63  VAL   B O    1 
ATOM   4876 C  CB   . VAL   B 1 63  ? 58.474 -10.841 4.837   1.00 15.51 ?  63  VAL   B CB   1 
ATOM   4877 C  CG1  . VAL   B 1 63  ? 58.703 -9.403  5.288   1.00 16.43 ?  63  VAL   B CG1  1 
ATOM   4878 C  CG2  . VAL   B 1 63  ? 59.666 -11.722 5.198   1.00 16.58 ?  63  VAL   B CG2  1 
ATOM   4879 H  H    . VAL   B 1 63  ? 57.385 -12.971 4.276   1.00 15.56 ?  63  VAL   B H    1 
ATOM   4880 H  HA   . VAL   B 1 63  ? 57.353 -11.496 6.424   1.00 16.71 ?  63  VAL   B HA   1 
ATOM   4881 H  HB   . VAL   B 1 63  ? 58.381 -10.846 3.872   1.00 18.61 ?  63  VAL   B HB   1 
ATOM   4882 H  HG11 . VAL   B 1 63  ? 59.618 -9.153  5.091   1.00 19.72 ?  63  VAL   B HG11 1 
ATOM   4883 H  HG12 . VAL   B 1 63  ? 58.090 -8.821  4.815   1.00 19.72 ?  63  VAL   B HG12 1 
ATOM   4884 H  HG13 . VAL   B 1 63  ? 58.545 -9.345  6.245   1.00 19.72 ?  63  VAL   B HG13 1 
ATOM   4885 H  HG21 . VAL   B 1 63  ? 60.470 -11.343 4.809   1.00 19.91 ?  63  VAL   B HG21 1 
ATOM   4886 H  HG22 . VAL   B 1 63  ? 59.753 -11.755 6.166   1.00 19.91 ?  63  VAL   B HG22 1 
ATOM   4887 H  HG23 . VAL   B 1 63  ? 59.520 -12.616 4.851   1.00 19.91 ?  63  VAL   B HG23 1 
ATOM   4888 N  N    . GLU   B 1 64  ? 55.427 -10.449 4.094   1.00 12.51 ?  64  GLU   B N    1 
ATOM   4889 C  CA   . GLU   B 1 64  ? 54.259 -9.615  3.820   1.00 12.23 ?  64  GLU   B CA   1 
ATOM   4890 C  C    . GLU   B 1 64  ? 53.078 -10.015 4.696   1.00 12.06 ?  64  GLU   B C    1 
ATOM   4891 O  O    . GLU   B 1 64  ? 52.336 -9.156  5.196   1.00 12.66 ?  64  GLU   B O    1 
ATOM   4892 C  CB   . GLU   B 1 64  ? 53.886 -9.770  2.345   1.00 12.50 ?  64  GLU   B CB   1 
ATOM   4893 C  CG   . GLU   B 1 64  ? 52.605 -9.046  1.923   1.00 12.69 ?  64  GLU   B CG   1 
ATOM   4894 C  CD   . GLU   B 1 64  ? 52.086 -9.530  0.577   1.00 13.40 ?  64  GLU   B CD   1 
ATOM   4895 O  OE1  . GLU   B 1 64  ? 52.262 -10.739 0.267   1.00 14.09 ?  64  GLU   B OE1  1 
ATOM   4896 O  OE2  . GLU   B 1 64  ? 51.477 -8.709  -0.161  1.00 14.10 -1 64  GLU   B OE2  1 
ATOM   4897 H  H    . GLU   B 1 64  ? 55.703 -10.909 3.418   1.00 15.02 ?  64  GLU   B H    1 
ATOM   4898 H  HA   . GLU   B 1 64  ? 54.474 -8.687  3.991   1.00 14.68 ?  64  GLU   B HA   1 
ATOM   4899 H  HB2  . GLU   B 1 64  ? 54.609 -9.409  1.802   1.00 15.00 ?  64  GLU   B HB2  1 
ATOM   4900 H  HB3  . GLU   B 1 64  ? 53.772 -10.709 2.149   1.00 15.00 ?  64  GLU   B HB3  1 
ATOM   4901 H  HG2  . GLU   B 1 64  ? 51.907 -9.204  2.585   1.00 15.24 ?  64  GLU   B HG2  1 
ATOM   4902 H  HG3  . GLU   B 1 64  ? 52.783 -8.096  1.859   1.00 15.24 ?  64  GLU   B HG3  1 
ATOM   4903 N  N    . SER   B 1 65  ? 52.891 -11.321 4.884   1.00 11.83 ?  65  SER   B N    1 
ATOM   4904 C  CA   . SER   B 1 65  ? 51.779 -11.827 5.681   1.00 12.09 ?  65  SER   B CA   1 
ATOM   4905 C  C    . SER   B 1 65  ? 51.909 -11.428 7.145   1.00 12.07 ?  65  SER   B C    1 
ATOM   4906 O  O    . SER   B 1 65  ? 50.908 -11.068 7.783   1.00 12.61 ?  65  SER   B O    1 
ATOM   4907 C  CB   . SER   B 1 65  ? 51.694 -13.351 5.550   1.00 12.50 ?  65  SER   B CB   1 
ATOM   4908 O  OG   . SER   B 1 65  ? 51.351 -13.753 4.231   1.00 12.57 ?  65  SER   B OG   1 
ATOM   4909 H  H    . SER   B 1 65  ? 53.404 -11.941 4.567   1.00 14.20 ?  65  SER   B H    1 
ATOM   4910 H  HA   . SER   B 1 65  ? 50.955 -11.451 5.338   1.00 14.52 ?  65  SER   B HA   1 
ATOM   4911 H  HB2  . SER   B 1 65  ? 52.550 -13.737 5.780   1.00 15.00 ?  65  SER   B HB2  1 
ATOM   4912 H  HB3  . SER   B 1 65  ? 51.009 -13.677 6.158   1.00 15.00 ?  65  SER   B HB3  1 
ATOM   4913 H  HG   . SER   B 1 65  ? 51.934 -13.465 3.685   1.00 15.09 ?  65  SER   B HG   1 
ATOM   4914 N  N    . ASP   B 1 66  ? 53.117 -11.527 7.711   1.00 12.63 ?  66  ASP   B N    1 
ATOM   4915 C  CA   . ASP   B 1 66  ? 53.307 -11.138 9.106   1.00 13.12 ?  66  ASP   B CA   1 
ATOM   4916 C  C    . ASP   B 1 66  ? 52.993 -9.661  9.303   1.00 13.26 ?  66  ASP   B C    1 
ATOM   4917 O  O    . ASP   B 1 66  ? 52.425 -9.267  10.327  1.00 13.95 ?  66  ASP   B O    1 
ATOM   4918 C  CB   . ASP   B 1 66  ? 54.741 -11.439 9.553   1.00 14.62 ?  66  ASP   B CB   1 
ATOM   4919 C  CG   . ASP   B 1 66  ? 55.017 -12.930 9.712   1.00 16.35 ?  66  ASP   B CG   1 
ATOM   4920 O  OD1  . ASP   B 1 66  ? 54.065 -13.740 9.641   1.00 16.63 ?  66  ASP   B OD1  1 
ATOM   4921 O  OD2  . ASP   B 1 66  ? 56.200 -13.292 9.917   1.00 19.03 -1 66  ASP   B OD2  1 
ATOM   4922 H  H    . ASP   B 1 66  ? 53.823 -11.818 7.318   1.00 15.16 ?  66  ASP   B H    1 
ATOM   4923 H  HA   . ASP   B 1 66  ? 52.703 -11.649 9.668   1.00 15.76 ?  66  ASP   B HA   1 
ATOM   4924 H  HB2  . ASP   B 1 66  ? 55.357 -11.088 8.892   1.00 17.55 ?  66  ASP   B HB2  1 
ATOM   4925 H  HB3  . ASP   B 1 66  ? 54.899 -11.008 10.411  1.00 17.55 ?  66  ASP   B HB3  1 
ATOM   4926 N  N    . ASP   B 1 67  ? 53.372 -8.824  8.341   1.00 12.70 ?  67  ASP   B N    1 
ATOM   4927 C  CA   . ASP   B 1 67  ? 53.026 -7.411  8.424   1.00 13.56 ?  67  ASP   B CA   1 
ATOM   4928 C  C    . ASP   B 1 67  ? 51.514 -7.203  8.339   1.00 13.44 ?  67  ASP   B C    1 
ATOM   4929 O  O    . ASP   B 1 67  ? 50.950 -6.392  9.086   1.00 14.22 ?  67  ASP   B O    1 
ATOM   4930 C  CB   . ASP   B 1 67  ? 53.750 -6.649  7.321   1.00 14.55 ?  67  ASP   B CB   1 
ATOM   4931 C  CG   . ASP   B 1 67  ? 53.333 -5.203  7.267   1.00 15.78 ?  67  ASP   B CG   1 
ATOM   4932 O  OD1  . ASP   B 1 67  ? 53.835 -4.395  8.085   1.00 17.10 ?  67  ASP   B OD1  1 
ATOM   4933 O  OD2  . ASP   B 1 67  ? 52.463 -4.905  6.431   1.00 17.34 -1 67  ASP   B OD2  1 
ATOM   4934 H  H    . ASP   B 1 67  ? 53.833 -9.046  7.650   1.00 15.24 ?  67  ASP   B H    1 
ATOM   4935 H  HA   . ASP   B 1 67  ? 53.328 -7.060  9.273   1.00 16.28 ?  67  ASP   B HA   1 
ATOM   4936 H  HB2  . ASP   B 1 67  ? 54.708 -6.681  7.483   1.00 17.47 ?  67  ASP   B HB2  1 
ATOM   4937 H  HB3  . ASP   B 1 67  ? 53.550 -7.058  6.461   1.00 17.47 ?  67  ASP   B HB3  1 
ATOM   4938 N  N    . TYR   B 1 68  ? 50.841 -7.929  7.439   1.00 12.95 ?  68  TYR   B N    1 
ATOM   4939 C  CA   . TYR   B 1 68  ? 49.385 -7.860  7.366   1.00 13.80 ?  68  TYR   B CA   1 
ATOM   4940 C  C    . TYR   B 1 68  ? 48.754 -8.204  8.710   1.00 13.21 ?  68  TYR   B C    1 
ATOM   4941 O  O    . TYR   B 1 68  ? 47.807 -7.538  9.151   1.00 14.01 ?  68  TYR   B O    1 
ATOM   4942 C  CB   . TYR   B 1 68  ? 48.855 -8.802  6.277   1.00 14.65 ?  68  TYR   B CB   1 
ATOM   4943 C  CG   . TYR   B 1 68  ? 47.344 -8.947  6.334   1.00 15.46 ?  68  TYR   B CG   1 
ATOM   4944 C  CD1  . TYR   B 1 68  ? 46.748 -9.886  7.172   1.00 16.36 ?  68  TYR   B CD1  1 
ATOM   4945 C  CD2  . TYR   B 1 68  ? 46.518 -8.121  5.590   1.00 16.44 ?  68  TYR   B CD2  1 
ATOM   4946 C  CE1  . TYR   B 1 68  ? 45.384 -10.001 7.264   1.00 17.33 ?  68  TYR   B CE1  1 
ATOM   4947 C  CE2  . TYR   B 1 68  ? 45.136 -8.242  5.666   1.00 16.70 ?  68  TYR   B CE2  1 
ATOM   4948 C  CZ   . TYR   B 1 68  ? 44.588 -9.182  6.509   1.00 17.28 ?  68  TYR   B CZ   1 
ATOM   4949 O  OH   . TYR   B 1 68  ? 43.218 -9.301  6.606   1.00 18.38 ?  68  TYR   B OH   1 
ATOM   4950 H  H    . TYR   B 1 68  ? 51.203 -8.472  6.868   1.00 15.55 ?  68  TYR   B H    1 
ATOM   4951 H  HA   . TYR   B 1 68  ? 49.126 -6.959  7.135   1.00 16.57 ?  68  TYR   B HA   1 
ATOM   4952 H  HB2  . TYR   B 1 68  ? 49.088 -8.446  5.407   1.00 17.59 ?  68  TYR   B HB2  1 
ATOM   4953 H  HB3  . TYR   B 1 68  ? 49.246 -9.682  6.396   1.00 17.59 ?  68  TYR   B HB3  1 
ATOM   4954 H  HD1  . TYR   B 1 68  ? 47.285 -10.447 7.687   1.00 19.63 ?  68  TYR   B HD1  1 
ATOM   4955 H  HD2  . TYR   B 1 68  ? 46.895 -7.481  5.034   1.00 19.73 ?  68  TYR   B HD2  1 
ATOM   4956 H  HE1  . TYR   B 1 68  ? 44.999 -10.644 7.821   1.00 20.80 ?  68  TYR   B HE1  1 
ATOM   4957 H  HE2  . TYR   B 1 68  ? 44.584 -7.683  5.170   1.00 20.05 ?  68  TYR   B HE2  1 
ATOM   4958 H  HH   . TYR   B 1 68  ? 42.834 -8.749  6.095   1.00 22.07 ?  68  TYR   B HH   1 
ATOM   4959 N  N    . ILE   B 1 69  ? 49.239 -9.267  9.357   1.00 13.10 ?  69  ILE   B N    1 
ATOM   4960 C  CA   . ILE   B 1 69  ? 48.681 -9.687  10.638  1.00 13.63 ?  69  ILE   B CA   1 
ATOM   4961 C  C    . ILE   B 1 69  ? 48.925 -8.632  11.710  1.00 13.44 ?  69  ILE   B C    1 
ATOM   4962 O  O    . ILE   B 1 69  ? 48.047 -8.353  12.536  1.00 13.79 ?  69  ILE   B O    1 
ATOM   4963 C  CB   . ILE   B 1 69  ? 49.253 -11.060 11.038  1.00 14.24 ?  69  ILE   B CB   1 
ATOM   4964 C  CG1  . ILE   B 1 69  ? 48.728 -12.164 10.111  1.00 14.55 ?  69  ILE   B CG1  1 
ATOM   4965 C  CG2  . ILE   B 1 69  ? 48.969 -11.371 12.501  1.00 15.46 ?  69  ILE   B CG2  1 
ATOM   4966 C  CD1  . ILE   B 1 69  ? 47.253 -12.482 10.278  1.00 15.20 ?  69  ILE   B CD1  1 
ATOM   4967 H  H    . ILE   B 1 69  ? 49.891 -9.753  9.079   1.00 15.73 ?  69  ILE   B H    1 
ATOM   4968 H  HA   . ILE   B 1 69  ? 47.725 -9.785  10.540  1.00 16.36 ?  69  ILE   B HA   1 
ATOM   4969 H  HB   . ILE   B 1 69  ? 50.219 -11.020 10.931  1.00 17.10 ?  69  ILE   B HB   1 
ATOM   4970 H  HG12 . ILE   B 1 69  ? 48.870 -11.886 9.191   1.00 17.47 ?  69  ILE   B HG12 1 
ATOM   4971 H  HG13 . ILE   B 1 69  ? 49.232 -12.977 10.283  1.00 17.47 ?  69  ILE   B HG13 1 
ATOM   4972 H  HG21 . ILE   B 1 69  ? 49.113 -12.319 12.652  1.00 18.56 ?  69  ILE   B HG21 1 
ATOM   4973 H  HG22 . ILE   B 1 69  ? 49.573 -10.857 13.061  1.00 18.56 ?  69  ILE   B HG22 1 
ATOM   4974 H  HG23 . ILE   B 1 69  ? 48.050 -11.141 12.700  1.00 18.56 ?  69  ILE   B HG23 1 
ATOM   4975 H  HD11 . ILE   B 1 69  ? 47.015 -13.190 9.661   1.00 18.25 ?  69  ILE   B HD11 1 
ATOM   4976 H  HD12 . ILE   B 1 69  ? 47.094 -12.775 11.191  1.00 18.25 ?  69  ILE   B HD12 1 
ATOM   4977 H  HD13 . ILE   B 1 69  ? 46.732 -11.689 10.089  1.00 18.25 ?  69  ILE   B HD13 1 
ATOM   4978 N  N    . ALA   B 1 70  ? 50.121 -8.044  11.739  1.00 13.38 ?  70  ALA   B N    1 
ATOM   4979 C  CA   . ALA   B 1 70  ? 50.391 -7.004  12.728  1.00 13.33 ?  70  ALA   B CA   1 
ATOM   4980 C  C    . ALA   B 1 70  ? 49.389 -5.864  12.609  1.00 13.74 ?  70  ALA   B C    1 
ATOM   4981 O  O    . ALA   B 1 70  ? 48.940 -5.318  13.620  1.00 14.22 ?  70  ALA   B O    1 
ATOM   4982 C  CB   . ALA   B 1 70  ? 51.818 -6.483  12.570  1.00 13.98 ?  70  ALA   B CB   1 
ATOM   4983 H  H    . ALA   B 1 70  ? 50.772 -8.222  11.213  1.00 16.06 ?  70  ALA   B H    1 
ATOM   4984 H  HA   . ALA   B 1 70  ? 50.314 -7.382  13.619  1.00 16.01 ?  70  ALA   B HA   1 
ATOM   4985 H  HB1  . ALA   B 1 70  ? 51.997 -5.828  13.265  1.00 16.78 ?  70  ALA   B HB1  1 
ATOM   4986 H  HB2  . ALA   B 1 70  ? 52.440 -7.225  12.654  1.00 16.78 ?  70  ALA   B HB2  1 
ATOM   4987 H  HB3  . ALA   B 1 70  ? 51.913 -6.073  11.696  1.00 16.78 ?  70  ALA   B HB3  1 
ATOM   4988 N  N    . THR   B 1 71  ? 49.025 -5.495  11.383  1.00 14.20 ?  71  THR   B N    1 
ATOM   4989 C  CA   . THR   B 1 71  ? 48.125 -4.366  11.171  1.00 15.13 ?  71  THR   B CA   1 
ATOM   4990 C  C    . THR   B 1 71  ? 46.659 -4.741  11.376  1.00 16.04 ?  71  THR   B C    1 
ATOM   4991 O  O    . THR   B 1 71  ? 45.873 -3.924  11.875  1.00 17.78 ?  71  THR   B O    1 
ATOM   4992 C  CB   . THR   B 1 71  ? 48.334 -3.815  9.760   1.00 17.28 ?  71  THR   B CB   1 
ATOM   4993 O  OG1  . THR   B 1 71  ? 49.662 -3.285  9.645   1.00 19.30 ?  71  THR   B OG1  1 
ATOM   4994 C  CG2  . THR   B 1 71  ? 47.316 -2.729  9.437   1.00 18.20 ?  71  THR   B CG2  1 
ATOM   4995 H  H    . THR   B 1 71  ? 49.292 -5.880  10.664  1.00 17.04 ?  71  THR   B H    1 
ATOM   4996 H  HA   . THR   B 1 71  ? 48.345 -3.663  11.801  1.00 18.16 ?  71  THR   B HA   1 
ATOM   4997 H  HB   . THR   B 1 71  ? 48.230 -4.531  9.115   1.00 20.74 ?  71  THR   B HB   1 
ATOM   4998 H  HG1  . THR   B 1 71  ? 49.779 -2.963  8.873   1.00 23.16 ?  71  THR   B HG1  1 
ATOM   4999 H  HG21 . THR   B 1 71  ? 47.616 -2.209  8.674   1.00 21.85 ?  71  THR   B HG21 1 
ATOM   5000 H  HG22 . THR   B 1 71  ? 46.457 -3.128  9.223   1.00 21.85 ?  71  THR   B HG22 1 
ATOM   5001 H  HG23 . THR   B 1 71  ? 47.209 -2.136  10.197  1.00 21.85 ?  71  THR   B HG23 1 
ATOM   5002 N  N    . ASN   B 1 72  ? 46.269 -5.961  10.994  1.00 15.47 ?  72  ASN   B N    1 
ATOM   5003 C  CA   . ASN   B 1 72  ? 44.865 -6.315  10.864  1.00 16.10 ?  72  ASN   B CA   1 
ATOM   5004 C  C    . ASN   B 1 72  ? 44.386 -7.405  11.809  1.00 16.32 ?  72  ASN   B C    1 
ATOM   5005 O  O    . ASN   B 1 72  ? 43.169 -7.563  11.964  1.00 17.84 ?  72  ASN   B O    1 
ATOM   5006 C  CB   . ASN   B 1 72  ? 44.553 -6.749  9.423   1.00 16.72 ?  72  ASN   B CB   1 
ATOM   5007 C  CG   . ASN   B 1 72  ? 44.824 -5.651  8.429   1.00 17.62 ?  72  ASN   B CG   1 
ATOM   5008 O  OD1  . ASN   B 1 72  ? 45.849 -5.651  7.741   1.00 19.09 ?  72  ASN   B OD1  1 
ATOM   5009 N  ND2  . ASN   B 1 72  ? 43.936 -4.680  8.380   1.00 19.15 ?  72  ASN   B ND2  1 
ATOM   5010 H  H    . ASN   B 1 72  ? 46.813 -6.607  10.802  1.00 18.57 ?  72  ASN   B H    1 
ATOM   5011 H  HA   . ASN   B 1 72  ? 44.338 -5.525  11.045  1.00 19.33 ?  72  ASN   B HA   1 
ATOM   5012 H  HB2  . ASN   B 1 72  ? 45.110 -7.509  9.193   1.00 20.07 ?  72  ASN   B HB2  1 
ATOM   5013 H  HB3  . ASN   B 1 72  ? 43.617 -6.988  9.361   1.00 20.07 ?  72  ASN   B HB3  1 
ATOM   5014 H  HD21 . ASN   B 1 72  ? 44.038 -4.026  7.830   1.00 22.99 ?  72  ASN   B HD21 1 
ATOM   5015 H  HD22 . ASN   B 1 72  ? 43.232 -4.712  8.878   1.00 22.99 ?  72  ASN   B HD22 1 
ATOM   5016 N  N    . GLY   B 1 73  ? 45.284 -8.160  12.434  1.00 15.85 ?  73  GLY   B N    1 
ATOM   5017 C  CA   . GLY   B 1 73  ? 44.877 -9.294  13.228  1.00 15.09 ?  73  GLY   B CA   1 
ATOM   5018 C  C    . GLY   B 1 73  ? 44.536 -10.488 12.364  1.00 13.84 ?  73  GLY   B C    1 
ATOM   5019 O  O    . GLY   B 1 73  ? 44.541 -10.414 11.133  1.00 14.05 ?  73  GLY   B O    1 
ATOM   5020 H  H    . GLY   B 1 73  ? 46.134 -8.030  12.412  1.00 19.02 ?  73  GLY   B H    1 
ATOM   5021 H  HA2  . GLY   B 1 73  ? 45.592 -9.537  13.837  1.00 18.11 ?  73  GLY   B HA2  1 
ATOM   5022 H  HA3  . GLY   B 1 73  ? 44.093 -9.058  13.754  1.00 18.11 ?  73  GLY   B HA3  1 
ATOM   5023 N  N    . PRO   B 1 74  ? 44.231 -11.612 13.005  1.00 13.76 ?  74  PRO   B N    1 
ATOM   5024 C  CA   . PRO   B 1 74  ? 43.990 -12.850 12.263  1.00 12.92 ?  74  PRO   B CA   1 
ATOM   5025 C  C    . PRO   B 1 74  ? 42.691 -12.800 11.472  1.00 12.89 ?  74  PRO   B C    1 
ATOM   5026 O  O    . PRO   B 1 74  ? 41.753 -12.060 11.787  1.00 14.28 ?  74  PRO   B O    1 
ATOM   5027 C  CB   . PRO   B 1 74  ? 43.914 -13.909 13.370  1.00 14.38 ?  74  PRO   B CB   1 
ATOM   5028 C  CG   . PRO   B 1 74  ? 43.454 -13.157 14.570  1.00 16.16 ?  74  PRO   B CG   1 
ATOM   5029 C  CD   . PRO   B 1 74  ? 44.117 -11.812 14.458  1.00 15.14 ?  74  PRO   B CD   1 
ATOM   5030 H  HA   . PRO   B 1 74  ? 44.737 -13.041 11.667  1.00 15.51 ?  74  PRO   B HA   1 
ATOM   5031 H  HB2  . PRO   B 1 74  ? 43.273 -14.594 13.116  1.00 17.27 ?  74  PRO   B HB2  1 
ATOM   5032 H  HB3  . PRO   B 1 74  ? 44.792 -14.296 13.512  1.00 17.27 ?  74  PRO   B HB3  1 
ATOM   5033 H  HG2  . PRO   B 1 74  ? 42.487 -13.068 14.548  1.00 19.40 ?  74  PRO   B HG2  1 
ATOM   5034 H  HG3  . PRO   B 1 74  ? 43.739 -13.618 15.372  1.00 19.40 ?  74  PRO   B HG3  1 
ATOM   5035 H  HD2  . PRO   B 1 74  ? 43.553 -11.124 14.857  1.00 18.17 ?  74  PRO   B HD2  1 
ATOM   5036 H  HD3  . PRO   B 1 74  ? 44.995 -11.830 14.870  1.00 18.17 ?  74  PRO   B HD3  1 
ATOM   5037 N  N    . LEU   B 1 75  ? 42.661 -13.610 10.420  1.00 12.34 ?  75  LEU   B N    1 
ATOM   5038 C  CA   . LEU   B 1 75  ? 41.447 -13.830 9.658   1.00 12.65 ?  75  LEU   B CA   1 
ATOM   5039 C  C    . LEU   B 1 75  ? 40.471 -14.681 10.467  1.00 13.07 ?  75  LEU   B C    1 
ATOM   5040 O  O    . LEU   B 1 75  ? 40.818 -15.267 11.493  1.00 14.12 ?  75  LEU   B O    1 
ATOM   5041 C  CB   . LEU   B 1 75  ? 41.767 -14.561 8.356   1.00 12.44 ?  75  LEU   B CB   1 
ATOM   5042 C  CG   . LEU   B 1 75  ? 42.593 -13.801 7.316   1.00 14.52 ?  75  LEU   B CG   1 
ATOM   5043 C  CD1  . LEU   B 1 75  ? 42.831 -14.657 6.081   1.00 15.94 ?  75  LEU   B CD1  1 
ATOM   5044 C  CD2  . LEU   B 1 75  ? 41.949 -12.496 6.935   1.00 18.25 ?  75  LEU   B CD2  1 
ATOM   5045 H  H    . LEU   B 1 75  ? 43.340 -14.052 10.124  1.00 14.82 ?  75  LEU   B H    1 
ATOM   5046 H  HA   . LEU   B 1 75  ? 41.024 -12.982 9.449   1.00 15.18 ?  75  LEU   B HA   1 
ATOM   5047 H  HB2  . LEU   B 1 75  ? 42.254 -15.372 8.573   1.00 14.94 ?  75  LEU   B HB2  1 
ATOM   5048 H  HB3  . LEU   B 1 75  ? 40.926 -14.806 7.928   1.00 14.94 ?  75  LEU   B HB3  1 
ATOM   5049 H  HG   . LEU   B 1 75  ? 43.458 -13.600 7.701   1.00 17.43 ?  75  LEU   B HG   1 
ATOM   5050 H  HD11 . LEU   B 1 75  ? 43.365 -14.153 5.443   1.00 19.14 ?  75  LEU   B HD11 1 
ATOM   5051 H  HD12 . LEU   B 1 75  ? 43.308 -15.464 6.339   1.00 19.14 ?  75  LEU   B HD12 1 
ATOM   5052 H  HD13 . LEU   B 1 75  ? 41.979 -14.892 5.683   1.00 19.14 ?  75  LEU   B HD13 1 
ATOM   5053 H  HD21 . LEU   B 1 75  ? 42.439 -12.108 6.198   1.00 21.91 ?  75  LEU   B HD21 1 
ATOM   5054 H  HD22 . LEU   B 1 75  ? 41.030 -12.666 6.674   1.00 21.91 ?  75  LEU   B HD22 1 
ATOM   5055 H  HD23 . LEU   B 1 75  ? 41.970 -11.902 7.701   1.00 21.91 ?  75  LEU   B HD23 1 
ATOM   5056 N  N    . LYS   B 1 76  ? 39.231 -14.743 9.982   1.00 14.33 ?  76  LYS   B N    1 
ATOM   5057 C  CA   . LYS   B 1 76  ? 38.243 -15.711 10.444  1.00 15.22 ?  76  LYS   B CA   1 
ATOM   5058 C  C    . LYS   B 1 76  ? 38.355 -16.992 9.622   1.00 13.85 ?  76  LYS   B C    1 
ATOM   5059 O  O    . LYS   B 1 76  ? 38.637 -16.951 8.426   1.00 13.55 ?  76  LYS   B O    1 
ATOM   5060 C  CB   . LYS   B 1 76  ? 36.826 -15.151 10.234  1.00 17.42 ?  76  LYS   B CB   1 
ATOM   5061 C  CG   . LYS   B 1 76  ? 36.538 -13.765 10.835  1.00 19.02 ?  76  LYS   B CG   1 
ATOM   5062 C  CD   . LYS   B 1 76  ? 35.129 -13.257 10.480  1.00 20.69 ?  76  LYS   B CD   1 
ATOM   5063 C  CE   . LYS   B 1 76  ? 34.861 -11.884 11.078  1.00 22.59 ?  76  LYS   B CE   1 
ATOM   5064 N  NZ   . LYS   B 1 76  ? 33.578 -11.292 10.608  1.00 22.98 ?  76  LYS   B NZ   1 
ATOM   5065 H  H    . LYS   B 1 76  ? 38.932 -14.222 9.366   1.00 17.20 ?  76  LYS   B H    1 
ATOM   5066 H  HA   . LYS   B 1 76  ? 38.375 -15.917 11.383  1.00 18.28 ?  76  LYS   B HA   1 
ATOM   5067 H  HB2  . LYS   B 1 76  ? 36.663 -15.088 9.280   1.00 20.91 ?  76  LYS   B HB2  1 
ATOM   5068 H  HB3  . LYS   B 1 76  ? 36.192 -15.770 10.628  1.00 20.91 ?  76  LYS   B HB3  1 
ATOM   5069 H  HG2  . LYS   B 1 76  ? 36.607 -13.814 11.802  1.00 22.83 ?  76  LYS   B HG2  1 
ATOM   5070 H  HG3  . LYS   B 1 76  ? 37.185 -13.125 10.490  1.00 22.83 ?  76  LYS   B HG3  1 
ATOM   5071 H  HD2  . LYS   B 1 76  ? 35.045 -13.188 9.515   1.00 24.84 ?  76  LYS   B HD2  1 
ATOM   5072 H  HD3  . LYS   B 1 76  ? 34.467 -13.874 10.830  1.00 24.84 ?  76  LYS   B HD3  1 
ATOM   5073 H  HE2  . LYS   B 1 76  ? 34.818 -11.962 12.044  1.00 27.11 ?  76  LYS   B HE2  1 
ATOM   5074 H  HE3  . LYS   B 1 76  ? 35.578 -11.282 10.825  1.00 27.11 ?  76  LYS   B HE3  1 
ATOM   5075 H  HZ1  . LYS   B 1 76  ? 33.455 -10.491 10.978  1.00 27.58 ?  76  LYS   B HZ1  1 
ATOM   5076 H  HZ2  . LYS   B 1 76  ? 33.589 -11.200 9.722   1.00 27.58 ?  76  LYS   B HZ2  1 
ATOM   5077 H  HZ3  . LYS   B 1 76  ? 32.896 -11.820 10.833  1.00 27.58 ?  76  LYS   B HZ3  1 
ATOM   5078 N  N    . VAL   B 1 77  ? 38.111 -18.140 10.263  1.00 14.23 ?  77  VAL   B N    1 
ATOM   5079 C  CA   . VAL   B 1 77  ? 37.904 -19.359 9.488   1.00 14.57 ?  77  VAL   B CA   1 
ATOM   5080 C  C    . VAL   B 1 77  ? 36.709 -19.137 8.567   1.00 13.55 ?  77  VAL   B C    1 
ATOM   5081 O  O    . VAL   B 1 77  ? 35.641 -18.691 9.008   1.00 13.39 ?  77  VAL   B O    1 
ATOM   5082 C  CB   . VAL   B 1 77  ? 37.710 -20.572 10.412  1.00 16.31 ?  77  VAL   B CB   1 
ATOM   5083 C  CG1  . VAL   B 1 77  ? 37.429 -21.819 9.582   1.00 17.09 ?  77  VAL   B CG1  1 
ATOM   5084 C  CG2  . VAL   B 1 77  ? 38.944 -20.785 11.301  1.00 17.77 ?  77  VAL   B CG2  1 
ATOM   5085 H  H    . VAL   B 1 77  ? 38.074 -18.237 11.116  1.00 17.08 ?  77  VAL   B H    1 
ATOM   5086 H  HA   . VAL   B 1 77  ? 38.683 -19.524 8.934   1.00 17.48 ?  77  VAL   B HA   1 
ATOM   5087 H  HB   . VAL   B 1 77  ? 36.945 -20.415 10.988  1.00 19.58 ?  77  VAL   B HB   1 
ATOM   5088 H  HG11 . VAL   B 1 77  ? 37.468 -22.596 10.161  1.00 20.51 ?  77  VAL   B HG11 1 
ATOM   5089 H  HG12 . VAL   B 1 77  ? 36.544 -21.747 9.189   1.00 20.51 ?  77  VAL   B HG12 1 
ATOM   5090 H  HG13 . VAL   B 1 77  ? 38.097 -21.890 8.885   1.00 20.51 ?  77  VAL   B HG13 1 
ATOM   5091 H  HG21 . VAL   B 1 77  ? 38.807 -21.580 11.839  1.00 21.33 ?  77  VAL   B HG21 1 
ATOM   5092 H  HG22 . VAL   B 1 77  ? 39.721 -20.895 10.735  1.00 21.33 ?  77  VAL   B HG22 1 
ATOM   5093 H  HG23 . VAL   B 1 77  ? 39.053 -20.011 11.874  1.00 21.33 ?  77  VAL   B HG23 1 
ATOM   5094 N  N    . GLY   B 1 78  ? 36.893 -19.417 7.278   1.00 12.94 ?  78  GLY   B N    1 
ATOM   5095 C  CA   . GLY   B 1 78  ? 35.912 -19.101 6.263   1.00 13.08 ?  78  GLY   B CA   1 
ATOM   5096 C  C    . GLY   B 1 78  ? 36.153 -17.786 5.552   1.00 12.40 ?  78  GLY   B C    1 
ATOM   5097 O  O    . GLY   B 1 78  ? 35.473 -17.508 4.558   1.00 12.71 ?  78  GLY   B O    1 
ATOM   5098 H  H    . GLY   B 1 78  ? 37.598 -19.800 6.967   1.00 15.53 ?  78  GLY   B H    1 
ATOM   5099 H  HA2  . GLY   B 1 78  ? 35.906 -19.803 5.601   1.00 15.70 ?  78  GLY   B HA2  1 
ATOM   5100 H  HA3  . GLY   B 1 78  ? 35.035 -19.058 6.674   1.00 15.70 ?  78  GLY   B HA3  1 
ATOM   5101 N  N    . GLY   B 1 79  ? 37.098 -16.975 6.036   1.00 12.34 ?  79  GLY   B N    1 
ATOM   5102 C  CA   . GLY   B 1 79  ? 37.396 -15.684 5.453   1.00 12.18 ?  79  GLY   B CA   1 
ATOM   5103 C  C    . GLY   B 1 79  ? 38.627 -15.707 4.558   1.00 11.52 ?  79  GLY   B C    1 
ATOM   5104 O  O    . GLY   B 1 79  ? 39.238 -16.746 4.305   1.00 12.13 ?  79  GLY   B O    1 
ATOM   5105 H  H    . GLY   B 1 79  ? 37.594 -17.161 6.713   1.00 14.82 ?  79  GLY   B H    1 
ATOM   5106 H  HA2  . GLY   B 1 79  ? 36.639 -15.384 4.922   1.00 14.62 ?  79  GLY   B HA2  1 
ATOM   5107 H  HA3  . GLY   B 1 79  ? 37.543 -15.035 6.161   1.00 14.62 ?  79  GLY   B HA3  1 
ATOM   5108 N  N    . SER   B 1 80  ? 38.994 -14.511 4.088   1.00 11.58 ?  80  SER   B N    1 
ATOM   5109 C  CA   . SER   B 1 80  ? 40.101 -14.377 3.151   1.00 11.42 ?  80  SER   B CA   1 
ATOM   5110 C  C    . SER   B 1 80  ? 40.687 -12.972 3.208   1.00 11.34 ?  80  SER   B C    1 
ATOM   5111 O  O    . SER   B 1 80  ? 40.075 -12.038 3.730   1.00 12.53 ?  80  SER   B O    1 
ATOM   5112 C  CB   . SER   B 1 80  ? 39.666 -14.672 1.713   1.00 11.86 ?  80  SER   B CB   1 
ATOM   5113 O  OG   . SER   B 1 80  ? 38.822 -13.656 1.192   1.00 12.87 ?  80  SER   B OG   1 
ATOM   5114 H  H    . SER   B 1 80  ? 38.621 -13.761 4.301   1.00 13.91 ?  80  SER   B H    1 
ATOM   5115 H  HA   . SER   B 1 80  ? 40.794 -15.002 3.401   1.00 13.71 ?  80  SER   B HA   1 
ATOM   5116 H  HB2  . SER   B 1 80  ? 40.452 -14.736 1.152   1.00 14.24 ?  80  SER   B HB2  1 
ATOM   5117 H  HB3  . SER   B 1 80  ? 39.182 -15.513 1.700   1.00 14.24 ?  80  SER   B HB3  1 
ATOM   5118 H  HG   . SER   B 1 80  ? 38.126 -13.587 1.668   1.00 15.45 ?  80  SER   B HG   1 
ATOM   5119 N  N    . CYS   B 1 81  ? 41.873 -12.825 2.620   1.00 11.30 ?  81  CYS   B N    1 
ATOM   5120 C  CA   . CYS   B 1 81  ? 42.420 -11.514 2.310   1.00 11.13 ?  81  CYS   B CA   1 
ATOM   5121 C  C    . CYS   B 1 81  ? 43.187 -11.596 0.998   1.00 10.44 ?  81  CYS   B C    1 
ATOM   5122 O  O    . CYS   B 1 81  ? 43.694 -12.658 0.618   1.00 11.54 ?  81  CYS   B O    1 
ATOM   5123 C  CB   . CYS   B 1 81  ? 43.313 -10.967 3.433   1.00 11.47 ?  81  CYS   B CB   1 
ATOM   5124 S  SG   . CYS   B 1 81  ? 44.835 -11.903 3.661   1.00 12.13 ?  81  CYS   B SG   1 
ATOM   5125 H  H    . CYS   B 1 81  ? 42.383 -13.476 2.388   1.00 13.57 ?  81  CYS   B H    1 
ATOM   5126 H  HA   . CYS   B 1 81  ? 41.684 -10.885 2.189   1.00 13.36 ?  81  CYS   B HA   1 
ATOM   5127 H  HB2  . CYS   B 1 81  ? 43.557 -10.050 3.231   1.00 13.77 ?  81  CYS   B HB2  1 
ATOM   5128 H  HB3  . CYS   B 1 81  ? 42.819 -10.992 4.273   1.00 13.77 ?  81  CYS   B HB3  1 
ATOM   5129 H  HG   . CYS   B 1 81  ? 45.471 -11.419 4.555   1.00 14.56 ?  81  CYS   B HG   1 
ATOM   5130 N  N    . VAL   B 1 82  ? 43.285 -10.453 0.322   1.00 11.07 ?  82  VAL   B N    1 
ATOM   5131 C  CA   . VAL   B 1 82  ? 44.046 -10.323 -0.915  1.00 11.09 ?  82  VAL   B CA   1 
ATOM   5132 C  C    . VAL   B 1 82  ? 45.391 -9.685  -0.602  1.00 11.12 ?  82  VAL   B C    1 
ATOM   5133 O  O    . VAL   B 1 82  ? 45.448 -8.568  -0.069  1.00 12.48 ?  82  VAL   B O    1 
ATOM   5134 C  CB   . VAL   B 1 82  ? 43.294 -9.477  -1.955  1.00 12.24 ?  82  VAL   B CB   1 
ATOM   5135 C  CG1  . VAL   B 1 82  ? 44.131 -9.337  -3.221  1.00 13.33 ?  82  VAL   B CG1  1 
ATOM   5136 C  CG2  . VAL   B 1 82  ? 41.935 -10.072 -2.259  1.00 13.19 ?  82  VAL   B CG2  1 
ATOM   5137 H  H    . VAL   B 1 82  ? 42.903 -9.717  0.567   1.00 13.29 ?  82  VAL   B H    1 
ATOM   5138 H  HA   . VAL   B 1 82  ? 44.203 -11.201 -1.290  1.00 13.32 ?  82  VAL   B HA   1 
ATOM   5139 H  HB   . VAL   B 1 82  ? 43.156 -8.587  -1.593  1.00 14.70 ?  82  VAL   B HB   1 
ATOM   5140 H  HG11 . VAL   B 1 82  ? 43.567 -9.011  -3.938  1.00 16.01 ?  82  VAL   B HG11 1 
ATOM   5141 H  HG12 . VAL   B 1 82  ? 44.854 -8.706  -3.059  1.00 16.01 ?  82  VAL   B HG12 1 
ATOM   5142 H  HG13 . VAL   B 1 82  ? 44.497 -10.204 -3.456  1.00 16.01 ?  82  VAL   B HG13 1 
ATOM   5143 H  HG21 . VAL   B 1 82  ? 41.503 -9.541  -2.949  1.00 15.84 ?  82  VAL   B HG21 1 
ATOM   5144 H  HG22 . VAL   B 1 82  ? 42.049 -10.984 -2.569  1.00 15.84 ?  82  VAL   B HG22 1 
ATOM   5145 H  HG23 . VAL   B 1 82  ? 41.395 -10.063 -1.452  1.00 15.84 ?  82  VAL   B HG23 1 
ATOM   5146 N  N    . LEU   B 1 83  ? 46.471 -10.370 -0.974  1.00 11.04 ?  83  LEU   B N    1 
ATOM   5147 C  CA   . LEU   B 1 83  ? 47.828 -9.854  -0.860  1.00 11.16 ?  83  LEU   B CA   1 
ATOM   5148 C  C    . LEU   B 1 83  ? 48.517 -10.005 -2.213  1.00 11.11 ?  83  LEU   B C    1 
ATOM   5149 O  O    . LEU   B 1 83  ? 47.904 -10.428 -3.197  1.00 11.14 ?  83  LEU   B O    1 
ATOM   5150 C  CB   . LEU   B 1 83  ? 48.582 -10.530 0.290   1.00 11.52 ?  83  LEU   B CB   1 
ATOM   5151 C  CG   . LEU   B 1 83  ? 48.088 -10.169 1.698   1.00 12.80 ?  83  LEU   B CG   1 
ATOM   5152 C  CD1  . LEU   B 1 83  ? 48.726 -11.035 2.770   1.00 13.13 ?  83  LEU   B CD1  1 
ATOM   5153 C  CD2  . LEU   B 1 83  ? 48.302 -8.682  2.010   1.00 14.33 ?  83  LEU   B CD2  1 
ATOM   5154 H  H    . LEU   B 1 83  ? 46.434 -11.161 -1.312  1.00 13.26 ?  83  LEU   B H    1 
ATOM   5155 H  HA   . LEU   B 1 83  ? 47.779 -8.909  -0.666  1.00 13.39 ?  83  LEU   B HA   1 
ATOM   5156 H  HB2  . LEU   B 1 83  ? 48.504 -11.491 0.193   1.00 13.83 ?  83  LEU   B HB2  1 
ATOM   5157 H  HB3  . LEU   B 1 83  ? 49.518 -10.275 0.234   1.00 13.83 ?  83  LEU   B HB3  1 
ATOM   5158 H  HG   . LEU   B 1 83  ? 47.135 -10.327 1.730   1.00 15.37 ?  83  LEU   B HG   1 
ATOM   5159 H  HD11 . LEU   B 1 83  ? 48.378 -10.772 3.638   1.00 15.76 ?  83  LEU   B HD11 1 
ATOM   5160 H  HD12 . LEU   B 1 83  ? 48.504 -11.964 2.596   1.00 15.76 ?  83  LEU   B HD12 1 
ATOM   5161 H  HD13 . LEU   B 1 83  ? 49.687 -10.914 2.750   1.00 15.76 ?  83  LEU   B HD13 1 
ATOM   5162 H  HD21 . LEU   B 1 83  ? 48.106 -8.524  2.947   1.00 17.20 ?  83  LEU   B HD21 1 
ATOM   5163 H  HD22 . LEU   B 1 83  ? 49.223 -8.446  1.821   1.00 17.20 ?  83  LEU   B HD22 1 
ATOM   5164 H  HD23 . LEU   B 1 83  ? 47.705 -8.152  1.456   1.00 17.20 ?  83  LEU   B HD23 1 
ATOM   5165 N  N    . SER   B 1 84  ? 49.792 -9.631  -2.278  1.00 12.26 ?  84  SER   B N    1 
ATOM   5166 C  CA   . SER   B 1 84  ? 50.532 -9.762  -3.527  1.00 12.28 ?  84  SER   B CA   1 
ATOM   5167 C  C    . SER   B 1 84  ? 50.685 -11.226 -3.918  1.00 11.20 ?  84  SER   B C    1 
ATOM   5168 O  O    . SER   B 1 84  ? 50.805 -12.107 -3.068  1.00 11.43 ?  84  SER   B O    1 
ATOM   5169 C  CB   . SER   B 1 84  ? 51.934 -9.165  -3.387  1.00 14.08 ?  84  SER   B CB   1 
ATOM   5170 O  OG   . SER   B 1 84  ? 52.671 -9.375  -4.577  1.00 15.42 ?  84  SER   B OG   1 
ATOM   5171 H  H    . SER   B 1 84  ? 50.242 -9.297  -1.626  1.00 14.72 ?  84  SER   B H    1 
ATOM   5172 H  HA   . SER   B 1 84  ? 50.065 -9.305  -4.238  1.00 14.74 ?  84  SER   B HA   1 
ATOM   5173 H  HB2  . SER   B 1 84  ? 51.858 -8.213  -3.215  1.00 16.90 ?  84  SER   B HB2  1 
ATOM   5174 H  HB3  . SER   B 1 84  ? 52.400 -9.600  -2.656  1.00 16.90 ?  84  SER   B HB3  1 
ATOM   5175 H  HG   . SER   B 1 84  ? 53.439 -9.030  -4.513  1.00 18.51 ?  84  SER   B HG   1 
ATOM   5176 N  N    . GLY   B 1 85  ? 50.750 -11.469 -5.221  1.00 12.03 ?  85  GLY   B N    1 
ATOM   5177 C  CA   . GLY   B 1 85  ? 51.110 -12.769 -5.735  1.00 12.93 ?  85  GLY   B CA   1 
ATOM   5178 C  C    . GLY   B 1 85  ? 52.576 -12.951 -6.053  1.00 12.34 ?  85  GLY   B C    1 
ATOM   5179 O  O    . GLY   B 1 85  ? 52.957 -14.030 -6.511  1.00 12.77 ?  85  GLY   B O    1 
ATOM   5180 H  H    . GLY   B 1 85  ? 50.596 -10.892 -5.831  1.00 14.44 ?  85  GLY   B H    1 
ATOM   5181 H  HA2  . GLY   B 1 85  ? 50.860 -13.450 -5.084  1.00 15.52 ?  85  GLY   B HA2  1 
ATOM   5182 H  HA3  . GLY   B 1 85  ? 50.608 -12.941 -6.544  1.00 15.52 ?  85  GLY   B HA3  1 
ATOM   5183 N  N    . HIS   B 1 86  ? 53.424 -11.944 -5.849  1.00 12.43 ?  86  HIS   B N    1 
ATOM   5184 C  CA   . HIS   B 1 86  ? 54.887 -12.108 -5.940  1.00 12.74 ?  86  HIS   B CA   1 
ATOM   5185 C  C    . HIS   B 1 86  ? 55.260 -12.625 -7.327  1.00 12.64 ?  86  HIS   B C    1 
ATOM   5186 O  O    . HIS   B 1 86  ? 54.868 -12.015 -8.334  1.00 13.38 ?  86  HIS   B O    1 
ATOM   5187 C  CB   . HIS   B 1 86  ? 55.383 -12.946 -4.763  1.00 12.86 ?  86  HIS   B CB   1 
ATOM   5188 C  CG   . HIS   B 1 86  ? 55.069 -12.335 -3.439  1.00 12.62 ?  86  HIS   B CG   1 
ATOM   5189 N  ND1  . HIS   B 1 86  ? 55.897 -11.421 -2.826  1.00 14.46 ?  86  HIS   B ND1  1 
ATOM   5190 C  CD2  . HIS   B 1 86  ? 53.995 -12.477 -2.628  1.00 13.14 ?  86  HIS   B CD2  1 
ATOM   5191 C  CE1  . HIS   B 1 86  ? 55.343 -11.024 -1.694  1.00 13.94 ?  86  HIS   B CE1  1 
ATOM   5192 N  NE2  . HIS   B 1 86  ? 54.184 -11.645 -1.553  1.00 13.52 ?  86  HIS   B NE2  1 
ATOM   5193 H  H    . HIS   B 1 86  ? 53.175 -11.144 -5.655  1.00 14.92 ?  86  HIS   B H    1 
ATOM   5194 H  HA   . HIS   B 1 86  ? 55.291 -11.235 -5.848  1.00 15.29 ?  86  HIS   B HA   1 
ATOM   5195 H  HB2  . HIS   B 1 86  ? 54.967 -13.822 -4.796  1.00 15.44 ?  86  HIS   B HB2  1 
ATOM   5196 H  HB3  . HIS   B 1 86  ? 56.349 -13.038 -4.825  1.00 15.44 ?  86  HIS   B HB3  1 
ATOM   5197 H  HD2  . HIS   B 1 86  ? 53.255 -13.023 -2.781  1.00 15.78 ?  86  HIS   B HD2  1 
ATOM   5198 H  HE1  . HIS   B 1 86  ? 55.712 -10.424 -1.088  1.00 16.73 ?  86  HIS   B HE1  1 
ATOM   5199 H  HE2  . HIS   B 1 86  ? 53.648 -11.567 -0.884  1.00 16.23 ?  86  HIS   B HE2  1 
ATOM   5200 N  N    . ASN   B 1 87  ? 56.022 -13.713 -7.434  1.00 12.75 ?  87  ASN   B N    1 
ATOM   5201 C  CA   . ASN   B 1 87  ? 56.402 -14.287 -8.715  1.00 13.68 ?  87  ASN   B CA   1 
ATOM   5202 C  C    . ASN   B 1 87  ? 55.411 -15.319 -9.220  1.00 13.46 ?  87  ASN   B C    1 
ATOM   5203 O  O    . ASN   B 1 87  ? 55.712 -16.016 -10.194 1.00 15.10 ?  87  ASN   B O    1 
ATOM   5204 C  CB   . ASN   B 1 87  ? 57.789 -14.929 -8.613  1.00 15.16 ?  87  ASN   B CB   1 
ATOM   5205 C  CG   . ASN   B 1 87  ? 57.856 -16.030 -7.557  1.00 16.06 ?  87  ASN   B CG   1 
ATOM   5206 O  OD1  . ASN   B 1 87  ? 57.230 -15.939 -6.494  1.00 15.10 ?  87  ASN   B OD1  1 
ATOM   5207 N  ND2  . ASN   B 1 87  ? 58.616 -17.092 -7.857  1.00 18.47 ?  87  ASN   B ND2  1 
ATOM   5208 H  H    . ASN   B 1 87  ? 56.326 -14.150 -6.761  1.00 15.30 ?  87  ASN   B H    1 
ATOM   5209 H  HA   . ASN   B 1 87  ? 56.450 -13.582 -9.372  1.00 16.43 ?  87  ASN   B HA   1 
ATOM   5210 H  HB2  . ASN   B 1 87  ? 58.024 -15.319 -9.473  1.00 18.20 ?  87  ASN   B HB2  1 
ATOM   5211 H  HB3  . ASN   B 1 87  ? 58.435 -14.246 -8.375  1.00 18.20 ?  87  ASN   B HB3  1 
ATOM   5212 H  HD21 . ASN   B 1 87  ? 58.694 -17.739 -7.299  1.00 22.17 ?  87  ASN   B HD21 1 
ATOM   5213 H  HD22 . ASN   B 1 87  ? 59.041 -17.124 -8.610  1.00 22.17 ?  87  ASN   B HD22 1 
ATOM   5214 N  N    . LEU   B 1 88  ? 54.240 -15.427 -8.591  1.00 12.73 ?  88  LEU   B N    1 
ATOM   5215 C  CA   . LEU   B 1 88  ? 53.256 -16.453 -8.914  1.00 13.34 ?  88  LEU   B CA   1 
ATOM   5216 C  C    . LEU   B 1 88  ? 52.025 -15.927 -9.634  1.00 12.87 ?  88  LEU   B C    1 
ATOM   5217 O  O    . LEU   B 1 88  ? 51.422 -16.664 -10.424 1.00 14.09 ?  88  LEU   B O    1 
ATOM   5218 C  CB   . LEU   B 1 88  ? 52.786 -17.133 -7.624  1.00 13.94 ?  88  LEU   B CB   1 
ATOM   5219 C  CG   . LEU   B 1 88  ? 53.903 -17.810 -6.842  1.00 16.06 ?  88  LEU   B CG   1 
ATOM   5220 C  CD1  . LEU   B 1 88  ? 53.428 -18.132 -5.437  1.00 17.87 ?  88  LEU   B CD1  1 
ATOM   5221 C  CD2  . LEU   B 1 88  ? 54.347 -19.066 -7.569  1.00 19.20 ?  88  LEU   B CD2  1 
ATOM   5222 H  H    . LEU   B 1 88  ? 53.990 -14.907 -7.949  1.00 15.28 ?  88  LEU   B H    1 
ATOM   5223 H  HA   . LEU   B 1 88  ? 53.668 -17.123 -9.473  1.00 16.01 ?  88  LEU   B HA   1 
ATOM   5224 H  HB2  . LEU   B 1 88  ? 52.379 -16.466 -7.045  1.00 16.74 ?  88  LEU   B HB2  1 
ATOM   5225 H  HB3  . LEU   B 1 88  ? 52.127 -17.811 -7.851  1.00 16.74 ?  88  LEU   B HB3  1 
ATOM   5226 H  HG   . LEU   B 1 88  ? 54.661 -17.207 -6.781  1.00 19.28 ?  88  LEU   B HG   1 
ATOM   5227 H  HD11 . LEU   B 1 88  ? 54.060 -18.739 -5.026  1.00 21.45 ?  88  LEU   B HD11 1 
ATOM   5228 H  HD12 . LEU   B 1 88  ? 53.375 -17.309 -4.928  1.00 21.45 ?  88  LEU   B HD12 1 
ATOM   5229 H  HD13 . LEU   B 1 88  ? 52.554 -18.546 -5.492  1.00 21.45 ?  88  LEU   B HD13 1 
ATOM   5230 H  HD21 . LEU   B 1 88  ? 55.004 -19.525 -7.026  1.00 23.04 ?  88  LEU   B HD21 1 
ATOM   5231 H  HD22 . LEU   B 1 88  ? 53.576 -19.635 -7.713  1.00 23.04 ?  88  LEU   B HD22 1 
ATOM   5232 H  HD23 . LEU   B 1 88  ? 54.739 -18.817 -8.422  1.00 23.04 ?  88  LEU   B HD23 1 
ATOM   5233 N  N    . ALA   B 1 89  ? 51.626 -14.690 -9.361  1.00 12.44 ?  89  ALA   B N    1 
ATOM   5234 C  CA   . ALA   B 1 89  ? 50.337 -14.185 -9.808  1.00 11.47 ?  89  ALA   B CA   1 
ATOM   5235 C  C    . ALA   B 1 89  ? 50.321 -12.696 -9.515  1.00 11.88 ?  89  ALA   B C    1 
ATOM   5236 O  O    . ALA   B 1 89  ? 51.160 -12.193 -8.767  1.00 12.75 ?  89  ALA   B O    1 
ATOM   5237 C  CB   . ALA   B 1 89  ? 49.201 -14.867 -9.057  1.00 11.72 ?  89  ALA   B CB   1 
ATOM   5238 H  H    . ALA   B 1 89  ? 52.088 -14.114 -8.918  1.00 14.94 ?  89  ALA   B H    1 
ATOM   5239 H  HA   . ALA   B 1 89  ? 50.229 -14.326 -10.768 1.00 13.77 ?  89  ALA   B HA   1 
ATOM   5240 H  HB1  . ALA   B 1 89  ? 48.355 -14.529 -9.391  1.00 14.07 ?  89  ALA   B HB1  1 
ATOM   5241 H  HB2  . ALA   B 1 89  ? 49.256 -15.826 -9.212  1.00 14.07 ?  89  ALA   B HB2  1 
ATOM   5242 H  HB3  . ALA   B 1 89  ? 49.291 -14.677 -8.115  1.00 14.07 ?  89  ALA   B HB3  1 
ATOM   5243 N  N    . LYS   B 1 90  ? 49.352 -11.991 -10.091 1.00 12.73 ?  90  LYS   B N    1 
ATOM   5244 C  CA   . LYS   B 1 90  ? 49.163 -10.606 -9.680  1.00 12.69 ?  90  LYS   B CA   1 
ATOM   5245 C  C    . LYS   B 1 90  ? 48.848 -10.535 -8.192  1.00 12.13 ?  90  LYS   B C    1 
ATOM   5246 O  O    . LYS   B 1 90  ? 49.489 -9.784  -7.443  1.00 13.20 ?  90  LYS   B O    1 
ATOM   5247 C  CB   . LYS   B 1 90  ? 48.082 -9.943  -10.530 1.00 14.15 ?  90  LYS   B CB   1 
ATOM   5248 C  CG   . LYS   B 1 90  ? 47.763 -8.518  -10.115 1.00 14.36 ?  90  LYS   B CG   1 
ATOM   5249 C  CD   . LYS   B 1 90  ? 48.943 -7.589  -10.212 1.00 16.74 ?  90  LYS   B CD   1 
ATOM   5250 C  CE   . LYS   B 1 90  ? 48.467 -6.183  -9.926  1.00 18.66 ?  90  LYS   B CE   1 
ATOM   5251 N  NZ   . LYS   B 1 90  ? 49.597 -5.223  -9.833  1.00 18.17 ?  90  LYS   B NZ   1 
ATOM   5252 H  H    . LYS   B 1 90  ? 48.813 -12.279 -10.698 1.00 15.29 ?  90  LYS   B H    1 
ATOM   5253 H  HA   . LYS   B 1 90  ? 49.990 -10.124 -9.832  1.00 15.23 ?  90  LYS   B HA   1 
ATOM   5254 H  HB2  . LYS   B 1 90  ? 48.379 -9.916  -11.457 1.00 16.99 ?  90  LYS   B HB2  1 
ATOM   5255 H  HB3  . LYS   B 1 90  ? 47.265 -10.459 -10.466 1.00 16.99 ?  90  LYS   B HB3  1 
ATOM   5256 H  HG2  . LYS   B 1 90  ? 47.065 -8.169  -10.694 1.00 17.24 ?  90  LYS   B HG2  1 
ATOM   5257 H  HG3  . LYS   B 1 90  ? 47.450 -8.512  -9.194  1.00 17.24 ?  90  LYS   B HG3  1 
ATOM   5258 H  HD2  . LYS   B 1 90  ? 49.612 -7.829  -9.551  1.00 20.10 ?  90  LYS   B HD2  1 
ATOM   5259 H  HD3  . LYS   B 1 90  ? 49.316 -7.617  -11.107 1.00 20.10 ?  90  LYS   B HD3  1 
ATOM   5260 H  HE2  . LYS   B 1 90  ? 47.885 -5.884  -10.645 1.00 22.40 ?  90  LYS   B HE2  1 
ATOM   5261 H  HE3  . LYS   B 1 90  ? 47.991 -6.162  -9.082  1.00 22.40 ?  90  LYS   B HE3  1 
ATOM   5262 H  HZ1  . LYS   B 1 90  ? 49.294 -4.400  -9.667  1.00 21.80 ?  90  LYS   B HZ1  1 
ATOM   5263 H  HZ2  . LYS   B 1 90  ? 50.149 -5.462  -9.177  1.00 21.80 ?  90  LYS   B HZ2  1 
ATOM   5264 H  HZ3  . LYS   B 1 90  ? 50.052 -5.208  -10.600 1.00 21.80 ?  90  LYS   B HZ3  1 
ATOM   5265 N  N    . HIS   B 1 91  ? 47.875 -11.339 -7.745  1.00 11.14 ?  91  HIS   B N    1 
ATOM   5266 C  CA   . HIS   B 1 91  ? 47.412 -11.366 -6.370  1.00 11.40 ?  91  HIS   B CA   1 
ATOM   5267 C  C    . HIS   B 1 91  ? 47.407 -12.795 -5.854  1.00 10.35 ?  91  HIS   B C    1 
ATOM   5268 O  O    . HIS   B 1 91  ? 47.175 -13.746 -6.611  1.00 11.03 ?  91  HIS   B O    1 
ATOM   5269 C  CB   . HIS   B 1 91  ? 45.956 -10.882 -6.249  1.00 12.63 ?  91  HIS   B CB   1 
ATOM   5270 C  CG   . HIS   B 1 91  ? 45.749 -9.470  -6.672  1.00 15.98 ?  91  HIS   B CG   1 
ATOM   5271 N  ND1  . HIS   B 1 91  ? 46.373 -8.404  -6.059  1.00 18.66 ?  91  HIS   B ND1  1 
ATOM   5272 C  CD2  . HIS   B 1 91  ? 44.957 -8.942  -7.630  1.00 18.51 ?  91  HIS   B CD2  1 
ATOM   5273 C  CE1  . HIS   B 1 91  ? 45.990 -7.279  -6.638  1.00 19.62 ?  91  HIS   B CE1  1 
ATOM   5274 N  NE2  . HIS   B 1 91  ? 45.126 -7.578  -7.591  1.00 20.04 ?  91  HIS   B NE2  1 
ATOM   5275 H  H    . HIS   B 1 91  ? 47.452 -11.892 -8.250  1.00 13.38 ?  91  HIS   B H    1 
ATOM   5276 H  HA   . HIS   B 1 91  ? 47.982 -10.811 -5.808  1.00 13.69 ?  91  HIS   B HA   1 
ATOM   5277 H  HB2  . HIS   B 1 91  ? 45.394 -11.441 -6.805  1.00 15.16 ?  91  HIS   B HB2  1 
ATOM   5278 H  HB3  . HIS   B 1 91  ? 45.678 -10.954 -5.321  1.00 15.16 ?  91  HIS   B HB3  1 
ATOM   5279 H  HD2  . HIS   B 1 91  ? 44.405 -9.406  -8.215  1.00 22.22 ?  91  HIS   B HD2  1 
ATOM   5280 H  HE1  . HIS   B 1 91  ? 46.273 -6.421  -6.405  1.00 23.56 ?  91  HIS   B HE1  1 
ATOM   5281 H  HE2  . HIS   B 1 91  ? 44.739 -7.005  -8.108  1.00 24.06 ?  91  HIS   B HE2  1 
ATOM   5282 N  N    . CYS   B 1 92  ? 47.584 -12.930 -4.549  1.00 10.36 ?  92  CYS   B N    1 
ATOM   5283 C  CA   . CYS   B 1 92  ? 47.289 -14.166 -3.841  1.00 10.08 ?  92  CYS   B CA   1 
ATOM   5284 C  C    . CYS   B 1 92  ? 46.065 -13.928 -2.961  1.00 9.83  ?  92  CYS   B C    1 
ATOM   5285 O  O    . CYS   B 1 92  ? 46.067 -13.026 -2.113  1.00 10.67 ?  92  CYS   B O    1 
ATOM   5286 C  CB   . CYS   B 1 92  ? 48.469 -14.628 -2.990  1.00 10.56 ?  92  CYS   B CB   1 
ATOM   5287 S  SG   . CYS   B 1 92  ? 48.099 -16.164 -2.095  1.00 10.77 ?  92  CYS   B SG   1 
ATOM   5288 H  H    . CYS   B 1 92  ? 47.894 -12.303 -4.037  1.00 12.44 ?  92  CYS   B H    1 
ATOM   5289 H  HA   . CYS   B 1 92  ? 47.085 -14.859 -4.486  1.00 12.11 ?  92  CYS   B HA   1 
ATOM   5290 H  HB2  . CYS   B 1 92  ? 49.231 -14.786 -3.563  1.00 12.68 ?  92  CYS   B HB2  1 
ATOM   5291 H  HB3  . CYS   B 1 92  ? 48.674 -13.940 -2.338  1.00 12.68 ?  92  CYS   B HB3  1 
ATOM   5292 H  HG   . CYS   B 1 92  ? 49.073 -16.483 -1.469  1.00 12.93 ?  92  CYS   B HG   1 
ATOM   5293 N  N    . LEU   B 1 93  ? 45.026 -14.732 -3.173  1.00 9.78  ?  93  LEU   B N    1 
ATOM   5294 C  CA   . LEU   B 1 93  ? 43.856 -14.750 -2.304  1.00 9.77  ?  93  LEU   B CA   1 
ATOM   5295 C  C    . LEU   B 1 93  ? 44.084 -15.817 -1.240  1.00 9.47  ?  93  LEU   B C    1 
ATOM   5296 O  O    . LEU   B 1 93  ? 44.033 -17.018 -1.534  1.00 10.23 ?  93  LEU   B O    1 
ATOM   5297 C  CB   . LEU   B 1 93  ? 42.595 -15.037 -3.113  1.00 10.31 ?  93  LEU   B CB   1 
ATOM   5298 C  CG   . LEU   B 1 93  ? 41.296 -15.056 -2.304  1.00 11.08 ?  93  LEU   B CG   1 
ATOM   5299 C  CD1  . LEU   B 1 93  ? 40.940 -13.666 -1.802  1.00 11.60 ?  93  LEU   B CD1  1 
ATOM   5300 C  CD2  . LEU   B 1 93  ? 40.166 -15.649 -3.130  1.00 11.51 ?  93  LEU   B CD2  1 
ATOM   5301 H  H    . LEU   B 1 93  ? 44.977 -15.298 -3.832  1.00 11.75 ?  93  LEU   B H    1 
ATOM   5302 H  HA   . LEU   B 1 93  ? 43.761 -13.891 -1.875  1.00 11.72 ?  93  LEU   B HA   1 
ATOM   5303 H  HB2  . LEU   B 1 93  ? 42.497 -14.349 -3.793  1.00 12.38 ?  93  LEU   B HB2  1 
ATOM   5304 H  HB3  . LEU   B 1 93  ? 42.679 -15.902 -3.536  1.00 12.38 ?  93  LEU   B HB3  1 
ATOM   5305 H  HG   . LEU   B 1 93  ? 41.417 -15.619 -1.528  1.00 13.30 ?  93  LEU   B HG   1 
ATOM   5306 H  HD11 . LEU   B 1 93  ? 40.087 -13.701 -1.342  1.00 13.93 ?  93  LEU   B HD11 1 
ATOM   5307 H  HD12 . LEU   B 1 93  ? 41.632 -13.361 -1.192  1.00 13.93 ?  93  LEU   B HD12 1 
ATOM   5308 H  HD13 . LEU   B 1 93  ? 40.880 -13.059 -2.559  1.00 13.93 ?  93  LEU   B HD13 1 
ATOM   5309 H  HD21 . LEU   B 1 93  ? 39.348 -15.639 -2.604  1.00 13.82 ?  93  LEU   B HD21 1 
ATOM   5310 H  HD22 . LEU   B 1 93  ? 40.045 -15.118 -3.933  1.00 13.82 ?  93  LEU   B HD22 1 
ATOM   5311 H  HD23 . LEU   B 1 93  ? 40.393 -16.561 -3.367  1.00 13.82 ?  93  LEU   B HD23 1 
ATOM   5312 N  N    . HIS   B 1 94  ? 44.374 -15.383 -0.021  1.00 9.29  ?  94  HIS   B N    1 
ATOM   5313 C  CA   . HIS   B 1 94  ? 44.580 -16.289 1.102   1.00 9.79  ?  94  HIS   B CA   1 
ATOM   5314 C  C    . HIS   B 1 94  ? 43.219 -16.636 1.680   1.00 10.09 ?  94  HIS   B C    1 
ATOM   5315 O  O    . HIS   B 1 94  ? 42.555 -15.764 2.242   1.00 11.84 ?  94  HIS   B O    1 
ATOM   5316 C  CB   . HIS   B 1 94  ? 45.453 -15.619 2.158   1.00 10.05 ?  94  HIS   B CB   1 
ATOM   5317 C  CG   . HIS   B 1 94  ? 46.831 -15.315 1.680   1.00 10.05 ?  94  HIS   B CG   1 
ATOM   5318 N  ND1  . HIS   B 1 94  ? 47.862 -16.227 1.760   1.00 10.33 ?  94  HIS   B ND1  1 
ATOM   5319 C  CD2  . HIS   B 1 94  ? 47.340 -14.200 1.099   1.00 10.22 ?  94  HIS   B CD2  1 
ATOM   5320 C  CE1  . HIS   B 1 94  ? 48.947 -15.677 1.246   1.00 10.36 ?  94  HIS   B CE1  1 
ATOM   5321 N  NE2  . HIS   B 1 94  ? 48.662 -14.449 0.843   1.00 10.40 ?  94  HIS   B NE2  1 
ATOM   5322 H  H    . HIS   B 1 94  ? 44.462 -14.544 0.183   1.00 11.15 ?  94  HIS   B H    1 
ATOM   5323 H  HA   . HIS   B 1 94  ? 45.017 -17.096 0.795   1.00 11.75 ?  94  HIS   B HA   1 
ATOM   5324 H  HB2  . HIS   B 1 94  ? 45.044 -14.782 2.426   1.00 12.07 ?  94  HIS   B HB2  1 
ATOM   5325 H  HB3  . HIS   B 1 94  ? 45.529 -16.210 2.923   1.00 12.07 ?  94  HIS   B HB3  1 
ATOM   5326 H  HD2  . HIS   B 1 94  ? 46.881 -13.419 0.906   1.00 12.27 ?  94  HIS   B HD2  1 
ATOM   5327 H  HE1  . HIS   B 1 94  ? 49.782 -16.094 1.190   1.00 12.44 ?  94  HIS   B HE1  1 
ATOM   5328 H  HE2  . HIS   B 1 94  ? 49.218 -13.911 0.476   1.00 12.49 ?  94  HIS   B HE2  1 
ATOM   5329 N  N    . VAL   B 1 95  ? 42.789 -17.892 1.533   1.00 10.39 ?  95  VAL   B N    1 
ATOM   5330 C  CA   . VAL   B 1 95  ? 41.464 -18.335 1.965   1.00 10.25 ?  95  VAL   B CA   1 
ATOM   5331 C  C    . VAL   B 1 95  ? 41.630 -19.371 3.062   1.00 9.95  ?  95  VAL   B C    1 
ATOM   5332 O  O    . VAL   B 1 95  ? 42.407 -20.319 2.905   1.00 11.07 ?  95  VAL   B O    1 
ATOM   5333 C  CB   . VAL   B 1 95  ? 40.647 -18.933 0.802   1.00 10.35 ?  95  VAL   B CB   1 
ATOM   5334 C  CG1  . VAL   B 1 95  ? 39.277 -19.371 1.294   1.00 11.79 ?  95  VAL   B CG1  1 
ATOM   5335 C  CG2  . VAL   B 1 95  ? 40.526 -17.947 -0.332  1.00 10.51 ?  95  VAL   B CG2  1 
ATOM   5336 H  H    . VAL   B 1 95  ? 43.259 -18.514 1.165   1.00 12.48 ?  95  VAL   B H    1 
ATOM   5337 H  HA   . VAL   B 1 95  ? 40.974 -17.584 2.326   1.00 12.31 ?  95  VAL   B HA   1 
ATOM   5338 H  HB   . VAL   B 1 95  ? 41.106 -19.716 0.464   1.00 12.42 ?  95  VAL   B HB   1 
ATOM   5339 H  HG11 . VAL   B 1 95  ? 38.706 -19.549 0.526   1.00 14.16 ?  95  VAL   B HG11 1 
ATOM   5340 H  HG12 . VAL   B 1 95  ? 39.368 -20.179 1.824   1.00 14.16 ?  95  VAL   B HG12 1 
ATOM   5341 H  HG13 . VAL   B 1 95  ? 38.888 -18.664 1.831   1.00 14.16 ?  95  VAL   B HG13 1 
ATOM   5342 H  HG21 . VAL   B 1 95  ? 39.949 -18.323 -1.012  1.00 12.62 ?  95  VAL   B HG21 1 
ATOM   5343 H  HG22 . VAL   B 1 95  ? 40.145 -17.124 0.011   1.00 12.62 ?  95  VAL   B HG22 1 
ATOM   5344 H  HG23 . VAL   B 1 95  ? 41.408 -17.780 -0.694  1.00 12.62 ?  95  VAL   B HG23 1 
ATOM   5345 N  N    . VAL   B 1 96  ? 40.904 -19.203 4.158   1.00 10.87 ?  96  VAL   B N    1 
ATOM   5346 C  CA   . VAL   B 1 96  ? 40.991 -20.112 5.300   1.00 10.96 ?  96  VAL   B CA   1 
ATOM   5347 C  C    . VAL   B 1 96  ? 39.803 -21.070 5.256   1.00 11.58 ?  96  VAL   B C    1 
ATOM   5348 O  O    . VAL   B 1 96  ? 38.685 -20.714 5.638   1.00 12.21 ?  96  VAL   B O    1 
ATOM   5349 C  CB   . VAL   B 1 96  ? 41.045 -19.360 6.632   1.00 11.72 ?  96  VAL   B CB   1 
ATOM   5350 C  CG1  . VAL   B 1 96  ? 41.206 -20.346 7.771   1.00 12.49 ?  96  VAL   B CG1  1 
ATOM   5351 C  CG2  . VAL   B 1 96  ? 42.162 -18.329 6.645   1.00 12.58 ?  96  VAL   B CG2  1 
ATOM   5352 H  H    . VAL   B 1 96  ? 40.346 -18.558 4.272   1.00 13.05 ?  96  VAL   B H    1 
ATOM   5353 H  HA   . VAL   B 1 96  ? 41.804 -20.637 5.225   1.00 13.16 ?  96  VAL   B HA   1 
ATOM   5354 H  HB   . VAL   B 1 96  ? 40.204 -18.893 6.765   1.00 14.07 ?  96  VAL   B HB   1 
ATOM   5355 H  HG11 . VAL   B 1 96  ? 41.407 -19.858 8.590   1.00 14.99 ?  96  VAL   B HG11 1 
ATOM   5356 H  HG12 . VAL   B 1 96  ? 40.381 -20.845 7.888   1.00 14.99 ?  96  VAL   B HG12 1 
ATOM   5357 H  HG13 . VAL   B 1 96  ? 41.934 -20.954 7.569   1.00 14.99 ?  96  VAL   B HG13 1 
ATOM   5358 H  HG21 . VAL   B 1 96  ? 42.202 -17.914 7.523   1.00 15.11 ?  96  VAL   B HG21 1 
ATOM   5359 H  HG22 . VAL   B 1 96  ? 43.002 -18.768 6.448   1.00 15.11 ?  96  VAL   B HG22 1 
ATOM   5360 H  HG23 . VAL   B 1 96  ? 41.975 -17.653 5.973   1.00 15.11 ?  96  VAL   B HG23 1 
ATOM   5361 N  N    . GLY   B 1 97  ? 40.036 -22.297 4.805   1.00 11.73 ?  97  GLY   B N    1 
ATOM   5362 C  CA   . GLY   B 1 97  ? 39.068 -23.356 4.978   1.00 12.09 ?  97  GLY   B CA   1 
ATOM   5363 C  C    . GLY   B 1 97  ? 39.208 -23.962 6.357   1.00 13.47 ?  97  GLY   B C    1 
ATOM   5364 O  O    . GLY   B 1 97  ? 40.255 -23.841 7.004   1.00 14.34 ?  97  GLY   B O    1 
ATOM   5365 H  H    . GLY   B 1 97  ? 40.756 -22.534 4.394   1.00 14.08 ?  97  GLY   B H    1 
ATOM   5366 H  HA2  . GLY   B 1 97  ? 38.173 -22.993 4.869   1.00 14.51 ?  97  GLY   B HA2  1 
ATOM   5367 H  HA3  . GLY   B 1 97  ? 39.210 -24.042 4.306   1.00 14.51 ?  97  GLY   B HA3  1 
ATOM   5368 N  N    . PRO   B 1 98  ? 38.159 -24.633 6.834   1.00 14.45 ?  98  PRO   B N    1 
ATOM   5369 C  CA   . PRO   B 1 98  ? 38.256 -25.322 8.124   1.00 15.69 ?  98  PRO   B CA   1 
ATOM   5370 C  C    . PRO   B 1 98  ? 39.280 -26.444 8.076   1.00 15.36 ?  98  PRO   B C    1 
ATOM   5371 O  O    . PRO   B 1 98  ? 39.371 -27.186 7.099   1.00 15.57 ?  98  PRO   B O    1 
ATOM   5372 C  CB   . PRO   B 1 98  ? 36.838 -25.866 8.338   1.00 16.08 ?  98  PRO   B CB   1 
ATOM   5373 C  CG   . PRO   B 1 98  ? 36.280 -26.015 6.964   1.00 15.59 ?  98  PRO   B CG   1 
ATOM   5374 C  CD   . PRO   B 1 98  ? 36.842 -24.835 6.203   1.00 14.89 ?  98  PRO   B CD   1 
ATOM   5375 H  HA   . PRO   B 1 98  ? 38.478 -24.701 8.827   1.00 18.83 ?  98  PRO   B HA   1 
ATOM   5376 H  HB2  . PRO   B 1 98  ? 36.878 -26.728 8.785   1.00 19.31 ?  98  PRO   B HB2  1 
ATOM   5377 H  HB3  . PRO   B 1 98  ? 36.315 -25.235 8.850   1.00 19.31 ?  98  PRO   B HB3  1 
ATOM   5378 H  HG2  . PRO   B 1 98  ? 36.580 -26.858 6.578   1.00 18.72 ?  98  PRO   B HG2  1 
ATOM   5379 H  HG3  . PRO   B 1 98  ? 35.310 -25.983 6.998   1.00 18.72 ?  98  PRO   B HG3  1 
ATOM   5380 H  HD2  . PRO   B 1 98  ? 36.937 -25.062 5.259   1.00 17.87 ?  98  PRO   B HD2  1 
ATOM   5381 H  HD3  . PRO   B 1 98  ? 36.281 -24.057 6.325   1.00 17.87 ?  98  PRO   B HD3  1 
ATOM   5382 N  N    . ASN   B 1 99  ? 40.033 -26.577 9.160   1.00 16.50 ?  99  ASN   B N    1 
ATOM   5383 C  CA   . ASN   B 1 99  ? 41.016 -27.647 9.315   1.00 17.47 ?  99  ASN   B CA   1 
ATOM   5384 C  C    . ASN   B 1 99  ? 40.396 -28.728 10.199  1.00 19.96 ?  99  ASN   B C    1 
ATOM   5385 O  O    . ASN   B 1 99  ? 40.330 -28.583 11.422  1.00 20.88 ?  99  ASN   B O    1 
ATOM   5386 C  CB   . ASN   B 1 99  ? 42.298 -27.089 9.921   1.00 17.58 ?  99  ASN   B CB   1 
ATOM   5387 C  CG   . ASN   B 1 99  ? 43.436 -28.097 9.928   1.00 18.76 ?  99  ASN   B CG   1 
ATOM   5388 O  OD1  . ASN   B 1 99  ? 43.224 -29.285 10.132  1.00 19.52 ?  99  ASN   B OD1  1 
ATOM   5389 N  ND2  . ASN   B 1 99  ? 44.647 -27.623 9.690   1.00 18.88 ?  99  ASN   B ND2  1 
ATOM   5390 H  H    . ASN   B 1 99  ? 39.990 -26.048 9.833   1.00 19.80 ?  99  ASN   B H    1 
ATOM   5391 H  HA   . ASN   B 1 99  ? 41.217 -28.037 8.450   1.00 20.97 ?  99  ASN   B HA   1 
ATOM   5392 H  HB2  . ASN   B 1 99  ? 42.575 -26.321 9.410   1.00 21.10 ?  99  ASN   B HB2  1 
ATOM   5393 H  HB3  . ASN   B 1 99  ? 42.118 -26.834 10.842  1.00 21.10 ?  99  ASN   B HB3  1 
ATOM   5394 H  HD21 . ASN   B 1 99  ? 45.318 -28.155 9.683   1.00 22.66 ?  99  ASN   B HD21 1 
ATOM   5395 H  HD22 . ASN   B 1 99  ? 44.753 -26.782 9.558   1.00 22.66 ?  99  ASN   B HD22 1 
ATOM   5396 N  N    A VAL   B 1 100 ? 39.931 -29.814 9.572   0.66 22.08 ?  100 VAL   B N    1 
ATOM   5397 N  N    B VAL   B 1 100 ? 39.943 -29.816 9.566   0.34 22.12 ?  100 VAL   B N    1 
ATOM   5398 C  CA   A VAL   B 1 100 ? 39.323 -30.904 10.331  0.66 24.68 ?  100 VAL   B CA   1 
ATOM   5399 C  CA   B VAL   B 1 100 ? 39.328 -30.917 10.303  0.34 24.40 ?  100 VAL   B CA   1 
ATOM   5400 C  C    A VAL   B 1 100 ? 40.345 -31.554 11.254  0.66 24.90 ?  100 VAL   B C    1 
ATOM   5401 C  C    B VAL   B 1 100 ? 40.338 -31.580 11.230  0.34 24.92 ?  100 VAL   B C    1 
ATOM   5402 O  O    A VAL   B 1 100 ? 40.000 -32.016 12.349  0.66 26.28 ?  100 VAL   B O    1 
ATOM   5403 O  O    B VAL   B 1 100 ? 39.976 -32.077 12.304  0.34 25.66 ?  100 VAL   B O    1 
ATOM   5404 C  CB   A VAL   B 1 100 ? 38.665 -31.922 9.377   0.66 27.21 ?  100 VAL   B CB   1 
ATOM   5405 C  CB   B VAL   B 1 100 ? 38.689 -31.920 9.320   0.34 26.14 ?  100 VAL   B CB   1 
ATOM   5406 C  CG1  A VAL   B 1 100 ? 38.187 -33.144 10.147  0.66 28.13 ?  100 VAL   B CG1  1 
ATOM   5407 C  CG1  B VAL   B 1 100 ? 38.212 -33.166 10.051  0.34 26.72 ?  100 VAL   B CG1  1 
ATOM   5408 C  CG2  A VAL   B 1 100 ? 37.504 -31.273 8.637   0.66 27.75 ?  100 VAL   B CG2  1 
ATOM   5409 C  CG2  B VAL   B 1 100 ? 37.534 -31.262 8.580   0.34 26.63 ?  100 VAL   B CG2  1 
ATOM   5410 H  H    A VAL   B 1 100 ? 39.957 -29.942 8.720   0.66 26.50 ?  100 VAL   B H    1 
ATOM   5411 H  H    B VAL   B 1 100 ? 39.981 -29.940 8.713   0.34 26.56 ?  100 VAL   B H    1 
ATOM   5412 H  HA   A VAL   B 1 100 ? 38.617 -30.538 10.884  0.66 29.63 ?  100 VAL   B HA   1 
ATOM   5413 H  HA   B VAL   B 1 100 ? 38.614 -30.561 10.852  0.34 29.28 ?  100 VAL   B HA   1 
ATOM   5414 H  HB   A VAL   B 1 100 ? 39.316 -32.216 8.721   0.66 32.66 ?  100 VAL   B HB   1 
ATOM   5415 H  HB   B VAL   B 1 100 ? 39.351 -32.193 8.664   0.34 31.38 ?  100 VAL   B HB   1 
ATOM   5416 H  HG11 A VAL   B 1 100 ? 37.581 -33.654 9.585   0.66 33.76 ?  100 VAL   B HG11 1 
ATOM   5417 H  HG11 B VAL   B 1 100 ? 37.620 -33.667 9.466   0.34 32.07 ?  100 VAL   B HG11 1 
ATOM   5418 H  HG12 A VAL   B 1 100 ? 38.951 -33.692 10.385  0.66 33.76 ?  100 VAL   B HG12 1 
ATOM   5419 H  HG12 B VAL   B 1 100 ? 38.979 -33.711 10.286  0.34 32.07 ?  100 VAL   B HG12 1 
ATOM   5420 H  HG13 A VAL   B 1 100 ? 37.724 -32.853 10.948  0.66 33.76 ?  100 VAL   B HG13 1 
ATOM   5421 H  HG13 B VAL   B 1 100 ? 37.735 -32.899 10.851  0.34 32.07 ?  100 VAL   B HG13 1 
ATOM   5422 H  HG21 A VAL   B 1 100 ? 37.095 -31.930 8.052   0.66 33.30 ?  100 VAL   B HG21 1 
ATOM   5423 H  HG21 B VAL   B 1 100 ? 37.133 -31.910 7.980   0.34 31.96 ?  100 VAL   B HG21 1 
ATOM   5424 H  HG22 A VAL   B 1 100 ? 36.855 -30.958 9.286   0.66 33.30 ?  100 VAL   B HG22 1 
ATOM   5425 H  HG22 B VAL   B 1 100 ? 36.878 -30.960 9.227   0.34 31.96 ?  100 VAL   B HG22 1 
ATOM   5426 H  HG23 A VAL   B 1 100 ? 37.840 -30.529 8.116   0.66 33.30 ?  100 VAL   B HG23 1 
ATOM   5427 H  HG23 B VAL   B 1 100 ? 37.873 -30.508 8.074   0.34 31.96 ?  100 VAL   B HG23 1 
ATOM   5428 N  N    . ASN   B 1 101 ? 41.612 -31.612 10.833  1.00 25.33 ?  101 ASN   B N    1 
ATOM   5429 C  CA   . ASN   B 1 101 ? 42.659 -32.145 11.704  1.00 27.50 ?  101 ASN   B CA   1 
ATOM   5430 C  C    . ASN   B 1 101 ? 42.849 -31.304 12.962  1.00 30.95 ?  101 ASN   B C    1 
ATOM   5431 O  O    . ASN   B 1 101 ? 43.469 -31.778 13.923  1.00 31.58 ?  101 ASN   B O    1 
ATOM   5432 C  CB   . ASN   B 1 101 ? 43.976 -32.273 10.935  1.00 26.79 ?  101 ASN   B CB   1 
ATOM   5433 C  CG   . ASN   B 1 101 ? 43.958 -33.422 9.945   1.00 25.83 ?  101 ASN   B CG   1 
ATOM   5434 O  OD1  . ASN   B 1 101 ? 43.271 -34.420 10.154  1.00 26.42 ?  101 ASN   B OD1  1 
ATOM   5435 N  ND2  . ASN   B 1 101 ? 44.704 -33.279 8.855   1.00 25.38 ?  101 ASN   B ND2  1 
ATOM   5436 H  H    A ASN   B 1 101 ? 41.879 -31.366 10.055  0.66 30.40 ?  101 ASN   B H    1 
ATOM   5437 H  H    B ASN   B 1 101 ? 41.887 -31.345 10.065  0.34 30.40 ?  101 ASN   B H    1 
ATOM   5438 H  HA   . ASN   B 1 101 ? 42.401 -33.033 11.988  1.00 33.01 ?  101 ASN   B HA   1 
ATOM   5439 H  HB2  . ASN   B 1 101 ? 44.143 -31.455 10.442  1.00 32.16 ?  101 ASN   B HB2  1 
ATOM   5440 H  HB3  . ASN   B 1 101 ? 44.696 -32.433 11.563  1.00 32.16 ?  101 ASN   B HB3  1 
ATOM   5441 H  HD21 . ASN   B 1 101 ? 44.725 -33.904 8.264   1.00 30.47 ?  101 ASN   B HD21 1 
ATOM   5442 H  HD22 . ASN   B 1 101 ? 45.172 -32.565 8.742   1.00 30.47 ?  101 ASN   B HD22 1 
ATOM   5443 N  N    A LYS   B 1 102 ? 42.339 -30.072 12.973  0.66 32.93 ?  102 LYS   B N    1 
ATOM   5444 N  N    B LYS   B 1 102 ? 42.337 -30.073 12.975  0.34 33.01 ?  102 LYS   B N    1 
ATOM   5445 C  CA   A LYS   B 1 102 ? 42.317 -29.230 14.162  0.66 35.15 ?  102 LYS   B CA   1 
ATOM   5446 C  CA   B LYS   B 1 102 ? 42.319 -29.237 14.168  0.34 35.07 ?  102 LYS   B CA   1 
ATOM   5447 C  C    A LYS   B 1 102 ? 40.947 -29.201 14.828  0.66 34.70 ?  102 LYS   B C    1 
ATOM   5448 C  C    B LYS   B 1 102 ? 40.948 -29.205 14.832  0.34 34.80 ?  102 LYS   B C    1 
ATOM   5449 O  O    A LYS   B 1 102 ? 40.736 -28.412 15.753  0.66 35.00 ?  102 LYS   B O    1 
ATOM   5450 O  O    B LYS   B 1 102 ? 40.742 -28.424 15.766  0.34 35.08 ?  102 LYS   B O    1 
ATOM   5451 C  CB   A LYS   B 1 102 ? 42.727 -27.799 13.812  0.66 37.96 ?  102 LYS   B CB   1 
ATOM   5452 C  CB   B LYS   B 1 102 ? 42.758 -27.811 13.829  0.34 37.40 ?  102 LYS   B CB   1 
ATOM   5453 C  CG   A LYS   B 1 102 ? 44.187 -27.611 13.446  0.66 40.46 ?  102 LYS   B CG   1 
ATOM   5454 C  CG   B LYS   B 1 102 ? 44.226 -27.667 13.468  0.34 39.37 ?  102 LYS   B CG   1 
ATOM   5455 C  CD   A LYS   B 1 102 ? 44.439 -26.159 13.066  0.66 42.96 ?  102 LYS   B CD   1 
ATOM   5456 C  CD   B LYS   B 1 102 ? 44.534 -26.239 13.043  0.34 41.26 ?  102 LYS   B CD   1 
ATOM   5457 C  CE   A LYS   B 1 102 ? 45.907 -25.879 12.803  0.66 44.77 ?  102 LYS   B CE   1 
ATOM   5458 C  CE   B LYS   B 1 102 ? 46.024 -26.012 12.855  0.34 42.59 ?  102 LYS   B CE   1 
ATOM   5459 N  NZ   A LYS   B 1 102 ? 46.124 -24.456 12.407  0.66 45.81 ?  102 LYS   B NZ   1 
ATOM   5460 N  NZ   B LYS   B 1 102 ? 46.310 -24.617 12.415  0.34 43.35 ?  102 LYS   B NZ   1 
ATOM   5461 H  H    A LYS   B 1 102 ? 41.990 -29.693 12.284  0.66 39.52 ?  102 LYS   B H    1 
ATOM   5462 H  H    B LYS   B 1 102 ? 41.985 -29.694 12.288  0.34 39.62 ?  102 LYS   B H    1 
ATOM   5463 H  HA   A LYS   B 1 102 ? 42.958 -29.574 14.802  0.66 42.18 ?  102 LYS   B HA   1 
ATOM   5464 H  HA   B LYS   B 1 102 ? 42.952 -29.594 14.808  0.34 42.09 ?  102 LYS   B HA   1 
ATOM   5465 H  HB2  A LYS   B 1 102 ? 42.197 -27.502 13.058  0.66 45.56 ?  102 LYS   B HB2  1 
ATOM   5466 H  HB2  B LYS   B 1 102 ? 42.238 -27.496 13.074  0.34 44.88 ?  102 LYS   B HB2  1 
ATOM   5467 H  HB3  A LYS   B 1 102 ? 42.546 -27.232 14.579  0.66 45.56 ?  102 LYS   B HB3  1 
ATOM   5468 H  HB3  B LYS   B 1 102 ? 42.591 -27.244 14.599  0.34 44.88 ?  102 LYS   B HB3  1 
ATOM   5469 H  HG2  A LYS   B 1 102 ? 44.746 -27.833 14.207  0.66 48.56 ?  102 LYS   B HG2  1 
ATOM   5470 H  HG2  B LYS   B 1 102 ? 44.773 -27.881 14.241  0.34 47.25 ?  102 LYS   B HG2  1 
ATOM   5471 H  HG3  A LYS   B 1 102 ? 44.407 -28.172 12.686  0.66 48.56 ?  102 LYS   B HG3  1 
ATOM   5472 H  HG3  B LYS   B 1 102 ? 44.437 -28.259 12.729  0.34 47.25 ?  102 LYS   B HG3  1 
ATOM   5473 H  HD2  A LYS   B 1 102 ? 43.942 -25.952 12.258  0.66 51.56 ?  102 LYS   B HD2  1 
ATOM   5474 H  HD2  B LYS   B 1 102 ? 44.090 -26.055 12.200  0.34 49.52 ?  102 LYS   B HD2  1 
ATOM   5475 H  HD3  A LYS   B 1 102 ? 44.147 -25.586 13.792  0.66 51.56 ?  102 LYS   B HD3  1 
ATOM   5476 H  HD3  B LYS   B 1 102 ? 44.217 -25.628 13.727  0.34 49.52 ?  102 LYS   B HD3  1 
ATOM   5477 H  HE2  A LYS   B 1 102 ? 46.416 -26.052 13.610  0.66 53.74 ?  102 LYS   B HE2  1 
ATOM   5478 H  HE2  B LYS   B 1 102 ? 46.480 -26.165 13.697  0.34 51.11 ?  102 LYS   B HE2  1 
ATOM   5479 H  HE3  A LYS   B 1 102 ? 46.218 -26.447 12.081  0.66 53.74 ?  102 LYS   B HE3  1 
ATOM   5480 H  HE3  B LYS   B 1 102 ? 46.358 -26.620 12.177  0.34 51.11 ?  102 LYS   B HE3  1 
ATOM   5481 H  HZ1  A LYS   B 1 102 ? 46.988 -24.310 12.257  0.66 54.98 ?  102 LYS   B HZ1  1 
ATOM   5482 H  HZ1  B LYS   B 1 102 ? 47.187 -24.505 12.311  0.34 52.02 ?  102 LYS   B HZ1  1 
ATOM   5483 H  HZ2  A LYS   B 1 102 ? 45.666 -24.274 11.665  0.66 54.98 ?  102 LYS   B HZ2  1 
ATOM   5484 H  HZ2  B LYS   B 1 102 ? 45.903 -24.453 11.640  0.34 52.02 ?  102 LYS   B HZ2  1 
ATOM   5485 H  HZ3  A LYS   B 1 102 ? 45.847 -23.914 13.057  0.66 54.98 ?  102 LYS   B HZ3  1 
ATOM   5486 H  HZ3  B LYS   B 1 102 ? 46.015 -24.040 13.025  0.34 52.02 ?  102 LYS   B HZ3  1 
ATOM   5487 N  N    . GLY   B 1 103 ? 40.007 -30.023 14.365  1.00 34.32 ?  103 GLY   B N    1 
ATOM   5488 C  CA   . GLY   B 1 103 ? 38.685 -30.080 14.956  1.00 33.93 ?  103 GLY   B CA   1 
ATOM   5489 C  C    . GLY   B 1 103 ? 37.726 -29.001 14.509  1.00 32.77 ?  103 GLY   B C    1 
ATOM   5490 O  O    . GLY   B 1 103 ? 36.647 -28.875 15.099  1.00 33.49 ?  103 GLY   B O    1 
ATOM   5491 H  H    A GLY   B 1 103 ? 40.114 -30.556 13.701  0.66 41.19 ?  103 GLY   B H    1 
ATOM   5492 H  H    B GLY   B 1 103 ? 40.115 -30.555 13.700  0.34 41.19 ?  103 GLY   B H    1 
ATOM   5493 H  HA2  . GLY   B 1 103 ? 38.286 -30.938 14.743  1.00 40.72 ?  103 GLY   B HA2  1 
ATOM   5494 H  HA3  . GLY   B 1 103 ? 38.769 -30.022 15.921  1.00 40.72 ?  103 GLY   B HA3  1 
ATOM   5495 N  N    A GLU   B 1 104 ? 38.082 -28.219 13.493  0.66 31.30 ?  104 GLU   B N    1 
ATOM   5496 N  N    B GLU   B 1 104 ? 38.068 -28.227 13.484  0.34 32.23 ?  104 GLU   B N    1 
ATOM   5497 C  CA   A GLU   B 1 104 ? 37.231 -27.133 13.038  0.66 29.67 ?  104 GLU   B CA   1 
ATOM   5498 C  CA   B GLU   B 1 104 ? 37.209 -27.137 13.046  0.34 31.44 ?  104 GLU   B CA   1 
ATOM   5499 C  C    A GLU   B 1 104 ? 36.056 -27.674 12.226  0.66 30.32 ?  104 GLU   B C    1 
ATOM   5500 C  C    B GLU   B 1 104 ? 36.035 -27.666 12.227  0.34 31.85 ?  104 GLU   B C    1 
ATOM   5501 O  O    A GLU   B 1 104 ? 36.106 -28.769 11.657  0.66 31.38 ?  104 GLU   B O    1 
ATOM   5502 O  O    B GLU   B 1 104 ? 36.108 -28.734 11.610  0.34 32.34 ?  104 GLU   B O    1 
ATOM   5503 C  CB   A GLU   B 1 104 ? 38.048 -26.126 12.227  0.66 28.31 ?  104 GLU   B CB   1 
ATOM   5504 C  CB   B GLU   B 1 104 ? 38.019 -26.124 12.238  0.34 30.49 ?  104 GLU   B CB   1 
ATOM   5505 C  CG   A GLU   B 1 104 ? 39.159 -25.488 13.051  0.66 26.91 ?  104 GLU   B CG   1 
ATOM   5506 C  CG   B GLU   B 1 104 ? 39.141 -25.506 13.057  0.34 29.62 ?  104 GLU   B CG   1 
ATOM   5507 C  CD   A GLU   B 1 104 ? 40.078 -24.583 12.258  0.66 25.79 ?  104 GLU   B CD   1 
ATOM   5508 C  CD   B GLU   B 1 104 ? 40.046 -24.598 12.251  0.34 28.96 ?  104 GLU   B CD   1 
ATOM   5509 O  OE1  A GLU   B 1 104 ? 40.081 -24.644 11.012  0.66 24.06 ?  104 GLU   B OE1  1 
ATOM   5510 O  OE1  B GLU   B 1 104 ? 39.978 -24.627 11.004  0.34 28.29 ?  104 GLU   B OE1  1 
ATOM   5511 O  OE2  A GLU   B 1 104 ? 40.808 -23.800 12.899  0.66 26.16 -1 104 GLU   B OE2  1 
ATOM   5512 O  OE2  B GLU   B 1 104 ? 40.831 -23.852 12.872  0.34 28.96 -1 104 GLU   B OE2  1 
ATOM   5513 H  H    A GLU   B 1 104 ? 38.819 -28.295 13.055  0.66 37.57 ?  104 GLU   B H    1 
ATOM   5514 H  H    B GLU   B 1 104 ? 38.793 -28.309 13.031  0.34 38.68 ?  104 GLU   B H    1 
ATOM   5515 H  HA   A GLU   B 1 104 ? 36.872 -26.670 13.813  0.66 35.61 ?  104 GLU   B HA   1 
ATOM   5516 H  HA   B GLU   B 1 104 ? 36.852 -26.683 13.825  0.34 37.73 ?  104 GLU   B HA   1 
ATOM   5517 H  HB2  A GLU   B 1 104 ? 38.453 -26.581 11.474  0.66 33.98 ?  104 GLU   B HB2  1 
ATOM   5518 H  HB2  B GLU   B 1 104 ? 38.413 -26.570 11.472  0.34 36.59 ?  104 GLU   B HB2  1 
ATOM   5519 H  HB3  A GLU   B 1 104 ? 37.460 -25.420 11.915  0.66 33.98 ?  104 GLU   B HB3  1 
ATOM   5520 H  HB3  B GLU   B 1 104 ? 37.431 -25.410 11.943  0.34 36.59 ?  104 GLU   B HB3  1 
ATOM   5521 H  HG2  A GLU   B 1 104 ? 38.760 -24.948 13.751  0.66 32.30 ?  104 GLU   B HG2  1 
ATOM   5522 H  HG2  B GLU   B 1 104 ? 38.752 -24.980 13.773  0.34 35.55 ?  104 GLU   B HG2  1 
ATOM   5523 H  HG3  A GLU   B 1 104 ? 39.702 -26.187 13.443  0.66 32.30 ?  104 GLU   B HG3  1 
ATOM   5524 H  HG3  B GLU   B 1 104 ? 39.686 -26.217 13.430  0.34 35.55 ?  104 GLU   B HG3  1 
ATOM   5525 N  N    A ASP   B 1 105 ? 34.985 -26.884 12.185  0.66 29.85 ?  105 ASP   B N    1 
ATOM   5526 N  N    B ASP   B 1 105 ? 34.944 -26.902 12.231  0.34 31.61 ?  105 ASP   B N    1 
ATOM   5527 C  CA   A ASP   B 1 105 ? 33.712 -27.333 11.637  0.66 30.64 ?  105 ASP   B CA   1 
ATOM   5528 C  CA   B ASP   B 1 105 ? 33.688 -27.368 11.655  0.34 31.60 ?  105 ASP   B CA   1 
ATOM   5529 C  C    A ASP   B 1 105 ? 33.781 -27.374 10.116  0.66 28.80 ?  105 ASP   B C    1 
ATOM   5530 C  C    B ASP   B 1 105 ? 33.778 -27.382 10.133  0.34 29.91 ?  105 ASP   B C    1 
ATOM   5531 O  O    A ASP   B 1 105 ? 33.937 -26.333 9.468   0.66 27.70 ?  105 ASP   B O    1 
ATOM   5532 O  O    B ASP   B 1 105 ? 33.963 -26.336 9.502   0.34 29.51 ?  105 ASP   B O    1 
ATOM   5533 C  CB   A ASP   B 1 105 ? 32.599 -26.389 12.087  0.66 33.76 ?  105 ASP   B CB   1 
ATOM   5534 C  CB   B ASP   B 1 105 ? 32.541 -26.471 12.117  0.34 33.14 ?  105 ASP   B CB   1 
ATOM   5535 C  CG   A ASP   B 1 105 ? 31.224 -26.867 11.668  0.66 36.46 ?  105 ASP   B CG   1 
ATOM   5536 C  CG   B ASP   B 1 105 ? 31.179 -27.052 11.784  0.34 34.51 ?  105 ASP   B CG   1 
ATOM   5537 O  OD1  A ASP   B 1 105 ? 31.121 -27.987 11.123  0.66 36.73 ?  105 ASP   B OD1  1 
ATOM   5538 O  OD1  B ASP   B 1 105 ? 31.126 -28.075 11.069  0.34 34.88 ?  105 ASP   B OD1  1 
ATOM   5539 O  OD2  A ASP   B 1 105 ? 30.244 -26.120 11.881  0.66 38.11 -1 105 ASP   B OD2  1 
ATOM   5540 O  OD2  B ASP   B 1 105 ? 30.161 -26.493 12.246  0.34 34.91 -1 105 ASP   B OD2  1 
ATOM   5541 H  H    A ASP   B 1 105 ? 34.973 -26.073 12.472  0.66 35.83 ?  105 ASP   B H    1 
ATOM   5542 H  H    B ASP   B 1 105 ? 34.904 -26.109 12.561  0.34 37.94 ?  105 ASP   B H    1 
ATOM   5543 H  HA   A ASP   B 1 105 ? 33.511 -28.225 11.963  0.66 36.77 ?  105 ASP   B HA   1 
ATOM   5544 H  HA   B ASP   B 1 105 ? 33.506 -28.271 11.959  0.34 37.93 ?  105 ASP   B HA   1 
ATOM   5545 H  HB2  A ASP   B 1 105 ? 32.625 -26.309 13.055  0.66 40.52 ?  105 ASP   B HB2  1 
ATOM   5546 H  HB2  B ASP   B 1 105 ? 32.589 -26.361 13.081  0.34 39.77 ?  105 ASP   B HB2  1 
ATOM   5547 H  HB3  A ASP   B 1 105 ? 32.737 -25.520 11.680  0.66 40.52 ?  105 ASP   B HB3  1 
ATOM   5548 H  HB3  B ASP   B 1 105 ? 32.616 -25.606 11.682  0.34 39.77 ?  105 ASP   B HB3  1 
ATOM   5549 N  N    . ILE   B 1 106 ? 33.633 -28.574 9.548   1.00 28.65 ?  106 ILE   B N    1 
ATOM   5550 C  CA   . ILE   B 1 106 ? 33.633 -28.732 8.100   1.00 27.22 ?  106 ILE   B CA   1 
ATOM   5551 C  C    . ILE   B 1 106 ? 32.527 -27.913 7.438   1.00 25.42 ?  106 ILE   B C    1 
ATOM   5552 O  O    . ILE   B 1 106 ? 32.616 -27.602 6.247   1.00 24.92 ?  106 ILE   B O    1 
ATOM   5553 C  CB   . ILE   B 1 106 ? 33.544 -30.241 7.757   1.00 28.11 ?  106 ILE   B CB   1 
ATOM   5554 C  CG1  . ILE   B 1 106 ? 33.769 -30.486 6.264   1.00 28.32 ?  106 ILE   B CG1  1 
ATOM   5555 C  CG2  . ILE   B 1 106 ? 32.200 -30.814 8.193   1.00 29.27 ?  106 ILE   B CG2  1 
ATOM   5556 C  CD1  . ILE   B 1 106 ? 35.100 -29.977 5.767   1.00 28.33 ?  106 ILE   B CD1  1 
ATOM   5557 H  H    A ILE   B 1 106 ? 33.524 -29.308 9.984   0.66 34.38 ?  106 ILE   B H    1 
ATOM   5558 H  H    B ILE   B 1 106 ? 33.531 -29.312 9.979   0.34 34.38 ?  106 ILE   B H    1 
ATOM   5559 H  HA   . ILE   B 1 106 ? 34.476 -28.401 7.762   1.00 32.67 ?  106 ILE   B HA   1 
ATOM   5560 H  HB   . ILE   B 1 106 ? 34.242 -30.704 8.246   1.00 33.74 ?  106 ILE   B HB   1 
ATOM   5561 H  HG12 . ILE   B 1 106 ? 33.740 -31.444 6.095   1.00 33.99 ?  106 ILE   B HG12 1 
ATOM   5562 H  HG13 . ILE   B 1 106 ? 33.072 -30.043 5.759   1.00 33.99 ?  106 ILE   B HG13 1 
ATOM   5563 H  HG21 . ILE   B 1 106 ? 32.214 -31.776 8.070   1.00 35.13 ?  106 ILE   B HG21 1 
ATOM   5564 H  HG22 . ILE   B 1 106 ? 32.055 -30.603 9.128   1.00 35.13 ?  106 ILE   B HG22 1 
ATOM   5565 H  HG23 . ILE   B 1 106 ? 31.497 -30.422 7.652   1.00 35.13 ?  106 ILE   B HG23 1 
ATOM   5566 H  HD11 . ILE   B 1 106 ? 35.289 -30.374 4.904   1.00 34.00 ?  106 ILE   B HD11 1 
ATOM   5567 H  HD12 . ILE   B 1 106 ? 35.058 -29.011 5.684   1.00 34.00 ?  106 ILE   B HD12 1 
ATOM   5568 H  HD13 . ILE   B 1 106 ? 35.791 -30.225 6.402   1.00 34.00 ?  106 ILE   B HD13 1 
ATOM   5569 N  N    A GLN   B 1 107 ? 31.476 -27.563 8.183   0.66 25.52 ?  107 GLN   B N    1 
ATOM   5570 N  N    B GLN   B 1 107 ? 31.487 -27.545 8.187   0.34 25.63 ?  107 GLN   B N    1 
ATOM   5571 C  CA   A GLN   B 1 107 ? 30.394 -26.760 7.622   0.66 25.13 ?  107 GLN   B CA   1 
ATOM   5572 C  CA   B GLN   B 1 107 ? 30.397 -26.756 7.624   0.34 25.55 ?  107 GLN   B CA   1 
ATOM   5573 C  C    A GLN   B 1 107 ? 30.872 -25.399 7.128   0.66 23.15 ?  107 GLN   B C    1 
ATOM   5574 C  C    B GLN   B 1 107 ? 30.860 -25.384 7.148   0.34 23.37 ?  107 GLN   B C    1 
ATOM   5575 O  O    A GLN   B 1 107 ? 30.217 -24.810 6.265   0.66 24.21 ?  107 GLN   B O    1 
ATOM   5576 O  O    B GLN   B 1 107 ? 30.177 -24.769 6.323   0.34 24.00 ?  107 GLN   B O    1 
ATOM   5577 C  CB   A GLN   B 1 107 ? 29.284 -26.579 8.660   0.66 28.65 ?  107 GLN   B CB   1 
ATOM   5578 C  CB   B GLN   B 1 107 ? 29.283 -26.604 8.662   0.34 28.26 ?  107 GLN   B CB   1 
ATOM   5579 C  CG   A GLN   B 1 107 ? 27.955 -26.093 8.086   0.66 32.17 ?  107 GLN   B CG   1 
ATOM   5580 C  CG   B GLN   B 1 107 ? 27.942 -26.145 8.101   0.34 30.77 ?  107 GLN   B CG   1 
ATOM   5581 C  CD   A GLN   B 1 107 ? 27.876 -24.581 7.965   0.66 34.80 ?  107 GLN   B CD   1 
ATOM   5582 C  CD   B GLN   B 1 107 ? 27.809 -24.634 8.044   0.34 32.72 ?  107 GLN   B CD   1 
ATOM   5583 O  OE1  A GLN   B 1 107 ? 28.698 -23.857 8.528   0.66 35.76 ?  107 GLN   B OE1  1 
ATOM   5584 O  OE1  B GLN   B 1 107 ? 28.599 -23.905 8.645   0.34 33.40 ?  107 GLN   B OE1  1 
ATOM   5585 N  NE2  A GLN   B 1 107 ? 26.876 -24.096 7.230   0.66 35.76 ?  107 GLN   B NE2  1 
ATOM   5586 N  NE2  B GLN   B 1 107 ? 26.801 -24.155 7.320   0.34 33.46 ?  107 GLN   B NE2  1 
ATOM   5587 H  H    A GLN   B 1 107 ? 31.365 -27.784 9.001   0.66 30.63 ?  107 GLN   B H    1 
ATOM   5588 H  H    B GLN   B 1 107 ? 31.392 -27.738 9.013   0.34 30.77 ?  107 GLN   B H    1 
ATOM   5589 H  HA   A GLN   B 1 107 ? 30.014 -27.235 6.864   0.66 30.16 ?  107 GLN   B HA   1 
ATOM   5590 H  HA   B GLN   B 1 107 ? 30.028 -27.230 6.859   0.34 30.66 ?  107 GLN   B HA   1 
ATOM   5591 H  HB2  A GLN   B 1 107 ? 29.125 -27.430 9.089   0.66 34.39 ?  107 GLN   B HB2  1 
ATOM   5592 H  HB2  B GLN   B 1 107 ? 29.143 -27.461 9.087   0.34 33.92 ?  107 GLN   B HB2  1 
ATOM   5593 H  HB3  A GLN   B 1 107 ? 29.581 -25.930 9.316   0.66 34.39 ?  107 GLN   B HB3  1 
ATOM   5594 H  HB3  B GLN   B 1 107 ? 29.566 -25.954 9.324   0.34 33.92 ?  107 GLN   B HB3  1 
ATOM   5595 H  HG2  A GLN   B 1 107 ? 27.835 -26.468 7.199   0.66 38.61 ?  107 GLN   B HG2  1 
ATOM   5596 H  HG2  B GLN   B 1 107 ? 27.839 -26.487 7.200   0.34 36.94 ?  107 GLN   B HG2  1 
ATOM   5597 H  HG3  A GLN   B 1 107 ? 27.236 -26.388 8.668   0.66 38.61 ?  107 GLN   B HG3  1 
ATOM   5598 H  HG3  B GLN   B 1 107 ? 27.230 -26.489 8.667   0.34 36.94 ?  107 GLN   B HG3  1 
ATOM   5599 H  HE21 A GLN   B 1 107 ? 26.320 -24.633 6.850   0.66 42.92 ?  107 GLN   B HE21 1 
ATOM   5600 H  HE21 B GLN   B 1 107 ? 26.269 -24.694 6.913   0.34 40.16 ?  107 GLN   B HE21 1 
ATOM   5601 H  HE22 A GLN   B 1 107 ? 26.783 -23.246 7.134   0.66 42.92 ?  107 GLN   B HE22 1 
ATOM   5602 H  HE22 B GLN   B 1 107 ? 26.681 -23.306 7.259   0.34 40.16 ?  107 GLN   B HE22 1 
ATOM   5603 N  N    . LEU   B 1 108 ? 32.002 -24.894 7.637   1.00 21.10 ?  108 LEU   B N    1 
ATOM   5604 C  CA   . LEU   B 1 108 ? 32.533 -23.594 7.222   1.00 19.00 ?  108 LEU   B CA   1 
ATOM   5605 C  C    . LEU   B 1 108 ? 33.166 -23.615 5.838   1.00 16.51 ?  108 LEU   B C    1 
ATOM   5606 O  O    . LEU   B 1 108 ? 33.582 -22.556 5.343   1.00 15.56 ?  108 LEU   B O    1 
ATOM   5607 C  CB   . LEU   B 1 108 ? 33.544 -23.091 8.252   1.00 19.79 ?  108 LEU   B CB   1 
ATOM   5608 C  CG   . LEU   B 1 108 ? 32.926 -22.555 9.544   1.00 21.06 ?  108 LEU   B CG   1 
ATOM   5609 C  CD1  . LEU   B 1 108 ? 33.934 -22.548 10.679  1.00 21.45 ?  108 LEU   B CD1  1 
ATOM   5610 C  CD2  . LEU   B 1 108 ? 32.390 -21.154 9.304   1.00 22.04 ?  108 LEU   B CD2  1 
ATOM   5611 H  H    A LEU   B 1 108 ? 32.474 -25.288 8.235   0.66 25.33 ?  108 LEU   B H    1 
ATOM   5612 H  H    B LEU   B 1 108 ? 32.484 -25.299 8.220   0.34 25.33 ?  108 LEU   B H    1 
ATOM   5613 H  HA   . LEU   B 1 108 ? 31.803 -22.962 7.192   1.00 22.81 ?  108 LEU   B HA   1 
ATOM   5614 H  HB2  . LEU   B 1 108 ? 34.131 -23.824 8.492   1.00 23.75 ?  108 LEU   B HB2  1 
ATOM   5615 H  HB3  . LEU   B 1 108 ? 34.059 -22.375 7.855   1.00 23.75 ?  108 LEU   B HB3  1 
ATOM   5616 H  HG   . LEU   B 1 108 ? 32.183 -23.122 9.803   1.00 25.28 ?  108 LEU   B HG   1 
ATOM   5617 H  HD11 . LEU   B 1 108 ? 33.491 -22.254 11.492  1.00 25.75 ?  108 LEU   B HD11 1 
ATOM   5618 H  HD12 . LEU   B 1 108 ? 34.280 -23.446 10.800  1.00 25.75 ?  108 LEU   B HD12 1 
ATOM   5619 H  HD13 . LEU   B 1 108 ? 34.655 -21.940 10.459  1.00 25.75 ?  108 LEU   B HD13 1 
ATOM   5620 H  HD21 . LEU   B 1 108 ? 32.021 -20.811 10.131  1.00 26.45 ?  108 LEU   B HD21 1 
ATOM   5621 H  HD22 . LEU   B 1 108 ? 33.118 -20.586 9.005   1.00 26.45 ?  108 LEU   B HD22 1 
ATOM   5622 H  HD23 . LEU   B 1 108 ? 31.700 -21.192 8.623   1.00 26.45 ?  108 LEU   B HD23 1 
ATOM   5623 N  N    . LEU   B 1 109 ? 33.232 -24.783 5.202   1.00 15.14 ?  109 LEU   B N    1 
ATOM   5624 C  CA   . LEU   B 1 109 ? 33.855 -24.889 3.891   1.00 14.43 ?  109 LEU   B CA   1 
ATOM   5625 C  C    . LEU   B 1 109 ? 33.083 -24.109 2.831   1.00 13.61 ?  109 LEU   B C    1 
ATOM   5626 O  O    . LEU   B 1 109 ? 33.692 -23.527 1.929   1.00 13.48 ?  109 LEU   B O    1 
ATOM   5627 C  CB   . LEU   B 1 109 ? 33.977 -26.366 3.512   1.00 14.60 ?  109 LEU   B CB   1 
ATOM   5628 C  CG   . LEU   B 1 109 ? 34.737 -26.709 2.235   1.00 14.27 ?  109 LEU   B CG   1 
ATOM   5629 C  CD1  . LEU   B 1 109 ? 36.113 -26.063 2.234   1.00 14.12 ?  109 LEU   B CD1  1 
ATOM   5630 C  CD2  . LEU   B 1 109 ? 34.844 -28.221 2.083   1.00 14.96 ?  109 LEU   B CD2  1 
ATOM   5631 H  H    . LEU   B 1 109 ? 32.933 -25.527 5.506   1.00 18.17 ?  109 LEU   B H    1 
ATOM   5632 H  HA   . LEU   B 1 109 ? 34.754 -24.521 3.935   1.00 17.32 ?  109 LEU   B HA   1 
ATOM   5633 H  HB2  . LEU   B 1 109 ? 34.428 -26.830 4.235   1.00 17.53 ?  109 LEU   B HB2  1 
ATOM   5634 H  HB3  . LEU   B 1 109 ? 33.084 -26.729 3.410   1.00 17.53 ?  109 LEU   B HB3  1 
ATOM   5635 H  HG   . LEU   B 1 109 ? 34.246 -26.375 1.467   1.00 17.13 ?  109 LEU   B HG   1 
ATOM   5636 H  HD11 . LEU   B 1 109 ? 36.635 -26.428 1.499   1.00 16.96 ?  109 LEU   B HD11 1 
ATOM   5637 H  HD12 . LEU   B 1 109 ? 36.012 -25.108 2.127   1.00 16.96 ?  109 LEU   B HD12 1 
ATOM   5638 H  HD13 . LEU   B 1 109 ? 36.552 -26.263 3.077   1.00 16.96 ?  109 LEU   B HD13 1 
ATOM   5639 H  HD21 . LEU   B 1 109 ? 35.408 -28.427 1.318   1.00 17.96 ?  109 LEU   B HD21 1 
ATOM   5640 H  HD22 . LEU   B 1 109 ? 35.234 -28.595 2.887   1.00 17.96 ?  109 LEU   B HD22 1 
ATOM   5641 H  HD23 . LEU   B 1 109 ? 33.957 -28.592 1.943   1.00 17.96 ?  109 LEU   B HD23 1 
ATOM   5642 N  N    . LYS   B 1 110 ? 31.749 -24.077 2.915   1.00 13.58 ?  110 LYS   B N    1 
ATOM   5643 C  CA   . LYS   B 1 110 ? 30.990 -23.317 1.924   1.00 13.30 ?  110 LYS   B CA   1 
ATOM   5644 C  C    . LYS   B 1 110 ? 31.322 -21.828 2.012   1.00 12.93 ?  110 LYS   B C    1 
ATOM   5645 O  O    . LYS   B 1 110 ? 31.567 -21.175 0.993   1.00 12.70 ?  110 LYS   B O    1 
ATOM   5646 C  CB   . LYS   B 1 110 ? 29.484 -23.569 2.068   1.00 13.79 ?  110 LYS   B CB   1 
ATOM   5647 C  CG   . LYS   B 1 110 ? 28.682 -22.953 0.916   1.00 14.20 ?  110 LYS   B CG   1 
ATOM   5648 C  CD   . LYS   B 1 110 ? 27.216 -23.378 0.949   1.00 14.17 ?  110 LYS   B CD   1 
ATOM   5649 C  CE   . LYS   B 1 110 ? 26.436 -22.838 -0.247  1.00 14.65 ?  110 LYS   B CE   1 
ATOM   5650 N  NZ   . LYS   B 1 110 ? 26.759 -23.533 -1.517  1.00 15.19 ?  110 LYS   B NZ   1 
ATOM   5651 H  H    . LYS   B 1 110 ? 31.281 -24.479 3.513   1.00 16.30 ?  110 LYS   B H    1 
ATOM   5652 H  HA   . LYS   B 1 110 ? 31.255 -23.620 1.041   1.00 15.97 ?  110 LYS   B HA   1 
ATOM   5653 H  HB2  . LYS   B 1 110 ? 29.324 -24.526 2.070   1.00 16.55 ?  110 LYS   B HB2  1 
ATOM   5654 H  HB3  . LYS   B 1 110 ? 29.174 -23.176 2.896   1.00 16.55 ?  110 LYS   B HB3  1 
ATOM   5655 H  HG2  . LYS   B 1 110 ? 28.714 -21.988 0.979   1.00 17.04 ?  110 LYS   B HG2  1 
ATOM   5656 H  HG3  . LYS   B 1 110 ? 29.057 -23.246 0.069   1.00 17.04 ?  110 LYS   B HG3  1 
ATOM   5657 H  HD2  . LYS   B 1 110 ? 27.163 -24.350 0.931   1.00 17.02 ?  110 LYS   B HD2  1 
ATOM   5658 H  HD3  . LYS   B 1 110 ? 26.803 -23.041 1.761   1.00 17.02 ?  110 LYS   B HD3  1 
ATOM   5659 H  HE2  . LYS   B 1 110 ? 25.485 -22.944 -0.081  1.00 17.59 ?  110 LYS   B HE2  1 
ATOM   5660 H  HE3  . LYS   B 1 110 ? 26.647 -21.897 -0.359  1.00 17.59 ?  110 LYS   B HE3  1 
ATOM   5661 H  HZ1  . LYS   B 1 110 ? 26.284 -23.184 -2.182  1.00 18.23 ?  110 LYS   B HZ1  1 
ATOM   5662 H  HZ2  . LYS   B 1 110 ? 27.624 -23.444 -1.699  1.00 18.23 ?  110 LYS   B HZ2  1 
ATOM   5663 H  HZ3  . LYS   B 1 110 ? 26.565 -24.399 -1.444  1.00 18.23 ?  110 LYS   B HZ3  1 
ATOM   5664 N  N    . SER   B 1 111 ? 31.342 -21.278 3.229   1.00 13.20 ?  111 SER   B N    1 
ATOM   5665 C  CA   . SER   B 1 111 ? 31.733 -19.879 3.400   1.00 12.96 ?  111 SER   B CA   1 
ATOM   5666 C  C    . SER   B 1 111 ? 33.108 -19.622 2.800   1.00 12.37 ?  111 SER   B C    1 
ATOM   5667 O  O    . SER   B 1 111 ? 33.329 -18.589 2.151   1.00 12.67 ?  111 SER   B O    1 
ATOM   5668 C  CB   . SER   B 1 111 ? 31.745 -19.519 4.883   1.00 13.81 ?  111 SER   B CB   1 
ATOM   5669 O  OG   . SER   B 1 111 ? 30.445 -19.526 5.428   1.00 15.44 ?  111 SER   B OG   1 
ATOM   5670 H  H    . SER   B 1 111 ? 31.145 -21.691 3.958   1.00 15.85 ?  111 SER   B H    1 
ATOM   5671 H  HA   . SER   B 1 111 ? 31.093 -19.312 2.951   1.00 15.56 ?  111 SER   B HA   1 
ATOM   5672 H  HB2  . SER   B 1 111 ? 32.283 -20.167 5.363   1.00 16.58 ?  111 SER   B HB2  1 
ATOM   5673 H  HB3  . SER   B 1 111 ? 32.127 -18.633 4.987   1.00 16.58 ?  111 SER   B HB3  1 
ATOM   5674 H  HG   . SER   B 1 111 ? 30.474 -19.312 6.250   1.00 18.53 ?  111 SER   B HG   1 
ATOM   5675 N  N    . ALA   B 1 112 ? 34.050 -20.545 3.012   1.00 12.56 ?  112 ALA   B N    1 
ATOM   5676 C  CA   . ALA   B 1 112 ? 35.394 -20.367 2.473   1.00 12.03 ?  112 ALA   B CA   1 
ATOM   5677 C  C    . ALA   B 1 112 ? 35.360 -20.270 0.951   1.00 11.65 ?  112 ALA   B C    1 
ATOM   5678 O  O    . ALA   B 1 112 ? 35.984 -19.379 0.355   1.00 12.19 ?  112 ALA   B O    1 
ATOM   5679 C  CB   . ALA   B 1 112 ? 36.303 -21.508 2.946   1.00 12.38 ?  112 ALA   B CB   1 
ATOM   5680 H  H    . ALA   B 1 112 ? 33.935 -21.272 3.459   1.00 15.08 ?  112 ALA   B H    1 
ATOM   5681 H  HA   . ALA   B 1 112 ? 35.758 -19.535 2.817   1.00 14.44 ?  112 ALA   B HA   1 
ATOM   5682 H  HB1  . ALA   B 1 112 ? 37.195 -21.368 2.586   1.00 14.86 ?  112 ALA   B HB1  1 
ATOM   5683 H  HB2  . ALA   B 1 112 ? 36.340 -21.500 3.918   1.00 14.86 ?  112 ALA   B HB2  1 
ATOM   5684 H  HB3  . ALA   B 1 112 ? 35.946 -22.349 2.635   1.00 14.86 ?  112 ALA   B HB3  1 
ATOM   5685 N  N    . TYR   B 1 113 ? 34.623 -21.173 0.298   1.00 11.58 ?  113 TYR   B N    1 
ATOM   5686 C  CA   . TYR   B 1 113 ? 34.548 -21.123 -1.156  1.00 11.19 ?  113 TYR   B CA   1 
ATOM   5687 C  C    . TYR   B 1 113 ? 33.844 -19.868 -1.666  1.00 11.04 ?  113 TYR   B C    1 
ATOM   5688 O  O    . TYR   B 1 113 ? 34.105 -19.439 -2.797  1.00 11.15 ?  113 TYR   B O    1 
ATOM   5689 C  CB   . TYR   B 1 113 ? 33.875 -22.382 -1.705  1.00 11.61 ?  113 TYR   B CB   1 
ATOM   5690 C  CG   . TYR   B 1 113 ? 34.839 -23.528 -1.962  1.00 12.11 ?  113 TYR   B CG   1 
ATOM   5691 C  CD1  . TYR   B 1 113 ? 35.824 -23.427 -2.938  1.00 12.50 ?  113 TYR   B CD1  1 
ATOM   5692 C  CD2  . TYR   B 1 113 ? 34.749 -24.714 -1.251  1.00 12.38 ?  113 TYR   B CD2  1 
ATOM   5693 C  CE1  . TYR   B 1 113 ? 36.703 -24.449 -3.188  1.00 12.85 ?  113 TYR   B CE1  1 
ATOM   5694 C  CE2  . TYR   B 1 113 ? 35.623 -25.765 -1.502  1.00 12.37 ?  113 TYR   B CE2  1 
ATOM   5695 C  CZ   . TYR   B 1 113 ? 36.594 -25.625 -2.478  1.00 12.65 ?  113 TYR   B CZ   1 
ATOM   5696 O  OH   . TYR   B 1 113 ? 37.474 -26.643 -2.757  1.00 13.79 ?  113 TYR   B OH   1 
ATOM   5697 H  H    . TYR   B 1 113 ? 34.170 -21.804 0.672   1.00 13.91 ?  113 TYR   B H    1 
ATOM   5698 H  HA   . TYR   B 1 113 ? 35.451 -21.104 -1.497  1.00 13.44 ?  113 TYR   B HA   1 
ATOM   5699 H  HB2  . TYR   B 1 113 ? 33.214 -22.695 -1.066  1.00 13.94 ?  113 TYR   B HB2  1 
ATOM   5700 H  HB3  . TYR   B 1 113 ? 33.441 -22.164 -2.544  1.00 13.94 ?  113 TYR   B HB3  1 
ATOM   5701 H  HD1  . TYR   B 1 113 ? 35.899 -22.633 -3.426  1.00 15.01 ?  113 TYR   B HD1  1 
ATOM   5702 H  HD2  . TYR   B 1 113 ? 34.088 -24.808 -0.606  1.00 14.87 ?  113 TYR   B HD2  1 
ATOM   5703 H  HE1  . TYR   B 1 113 ? 37.351 -24.356 -3.850  1.00 15.43 ?  113 TYR   B HE1  1 
ATOM   5704 H  HE2  . TYR   B 1 113 ? 35.550 -26.560 -1.026  1.00 14.86 ?  113 TYR   B HE2  1 
ATOM   5705 H  HH   . TYR   B 1 113 ? 37.305 -27.310 -2.270  1.00 16.55 ?  113 TYR   B HH   1 
ATOM   5706 N  N    . GLU   B 1 114 ? 32.918 -19.295 -0.882  1.00 11.62 ?  114 GLU   B N    1 
ATOM   5707 C  CA   . GLU   B 1 114 ? 32.235 -18.083 -1.332  1.00 11.22 ?  114 GLU   B CA   1 
ATOM   5708 C  C    . GLU   B 1 114 ? 33.215 -16.959 -1.629  1.00 11.10 ?  114 GLU   B C    1 
ATOM   5709 O  O    . GLU   B 1 114 ? 32.930 -16.102 -2.470  1.00 11.40 ?  114 GLU   B O    1 
ATOM   5710 C  CB   . GLU   B 1 114 ? 31.176 -17.649 -0.317  1.00 11.87 ?  114 GLU   B CB   1 
ATOM   5711 C  CG   . GLU   B 1 114 ? 29.964 -18.579 -0.384  1.00 11.99 ?  114 GLU   B CG   1 
ATOM   5712 C  CD   . GLU   B 1 114 ? 28.939 -18.400 0.725   1.00 12.32 ?  114 GLU   B CD   1 
ATOM   5713 O  OE1  . GLU   B 1 114 ? 29.230 -17.787 1.772   1.00 12.63 ?  114 GLU   B OE1  1 
ATOM   5714 O  OE2  . GLU   B 1 114 ? 27.815 -18.933 0.555   1.00 13.15 -1 114 GLU   B OE2  1 
ATOM   5715 H  H    . GLU   B 1 114 ? 32.667 -19.590 -0.108  1.00 13.94 ?  114 GLU   B H    1 
ATOM   5716 H  HA   . GLU   B 1 114 ? 31.771 -18.286 -2.155  1.00 13.47 ?  114 GLU   B HA   1 
ATOM   5717 H  HB2  . GLU   B 1 114 ? 31.546 -17.692 0.582   1.00 14.25 ?  114 GLU   B HB2  1 
ATOM   5718 H  HB3  . GLU   B 1 114 ? 30.881 -16.748 -0.518  1.00 14.25 ?  114 GLU   B HB3  1 
ATOM   5719 H  HG2  . GLU   B 1 114 ? 29.511 -18.430 -1.223  1.00 14.40 ?  114 GLU   B HG2  1 
ATOM   5720 H  HG3  . GLU   B 1 114 ? 30.282 -19.496 -0.341  1.00 14.40 ?  114 GLU   B HG3  1 
ATOM   5721 N  N    . ASN   B 1 115 ? 34.386 -16.960 -0.988  1.00 11.16 ?  115 ASN   B N    1 
ATOM   5722 C  CA   . ASN   B 1 115 ? 35.373 -15.926 -1.286  1.00 11.05 ?  115 ASN   B CA   1 
ATOM   5723 C  C    . ASN   B 1 115 ? 35.780 -15.944 -2.756  1.00 10.78 ?  115 ASN   B C    1 
ATOM   5724 O  O    . ASN   B 1 115 ? 36.163 -14.903 -3.310  1.00 11.30 ?  115 ASN   B O    1 
ATOM   5725 C  CB   . ASN   B 1 115 ? 36.617 -16.100 -0.406  1.00 11.47 ?  115 ASN   B CB   1 
ATOM   5726 C  CG   . ASN   B 1 115 ? 36.350 -15.834 1.057   1.00 11.87 ?  115 ASN   B CG   1 
ATOM   5727 O  OD1  . ASN   B 1 115 ? 36.341 -14.684 1.494   1.00 13.70 ?  115 ASN   B OD1  1 
ATOM   5728 N  ND2  . ASN   B 1 115 ? 36.187 -16.898 1.838   1.00 11.91 ?  115 ASN   B ND2  1 
ATOM   5729 H  H    . ASN   B 1 115 ? 34.626 -17.530 -0.381  1.00 13.40 ?  115 ASN   B H    1 
ATOM   5730 H  HA   . ASN   B 1 115 ? 34.992 -15.057 -1.089  1.00 13.27 ?  115 ASN   B HA   1 
ATOM   5731 H  HB2  . ASN   B 1 115 ? 36.943 -17.011 -0.494  1.00 13.77 ?  115 ASN   B HB2  1 
ATOM   5732 H  HB3  . ASN   B 1 115 ? 37.302 -15.478 -0.700  1.00 13.77 ?  115 ASN   B HB3  1 
ATOM   5733 H  HD21 . ASN   B 1 115 ? 36.044 -16.795 2.681   1.00 14.30 ?  115 ASN   B HD21 1 
ATOM   5734 H  HD22 . ASN   B 1 115 ? 36.209 -17.688 1.501   1.00 14.30 ?  115 ASN   B HD22 1 
ATOM   5735 N  N    . PHE   B 1 116 ? 35.751 -17.120 -3.393  1.00 10.66 ?  116 PHE   B N    1 
ATOM   5736 C  CA   . PHE   B 1 116 ? 36.177 -17.210 -4.784  1.00 10.96 ?  116 PHE   B CA   1 
ATOM   5737 C  C    . PHE   B 1 116 ? 35.272 -16.382 -5.690  1.00 10.40 ?  116 PHE   B C    1 
ATOM   5738 O  O    . PHE   B 1 116 ? 35.694 -15.965 -6.770  1.00 11.16 ?  116 PHE   B O    1 
ATOM   5739 C  CB   . PHE   B 1 116 ? 36.141 -18.655 -5.312  1.00 10.38 ?  116 PHE   B CB   1 
ATOM   5740 C  CG   . PHE   B 1 116 ? 37.215 -19.615 -4.765  1.00 10.77 ?  116 PHE   B CG   1 
ATOM   5741 C  CD1  . PHE   B 1 116 ? 37.869 -19.430 -3.554  1.00 11.61 ?  116 PHE   B CD1  1 
ATOM   5742 C  CD2  . PHE   B 1 116 ? 37.517 -20.751 -5.504  1.00 11.14 ?  116 PHE   B CD2  1 
ATOM   5743 C  CE1  . PHE   B 1 116 ? 38.805 -20.370 -3.107  1.00 11.67 ?  116 PHE   B CE1  1 
ATOM   5744 C  CE2  . PHE   B 1 116 ? 38.448 -21.680 -5.063  1.00 11.20 ?  116 PHE   B CE2  1 
ATOM   5745 C  CZ   . PHE   B 1 116 ? 39.082 -21.494 -3.869  1.00 11.37 ?  116 PHE   B CZ   1 
ATOM   5746 H  H    . PHE   B 1 116 ? 35.494 -17.869 -3.046  1.00 12.80 ?  116 PHE   B H    1 
ATOM   5747 H  HA   . PHE   B 1 116 ? 37.082 -16.880 -4.868  1.00 13.16 ?  116 PHE   B HA   1 
ATOM   5748 H  HB2  . PHE   B 1 116 ? 35.269 -19.034 -5.094  1.00 12.47 ?  116 PHE   B HB2  1 
ATOM   5749 H  HB3  . PHE   B 1 116 ? 36.239 -18.628 -6.276  1.00 12.47 ?  116 PHE   B HB3  1 
ATOM   5750 H  HD1  . PHE   B 1 116 ? 37.667 -18.683 -3.035  1.00 13.94 ?  116 PHE   B HD1  1 
ATOM   5751 H  HD2  . PHE   B 1 116 ? 37.074 -20.895 -6.313  1.00 13.38 ?  116 PHE   B HD2  1 
ATOM   5752 H  HE1  . PHE   B 1 116 ? 39.240 -20.235 -2.298  1.00 14.01 ?  116 PHE   B HE1  1 
ATOM   5753 H  HE2  . PHE   B 1 116 ? 38.633 -22.428 -5.578  1.00 13.45 ?  116 PHE   B HE2  1 
ATOM   5754 H  HZ   . PHE   B 1 116 ? 39.716 -22.107 -3.578  1.00 13.65 ?  116 PHE   B HZ   1 
ATOM   5755 N  N    . ASN   B 1 117 ? 34.006 -16.188 -5.300  1.00 11.17 ?  117 ASN   B N    1 
ATOM   5756 C  CA   . ASN   B 1 117 ? 33.051 -15.480 -6.158  1.00 11.39 ?  117 ASN   B CA   1 
ATOM   5757 C  C    . ASN   B 1 117 ? 33.365 -14.002 -6.305  1.00 11.90 ?  117 ASN   B C    1 
ATOM   5758 O  O    . ASN   B 1 117 ? 32.764 -13.345 -7.155  1.00 12.81 ?  117 ASN   B O    1 
ATOM   5759 C  CB   . ASN   B 1 117 ? 31.630 -15.703 -5.662  1.00 11.71 ?  117 ASN   B CB   1 
ATOM   5760 C  CG   . ASN   B 1 117 ? 31.180 -17.111 -5.917  1.00 11.85 ?  117 ASN   B CG   1 
ATOM   5761 O  OD1  . ASN   B 1 117 ? 31.530 -17.697 -6.944  1.00 12.78 ?  117 ASN   B OD1  1 
ATOM   5762 N  ND2  . ASN   B 1 117 ? 30.445 -17.684 -4.980  1.00 11.81 ?  117 ASN   B ND2  1 
ATOM   5763 H  H    . ASN   B 1 117 ? 33.682 -16.446 -4.543  1.00 13.41 ?  117 ASN   B H    1 
ATOM   5764 H  HA   . ASN   B 1 117 ? 33.106 -15.872 -7.037  1.00 13.67 ?  117 ASN   B HA   1 
ATOM   5765 H  HB2  . ASN   B 1 117 ? 31.593 -15.539 -4.701  1.00 14.06 ?  117 ASN   B HB2  1 
ATOM   5766 H  HB3  . ASN   B 1 117 ? 31.031 -15.094 -6.123  1.00 14.06 ?  117 ASN   B HB3  1 
ATOM   5767 H  HD21 . ASN   B 1 117 ? 30.170 -18.492 -5.081  1.00 14.18 ?  117 ASN   B HD21 1 
ATOM   5768 H  HD22 . ASN   B 1 117 ? 30.230 -17.244 -4.270  1.00 14.18 ?  117 ASN   B HD22 1 
ATOM   5769 N  N    . GLN   B 1 118 ? 34.306 -13.480 -5.530  1.00 11.47 ?  118 GLN   B N    1 
ATOM   5770 C  CA   . GLN   B 1 118 ? 34.735 -12.090 -5.660  1.00 11.98 ?  118 GLN   B CA   1 
ATOM   5771 C  C    . GLN   B 1 118 ? 35.802 -11.894 -6.733  1.00 11.99 ?  118 GLN   B C    1 
ATOM   5772 O  O    . GLN   B 1 118 ? 36.274 -10.764 -6.909  1.00 13.43 ?  118 GLN   B O    1 
ATOM   5773 C  CB   . GLN   B 1 118 ? 35.208 -11.571 -4.297  1.00 12.47 ?  118 GLN   B CB   1 
ATOM   5774 C  CG   . GLN   B 1 118 ? 34.121 -11.605 -3.230  1.00 12.64 ?  118 GLN   B CG   1 
ATOM   5775 C  CD   . GLN   B 1 118 ? 32.950 -10.700 -3.569  1.00 12.98 ?  118 GLN   B CD   1 
ATOM   5776 O  OE1  . GLN   B 1 118 ? 33.141 -9.563  -4.018  1.00 13.30 ?  118 GLN   B OE1  1 
ATOM   5777 N  NE2  . GLN   B 1 118 ? 31.733 -11.199 -3.372  1.00 13.24 ?  118 GLN   B NE2  1 
ATOM   5778 H  H    . GLN   B 1 118 ? 34.725 -13.910 -4.914  1.00 13.77 ?  118 GLN   B H    1 
ATOM   5779 H  HA   . GLN   B 1 118 ? 33.971 -11.557 -5.923  1.00 14.38 ?  118 GLN   B HA   1 
ATOM   5780 H  HB2  . GLN   B 1 118 ? 35.945 -12.115 -3.987  1.00 14.97 ?  118 GLN   B HB2  1 
ATOM   5781 H  HB3  . GLN   B 1 118 ? 35.494 -10.647 -4.392  1.00 14.97 ?  118 GLN   B HB3  1 
ATOM   5782 H  HG2  . GLN   B 1 118 ? 33.787 -12.516 -3.146  1.00 15.18 ?  118 GLN   B HG2  1 
ATOM   5783 H  HG3  . GLN   B 1 118 ? 34.493 -11.312 -2.384  1.00 15.18 ?  118 GLN   B HG3  1 
ATOM   5784 H  HE21 . GLN   B 1 118 ? 31.641 -11.996 -3.054  1.00 15.89 ?  118 GLN   B HE21 1 
ATOM   5785 H  HE22 . GLN   B 1 118 ? 31.045 -10.723 -3.548  1.00 15.89 ?  118 GLN   B HE22 1 
ATOM   5786 N  N    . HIS   B 1 119 ? 36.156 -12.946 -7.478  1.00 11.78 ?  119 HIS   B N    1 
ATOM   5787 C  CA   . HIS   B 1 119 ? 37.202 -12.897 -8.492  1.00 11.83 ?  119 HIS   B CA   1 
ATOM   5788 C  C    . HIS   B 1 119 ? 36.714 -13.621 -9.735  1.00 11.99 ?  119 HIS   B C    1 
ATOM   5789 O  O    . HIS   B 1 119 ? 36.197 -14.737 -9.645  1.00 12.60 ?  119 HIS   B O    1 
ATOM   5790 C  CB   . HIS   B 1 119 ? 38.478 -13.537 -7.946  1.00 12.41 ?  119 HIS   B CB   1 
ATOM   5791 C  CG   . HIS   B 1 119 ? 38.949 -12.860 -6.706  1.00 13.46 ?  119 HIS   B CG   1 
ATOM   5792 N  ND1  . HIS   B 1 119 ? 39.752 -11.739 -6.734  1.00 15.54 ?  119 HIS   B ND1  1 
ATOM   5793 C  CD2  . HIS   B 1 119 ? 38.641 -13.074 -5.406  1.00 14.61 ?  119 HIS   B CD2  1 
ATOM   5794 C  CE1  . HIS   B 1 119 ? 39.949 -11.320 -5.497  1.00 16.27 ?  119 HIS   B CE1  1 
ATOM   5795 N  NE2  . HIS   B 1 119 ? 39.281 -12.108 -4.675  1.00 16.24 ?  119 HIS   B NE2  1 
ATOM   5796 H  H    . HIS   B 1 119 ? 35.776 -13.716 -7.417  1.00 14.14 ?  119 HIS   B H    1 
ATOM   5797 H  HA   . HIS   B 1 119 ? 37.388 -11.974 -8.724  1.00 14.20 ?  119 HIS   B HA   1 
ATOM   5798 H  HB2  . HIS   B 1 119 ? 38.304 -14.467 -7.739  1.00 14.90 ?  119 HIS   B HB2  1 
ATOM   5799 H  HB3  . HIS   B 1 119 ? 39.177 -13.467 -8.615  1.00 14.90 ?  119 HIS   B HB3  1 
ATOM   5800 H  HD2  . HIS   B 1 119 ? 38.100 -13.758 -5.072  1.00 17.54 ?  119 HIS   B HD2  1 
ATOM   5801 H  HE1  . HIS   B 1 119 ? 40.482 -10.602 -5.242  1.00 19.53 ?  119 HIS   B HE1  1 
ATOM   5802 H  HE2  . HIS   B 1 119 ? 39.274 -12.048 -3.814  1.00 19.49 ?  119 HIS   B HE2  1 
ATOM   5803 N  N    A GLU   B 1 120 ? 36.877 -12.992 -10.897 0.66 12.15 ?  120 GLU   B N    1 
ATOM   5804 N  N    B GLU   B 1 120 ? 36.880 -12.987 -10.898 0.34 13.25 ?  120 GLU   B N    1 
ATOM   5805 C  CA   A GLU   B 1 120 ? 36.292 -13.555 -12.109 0.66 13.59 ?  120 GLU   B CA   1 
ATOM   5806 C  CA   B GLU   B 1 120 ? 36.306 -13.540 -12.120 0.34 14.91 ?  120 GLU   B CA   1 
ATOM   5807 C  C    A GLU   B 1 120 ? 36.959 -14.860 -12.525 0.66 12.95 ?  120 GLU   B C    1 
ATOM   5808 C  C    B GLU   B 1 120 ? 36.962 -14.854 -12.524 0.34 13.57 ?  120 GLU   B C    1 
ATOM   5809 O  O    A GLU   B 1 120 ? 36.294 -15.734 -13.096 0.66 12.97 ?  120 GLU   B O    1 
ATOM   5810 O  O    B GLU   B 1 120 ? 36.292 -15.730 -13.084 0.34 13.42 ?  120 GLU   B O    1 
ATOM   5811 C  CB   A GLU   B 1 120 ? 36.324 -12.532 -13.242 0.66 17.91 ?  120 GLU   B CB   1 
ATOM   5812 C  CB   B GLU   B 1 120 ? 36.391 -12.519 -13.256 0.34 18.74 ?  120 GLU   B CB   1 
ATOM   5813 C  CG   A GLU   B 1 120 ? 35.282 -11.435 -13.088 0.66 23.88 ?  120 GLU   B CG   1 
ATOM   5814 C  CG   B GLU   B 1 120 ? 35.460 -11.330 -13.079 0.34 23.07 ?  120 GLU   B CG   1 
ATOM   5815 C  CD   A GLU   B 1 120 ? 35.145 -10.568 -14.323 0.66 29.10 ?  120 GLU   B CD   1 
ATOM   5816 C  CD   B GLU   B 1 120 ? 35.415 -10.435 -14.304 0.34 26.98 ?  120 GLU   B CD   1 
ATOM   5817 O  OE1  A GLU   B 1 120 ? 36.169 -10.308 -14.990 0.66 30.87 ?  120 GLU   B OE1  1 
ATOM   5818 O  OE1  B GLU   B 1 120 ? 36.374 -10.476 -15.104 0.34 28.10 ?  120 GLU   B OE1  1 
ATOM   5819 O  OE2  A GLU   B 1 120 ? 34.008 -10.147 -14.625 0.66 31.50 -1 120 GLU   B OE2  1 
ATOM   5820 O  OE2  B GLU   B 1 120 ? 34.427 -9.688  -14.464 0.34 28.31 -1 120 GLU   B OE2  1 
ATOM   5821 H  H    A GLU   B 1 120 ? 37.314 -12.253 -11.010 0.66 14.58 ?  120 GLU   B H    1 
ATOM   5822 H  H    B GLU   B 1 120 ? 37.315 -12.249 -11.003 0.34 15.91 ?  120 GLU   B H    1 
ATOM   5823 H  HA   A GLU   B 1 120 ? 35.366 -13.755 -11.929 0.66 16.32 ?  120 GLU   B HA   1 
ATOM   5824 H  HA   B GLU   B 1 120 ? 35.371 -13.721 -11.962 0.34 17.90 ?  120 GLU   B HA   1 
ATOM   5825 H  HB2  A GLU   B 1 120 ? 37.195 -12.108 -13.266 0.66 21.50 ?  120 GLU   B HB2  1 
ATOM   5826 H  HB2  B GLU   B 1 120 ? 37.297 -12.177 -13.307 0.34 22.50 ?  120 GLU   B HB2  1 
ATOM   5827 H  HB3  A GLU   B 1 120 ? 36.153 -12.985 -14.082 0.66 21.50 ?  120 GLU   B HB3  1 
ATOM   5828 H  HB3  B GLU   B 1 120 ? 36.157 -12.958 -14.089 0.34 22.50 ?  120 GLU   B HB3  1 
ATOM   5829 H  HG2  A GLU   B 1 120 ? 34.417 -11.841 -12.915 0.66 28.67 ?  120 GLU   B HG2  1 
ATOM   5830 H  HG2  B GLU   B 1 120 ? 34.563 -11.657 -12.887 0.34 27.69 ?  120 GLU   B HG2  1 
ATOM   5831 H  HG3  A GLU   B 1 120 ? 35.532 -10.859 -12.351 0.66 28.67 ?  120 GLU   B HG3  1 
ATOM   5832 H  HG3  B GLU   B 1 120 ? 35.775 -10.785 -12.344 0.34 27.69 ?  120 GLU   B HG3  1 
ATOM   5833 N  N    . VAL   B 1 121 ? 38.256 -15.011 -12.253 1.00 12.59 ?  121 VAL   B N    1 
ATOM   5834 C  CA   . VAL   B 1 121 ? 38.995 -16.223 -12.609 1.00 12.26 ?  121 VAL   B CA   1 
ATOM   5835 C  C    . VAL   B 1 121 ? 40.110 -16.437 -11.592 1.00 11.79 ?  121 VAL   B C    1 
ATOM   5836 O  O    . VAL   B 1 121 ? 40.794 -15.487 -11.194 1.00 12.62 ?  121 VAL   B O    1 
ATOM   5837 C  CB   . VAL   B 1 121 ? 39.509 -16.170 -14.067 1.00 14.27 ?  121 VAL   B CB   1 
ATOM   5838 C  CG1  . VAL   B 1 121 ? 40.367 -14.929 -14.312 1.00 15.68 ?  121 VAL   B CG1  1 
ATOM   5839 C  CG2  . VAL   B 1 121 ? 40.259 -17.444 -14.428 1.00 15.60 ?  121 VAL   B CG2  1 
ATOM   5840 H  H    A VAL   B 1 121 ? 38.741 -14.418 -11.859 0.66 15.12 ?  121 VAL   B H    1 
ATOM   5841 H  H    B VAL   B 1 121 ? 38.742 -14.419 -11.858 0.34 15.12 ?  121 VAL   B H    1 
ATOM   5842 H  HA   . VAL   B 1 121 ? 38.387 -16.975 -12.543 1.00 14.72 ?  121 VAL   B HA   1 
ATOM   5843 H  HB   . VAL   B 1 121 ? 38.739 -16.113 -14.658 1.00 17.13 ?  121 VAL   B HB   1 
ATOM   5844 H  HG11 . VAL   B 1 121 ? 40.682 -14.940 -15.230 1.00 18.82 ?  121 VAL   B HG11 1 
ATOM   5845 H  HG12 . VAL   B 1 121 ? 39.824 -14.136 -14.163 1.00 18.82 ?  121 VAL   B HG12 1 
ATOM   5846 H  HG13 . VAL   B 1 121 ? 41.117 -14.936 -13.703 1.00 18.82 ?  121 VAL   B HG13 1 
ATOM   5847 H  HG21 . VAL   B 1 121 ? 40.456 -17.434 -15.379 1.00 18.72 ?  121 VAL   B HG21 1 
ATOM   5848 H  HG22 . VAL   B 1 121 ? 41.086 -17.479 -13.921 1.00 18.72 ?  121 VAL   B HG22 1 
ATOM   5849 H  HG23 . VAL   B 1 121 ? 39.705 -18.210 -14.215 1.00 18.72 ?  121 VAL   B HG23 1 
ATOM   5850 N  N    . LEU   B 1 122 ? 40.293 -17.691 -11.169 1.00 11.43 ?  122 LEU   B N    1 
ATOM   5851 C  CA   . LEU   B 1 122 ? 41.278 -18.049 -10.152 1.00 10.93 ?  122 LEU   B CA   1 
ATOM   5852 C  C    . LEU   B 1 122 ? 41.925 -19.382 -10.483 1.00 10.90 ?  122 LEU   B C    1 
ATOM   5853 O  O    . LEU   B 1 122 ? 41.256 -20.305 -10.971 1.00 12.24 ?  122 LEU   B O    1 
ATOM   5854 C  CB   . LEU   B 1 122 ? 40.637 -18.285 -8.771  1.00 12.97 ?  122 LEU   B CB   1 
ATOM   5855 C  CG   . LEU   B 1 122 ? 39.595 -17.274 -8.287  1.00 12.87 ?  122 LEU   B CG   1 
ATOM   5856 C  CD1  . LEU   B 1 122 ? 38.204 -17.655 -8.761  1.00 13.80 ?  122 LEU   B CD1  1 
ATOM   5857 C  CD2  . LEU   B 1 122 ? 39.640 -17.157 -6.780  1.00 12.29 ?  122 LEU   B CD2  1 
ATOM   5858 H  H    . LEU   B 1 122 ? 39.852 -18.366 -11.467 1.00 13.73 ?  122 LEU   B H    1 
ATOM   5859 H  HA   . LEU   B 1 122 ? 41.958 -17.358 -10.075 1.00 13.12 ?  122 LEU   B HA   1 
ATOM   5860 H  HB2  . LEU   B 1 122 ? 40.200 -19.151 -8.790  1.00 15.57 ?  122 LEU   B HB2  1 
ATOM   5861 H  HB3  . LEU   B 1 122 ? 41.343 -18.299 -8.109  1.00 15.57 ?  122 LEU   B HB3  1 
ATOM   5862 H  HG   . LEU   B 1 122 ? 39.806 -16.405 -8.662  1.00 15.45 ?  122 LEU   B HG   1 
ATOM   5863 H  HD11 . LEU   B 1 122 ? 37.562 -17.020 -8.405  1.00 16.56 ?  122 LEU   B HD11 1 
ATOM   5864 H  HD12 . LEU   B 1 122 ? 38.178 -17.637 -9.732  1.00 16.56 ?  122 LEU   B HD12 1 
ATOM   5865 H  HD13 . LEU   B 1 122 ? 37.992 -18.548 -8.444  1.00 16.56 ?  122 LEU   B HD13 1 
ATOM   5866 H  HD21 . LEU   B 1 122 ? 38.954 -16.539 -6.490  1.00 14.76 ?  122 LEU   B HD21 1 
ATOM   5867 H  HD22 . LEU   B 1 122 ? 39.492 -18.031 -6.391  1.00 14.76 ?  122 LEU   B HD22 1 
ATOM   5868 H  HD23 . LEU   B 1 122 ? 40.517 -16.824 -6.519  1.00 14.76 ?  122 LEU   B HD23 1 
ATOM   5869 N  N    . LEU   B 1 123 ? 43.213 -19.498 -10.127 1.00 10.50 ?  123 LEU   B N    1 
ATOM   5870 C  CA   . LEU   B 1 123 ? 43.923 -20.774 -10.006 1.00 10.64 ?  123 LEU   B CA   1 
ATOM   5871 C  C    . LEU   B 1 123 ? 43.903 -21.172 -8.535  1.00 10.34 ?  123 LEU   B C    1 
ATOM   5872 O  O    . LEU   B 1 123 ? 44.246 -20.345 -7.677  1.00 10.92 ?  123 LEU   B O    1 
ATOM   5873 C  CB   . LEU   B 1 123 ? 45.368 -20.599 -10.480 1.00 11.01 ?  123 LEU   B CB   1 
ATOM   5874 C  CG   . LEU   B 1 123 ? 46.314 -21.783 -10.254 1.00 11.70 ?  123 LEU   B CG   1 
ATOM   5875 C  CD1  . LEU   B 1 123 ? 45.863 -23.026 -11.010 1.00 12.48 ?  123 LEU   B CD1  1 
ATOM   5876 C  CD2  . LEU   B 1 123 ? 47.731 -21.398 -10.644 1.00 12.86 ?  123 LEU   B CD2  1 
ATOM   5877 H  H    . LEU   B 1 123 ? 43.713 -18.819 -9.931  1.00 12.61 ?  123 LEU   B H    1 
ATOM   5878 H  HA   . LEU   B 1 123 ? 43.478 -21.456 -10.533 1.00 12.77 ?  123 LEU   B HA   1 
ATOM   5879 H  HB2  . LEU   B 1 123 ? 45.350 -20.423 -11.432 1.00 13.21 ?  123 LEU   B HB2  1 
ATOM   5880 H  HB3  . LEU   B 1 123 ? 45.746 -19.838 -10.017 1.00 13.21 ?  123 LEU   B HB3  1 
ATOM   5881 H  HG   . LEU   B 1 123 ? 46.322 -22.004 -9.310  1.00 14.05 ?  123 LEU   B HG   1 
ATOM   5882 H  HD11 . LEU   B 1 123 ? 46.501 -23.737 -10.855 1.00 14.99 ?  123 LEU   B HD11 1 
ATOM   5883 H  HD12 . LEU   B 1 123 ? 44.986 -23.290 -10.683 1.00 14.99 ?  123 LEU   B HD12 1 
ATOM   5884 H  HD13 . LEU   B 1 123 ? 45.815 -22.819 -11.955 1.00 14.99 ?  123 LEU   B HD13 1 
ATOM   5885 H  HD21 . LEU   B 1 123 ? 48.316 -22.158 -10.497 1.00 15.44 ?  123 LEU   B HD21 1 
ATOM   5886 H  HD22 . LEU   B 1 123 ? 47.744 -21.148 -11.581 1.00 15.44 ?  123 LEU   B HD22 1 
ATOM   5887 H  HD23 . LEU   B 1 123 ? 48.015 -20.650 -10.097 1.00 15.44 ?  123 LEU   B HD23 1 
ATOM   5888 N  N    . ALA   B 1 124 ? 43.466 -22.404 -8.229  1.00 10.50 ?  124 ALA   B N    1 
ATOM   5889 C  CA   . ALA   B 1 124 ? 43.206 -22.720 -6.831  1.00 10.69 ?  124 ALA   B CA   1 
ATOM   5890 C  C    . ALA   B 1 124 ? 43.485 -24.180 -6.511  1.00 10.04 ?  124 ALA   B C    1 
ATOM   5891 O  O    . ALA   B 1 124 ? 43.352 -25.056 -7.377  1.00 10.87 ?  124 ALA   B O    1 
ATOM   5892 C  CB   . ALA   B 1 124 ? 41.757 -22.408 -6.456  1.00 11.42 ?  124 ALA   B CB   1 
ATOM   5893 H  H    . ALA   B 1 124 ? 43.304 -23.037 -8.793  1.00 12.61 ?  124 ALA   B H    1 
ATOM   5894 H  HA   . ALA   B 1 124 ? 43.786 -22.175 -6.289  1.00 12.83 ?  124 ALA   B HA   1 
ATOM   5895 H  HB1  . ALA   B 1 124 ? 41.612 -22.631 -5.524  1.00 13.71 ?  124 ALA   B HB1  1 
ATOM   5896 H  HB2  . ALA   B 1 124 ? 41.593 -21.460 -6.597  1.00 13.71 ?  124 ALA   B HB2  1 
ATOM   5897 H  HB3  . ALA   B 1 124 ? 41.159 -22.929 -7.018  1.00 13.71 ?  124 ALA   B HB3  1 
ATOM   5898 N  N    . PRO   B 1 125 ? 43.782 -24.478 -5.248  1.00 10.51 ?  125 PRO   B N    1 
ATOM   5899 C  CA   . PRO   B 1 125 ? 43.729 -25.846 -4.733  1.00 11.36 ?  125 PRO   B CA   1 
ATOM   5900 C  C    . PRO   B 1 125 ? 42.331 -26.119 -4.181  1.00 11.69 ?  125 PRO   B C    1 
ATOM   5901 O  O    . PRO   B 1 125 ? 41.530 -25.205 -3.979  1.00 12.07 ?  125 PRO   B O    1 
ATOM   5902 C  CB   . PRO   B 1 125 ? 44.728 -25.776 -3.570  1.00 12.51 ?  125 PRO   B CB   1 
ATOM   5903 C  CG   . PRO   B 1 125 ? 44.461 -24.395 -2.980  1.00 12.57 ?  125 PRO   B CG   1 
ATOM   5904 C  CD   . PRO   B 1 125 ? 44.117 -23.512 -4.180  1.00 11.19 ?  125 PRO   B CD   1 
ATOM   5905 H  HA   . PRO   B 1 125 ? 44.005 -26.508 -5.389  1.00 13.64 ?  125 PRO   B HA   1 
ATOM   5906 H  HB2  . PRO   B 1 125 ? 44.538 -26.472 -2.918  1.00 15.02 ?  125 PRO   B HB2  1 
ATOM   5907 H  HB3  . PRO   B 1 125 ? 45.639 -25.843 -3.895  1.00 15.02 ?  125 PRO   B HB3  1 
ATOM   5908 H  HG2  . PRO   B 1 125 ? 43.711 -24.434 -2.361  1.00 15.09 ?  125 PRO   B HG2  1 
ATOM   5909 H  HG3  . PRO   B 1 125 ? 45.256 -24.064 -2.524  1.00 15.09 ?  125 PRO   B HG3  1 
ATOM   5910 H  HD2  . PRO   B 1 125 ? 43.356 -22.948 -3.987  1.00 13.44 ?  125 PRO   B HD2  1 
ATOM   5911 H  HD3  . PRO   B 1 125 ? 44.894 -22.978 -4.438  1.00 13.44 ?  125 PRO   B HD3  1 
ATOM   5912 N  N    . LEU   B 1 126 ? 42.066 -27.395 -3.894  1.00 12.09 ?  126 LEU   B N    1 
ATOM   5913 C  CA   . LEU   B 1 126 ? 40.844 -27.757 -3.181  1.00 12.41 ?  126 LEU   B CA   1 
ATOM   5914 C  C    . LEU   B 1 126 ? 40.962 -27.354 -1.719  1.00 12.63 ?  126 LEU   B C    1 
ATOM   5915 O  O    . LEU   B 1 126 ? 41.860 -27.811 -1.004  1.00 14.55 ?  126 LEU   B O    1 
ATOM   5916 C  CB   . LEU   B 1 126 ? 40.587 -29.254 -3.286  1.00 13.98 ?  126 LEU   B CB   1 
ATOM   5917 C  CG   . LEU   B 1 126 ? 40.074 -29.735 -4.643  1.00 15.08 ?  126 LEU   B CG   1 
ATOM   5918 C  CD1  . LEU   B 1 126 ? 40.125 -31.245 -4.720  1.00 16.75 ?  126 LEU   B CD1  1 
ATOM   5919 C  CD2  . LEU   B 1 126 ? 38.655 -29.234 -4.907  1.00 15.05 ?  126 LEU   B CD2  1 
ATOM   5920 H  H    . LEU   B 1 126 ? 42.575 -28.063 -4.095  1.00 14.52 ?  126 LEU   B H    1 
ATOM   5921 H  HA   . LEU   B 1 126 ? 40.096 -27.278 -3.572  1.00 14.90 ?  126 LEU   B HA   1 
ATOM   5922 H  HB2  . LEU   B 1 126 ? 41.415 -29.717 -3.103  1.00 16.78 ?  126 LEU   B HB2  1 
ATOM   5923 H  HB3  . LEU   B 1 126 ? 39.922 -29.491 -2.623  1.00 16.78 ?  126 LEU   B HB3  1 
ATOM   5924 H  HG   . LEU   B 1 126 ? 40.652 -29.374 -5.339  1.00 18.10 ?  126 LEU   B HG   1 
ATOM   5925 H  HD11 . LEU   B 1 126 ? 39.796 -31.525 -5.586  1.00 20.10 ?  126 LEU   B HD11 1 
ATOM   5926 H  HD12 . LEU   B 1 126 ? 41.042 -31.535 -4.599  1.00 20.10 ?  126 LEU   B HD12 1 
ATOM   5927 H  HD13 . LEU   B 1 126 ? 39.566 -31.610 -4.016  1.00 20.10 ?  126 LEU   B HD13 1 
ATOM   5928 H  HD21 . LEU   B 1 126 ? 38.323 -29.647 -5.717  1.00 18.06 ?  126 LEU   B HD21 1 
ATOM   5929 H  HD22 . LEU   B 1 126 ? 38.093 -29.473 -4.155  1.00 18.06 ?  126 LEU   B HD22 1 
ATOM   5930 H  HD23 . LEU   B 1 126 ? 38.671 -28.267 -5.012  1.00 18.06 ?  126 LEU   B HD23 1 
ATOM   5931 N  N    . LEU   B 1 127 ? 40.035 -26.524 -1.259  1.00 12.54 ?  127 LEU   B N    1 
ATOM   5932 C  CA   . LEU   B 1 127 ? 40.093 -26.037 0.107   1.00 12.80 ?  127 LEU   B CA   1 
ATOM   5933 C  C    . LEU   B 1 127 ? 39.812 -27.156 1.104   1.00 12.85 ?  127 LEU   B C    1 
ATOM   5934 O  O    . LEU   B 1 127 ? 38.982 -28.046 0.882   1.00 13.22 ?  127 LEU   B O    1 
ATOM   5935 C  CB   . LEU   B 1 127 ? 39.082 -24.909 0.313   1.00 13.39 ?  127 LEU   B CB   1 
ATOM   5936 C  CG   . LEU   B 1 127 ? 39.261 -23.649 -0.530  1.00 14.18 ?  127 LEU   B CG   1 
ATOM   5937 C  CD1  . LEU   B 1 127 ? 38.136 -22.679 -0.198  1.00 14.13 ?  127 LEU   B CD1  1 
ATOM   5938 C  CD2  . LEU   B 1 127 ? 40.624 -23.010 -0.298  1.00 14.59 ?  127 LEU   B CD2  1 
ATOM   5939 H  H    . LEU   B 1 127 ? 39.362 -26.224 -1.716  1.00 15.06 ?  127 LEU   B H    1 
ATOM   5940 H  HA   . LEU   B 1 127 ? 40.983 -25.681 0.279   1.00 15.37 ?  127 LEU   B HA   1 
ATOM   5941 H  HB2  . LEU   B 1 127 ? 38.200 -25.260 0.119   1.00 16.07 ?  127 LEU   B HB2  1 
ATOM   5942 H  HB3  . LEU   B 1 127 ? 39.121 -24.638 1.243   1.00 16.07 ?  127 LEU   B HB3  1 
ATOM   5943 H  HG   . LEU   B 1 127 ? 39.186 -23.878 -1.467  1.00 17.02 ?  127 LEU   B HG   1 
ATOM   5944 H  HD11 . LEU   B 1 127 ? 38.249 -21.871 -0.724  1.00 16.96 ?  127 LEU   B HD11 1 
ATOM   5945 H  HD12 . LEU   B 1 127 ? 37.286 -23.094 -0.406  1.00 16.96 ?  127 LEU   B HD12 1 
ATOM   5946 H  HD13 . LEU   B 1 127 ? 38.175 -22.462 0.749   1.00 16.96 ?  127 LEU   B HD13 1 
ATOM   5947 H  HD21 . LEU   B 1 127 ? 40.662 -22.162 -0.763  1.00 17.52 ?  127 LEU   B HD21 1 
ATOM   5948 H  HD22 . LEU   B 1 127 ? 40.750 -22.871 0.656   1.00 17.52 ?  127 LEU   B HD22 1 
ATOM   5949 H  HD23 . LEU   B 1 127 ? 41.311 -23.606 -0.636  1.00 17.52 ?  127 LEU   B HD23 1 
ATOM   5950 N  N    . SER   B 1 128 ? 40.493 -27.077 2.238   1.00 12.74 ?  128 SER   B N    1 
ATOM   5951 C  CA   . SER   B 1 128 ? 40.374 -27.985 3.369   1.00 13.02 ?  128 SER   B CA   1 
ATOM   5952 C  C    . SER   B 1 128 ? 40.862 -29.397 3.054   1.00 14.59 ?  128 SER   B C    1 
ATOM   5953 O  O    . SER   B 1 128 ? 40.764 -30.273 3.918   1.00 16.05 ?  128 SER   B O    1 
ATOM   5954 C  CB   . SER   B 1 128 ? 38.968 -27.982 3.992   1.00 13.31 ?  128 SER   B CB   1 
ATOM   5955 O  OG   . SER   B 1 128 ? 38.664 -26.706 4.551   1.00 14.24 ?  128 SER   B OG   1 
ATOM   5956 H  H    . SER   B 1 128 ? 41.064 -26.446 2.385   1.00 15.29 ?  128 SER   B H    1 
ATOM   5957 H  HA   . SER   B 1 128 ? 40.962 -27.648 4.051   1.00 15.63 ?  128 SER   B HA   1 
ATOM   5958 H  HB2  . SER   B 1 128 ? 38.312 -28.200 3.306   1.00 15.98 ?  128 SER   B HB2  1 
ATOM   5959 H  HB3  . SER   B 1 128 ? 38.938 -28.659 4.694   1.00 15.98 ?  128 SER   B HB3  1 
ATOM   5960 H  HG   . SER   B 1 128 ? 39.231 -26.520 5.142   1.00 17.10 ?  128 SER   B HG   1 
ATOM   5961 N  N    . ALA   B 1 129 ? 41.425 -29.632 1.867   1.00 15.73 ?  129 ALA   B N    1 
ATOM   5962 C  CA   . ALA   B 1 129 ? 41.963 -30.932 1.504   1.00 16.53 ?  129 ALA   B CA   1 
ATOM   5963 C  C    . ALA   B 1 129 ? 43.364 -31.108 2.083   1.00 15.84 ?  129 ALA   B C    1 
ATOM   5964 O  O    . ALA   B 1 129 ? 43.918 -30.218 2.743   1.00 15.28 ?  129 ALA   B O    1 
ATOM   5965 C  CB   . ALA   B 1 129 ? 41.991 -31.091 -0.014  1.00 18.50 ?  129 ALA   B CB   1 
ATOM   5966 H  H    . ALA   B 1 129 ? 41.500 -29.043 1.240   1.00 18.89 ?  129 ALA   B H    1 
ATOM   5967 H  HA   . ALA   B 1 129 ? 41.394 -31.625 1.869   1.00 19.85 ?  129 ALA   B HA   1 
ATOM   5968 H  HB1  . ALA   B 1 129 ? 42.343 -31.968 -0.234  1.00 22.21 ?  129 ALA   B HB1  1 
ATOM   5969 H  HB2  . ALA   B 1 129 ? 41.090 -31.000 -0.358  1.00 22.21 ?  129 ALA   B HB2  1 
ATOM   5970 H  HB3  . ALA   B 1 129 ? 42.562 -30.403 -0.394  1.00 22.21 ?  129 ALA   B HB3  1 
ATOM   5971 N  N    . GLY   B 1 130 ? 43.941 -32.279 1.825   1.00 15.46 ?  130 GLY   B N    1 
ATOM   5972 C  CA   . GLY   B 1 130 ? 45.332 -32.508 2.174   1.00 15.70 ?  130 GLY   B CA   1 
ATOM   5973 C  C    . GLY   B 1 130 ? 45.546 -32.425 3.669   1.00 15.81 ?  130 GLY   B C    1 
ATOM   5974 O  O    . GLY   B 1 130 ? 44.842 -33.066 4.463   1.00 16.89 ?  130 GLY   B O    1 
ATOM   5975 H  H    . GLY   B 1 130 ? 43.554 -32.944 1.441   1.00 18.56 ?  130 GLY   B H    1 
ATOM   5976 H  HA2  . GLY   B 1 130 ? 45.603 -33.388 1.862   1.00 18.85 ?  130 GLY   B HA2  1 
ATOM   5977 H  HA3  . GLY   B 1 130 ? 45.891 -31.844 1.741   1.00 18.85 ?  130 GLY   B HA3  1 
ATOM   5978 N  N    . ILE   B 1 131 ? 46.523 -31.601 4.063   1.00 16.41 ?  131 ILE   B N    1 
ATOM   5979 C  CA   . ILE   B 1 131 ? 46.892 -31.484 5.468   1.00 17.47 ?  131 ILE   B CA   1 
ATOM   5980 C  C    . ILE   B 1 131 ? 45.785 -30.881 6.316   1.00 16.67 ?  131 ILE   B C    1 
ATOM   5981 O  O    . ILE   B 1 131 ? 45.869 -30.942 7.547   1.00 18.00 ?  131 ILE   B O    1 
ATOM   5982 C  CB   . ILE   B 1 131 ? 48.214 -30.707 5.663   1.00 19.18 ?  131 ILE   B CB   1 
ATOM   5983 C  CG1  . ILE   B 1 131 ? 48.051 -29.226 5.295   1.00 20.00 ?  131 ILE   B CG1  1 
ATOM   5984 C  CG2  . ILE   B 1 131 ? 49.342 -31.344 4.849   1.00 20.27 ?  131 ILE   B CG2  1 
ATOM   5985 C  CD1  . ILE   B 1 131 ? 49.263 -28.371 5.630   1.00 21.24 ?  131 ILE   B CD1  1 
ATOM   5986 H  H    . ILE   B 1 131 ? 46.976 -31.096 3.534   1.00 19.70 ?  131 ILE   B H    1 
ATOM   5987 H  HA   . ILE   B 1 131 ? 47.040 -32.379 5.805   1.00 20.97 ?  131 ILE   B HA   1 
ATOM   5988 H  HB   . ILE   B 1 131 ? 48.451 -30.759 6.601   1.00 23.02 ?  131 ILE   B HB   1 
ATOM   5989 H  HG12 . ILE   B 1 131 ? 47.889 -29.159 4.342   1.00 24.01 ?  131 ILE   B HG12 1 
ATOM   5990 H  HG13 . ILE   B 1 131 ? 47.293 -28.857 5.780   1.00 24.01 ?  131 ILE   B HG13 1 
ATOM   5991 H  HG21 . ILE   B 1 131 ? 50.182 -30.932 5.104   1.00 24.33 ?  131 ILE   B HG21 1 
ATOM   5992 H  HG22 . ILE   B 1 131 ? 49.365 -32.292 5.034   1.00 24.33 ?  131 ILE   B HG22 1 
ATOM   5993 H  HG23 . ILE   B 1 131 ? 49.171 -31.191 3.906   1.00 24.33 ?  131 ILE   B HG23 1 
ATOM   5994 H  HD11 . ILE   B 1 131 ? 49.043 -27.440 5.467   1.00 25.49 ?  131 ILE   B HD11 1 
ATOM   5995 H  HD12 . ILE   B 1 131 ? 49.488 -28.498 6.565   1.00 25.49 ?  131 ILE   B HD12 1 
ATOM   5996 H  HD13 . ILE   B 1 131 ? 50.003 -28.641 5.069   1.00 25.49 ?  131 ILE   B HD13 1 
ATOM   5997 N  N    . PHE   B 1 132 ? 44.754 -30.299 5.696   1.00 15.49 ?  132 PHE   B N    1 
ATOM   5998 C  CA   . PHE   B 1 132 ? 43.608 -29.782 6.439   1.00 15.81 ?  132 PHE   B CA   1 
ATOM   5999 C  C    . PHE   B 1 132 ? 42.585 -30.864 6.783   1.00 17.46 ?  132 PHE   B C    1 
ATOM   6000 O  O    . PHE   B 1 132 ? 41.689 -30.601 7.593   1.00 19.35 ?  132 PHE   B O    1 
ATOM   6001 C  CB   . PHE   B 1 132 ? 42.926 -28.649 5.662   1.00 14.62 ?  132 PHE   B CB   1 
ATOM   6002 C  CG   . PHE   B 1 132 ? 43.626 -27.309 5.765   1.00 14.25 ?  132 PHE   B CG   1 
ATOM   6003 C  CD1  . PHE   B 1 132 ? 44.922 -27.133 5.295   1.00 16.03 ?  132 PHE   B CD1  1 
ATOM   6004 C  CD2  . PHE   B 1 132 ? 42.949 -26.208 6.278   1.00 14.37 ?  132 PHE   B CD2  1 
ATOM   6005 C  CE1  . PHE   B 1 132 ? 45.542 -25.896 5.378   1.00 16.56 ?  132 PHE   B CE1  1 
ATOM   6006 C  CE2  . PHE   B 1 132 ? 43.559 -24.970 6.362   1.00 14.69 ?  132 PHE   B CE2  1 
ATOM   6007 C  CZ   . PHE   B 1 132 ? 44.856 -24.811 5.907   1.00 15.58 ?  132 PHE   B CZ   1 
ATOM   6008 H  H    . PHE   B 1 132 ? 44.696 -30.193 4.842   1.00 18.60 ?  132 PHE   B H    1 
ATOM   6009 H  HA   . PHE   B 1 132 ? 43.931 -29.411 7.273   1.00 18.98 ?  132 PHE   B HA   1 
ATOM   6010 H  HB2  . PHE   B 1 132 ? 42.900 -28.893 4.725   1.00 17.55 ?  132 PHE   B HB2  1 
ATOM   6011 H  HB3  . PHE   B 1 132 ? 42.026 -28.541 6.001   1.00 17.55 ?  132 PHE   B HB3  1 
ATOM   6012 H  HD1  . PHE   B 1 132 ? 45.386 -27.861 4.944   1.00 19.25 ?  132 PHE   B HD1  1 
ATOM   6013 H  HD2  . PHE   B 1 132 ? 42.077 -26.310 6.587   1.00 17.25 ?  132 PHE   B HD2  1 
ATOM   6014 H  HE1  . PHE   B 1 132 ? 46.414 -25.792 5.074   1.00 19.87 ?  132 PHE   B HE1  1 
ATOM   6015 H  HE2  . PHE   B 1 132 ? 43.098 -24.242 6.720   1.00 17.63 ?  132 PHE   B HE2  1 
ATOM   6016 H  HZ   . PHE   B 1 132 ? 45.271 -23.976 5.966   1.00 18.70 ?  132 PHE   B HZ   1 
ATOM   6017 N  N    . GLY   B 1 133 ? 42.678 -32.061 6.187   1.00 16.91 ?  133 GLY   B N    1 
ATOM   6018 C  CA   . GLY   B 1 133 ? 41.964 -33.223 6.690   1.00 18.07 ?  133 GLY   B CA   1 
ATOM   6019 C  C    . GLY   B 1 133 ? 40.575 -33.498 6.143   1.00 18.68 ?  133 GLY   B C    1 
ATOM   6020 O  O    . GLY   B 1 133 ? 39.996 -34.528 6.501   1.00 20.86 ?  133 GLY   B O    1 
ATOM   6021 H  H    . GLY   B 1 133 ? 43.157 -32.216 5.486   1.00 20.30 ?  133 GLY   B H    1 
ATOM   6022 H  HA2  . GLY   B 1 133 ? 42.504 -34.007 6.515   1.00 21.69 ?  133 GLY   B HA2  1 
ATOM   6023 H  HA3  . GLY   B 1 133 ? 41.880 -33.131 7.650   1.00 21.69 ?  133 GLY   B HA3  1 
ATOM   6024 N  N    . ALA   B 1 134 ? 40.014 -32.634 5.303   1.00 17.49 ?  134 ALA   B N    1 
ATOM   6025 C  CA   . ALA   B 1 134 ? 38.693 -32.918 4.761   1.00 17.63 ?  134 ALA   B CA   1 
ATOM   6026 C  C    . ALA   B 1 134 ? 38.794 -33.889 3.588   1.00 17.39 ?  134 ALA   B C    1 
ATOM   6027 O  O    . ALA   B 1 134 ? 39.852 -34.059 2.974   1.00 18.31 ?  134 ALA   B O    1 
ATOM   6028 C  CB   . ALA   B 1 134 ? 37.996 -31.634 4.317   1.00 18.29 ?  134 ALA   B CB   1 
ATOM   6029 H  H    . ALA   B 1 134 ? 40.367 -31.895 5.037   1.00 20.99 ?  134 ALA   B H    1 
ATOM   6030 H  HA   . ALA   B 1 134 ? 38.153 -33.335 5.450   1.00 21.17 ?  134 ALA   B HA   1 
ATOM   6031 H  HB1  . ALA   B 1 134 ? 37.112 -31.857 3.984   1.00 21.96 ?  134 ALA   B HB1  1 
ATOM   6032 H  HB2  . ALA   B 1 134 ? 37.923 -31.038 5.077   1.00 21.96 ?  134 ALA   B HB2  1 
ATOM   6033 H  HB3  . ALA   B 1 134 ? 38.519 -31.218 3.616   1.00 21.96 ?  134 ALA   B HB3  1 
ATOM   6034 N  N    . ASP   B 1 135 ? 37.668 -34.524 3.281   1.00 17.76 ?  135 ASP   B N    1 
ATOM   6035 C  CA   . ASP   B 1 135 ? 37.583 -35.415 2.132   1.00 18.76 ?  135 ASP   B CA   1 
ATOM   6036 C  C    . ASP   B 1 135 ? 37.665 -34.573 0.866   1.00 17.36 ?  135 ASP   B C    1 
ATOM   6037 O  O    . ASP   B 1 135 ? 36.798 -33.712 0.652   1.00 17.64 ?  135 ASP   B O    1 
ATOM   6038 C  CB   . ASP   B 1 135 ? 36.249 -36.159 2.187   1.00 20.89 ?  135 ASP   B CB   1 
ATOM   6039 C  CG   . ASP   B 1 135 ? 36.087 -37.167 1.063   1.00 22.78 ?  135 ASP   B CG   1 
ATOM   6040 O  OD1  . ASP   B 1 135 ? 36.948 -37.198 0.156   1.00 22.19 ?  135 ASP   B OD1  1 
ATOM   6041 O  OD2  . ASP   B 1 135 ? 35.105 -37.945 1.100   1.00 25.68 -1 135 ASP   B OD2  1 
ATOM   6042 H  H    . ASP   B 1 135 ? 36.934 -34.447 3.717   1.00 21.31 ?  135 ASP   B H    1 
ATOM   6043 H  HA   . ASP   B 1 135 ? 38.309 -36.059 2.155   1.00 22.52 ?  135 ASP   B HA   1 
ATOM   6044 H  HB2  . ASP   B 1 135 ? 36.194 -36.632 3.030   1.00 25.07 ?  135 ASP   B HB2  1 
ATOM   6045 H  HB3  . ASP   B 1 135 ? 35.532 -35.510 2.121   1.00 25.07 ?  135 ASP   B HB3  1 
ATOM   6046 N  N    . PRO   B 1 136 ? 38.675 -34.762 0.011   1.00 17.76 ?  136 PRO   B N    1 
ATOM   6047 C  CA   . PRO   B 1 136 ? 38.753 -33.933 -1.203  1.00 16.98 ?  136 PRO   B CA   1 
ATOM   6048 C  C    . PRO   B 1 136 ? 37.557 -34.097 -2.118  1.00 16.30 ?  136 PRO   B C    1 
ATOM   6049 O  O    . PRO   B 1 136 ? 37.214 -33.155 -2.839  1.00 15.39 ?  136 PRO   B O    1 
ATOM   6050 C  CB   . PRO   B 1 136 ? 40.062 -34.393 -1.864  1.00 18.01 ?  136 PRO   B CB   1 
ATOM   6051 C  CG   . PRO   B 1 136 ? 40.272 -35.784 -1.345  1.00 19.26 ?  136 PRO   B CG   1 
ATOM   6052 C  CD   . PRO   B 1 136 ? 39.754 -35.760 0.064   1.00 18.78 ?  136 PRO   B CD   1 
ATOM   6053 H  HA   . PRO   B 1 136 ? 38.830 -32.996 -0.968  1.00 20.39 ?  136 PRO   B HA   1 
ATOM   6054 H  HB2  . PRO   B 1 136 ? 39.965 -34.393 -2.832  1.00 21.62 ?  136 PRO   B HB2  1 
ATOM   6055 H  HB3  . PRO   B 1 136 ? 40.788 -33.807 -1.594  1.00 21.62 ?  136 PRO   B HB3  1 
ATOM   6056 H  HG2  . PRO   B 1 136 ? 39.766 -36.413 -1.884  1.00 23.12 ?  136 PRO   B HG2  1 
ATOM   6057 H  HG3  . PRO   B 1 136 ? 41.216 -35.999 -1.358  1.00 23.12 ?  136 PRO   B HG3  1 
ATOM   6058 H  HD2  . PRO   B 1 136 ? 39.400 -36.628 0.309   1.00 22.54 ?  136 PRO   B HD2  1 
ATOM   6059 H  HD3  . PRO   B 1 136 ? 40.445 -35.467 0.677   1.00 22.54 ?  136 PRO   B HD3  1 
ATOM   6060 N  N    . ILE   B 1 137 ? 36.909 -35.264 -2.116  1.00 16.59 ?  137 ILE   B N    1 
ATOM   6061 C  CA   . ILE   B 1 137 ? 35.686 -35.433 -2.899  1.00 16.97 ?  137 ILE   B CA   1 
ATOM   6062 C  C    . ILE   B 1 137 ? 34.611 -34.472 -2.414  1.00 16.67 ?  137 ILE   B C    1 
ATOM   6063 O  O    . ILE   B 1 137 ? 33.883 -33.866 -3.212  1.00 16.27 ?  137 ILE   B O    1 
ATOM   6064 C  CB   . ILE   B 1 137 ? 35.214 -36.902 -2.839  1.00 18.96 ?  137 ILE   B CB   1 
ATOM   6065 C  CG1  . ILE   B 1 137 ? 36.201 -37.812 -3.573  1.00 21.42 ?  137 ILE   B CG1  1 
ATOM   6066 C  CG2  . ILE   B 1 137 ? 33.823 -37.050 -3.443  1.00 19.48 ?  137 ILE   B CG2  1 
ATOM   6067 C  CD1  . ILE   B 1 137 ? 35.888 -39.297 -3.443  1.00 23.66 ?  137 ILE   B CD1  1 
ATOM   6068 H  H    . ILE   B 1 137 ? 37.154 -35.966 -1.682  1.00 19.91 ?  137 ILE   B H    1 
ATOM   6069 H  HA   . ILE   B 1 137 ? 35.874 -35.229 -3.829  1.00 20.37 ?  137 ILE   B HA   1 
ATOM   6070 H  HB   . ILE   B 1 137 ? 35.174 -37.180 -1.915  1.00 22.76 ?  137 ILE   B HB   1 
ATOM   6071 H  HG12 . ILE   B 1 137 ? 36.190 -37.596 -4.519  1.00 25.71 ?  137 ILE   B HG12 1 
ATOM   6072 H  HG13 . ILE   B 1 137 ? 37.088 -37.669 -3.213  1.00 25.71 ?  137 ILE   B HG13 1 
ATOM   6073 H  HG21 . ILE   B 1 137 ? 33.559 -37.985 -3.433  1.00 23.38 ?  137 ILE   B HG21 1 
ATOM   6074 H  HG22 . ILE   B 1 137 ? 33.188 -36.543 -2.918  1.00 23.38 ?  137 ILE   B HG22 1 
ATOM   6075 H  HG23 . ILE   B 1 137 ? 33.838 -36.726 -4.356  1.00 23.38 ?  137 ILE   B HG23 1 
ATOM   6076 H  HD11 . ILE   B 1 137 ? 36.510 -39.785 -3.998  1.00 28.40 ?  137 ILE   B HD11 1 
ATOM   6077 H  HD12 . ILE   B 1 137 ? 35.986 -39.563 -2.514  1.00 28.40 ?  137 ILE   B HD12 1 
ATOM   6078 H  HD13 . ILE   B 1 137 ? 34.984 -39.475 -3.745  1.00 28.40 ?  137 ILE   B HD13 1 
ATOM   6079 N  N    . HIS   B 1 138 ? 34.483 -34.330 -1.098  1.00 16.89 ?  138 HIS   B N    1 
ATOM   6080 C  CA   . HIS   B 1 138 ? 33.535 -33.364 -0.557  1.00 16.86 ?  138 HIS   B CA   1 
ATOM   6081 C  C    . HIS   B 1 138 ? 33.949 -31.936 -0.883  1.00 15.86 ?  138 HIS   B C    1 
ATOM   6082 O  O    . HIS   B 1 138 ? 33.100 -31.092 -1.190  1.00 16.23 ?  138 HIS   B O    1 
ATOM   6083 C  CB   . HIS   B 1 138 ? 33.421 -33.545 0.948   1.00 18.26 ?  138 HIS   B CB   1 
ATOM   6084 C  CG   . HIS   B 1 138 ? 32.495 -32.566 1.590   1.00 19.70 ?  138 HIS   B CG   1 
ATOM   6085 N  ND1  . HIS   B 1 138 ? 31.156 -32.497 1.272   1.00 21.21 ?  138 HIS   B ND1  1 
ATOM   6086 C  CD2  . HIS   B 1 138 ? 32.716 -31.599 2.510   1.00 20.34 ?  138 HIS   B CD2  1 
ATOM   6087 C  CE1  . HIS   B 1 138 ? 30.588 -31.537 1.981   1.00 21.38 ?  138 HIS   B CE1  1 
ATOM   6088 N  NE2  . HIS   B 1 138 ? 31.513 -30.976 2.739   1.00 20.54 ?  138 HIS   B NE2  1 
ATOM   6089 H  H    . HIS   B 1 138 ? 34.933 -34.769 -0.512  1.00 20.28 ?  138 HIS   B H    1 
ATOM   6090 H  HA   . HIS   B 1 138 ? 32.665 -33.527 -0.951  1.00 20.23 ?  138 HIS   B HA   1 
ATOM   6091 H  HB2  . HIS   B 1 138 ? 33.087 -34.437 1.131   1.00 21.92 ?  138 HIS   B HB2  1 
ATOM   6092 H  HB3  . HIS   B 1 138 ? 34.296 -33.431 1.346   1.00 21.92 ?  138 HIS   B HB3  1 
ATOM   6093 H  HD1  . HIS   B 1 138 ? 30.751 -33.006 0.703   1.00 25.45 ?  138 HIS   B HD1  1 
ATOM   6094 H  HD2  . HIS   B 1 138 ? 33.522 -31.401 2.921   1.00 24.41 ?  138 HIS   B HD2  1 
ATOM   6095 H  HE1  . HIS   B 1 138 ? 29.684 -31.305 1.949   1.00 25.66 ?  138 HIS   B HE1  1 
ATOM   6096 N  N    . SER   B 1 139 ? 35.245 -31.637 -0.815  1.00 15.27 ?  139 SER   B N    1 
ATOM   6097 C  CA   . SER   B 1 139 ? 35.679 -30.285 -1.131  1.00 14.63 ?  139 SER   B CA   1 
ATOM   6098 C  C    . SER   B 1 139 ? 35.337 -29.928 -2.569  1.00 13.68 ?  139 SER   B C    1 
ATOM   6099 O  O    . SER   B 1 139 ? 34.894 -28.807 -2.845  1.00 13.92 ?  139 SER   B O    1 
ATOM   6100 C  CB   . SER   B 1 139 ? 37.175 -30.138 -0.875  1.00 14.91 ?  139 SER   B CB   1 
ATOM   6101 O  OG   . SER   B 1 139 ? 37.587 -28.806 -1.135  1.00 14.65 ?  139 SER   B OG   1 
ATOM   6102 H  H    . SER   B 1 139 ? 35.873 -32.180 -0.603  1.00 18.33 ?  139 SER   B H    1 
ATOM   6103 H  HA   . SER   B 1 139 ? 35.211 -29.660 -0.562  1.00 17.56 ?  139 SER   B HA   1 
ATOM   6104 H  HB2  . SER   B 1 139 ? 37.359 -30.355 0.051   1.00 17.90 ?  139 SER   B HB2  1 
ATOM   6105 H  HB3  . SER   B 1 139 ? 37.663 -30.739 -1.463  1.00 17.90 ?  139 SER   B HB3  1 
ATOM   6106 H  HG   . SER   B 1 139 ? 38.416 -28.726 -0.986  1.00 17.58 ?  139 SER   B HG   1 
ATOM   6107 N  N    . LEU   B 1 140 ? 35.514 -30.874 -3.495  1.00 14.00 ?  140 LEU   B N    1 
ATOM   6108 C  CA   . LEU   B 1 140 ? 35.142 -30.621 -4.881  1.00 13.91 ?  140 LEU   B CA   1 
ATOM   6109 C  C    . LEU   B 1 140 ? 33.639 -30.387 -5.002  1.00 13.92 ?  140 LEU   B C    1 
ATOM   6110 O  O    . LEU   B 1 140 ? 33.200 -29.494 -5.731  1.00 14.01 ?  140 LEU   B O    1 
ATOM   6111 C  CB   . LEU   B 1 140 ? 35.606 -31.782 -5.766  1.00 13.82 ?  140 LEU   B CB   1 
ATOM   6112 C  CG   . LEU   B 1 140 ? 35.238 -31.670 -7.237  1.00 14.17 ?  140 LEU   B CG   1 
ATOM   6113 C  CD1  . LEU   B 1 140 ? 35.811 -30.393 -7.826  1.00 15.22 ?  140 LEU   B CD1  1 
ATOM   6114 C  CD2  . LEU   B 1 140 ? 35.705 -32.895 -8.000  1.00 14.92 ?  140 LEU   B CD2  1 
ATOM   6115 H  H    . LEU   B 1 140 ? 35.842 -31.654 -3.354  1.00 16.80 ?  140 LEU   B H    1 
ATOM   6116 H  HA   . LEU   B 1 140 ? 35.595 -29.822 -5.191  1.00 16.70 ?  140 LEU   B HA   1 
ATOM   6117 H  HB2  . LEU   B 1 140 ? 36.576 -31.846 -5.718  1.00 16.59 ?  140 LEU   B HB2  1 
ATOM   6118 H  HB3  . LEU   B 1 140 ? 35.213 -32.605 -5.438  1.00 16.59 ?  140 LEU   B HB3  1 
ATOM   6119 H  HG   . LEU   B 1 140 ? 34.274 -31.617 -7.314  1.00 17.00 ?  140 LEU   B HG   1 
ATOM   6120 H  HD11 . LEU   B 1 140 ? 35.707 -30.415 -8.787  1.00 18.27 ?  140 LEU   B HD11 1 
ATOM   6121 H  HD12 . LEU   B 1 140 ? 35.329 -29.630 -7.460  1.00 18.27 ?  140 LEU   B HD12 1 
ATOM   6122 H  HD13 . LEU   B 1 140 ? 36.750 -30.330 -7.593  1.00 18.27 ?  140 LEU   B HD13 1 
ATOM   6123 H  HD21 . LEU   B 1 140 ? 35.454 -32.794 -8.932  1.00 17.91 ?  140 LEU   B HD21 1 
ATOM   6124 H  HD22 . LEU   B 1 140 ? 36.664 -32.970 -7.918  1.00 17.91 ?  140 LEU   B HD22 1 
ATOM   6125 H  HD23 . LEU   B 1 140 ? 35.272 -33.675 -7.623  1.00 17.91 ?  140 LEU   B HD23 1 
ATOM   6126 N  N    . ARG   B 1 141 ? 32.839 -31.185 -4.287  1.00 14.14 ?  141 ARG   B N    1 
ATOM   6127 C  CA   . ARG   B 1 141 ? 31.390 -31.013 -4.260  1.00 15.13 ?  141 ARG   B CA   1 
ATOM   6128 C  C    . ARG   B 1 141 ? 31.014 -29.601 -3.834  1.00 14.62 ?  141 ARG   B C    1 
ATOM   6129 O  O    . ARG   B 1 141 ? 30.210 -28.924 -4.493  1.00 14.68 ?  141 ARG   B O    1 
ATOM   6130 C  CB   . ARG   B 1 141 ? 30.815 -32.035 -3.269  1.00 16.43 ?  141 ARG   B CB   1 
ATOM   6131 C  CG   . ARG   B 1 141 ? 29.346 -31.926 -2.958  1.00 18.35 ?  141 ARG   B CG   1 
ATOM   6132 C  CD   . ARG   B 1 141 ? 28.557 -32.556 -4.033  1.00 20.27 ?  141 ARG   B CD   1 
ATOM   6133 N  NE   . ARG   B 1 141 ? 28.278 -31.635 -5.122  1.00 20.27 ?  141 ARG   B NE   1 
ATOM   6134 C  CZ   . ARG   B 1 141 ? 28.254 -31.972 -6.405  1.00 19.41 ?  141 ARG   B CZ   1 
ATOM   6135 N  NH1  . ARG   B 1 141 ? 28.698 -33.148 -6.822  1.00 19.30 ?  141 ARG   B NH1  1 
ATOM   6136 N  NH2  . ARG   B 1 141 ? 27.761 -31.110 -7.290  1.00 20.55 ?  141 ARG   B NH2  1 
ATOM   6137 H  H    . ARG   B 1 141 ? 33.126 -31.840 -3.808  1.00 16.98 ?  141 ARG   B H    1 
ATOM   6138 H  HA   . ARG   B 1 141 ? 31.023 -31.183 -5.137  1.00 18.17 ?  141 ARG   B HA   1 
ATOM   6139 H  HB2  . ARG   B 1 141 ? 30.982 -32.923 -3.621  1.00 19.72 ?  141 ARG   B HB2  1 
ATOM   6140 H  HB3  . ARG   B 1 141 ? 31.291 -31.938 -2.429  1.00 19.72 ?  141 ARG   B HB3  1 
ATOM   6141 H  HG2  . ARG   B 1 141 ? 29.166 -32.382 -2.125  1.00 22.03 ?  141 ARG   B HG2  1 
ATOM   6142 H  HG3  . ARG   B 1 141 ? 29.089 -30.989 -2.889  1.00 22.03 ?  141 ARG   B HG3  1 
ATOM   6143 H  HD2  . ARG   B 1 141 ? 29.053 -33.317 -4.383  1.00 24.33 ?  141 ARG   B HD2  1 
ATOM   6144 H  HD3  . ARG   B 1 141 ? 27.718 -32.859 -3.666  1.00 24.33 ?  141 ARG   B HD3  1 
ATOM   6145 H  HE   . ARG   B 1 141 ? 28.104 -30.818 -4.919  1.00 24.33 ?  141 ARG   B HE   1 
ATOM   6146 H  HH11 . ARG   B 1 141 ? 29.007 -33.722 -6.262  1.00 23.16 ?  141 ARG   B HH11 1 
ATOM   6147 H  HH12 . ARG   B 1 141 ? 28.678 -33.338 -7.659  1.00 23.16 ?  141 ARG   B HH12 1 
ATOM   6148 H  HH21 . ARG   B 1 141 ? 27.476 -30.341 -7.031  1.00 24.66 ?  141 ARG   B HH21 1 
ATOM   6149 H  HH22 . ARG   B 1 141 ? 27.758 -31.308 -8.127  1.00 24.66 ?  141 ARG   B HH22 1 
ATOM   6150 N  N    . VAL   B 1 142 ? 31.564 -29.154 -2.708  1.00 14.29 ?  142 VAL   B N    1 
ATOM   6151 C  CA   . VAL   B 1 142 ? 31.239 -27.821 -2.217  1.00 14.17 ?  142 VAL   B CA   1 
ATOM   6152 C  C    . VAL   B 1 142 ? 31.709 -26.761 -3.205  1.00 14.10 ?  142 VAL   B C    1 
ATOM   6153 O  O    . VAL   B 1 142 ? 31.012 -25.772 -3.454  1.00 14.18 ?  142 VAL   B O    1 
ATOM   6154 C  CB   . VAL   B 1 142 ? 31.795 -27.594 -0.797  1.00 14.75 ?  142 VAL   B CB   1 
ATOM   6155 C  CG1  . VAL   B 1 142 ? 31.468 -26.172 -0.317  1.00 14.44 ?  142 VAL   B CG1  1 
ATOM   6156 C  CG2  . VAL   B 1 142 ? 31.242 -28.625 0.167   1.00 15.75 ?  142 VAL   B CG2  1 
ATOM   6157 H  H    . VAL   B 1 142 ? 32.122 -29.589 -2.220  1.00 17.16 ?  142 VAL   B H    1 
ATOM   6158 H  HA   . VAL   B 1 142 ? 30.278 -27.744 -2.157  1.00 17.01 ?  142 VAL   B HA   1 
ATOM   6159 H  HB   . VAL   B 1 142 ? 32.762 -27.688 -0.814  1.00 17.71 ?  142 VAL   B HB   1 
ATOM   6160 H  HG11 . VAL   B 1 142 ? 31.658 -26.110 0.632   1.00 17.34 ?  142 VAL   B HG11 1 
ATOM   6161 H  HG12 . VAL   B 1 142 ? 32.021 -25.539 -0.804  1.00 17.34 ?  142 VAL   B HG12 1 
ATOM   6162 H  HG13 . VAL   B 1 142 ? 30.532 -25.993 -0.482  1.00 17.34 ?  142 VAL   B HG13 1 
ATOM   6163 H  HG21 . VAL   B 1 142 ? 31.577 -28.432 1.057   1.00 18.91 ?  142 VAL   B HG21 1 
ATOM   6164 H  HG22 . VAL   B 1 142 ? 30.277 -28.577 0.155   1.00 18.91 ?  142 VAL   B HG22 1 
ATOM   6165 H  HG23 . VAL   B 1 142 ? 31.538 -29.505 -0.114  1.00 18.91 ?  142 VAL   B HG23 1 
ATOM   6166 N  N    . CYS   B 1 143 ? 32.886 -26.960 -3.799  1.00 13.05 ?  143 CYS   B N    1 
ATOM   6167 C  CA   . CYS   B 1 143 ? 33.371 -26.018 -4.803  1.00 13.17 ?  143 CYS   B CA   1 
ATOM   6168 C  C    . CYS   B 1 143 ? 32.364 -25.872 -5.938  1.00 13.01 ?  143 CYS   B C    1 
ATOM   6169 O  O    . CYS   B 1 143 ? 31.950 -24.763 -6.288  1.00 13.45 ?  143 CYS   B O    1 
ATOM   6170 C  CB   . CYS   B 1 143 ? 34.721 -26.505 -5.340  1.00 13.58 ?  143 CYS   B CB   1 
ATOM   6171 S  SG   . CYS   B 1 143 ? 35.476 -25.398 -6.566  1.00 13.75 ?  143 CYS   B SG   1 
ATOM   6172 H  H    . CYS   B 1 143 ? 33.414 -27.622 -3.642  1.00 15.67 ?  143 CYS   B H    1 
ATOM   6173 H  HA   . CYS   B 1 143 ? 33.501 -25.149 -4.398  1.00 15.80 ?  143 CYS   B HA   1 
ATOM   6174 H  HB2  . CYS   B 1 143 ? 35.348 -26.589 -4.603  1.00 16.30 ?  143 CYS   B HB2  1 
ATOM   6175 H  HB3  . CYS   B 1 143 ? 34.602 -27.368 -5.761  1.00 16.30 ?  143 CYS   B HB3  1 
ATOM   6176 H  HG   . CYS   B 1 143 ? 36.544 -25.838 -6.897  1.00 16.51 ?  143 CYS   B HG   1 
ATOM   6177 N  N    . VAL   B 1 144 ? 31.964 -26.994 -6.537  1.00 13.89 ?  144 VAL   B N    1 
ATOM   6178 C  CA   . VAL   B 1 144 ? 31.051 -26.928 -7.673  1.00 15.01 ?  144 VAL   B CA   1 
ATOM   6179 C  C    . VAL   B 1 144 ? 29.708 -26.320 -7.292  1.00 14.63 ?  144 VAL   B C    1 
ATOM   6180 O  O    . VAL   B 1 144 ? 29.088 -25.617 -8.099  1.00 15.68 ?  144 VAL   B O    1 
ATOM   6181 C  CB   . VAL   B 1 144 ? 30.897 -28.338 -8.254  1.00 17.58 ?  144 VAL   B CB   1 
ATOM   6182 C  CG1  . VAL   B 1 144 ? 29.612 -28.481 -9.066  1.00 20.23 ?  144 VAL   B CG1  1 
ATOM   6183 C  CG2  . VAL   B 1 144 ? 32.141 -28.730 -9.061  1.00 17.96 ?  144 VAL   B CG2  1 
ATOM   6184 H  H    . VAL   B 1 144 ? 32.204 -27.789 -6.312  1.00 16.67 ?  144 VAL   B H    1 
ATOM   6185 H  HA   . VAL   B 1 144 ? 31.441 -26.369 -8.362  1.00 18.02 ?  144 VAL   B HA   1 
ATOM   6186 H  HB   . VAL   B 1 144 ? 30.839 -28.966 -7.516  1.00 21.11 ?  144 VAL   B HB   1 
ATOM   6187 H  HG11 . VAL   B 1 144 ? 29.686 -29.274 -9.628  1.00 24.29 ?  144 VAL   B HG11 1 
ATOM   6188 H  HG12 . VAL   B 1 144 ? 28.865 -28.583 -8.459  1.00 24.29 ?  144 VAL   B HG12 1 
ATOM   6189 H  HG13 . VAL   B 1 144 ? 29.498 -27.698 -9.620  1.00 24.29 ?  144 VAL   B HG13 1 
ATOM   6190 H  HG21 . VAL   B 1 144 ? 32.023 -29.629 -9.412  1.00 21.55 ?  144 VAL   B HG21 1 
ATOM   6191 H  HG22 . VAL   B 1 144 ? 32.253 -28.104 -9.794  1.00 21.55 ?  144 VAL   B HG22 1 
ATOM   6192 H  HG23 . VAL   B 1 144 ? 32.918 -28.704 -8.481  1.00 21.55 ?  144 VAL   B HG23 1 
ATOM   6193 N  N    . ASP   B 1 145 ? 29.254 -26.555 -6.068  1.00 14.65 ?  145 ASP   B N    1 
ATOM   6194 C  CA   . ASP   B 1 145 ? 27.945 -26.098 -5.628  1.00 15.18 ?  145 ASP   B CA   1 
ATOM   6195 C  C    . ASP   B 1 145 ? 27.972 -24.676 -5.089  1.00 14.99 ?  145 ASP   B C    1 
ATOM   6196 O  O    . ASP   B 1 145 ? 26.912 -24.139 -4.755  1.00 17.14 ?  145 ASP   B O    1 
ATOM   6197 C  CB   . ASP   B 1 145 ? 27.386 -27.024 -4.540  1.00 16.88 ?  145 ASP   B CB   1 
ATOM   6198 C  CG   . ASP   B 1 145 ? 26.988 -28.388 -5.060  1.00 18.51 ?  145 ASP   B CG   1 
ATOM   6199 O  OD1  . ASP   B 1 145 ? 26.871 -28.570 -6.290  1.00 18.92 ?  145 ASP   B OD1  1 
ATOM   6200 O  OD2  . ASP   B 1 145 ? 26.791 -29.278 -4.213  1.00 20.66 -1 145 ASP   B OD2  1 
ATOM   6201 H  H    . ASP   B 1 145 ? 29.702 -26.972 -5.463  1.00 17.59 ?  145 ASP   B H    1 
ATOM   6202 H  HA   . ASP   B 1 145 ? 27.344 -26.101 -6.382  1.00 18.23 ?  145 ASP   B HA   1 
ATOM   6203 H  HB2  . ASP   B 1 145 ? 28.057 -27.149 -3.860  1.00 20.27 ?  145 ASP   B HB2  1 
ATOM   6204 H  HB3  . ASP   B 1 145 ? 26.594 -26.608 -4.163  1.00 20.27 ?  145 ASP   B HB3  1 
ATOM   6205 N  N    . THR   B 1 146 ? 29.148 -24.057 -4.989  1.00 13.66 ?  146 THR   B N    1 
ATOM   6206 C  CA   . THR   B 1 146 ? 29.292 -22.738 -4.380  1.00 13.36 ?  146 THR   B CA   1 
ATOM   6207 C  C    . THR   B 1 146 ? 29.919 -21.710 -5.304  1.00 13.09 ?  146 THR   B C    1 
ATOM   6208 O  O    . THR   B 1 146 ? 29.464 -20.554 -5.352  1.00 13.02 ?  146 THR   B O    1 
ATOM   6209 C  CB   . THR   B 1 146 ? 30.124 -22.846 -3.094  1.00 13.77 ?  146 THR   B CB   1 
ATOM   6210 O  OG1  . THR   B 1 146 ? 29.548 -23.842 -2.234  1.00 13.93 ?  146 THR   B OG1  1 
ATOM   6211 C  CG2  . THR   B 1 146 ? 30.206 -21.507 -2.373  1.00 13.61 ?  146 THR   B CG2  1 
ATOM   6212 H  H    . THR   B 1 146 ? 29.902 -24.377 -5.277  1.00 16.39 ?  146 THR   B H    1 
ATOM   6213 H  HA   . THR   B 1 146 ? 28.422 -22.410 -4.132  1.00 16.04 ?  146 THR   B HA   1 
ATOM   6214 H  HB   . THR   B 1 146 ? 31.035 -23.105 -3.324  1.00 16.54 ?  146 THR   B HB   1 
ATOM   6215 H  HG1  . THR   B 1 146 ? 29.591 -24.601 -2.614  1.00 16.72 ?  146 THR   B HG1  1 
ATOM   6216 H  HG21 . THR   B 1 146 ? 30.566 -21.633 -1.482  1.00 16.34 ?  146 THR   B HG21 1 
ATOM   6217 H  HG22 . THR   B 1 146 ? 30.790 -20.902 -2.863  1.00 16.34 ?  146 THR   B HG22 1 
ATOM   6218 H  HG23 . THR   B 1 146 ? 29.326 -21.115 -2.309  1.00 16.34 ?  146 THR   B HG23 1 
ATOM   6219 N  N    . VAL   B 1 147 ? 30.981 -22.082 -6.009  1.00 13.07 ?  147 VAL   B N    1 
ATOM   6220 C  CA   . VAL   B 1 147 ? 31.704 -21.136 -6.846  1.00 12.77 ?  147 VAL   B CA   1 
ATOM   6221 C  C    . VAL   B 1 147 ? 30.967 -20.998 -8.167  1.00 12.89 ?  147 VAL   B C    1 
ATOM   6222 O  O    . VAL   B 1 147 ? 30.584 -22.000 -8.791  1.00 13.81 ?  147 VAL   B O    1 
ATOM   6223 C  CB   . VAL   B 1 147 ? 33.157 -21.591 -7.055  1.00 12.37 ?  147 VAL   B CB   1 
ATOM   6224 C  CG1  . VAL   B 1 147 ? 33.914 -20.557 -7.868  1.00 12.82 ?  147 VAL   B CG1  1 
ATOM   6225 C  CG2  . VAL   B 1 147 ? 33.839 -21.801 -5.718  1.00 12.89 ?  147 VAL   B CG2  1 
ATOM   6226 H  H    . VAL   B 1 147 ? 31.301 -22.883 -6.029  1.00 15.70 ?  147 VAL   B H    1 
ATOM   6227 H  HA   . VAL   B 1 147 ? 31.717 -20.270 -6.412  1.00 15.33 ?  147 VAL   B HA   1 
ATOM   6228 H  HB   . VAL   B 1 147 ? 33.169 -22.431 -7.543  1.00 14.85 ?  147 VAL   B HB   1 
ATOM   6229 H  HG11 . VAL   B 1 147 ? 34.858 -20.780 -7.862  1.00 15.39 ?  147 VAL   B HG11 1 
ATOM   6230 H  HG12 . VAL   B 1 147 ? 33.580 -20.557 -8.777  1.00 15.39 ?  147 VAL   B HG12 1 
ATOM   6231 H  HG13 . VAL   B 1 147 ? 33.780 -19.682 -7.466  1.00 15.39 ?  147 VAL   B HG13 1 
ATOM   6232 H  HG21 . VAL   B 1 147 ? 34.777 -21.993 -5.868  1.00 15.47 ?  147 VAL   B HG21 1 
ATOM   6233 H  HG22 . VAL   B 1 147 ? 33.747 -20.991 -5.190  1.00 15.47 ?  147 VAL   B HG22 1 
ATOM   6234 H  HG23 . VAL   B 1 147 ? 33.416 -22.543 -5.260  1.00 15.47 ?  147 VAL   B HG23 1 
ATOM   6235 N  N    . ARG   B 1 148 ? 30.758 -19.749 -8.586  1.00 12.81 ?  148 ARG   B N    1 
ATOM   6236 C  CA   . ARG   B 1 148 ? 30.127 -19.429 -9.855  1.00 12.70 ?  148 ARG   B CA   1 
ATOM   6237 C  C    . ARG   B 1 148 ? 31.076 -18.739 -10.823 1.00 12.85 ?  148 ARG   B C    1 
ATOM   6238 O  O    . ARG   B 1 148 ? 30.788 -18.704 -12.020 1.00 13.89 ?  148 ARG   B O    1 
ATOM   6239 C  CB   . ARG   B 1 148 ? 28.888 -18.551 -9.624  1.00 13.21 ?  148 ARG   B CB   1 
ATOM   6240 C  CG   . ARG   B 1 148 ? 27.816 -19.274 -8.822  1.00 14.08 ?  148 ARG   B CG   1 
ATOM   6241 C  CD   . ARG   B 1 148 ? 26.596 -18.406 -8.509  1.00 14.96 ?  148 ARG   B CD   1 
ATOM   6242 N  NE   . ARG   B 1 148 ? 26.962 -17.200 -7.775  1.00 14.88 ?  148 ARG   B NE   1 
ATOM   6243 C  CZ   . ARG   B 1 148 ? 27.265 -17.164 -6.483  1.00 13.83 ?  148 ARG   B CZ   1 
ATOM   6244 N  NH1  . ARG   B 1 148 ? 27.224 -18.254 -5.729  1.00 13.73 ?  148 ARG   B NH1  1 
ATOM   6245 N  NH2  . ARG   B 1 148 ? 27.653 -16.014 -5.939  1.00 14.01 ?  148 ARG   B NH2  1 
ATOM   6246 H  H    . ARG   B 1 148 ? 30.989 -19.047 -8.130  1.00 15.38 ?  148 ARG   B H    1 
ATOM   6247 H  HA   . ARG   B 1 148 ? 29.835 -20.251 -10.266 1.00 15.24 ?  148 ARG   B HA   1 
ATOM   6248 H  HB2  . ARG   B 1 148 ? 29.150 -17.756 -9.132  1.00 15.86 ?  148 ARG   B HB2  1 
ATOM   6249 H  HB3  . ARG   B 1 148 ? 28.514 -18.305 -10.482 1.00 15.86 ?  148 ARG   B HB3  1 
ATOM   6250 H  HG2  . ARG   B 1 148 ? 27.513 -20.043 -9.331  1.00 16.90 ?  148 ARG   B HG2  1 
ATOM   6251 H  HG3  . ARG   B 1 148 ? 28.198 -19.568 -7.980  1.00 16.90 ?  148 ARG   B HG3  1 
ATOM   6252 H  HD2  . ARG   B 1 148 ? 26.172 -18.139 -9.339  1.00 17.96 ?  148 ARG   B HD2  1 
ATOM   6253 H  HD3  . ARG   B 1 148 ? 25.973 -18.917 -7.965  1.00 17.96 ?  148 ARG   B HD3  1 
ATOM   6254 H  HE   . ARG   B 1 148 ? 26.988 -16.461 -8.210  1.00 17.86 ?  148 ARG   B HE   1 
ATOM   6255 H  HH11 . ARG   B 1 148 ? 26.977 -19.006 -6.064  1.00 16.48 ?  148 ARG   B HH11 1 
ATOM   6256 H  HH12 . ARG   B 1 148 ? 27.422 -18.205 -4.891  1.00 16.48 ?  148 ARG   B HH12 1 
ATOM   6257 H  HH21 . ARG   B 1 148 ? 27.690 -15.303 -6.421  1.00 16.82 ?  148 ARG   B HH21 1 
ATOM   6258 H  HH22 . ARG   B 1 148 ? 27.852 -15.977 -5.104  1.00 16.82 ?  148 ARG   B HH22 1 
ATOM   6259 N  N    . THR   B 1 149 ? 32.184 -18.190 -10.335 1.00 12.88 ?  149 THR   B N    1 
ATOM   6260 C  CA   . THR   B 1 149 ? 33.223 -17.627 -11.186 1.00 12.71 ?  149 THR   B CA   1 
ATOM   6261 C  C    . THR   B 1 149 ? 34.106 -18.758 -11.712 1.00 12.32 ?  149 THR   B C    1 
ATOM   6262 O  O    . THR   B 1 149 ? 33.913 -19.933 -11.390 1.00 13.42 ?  149 THR   B O    1 
ATOM   6263 C  CB   . THR   B 1 149 ? 34.002 -16.574 -10.405 1.00 12.86 ?  149 THR   B CB   1 
ATOM   6264 O  OG1  . THR   B 1 149 ? 34.460 -17.177 -9.192  1.00 12.52 ?  149 THR   B OG1  1 
ATOM   6265 C  CG2  . THR   B 1 149 ? 33.108 -15.367 -10.103 1.00 13.49 ?  149 THR   B CG2  1 
ATOM   6266 H  H    . THR   B 1 149 ? 32.353 -18.116 -9.494  1.00 15.46 ?  149 THR   B H    1 
ATOM   6267 H  HA   . THR   B 1 149 ? 32.807 -17.187 -11.946 1.00 15.26 ?  149 THR   B HA   1 
ATOM   6268 H  HB   . THR   B 1 149 ? 34.762 -16.280 -10.925 1.00 15.44 ?  149 THR   B HB   1 
ATOM   6269 H  HG1  . THR   B 1 149 ? 34.879 -16.609 -8.731  1.00 15.04 ?  149 THR   B HG1  1 
ATOM   6270 H  HG21 . THR   B 1 149 ? 33.616 -14.694 -9.620  1.00 16.20 ?  149 THR   B HG21 1 
ATOM   6271 H  HG22 . THR   B 1 149 ? 32.784 -14.978 -10.931 1.00 16.20 ?  149 THR   B HG22 1 
ATOM   6272 H  HG23 . THR   B 1 149 ? 32.351 -15.637 -9.563  1.00 16.20 ?  149 THR   B HG23 1 
ATOM   6273 N  N    . ASN   B 1 150 ? 35.069 -18.427 -12.559 1.00 12.30 ?  150 ASN   B N    1 
ATOM   6274 C  CA   . ASN   B 1 150 ? 35.830 -19.451 -13.265 1.00 13.11 ?  150 ASN   B CA   1 
ATOM   6275 C  C    . ASN   B 1 150 ? 37.000 -19.905 -12.400 1.00 12.87 ?  150 ASN   B C    1 
ATOM   6276 O  O    . ASN   B 1 150 ? 37.940 -19.143 -12.156 1.00 13.42 ?  150 ASN   B O    1 
ATOM   6277 C  CB   . ASN   B 1 150 ? 36.301 -18.924 -14.613 1.00 15.13 ?  150 ASN   B CB   1 
ATOM   6278 C  CG   . ASN   B 1 150 ? 35.157 -18.696 -15.561 1.00 18.09 ?  150 ASN   B CG   1 
ATOM   6279 O  OD1  . ASN   B 1 150 ? 34.248 -19.515 -15.643 1.00 19.06 ?  150 ASN   B OD1  1 
ATOM   6280 N  ND2  . ASN   B 1 150 ? 35.175 -17.573 -16.259 1.00 20.25 ?  150 ASN   B ND2  1 
ATOM   6281 H  H    . ASN   B 1 150 ? 35.305 -17.619 -12.742 1.00 14.77 ?  150 ASN   B H    1 
ATOM   6282 H  HA   . ASN   B 1 150 ? 35.248 -20.217 -13.427 1.00 15.74 ?  150 ASN   B HA   1 
ATOM   6283 H  HB2  . ASN   B 1 150 ? 36.756 -18.078 -14.478 1.00 18.16 ?  150 ASN   B HB2  1 
ATOM   6284 H  HB3  . ASN   B 1 150 ? 36.905 -19.570 -15.010 1.00 18.16 ?  150 ASN   B HB3  1 
ATOM   6285 H  HD21 . ASN   B 1 150 ? 34.545 -17.397 -16.818 1.00 24.30 ?  150 ASN   B HD21 1 
ATOM   6286 H  HD22 . ASN   B 1 150 ? 35.828 -17.014 -16.166 1.00 24.30 ?  150 ASN   B HD22 1 
ATOM   6287 N  N    . VAL   B 1 151 ? 36.954 -21.152 -11.943 1.00 12.19 ?  151 VAL   B N    1 
ATOM   6288 C  CA   . VAL   B 1 151 ? 37.975 -21.689 -11.057 1.00 12.36 ?  151 VAL   B CA   1 
ATOM   6289 C  C    . VAL   B 1 151 ? 38.675 -22.859 -11.740 1.00 11.87 ?  151 VAL   B C    1 
ATOM   6290 O  O    . VAL   B 1 151 ? 38.028 -23.789 -12.242 1.00 13.28 ?  151 VAL   B O    1 
ATOM   6291 C  CB   . VAL   B 1 151 ? 37.415 -22.034 -9.661  1.00 13.21 ?  151 VAL   B CB   1 
ATOM   6292 C  CG1  . VAL   B 1 151 ? 36.237 -23.024 -9.739  1.00 14.19 ?  151 VAL   B CG1  1 
ATOM   6293 C  CG2  . VAL   B 1 151 ? 38.519 -22.551 -8.756  1.00 13.96 ?  151 VAL   B CG2  1 
ATOM   6294 H  H    . VAL   B 1 151 ? 36.328 -21.713 -12.138 1.00 14.64 ?  151 VAL   B H    1 
ATOM   6295 H  HA   . VAL   B 1 151 ? 38.642 -20.996 -10.922 1.00 14.84 ?  151 VAL   B HA   1 
ATOM   6296 H  HB   . VAL   B 1 151 ? 37.075 -21.218 -9.259  1.00 15.86 ?  151 VAL   B HB   1 
ATOM   6297 H  HG11 . VAL   B 1 151 ? 35.922 -23.219 -8.841  1.00 17.03 ?  151 VAL   B HG11 1 
ATOM   6298 H  HG12 . VAL   B 1 151 ? 35.517 -22.625 -10.258 1.00 17.03 ?  151 VAL   B HG12 1 
ATOM   6299 H  HG13 . VAL   B 1 151 ? 36.534 -23.842 -10.168 1.00 17.03 ?  151 VAL   B HG13 1 
ATOM   6300 H  HG21 . VAL   B 1 151 ? 38.173 -22.628 -7.851  1.00 16.76 ?  151 VAL   B HG21 1 
ATOM   6301 H  HG22 . VAL   B 1 151 ? 38.807 -23.422 -9.072  1.00 16.76 ?  151 VAL   B HG22 1 
ATOM   6302 H  HG23 . VAL   B 1 151 ? 39.261 -21.928 -8.774  1.00 16.76 ?  151 VAL   B HG23 1 
ATOM   6303 N  N    . TYR   B 1 152 ? 40.005 -22.775 -11.769 1.00 11.66 ?  152 TYR   B N    1 
ATOM   6304 C  CA   . TYR   B 1 152 ? 40.904 -23.761 -12.350 1.00 12.13 ?  152 TYR   B CA   1 
ATOM   6305 C  C    . TYR   B 1 152 ? 41.623 -24.447 -11.190 1.00 11.49 ?  152 TYR   B C    1 
ATOM   6306 O  O    . TYR   B 1 152 ? 42.473 -23.837 -10.534 1.00 12.11 ?  152 TYR   B O    1 
ATOM   6307 C  CB   . TYR   B 1 152 ? 41.875 -23.053 -13.298 1.00 13.07 ?  152 TYR   B CB   1 
ATOM   6308 C  CG   . TYR   B 1 152 ? 41.194 -22.580 -14.558 1.00 13.55 ?  152 TYR   B CG   1 
ATOM   6309 C  CD1  . TYR   B 1 152 ? 40.559 -21.343 -14.615 1.00 14.23 ?  152 TYR   B CD1  1 
ATOM   6310 C  CD2  . TYR   B 1 152 ? 41.171 -23.382 -15.688 1.00 14.68 ?  152 TYR   B CD2  1 
ATOM   6311 C  CE1  . TYR   B 1 152 ? 39.922 -20.925 -15.769 1.00 15.61 ?  152 TYR   B CE1  1 
ATOM   6312 C  CE2  . TYR   B 1 152 ? 40.542 -22.976 -16.841 1.00 15.82 ?  152 TYR   B CE2  1 
ATOM   6313 C  CZ   . TYR   B 1 152 ? 39.919 -21.745 -16.880 1.00 15.81 ?  152 TYR   B CZ   1 
ATOM   6314 O  OH   . TYR   B 1 152 ? 39.293 -21.347 -18.034 1.00 18.35 ?  152 TYR   B OH   1 
ATOM   6315 H  H    . TYR   B 1 152 ? 40.437 -22.102 -11.434 1.00 14.00 ?  152 TYR   B H    1 
ATOM   6316 H  HA   . TYR   B 1 152 ? 40.393 -24.419 -12.846 1.00 14.57 ?  152 TYR   B HA   1 
ATOM   6317 H  HB2  . TYR   B 1 152 ? 42.250 -22.281 -12.844 1.00 15.70 ?  152 TYR   B HB2  1 
ATOM   6318 H  HB3  . TYR   B 1 152 ? 42.581 -23.668 -13.545 1.00 15.70 ?  152 TYR   B HB3  1 
ATOM   6319 H  HD1  . TYR   B 1 152 ? 40.557 -20.792 -13.863 1.00 17.09 ?  152 TYR   B HD1  1 
ATOM   6320 H  HD2  . TYR   B 1 152 ? 41.587 -24.215 -15.663 1.00 17.62 ?  152 TYR   B HD2  1 
ATOM   6321 H  HE1  . TYR   B 1 152 ? 39.500 -20.095 -15.801 1.00 18.74 ?  152 TYR   B HE1  1 
ATOM   6322 H  HE2  . TYR   B 1 152 ? 40.540 -23.529 -17.589 1.00 19.00 ?  152 TYR   B HE2  1 
ATOM   6323 H  HH   . TYR   B 1 152 ? 39.374 -21.944 -18.627 1.00 22.03 ?  152 TYR   B HH   1 
ATOM   6324 N  N    . LEU   B 1 153 ? 41.258 -25.705 -10.925 1.00 11.88 ?  153 LEU   B N    1 
ATOM   6325 C  CA   . LEU   B 1 153 ? 41.766 -26.460 -9.787  1.00 11.55 ?  153 LEU   B CA   1 
ATOM   6326 C  C    . LEU   B 1 153 ? 42.998 -27.257 -10.189 1.00 11.48 ?  153 LEU   B C    1 
ATOM   6327 O  O    . LEU   B 1 153 ? 42.975 -27.991 -11.180 1.00 13.20 ?  153 LEU   B O    1 
ATOM   6328 C  CB   . LEU   B 1 153 ? 40.692 -27.427 -9.281  1.00 12.11 ?  153 LEU   B CB   1 
ATOM   6329 C  CG   . LEU   B 1 153 ? 39.442 -26.766 -8.701  1.00 12.55 ?  153 LEU   B CG   1 
ATOM   6330 C  CD1  . LEU   B 1 153 ? 38.334 -27.810 -8.547  1.00 13.20 ?  153 LEU   B CD1  1 
ATOM   6331 C  CD2  . LEU   B 1 153 ? 39.734 -26.107 -7.362  1.00 13.27 ?  153 LEU   B CD2  1 
ATOM   6332 H  H    . LEU   B 1 153 ? 40.689 -26.148 -11.405 1.00 14.26 ?  153 LEU   B H    1 
ATOM   6333 H  HA   . LEU   B 1 153 ? 41.994 -25.850 -9.075  1.00 13.87 ?  153 LEU   B HA   1 
ATOM   6334 H  HB2  . LEU   B 1 153 ? 40.404 -27.988 -10.017 1.00 14.53 ?  153 LEU   B HB2  1 
ATOM   6335 H  HB3  . LEU   B 1 153 ? 41.075 -27.977 -8.581  1.00 14.53 ?  153 LEU   B HB3  1 
ATOM   6336 H  HG   . LEU   B 1 153 ? 39.125 -26.076 -9.310  1.00 15.06 ?  153 LEU   B HG   1 
ATOM   6337 H  HD11 . LEU   B 1 153 ? 37.531 -27.372 -8.219  1.00 15.85 ?  153 LEU   B HD11 1 
ATOM   6338 H  HD12 . LEU   B 1 153 ? 38.162 -28.213 -9.409  1.00 15.85 ?  153 LEU   B HD12 1 
ATOM   6339 H  HD13 . LEU   B 1 153 ? 38.626 -28.482 -7.913  1.00 15.85 ?  153 LEU   B HD13 1 
ATOM   6340 H  HD21 . LEU   B 1 153 ? 38.917 -25.736 -6.999  1.00 15.94 ?  153 LEU   B HD21 1 
ATOM   6341 H  HD22 . LEU   B 1 153 ? 40.094 -26.775 -6.755  1.00 15.94 ?  153 LEU   B HD22 1 
ATOM   6342 H  HD23 . LEU   B 1 153 ? 40.389 -25.400 -7.493  1.00 15.94 ?  153 LEU   B HD23 1 
ATOM   6343 N  N    . ALA   B 1 154 ? 44.055 -27.145 -9.394  1.00 11.78 ?  154 ALA   B N    1 
ATOM   6344 C  CA   . ALA   B 1 154 ? 45.285 -27.898 -9.589  1.00 12.76 ?  154 ALA   B CA   1 
ATOM   6345 C  C    . ALA   B 1 154 ? 45.356 -28.983 -8.523  1.00 13.36 ?  154 ALA   B C    1 
ATOM   6346 O  O    . ALA   B 1 154 ? 45.312 -28.693 -7.321  1.00 15.15 ?  154 ALA   B O    1 
ATOM   6347 C  CB   . ALA   B 1 154 ? 46.503 -26.978 -9.514  1.00 13.98 ?  154 ALA   B CB   1 
ATOM   6348 H  H    . ALA   B 1 154 ? 44.075 -26.618 -8.710  1.00 14.15 ?  154 ALA   B H    1 
ATOM   6349 H  HA   . ALA   B 1 154 ? 45.269 -28.318 -10.459 1.00 15.32 ?  154 ALA   B HA   1 
ATOM   6350 H  HB1  . ALA   B 1 154 ? 47.304 -27.505 -9.647  1.00 16.78 ?  154 ALA   B HB1  1 
ATOM   6351 H  HB2  . ALA   B 1 154 ? 46.433 -26.301 -10.208 1.00 16.78 ?  154 ALA   B HB2  1 
ATOM   6352 H  HB3  . ALA   B 1 154 ? 46.527 -26.551 -8.642  1.00 16.78 ?  154 ALA   B HB3  1 
ATOM   6353 N  N    . VAL   B 1 155 ? 45.457 -30.228 -8.965  1.00 13.26 ?  155 VAL   B N    1 
ATOM   6354 C  CA   . VAL   B 1 155 ? 45.554 -31.380 -8.077  1.00 13.31 ?  155 VAL   B CA   1 
ATOM   6355 C  C    . VAL   B 1 155 ? 46.885 -32.063 -8.360  1.00 13.38 ?  155 VAL   B C    1 
ATOM   6356 O  O    . VAL   B 1 155 ? 47.123 -32.540 -9.479  1.00 15.38 ?  155 VAL   B O    1 
ATOM   6357 C  CB   . VAL   B 1 155 ? 44.387 -32.362 -8.270  1.00 14.88 ?  155 VAL   B CB   1 
ATOM   6358 C  CG1  . VAL   B 1 155 ? 44.570 -33.567 -7.365  1.00 14.94 ?  155 VAL   B CG1  1 
ATOM   6359 C  CG2  . VAL   B 1 155 ? 43.054 -31.668 -7.992  1.00 16.18 ?  155 VAL   B CG2  1 
ATOM   6360 H  H    . VAL   B 1 155 ? 45.479 -30.439 -9.800  1.00 15.92 ?  155 VAL   B H    1 
ATOM   6361 H  HA   . VAL   B 1 155 ? 45.547 -31.083 -7.155  1.00 15.98 ?  155 VAL   B HA   1 
ATOM   6362 H  HB   . VAL   B 1 155 ? 44.375 -32.672 -9.189  1.00 17.86 ?  155 VAL   B HB   1 
ATOM   6363 H  HG11 . VAL   B 1 155 ? 43.733 -34.062 -7.322  1.00 17.94 ?  155 VAL   B HG11 1 
ATOM   6364 H  HG12 . VAL   B 1 155 ? 45.265 -34.138 -7.730  1.00 17.94 ?  155 VAL   B HG12 1 
ATOM   6365 H  HG13 . VAL   B 1 155 ? 44.816 -33.266 -6.478  1.00 17.94 ?  155 VAL   B HG13 1 
ATOM   6366 H  HG21 . VAL   B 1 155 ? 42.333 -32.311 -8.089  1.00 19.43 ?  155 VAL   B HG21 1 
ATOM   6367 H  HG22 . VAL   B 1 155 ? 43.062 -31.315 -7.089  1.00 19.43 ?  155 VAL   B HG22 1 
ATOM   6368 H  HG23 . VAL   B 1 155 ? 42.935 -30.944 -8.628  1.00 19.43 ?  155 VAL   B HG23 1 
ATOM   6369 N  N    . PHE   B 1 156 ? 47.756 -32.105 -7.349  1.00 14.11 ?  156 PHE   B N    1 
ATOM   6370 C  CA   . PHE   B 1 156 ? 49.134 -32.558 -7.559  1.00 15.14 ?  156 PHE   B CA   1 
ATOM   6371 C  C    . PHE   B 1 156 ? 49.234 -34.053 -7.852  1.00 16.40 ?  156 PHE   B C    1 
ATOM   6372 O  O    . PHE   B 1 156 ? 49.957 -34.472 -8.769  1.00 17.69 ?  156 PHE   B O    1 
ATOM   6373 C  CB   . PHE   B 1 156 ? 49.966 -32.201 -6.331  1.00 14.89 ?  156 PHE   B CB   1 
ATOM   6374 C  CG   . PHE   B 1 156 ? 51.391 -32.665 -6.399  1.00 15.30 ?  156 PHE   B CG   1 
ATOM   6375 C  CD1  . PHE   B 1 156 ? 52.260 -32.140 -7.335  1.00 17.34 ?  156 PHE   B CD1  1 
ATOM   6376 C  CD2  . PHE   B 1 156 ? 51.865 -33.603 -5.501  1.00 15.41 ?  156 PHE   B CD2  1 
ATOM   6377 C  CE1  . PHE   B 1 156 ? 53.582 -32.558 -7.390  1.00 18.12 ?  156 PHE   B CE1  1 
ATOM   6378 C  CE2  . PHE   B 1 156 ? 53.186 -34.023 -5.549  1.00 16.85 ?  156 PHE   B CE2  1 
ATOM   6379 C  CZ   . PHE   B 1 156 ? 54.039 -33.497 -6.499  1.00 17.47 ?  156 PHE   B CZ   1 
ATOM   6380 H  H    . PHE   B 1 156 ? 47.572 -31.878 -6.538  1.00 16.94 ?  156 PHE   B H    1 
ATOM   6381 H  HA   . PHE   B 1 156 ? 49.503 -32.083 -8.313  1.00 18.18 ?  156 PHE   B HA   1 
ATOM   6382 H  HB2  . PHE   B 1 156 ? 49.974 -31.235 -6.233  1.00 17.88 ?  156 PHE   B HB2  1 
ATOM   6383 H  HB3  . PHE   B 1 156 ? 49.559 -32.604 -5.545  1.00 17.88 ?  156 PHE   B HB3  1 
ATOM   6384 H  HD1  . PHE   B 1 156 ? 51.954 -31.501 -7.939  1.00 20.82 ?  156 PHE   B HD1  1 
ATOM   6385 H  HD2  . PHE   B 1 156 ? 51.286 -33.962 -4.863  1.00 18.49 ?  156 PHE   B HD2  1 
ATOM   6386 H  HE1  . PHE   B 1 156 ? 54.158 -32.200 -8.027  1.00 21.75 ?  156 PHE   B HE1  1 
ATOM   6387 H  HE2  . PHE   B 1 156 ? 53.491 -34.665 -4.947  1.00 20.22 ?  156 PHE   B HE2  1 
ATOM   6388 H  HZ   . PHE   B 1 156 ? 54.923 -33.781 -6.532  1.00 20.98 ?  156 PHE   B HZ   1 
ATOM   6389 N  N    . ASP   B 1 157 ? 48.576 -34.878 -7.052  1.00 16.65 ?  157 ASP   B N    1 
ATOM   6390 C  CA   . ASP   B 1 157 ? 48.726 -36.323 -7.162  1.00 18.32 ?  157 ASP   B CA   1 
ATOM   6391 C  C    . ASP   B 1 157 ? 47.803 -36.865 -8.249  1.00 17.91 ?  157 ASP   B C    1 
ATOM   6392 O  O    . ASP   B 1 157 ? 46.578 -36.747 -8.145  1.00 17.46 ?  157 ASP   B O    1 
ATOM   6393 C  CB   . ASP   B 1 157 ? 48.379 -36.944 -5.816  1.00 19.53 ?  157 ASP   B CB   1 
ATOM   6394 C  CG   . ASP   B 1 157 ? 48.518 -38.448 -5.810  1.00 21.56 ?  157 ASP   B CG   1 
ATOM   6395 O  OD1  . ASP   B 1 157 ? 48.843 -39.049 -6.861  1.00 21.72 ?  157 ASP   B OD1  1 
ATOM   6396 O  OD2  . ASP   B 1 157 ? 48.307 -39.031 -4.731  1.00 23.99 -1 157 ASP   B OD2  1 
ATOM   6397 H  H    . ASP   B 1 157 ? 48.040 -34.627 -6.428  1.00 19.99 ?  157 ASP   B H    1 
ATOM   6398 H  HA   . ASP   B 1 157 ? 49.641 -36.548 -7.387  1.00 21.99 ?  157 ASP   B HA   1 
ATOM   6399 H  HB2  . ASP   B 1 157 ? 48.963 -36.576 -5.140  1.00 23.45 ?  157 ASP   B HB2  1 
ATOM   6400 H  HB3  . ASP   B 1 157 ? 47.455 -36.736 -5.606  1.00 23.45 ?  157 ASP   B HB3  1 
ATOM   6401 N  N    A LYS   B 1 158 ? 48.391 -37.507 -9.263  0.66 18.79 ?  158 LYS   B N    1 
ATOM   6402 N  N    B LYS   B 1 158 ? 48.396 -37.447 -9.297  0.34 18.51 ?  158 LYS   B N    1 
ATOM   6403 C  CA   A LYS   B 1 158 ? 47.609 -38.124 -10.335 0.66 20.04 ?  158 LYS   B CA   1 
ATOM   6404 C  CA   B LYS   B 1 158 ? 47.620 -38.008 -10.402 0.34 19.53 ?  158 LYS   B CA   1 
ATOM   6405 C  C    A LYS   B 1 158 ? 46.549 -39.082 -9.794  0.66 20.02 ?  158 LYS   B C    1 
ATOM   6406 C  C    B LYS   B 1 158 ? 46.561 -38.988 -9.909  0.34 19.22 ?  158 LYS   B C    1 
ATOM   6407 O  O    A LYS   B 1 158 ? 45.431 -39.145 -10.320 0.66 20.22 ?  158 LYS   B O    1 
ATOM   6408 O  O    B LYS   B 1 158 ? 45.469 -39.075 -10.485 0.34 19.16 ?  158 LYS   B O    1 
ATOM   6409 C  CB   A LYS   B 1 158 ? 48.559 -38.851 -11.296 0.66 21.52 ?  158 LYS   B CB   1 
ATOM   6410 C  CB   B LYS   B 1 158 ? 48.572 -38.689 -11.395 0.34 20.85 ?  158 LYS   B CB   1 
ATOM   6411 C  CG   A LYS   B 1 158 ? 47.884 -39.762 -12.313 0.66 23.24 ?  158 LYS   B CG   1 
ATOM   6412 C  CG   B LYS   B 1 158 ? 47.910 -39.624 -12.402 0.34 22.22 ?  158 LYS   B CG   1 
ATOM   6413 C  CD   A LYS   B 1 158 ? 47.019 -38.991 -13.284 0.66 25.26 ?  158 LYS   B CD   1 
ATOM   6414 C  CD   B LYS   B 1 158 ? 47.009 -38.879 -13.367 0.34 23.84 ?  158 LYS   B CD   1 
ATOM   6415 C  CE   A LYS   B 1 158 ? 46.435 -39.914 -14.339 0.66 26.68 ?  158 LYS   B CE   1 
ATOM   6416 C  CE   B LYS   B 1 158 ? 46.444 -39.817 -14.423 0.34 24.98 ?  158 LYS   B CE   1 
ATOM   6417 N  NZ   A LYS   B 1 158 ? 45.369 -39.244 -15.136 0.66 26.88 ?  158 LYS   B NZ   1 
ATOM   6418 N  NZ   B LYS   B 1 158 ? 45.407 -39.153 -15.260 0.34 25.38 ?  158 LYS   B NZ   1 
ATOM   6419 H  H    A LYS   B 1 158 ? 49.242 -37.604 -9.348  0.66 22.56 ?  158 LYS   B H    1 
ATOM   6420 H  H    B LYS   B 1 158 ? 49.246 -37.526 -9.392  0.34 22.22 ?  158 LYS   B H    1 
ATOM   6421 H  HA   A LYS   B 1 158 ? 47.159 -37.430 -10.838 0.66 24.06 ?  158 LYS   B HA   1 
ATOM   6422 H  HA   B LYS   B 1 158 ? 47.168 -37.292 -10.872 0.34 23.44 ?  158 LYS   B HA   1 
ATOM   6423 H  HB2  A LYS   B 1 158 ? 49.065 -38.187 -11.797 0.66 25.83 ?  158 LYS   B HB2  1 
ATOM   6424 H  HB2  B LYS   B 1 158 ? 49.034 -38.001 -11.904 0.34 25.03 ?  158 LYS   B HB2  1 
ATOM   6425 H  HB3  A LYS   B 1 158 ? 49.172 -39.396 -10.778 0.66 25.83 ?  158 LYS   B HB3  1 
ATOM   6426 H  HB3  B LYS   B 1 158 ? 49.221 -39.210 -10.898 0.34 25.03 ?  158 LYS   B HB3  1 
ATOM   6427 H  HG2  A LYS   B 1 158 ? 48.569 -40.220 -12.826 0.66 27.90 ?  158 LYS   B HG2  1 
ATOM   6428 H  HG2  B LYS   B 1 158 ? 48.603 -40.060 -12.922 0.34 26.67 ?  158 LYS   B HG2  1 
ATOM   6429 H  HG3  A LYS   B 1 158 ? 47.329 -40.416 -11.858 0.66 27.90 ?  158 LYS   B HG3  1 
ATOM   6430 H  HG3  B LYS   B 1 158 ? 47.382 -40.296 -11.940 0.34 26.67 ?  158 LYS   B HG3  1 
ATOM   6431 H  HD2  A LYS   B 1 158 ? 46.287 -38.572 -12.804 0.66 30.32 ?  158 LYS   B HD2  1 
ATOM   6432 H  HD2  B LYS   B 1 158 ? 46.268 -38.486 -12.880 0.34 28.62 ?  158 LYS   B HD2  1 
ATOM   6433 H  HD3  A LYS   B 1 158 ? 47.556 -38.318 -13.732 0.66 30.32 ?  158 LYS   B HD3  1 
ATOM   6434 H  HD3  B LYS   B 1 158 ? 47.521 -38.188 -13.817 0.34 28.62 ?  158 LYS   B HD3  1 
ATOM   6435 H  HE2  A LYS   B 1 158 ? 47.137 -40.190 -14.946 0.66 32.02 ?  158 LYS   B HE2  1 
ATOM   6436 H  HE2  B LYS   B 1 158 ? 47.162 -40.112 -15.006 0.34 29.98 ?  158 LYS   B HE2  1 
ATOM   6437 H  HE3  A LYS   B 1 158 ? 46.046 -40.690 -13.904 0.66 32.02 ?  158 LYS   B HE3  1 
ATOM   6438 H  HE3  B LYS   B 1 158 ? 46.036 -40.582 -13.985 0.34 29.98 ?  158 LYS   B HE3  1 
ATOM   6439 H  HZ1  A LYS   B 1 158 ? 45.044 -39.805 -15.743 0.66 32.27 ?  158 LYS   B HZ1  1 
ATOM   6440 H  HZ1  B LYS   B 1 158 ? 45.094 -39.723 -15.867 0.34 30.46 ?  158 LYS   B HZ1  1 
ATOM   6441 H  HZ2  A LYS   B 1 158 ? 44.708 -38.982 -14.600 0.66 32.27 ?  158 LYS   B HZ2  1 
ATOM   6442 H  HZ2  B LYS   B 1 158 ? 44.733 -38.878 -14.747 0.34 30.46 ?  158 LYS   B HZ2  1 
ATOM   6443 H  HZ3  A LYS   B 1 158 ? 45.704 -38.530 -15.550 0.66 32.27 ?  158 LYS   B HZ3  1 
ATOM   6444 H  HZ3  B LYS   B 1 158 ? 45.759 -38.450 -15.678 0.34 30.46 ?  158 LYS   B HZ3  1 
ATOM   6445 N  N    A ASN   B 1 159 ? 46.882 -39.851 -8.755  0.66 19.91 ?  159 ASN   B N    1 
ATOM   6446 N  N    B ASN   B 1 159 ? 46.865 -39.744 -8.853  0.34 19.06 ?  159 ASN   B N    1 
ATOM   6447 C  CA   A ASN   B 1 159 ? 45.920 -40.821 -8.238  0.66 20.51 ?  159 ASN   B CA   1 
ATOM   6448 C  CA   B ASN   B 1 159 ? 45.911 -40.734 -8.363  0.34 19.22 ?  159 ASN   B CA   1 
ATOM   6449 C  C    A ASN   B 1 159 ? 44.736 -40.138 -7.559  0.66 19.50 ?  159 ASN   B C    1 
ATOM   6450 C  C    B ASN   B 1 159 ? 44.721 -40.068 -7.674  0.34 18.81 ?  159 ASN   B C    1 
ATOM   6451 O  O    A ASN   B 1 159 ? 43.610 -40.644 -7.623  0.66 19.64 ?  159 ASN   B O    1 
ATOM   6452 O  O    B ASN   B 1 159 ? 43.580 -40.519 -7.829  0.34 18.63 ?  159 ASN   B O    1 
ATOM   6453 C  CB   A ASN   B 1 159 ? 46.614 -41.798 -7.292  0.66 22.07 ?  159 ASN   B CB   1 
ATOM   6454 C  CB   B ASN   B 1 159 ? 46.614 -41.733 -7.444  0.34 19.70 ?  159 ASN   B CB   1 
ATOM   6455 C  CG   A ASN   B 1 159 ? 47.658 -42.643 -7.995  0.66 23.75 ?  159 ASN   B CG   1 
ATOM   6456 C  CG   B ASN   B 1 159 ? 47.655 -42.560 -8.177  0.34 20.44 ?  159 ASN   B CG   1 
ATOM   6457 O  OD1  A ASN   B 1 159 ? 47.420 -43.157 -9.090  0.66 24.69 ?  159 ASN   B OD1  1 
ATOM   6458 O  OD1  B ASN   B 1 159 ? 47.437 -42.982 -9.314  0.34 20.79 ?  159 ASN   B OD1  1 
ATOM   6459 N  ND2  A ASN   B 1 159 ? 48.827 -42.782 -7.374  0.66 24.23 ?  159 ASN   B ND2  1 
ATOM   6460 N  ND2  B ASN   B 1 159 ? 48.799 -42.789 -7.533  0.34 20.76 ?  159 ASN   B ND2  1 
ATOM   6461 H  H    A ASN   B 1 159 ? 47.633 -39.822 -8.342  0.66 23.90 ?  159 ASN   B H    1 
ATOM   6462 H  H    B ASN   B 1 159 ? 47.602 -39.704 -8.415  0.34 22.88 ?  159 ASN   B H    1 
ATOM   6463 H  HA   A ASN   B 1 159 ? 45.574 -41.332 -8.985  0.66 24.62 ?  159 ASN   B HA   1 
ATOM   6464 H  HA   B ASN   B 1 159 ? 45.569 -41.233 -9.122  0.34 23.07 ?  159 ASN   B HA   1 
ATOM   6465 H  HB2  A ASN   B 1 159 ? 47.054 -41.301 -6.588  0.66 26.49 ?  159 ASN   B HB2  1 
ATOM   6466 H  HB2  B ASN   B 1 159 ? 47.062 -41.255 -6.732  0.34 23.65 ?  159 ASN   B HB2  1 
ATOM   6467 H  HB3  A ASN   B 1 159 ? 45.950 -42.396 -6.916  0.66 26.49 ?  159 ASN   B HB3  1 
ATOM   6468 H  HB3  B ASN   B 1 159 ? 45.955 -42.344 -7.074  0.34 23.65 ?  159 ASN   B HB3  1 
ATOM   6469 H  HD21 A ASN   B 1 159 ? 49.451 -43.255 -7.732  0.66 29.08 ?  159 ASN   B HD21 1 
ATOM   6470 H  HD21 B ASN   B 1 159 ? 49.421 -43.257 -7.904  0.34 24.92 ?  159 ASN   B HD21 1 
ATOM   6471 H  HD22 A ASN   B 1 159 ? 48.953 -42.415 -6.608  0.66 29.08 ?  159 ASN   B HD22 1 
ATOM   6472 H  HD22 B ASN   B 1 159 ? 48.916 -42.478 -6.739  0.34 24.92 ?  159 ASN   B HD22 1 
ATOM   6473 N  N    . LEU   B 1 160 ? 44.957 -38.986 -6.922  1.00 18.72 ?  160 LEU   B N    1 
ATOM   6474 C  CA   . LEU   B 1 160 ? 43.833 -38.246 -6.354  1.00 17.77 ?  160 LEU   B CA   1 
ATOM   6475 C  C    . LEU   B 1 160 ? 43.028 -37.581 -7.460  1.00 17.22 ?  160 LEU   B C    1 
ATOM   6476 O  O    . LEU   B 1 160 ? 41.790 -37.573 -7.420  1.00 16.99 ?  160 LEU   B O    1 
ATOM   6477 C  CB   . LEU   B 1 160 ? 44.305 -37.210 -5.333  1.00 17.31 ?  160 LEU   B CB   1 
ATOM   6478 C  CG   . LEU   B 1 160 ? 43.172 -36.323 -4.793  1.00 17.22 ?  160 LEU   B CG   1 
ATOM   6479 C  CD1  . LEU   B 1 160 ? 42.065 -37.161 -4.153  1.00 18.32 ?  160 LEU   B CD1  1 
ATOM   6480 C  CD2  . LEU   B 1 160 ? 43.712 -35.299 -3.806  1.00 17.18 ?  160 LEU   B CD2  1 
ATOM   6481 H  H    A LEU   B 1 160 ? 45.728 -38.621 -6.813  0.66 22.47 ?  160 LEU   B H    1 
ATOM   6482 H  H    B LEU   B 1 160 ? 45.735 -38.666 -6.745  0.34 22.47 ?  160 LEU   B H    1 
ATOM   6483 H  HA   . LEU   B 1 160 ? 43.251 -38.874 -5.900  1.00 21.33 ?  160 LEU   B HA   1 
ATOM   6484 H  HB2  . LEU   B 1 160 ? 44.713 -37.678 -4.584  1.00 20.77 ?  160 LEU   B HB2  1 
ATOM   6485 H  HB3  . LEU   B 1 160 ? 44.968 -36.637 -5.756  1.00 20.77 ?  160 LEU   B HB3  1 
ATOM   6486 H  HG   . LEU   B 1 160 ? 42.783 -35.838 -5.534  1.00 20.67 ?  160 LEU   B HG   1 
ATOM   6487 H  HD11 . LEU   B 1 160 ? 41.438 -36.567 -3.720  1.00 22.00 ?  160 LEU   B HD11 1 
ATOM   6488 H  HD12 . LEU   B 1 160 ? 41.615 -37.677 -4.841  1.00 22.00 ?  160 LEU   B HD12 1 
ATOM   6489 H  HD13 . LEU   B 1 160 ? 42.461 -37.761 -3.498  1.00 22.00 ?  160 LEU   B HD13 1 
ATOM   6490 H  HD21 . LEU   B 1 160 ? 42.975 -34.743 -3.506  1.00 20.63 ?  160 LEU   B HD21 1 
ATOM   6491 H  HD22 . LEU   B 1 160 ? 44.108 -35.761 -3.055  1.00 20.63 ?  160 LEU   B HD22 1 
ATOM   6492 H  HD23 . LEU   B 1 160 ? 44.377 -34.753 -4.253  1.00 20.63 ?  160 LEU   B HD23 1 
ATOM   6493 N  N    A TYR   B 1 161 ? 43.718 -37.015 -8.452  0.66 17.29 ?  161 TYR   B N    1 
ATOM   6494 N  N    B TYR   B 1 161 ? 43.714 -37.024 -8.463  0.34 17.07 ?  161 TYR   B N    1 
ATOM   6495 C  CA   A TYR   B 1 161 ? 43.037 -36.449 -9.609  0.66 16.94 ?  161 TYR   B CA   1 
ATOM   6496 C  CA   B TYR   B 1 161 ? 43.023 -36.443 -9.610  0.34 16.77 ?  161 TYR   B CA   1 
ATOM   6497 C  C    A TYR   B 1 161 ? 42.086 -37.467 -10.221 0.66 16.65 ?  161 TYR   B C    1 
ATOM   6498 C  C    B TYR   B 1 161 ? 42.089 -37.460 -10.249 0.34 16.67 ?  161 TYR   B C    1 
ATOM   6499 O  O    A TYR   B 1 161 ? 40.911 -37.170 -10.461 0.66 16.85 ?  161 TYR   B O    1 
ATOM   6500 O  O    B TYR   B 1 161 ? 40.928 -37.155 -10.545 0.34 16.69 ?  161 TYR   B O    1 
ATOM   6501 C  CB   A TYR   B 1 161 ? 44.077 -35.984 -10.636 0.66 17.52 ?  161 TYR   B CB   1 
ATOM   6502 C  CB   B TYR   B 1 161 ? 44.047 -35.932 -10.630 0.34 16.99 ?  161 TYR   B CB   1 
ATOM   6503 C  CG   A TYR   B 1 161 ? 43.493 -35.508 -11.944 0.66 17.77 ?  161 TYR   B CG   1 
ATOM   6504 C  CG   B TYR   B 1 161 ? 43.445 -35.465 -11.940 0.34 17.26 ?  161 TYR   B CG   1 
ATOM   6505 C  CD1  A TYR   B 1 161 ? 43.119 -34.181 -12.111 0.66 17.64 ?  161 TYR   B CD1  1 
ATOM   6506 C  CD1  B TYR   B 1 161 ? 43.044 -34.145 -12.108 0.34 17.35 ?  161 TYR   B CD1  1 
ATOM   6507 C  CD2  A TYR   B 1 161 ? 43.306 -36.381 -13.010 0.66 18.43 ?  161 TYR   B CD2  1 
ATOM   6508 C  CD2  B TYR   B 1 161 ? 43.275 -36.341 -13.007 0.34 17.52 ?  161 TYR   B CD2  1 
ATOM   6509 C  CE1  A TYR   B 1 161 ? 42.581 -33.736 -13.296 0.66 18.91 ?  161 TYR   B CE1  1 
ATOM   6510 C  CE1  B TYR   B 1 161 ? 42.491 -33.711 -13.297 0.34 17.95 ?  161 TYR   B CE1  1 
ATOM   6511 C  CE2  A TYR   B 1 161 ? 42.763 -35.945 -14.199 0.66 19.66 ?  161 TYR   B CE2  1 
ATOM   6512 C  CE2  B TYR   B 1 161 ? 42.720 -35.915 -14.199 0.34 18.19 ?  161 TYR   B CE2  1 
ATOM   6513 C  CZ   A TYR   B 1 161 ? 42.406 -34.621 -14.337 0.66 19.73 ?  161 TYR   B CZ   1 
ATOM   6514 C  CZ   B TYR   B 1 161 ? 42.332 -34.599 -14.339 0.34 18.32 ?  161 TYR   B CZ   1 
ATOM   6515 O  OH   A TYR   B 1 161 ? 41.865 -34.180 -15.519 0.66 21.66 ?  161 TYR   B OH   1 
ATOM   6516 O  OH   B TYR   B 1 161 ? 41.779 -34.171 -15.523 0.34 19.38 ?  161 TYR   B OH   1 
ATOM   6517 H  H    A TYR   B 1 161 ? 44.573 -36.955 -8.483  0.66 20.75 ?  161 TYR   B H    1 
ATOM   6518 H  H    B TYR   B 1 161 ? 44.570 -36.976 -8.505  0.34 20.50 ?  161 TYR   B H    1 
ATOM   6519 H  HA   A TYR   B 1 161 ? 42.520 -35.676 -9.331  0.66 20.33 ?  161 TYR   B HA   1 
ATOM   6520 H  HA   B TYR   B 1 161 ? 42.491 -35.687 -9.314  0.34 20.13 ?  161 TYR   B HA   1 
ATOM   6521 H  HB2  A TYR   B 1 161 ? 44.584 -35.247 -10.256 0.66 21.03 ?  161 TYR   B HB2  1 
ATOM   6522 H  HB2  B TYR   B 1 161 ? 44.526 -35.182 -10.244 0.34 20.40 ?  161 TYR   B HB2  1 
ATOM   6523 H  HB3  A TYR   B 1 161 ? 44.673 -36.721 -10.835 0.66 21.03 ?  161 TYR   B HB3  1 
ATOM   6524 H  HB3  B TYR   B 1 161 ? 44.669 -36.648 -10.833 0.34 20.40 ?  161 TYR   B HB3  1 
ATOM   6525 H  HD1  A TYR   B 1 161 ? 43.237 -33.574 -11.411 0.66 21.18 ?  161 TYR   B HD1  1 
ATOM   6526 H  HD1  B TYR   B 1 161 ? 43.149 -33.540 -11.409 0.34 20.83 ?  161 TYR   B HD1  1 
ATOM   6527 H  HD2  A TYR   B 1 161 ? 43.544 -37.272 -12.919 0.66 22.12 ?  161 TYR   B HD2  1 
ATOM   6528 H  HD2  B TYR   B 1 161 ? 43.534 -37.228 -12.917 0.34 21.03 ?  161 TYR   B HD2  1 
ATOM   6529 H  HE1  A TYR   B 1 161 ? 42.337 -32.839 -13.391 0.66 22.70 ?  161 TYR   B HE1  1 
ATOM   6530 H  HE1  B TYR   B 1 161 ? 42.228 -32.822 -13.393 0.34 21.55 ?  161 TYR   B HE1  1 
ATOM   6531 H  HE2  A TYR   B 1 161 ? 42.641 -36.534 -14.905 0.66 23.59 ?  161 TYR   B HE2  1 
ATOM   6532 H  HE2  B TYR   B 1 161 ? 42.612 -36.511 -14.904 0.34 21.83 ?  161 TYR   B HE2  1 
ATOM   6533 H  HH   A TYR   B 1 161 ? 41.812 -34.816 -16.065 0.66 26.00 ?  161 TYR   B HH   1 
ATOM   6534 H  HH   B TYR   B 1 161 ? 41.738 -34.810 -16.068 0.34 23.26 ?  161 TYR   B HH   1 
ATOM   6535 N  N    . ASP   B 1 162 ? 42.581 -38.682 -10.468 1.00 17.10 ?  162 ASP   B N    1 
ATOM   6536 C  CA   . ASP   B 1 162 ? 41.746 -39.715 -11.070 1.00 17.29 ?  162 ASP   B CA   1 
ATOM   6537 C  C    . ASP   B 1 162 ? 40.551 -40.052 -10.185 1.00 16.83 ?  162 ASP   B C    1 
ATOM   6538 O  O    . ASP   B 1 162 ? 39.444 -40.272 -10.688 1.00 17.51 ?  162 ASP   B O    1 
ATOM   6539 C  CB   . ASP   B 1 162 ? 42.566 -40.983 -11.337 1.00 18.94 ?  162 ASP   B CB   1 
ATOM   6540 C  CG   . ASP   B 1 162 ? 43.583 -40.822 -12.458 1.00 20.02 ?  162 ASP   B CG   1 
ATOM   6541 O  OD1  . ASP   B 1 162 ? 43.463 -39.879 -13.263 1.00 20.32 ?  162 ASP   B OD1  1 
ATOM   6542 O  OD2  . ASP   B 1 162 ? 44.488 -41.685 -12.551 1.00 21.89 -1 162 ASP   B OD2  1 
ATOM   6543 H  H    A ASP   B 1 162 ? 43.388 -38.926 -10.301 0.66 20.53 ?  162 ASP   B H    1 
ATOM   6544 H  H    B ASP   B 1 162 ? 43.382 -38.930 -10.282 0.34 20.53 ?  162 ASP   B H    1 
ATOM   6545 H  HA   . ASP   B 1 162 ? 41.403 -39.391 -11.916 1.00 20.75 ?  162 ASP   B HA   1 
ATOM   6546 H  HB2  . ASP   B 1 162 ? 43.051 -41.220 -10.538 1.00 22.74 ?  162 ASP   B HB2  1 
ATOM   6547 H  HB3  . ASP   B 1 162 ? 41.964 -41.696 -11.595 1.00 22.74 ?  162 ASP   B HB3  1 
ATOM   6548 N  N    A LYS   B 1 163 ? 40.757 -40.122 -8.867  0.66 16.24 ?  163 LYS   B N    1 
ATOM   6549 N  N    B LYS   B 1 163 ? 40.756 -40.117 -8.867  0.34 16.92 ?  163 LYS   B N    1 
ATOM   6550 C  CA   A LYS   B 1 163 ? 39.641 -40.401 -7.968  0.66 17.09 ?  163 LYS   B CA   1 
ATOM   6551 C  CA   B LYS   B 1 163 ? 39.641 -40.400 -7.968  0.34 17.79 ?  163 LYS   B CA   1 
ATOM   6552 C  C    A LYS   B 1 163 ? 38.599 -39.292 -8.025  0.66 16.22 ?  163 LYS   B C    1 
ATOM   6553 C  C    B LYS   B 1 163 ? 38.600 -39.289 -8.018  0.34 16.51 ?  163 LYS   B C    1 
ATOM   6554 O  O    A LYS   B 1 163 ? 37.388 -39.560 -8.022  0.66 17.09 ?  163 LYS   B O    1 
ATOM   6555 O  O    B LYS   B 1 163 ? 37.391 -39.555 -8.008  0.34 16.89 ?  163 LYS   B O    1 
ATOM   6556 C  CB   A LYS   B 1 163 ? 40.138 -40.582 -6.535  0.66 19.80 ?  163 LYS   B CB   1 
ATOM   6557 C  CB   B LYS   B 1 163 ? 40.146 -40.586 -6.538  0.34 20.43 ?  163 LYS   B CB   1 
ATOM   6558 C  CG   A LYS   B 1 163 ? 39.067 -41.109 -5.599  0.66 24.08 ?  163 LYS   B CG   1 
ATOM   6559 C  CG   B LYS   B 1 163 ? 39.079 -41.089 -5.584  0.34 23.54 ?  163 LYS   B CG   1 
ATOM   6560 C  CD   A LYS   B 1 163 ? 39.523 -41.163 -4.153  0.66 28.26 ?  163 LYS   B CD   1 
ATOM   6561 C  CD   B LYS   B 1 163 ? 39.608 -41.277 -4.173  0.34 26.60 ?  163 LYS   B CD   1 
ATOM   6562 C  CE   A LYS   B 1 163 ? 38.463 -41.839 -3.291  0.66 31.25 ?  163 LYS   B CE   1 
ATOM   6563 C  CE   B LYS   B 1 163 ? 38.556 -41.934 -3.293  0.34 28.99 ?  163 LYS   B CE   1 
ATOM   6564 N  NZ   A LYS   B 1 163 ? 38.594 -41.506 -1.846  0.66 33.13 ?  163 LYS   B NZ   1 
ATOM   6565 N  NZ   B LYS   B 1 163 ? 38.824 -41.739 -1.842  0.34 30.16 ?  163 LYS   B NZ   1 
ATOM   6566 H  H    A LYS   B 1 163 ? 41.518 -40.017 -8.478  0.66 19.50 ?  163 LYS   B H    1 
ATOM   6567 H  H    B LYS   B 1 163 ? 41.515 -40.009 -8.477  0.34 20.31 ?  163 LYS   B H    1 
ATOM   6568 H  HA   A LYS   B 1 163 ? 39.212 -41.222 -8.240  0.66 20.51 ?  163 LYS   B HA   1 
ATOM   6569 H  HA   B LYS   B 1 163 ? 39.211 -41.221 -8.242  0.34 21.35 ?  163 LYS   B HA   1 
ATOM   6570 H  HB2  A LYS   B 1 163 ? 40.874 -41.216 -6.533  0.66 23.77 ?  163 LYS   B HB2  1 
ATOM   6571 H  HB2  B LYS   B 1 163 ? 40.870 -41.232 -6.541  0.34 24.52 ?  163 LYS   B HB2  1 
ATOM   6572 H  HB3  A LYS   B 1 163 ? 40.439 -39.727 -6.190  0.66 23.77 ?  163 LYS   B HB3  1 
ATOM   6573 H  HB3  B LYS   B 1 163 ? 40.466 -39.734 -6.201  0.34 24.52 ?  163 LYS   B HB3  1 
ATOM   6574 H  HG2  A LYS   B 1 163 ? 38.290 -40.533 -5.644  0.66 28.90 ?  163 LYS   B HG2  1 
ATOM   6575 H  HG2  B LYS   B 1 163 ? 38.353 -40.447 -5.548  0.34 28.26 ?  163 LYS   B HG2  1 
ATOM   6576 H  HG3  A LYS   B 1 163 ? 38.827 -42.012 -5.870  0.66 28.90 ?  163 LYS   B HG3  1 
ATOM   6577 H  HG3  B LYS   B 1 163 ? 38.751 -41.947 -5.898  0.34 28.26 ?  163 LYS   B HG3  1 
ATOM   6578 H  HD2  A LYS   B 1 163 ? 40.343 -41.680 -4.090  0.66 33.92 ?  163 LYS   B HD2  1 
ATOM   6579 H  HD2  B LYS   B 1 163 ? 40.391 -41.851 -4.195  0.34 31.93 ?  163 LYS   B HD2  1 
ATOM   6580 H  HD3  A LYS   B 1 163 ? 39.661 -40.263 -3.823  0.66 33.92 ?  163 LYS   B HD3  1 
ATOM   6581 H  HD3  B LYS   B 1 163 ? 39.832 -40.414 -3.793  0.34 31.93 ?  163 LYS   B HD3  1 
ATOM   6582 H  HE2  A LYS   B 1 163 ? 37.583 -41.563 -3.589  0.66 37.51 ?  163 LYS   B HE2  1 
ATOM   6583 H  HE2  B LYS   B 1 163 ? 37.688 -41.552 -3.495  0.34 34.79 ?  163 LYS   B HE2  1 
ATOM   6584 H  HE3  A LYS   B 1 163 ? 38.552 -42.800 -3.383  0.66 37.51 ?  163 LYS   B HE3  1 
ATOM   6585 H  HE3  B LYS   B 1 163 ? 38.546 -42.888 -3.471  0.34 34.79 ?  163 LYS   B HE3  1 
ATOM   6586 H  HZ1  A LYS   B 1 163 ? 37.956 -41.918 -1.381  0.66 39.76 ?  163 LYS   B HZ1  1 
ATOM   6587 H  HZ1  B LYS   B 1 163 ? 38.188 -42.134 -1.361  0.34 36.20 ?  163 LYS   B HZ1  1 
ATOM   6588 H  HZ2  A LYS   B 1 163 ? 39.388 -41.769 -1.545  0.66 39.76 ?  163 LYS   B HZ2  1 
ATOM   6589 H  HZ2  B LYS   B 1 163 ? 39.612 -42.091 -1.629  0.34 36.20 ?  163 LYS   B HZ2  1 
ATOM   6590 H  HZ3  A LYS   B 1 163 ? 38.515 -40.627 -1.728  0.66 39.76 ?  163 LYS   B HZ3  1 
ATOM   6591 H  HZ3  B LYS   B 1 163 ? 38.833 -40.869 -1.650  0.34 36.20 ?  163 LYS   B HZ3  1 
ATOM   6592 N  N    . LEU   B 1 164 ? 39.056 -38.036 -8.069  1.00 15.42 ?  164 LEU   B N    1 
ATOM   6593 C  CA   . LEU   B 1 164 ? 38.142 -36.901 -8.114  1.00 14.82 ?  164 LEU   B CA   1 
ATOM   6594 C  C    . LEU   B 1 164 ? 37.346 -36.886 -9.412  1.00 14.89 ?  164 LEU   B C    1 
ATOM   6595 O  O    . LEU   B 1 164 ? 36.126 -36.680 -9.399  1.00 15.98 ?  164 LEU   B O    1 
ATOM   6596 C  CB   . LEU   B 1 164 ? 38.934 -35.600 -7.955  1.00 14.30 ?  164 LEU   B CB   1 
ATOM   6597 C  CG   . LEU   B 1 164 ? 39.486 -35.341 -6.557  1.00 14.96 ?  164 LEU   B CG   1 
ATOM   6598 C  CD1  . LEU   B 1 164 ? 40.577 -34.276 -6.601  1.00 15.09 ?  164 LEU   B CD1  1 
ATOM   6599 C  CD2  . LEU   B 1 164 ? 38.383 -34.919 -5.611  1.00 16.90 ?  164 LEU   B CD2  1 
ATOM   6600 H  H    A LEU   B 1 164 ? 39.890 -37.813 -8.077  0.66 18.52 ?  164 LEU   B H    1 
ATOM   6601 H  H    B LEU   B 1 164 ? 39.890 -37.814 -8.079  0.34 18.52 ?  164 LEU   B H    1 
ATOM   6602 H  HA   . LEU   B 1 164 ? 37.517 -36.966 -7.382  1.00 17.79 ?  164 LEU   B HA   1 
ATOM   6603 H  HB2  . LEU   B 1 164 ? 39.684 -35.619 -8.571  1.00 17.17 ?  164 LEU   B HB2  1 
ATOM   6604 H  HB3  . LEU   B 1 164 ? 38.351 -34.857 -8.183  1.00 17.17 ?  164 LEU   B HB3  1 
ATOM   6605 H  HG   . LEU   B 1 164 ? 39.881 -36.158 -6.221  1.00 17.96 ?  164 LEU   B HG   1 
ATOM   6606 H  HD11 . LEU   B 1 164 ? 40.911 -34.129 -5.700  1.00 18.12 ?  164 LEU   B HD11 1 
ATOM   6607 H  HD12 . LEU   B 1 164 ? 41.304 -34.586 -7.170  1.00 18.12 ?  164 LEU   B HD12 1 
ATOM   6608 H  HD13 . LEU   B 1 164 ? 40.210 -33.454 -6.956  1.00 18.12 ?  164 LEU   B HD13 1 
ATOM   6609 H  HD21 . LEU   B 1 164 ? 38.768 -34.714 -4.747  1.00 20.28 ?  164 LEU   B HD21 1 
ATOM   6610 H  HD22 . LEU   B 1 164 ? 37.938 -34.136 -5.971  1.00 20.28 ?  164 LEU   B HD22 1 
ATOM   6611 H  HD23 . LEU   B 1 164 ? 37.746 -35.648 -5.525  1.00 20.28 ?  164 LEU   B HD23 1 
ATOM   6612 N  N    . VAL   B 1 165 ? 38.025 -37.044 -10.549 1.00 16.70 ?  165 VAL   B N    1 
ATOM   6613 C  CA   . VAL   B 1 165 ? 37.355 -36.976 -11.845 1.00 18.03 ?  165 VAL   B CA   1 
ATOM   6614 C  C    . VAL   B 1 165 ? 36.432 -38.172 -12.027 1.00 20.07 ?  165 VAL   B C    1 
ATOM   6615 O  O    . VAL   B 1 165 ? 35.264 -38.032 -12.415 1.00 21.28 ?  165 VAL   B O    1 
ATOM   6616 C  CB   . VAL   B 1 165 ? 38.393 -36.893 -12.979 1.00 19.25 ?  165 VAL   B CB   1 
ATOM   6617 C  CG1  . VAL   B 1 165 ? 37.718 -37.017 -14.324 1.00 20.39 ?  165 VAL   B CG1  1 
ATOM   6618 C  CG2  . VAL   B 1 165 ? 39.172 -35.598 -12.896 1.00 19.13 ?  165 VAL   B CG2  1 
ATOM   6619 H  H    . VAL   B 1 165 ? 38.873 -37.194 -10.596 1.00 20.05 ?  165 VAL   B H    1 
ATOM   6620 H  HA   . VAL   B 1 165 ? 36.816 -36.174 -11.881 1.00 21.64 ?  165 VAL   B HA   1 
ATOM   6621 H  HB   . VAL   B 1 165 ? 39.028 -37.622 -12.889 1.00 23.11 ?  165 VAL   B HB   1 
ATOM   6622 H  HG11 . VAL   B 1 165 ? 38.315 -36.687 -15.011 1.00 24.47 ?  165 VAL   B HG11 1 
ATOM   6623 H  HG12 . VAL   B 1 165 ? 37.519 -37.954 -14.487 1.00 24.47 ?  165 VAL   B HG12 1 
ATOM   6624 H  HG13 . VAL   B 1 165 ? 36.900 -36.500 -14.315 1.00 24.47 ?  165 VAL   B HG13 1 
ATOM   6625 H  HG21 . VAL   B 1 165 ? 39.794 -35.553 -13.641 1.00 22.97 ?  165 VAL   B HG21 1 
ATOM   6626 H  HG22 . VAL   B 1 165 ? 38.551 -34.853 -12.941 1.00 22.97 ?  165 VAL   B HG22 1 
ATOM   6627 H  HG23 . VAL   B 1 165 ? 39.659 -35.572 -12.058 1.00 22.97 ?  165 VAL   B HG23 1 
ATOM   6628 N  N    . SER   B 1 166 ? 36.956 -39.371 -11.758 1.00 21.00 ?  166 SER   B N    1 
ATOM   6629 C  CA   . SER   B 1 166 ? 36.207 -40.587 -12.045 1.00 22.53 ?  166 SER   B CA   1 
ATOM   6630 C  C    . SER   B 1 166 ? 34.951 -40.683 -11.193 1.00 22.82 ?  166 SER   B C    1 
ATOM   6631 O  O    . SER   B 1 166 ? 33.978 -41.311 -11.611 1.00 23.84 ?  166 SER   B O    1 
ATOM   6632 C  CB   . SER   B 1 166 ? 37.086 -41.837 -11.877 1.00 23.52 ?  166 SER   B CB   1 
ATOM   6633 O  OG   . SER   B 1 166 ? 37.439 -42.059 -10.521 1.00 23.51 ?  166 SER   B OG   1 
ATOM   6634 H  H    . SER   B 1 166 ? 37.743 -39.504 -11.425 1.00 25.21 ?  166 SER   B H    1 
ATOM   6635 H  HA   . SER   B 1 166 ? 35.933 -40.566 -12.975 1.00 27.04 ?  166 SER   B HA   1 
ATOM   6636 H  HB2  . SER   B 1 166 ? 36.601 -42.611 -12.200 1.00 28.23 ?  166 SER   B HB2  1 
ATOM   6637 H  HB3  . SER   B 1 166 ? 37.903 -41.725 -12.398 1.00 28.23 ?  166 SER   B HB3  1 
ATOM   6638 H  HG   . SER   B 1 166 ? 37.876 -41.397 -10.231 1.00 28.22 ?  166 SER   B HG   1 
ATOM   6639 N  N    . SER   B 1 167 ? 34.939 -40.066 -10.013 1.00 21.25 ?  167 SER   B N    1 
ATOM   6640 C  CA   . SER   B 1 167 ? 33.789 -40.133 -9.118  1.00 21.02 ?  167 SER   B CA   1 
ATOM   6641 C  C    . SER   B 1 167 ? 32.869 -38.913 -9.202  1.00 20.36 ?  167 SER   B C    1 
ATOM   6642 O  O    . SER   B 1 167 ? 31.797 -38.919 -8.588  1.00 20.15 ?  167 SER   B O    1 
ATOM   6643 C  CB   . SER   B 1 167 ? 34.251 -40.323 -7.665  1.00 20.73 ?  167 SER   B CB   1 
ATOM   6644 O  OG   . SER   B 1 167 ? 34.912 -39.156 -7.187  1.00 20.35 ?  167 SER   B OG   1 
ATOM   6645 H  H    . SER   B 1 167 ? 35.594 -39.603 -9.709  1.00 25.51 ?  167 SER   B H    1 
ATOM   6646 H  HA   . SER   B 1 167 ? 33.264 -40.913 -9.361  1.00 25.23 ?  167 SER   B HA   1 
ATOM   6647 H  HB2  . SER   B 1 167 ? 33.471 -40.503 -7.114  1.00 24.88 ?  167 SER   B HB2  1 
ATOM   6648 H  HB3  . SER   B 1 167 ? 34.857 -41.088 -7.627  1.00 24.88 ?  167 SER   B HB3  1 
ATOM   6649 H  HG   . SER   B 1 167 ? 35.593 -39.015 -7.657  1.00 24.42 ?  167 SER   B HG   1 
ATOM   6650 N  N    . PHE   B 1 168 ? 33.249 -37.865 -9.934  1.00 19.90 ?  168 PHE   B N    1 
ATOM   6651 C  CA   . PHE   B 1 168 ? 32.407 -36.668 -9.992  1.00 18.72 ?  168 PHE   B CA   1 
ATOM   6652 C  C    . PHE   B 1 168 ? 31.106 -36.936 -10.743 1.00 16.11 ?  168 PHE   B C    1 
ATOM   6653 O  O    . PHE   B 1 168 ? 30.054 -36.352 -10.414 1.00 16.83 ?  168 PHE   B O    1 
ATOM   6654 C  CB   . PHE   B 1 168 ? 33.167 -35.515 -10.649 1.00 19.36 ?  168 PHE   B CB   1 
ATOM   6655 C  CG   . PHE   B 1 168 ? 32.347 -34.277 -10.813 1.00 19.54 ?  168 PHE   B CG   1 
ATOM   6656 C  CD1  . PHE   B 1 168 ? 31.994 -33.522 -9.705  1.00 21.01 ?  168 PHE   B CD1  1 
ATOM   6657 C  CD2  . PHE   B 1 168 ? 31.912 -33.877 -12.061 1.00 18.74 ?  168 PHE   B CD2  1 
ATOM   6658 C  CE1  . PHE   B 1 168 ? 31.224 -32.388 -9.836  1.00 21.31 ?  168 PHE   B CE1  1 
ATOM   6659 C  CE2  . PHE   B 1 168 ? 31.151 -32.722 -12.208 1.00 20.09 ?  168 PHE   B CE2  1 
ATOM   6660 C  CZ   . PHE   B 1 168 ? 30.801 -31.980 -11.091 1.00 20.25 ?  168 PHE   B CZ   1 
ATOM   6661 H  H    . PHE   B 1 168 ? 33.979 -37.817 -10.391 1.00 23.88 ?  168 PHE   B H    1 
ATOM   6662 H  HA   . PHE   B 1 168 ? 32.179 -36.403 -9.089  1.00 22.47 ?  168 PHE   B HA   1 
ATOM   6663 H  HB2  . PHE   B 1 168 ? 33.933 -35.291 -10.097 1.00 23.24 ?  168 PHE   B HB2  1 
ATOM   6664 H  HB3  . PHE   B 1 168 ? 33.463 -35.793 -11.528 1.00 23.24 ?  168 PHE   B HB3  1 
ATOM   6665 H  HD1  . PHE   B 1 168 ? 32.272 -33.795 -8.861  1.00 25.22 ?  168 PHE   B HD1  1 
ATOM   6666 H  HD2  . PHE   B 1 168 ? 32.145 -34.372 -12.812 1.00 22.50 ?  168 PHE   B HD2  1 
ATOM   6667 H  HE1  . PHE   B 1 168 ? 30.993 -31.893 -9.085  1.00 25.57 ?  168 PHE   B HE1  1 
ATOM   6668 H  HE2  . PHE   B 1 168 ? 30.858 -32.460 -13.053 1.00 24.11 ?  168 PHE   B HE2  1 
ATOM   6669 H  HZ   . PHE   B 1 168 ? 30.279 -31.216 -11.186 1.00 24.31 ?  168 PHE   B HZ   1 
ATOM   6670 N  N    A LEU   B 1 169 ? 31.155 -37.810 -11.742 0.66 16.29 ?  169 LEU   B N    1 
ATOM   6671 N  N    B LEU   B 1 169 ? 31.151 -37.812 -11.744 0.34 16.62 ?  169 LEU   B N    1 
ATOM   6672 C  CA   A LEU   B 1 169 ? 29.980 -38.148 -12.535 0.66 18.83 ?  169 LEU   B CA   1 
ATOM   6673 C  CA   B LEU   B 1 169 ? 29.979 -38.110 -12.557 0.34 18.30 ?  169 LEU   B CA   1 
ATOM   6674 C  C    A LEU   B 1 169 ? 29.977 -39.607 -12.961 0.66 21.76 ?  169 LEU   B C    1 
ATOM   6675 C  C    B LEU   B 1 169 ? 29.925 -39.554 -13.042 0.34 19.59 ?  169 LEU   B C    1 
ATOM   6676 O  O    A LEU   B 1 169 ? 29.000 -40.114 -13.519 0.66 24.02 ?  169 LEU   B O    1 
ATOM   6677 O  O    B LEU   B 1 169 ? 29.091 -39.892 -13.883 0.34 20.80 ?  169 LEU   B O    1 
ATOM   6678 C  CB   A LEU   B 1 169 ? 29.911 -37.269 -13.781 0.66 20.62 ?  169 LEU   B CB   1 
ATOM   6679 C  CB   B LEU   B 1 169 ? 29.930 -37.182 -13.771 0.34 19.73 ?  169 LEU   B CB   1 
ATOM   6680 C  CG   A LEU   B 1 169 ? 28.714 -36.324 -13.838 0.66 23.63 ?  169 LEU   B CG   1 
ATOM   6681 C  CG   B LEU   B 1 169 ? 28.698 -36.285 -13.865 0.34 21.80 ?  169 LEU   B CG   1 
ATOM   6682 C  CD1  A LEU   B 1 169 ? 28.641 -35.648 -15.192 0.66 24.41 ?  169 LEU   B CD1  1 
ATOM   6683 C  CD1  B LEU   B 1 169 ? 28.607 -35.669 -15.246 0.34 22.30 ?  169 LEU   B CD1  1 
ATOM   6684 C  CD2  A LEU   B 1 169 ? 27.423 -37.067 -13.533 0.66 24.11 ?  169 LEU   B CD2  1 
ATOM   6685 C  CD2  B LEU   B 1 169 ? 27.434 -37.062 -13.535 0.34 22.16 ?  169 LEU   B CD2  1 
ATOM   6686 O  OXT  A LEU   B 1 169 ? 30.961 -40.309 -12.764 0.66 22.53 -1 169 LEU   B OXT  1 
ATOM   6687 O  OXT  B LEU   B 1 169 ? 30.699 -40.411 -12.623 0.34 19.86 -1 169 LEU   B OXT  1 
ATOM   6688 H  H    A LEU   B 1 169 ? 31.867 -38.227 -11.987 0.66 19.55 ?  169 LEU   B H    1 
ATOM   6689 H  H    B LEU   B 1 169 ? 31.854 -38.248 -11.976 0.34 19.95 ?  169 LEU   B H    1 
ATOM   6690 H  HA   A LEU   B 1 169 ? 29.194 -37.993 -11.995 0.66 22.60 ?  169 LEU   B HA   1 
ATOM   6691 H  HA   B LEU   B 1 169 ? 29.196 -37.960 -12.012 0.34 21.97 ?  169 LEU   B HA   1 
ATOM   6692 H  HB2  A LEU   B 1 169 ? 30.715 -36.726 -13.822 0.66 24.76 ?  169 LEU   B HB2  1 
ATOM   6693 H  HB2  B LEU   B 1 169 ? 30.710 -36.604 -13.750 0.34 23.69 ?  169 LEU   B HB2  1 
ATOM   6694 H  HB3  A LEU   B 1 169 ? 29.866 -37.841 -14.564 0.66 24.76 ?  169 LEU   B HB3  1 
ATOM   6695 H  HB3  B LEU   B 1 169 ? 29.954 -37.724 -14.577 0.34 23.69 ?  169 LEU   B HB3  1 
ATOM   6696 H  HG   A LEU   B 1 169 ? 28.826 -35.633 -13.166 0.66 28.36 ?  169 LEU   B HG   1 
ATOM   6697 H  HG   B LEU   B 1 169 ? 28.784 -35.564 -13.222 0.34 26.16 ?  169 LEU   B HG   1 
ATOM   6698 H  HD11 A LEU   B 1 169 ? 27.889 -35.035 -15.198 0.66 29.30 ?  169 LEU   B HD11 1 
ATOM   6699 H  HD11 B LEU   B 1 169 ? 27.836 -35.082 -15.278 0.34 26.77 ?  169 LEU   B HD11 1 
ATOM   6700 H  HD12 A LEU   B 1 169 ? 29.466 -35.162 -15.346 0.66 29.30 ?  169 LEU   B HD12 1 
ATOM   6701 H  HD12 B LEU   B 1 169 ? 29.416 -35.163 -15.419 0.34 26.77 ?  169 LEU   B HD12 1 
ATOM   6702 H  HD13 A LEU   B 1 169 ? 28.522 -36.325 -15.875 0.66 29.30 ?  169 LEU   B HD13 1 
ATOM   6703 H  HD13 B LEU   B 1 169 ? 28.512 -36.378 -15.901 0.34 26.77 ?  169 LEU   B HD13 1 
ATOM   6704 H  HD21 A LEU   B 1 169 ? 26.690 -36.628 -13.985 0.66 28.94 ?  169 LEU   B HD21 1 
ATOM   6705 H  HD21 B LEU   B 1 169 ? 26.686 -36.652 -13.987 0.34 26.60 ?  169 LEU   B HD21 1 
ATOM   6706 H  HD22 A LEU   B 1 169 ? 27.507 -37.983 -13.848 0.66 28.94 ?  169 LEU   B HD22 1 
ATOM   6707 H  HD22 B LEU   B 1 169 ? 27.543 -37.980 -13.835 0.34 26.60 ?  169 LEU   B HD22 1 
ATOM   6708 H  HD23 A LEU   B 1 169 ? 27.275 -37.063 -12.574 0.66 28.94 ?  169 LEU   B HD23 1 
ATOM   6709 H  HD23 B LEU   B 1 169 ? 27.295 -37.044 -12.575 0.34 26.60 ?  169 LEU   B HD23 1 
HETATM 6710 S  S    B DMS   C 2 .   ? 12.465 5.552   6.235   0.34 14.87 ?  301 DMS   A S    1 
HETATM 6711 O  O    B DMS   C 2 .   ? 13.760 6.329   6.214   0.34 14.48 ?  301 DMS   A O    1 
HETATM 6712 C  C1   B DMS   C 2 .   ? 11.873 5.434   4.511   0.34 15.86 ?  301 DMS   A C1   1 
HETATM 6713 C  C2   B DMS   C 2 .   ? 11.163 6.615   6.954   0.34 16.04 ?  301 DMS   A C2   1 
HETATM 6714 H  H11  B DMS   C 2 .   ? 12.429 4.689   4.040   0.34 19.04 ?  301 DMS   A H11  1 
HETATM 6715 H  H12  B DMS   C 2 .   ? 10.864 5.211   4.564   0.34 19.04 ?  301 DMS   A H12  1 
HETATM 6716 H  H13  B DMS   C 2 .   ? 12.050 6.371   4.100   0.34 19.04 ?  301 DMS   A H13  1 
HETATM 6717 H  H21  B DMS   C 2 .   ? 10.270 6.268   6.564   0.34 19.26 ?  301 DMS   A H21  1 
HETATM 6718 H  H22  B DMS   C 2 .   ? 11.378 7.579   6.632   0.34 19.26 ?  301 DMS   A H22  1 
HETATM 6719 H  H23  B DMS   C 2 .   ? 11.206 6.526   7.993   0.34 19.26 ?  301 DMS   A H23  1 
HETATM 6720 N  N2   B A1A58 D 3 .   ? 13.918 -0.164  5.077   0.34 10.15 ?  302 A1A58 A N2   1 
HETATM 6721 C  C3   B A1A58 D 3 .   ? 13.704 -1.731  1.195   0.34 11.88 ?  302 A1A58 A C3   1 
HETATM 6722 C  C6   B A1A58 D 3 .   ? 14.300 0.558   4.003   0.34 9.82  ?  302 A1A58 A C6   1 
HETATM 6723 C  C9   B A1A58 D 3 .   ? 14.848 1.882   4.183   0.34 10.47 ?  302 A1A58 A C9   1 
HETATM 6724 C  C1   B A1A58 D 3 .   ? 15.105 -2.420  3.115   0.34 10.70 ?  302 A1A58 A C1   1 
HETATM 6725 C  C10  B A1A58 D 3 .   ? 15.382 3.028   3.439   0.34 11.06 ?  302 A1A58 A C10  1 
HETATM 6726 C  C11  B A1A58 D 3 .   ? 15.725 4.008   4.374   0.34 11.18 ?  302 A1A58 A C11  1 
HETATM 6727 C  C2   B A1A58 D 3 .   ? 13.888 -1.493  2.646   0.34 10.92 ?  302 A1A58 A C2   1 
HETATM 6728 C  C4   B A1A58 D 3 .   ? 14.378 -0.576  0.453   0.34 11.38 ?  302 A1A58 A C4   1 
HETATM 6729 C  C5   B A1A58 D 3 .   ? 14.513 0.569   1.480   0.34 10.92 ?  302 A1A58 A C5   1 
HETATM 6730 C  C7   B A1A58 D 3 .   ? 14.044 0.349   6.349   0.34 9.27  ?  302 A1A58 A C7   1 
HETATM 6731 C  C8   B A1A58 D 3 .   ? 14.921 2.273   5.562   0.34 10.47 ?  302 A1A58 A C8   1 
HETATM 6732 F  F1   B A1A58 D 3 .   ? 15.633 -0.988  0.048   0.34 11.63 ?  302 A1A58 A F1   1 
HETATM 6733 N  N1   B A1A58 D 3 .   ? 14.157 -0.050  2.781   0.34 10.31 ?  302 A1A58 A N1   1 
HETATM 6734 N  N3   B A1A58 D 3 .   ? 14.524 1.564   6.628   0.34 10.09 ?  302 A1A58 A N3   1 
HETATM 6735 N  N4   B A1A58 D 3 .   ? 15.449 3.512   5.600   0.34 10.78 ?  302 A1A58 A N4   1 
HETATM 6736 O  O1   B A1A58 D 3 .   ? 14.689 -3.758  3.149   0.34 11.10 ?  302 A1A58 A O1   1 
HETATM 6737 H  H7   B A1A58 D 3 .   ? 14.130 -2.691  0.924   0.34 14.27 ?  302 A1A58 A H7   1 
HETATM 6738 H  H6   B A1A58 D 3 .   ? 12.619 -1.785  0.932   0.34 14.27 ?  302 A1A58 A H6   1 
HETATM 6739 H  H5   B A1A58 D 3 .   ? 15.459 -2.088  4.103   0.34 12.85 ?  302 A1A58 A H5   1 
HETATM 6740 H  H4   B A1A58 D 3 .   ? 15.939 -2.306  2.378   0.34 12.85 ?  302 A1A58 A H4   1 
HETATM 6741 H  H11  B A1A58 D 3 .   ? 15.529 3.163   2.381   0.34 13.28 ?  302 A1A58 A H11  1 
HETATM 6742 H  H12  B A1A58 D 3 .   ? 16.165 5.013   4.321   0.34 13.42 ?  302 A1A58 A H12  1 
HETATM 6743 H  H1   B A1A58 D 3 .   ? 12.948 -1.753  3.209   0.34 13.11 ?  302 A1A58 A H1   1 
HETATM 6744 H  H2   B A1A58 D 3 .   ? 13.801 -0.230  -0.452  0.34 13.66 ?  302 A1A58 A H2   1 
HETATM 6745 H  H9   B A1A58 D 3 .   ? 13.811 1.404   1.198   0.34 13.12 ?  302 A1A58 A H9   1 
HETATM 6746 H  H8   B A1A58 D 3 .   ? 15.543 1.004   1.435   0.34 13.12 ?  302 A1A58 A H8   1 
HETATM 6747 H  H10  B A1A58 D 3 .   ? 13.708 -0.290  7.239   0.34 11.13 ?  302 A1A58 A H10  1 
HETATM 6748 H  H13  B A1A58 D 3 .   ? 15.596 4.054   6.504   0.34 12.94 ?  302 A1A58 A H13  1 
HETATM 6749 H  H3   B A1A58 D 3 .   ? 14.333 -3.976  4.040   0.34 13.33 ?  302 A1A58 A H3   1 
HETATM 6750 CL CL   B CL    E 4 .   ? 15.632 2.948   -1.005  0.34 11.35 ?  303 CL    A CL   1 
HETATM 6751 O  O    B HOH   F 5 .   ? 19.048 2.081   1.051   0.34 44.41 ?  401 HOH   A O    1 
HETATM 6752 O  O    . HOH   F 5 .   ? 14.780 -4.817  20.501  1.00 42.68 ?  402 HOH   A O    1 
HETATM 6753 O  O    . HOH   F 5 .   ? -0.643 -8.643  2.209   1.00 43.61 ?  403 HOH   A O    1 
HETATM 6754 O  O    . HOH   F 5 .   ? 18.567 -2.451  -16.352 1.00 43.66 ?  404 HOH   A O    1 
HETATM 6755 O  O    . HOH   F 5 .   ? 12.125 0.236   14.888  1.00 34.09 ?  405 HOH   A O    1 
HETATM 6756 O  O    . HOH   F 5 .   ? 11.649 -10.812 -9.959  1.00 42.33 ?  406 HOH   A O    1 
HETATM 6757 O  O    . HOH   F 5 .   ? 4.806  3.955   0.699   1.00 28.11 ?  407 HOH   A O    1 
HETATM 6758 O  O    B HOH   F 5 .   ? 8.432  0.013   -1.418  0.34 20.46 ?  408 HOH   A O    1 
HETATM 6759 O  O    . HOH   F 5 .   ? 15.185 -12.296 18.740  1.00 45.22 ?  409 HOH   A O    1 
HETATM 6760 O  O    . HOH   F 5 .   ? 34.418 -1.859  12.527  1.00 39.51 ?  410 HOH   A O    1 
HETATM 6761 O  O    . HOH   F 5 .   ? 26.826 11.369  1.665   1.00 16.15 ?  411 HOH   A O    1 
HETATM 6762 O  O    . HOH   F 5 .   ? 19.015 -22.036 6.935   1.00 32.64 ?  412 HOH   A O    1 
HETATM 6763 O  O    . HOH   F 5 .   ? 9.134  -10.092 19.401  1.00 41.09 ?  413 HOH   A O    1 
HETATM 6764 O  O    . HOH   F 5 .   ? 0.785  -4.794  0.234   1.00 32.65 ?  414 HOH   A O    1 
HETATM 6765 O  O    . HOH   F 5 .   ? 28.919 0.443   -9.721  1.00 23.07 ?  415 HOH   A O    1 
HETATM 6766 O  O    B HOH   F 5 .   ? 18.382 -1.896  0.521   0.34 12.10 ?  416 HOH   A O    1 
HETATM 6767 O  O    . HOH   F 5 .   ? 28.632 -10.560 -14.066 1.00 39.37 ?  417 HOH   A O    1 
HETATM 6768 O  O    . HOH   F 5 .   ? 7.678  -6.250  -6.449  1.00 39.84 ?  418 HOH   A O    1 
HETATM 6769 O  O    . HOH   F 5 .   ? 14.459 -24.703 11.619  1.00 33.89 ?  419 HOH   A O    1 
HETATM 6770 O  O    . HOH   F 5 .   ? 28.341 -6.291  19.563  1.00 39.93 ?  420 HOH   A O    1 
HETATM 6771 O  O    B HOH   F 5 .   ? 15.788 5.349   7.821   0.34 14.77 ?  421 HOH   A O    1 
HETATM 6772 O  O    . HOH   F 5 .   ? 7.993  -12.777 -0.862  1.00 20.86 ?  422 HOH   A O    1 
HETATM 6773 O  O    . HOH   F 5 .   ? 30.283 -13.307 -8.432  1.00 24.32 ?  423 HOH   A O    1 
HETATM 6774 O  O    . HOH   F 5 .   ? 42.419 10.551  5.092   1.00 20.07 ?  424 HOH   A O    1 
HETATM 6775 O  O    . HOH   F 5 .   ? 30.820 6.231   -12.260 1.00 28.64 ?  425 HOH   A O    1 
HETATM 6776 O  O    . HOH   F 5 .   ? 17.264 -18.131 15.137  1.00 27.22 ?  426 HOH   A O    1 
HETATM 6777 O  O    A HOH   F 5 .   ? 14.313 0.516   6.849   0.66 30.76 ?  427 HOH   A O    1 
HETATM 6778 O  O    A HOH   F 5 .   ? 3.656  -9.538  9.793   0.66 32.61 ?  428 HOH   A O    1 
HETATM 6779 O  O    . HOH   F 5 .   ? 36.214 -5.066  -0.488  1.00 28.28 ?  429 HOH   A O    1 
HETATM 6780 O  O    . HOH   F 5 .   ? 6.770  -3.515  13.012  1.00 31.73 ?  430 HOH   A O    1 
HETATM 6781 O  O    . HOH   F 5 .   ? 17.086 -19.355 4.950   1.00 14.60 ?  431 HOH   A O    1 
HETATM 6782 O  O    . HOH   F 5 .   ? 14.937 3.738   17.758  1.00 34.29 ?  432 HOH   A O    1 
HETATM 6783 O  O    . HOH   F 5 .   ? 37.516 2.817   10.268  1.00 24.00 ?  433 HOH   A O    1 
HETATM 6784 O  O    B HOH   F 5 .   ? 19.196 -0.413  -2.054  0.34 12.61 ?  434 HOH   A O    1 
HETATM 6785 O  O    . HOH   F 5 .   ? 38.237 10.203  7.077   1.00 44.30 ?  435 HOH   A O    1 
HETATM 6786 O  O    . HOH   F 5 .   ? 19.966 -12.644 -8.811  1.00 25.90 ?  436 HOH   A O    1 
HETATM 6787 O  O    . HOH   F 5 .   ? 14.117 -4.586  -11.792 1.00 30.64 ?  437 HOH   A O    1 
HETATM 6788 O  O    . HOH   F 5 .   ? 11.068 1.465   12.845  1.00 23.92 ?  438 HOH   A O    1 
HETATM 6789 O  O    . HOH   F 5 .   ? 14.753 -14.000 16.723  1.00 28.10 ?  439 HOH   A O    1 
HETATM 6790 O  O    . HOH   F 5 .   ? 26.548 -19.360 -1.781  1.00 13.90 ?  440 HOH   A O    1 
HETATM 6791 O  O    . HOH   F 5 .   ? 28.309 -0.146  -13.361 1.00 35.93 ?  441 HOH   A O    1 
HETATM 6792 O  O    . HOH   F 5 .   ? 31.089 -18.167 7.817   1.00 18.83 ?  442 HOH   A O    1 
HETATM 6793 O  O    . HOH   F 5 .   ? 21.291 -2.426  -2.181  1.00 14.58 ?  443 HOH   A O    1 
HETATM 6794 O  O    . HOH   F 5 .   ? 34.012 -1.099  -8.923  1.00 26.44 ?  444 HOH   A O    1 
HETATM 6795 O  O    . HOH   F 5 .   ? 27.905 0.802   -7.140  1.00 14.42 ?  445 HOH   A O    1 
HETATM 6796 O  O    B HOH   F 5 .   ? 15.177 8.000   4.649   0.34 20.81 ?  446 HOH   A O    1 
HETATM 6797 O  O    . HOH   F 5 .   ? 22.316 -19.340 11.392  1.00 32.37 ?  447 HOH   A O    1 
HETATM 6798 O  O    . HOH   F 5 .   ? 27.357 13.736  2.826   1.00 31.19 ?  448 HOH   A O    1 
HETATM 6799 O  O    . HOH   F 5 .   ? 13.324 -1.480  -6.543  1.00 17.09 ?  449 HOH   A O    1 
HETATM 6800 O  O    . HOH   F 5 .   ? 18.757 -19.418 13.592  1.00 34.49 ?  450 HOH   A O    1 
HETATM 6801 O  O    . HOH   F 5 .   ? 38.579 5.008   7.013   1.00 15.20 ?  451 HOH   A O    1 
HETATM 6802 O  O    . HOH   F 5 .   ? 14.164 -23.136 7.446   1.00 18.74 ?  452 HOH   A O    1 
HETATM 6803 O  O    . HOH   F 5 .   ? 31.655 8.248   14.788  1.00 23.63 ?  453 HOH   A O    1 
HETATM 6804 O  O    . HOH   F 5 .   ? 22.774 12.479  1.639   1.00 14.51 ?  454 HOH   A O    1 
HETATM 6805 O  O    A HOH   F 5 .   ? 7.008  -8.233  11.905  0.66 20.07 ?  455 HOH   A O    1 
HETATM 6806 O  O    . HOH   F 5 .   ? 22.389 5.324   19.078  1.00 43.14 ?  456 HOH   A O    1 
HETATM 6807 O  O    . HOH   F 5 .   ? 15.325 -21.647 14.265  1.00 18.25 ?  457 HOH   A O    1 
HETATM 6808 O  O    . HOH   F 5 .   ? 20.659 -19.794 -5.066  1.00 26.81 ?  458 HOH   A O    1 
HETATM 6809 O  O    . HOH   F 5 .   ? -0.441 -3.191  3.118   1.00 43.78 ?  459 HOH   A O    1 
HETATM 6810 O  O    . HOH   F 5 .   ? 25.731 -0.859  -7.351  1.00 15.54 ?  460 HOH   A O    1 
HETATM 6811 O  O    . HOH   F 5 .   ? 44.332 7.125   6.406   1.00 26.68 ?  461 HOH   A O    1 
HETATM 6812 O  O    . HOH   F 5 .   ? 22.677 -12.001 21.877  1.00 50.08 ?  462 HOH   A O    1 
HETATM 6813 O  O    . HOH   F 5 .   ? 35.836 -12.687 6.821   1.00 15.75 ?  463 HOH   A O    1 
HETATM 6814 O  O    . HOH   F 5 .   ? 42.544 4.250   5.412   1.00 34.88 ?  464 HOH   A O    1 
HETATM 6815 O  O    . HOH   F 5 .   ? 18.598 9.372   9.078   1.00 20.52 ?  465 HOH   A O    1 
HETATM 6816 O  O    B HOH   F 5 .   ? 21.238 2.683   -0.041  0.34 14.47 ?  466 HOH   A O    1 
HETATM 6817 O  O    . HOH   F 5 .   ? 39.774 -1.021  -5.187  1.00 19.94 ?  467 HOH   A O    1 
HETATM 6818 O  O    . HOH   F 5 .   ? 37.280 11.955  4.915   1.00 29.56 ?  468 HOH   A O    1 
HETATM 6819 O  O    . HOH   F 5 .   ? 14.409 -21.272 -4.273  1.00 27.56 ?  469 HOH   A O    1 
HETATM 6820 O  O    . HOH   F 5 .   ? 9.919  -21.435 5.739   1.00 18.36 ?  470 HOH   A O    1 
HETATM 6821 O  O    . HOH   F 5 .   ? 13.537 -15.300 -7.479  1.00 28.03 ?  471 HOH   A O    1 
HETATM 6822 O  O    . HOH   F 5 .   ? 15.549 12.005  7.857   1.00 35.25 ?  472 HOH   A O    1 
HETATM 6823 O  O    . HOH   F 5 .   ? 24.067 -2.160  -2.082  1.00 11.03 ?  473 HOH   A O    1 
HETATM 6824 O  O    . HOH   F 5 .   ? 43.356 7.795   2.632   1.00 32.56 ?  474 HOH   A O    1 
HETATM 6825 O  O    . HOH   F 5 .   ? 17.204 -17.848 -5.027  1.00 26.25 ?  475 HOH   A O    1 
HETATM 6826 O  O    . HOH   F 5 .   ? 33.701 -7.183  4.310   1.00 16.41 ?  476 HOH   A O    1 
HETATM 6827 O  O    . HOH   F 5 .   ? 8.346  -21.561 4.011   1.00 46.25 ?  477 HOH   A O    1 
HETATM 6828 O  O    A HOH   F 5 .   ? 17.524 -1.762  0.484   0.66 18.97 ?  478 HOH   A O    1 
HETATM 6829 O  O    . HOH   F 5 .   ? 30.832 3.059   8.296   1.00 12.16 ?  479 HOH   A O    1 
HETATM 6830 O  O    . HOH   F 5 .   ? 31.863 -9.379  -6.633  1.00 24.42 ?  480 HOH   A O    1 
HETATM 6831 O  O    . HOH   F 5 .   ? 14.039 -4.997  17.580  1.00 24.30 ?  481 HOH   A O    1 
HETATM 6832 O  O    . HOH   F 5 .   ? 37.257 -2.882  9.745   1.00 44.52 ?  482 HOH   A O    1 
HETATM 6833 O  O    B HOH   F 5 .   ? 10.661 6.493   10.715  0.34 20.29 ?  483 HOH   A O    1 
HETATM 6834 O  O    . HOH   F 5 .   ? 31.149 -13.959 -2.433  1.00 13.76 ?  484 HOH   A O    1 
HETATM 6835 O  O    A HOH   F 5 .   ? 20.103 4.504   -7.504  0.66 20.61 ?  485 HOH   A O    1 
HETATM 6836 O  O    . HOH   F 5 .   ? 14.531 -0.567  -11.987 1.00 24.50 ?  486 HOH   A O    1 
HETATM 6837 O  O    . HOH   F 5 .   ? 27.562 -10.633 14.076  1.00 16.70 ?  487 HOH   A O    1 
HETATM 6838 O  O    A HOH   F 5 .   ? 14.671 -3.709  3.143   0.66 20.99 ?  488 HOH   A O    1 
HETATM 6839 O  O    . HOH   F 5 .   ? 21.265 10.357  14.983  1.00 33.39 ?  489 HOH   A O    1 
HETATM 6840 O  O    . HOH   F 5 .   ? 21.911 -21.938 8.386   1.00 28.76 ?  490 HOH   A O    1 
HETATM 6841 O  O    . HOH   F 5 .   ? 24.391 3.522   -1.812  1.00 14.75 ?  491 HOH   A O    1 
HETATM 6842 O  O    B HOH   F 5 .   ? 10.887 0.100   2.619   0.34 14.31 ?  492 HOH   A O    1 
HETATM 6843 O  O    . HOH   F 5 .   ? 19.679 -11.239 24.049  1.00 72.67 ?  493 HOH   A O    1 
HETATM 6844 O  O    . HOH   F 5 .   ? 31.873 -7.237  -9.798  1.00 21.49 ?  494 HOH   A O    1 
HETATM 6845 O  O    . HOH   F 5 .   ? 24.798 -17.572 12.761  1.00 23.49 ?  495 HOH   A O    1 
HETATM 6846 O  O    . HOH   F 5 .   ? 24.340 -7.815  14.492  1.00 16.39 ?  496 HOH   A O    1 
HETATM 6847 O  O    . HOH   F 5 .   ? 43.928 8.540   -3.056  1.00 28.33 ?  497 HOH   A O    1 
HETATM 6848 O  O    . HOH   F 5 .   ? 37.570 -2.064  5.817   1.00 27.47 ?  498 HOH   A O    1 
HETATM 6849 O  O    . HOH   F 5 .   ? 27.420 -6.063  -13.968 1.00 36.11 ?  499 HOH   A O    1 
HETATM 6850 O  O    . HOH   F 5 .   ? 32.824 -9.294  5.947   1.00 19.79 ?  500 HOH   A O    1 
HETATM 6851 O  O    . HOH   F 5 .   ? 16.571 -22.123 1.076   1.00 27.27 ?  501 HOH   A O    1 
HETATM 6852 O  O    A HOH   F 5 .   ? 15.837 -1.000  5.316   0.66 37.81 ?  502 HOH   A O    1 
HETATM 6853 O  O    . HOH   F 5 .   ? 30.698 1.873   16.725  1.00 20.64 ?  503 HOH   A O    1 
HETATM 6854 O  O    . HOH   F 5 .   ? 26.931 4.134   -0.636  1.00 12.50 ?  504 HOH   A O    1 
HETATM 6855 O  O    . HOH   F 5 .   ? 15.793 2.123   24.754  1.00 47.88 ?  505 HOH   A O    1 
HETATM 6856 O  O    . HOH   F 5 .   ? 20.603 -20.075 2.823   1.00 18.05 ?  506 HOH   A O    1 
HETATM 6857 O  O    . HOH   F 5 .   ? 15.162 -8.113  -9.717  1.00 24.07 ?  507 HOH   A O    1 
HETATM 6858 O  O    . HOH   F 5 .   ? 23.456 11.348  4.109   1.00 12.20 ?  508 HOH   A O    1 
HETATM 6859 O  O    . HOH   F 5 .   ? 24.591 1.942   -6.999  1.00 19.70 ?  509 HOH   A O    1 
HETATM 6860 O  O    . HOH   F 5 .   ? 27.342 2.296   18.717  1.00 30.54 ?  510 HOH   A O    1 
HETATM 6861 O  O    . HOH   F 5 .   ? 24.087 3.890   -4.829  1.00 23.88 ?  511 HOH   A O    1 
HETATM 6862 O  O    . HOH   F 5 .   ? -1.612 -5.096  7.757   1.00 38.31 ?  512 HOH   A O    1 
HETATM 6863 O  O    A HOH   F 5 .   ? 21.368 3.113   -0.311  0.66 10.57 ?  513 HOH   A O    1 
HETATM 6864 O  O    . HOH   F 5 .   ? 30.132 -10.129 13.011  1.00 22.45 ?  514 HOH   A O    1 
HETATM 6865 O  O    . HOH   F 5 .   ? 16.272 16.704  8.725   1.00 33.20 ?  515 HOH   A O    1 
HETATM 6866 O  O    B HOH   F 5 .   ? 22.651 5.742   -1.791  0.34 15.76 ?  516 HOH   A O    1 
HETATM 6867 O  O    . HOH   F 5 .   ? 5.029  2.509   5.124   1.00 31.19 ?  517 HOH   A O    1 
HETATM 6868 O  O    . HOH   F 5 .   ? 21.815 -13.926 -8.086  1.00 43.55 ?  518 HOH   A O    1 
HETATM 6869 O  O    . HOH   F 5 .   ? 35.140 -5.240  -3.107  1.00 17.42 ?  519 HOH   A O    1 
HETATM 6870 O  O    . HOH   F 5 .   ? 38.076 -1.337  -1.931  1.00 19.46 ?  520 HOH   A O    1 
HETATM 6871 O  O    . HOH   F 5 .   ? 32.566 -10.662 3.217   1.00 30.40 ?  521 HOH   A O    1 
HETATM 6872 O  O    . HOH   F 5 .   ? 10.489 -22.210 -1.247  1.00 58.86 ?  522 HOH   A O    1 
HETATM 6873 O  O    . HOH   F 5 .   ? 24.003 -20.320 -1.334  1.00 16.19 ?  523 HOH   A O    1 
HETATM 6874 O  O    A HOH   F 5 .   ? 11.096 -0.438  1.989   0.66 20.73 ?  524 HOH   A O    1 
HETATM 6875 O  O    . HOH   F 5 .   ? 30.419 -12.944 13.549  1.00 20.14 ?  525 HOH   A O    1 
HETATM 6876 O  O    . HOH   F 5 .   ? 11.813 -10.827 17.051  1.00 26.09 ?  526 HOH   A O    1 
HETATM 6877 O  O    . HOH   F 5 .   ? 40.951 -8.259  -6.802  1.00 34.63 ?  527 HOH   A O    1 
HETATM 6878 O  O    . HOH   F 5 .   ? 41.623 1.485   5.011   1.00 38.22 ?  528 HOH   A O    1 
HETATM 6879 O  O    A HOH   F 5 .   ? 6.521  -5.677  11.238  0.66 19.84 ?  529 HOH   A O    1 
HETATM 6880 O  O    A HOH   F 5 .   ? 18.981 -0.714  -1.586  0.66 11.02 ?  530 HOH   A O    1 
HETATM 6881 O  O    . HOH   F 5 .   ? 32.713 -4.382  -9.898  1.00 27.48 ?  531 HOH   A O    1 
HETATM 6882 O  O    . HOH   F 5 .   ? 36.753 -5.032  5.409   1.00 23.77 ?  532 HOH   A O    1 
HETATM 6883 O  O    . HOH   F 5 .   ? 23.847 -15.803 -9.140  1.00 33.30 ?  533 HOH   A O    1 
HETATM 6884 O  O    . HOH   F 5 .   ? 10.448 -13.836 -1.684  1.00 17.46 ?  534 HOH   A O    1 
HETATM 6885 O  O    . HOH   F 5 .   ? 22.646 8.112   18.357  1.00 39.49 ?  535 HOH   A O    1 
HETATM 6886 O  O    . HOH   F 5 .   ? 45.002 -0.557  2.957   1.00 44.27 ?  536 HOH   A O    1 
HETATM 6887 O  O    . HOH   F 5 .   ? 16.339 -14.294 20.264  1.00 48.23 ?  537 HOH   A O    1 
HETATM 6888 O  O    . HOH   F 5 .   ? 27.070 -3.227  19.375  1.00 34.13 ?  538 HOH   A O    1 
HETATM 6889 O  O    . HOH   F 5 .   ? 21.372 -9.264  21.325  1.00 48.13 ?  539 HOH   A O    1 
HETATM 6890 O  O    A HOH   F 5 .   ? 18.884 1.988   -0.709  0.66 11.32 ?  540 HOH   A O    1 
HETATM 6891 O  O    . HOH   F 5 .   ? 9.425  -12.381 17.434  1.00 53.36 ?  541 HOH   A O    1 
HETATM 6892 O  O    B HOH   F 5 .   ? 11.934 -1.722  -2.464  0.34 13.03 ?  542 HOH   A O    1 
HETATM 6893 O  O    A HOH   F 5 .   ? 16.038 6.903   3.041   0.66 14.97 ?  543 HOH   A O    1 
HETATM 6894 O  O    . HOH   F 5 .   ? 23.604 -8.048  17.102  1.00 21.30 ?  544 HOH   A O    1 
HETATM 6895 O  O    . HOH   F 5 .   ? 20.640 -17.771 24.824  1.00 49.31 ?  545 HOH   A O    1 
HETATM 6896 O  O    . HOH   F 5 .   ? 37.771 -8.819  -3.415  1.00 22.27 ?  546 HOH   A O    1 
HETATM 6897 O  O    A HOH   F 5 .   ? 9.431  -16.384 -1.937  0.66 37.70 ?  547 HOH   A O    1 
HETATM 6898 O  O    . HOH   F 5 .   ? 23.440 -20.988 1.318   1.00 18.71 ?  548 HOH   A O    1 
HETATM 6899 O  O    . HOH   F 5 .   ? 30.575 14.746  2.810   1.00 18.86 ?  549 HOH   A O    1 
HETATM 6900 O  O    . HOH   F 5 .   ? 34.491 -8.069  -0.527  1.00 28.02 ?  550 HOH   A O    1 
HETATM 6901 O  O    . HOH   F 5 .   ? 18.506 4.885   -15.043 1.00 51.96 ?  551 HOH   A O    1 
HETATM 6902 O  O    A HOH   F 5 .   ? 16.276 2.899   -1.393  0.66 19.07 ?  552 HOH   A O    1 
HETATM 6903 O  O    . HOH   F 5 .   ? 18.487 -16.136 16.341  1.00 37.37 ?  553 HOH   A O    1 
HETATM 6904 O  O    . HOH   F 5 .   ? 23.290 7.642   -3.198  1.00 25.58 ?  554 HOH   A O    1 
HETATM 6905 O  O    . HOH   F 5 .   ? 31.385 -12.833 0.081   1.00 19.34 ?  555 HOH   A O    1 
HETATM 6906 O  O    A HOH   F 5 .   ? 14.060 -0.394  3.511   0.66 33.14 ?  556 HOH   A O    1 
HETATM 6907 O  O    . HOH   F 5 .   ? 21.679 -14.860 17.931  1.00 53.07 ?  557 HOH   A O    1 
HETATM 6908 O  O    . HOH   F 5 .   ? 27.746 7.054   -6.444  1.00 36.47 ?  558 HOH   A O    1 
HETATM 6909 O  O    . HOH   F 5 .   ? 29.799 -2.014  -12.704 1.00 49.65 ?  559 HOH   A O    1 
HETATM 6910 O  O    . HOH   F 5 .   ? 30.020 -16.189 10.805  1.00 33.76 ?  560 HOH   A O    1 
HETATM 6911 O  O    . HOH   F 5 .   ? 32.474 -16.022 10.862  1.00 33.53 ?  561 HOH   A O    1 
HETATM 6912 O  O    . HOH   F 5 .   ? 25.435 8.269   -4.817  1.00 23.94 ?  562 HOH   A O    1 
HETATM 6913 O  O    . HOH   F 5 .   ? 19.945 -17.389 -5.033  1.00 23.89 ?  563 HOH   A O    1 
HETATM 6914 O  O    . HOH   F 5 .   ? 24.828 5.645   20.752  1.00 51.97 ?  564 HOH   A O    1 
HETATM 6915 O  O    . HOH   F 5 .   ? 23.308 -22.390 -3.327  1.00 35.67 ?  565 HOH   A O    1 
HETATM 6916 O  O    B HOH   F 5 .   ? 13.142 -3.134  -0.929  0.34 36.14 ?  566 HOH   A O    1 
HETATM 6917 O  O    . HOH   F 5 .   ? 24.587 14.602  7.828   1.00 36.63 ?  567 HOH   A O    1 
HETATM 6918 O  O    . HOH   F 5 .   ? 26.955 11.580  -1.231  1.00 30.55 ?  568 HOH   A O    1 
HETATM 6919 O  O    . HOH   F 5 .   ? 15.812 -21.616 3.754   1.00 21.80 ?  569 HOH   A O    1 
HETATM 6920 O  O    B HOH   F 5 .   ? 18.284 2.078   -1.029  0.34 11.35 ?  570 HOH   A O    1 
HETATM 6921 O  O    . HOH   F 5 .   ? 39.722 -7.035  -3.506  1.00 47.29 ?  571 HOH   A O    1 
HETATM 6922 O  O    B HOH   F 5 .   ? 16.278 7.905   8.614   0.34 16.80 ?  572 HOH   A O    1 
HETATM 6923 O  O    . HOH   F 5 .   ? 18.766 10.807  11.379  1.00 31.15 ?  573 HOH   A O    1 
HETATM 6924 O  O    A HOH   F 5 .   ? 21.971 5.229   -5.797  0.66 26.20 ?  574 HOH   A O    1 
HETATM 6925 O  O    . HOH   F 5 .   ? 27.612 -11.403 16.579  1.00 38.35 ?  575 HOH   A O    1 
HETATM 6926 O  O    B HOH   F 5 .   ? 6.975  -1.712  -3.492  0.34 30.53 ?  576 HOH   A O    1 
HETATM 6927 O  O    . HOH   F 5 .   ? 25.887 10.799  -3.626  1.00 23.07 ?  577 HOH   A O    1 
HETATM 6928 O  O    . HOH   F 5 .   ? 23.465 13.672  5.601   1.00 19.21 ?  578 HOH   A O    1 
HETATM 6929 O  O    . HOH   F 5 .   ? 12.275 1.648   17.373  1.00 39.38 ?  579 HOH   A O    1 
HETATM 6930 O  O    . HOH   F 5 .   ? 12.033 -13.517 16.512  1.00 52.43 ?  580 HOH   A O    1 
HETATM 6931 O  O    . HOH   F 5 .   ? 11.094 -15.059 -6.096  1.00 34.66 ?  581 HOH   A O    1 
HETATM 6932 O  O    B HOH   F 5 .   ? 11.443 2.837   2.473   0.34 16.11 ?  582 HOH   A O    1 
HETATM 6933 O  O    . HOH   F 5 .   ? 28.762 9.014   17.476  1.00 34.40 ?  583 HOH   A O    1 
HETATM 6934 O  O    . HOH   F 5 .   ? 23.228 11.897  -3.993  1.00 20.26 ?  584 HOH   A O    1 
HETATM 6935 O  O    . HOH   F 5 .   ? 16.831 -20.605 16.208  1.00 29.15 ?  585 HOH   A O    1 
HETATM 6936 O  O    . HOH   F 5 .   ? 35.192 7.487   12.207  1.00 49.67 ?  586 HOH   A O    1 
HETATM 6937 O  O    . HOH   F 5 .   ? 18.222 -16.310 -8.800  1.00 41.75 ?  587 HOH   A O    1 
HETATM 6938 O  O    . HOH   F 5 .   ? 41.052 -3.981  -0.361  1.00 38.04 ?  588 HOH   A O    1 
HETATM 6939 O  O    B HOH   F 5 .   ? 15.910 9.891   6.502   0.34 21.97 ?  589 HOH   A O    1 
HETATM 6940 O  O    B HOH   F 5 .   ? 10.861 -1.266  -5.050  0.34 14.49 ?  590 HOH   A O    1 
HETATM 6941 O  O    . HOH   F 5 .   ? 30.963 0.715   19.117  1.00 41.45 ?  591 HOH   A O    1 
HETATM 6942 O  O    . HOH   F 5 .   ? 23.276 -12.917 19.359  1.00 53.06 ?  592 HOH   A O    1 
HETATM 6943 O  O    . HOH   F 5 .   ? 15.722 -17.292 -6.974  1.00 32.10 ?  593 HOH   A O    1 
HETATM 6944 O  O    . HOH   F 5 .   ? 28.618 -4.747  -12.305 1.00 39.43 ?  594 HOH   A O    1 
HETATM 6945 O  O    . HOH   F 5 .   ? 13.996 -10.302 -10.856 1.00 33.55 ?  595 HOH   A O    1 
HETATM 6946 O  O    . HOH   F 5 .   ? 17.423 -18.783 19.717  1.00 48.06 ?  596 HOH   A O    1 
HETATM 6947 O  O    . HOH   F 5 .   ? 44.434 10.457  -1.698  1.00 34.18 ?  597 HOH   A O    1 
HETATM 6948 O  O    . HOH   F 5 .   ? 15.994 -6.856  -11.710 1.00 43.00 ?  598 HOH   A O    1 
HETATM 6949 O  O    . HOH   F 5 .   ? 16.200 -23.448 5.777   1.00 28.71 ?  599 HOH   A O    1 
HETATM 6950 O  O    . HOH   F 5 .   ? 20.125 -22.390 4.229   1.00 31.04 ?  600 HOH   A O    1 
HETATM 6951 O  O    . HOH   F 5 .   ? 41.720 9.477   -3.920  1.00 30.91 ?  601 HOH   A O    1 
HETATM 6952 O  O    B HOH   F 5 .   ? 8.841  2.501   -2.783  0.34 19.95 ?  602 HOH   A O    1 
HETATM 6953 O  O    . HOH   F 5 .   ? 39.237 2.348   7.447   1.00 30.97 ?  603 HOH   A O    1 
HETATM 6954 O  O    . HOH   F 5 .   ? 14.101 -25.409 8.918   1.00 34.13 ?  604 HOH   A O    1 
HETATM 6955 O  O    . HOH   F 5 .   ? 18.560 -23.286 1.965   1.00 45.83 ?  605 HOH   A O    1 
HETATM 6956 O  O    . HOH   F 5 .   ? 30.743 5.818   -14.726 1.00 35.84 ?  606 HOH   A O    1 
HETATM 6957 O  O    . HOH   F 5 .   ? 28.809 -7.918  -15.188 1.00 44.75 ?  607 HOH   A O    1 
HETATM 6958 O  O    . HOH   F 5 .   ? 31.506 -0.617  -10.558 1.00 25.35 ?  608 HOH   A O    1 
HETATM 6959 O  O    B HOH   F 5 .   ? 12.529 2.608   -0.436  0.34 14.62 ?  609 HOH   A O    1 
HETATM 6960 O  O    . HOH   F 5 .   ? 40.485 -0.300  -7.876  1.00 32.12 ?  610 HOH   A O    1 
HETATM 6961 O  O    B HOH   F 5 .   ? 11.036 0.030   -0.462  0.34 14.52 ?  611 HOH   A O    1 
HETATM 6962 O  O    B HOH   F 5 .   ? 8.890  4.016   1.693   0.34 20.32 ?  612 HOH   A O    1 
HETATM 6963 O  O    . HOH   F 5 .   ? 30.752 -5.832  -11.835 1.00 47.40 ?  613 HOH   A O    1 
HETATM 6964 O  O    . HOH   F 5 .   ? 28.929 14.403  0.958   1.00 50.16 ?  614 HOH   A O    1 
HETATM 6965 O  O    . HOH   F 5 .   ? 20.621 -16.090 -7.349  1.00 29.62 ?  615 HOH   A O    1 
HETATM 6966 O  O    . HOH   F 5 .   ? 37.498 -6.629  7.586   1.00 25.30 ?  616 HOH   A O    1 
HETATM 6967 O  O    . HOH   F 5 .   ? 8.289  -2.956  -5.589  1.00 48.25 ?  617 HOH   A O    1 
HETATM 6968 O  O    . HOH   F 5 .   ? 23.216 -23.816 1.635   1.00 32.59 ?  618 HOH   A O    1 
HETATM 6969 O  O    . HOH   F 5 .   ? 39.604 -0.056  6.571   1.00 28.71 ?  619 HOH   A O    1 
HETATM 6970 O  O    B HOH   F 5 .   ? 10.098 1.355   -5.021  0.34 17.15 ?  620 HOH   A O    1 
HETATM 6971 O  O    . HOH   F 5 .   ? 38.032 13.979  6.620   1.00 40.77 ?  621 HOH   A O    1 
HETATM 6972 O  O    . HOH   F 5 .   ? 22.136 -24.099 4.517   1.00 26.32 ?  622 HOH   A O    1 
HETATM 6973 O  O    . HOH   F 5 .   ? 36.533 -6.507  10.224  1.00 44.96 ?  623 HOH   A O    1 
HETATM 6974 O  O    . HOH   F 5 .   ? 17.496 -6.867  -14.063 1.00 39.85 ?  624 HOH   A O    1 
HETATM 6975 O  O    B HOH   F 5 .   ? 9.962  3.982   -0.637  0.34 19.01 ?  625 HOH   A O    1 
HETATM 6976 O  O    A HOH   F 5 .   ? 14.873 8.595   4.944   0.66 26.63 ?  626 HOH   A O    1 
HETATM 6977 O  O    . HOH   F 5 .   ? 24.122 9.068   -7.183  1.00 36.70 ?  627 HOH   A O    1 
HETATM 6978 O  O    . HOH   F 5 .   ? 16.344 -21.201 18.825  1.00 35.38 ?  628 HOH   A O    1 
HETATM 6979 O  O    . HOH   F 5 .   ? 15.851 -12.311 27.462  1.00 44.42 ?  629 HOH   A O    1 
HETATM 6980 O  O    B HOH   F 5 .   ? 6.052  6.872   1.640   0.34 24.53 ?  630 HOH   A O    1 
HETATM 6981 O  O    B HOH   F 5 .   ? 8.688  7.153   2.267   0.34 24.28 ?  631 HOH   A O    1 
HETATM 6982 O  O    B HOH   F 5 .   ? 5.803  6.827   4.506   0.34 20.73 ?  632 HOH   A O    1 
HETATM 6983 O  O    . HOH   F 5 .   ? 14.636 -22.763 19.879  1.00 34.55 ?  633 HOH   A O    1 
HETATM 6984 O  O    . HOH   G 5 .   ? 29.945 -22.455 5.510   1.00 19.23 ?  201 HOH   B O    1 
HETATM 6985 O  O    . HOH   G 5 .   ? 27.923 -41.678 -15.169 1.00 34.97 ?  202 HOH   B O    1 
HETATM 6986 O  O    . HOH   G 5 .   ? 27.767 -29.177 -1.877  1.00 33.99 ?  203 HOH   B O    1 
HETATM 6987 O  O    . HOH   G 5 .   ? 41.670 -35.979 -17.317 1.00 32.86 ?  204 HOH   B O    1 
HETATM 6988 O  O    . HOH   G 5 .   ? 59.207 -18.683 6.825   1.00 36.53 ?  205 HOH   B O    1 
HETATM 6989 O  O    . HOH   G 5 .   ? 38.119 -39.468 -0.265  1.00 43.30 ?  206 HOH   B O    1 
HETATM 6990 O  O    . HOH   G 5 .   ? 30.066 -26.312 4.143   1.00 26.26 ?  207 HOH   B O    1 
HETATM 6991 O  O    . HOH   G 5 .   ? 53.016 -13.449 -20.305 1.00 34.81 ?  208 HOH   B O    1 
HETATM 6992 O  O    . HOH   G 5 .   ? 49.348 -22.797 -19.809 1.00 45.73 ?  209 HOH   B O    1 
HETATM 6993 O  O    . HOH   G 5 .   ? 41.351 -7.834  5.490   1.00 38.19 ?  210 HOH   B O    1 
HETATM 6994 O  O    . HOH   G 5 .   ? 30.233 -40.981 -8.155  1.00 16.85 ?  211 HOH   B O    1 
HETATM 6995 O  O    . HOH   G 5 .   ? 48.122 -6.957  15.504  1.00 30.82 ?  212 HOH   B O    1 
HETATM 6996 O  O    . HOH   G 5 .   ? 54.503 -9.443  -8.732  1.00 19.34 ?  213 HOH   B O    1 
HETATM 6997 O  O    . HOH   G 5 .   ? 50.281 -3.417  7.083   1.00 35.98 ?  214 HOH   B O    1 
HETATM 6998 O  O    . HOH   G 5 .   ? 56.448 -19.791 6.989   1.00 29.25 ?  215 HOH   B O    1 
HETATM 6999 O  O    . HOH   G 5 .   ? 58.310 -13.000 8.332   1.00 29.04 ?  216 HOH   B O    1 
HETATM 7000 O  O    . HOH   G 5 .   ? 57.790 -24.463 5.016   1.00 38.74 ?  217 HOH   B O    1 
HETATM 7001 O  O    . HOH   G 5 .   ? 44.530 -7.103  1.956   1.00 35.49 ?  218 HOH   B O    1 
HETATM 7002 O  O    . HOH   G 5 .   ? 57.159 -26.905 -7.602  1.00 37.86 ?  219 HOH   B O    1 
HETATM 7003 O  O    . HOH   G 5 .   ? 50.856 -6.122  0.131   1.00 25.93 ?  220 HOH   B O    1 
HETATM 7004 O  O    . HOH   G 5 .   ? 55.356 -16.494 -14.371 1.00 30.30 ?  221 HOH   B O    1 
HETATM 7005 O  O    . HOH   G 5 .   ? 56.757 -30.778 -7.807  1.00 28.66 ?  222 HOH   B O    1 
HETATM 7006 O  O    . HOH   G 5 .   ? 34.563 -36.393 -7.224  1.00 18.96 ?  223 HOH   B O    1 
HETATM 7007 O  O    . HOH   G 5 .   ? 41.537 -39.155 -15.005 1.00 21.48 ?  224 HOH   B O    1 
HETATM 7008 O  O    . HOH   G 5 .   ? 47.484 -7.315  -3.857  1.00 44.83 ?  225 HOH   B O    1 
HETATM 7009 O  O    . HOH   G 5 .   ? 40.603 -16.117 14.043  1.00 23.55 ?  226 HOH   B O    1 
HETATM 7010 O  O    . HOH   G 5 .   ? 29.874 -34.171 -0.409  1.00 33.66 ?  227 HOH   B O    1 
HETATM 7011 O  O    . HOH   G 5 .   ? 57.402 -16.279 -12.284 1.00 18.79 ?  228 HOH   B O    1 
HETATM 7012 O  O    . HOH   G 5 .   ? 32.746 -43.716 -11.398 1.00 21.98 ?  229 HOH   B O    1 
HETATM 7013 O  O    . HOH   G 5 .   ? 44.991 -43.534 -10.627 1.00 26.70 ?  230 HOH   B O    1 
HETATM 7014 O  O    . HOH   G 5 .   ? 30.492 -42.247 -10.633 1.00 28.65 ?  231 HOH   B O    1 
HETATM 7015 O  O    . HOH   G 5 .   ? 41.463 -9.645  13.001  1.00 22.18 ?  232 HOH   B O    1 
HETATM 7016 O  O    . HOH   G 5 .   ? 39.395 -10.881 6.095   1.00 24.58 ?  233 HOH   B O    1 
HETATM 7017 O  O    . HOH   G 5 .   ? 46.419 -1.616  13.206  1.00 27.72 ?  234 HOH   B O    1 
HETATM 7018 O  O    . HOH   G 5 .   ? 51.745 -6.516  4.349   1.00 20.07 ?  235 HOH   B O    1 
HETATM 7019 O  O    . HOH   G 5 .   ? 43.077 -43.239 -8.280  1.00 28.57 ?  236 HOH   B O    1 
HETATM 7020 O  O    . HOH   G 5 .   ? 31.053 -28.796 4.354   1.00 27.62 ?  237 HOH   B O    1 
HETATM 7021 O  O    . HOH   G 5 .   ? 48.544 -36.543 -15.638 1.00 43.14 ?  238 HOH   B O    1 
HETATM 7022 O  O    . HOH   G 5 .   ? 50.817 -13.005 -0.482  1.00 11.72 ?  239 HOH   B O    1 
HETATM 7023 O  O    . HOH   G 5 .   ? 38.509 -11.088 -2.252  1.00 18.42 ?  240 HOH   B O    1 
HETATM 7024 O  O    . HOH   G 5 .   ? 37.113 -19.691 -18.165 1.00 43.95 ?  241 HOH   B O    1 
HETATM 7025 O  O    . HOH   G 5 .   ? 35.000 -24.657 13.806  1.00 32.19 ?  242 HOH   B O    1 
HETATM 7026 O  O    . HOH   G 5 .   ? 35.169 -8.021  -3.001  1.00 18.57 ?  243 HOH   B O    1 
HETATM 7027 O  O    . HOH   G 5 .   ? 44.590 -27.767 -0.700  1.00 20.60 ?  244 HOH   B O    1 
HETATM 7028 O  O    . HOH   G 5 .   ? 57.676 -24.394 -3.839  1.00 20.74 ?  245 HOH   B O    1 
HETATM 7029 O  O    . HOH   G 5 .   ? 58.246 -10.660 -4.041  1.00 19.63 ?  246 HOH   B O    1 
HETATM 7030 O  O    . HOH   G 5 .   ? 25.443 -25.947 -1.348  1.00 32.68 ?  247 HOH   B O    1 
HETATM 7031 O  O    . HOH   G 5 .   ? 40.406 -12.774 -11.495 1.00 15.22 ?  248 HOH   B O    1 
HETATM 7032 O  O    . HOH   G 5 .   ? 42.725 -22.890 3.849   1.00 11.81 ?  249 HOH   B O    1 
HETATM 7033 O  O    . HOH   G 5 .   ? 45.226 -35.072 6.826   1.00 38.37 ?  250 HOH   B O    1 
HETATM 7034 O  O    . HOH   G 5 .   ? 39.047 -12.013 12.319  1.00 34.17 ?  251 HOH   B O    1 
HETATM 7035 O  O    . HOH   G 5 .   ? 41.950 -23.552 9.298   1.00 17.90 ?  252 HOH   B O    1 
HETATM 7036 O  O    . HOH   G 5 .   ? 28.448 -19.657 -13.140 1.00 24.44 ?  253 HOH   B O    1 
HETATM 7037 O  O    . HOH   G 5 .   ? 28.530 -30.876 -14.777 1.00 30.06 ?  254 HOH   B O    1 
HETATM 7038 O  O    . HOH   G 5 .   ? 42.644 -25.385 2.644   1.00 14.44 ?  255 HOH   B O    1 
HETATM 7039 O  O    . HOH   G 5 .   ? 43.179 -32.383 -17.163 1.00 24.44 ?  256 HOH   B O    1 
HETATM 7040 O  O    . HOH   G 5 .   ? 39.603 -11.150 0.294   1.00 16.53 ?  257 HOH   B O    1 
HETATM 7041 O  O    . HOH   G 5 .   ? 36.073 -43.362 -8.485  1.00 38.46 ?  258 HOH   B O    1 
HETATM 7042 O  O    . HOH   G 5 .   ? 33.611 -17.033 8.080   1.00 18.92 ?  259 HOH   B O    1 
HETATM 7043 O  O    . HOH   G 5 .   ? 34.421 -18.423 11.496  1.00 25.67 ?  260 HOH   B O    1 
HETATM 7044 O  O    . HOH   G 5 .   ? 34.930 -33.231 -19.261 1.00 30.89 ?  261 HOH   B O    1 
HETATM 7045 O  O    . HOH   G 5 .   ? 30.935 -15.770 2.689   1.00 13.68 ?  262 HOH   B O    1 
HETATM 7046 O  O    . HOH   G 5 .   ? 29.753 -25.197 -10.783 1.00 16.16 ?  263 HOH   B O    1 
HETATM 7047 O  O    . HOH   G 5 .   ? 51.609 -13.830 10.986  1.00 27.99 ?  264 HOH   B O    1 
HETATM 7048 O  O    . HOH   G 5 .   ? 51.032 -39.957 -8.364  1.00 33.82 ?  265 HOH   B O    1 
HETATM 7049 O  O    . HOH   G 5 .   ? 42.770 -20.249 -20.671 1.00 36.53 ?  266 HOH   B O    1 
HETATM 7050 O  O    . HOH   G 5 .   ? 57.574 -9.260  1.374   1.00 19.38 ?  267 HOH   B O    1 
HETATM 7051 O  O    . HOH   G 5 .   ? 31.842 -17.960 -14.518 1.00 30.42 ?  268 HOH   B O    1 
HETATM 7052 O  O    . HOH   G 5 .   ? 49.356 -28.729 -6.990  1.00 15.68 ?  269 HOH   B O    1 
HETATM 7053 O  O    . HOH   G 5 .   ? 48.117 -22.805 5.831   1.00 17.45 ?  270 HOH   B O    1 
HETATM 7054 O  O    . HOH   G 5 .   ? 43.453 -15.807 -12.189 1.00 14.20 ?  271 HOH   B O    1 
HETATM 7055 O  O    . HOH   G 5 .   ? 42.470 -9.978  9.268   1.00 20.56 ?  272 HOH   B O    1 
HETATM 7056 O  O    . HOH   G 5 .   ? 57.029 -8.659  8.395   1.00 19.73 ?  273 HOH   B O    1 
HETATM 7057 O  O    . HOH   G 5 .   ? 27.172 -31.810 -9.969  1.00 20.35 ?  274 HOH   B O    1 
HETATM 7058 O  O    . HOH   G 5 .   ? 46.644 -31.277 -4.878  1.00 23.56 ?  275 HOH   B O    1 
HETATM 7059 O  O    . HOH   G 5 .   ? 46.934 -29.583 9.796   1.00 29.95 ?  276 HOH   B O    1 
HETATM 7060 O  O    . HOH   G 5 .   ? 34.550 -12.813 2.652   1.00 24.06 ?  277 HOH   B O    1 
HETATM 7061 O  O    . HOH   G 5 .   ? 57.213 -12.057 12.265  1.00 37.53 ?  278 HOH   B O    1 
HETATM 7062 O  O    . HOH   G 5 .   ? 56.222 -23.526 -14.807 1.00 27.19 ?  279 HOH   B O    1 
HETATM 7063 O  O    . HOH   G 5 .   ? 42.506 -34.681 3.801   1.00 25.33 ?  280 HOH   B O    1 
HETATM 7064 O  O    . HOH   G 5 .   ? 27.648 -26.771 -15.691 1.00 33.72 ?  281 HOH   B O    1 
HETATM 7065 O  O    . HOH   G 5 .   ? 28.309 -34.326 -9.416  1.00 19.12 ?  282 HOH   B O    1 
HETATM 7066 O  O    . HOH   G 5 .   ? 48.486 -25.077 3.107   1.00 13.56 ?  283 HOH   B O    1 
HETATM 7067 O  O    . HOH   G 5 .   ? 27.994 -22.897 -7.968  1.00 16.95 ?  284 HOH   B O    1 
HETATM 7068 O  O    . HOH   G 5 .   ? 36.871 -12.790 -1.506  1.00 27.70 ?  285 HOH   B O    1 
HETATM 7069 O  O    . HOH   G 5 .   ? 51.645 -6.014  -7.986  1.00 40.10 ?  286 HOH   B O    1 
HETATM 7070 O  O    . HOH   G 5 .   ? 52.616 -10.420 12.952  1.00 22.76 ?  287 HOH   B O    1 
HETATM 7071 O  O    . HOH   G 5 .   ? 49.768 -0.466  10.194  1.00 31.31 ?  288 HOH   B O    1 
HETATM 7072 O  O    . HOH   G 5 .   ? 45.352 -33.364 -16.042 1.00 24.65 ?  289 HOH   B O    1 
HETATM 7073 O  O    . HOH   G 5 .   ? 48.788 -20.054 5.915   1.00 14.21 ?  290 HOH   B O    1 
HETATM 7074 O  O    . HOH   G 5 .   ? 33.586 -15.247 -13.957 1.00 21.32 ?  291 HOH   B O    1 
HETATM 7075 O  O    . HOH   G 5 .   ? 47.134 -33.998 -4.715  1.00 18.87 ?  292 HOH   B O    1 
HETATM 7076 O  O    . HOH   G 5 .   ? 47.846 -24.486 -17.896 1.00 33.22 ?  293 HOH   B O    1 
HETATM 7077 O  O    . HOH   G 5 .   ? 26.016 -21.514 -3.450  1.00 16.17 ?  294 HOH   B O    1 
HETATM 7078 O  O    . HOH   G 5 .   ? 59.883 -15.303 8.139   1.00 28.53 ?  295 HOH   B O    1 
HETATM 7079 O  O    . HOH   G 5 .   ? 35.212 -33.674 4.557   1.00 31.36 ?  296 HOH   B O    1 
HETATM 7080 O  O    . HOH   G 5 .   ? 51.250 -37.570 -9.786  1.00 24.28 ?  297 HOH   B O    1 
HETATM 7081 O  O    . HOH   G 5 .   ? 41.190 -5.499  11.480  1.00 43.13 ?  298 HOH   B O    1 
HETATM 7082 O  O    . HOH   G 5 .   ? 38.407 -12.189 -16.270 1.00 44.87 ?  299 HOH   B O    1 
HETATM 7083 O  O    . HOH   G 5 .   ? 42.759 -12.183 -18.450 1.00 27.58 ?  300 HOH   B O    1 
HETATM 7084 O  O    . HOH   G 5 .   ? 44.686 -27.505 1.999   1.00 15.23 ?  301 HOH   B O    1 
HETATM 7085 O  O    . HOH   G 5 .   ? 53.479 -30.255 4.496   1.00 18.50 ?  302 HOH   B O    1 
HETATM 7086 O  O    . HOH   G 5 .   ? 52.650 -35.636 -8.830  1.00 30.52 ?  303 HOH   B O    1 
HETATM 7087 O  O    . HOH   G 5 .   ? 62.886 -20.164 -0.844  1.00 41.98 ?  304 HOH   B O    1 
HETATM 7088 O  O    . HOH   G 5 .   ? 40.309 -10.859 -9.483  1.00 17.31 ?  305 HOH   B O    1 
HETATM 7089 O  O    . HOH   G 5 .   ? 37.933 -10.241 -10.711 1.00 17.42 ?  306 HOH   B O    1 
HETATM 7090 O  O    . HOH   G 5 .   ? 52.546 -29.240 -13.147 1.00 24.36 ?  307 HOH   B O    1 
HETATM 7091 O  O    . HOH   G 5 .   ? 32.878 -34.604 -5.893  1.00 17.03 ?  308 HOH   B O    1 
HETATM 7092 O  O    . HOH   G 5 .   ? 44.110 -29.377 -4.694  1.00 22.82 ?  309 HOH   B O    1 
HETATM 7093 O  O    . HOH   G 5 .   ? 45.924 -40.447 -3.687  1.00 30.35 ?  310 HOH   B O    1 
HETATM 7094 O  O    . HOH   G 5 .   ? 37.540 -18.077 13.172  1.00 31.50 ?  311 HOH   B O    1 
HETATM 7095 O  O    . HOH   G 5 .   ? 43.321 -21.450 10.691  1.00 15.46 ?  312 HOH   B O    1 
HETATM 7096 O  O    . HOH   G 5 .   ? 41.812 -8.107  1.388   1.00 23.55 ?  313 HOH   B O    1 
HETATM 7097 O  O    . HOH   G 5 .   ? 28.892 -42.836 -12.340 1.00 43.29 ?  314 HOH   B O    1 
HETATM 7098 O  O    . HOH   G 5 .   ? 53.133 -16.040 -12.769 1.00 27.34 ?  315 HOH   B O    1 
HETATM 7099 O  O    . HOH   G 5 .   ? 43.250 -34.508 -0.011  1.00 22.22 ?  316 HOH   B O    1 
HETATM 7100 O  O    . HOH   G 5 .   ? 37.382 -35.685 7.317   1.00 35.24 ?  317 HOH   B O    1 
HETATM 7101 O  O    . HOH   G 5 .   ? 38.403 -12.737 7.948   1.00 17.27 ?  318 HOH   B O    1 
HETATM 7102 O  O    . HOH   G 5 .   ? 62.800 -13.592 4.706   1.00 26.75 ?  319 HOH   B O    1 
HETATM 7103 O  O    . HOH   G 5 .   ? 26.394 -21.073 -6.213  1.00 15.81 ?  320 HOH   B O    1 
HETATM 7104 O  O    . HOH   G 5 .   ? 37.098 -30.516 -21.070 1.00 29.97 ?  321 HOH   B O    1 
HETATM 7105 O  O    . HOH   G 5 .   ? 50.061 -24.654 5.891   1.00 36.36 ?  322 HOH   B O    1 
HETATM 7106 O  O    . HOH   G 5 .   ? 38.441 -9.375  -13.247 1.00 30.85 ?  323 HOH   B O    1 
HETATM 7107 O  O    . HOH   G 5 .   ? 48.068 -32.686 -16.741 1.00 44.67 ?  324 HOH   B O    1 
HETATM 7108 O  O    . HOH   G 5 .   ? 53.690 -12.585 -22.243 1.00 31.35 ?  325 HOH   B O    1 
HETATM 7109 O  O    . HOH   G 5 .   ? 42.414 -9.772  -14.898 1.00 35.22 ?  326 HOH   B O    1 
HETATM 7110 O  O    . HOH   G 5 .   ? 45.734 -36.315 -16.164 1.00 38.07 ?  327 HOH   B O    1 
HETATM 7111 O  O    . HOH   G 5 .   ? 44.718 -24.623 9.586   1.00 20.25 ?  328 HOH   B O    1 
HETATM 7112 O  O    . HOH   G 5 .   ? 36.828 -12.426 4.326   1.00 18.21 ?  329 HOH   B O    1 
HETATM 7113 O  O    . HOH   G 5 .   ? 33.778 -31.161 11.113  1.00 36.99 ?  330 HOH   B O    1 
HETATM 7114 O  O    . HOH   G 5 .   ? 47.316 -24.503 8.161   1.00 24.82 ?  331 HOH   B O    1 
HETATM 7115 O  O    . HOH   G 5 .   ? 43.564 -15.421 18.116  1.00 31.98 ?  332 HOH   B O    1 
HETATM 7116 O  O    . HOH   G 5 .   ? 48.648 -12.022 -14.149 1.00 27.18 ?  333 HOH   B O    1 
HETATM 7117 O  O    . HOH   G 5 .   ? 59.956 -17.291 -10.590 1.00 36.12 ?  334 HOH   B O    1 
HETATM 7118 O  O    . HOH   G 5 .   ? 51.512 -33.081 -11.012 1.00 43.52 ?  335 HOH   B O    1 
HETATM 7119 O  O    . HOH   G 5 .   ? 57.627 -22.015 3.270   1.00 29.62 ?  336 HOH   B O    1 
HETATM 7120 O  O    . HOH   G 5 .   ? 42.912 -43.538 -14.432 1.00 42.41 ?  337 HOH   B O    1 
HETATM 7121 O  O    . HOH   G 5 .   ? 44.199 -1.698  7.650   1.00 45.43 ?  338 HOH   B O    1 
HETATM 7122 O  O    . HOH   G 5 .   ? 47.539 -27.451 1.999   1.00 15.18 ?  339 HOH   B O    1 
HETATM 7123 O  O    . HOH   G 5 .   ? 41.447 -24.578 15.847  1.00 44.54 ?  340 HOH   B O    1 
HETATM 7124 O  O    . HOH   G 5 .   ? 27.738 -14.737 -9.532  1.00 39.19 ?  341 HOH   B O    1 
HETATM 7125 O  O    . HOH   G 5 .   ? 37.098 -15.107 -16.519 1.00 39.37 ?  342 HOH   B O    1 
HETATM 7126 O  O    . HOH   G 5 .   ? 46.956 -19.951 12.235  1.00 31.05 ?  343 HOH   B O    1 
HETATM 7127 O  O    . HOH   G 5 .   ? 39.637 -23.559 -20.345 1.00 39.06 ?  344 HOH   B O    1 
HETATM 7128 O  O    . HOH   G 5 .   ? 37.054 -45.162 -9.741  1.00 35.83 ?  345 HOH   B O    1 
HETATM 7129 O  O    . HOH   G 5 .   ? 34.572 -10.398 7.665   1.00 22.20 ?  346 HOH   B O    1 
HETATM 7130 O  O    . HOH   G 5 .   ? 33.074 -14.683 1.055   1.00 19.04 ?  347 HOH   B O    1 
HETATM 7131 O  O    . HOH   G 5 .   ? 39.861 -44.170 -11.280 1.00 43.27 ?  348 HOH   B O    1 
HETATM 7132 O  O    . HOH   G 5 .   ? 33.612 -9.926  -8.727  1.00 30.60 ?  349 HOH   B O    1 
HETATM 7133 O  O    . HOH   G 5 .   ? 38.634 -22.353 15.032  1.00 44.17 ?  350 HOH   B O    1 
HETATM 7134 O  O    . HOH   G 5 .   ? 40.396 -43.467 -9.201  1.00 27.07 ?  351 HOH   B O    1 
HETATM 7135 O  O    . HOH   G 5 .   ? 44.220 -37.453 -17.939 1.00 35.29 ?  352 HOH   B O    1 
HETATM 7136 O  O    . HOH   G 5 .   ? 55.705 -8.247  10.773  1.00 24.71 ?  353 HOH   B O    1 
HETATM 7137 O  O    . HOH   G 5 .   ? 62.572 -20.140 -4.936  1.00 43.25 ?  354 HOH   B O    1 
HETATM 7138 O  O    . HOH   G 5 .   ? 27.848 -26.680 -0.557  1.00 29.31 ?  355 HOH   B O    1 
HETATM 7139 O  O    . HOH   G 5 .   ? 23.364 -23.698 6.830   1.00 34.09 ?  356 HOH   B O    1 
HETATM 7140 O  O    . HOH   G 5 .   ? 34.019 -7.911  11.508  1.00 41.33 ?  357 HOH   B O    1 
HETATM 7141 O  O    . HOH   G 5 .   ? 56.697 -7.307  2.997   1.00 28.27 ?  358 HOH   B O    1 
HETATM 7142 O  O    . HOH   G 5 .   ? 36.238 -8.466  -9.690  1.00 34.55 ?  359 HOH   B O    1 
HETATM 7143 O  O    . HOH   G 5 .   ? 43.205 -12.726 -21.182 1.00 39.23 ?  360 HOH   B O    1 
HETATM 7144 O  O    . HOH   G 5 .   ? 61.606 -19.918 1.644   1.00 34.66 ?  361 HOH   B O    1 
HETATM 7145 O  O    . HOH   G 5 .   ? 56.911 -21.569 -16.452 1.00 41.39 ?  362 HOH   B O    1 
HETATM 7146 O  O    . HOH   G 5 .   ? 27.207 -25.934 -11.348 1.00 33.03 ?  363 HOH   B O    1 
HETATM 7147 O  O    . HOH   G 5 .   ? 40.294 -8.878  9.879   1.00 34.96 ?  364 HOH   B O    1 
HETATM 7148 O  O    . HOH   G 5 .   ? 40.378 -11.322 -13.857 1.00 31.82 ?  365 HOH   B O    1 
HETATM 7149 O  O    . HOH   G 5 .   ? 48.401 -26.502 8.771   1.00 41.36 ?  366 HOH   B O    1 
HETATM 7150 O  O    . HOH   G 5 .   ? 54.291 -5.736  2.919   1.00 39.07 ?  367 HOH   B O    1 
HETATM 7151 O  O    . HOH   G 5 .   ? 59.099 -10.550 9.138   1.00 41.38 ?  368 HOH   B O    1 
HETATM 7152 O  O    . HOH   G 5 .   ? 32.639 -23.588 14.028  1.00 42.14 ?  369 HOH   B O    1 
HETATM 7153 O  O    . HOH   G 5 .   ? 36.295 -8.745  8.907   1.00 34.02 ?  370 HOH   B O    1 
HETATM 7154 O  O    . HOH   G 5 .   ? 39.885 -7.131  7.811   1.00 41.22 ?  371 HOH   B O    1 
HETATM 7155 O  O    . HOH   G 5 .   ? 41.866 -10.010 -17.442 1.00 57.59 ?  372 HOH   B O    1 
HETATM 7156 O  O    . HOH   G 5 .   ? 56.035 -7.805  -0.595  1.00 36.54 ?  373 HOH   B O    1 
HETATM 7157 O  O    . HOH   G 5 .   ? 52.062 -12.921 13.335  1.00 30.02 ?  374 HOH   B O    1 
HETATM 7158 O  O    . HOH   G 5 .   ? 63.085 -12.398 6.980   1.00 37.16 ?  375 HOH   B O    1 
HETATM 7159 O  O    . HOH   G 5 .   ? 42.756 -17.196 -23.145 1.00 41.93 ?  376 HOH   B O    1 
HETATM 7160 O  O    . HOH   G 5 .   ? 41.852 -6.795  -4.895  1.00 49.24 ?  377 HOH   B O    1 
HETATM 7161 O  O    . HOH   G 5 .   ? 38.102 -10.559 10.027  1.00 28.65 ?  378 HOH   B O    1 
HETATM 7162 O  O    . HOH   G 5 .   ? 36.585 -22.899 13.277  1.00 26.10 ?  379 HOH   B O    1 
HETATM 7163 O  O    . HOH   G 5 .   ? 40.250 -7.685  3.116   1.00 42.47 ?  380 HOH   B O    1 
HETATM 7164 O  O    . HOH   G 5 .   ? 39.715 -14.144 15.627  1.00 50.36 ?  381 HOH   B O    1 
HETATM 7165 O  O    . HOH   G 5 .   ? 44.055 -5.576  -3.506  1.00 39.49 ?  382 HOH   B O    1 
HETATM 7166 O  O    . HOH   G 5 .   ? 60.508 -22.284 2.821   1.00 48.49 ?  383 HOH   B O    1 
HETATM 7167 O  O    . HOH   G 5 .   ? 52.884 -29.944 7.151   1.00 22.75 ?  384 HOH   B O    1 
HETATM 7168 O  O    . HOH   G 5 .   ? 23.945 -20.868 -7.612  1.00 28.75 ?  385 HOH   B O    1 
HETATM 7169 O  O    . HOH   G 5 .   ? 25.859 -18.942 -11.917 1.00 38.20 ?  386 HOH   B O    1 
HETATM 7170 O  O    . HOH   G 5 .   ? 46.859 -5.333  2.929   1.00 41.47 ?  387 HOH   B O    1 
HETATM 7171 O  O    . HOH   G 5 .   ? 41.034 -9.724  15.796  1.00 46.38 ?  388 HOH   B O    1 
HETATM 7172 O  O    . HOH   G 5 .   ? 35.484 -33.760 7.402   1.00 41.57 ?  389 HOH   B O    1 
HETATM 7173 O  O    . HOH   G 5 .   ? 35.383 -20.425 13.358  1.00 31.96 ?  390 HOH   B O    1 
HETATM 7174 O  O    . HOH   G 5 .   ? 40.780 -6.641  -0.810  1.00 25.42 ?  391 HOH   B O    1 
HETATM 7175 O  O    . HOH   G 5 .   ? 44.165 -31.752 -3.905  1.00 35.88 ?  392 HOH   B O    1 
HETATM 7176 O  O    . HOH   G 5 .   ? 28.079 -27.107 2.311   1.00 30.21 ?  393 HOH   B O    1 
HETATM 7177 O  O    . HOH   G 5 .   ? 26.656 -27.928 -13.404 1.00 37.29 ?  394 HOH   B O    1 
HETATM 7178 O  O    . HOH   G 5 .   ? 24.636 -20.664 -10.399 1.00 38.82 ?  395 HOH   B O    1 
HETATM 7179 O  O    . HOH   G 5 .   ? 50.676 -30.898 8.685   1.00 29.31 ?  396 HOH   B O    1 
HETATM 7180 O  O    . HOH   G 5 .   ? 34.447 -33.522 9.596   1.00 35.40 ?  397 HOH   B O    1 
HETATM 7181 O  O    . HOH   G 5 .   ? 26.852 -30.608 -12.655 1.00 26.79 ?  398 HOH   B O    1 
HETATM 7182 O  O    . HOH   G 5 .   ? 45.803 -20.112 15.250  1.00 41.69 ?  399 HOH   B O    1 
HETATM 7183 O  O    . HOH   G 5 .   ? 57.540 -6.372  -2.302  1.00 31.31 ?  400 HOH   B O    1 
HETATM 7184 O  O    . HOH   G 5 .   ? 40.839 -11.836 -22.288 1.00 44.43 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   A VAL   A 3   ? 0.7256 0.7178 0.7942 -0.0017 -0.0162 0.0789  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.7219 0.7166 0.7701 -0.0028 -0.0179 0.0604  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.7220 0.7153 0.7859 -0.0027 -0.0158 0.0786  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.7186 0.7139 0.7639 -0.0036 -0.0176 0.0614  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.7020 0.6999 0.7568 -0.0060 -0.0200 0.0791  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.7005 0.6989 0.7433 -0.0068 -0.0207 0.0693  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.7047 0.7033 0.7706 -0.0045 -0.0210 0.0818  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.7037 0.7020 0.7546 -0.0058 -0.0216 0.0703  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.7348 0.7253 0.7975 -0.0012 -0.0116 0.0775  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.7298 0.7233 0.7712 -0.0019 -0.0145 0.0556  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.7393 0.7283 0.7997 -0.0004 -0.0102 0.0767  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.7337 0.7263 0.7723 -0.0012 -0.0134 0.0534  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.7388 0.7289 0.7997 -0.0010 -0.0099 0.0779  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.7333 0.7265 0.7722 -0.0014 -0.0134 0.0540  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.6755 0.6780 0.7023 -0.0113 -0.0217 0.0759  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.6203 0.6316 0.5989 -0.0213 -0.0207 0.0765  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.5461 0.5743 0.5208 -0.0358 -0.0029 0.0507  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.5481 0.5766 0.5185 -0.0389 -0.0006 0.0582  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.6342 0.6391 0.5646 -0.0183 -0.0351 0.1015  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.6437 0.6437 0.5311 -0.0164 -0.0510 0.1228  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.6482 0.6468 0.5222 -0.0161 -0.0600 0.1278  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.6459 0.6435 0.5232 -0.0146 -0.0551 0.1338  4   ASN   A ND2 
46   N  N   A SER   A 5   ? 0.5029 0.5443 0.4748 -0.0475 0.0106  0.0348  5   SER   A N   
47   N  N   B SER   A 5   ? 0.5099 0.5402 0.4831 -0.0370 0.0014  0.0340  5   SER   A N   
48   C  CA  A SER   A 5   ? 0.4568 0.5122 0.4253 -0.0594 0.0312  0.0180  5   SER   A CA  
49   C  CA  B SER   A 5   ? 0.4706 0.5041 0.4420 -0.0386 0.0094  0.0178  5   SER   A CA  
50   C  C   A SER   A 5   ? 0.4022 0.4676 0.3691 -0.0698 0.0520  0.0080  5   SER   A C   
51   C  C   B SER   A 5   ? 0.4249 0.4602 0.3900 -0.0396 0.0171  0.0056  5   SER   A C   
52   O  O   A SER   A 5   ? 0.4088 0.4733 0.3624 -0.0627 0.0556  -0.0037 5   SER   A O   
53   O  O   B SER   A 5   ? 0.4271 0.4619 0.3864 -0.0375 0.0184  0.0012  5   SER   A O   
54   C  CB  A SER   A 5   ? 0.4634 0.5221 0.4432 -0.0613 0.0313  0.0129  5   SER   A CB  
55   C  CB  B SER   A 5   ? 0.4756 0.5104 0.4583 -0.0393 0.0094  0.0147  5   SER   A CB  
56   O  OG  A SER   A 5   ? 0.4664 0.5273 0.4491 -0.0630 0.0314  0.0093  5   SER   A OG  
57   O  OG  B SER   A 5   ? 0.4779 0.5139 0.4650 -0.0399 0.0084  0.0122  5   SER   A OG  
68   N  N   A PHE   A 6   ? 0.3377 0.4154 0.3077 -0.0889 0.0735  0.0106  6   PHE   A N   
69   N  N   B PHE   A 6   ? 0.3752 0.4137 0.3394 -0.0431 0.0243  -0.0021 6   PHE   A N   
70   C  CA  A PHE   A 6   ? 0.2800 0.3611 0.2573 -0.1002 0.0786  0.0225  6   PHE   A CA  
71   C  CA  B PHE   A 6   ? 0.3275 0.3667 0.2953 -0.0450 0.0300  -0.0053 6   PHE   A CA  
72   C  C   A PHE   A 6   ? 0.2714 0.3553 0.2701 -0.1052 0.0871  0.0139  6   PHE   A C   
73   C  C   B PHE   A 6   ? 0.3114 0.3484 0.2973 -0.0464 0.0370  -0.0059 6   PHE   A C   
74   O  O   A PHE   A 6   ? 0.2709 0.3600 0.3105 -0.1106 0.0859  0.0230  6   PHE   A O   
75   O  O   B PHE   A 6   ? 0.3132 0.3501 0.3214 -0.0471 0.0358  -0.0048 6   PHE   A O   
76   C  CB  A PHE   A 6   ? 0.2458 0.3165 0.2181 -0.0932 0.0589  0.0303  6   PHE   A CB  
77   C  CB  B PHE   A 6   ? 0.2990 0.3389 0.2559 -0.0434 0.0302  -0.0116 6   PHE   A CB  
78   C  CG  A PHE   A 6   ? 0.2195 0.2825 0.1892 -0.0801 0.0398  0.0312  6   PHE   A CG  
79   C  CG  B PHE   A 6   ? 0.2750 0.3131 0.2275 -0.0418 0.0276  -0.0169 6   PHE   A CG  
80   C  CD1 A PHE   A 6   ? 0.2043 0.2716 0.1691 -0.0692 0.0283  0.0314  6   PHE   A CD1 
81   C  CD1 B PHE   A 6   ? 0.2635 0.3027 0.2094 -0.0413 0.0245  -0.0162 6   PHE   A CD1 
82   C  CD2 A PHE   A 6   ? 0.2249 0.2703 0.2133 -0.0598 0.0329  0.0351  6   PHE   A CD2 
83   C  CD2 B PHE   A 6   ? 0.2695 0.3014 0.2286 -0.0368 0.0295  -0.0207 6   PHE   A CD2 
84   C  CE1 A PHE   A 6   ? 0.2007 0.2636 0.1808 -0.0664 0.0137  0.0392  6   PHE   A CE1 
85   C  CE1 B PHE   A 6   ? 0.2575 0.2942 0.2064 -0.0417 0.0274  -0.0137 6   PHE   A CE1 
86   C  CE2 A PHE   A 6   ? 0.2194 0.2651 0.2182 -0.0511 0.0217  0.0379  6   PHE   A CE2 
87   C  CE2 B PHE   A 6   ? 0.2627 0.2927 0.2220 -0.0359 0.0303  -0.0194 6   PHE   A CE2 
88   C  CZ  A PHE   A 6   ? 0.2085 0.2590 0.1944 -0.0607 0.0162  0.0390  6   PHE   A CZ  
89   C  CZ  B PHE   A 6   ? 0.2576 0.2909 0.2093 -0.0396 0.0298  -0.0165 6   PHE   A CZ  
108  N  N   A SER   A 7   ? 0.2537 0.3377 0.2474 -0.1074 0.0976  0.0016  7   SER   A N   
109  N  N   B SER   A 7   ? 0.2911 0.3281 0.2740 -0.0471 0.0418  -0.0106 7   SER   A N   
110  C  CA  A SER   A 7   ? 0.2589 0.3298 0.2655 -0.0943 0.0896  -0.0215 7   SER   A CA  
111  C  CA  B SER   A 7   ? 0.2778 0.3091 0.2656 -0.0461 0.0468  -0.0137 7   SER   A CA  
112  C  C   A SER   A 7   ? 0.2403 0.3002 0.2559 -0.0937 0.0900  -0.0239 7   SER   A C   
113  C  C   B SER   A 7   ? 0.2571 0.2872 0.2579 -0.0426 0.0516  -0.0161 7   SER   A C   
114  O  O   A SER   A 7   ? 0.2507 0.2955 0.2545 -0.1024 0.0873  -0.0170 7   SER   A O   
115  O  O   B SER   A 7   ? 0.2595 0.2852 0.2588 -0.0415 0.0486  -0.0159 7   SER   A O   
116  C  CB  A SER   A 7   ? 0.2807 0.3488 0.2934 -0.0797 0.0842  -0.0271 7   SER   A CB  
117  C  CB  B SER   A 7   ? 0.2866 0.3100 0.2736 -0.0458 0.0450  -0.0155 7   SER   A CB  
118  O  OG  A SER   A 7   ? 0.2956 0.3614 0.3168 -0.0690 0.0745  -0.0347 7   SER   A OG  
119  O  OG  B SER   A 7   ? 0.2935 0.3122 0.2735 -0.0434 0.0421  -0.0190 7   SER   A OG  
130  N  N   A GLY   A 8   ? 0.2191 0.2774 0.2574 -0.0836 0.0837  -0.0309 8   GLY   A N   
131  N  N   B GLY   A 8   ? 0.2373 0.2683 0.2518 -0.0403 0.0568  -0.0219 8   GLY   A N   
132  C  CA  A GLY   A 8   ? 0.2039 0.2573 0.2675 -0.0631 0.0808  -0.0336 8   GLY   A CA  
133  C  CA  B GLY   A 8   ? 0.2195 0.2495 0.2479 -0.0337 0.0578  -0.0233 8   GLY   A CA  
134  C  C   A GLY   A 8   ? 0.1864 0.2447 0.2561 -0.0478 0.0681  -0.0337 8   GLY   A C   
135  C  C   B GLY   A 8   ? 0.2027 0.2344 0.2317 -0.0289 0.0500  -0.0262 8   GLY   A C   
136  O  O   A GLY   A 8   ? 0.1886 0.2427 0.2896 -0.0371 0.0628  -0.0454 8   GLY   A O   
137  O  O   B GLY   A 8   ? 0.2037 0.2333 0.2515 -0.0235 0.0526  -0.0343 8   GLY   A O   
144  N  N   A TYR   A 9   ? 0.1725 0.2336 0.2391 -0.0352 0.0483  -0.0142 9   TYR   A N   
145  N  N   B TYR   A 9   ? 0.1844 0.2207 0.2139 -0.0234 0.0358  -0.0170 9   TYR   A N   
146  C  CA  A TYR   A 9   ? 0.1619 0.2177 0.2106 -0.0271 0.0309  -0.0031 9   TYR   A CA  
147  C  CA  B TYR   A 9   ? 0.1694 0.2038 0.1967 -0.0163 0.0277  -0.0070 9   TYR   A CA  
148  C  C   A TYR   A 9   ? 0.1600 0.1937 0.2142 -0.0193 0.0367  0.0162  9   TYR   A C   
149  C  C   B TYR   A 9   ? 0.1675 0.1869 0.1941 -0.0146 0.0288  0.0111  9   TYR   A C   
150  O  O   A TYR   A 9   ? 0.1736 0.2137 0.2303 -0.0201 0.0362  0.0146  9   TYR   A O   
151  O  O   B TYR   A 9   ? 0.1757 0.1982 0.1988 -0.0134 0.0383  0.0158  9   TYR   A O   
152  C  CB  A TYR   A 9   ? 0.1579 0.2358 0.2094 -0.0156 0.0246  -0.0029 9   TYR   A CB  
153  C  CB  B TYR   A 9   ? 0.1526 0.2055 0.1814 -0.0042 0.0212  -0.0083 9   TYR   A CB  
154  C  CG  A TYR   A 9   ? 0.1524 0.2456 0.1989 -0.0085 0.0307  -0.0185 9   TYR   A CG  
155  C  CG  B TYR   A 9   ? 0.1375 0.2034 0.1610 0.0068  0.0178  -0.0128 9   TYR   A CG  
156  C  CD1 A TYR   A 9   ? 0.1508 0.2548 0.2068 -0.0169 0.0284  -0.0190 9   TYR   A CD1 
157  C  CD1 B TYR   A 9   ? 0.1357 0.2048 0.1594 0.0047  0.0159  -0.0051 9   TYR   A CD1 
158  C  CD2 A TYR   A 9   ? 0.1469 0.2403 0.1971 -0.0075 0.0134  -0.0068 9   TYR   A CD2 
159  C  CD2 B TYR   A 9   ? 0.1360 0.1986 0.1639 0.0051  0.0096  -0.0144 9   TYR   A CD2 
160  C  CE1 A TYR   A 9   ? 0.1458 0.2540 0.2135 -0.0106 0.0280  -0.0264 9   TYR   A CE1 
161  C  CE1 B TYR   A 9   ? 0.1368 0.2082 0.1656 0.0035  0.0177  -0.0100 9   TYR   A CE1 
162  C  CE2 A TYR   A 9   ? 0.1438 0.2430 0.2056 -0.0072 0.0237  -0.0150 9   TYR   A CE2 
163  C  CE2 B TYR   A 9   ? 0.1355 0.2028 0.1668 0.0037  0.0164  -0.0155 9   TYR   A CE2 
164  C  CZ  A TYR   A 9   ? 0.1393 0.2494 0.2188 -0.0176 0.0279  -0.0171 9   TYR   A CZ  
165  C  CZ  B TYR   A 9   ? 0.1399 0.2102 0.1762 -0.0033 0.0195  -0.0083 9   TYR   A CZ  
166  O  OH  A TYR   A 9   ? 0.1377 0.2534 0.2338 -0.0278 0.0267  -0.0149 9   TYR   A OH  
167  O  OH  B TYR   A 9   ? 0.1527 0.2147 0.1953 -0.0055 0.0170  0.0000  9   TYR   A OH  
186  N  N   A LEU   A 10  ? 0.1461 0.1708 0.2134 -0.0121 0.0217  0.0186  10  LEU   A N   
187  N  N   B LEU   A 10  ? 0.1554 0.1693 0.1840 -0.0131 0.0085  0.0172  10  LEU   A N   
188  C  CA  A LEU   A 10  ? 0.1441 0.1679 0.2030 -0.0177 0.0115  0.0322  10  LEU   A CA  
189  C  CA  B LEU   A 10  ? 0.1518 0.1627 0.1821 -0.0156 0.0142  0.0144  10  LEU   A CA  
190  C  C   A LEU   A 10  ? 0.1429 0.1601 0.1974 -0.0231 0.0071  0.0293  10  LEU   A C   
191  C  C   B LEU   A 10  ? 0.1363 0.1502 0.1529 -0.0137 0.0181  0.0162  10  LEU   A C   
192  O  O   A LEU   A 10  ? 0.1450 0.1497 0.2130 -0.0339 0.0075  0.0269  10  LEU   A O   
193  O  O   B LEU   A 10  ? 0.1349 0.1352 0.1463 -0.0211 0.0241  0.0151  10  LEU   A O   
194  C  CB  A LEU   A 10  ? 0.1486 0.1783 0.2257 -0.0186 0.0112  0.0486  10  LEU   A CB  
195  C  CB  B LEU   A 10  ? 0.1602 0.1700 0.2026 -0.0209 0.0039  0.0114  10  LEU   A CB  
196  C  CG  A LEU   A 10  ? 0.1740 0.1907 0.2619 -0.0163 -0.0005 0.0527  10  LEU   A CG  
197  C  CG  B LEU   A 10  ? 0.1764 0.1776 0.2268 -0.0222 -0.0107 0.0042  10  LEU   A CG  
198  C  CD1 A LEU   A 10  ? 0.1871 0.1960 0.2881 -0.0211 0.0024  0.0472  10  LEU   A CD1 
199  C  CD1 B LEU   A 10  ? 0.1806 0.1805 0.2310 -0.0245 -0.0191 -0.0032 10  LEU   A CD1 
200  C  CD2 A LEU   A 10  ? 0.1895 0.2026 0.2747 -0.0070 0.0138  0.0265  10  LEU   A CD2 
201  C  CD2 B LEU   A 10  ? 0.1895 0.1848 0.2513 -0.0176 -0.0112 -0.0044 10  LEU   A CD2 
224  N  N   A LYS   A 11  ? 0.1490 0.1580 0.1864 -0.0229 0.0065  0.0415  11  LYS   A N   
225  N  N   B LYS   A 11  ? 0.1330 0.1534 0.1434 -0.0093 0.0136  0.0255  11  LYS   A N   
226  C  CA  A LYS   A 11  ? 0.1570 0.1528 0.2076 -0.0294 0.0115  0.0378  11  LYS   A CA  
227  C  CA  B LYS   A 11  ? 0.1353 0.1499 0.1527 -0.0098 0.0106  0.0293  11  LYS   A CA  
228  C  C   A LYS   A 11  ? 0.1475 0.1599 0.2123 -0.0302 0.0277  0.0245  11  LYS   A C   
229  C  C   B LYS   A 11  ? 0.1332 0.1399 0.1506 -0.0206 0.0134  0.0229  11  LYS   A C   
230  O  O   A LYS   A 11  ? 0.1467 0.1826 0.2454 -0.0457 0.0411  0.0071  11  LYS   A O   
231  O  O   B LYS   A 11  ? 0.1330 0.1382 0.1745 -0.0351 0.0169  -0.0045 11  LYS   A O   
232  C  CB  A LYS   A 11  ? 0.1765 0.1427 0.1999 -0.0255 -0.0011 0.0276  11  LYS   A CB  
233  C  CB  B LYS   A 11  ? 0.1418 0.1566 0.1464 -0.0041 0.0084  0.0329  11  LYS   A CB  
234  C  CG  A LYS   A 11  ? 0.1823 0.1361 0.1950 -0.0318 0.0131  0.0332  11  LYS   A CG  
235  C  CG  B LYS   A 11  ? 0.1449 0.1608 0.1505 0.0006  0.0140  0.0322  11  LYS   A CG  
236  C  CD  A LYS   A 11  ? 0.1881 0.1402 0.1871 -0.0240 0.0171  0.0213  11  LYS   A CD  
237  C  CD  B LYS   A 11  ? 0.1524 0.1650 0.1608 0.0008  0.0148  0.0328  11  LYS   A CD  
238  C  CE  A LYS   A 11  ? 0.1882 0.1483 0.1969 -0.0171 0.0209  0.0287  11  LYS   A CE  
239  C  CE  B LYS   A 11  ? 0.1513 0.1664 0.1605 0.0013  0.0121  0.0429  11  LYS   A CE  
240  N  NZ  A LYS   A 11  ? 0.1835 0.1509 0.2095 -0.0164 -0.0024 0.0266  11  LYS   A NZ  
241  N  NZ  B LYS   A 11  ? 0.1505 0.1693 0.1637 -0.0033 0.0074  0.0400  11  LYS   A NZ  
268  N  N   A LEU   A 12  ? 0.1425 0.1556 0.1996 -0.0302 0.0169  0.0196  12  LEU   A N   
269  N  N   B LEU   A 12  ? 0.1323 0.1485 0.1471 -0.0202 0.0049  0.0293  12  LEU   A N   
270  C  CA  A LEU   A 12  ? 0.1474 0.1572 0.1861 -0.0260 0.0166  0.0224  12  LEU   A CA  
271  C  CA  B LEU   A 12  ? 0.1346 0.1633 0.1579 -0.0164 0.0044  0.0270  12  LEU   A CA  
272  C  C   A LEU   A 12  ? 0.1449 0.1505 0.1808 -0.0285 0.0177  0.0281  12  LEU   A C   
273  C  C   B LEU   A 12  ? 0.1328 0.1605 0.1556 -0.0198 0.0087  0.0334  12  LEU   A C   
274  O  O   A LEU   A 12  ? 0.1479 0.1584 0.2038 -0.0237 0.0054  0.0136  12  LEU   A O   
275  O  O   B LEU   A 12  ? 0.1336 0.1564 0.1469 -0.0169 0.0100  0.0350  12  LEU   A O   
276  C  CB  A LEU   A 12  ? 0.1575 0.1480 0.1861 -0.0158 0.0132  0.0227  12  LEU   A CB  
277  C  CB  B LEU   A 12  ? 0.1375 0.1734 0.1821 -0.0053 0.0046  0.0199  12  LEU   A CB  
278  C  CG  A LEU   A 12  ? 0.1609 0.1476 0.1889 -0.0091 0.0256  0.0216  12  LEU   A CG  
279  C  CG  B LEU   A 12  ? 0.1343 0.1756 0.1928 -0.0021 0.0101  0.0042  12  LEU   A CG  
280  C  CD1 A LEU   A 12  ? 0.1688 0.1577 0.2090 0.0097  0.0307  0.0341  12  LEU   A CD1 
281  C  CD1 B LEU   A 12  ? 0.1394 0.1851 0.2163 0.0035  0.0166  0.0081  12  LEU   A CD1 
282  C  CD2 A LEU   A 12  ? 0.1614 0.1515 0.2039 0.0005  0.0315  0.0226  12  LEU   A CD2 
283  C  CD2 B LEU   A 12  ? 0.1316 0.1717 0.1909 0.0004  0.0091  -0.0121 12  LEU   A CD2 
306  N  N   A THR   A 13  ? 0.1433 0.1446 0.1739 -0.0242 0.0094  0.0274  13  THR   A N   
307  N  N   B THR   A 13  ? 0.1350 0.1607 0.1759 -0.0217 0.0119  0.0235  13  THR   A N   
308  C  CA  A THR   A 13  ? 0.1470 0.1426 0.1684 -0.0252 0.0091  0.0232  13  THR   A CA  
309  C  CA  B THR   A 13  ? 0.1397 0.1599 0.1847 -0.0201 0.0135  0.0163  13  THR   A CA  
310  C  C   A THR   A 13  ? 0.1477 0.1411 0.1652 -0.0263 0.0094  0.0230  13  THR   A C   
311  C  C   B THR   A 13  ? 0.1372 0.1617 0.1878 -0.0249 0.0220  -0.0023 13  THR   A C   
312  O  O   A THR   A 13  ? 0.1485 0.1391 0.1836 -0.0193 0.0057  0.0272  13  THR   A O   
313  O  O   B THR   A 13  ? 0.1370 0.1630 0.1930 -0.0217 0.0301  -0.0050 13  THR   A O   
314  C  CB  A THR   A 13  ? 0.1492 0.1604 0.1786 -0.0200 0.0029  0.0272  13  THR   A CB  
315  C  CB  B THR   A 13  ? 0.1417 0.1646 0.1777 -0.0095 -0.0030 0.0388  13  THR   A CB  
316  O  OG1 A THR   A 13  ? 0.1381 0.1547 0.1621 -0.0162 -0.0127 0.0429  13  THR   A OG1 
317  O  OG1 B THR   A 13  ? 0.1406 0.1698 0.1835 -0.0194 -0.0030 0.0313  13  THR   A OG1 
318  C  CG2 A THR   A 13  ? 0.1478 0.1782 0.1887 -0.0246 0.0086  0.0178  13  THR   A CG2 
319  C  CG2 B THR   A 13  ? 0.1429 0.1740 0.1901 -0.0035 -0.0028 0.0415  13  THR   A CG2 
334  N  N   A ASP   A 14  ? 0.1571 0.1471 0.1761 -0.0259 0.0101  0.0283  14  ASP   A N   
335  N  N   B ASP   A 14  ? 0.1385 0.1623 0.1901 -0.0272 0.0169  -0.0120 14  ASP   A N   
336  C  CA  A ASP   A 14  ? 0.1611 0.1454 0.1869 -0.0231 -0.0005 0.0346  14  ASP   A CA  
337  C  CA  B ASP   A 14  ? 0.1418 0.1637 0.1890 -0.0247 0.0140  -0.0002 14  ASP   A CA  
338  C  C   A ASP   A 14  ? 0.1596 0.1447 0.1654 -0.0196 0.0013  0.0426  14  ASP   A C   
339  C  C   B ASP   A 14  ? 0.1334 0.1521 0.1610 -0.0159 0.0152  0.0099  14  ASP   A C   
340  O  O   A ASP   A 14  ? 0.1726 0.1542 0.1831 -0.0230 0.0063  0.0305  14  ASP   A O   
341  O  O   B ASP   A 14  ? 0.1389 0.1541 0.1639 -0.0125 0.0181  0.0092  14  ASP   A O   
342  C  CB  A ASP   A 14  ? 0.1769 0.1583 0.2428 -0.0302 -0.0112 0.0297  14  ASP   A CB  
343  C  CB  B ASP   A 14  ? 0.1571 0.1864 0.2188 -0.0282 0.0151  0.0086  14  ASP   A CB  
344  C  CG  A ASP   A 14  ? 0.2004 0.2082 0.3265 -0.0337 -0.0185 0.0221  14  ASP   A CG  
345  C  CG  B ASP   A 14  ? 0.1739 0.2164 0.2551 -0.0387 0.0072  0.0069  14  ASP   A CG  
346  O  OD1 A ASP   A 14  ? 0.2142 0.2270 0.3548 -0.0220 -0.0433 0.0230  14  ASP   A OD1 
347  O  OD1 B ASP   A 14  ? 0.1853 0.2213 0.2692 -0.0379 0.0037  0.0094  14  ASP   A OD1 
348  O  OD2 A ASP   A 14  ? 0.2214 0.2424 0.3730 -0.0345 -0.0209 0.0007  14  ASP   A OD2 
349  O  OD2 B ASP   A 14  ? 0.1806 0.2365 0.2785 -0.0361 -0.0011 0.0004  14  ASP   A OD2 
358  N  N   A ASN   A 15  ? 0.1501 0.1457 0.1709 -0.0189 0.0110  0.0390  15  ASN   A N   
359  N  N   B ASN   A 15  ? 0.1220 0.1412 0.1389 -0.0212 0.0168  0.0091  15  ASN   A N   
360  C  CA  A ASN   A 15  ? 0.1478 0.1514 0.1887 -0.0209 -0.0013 0.0267  15  ASN   A CA  
361  C  CA  B ASN   A 15  ? 0.1213 0.1399 0.1452 -0.0186 0.0203  0.0038  15  ASN   A CA  
362  C  C   A ASN   A 15  ? 0.1389 0.1459 0.1954 -0.0222 0.0136  0.0276  15  ASN   A C   
363  C  C   B ASN   A 15  ? 0.1279 0.1363 0.1619 -0.0160 0.0205  0.0016  15  ASN   A C   
364  O  O   A ASN   A 15  ? 0.1419 0.1452 0.2059 -0.0173 0.0068  0.0205  15  ASN   A O   
365  O  O   B ASN   A 15  ? 0.1226 0.1394 0.1732 -0.0044 0.0249  -0.0056 15  ASN   A O   
366  C  CB  A ASN   A 15  ? 0.1498 0.1528 0.1798 -0.0117 -0.0018 0.0322  15  ASN   A CB  
367  C  CB  B ASN   A 15  ? 0.1141 0.1349 0.1428 -0.0155 0.0232  -0.0047 15  ASN   A CB  
368  C  CG  A ASN   A 15  ? 0.1504 0.1621 0.1769 -0.0090 0.0210  0.0219  15  ASN   A CG  
369  C  CG  B ASN   A 15  ? 0.1094 0.1465 0.1606 -0.0128 0.0316  -0.0065 15  ASN   A CG  
370  O  OD1 A ASN   A 15  ? 0.1466 0.1540 0.1871 -0.0073 0.0305  0.0197  15  ASN   A OD1 
371  O  OD1 B ASN   A 15  ? 0.1073 0.1527 0.1538 -0.0150 0.0201  -0.0123 15  ASN   A OD1 
372  N  ND2 A ASN   A 15  ? 0.1562 0.1787 0.1825 -0.0148 0.0159  0.0332  15  ASN   A ND2 
373  N  ND2 B ASN   A 15  ? 0.1170 0.1544 0.1673 -0.0113 0.0184  0.0052  15  ASN   A ND2 
386  N  N   A VAL   A 16  ? 0.1402 0.1418 0.2071 -0.0222 0.0046  0.0336  16  VAL   A N   
387  N  N   B VAL   A 16  ? 0.1382 0.1306 0.1689 -0.0122 0.0156  0.0026  16  VAL   A N   
388  C  CA  A VAL   A 16  ? 0.1291 0.1474 0.1994 -0.0207 0.0139  0.0471  16  VAL   A CA  
389  C  CA  B VAL   A 16  ? 0.1409 0.1335 0.1720 -0.0116 0.0142  0.0072  16  VAL   A CA  
390  C  C   A VAL   A 16  ? 0.1229 0.1541 0.1996 -0.0192 0.0116  0.0516  16  VAL   A C   
391  C  C   B VAL   A 16  ? 0.1436 0.1379 0.1730 -0.0098 0.0103  0.0133  16  VAL   A C   
392  O  O   A VAL   A 16  ? 0.1175 0.1566 0.2172 -0.0184 0.0204  0.0426  16  VAL   A O   
393  O  O   B VAL   A 16  ? 0.1431 0.1399 0.1880 -0.0117 0.0139  0.0096  16  VAL   A O   
394  C  CB  A VAL   A 16  ? 0.1348 0.1599 0.1884 -0.0067 0.0247  0.0478  16  VAL   A CB  
395  C  CB  B VAL   A 16  ? 0.1455 0.1424 0.1748 -0.0066 0.0184  0.0114  16  VAL   A CB  
396  C  CG1 A VAL   A 16  ? 0.1461 0.1717 0.2011 0.0033  0.0158  0.0366  16  VAL   A CG1 
397  C  CG1 B VAL   A 16  ? 0.1551 0.1493 0.1847 0.0041  0.0138  0.0126  16  VAL   A CG1 
398  C  CG2 A VAL   A 16  ? 0.1440 0.1750 0.2069 -0.0001 0.0309  0.0504  16  VAL   A CG2 
399  C  CG2 B VAL   A 16  ? 0.1449 0.1549 0.1746 -0.0136 0.0137  0.0026  16  VAL   A CG2 
418  N  N   A TYR   A 17  ? 0.1215 0.1480 0.1974 -0.0156 0.0191  0.0437  17  TYR   A N   
419  N  N   B TYR   A 17  ? 0.1434 0.1359 0.1629 -0.0026 0.0139  0.0079  17  TYR   A N   
420  C  CA  A TYR   A 17  ? 0.1328 0.1552 0.1844 -0.0217 0.0134  0.0503  17  TYR   A CA  
421  C  CA  B TYR   A 17  ? 0.1471 0.1403 0.1510 -0.0076 0.0139  0.0121  17  TYR   A CA  
422  C  C   A TYR   A 17  ? 0.1318 0.1523 0.1975 -0.0221 0.0111  0.0485  17  TYR   A C   
423  C  C   B TYR   A 17  ? 0.1420 0.1407 0.1603 -0.0015 0.0136  -0.0020 17  TYR   A C   
424  O  O   A TYR   A 17  ? 0.1318 0.1581 0.2039 -0.0228 0.0166  0.0545  17  TYR   A O   
425  O  O   B TYR   A 17  ? 0.1417 0.1391 0.1665 0.0020  0.0211  -0.0109 17  TYR   A O   
426  C  CB  A TYR   A 17  ? 0.1436 0.1582 0.1986 -0.0252 0.0058  0.0428  17  TYR   A CB  
427  C  CB  B TYR   A 17  ? 0.1608 0.1416 0.1531 -0.0104 0.0051  0.0195  17  TYR   A CB  
428  C  CG  A TYR   A 17  ? 0.1552 0.1685 0.1899 -0.0261 0.0030  0.0365  17  TYR   A CG  
429  C  CG  B TYR   A 17  ? 0.1757 0.1478 0.1470 -0.0152 -0.0066 0.0264  17  TYR   A CG  
430  C  CD1 A TYR   A 17  ? 0.1600 0.1737 0.2047 -0.0217 -0.0039 0.0330  17  TYR   A CD1 
431  C  CD1 B TYR   A 17  ? 0.1793 0.1588 0.1538 -0.0141 -0.0052 0.0330  17  TYR   A CD1 
432  C  CD2 A TYR   A 17  ? 0.1628 0.1731 0.1878 -0.0242 0.0101  0.0347  17  TYR   A CD2 
433  C  CD2 B TYR   A 17  ? 0.1853 0.1470 0.1473 -0.0213 -0.0084 0.0257  17  TYR   A CD2 
434  C  CE1 A TYR   A 17  ? 0.1748 0.1710 0.1970 -0.0201 0.0106  0.0335  17  TYR   A CE1 
435  C  CE1 B TYR   A 17  ? 0.1807 0.1575 0.1564 -0.0156 -0.0055 0.0350  17  TYR   A CE1 
436  C  CE2 A TYR   A 17  ? 0.1728 0.1690 0.1915 -0.0155 0.0175  0.0270  17  TYR   A CE2 
437  C  CE2 B TYR   A 17  ? 0.1907 0.1507 0.1470 -0.0185 -0.0123 0.0236  17  TYR   A CE2 
438  C  CZ  A TYR   A 17  ? 0.1705 0.1672 0.1832 -0.0161 0.0079  0.0358  17  TYR   A CZ  
439  C  CZ  B TYR   A 17  ? 0.1895 0.1517 0.1514 -0.0187 -0.0102 0.0305  17  TYR   A CZ  
440  O  OH  A TYR   A 17  ? 0.1683 0.1666 0.1969 -0.0112 0.0178  0.0323  17  TYR   A OH  
441  O  OH  B TYR   A 17  ? 0.2015 0.1484 0.1577 -0.0151 -0.0090 0.0253  17  TYR   A OH  
460  N  N   A ILE   A 18  ? 0.1351 0.1456 0.1937 -0.0267 0.0159  0.0490  18  ILE   A N   
461  N  N   B ILE   A 18  ? 0.1390 0.1438 0.1578 -0.0069 0.0147  0.0028  18  ILE   A N   
462  C  CA  A ILE   A 18  ? 0.1441 0.1410 0.2038 -0.0170 0.0200  0.0293  18  ILE   A CA  
463  C  CA  B ILE   A 18  ? 0.1364 0.1451 0.1556 -0.0027 0.0118  -0.0014 18  ILE   A CA  
464  C  C   A ILE   A 18  ? 0.1415 0.1527 0.2078 -0.0139 0.0204  0.0272  18  ILE   A C   
465  C  C   B ILE   A 18  ? 0.1302 0.1601 0.1502 -0.0025 0.0037  0.0056  18  ILE   A C   
466  O  O   A ILE   A 18  ? 0.1351 0.1634 0.2221 -0.0239 0.0285  0.0257  18  ILE   A O   
467  O  O   B ILE   A 18  ? 0.1266 0.1714 0.1653 -0.0072 0.0141  0.0121  18  ILE   A O   
468  C  CB  A ILE   A 18  ? 0.1591 0.1440 0.1841 -0.0107 0.0109  0.0381  18  ILE   A CB  
469  C  CB  B ILE   A 18  ? 0.1398 0.1438 0.1462 -0.0030 0.0105  0.0189  18  ILE   A CB  
470  C  CG1 A ILE   A 18  ? 0.1673 0.1436 0.1739 -0.0040 0.0069  0.0425  18  ILE   A CG1 
471  C  CG1 B ILE   A 18  ? 0.1532 0.1472 0.1603 -0.0072 0.0101  0.0251  18  ILE   A CG1 
472  C  CG2 A ILE   A 18  ? 0.1666 0.1481 0.1913 -0.0145 0.0110  0.0228  18  ILE   A CG2 
473  C  CG2 B ILE   A 18  ? 0.1400 0.1519 0.1474 -0.0056 0.0129  0.0229  18  ILE   A CG2 
474  C  CD1 A ILE   A 18  ? 0.1956 0.1555 0.2126 0.0060  0.0024  0.0360  18  ILE   A CD1 
475  C  CD1 B ILE   A 18  ? 0.1740 0.1577 0.1815 -0.0069 0.0053  0.0220  18  ILE   A CD1 
498  N  N   A LYS   A 19  ? 0.1431 0.1518 0.1966 -0.0128 0.0310  0.0252  19  LYS   A N   
499  N  N   B LYS   A 19  ? 0.1363 0.1639 0.1437 0.0016  -0.0021 -0.0033 19  LYS   A N   
500  C  CA  A LYS   A 19  ? 0.1524 0.1579 0.2132 -0.0062 0.0248  0.0213  19  LYS   A CA  
501  C  CA  B LYS   A 19  ? 0.1436 0.1755 0.1465 -0.0005 0.0016  -0.0090 19  LYS   A CA  
502  C  C   A LYS   A 19  ? 0.1431 0.1503 0.2182 -0.0034 0.0235  0.0219  19  LYS   A C   
503  C  C   B LYS   A 19  ? 0.1419 0.1764 0.1594 0.0138  0.0071  -0.0102 19  LYS   A C   
504  O  O   A LYS   A 19  ? 0.1392 0.1438 0.2149 -0.0073 0.0132  0.0313  19  LYS   A O   
505  O  O   B LYS   A 19  ? 0.1375 0.1697 0.1562 0.0162  0.0025  0.0014  19  LYS   A O   
506  C  CB  A LYS   A 19  ? 0.1556 0.1767 0.2187 -0.0029 0.0308  0.0076  19  LYS   A CB  
507  C  CB  B LYS   A 19  ? 0.1523 0.1903 0.1512 -0.0080 0.0050  -0.0073 19  LYS   A CB  
508  C  CG  A LYS   A 19  ? 0.1818 0.1844 0.2244 -0.0087 0.0217  -0.0041 19  LYS   A CG  
509  C  CG  B LYS   A 19  ? 0.1662 0.2006 0.1576 -0.0141 0.0066  -0.0001 19  LYS   A CG  
510  C  CD  A LYS   A 19  ? 0.2075 0.2079 0.2325 -0.0145 0.0226  -0.0124 19  LYS   A CD  
511  C  CD  B LYS   A 19  ? 0.1763 0.2122 0.1581 -0.0215 0.0091  0.0048  19  LYS   A CD  
512  C  CE  A LYS   A 19  ? 0.2256 0.2199 0.2382 -0.0222 0.0221  -0.0175 19  LYS   A CE  
513  C  CE  B LYS   A 19  ? 0.1844 0.2199 0.1647 -0.0311 0.0040  0.0052  19  LYS   A CE  
514  N  NZ  A LYS   A 19  ? 0.2391 0.2335 0.2189 -0.0336 0.0279  -0.0310 19  LYS   A NZ  
515  N  NZ  B LYS   A 19  ? 0.1909 0.2238 0.1689 -0.0364 0.0076  0.0074  19  LYS   A NZ  
542  N  N   A ASN   A 20  ? 0.1482 0.1531 0.2500 -0.0088 0.0239  0.0318  20  ASN   A N   
543  N  N   B ASN   A 20  ? 0.1503 0.1860 0.1781 0.0154  0.0225  -0.0067 20  ASN   A N   
544  C  CA  A ASN   A 20  ? 0.1574 0.1653 0.2806 0.0130  0.0371  0.0282  20  ASN   A CA  
545  C  CA  B ASN   A 20  ? 0.1571 0.1945 0.2031 0.0210  0.0291  -0.0014 20  ASN   A CA  
546  C  C   A ASN   A 20  ? 0.1779 0.1721 0.2959 0.0095  0.0527  0.0123  20  ASN   A C   
547  C  C   B ASN   A 20  ? 0.1729 0.1935 0.1933 0.0193  0.0275  -0.0162 20  ASN   A C   
548  O  O   A ASN   A 20  ? 0.2098 0.1867 0.3084 -0.0065 0.0648  0.0053  20  ASN   A O   
549  O  O   B ASN   A 20  ? 0.1963 0.1991 0.2002 0.0138  0.0333  -0.0361 20  ASN   A O   
550  C  CB  A ASN   A 20  ? 0.1589 0.1726 0.3094 0.0237  0.0413  0.0376  20  ASN   A CB  
551  C  CB  B ASN   A 20  ? 0.1594 0.2006 0.2302 0.0203  0.0363  0.0221  20  ASN   A CB  
552  C  CG  A ASN   A 20  ? 0.1650 0.1790 0.3531 0.0386  0.0351  0.0490  20  ASN   A CG  
553  C  CG  B ASN   A 20  ? 0.1635 0.2040 0.2599 0.0185  0.0408  0.0350  20  ASN   A CG  
554  O  OD1 A ASN   A 20  ? 0.1849 0.1864 0.3973 0.0356  0.0577  0.0357  20  ASN   A OD1 
555  O  OD1 B ASN   A 20  ? 0.1651 0.2090 0.2896 0.0162  0.0478  0.0337  20  ASN   A OD1 
556  N  ND2 A ASN   A 20  ? 0.1793 0.1810 0.3670 0.0372  0.0191  0.0683  20  ASN   A ND2 
557  N  ND2 B ASN   A 20  ? 0.1717 0.2036 0.2610 0.0180  0.0451  0.0418  20  ASN   A ND2 
570  N  N   A ALA   A 21  ? 0.1741 0.1741 0.2974 0.0096  0.0375  0.0066  21  ALA   A N   
571  N  N   B ALA   A 21  ? 0.1750 0.1927 0.2017 0.0147  0.0073  -0.0105 21  ALA   A N   
572  C  CA  A ALA   A 21  ? 0.1830 0.1762 0.2724 0.0043  0.0410  0.0137  21  ALA   A CA  
573  C  CA  B ALA   A 21  ? 0.1836 0.1961 0.2173 0.0116  -0.0034 -0.0070 21  ALA   A CA  
574  C  C   A ALA   A 21  ? 0.1796 0.1723 0.2576 0.0001  0.0320  0.0157  21  ALA   A C   
575  C  C   B ALA   A 21  ? 0.1701 0.1853 0.2080 0.0069  -0.0055 0.0048  21  ALA   A C   
576  O  O   A ALA   A 21  ? 0.1769 0.1761 0.2565 -0.0008 0.0259  0.0047  21  ALA   A O   
577  O  O   B ALA   A 21  ? 0.1566 0.1822 0.1985 -0.0068 -0.0011 0.0237  21  ALA   A O   
578  C  CB  A ALA   A 21  ? 0.2043 0.1886 0.2767 -0.0052 0.0405  0.0237  21  ALA   A CB  
579  C  CB  B ALA   A 21  ? 0.2023 0.2066 0.2426 0.0084  -0.0137 -0.0055 21  ALA   A CB  
590  N  N   A ASP   A 22  ? 0.1881 0.1695 0.2582 -0.0074 0.0306  0.0249  22  ASP   A N   
591  N  N   B ASP   A 22  ? 0.1718 0.1781 0.2122 0.0109  -0.0058 0.0030  22  ASP   A N   
592  C  CA  A ASP   A 22  ? 0.1940 0.1740 0.2533 -0.0166 0.0115  0.0350  22  ASP   A CA  
593  C  CA  B ASP   A 22  ? 0.1661 0.1757 0.2157 0.0076  -0.0132 0.0027  22  ASP   A CA  
594  C  C   A ASP   A 22  ? 0.1778 0.1835 0.1947 -0.0262 0.0329  0.0364  22  ASP   A C   
595  C  C   B ASP   A 22  ? 0.1695 0.1843 0.1947 0.0025  -0.0109 0.0037  22  ASP   A C   
596  O  O   A ASP   A 22  ? 0.1822 0.2043 0.1942 -0.0187 0.0376  0.0271  22  ASP   A O   
597  O  O   B ASP   A 22  ? 0.1749 0.1966 0.2009 0.0033  -0.0102 -0.0019 22  ASP   A O   
598  C  CB  A ASP   A 22  ? 0.2258 0.1861 0.3302 -0.0090 -0.0073 0.0266  22  ASP   A CB  
599  C  CB  B ASP   A 22  ? 0.1684 0.1677 0.2464 0.0044  -0.0179 -0.0018 22  ASP   A CB  
600  C  CG  A ASP   A 22  ? 0.2464 0.1927 0.3884 -0.0145 -0.0296 0.0374  22  ASP   A CG  
601  C  CG  B ASP   A 22  ? 0.1575 0.1546 0.2603 0.0001  -0.0212 -0.0024 22  ASP   A CG  
602  O  OD1 A ASP   A 22  ? 0.2535 0.1916 0.3932 -0.0297 -0.0380 0.0613  22  ASP   A OD1 
603  O  OD1 B ASP   A 22  ? 0.1537 0.1410 0.2612 -0.0098 -0.0079 -0.0138 22  ASP   A OD1 
604  O  OD2 A ASP   A 22  ? 0.2596 0.2081 0.4286 -0.0104 -0.0404 0.0324  22  ASP   A OD2 
605  O  OD2 B ASP   A 22  ? 0.1479 0.1581 0.2761 0.0042  -0.0242 0.0095  22  ASP   A OD2 
614  N  N   A ILE   A 23  ? 0.1758 0.1881 0.1720 -0.0264 0.0285  0.0360  23  ILE   A N   
615  N  N   B ILE   A 23  ? 0.1737 0.1863 0.1791 0.0017  -0.0053 0.0061  23  ILE   A N   
616  C  CA  A ILE   A 23  ? 0.1701 0.1790 0.1608 -0.0228 0.0202  0.0322  23  ILE   A CA  
617  C  CA  B ILE   A 23  ? 0.1766 0.1836 0.1677 0.0006  0.0072  0.0062  23  ILE   A CA  
618  C  C   A ILE   A 23  ? 0.1646 0.1847 0.1537 -0.0095 0.0261  0.0202  23  ILE   A C   
619  C  C   B ILE   A 23  ? 0.1723 0.1848 0.1673 -0.0004 0.0130  0.0074  23  ILE   A C   
620  O  O   A ILE   A 23  ? 0.1657 0.1872 0.1501 -0.0057 0.0296  0.0179  23  ILE   A O   
621  O  O   B ILE   A 23  ? 0.1732 0.1838 0.1673 0.0010  0.0103  0.0070  23  ILE   A O   
622  C  CB  A ILE   A 23  ? 0.1779 0.1803 0.1499 -0.0186 0.0104  0.0350  23  ILE   A CB  
623  C  CB  B ILE   A 23  ? 0.1856 0.1867 0.1532 0.0036  0.0082  0.0060  23  ILE   A CB  
624  C  CG1 A ILE   A 23  ? 0.1806 0.1886 0.1454 -0.0248 0.0061  0.0246  23  ILE   A CG1 
625  C  CG1 B ILE   A 23  ? 0.1890 0.1864 0.1349 0.0032  0.0065  -0.0030 23  ILE   A CG1 
626  C  CG2 A ILE   A 23  ? 0.1810 0.1793 0.1497 -0.0141 0.0137  0.0335  23  ILE   A CG2 
627  C  CG2 B ILE   A 23  ? 0.1867 0.1901 0.1565 0.0042  0.0106  0.0094  23  ILE   A CG2 
628  C  CD1 A ILE   A 23  ? 0.1814 0.1906 0.1476 -0.0316 -0.0096 0.0086  23  ILE   A CD1 
629  C  CD1 B ILE   A 23  ? 0.1937 0.1854 0.1214 0.0052  0.0017  -0.0086 23  ILE   A CD1 
652  N  N   . VAL   A 24  ? 0.1727 0.1875 0.1792 -0.0124 0.0140  0.0113  24  VAL   A N   
653  C  CA  . VAL   A 24  ? 0.1845 0.1961 0.2053 -0.0176 0.0069  0.0097  24  VAL   A CA  
654  C  C   . VAL   A 24  ? 0.1891 0.2085 0.2049 -0.0239 0.0170  0.0086  24  VAL   A C   
655  O  O   . VAL   A 24  ? 0.2019 0.2071 0.2070 -0.0149 0.0130  0.0018  24  VAL   A O   
656  C  CB  . VAL   A 24  ? 0.1828 0.1986 0.2497 -0.0253 0.0091  0.0226  24  VAL   A CB  
657  C  CG1 . VAL   A 24  ? 0.1993 0.2128 0.2829 -0.0235 0.0037  0.0149  24  VAL   A CG1 
658  C  CG2 . VAL   A 24  ? 0.1976 0.2130 0.2788 -0.0076 0.0380  0.0403  24  VAL   A CG2 
669  N  N   A GLU   A 25  ? 0.1905 0.2303 0.2045 -0.0293 0.0186  0.0065  25  GLU   A N   
670  N  N   B GLU   A 25  ? 0.1966 0.2239 0.2094 -0.0214 0.0251  0.0025  25  GLU   A N   
671  C  CA  A GLU   A 25  ? 0.2116 0.2539 0.2124 -0.0223 0.0291  0.0040  25  GLU   A CA  
672  C  CA  B GLU   A 25  ? 0.2123 0.2405 0.2217 -0.0179 0.0368  -0.0018 25  GLU   A CA  
673  C  C   A GLU   A 25  ? 0.1971 0.2529 0.1649 -0.0345 0.0280  0.0006  25  GLU   A C   
674  C  C   B GLU   A 25  ? 0.2067 0.2435 0.1945 -0.0196 0.0418  -0.0105 25  GLU   A C   
675  O  O   A GLU   A 25  ? 0.2038 0.2629 0.1709 -0.0328 0.0262  -0.0021 25  GLU   A O   
676  O  O   B GLU   A 25  ? 0.2107 0.2489 0.1903 -0.0213 0.0498  -0.0216 25  GLU   A O   
677  C  CB  A GLU   A 25  ? 0.2421 0.2808 0.2624 -0.0145 0.0464  0.0098  25  GLU   A CB  
678  C  CB  B GLU   A 25  ? 0.2319 0.2548 0.2588 -0.0159 0.0448  0.0043  25  GLU   A CB  
679  C  CG  A GLU   A 25  ? 0.2747 0.3092 0.3292 -0.0096 0.0451  0.0033  25  GLU   A CG  
680  C  CG  B GLU   A 25  ? 0.2543 0.2727 0.3095 -0.0139 0.0427  0.0060  25  GLU   A CG  
681  C  CD  A GLU   A 25  ? 0.3035 0.3371 0.3936 -0.0073 0.0382  0.0022  25  GLU   A CD  
682  C  CD  B GLU   A 25  ? 0.2731 0.2895 0.3545 -0.0148 0.0358  0.0072  25  GLU   A CD  
683  O  OE1 A GLU   A 25  ? 0.3186 0.3523 0.4171 -0.0037 0.0223  -0.0048 25  GLU   A OE1 
684  O  OE1 B GLU   A 25  ? 0.2825 0.2983 0.3714 -0.0139 0.0309  0.0065  25  GLU   A OE1 
685  O  OE2 A GLU   A 25  ? 0.3118 0.3430 0.4267 -0.0086 0.0367  -0.0047 25  GLU   A OE2 
686  O  OE2 B GLU   A 25  ? 0.2809 0.2924 0.3765 -0.0182 0.0345  0.0042  25  GLU   A OE2 
699  N  N   A GLU   A 26  ? 0.1899 0.2433 0.1768 -0.0506 0.0328  -0.0040 26  GLU   A N   
700  N  N   B GLU   A 26  ? 0.2037 0.2403 0.1957 -0.0209 0.0417  -0.0147 26  GLU   A N   
701  C  CA  A GLU   A 26  ? 0.2065 0.2395 0.1592 -0.0670 0.0210  0.0034  26  GLU   A CA  
702  C  CA  B GLU   A 26  ? 0.2120 0.2373 0.1944 -0.0222 0.0365  -0.0127 26  GLU   A CA  
703  C  C   A GLU   A 26  ? 0.2015 0.2291 0.1227 -0.0608 0.0246  0.0059  26  GLU   A C   
704  C  C   B GLU   A 26  ? 0.2173 0.2416 0.1781 -0.0138 0.0358  -0.0131 26  GLU   A C   
705  O  O   A GLU   A 26  ? 0.2108 0.2308 0.1203 -0.0684 0.0211  0.0121  26  GLU   A O   
706  O  O   B GLU   A 26  ? 0.2178 0.2386 0.1679 -0.0139 0.0407  -0.0202 26  GLU   A O   
707  C  CB  A GLU   A 26  ? 0.2377 0.2418 0.1948 -0.0766 0.0033  0.0212  26  GLU   A CB  
708  C  CB  B GLU   A 26  ? 0.2167 0.2257 0.2113 -0.0257 0.0261  -0.0138 26  GLU   A CB  
709  C  CG  A GLU   A 26  ? 0.2572 0.2573 0.2749 -0.0810 0.0147  0.0213  26  GLU   A CG  
710  C  CG  B GLU   A 26  ? 0.2151 0.2116 0.2373 -0.0266 0.0418  -0.0194 26  GLU   A CG  
711  C  CD  A GLU   A 26  ? 0.2647 0.2697 0.3156 -0.0864 0.0313  0.0166  26  GLU   A CD  
712  C  CD  B GLU   A 26  ? 0.1995 0.1925 0.2345 -0.0415 0.0736  -0.0196 26  GLU   A CD  
713  O  OE1 A GLU   A 26  ? 0.2719 0.2844 0.3362 -0.0698 0.0458  0.0075  26  GLU   A OE1 
714  O  OE1 B GLU   A 26  ? 0.1882 0.1931 0.2194 -0.0217 0.0911  -0.0191 26  GLU   A OE1 
715  O  OE2 A GLU   A 26  ? 0.2718 0.2741 0.3193 -0.0983 0.0372  0.0018  26  GLU   A OE2 
716  O  OE2 B GLU   A 26  ? 0.1868 0.1749 0.2267 -0.0608 0.0895  -0.0540 26  GLU   A OE2 
729  N  N   A ALA   A 27  ? 0.1798 0.2150 0.1208 -0.0570 0.0327  0.0080  27  ALA   A N   
730  N  N   B ALA   A 27  ? 0.2197 0.2466 0.1738 -0.0069 0.0279  -0.0059 27  ALA   A N   
731  C  CA  A ALA   A 27  ? 0.1839 0.2202 0.1076 -0.0488 0.0295  0.0036  27  ALA   A CA  
732  C  CA  B ALA   A 27  ? 0.2324 0.2575 0.1666 -0.0021 0.0214  -0.0030 27  ALA   A CA  
733  C  C   A ALA   A 27  ? 0.2058 0.2428 0.1185 -0.0608 0.0310  -0.0102 27  ALA   A C   
734  C  C   B ALA   A 27  ? 0.2543 0.2795 0.1791 -0.0058 0.0165  -0.0082 27  ALA   A C   
735  O  O   A ALA   A 27  ? 0.2115 0.2505 0.1189 -0.0644 0.0123  -0.0062 27  ALA   A O   
736  O  O   B ALA   A 27  ? 0.2559 0.2816 0.1773 -0.0065 0.0079  -0.0060 27  ALA   A O   
737  C  CB  A ALA   A 27  ? 0.1705 0.2051 0.1183 -0.0443 0.0190  0.0020  27  ALA   A CB  
738  C  CB  B ALA   A 27  ? 0.2262 0.2511 0.1611 -0.0003 0.0215  -0.0028 27  ALA   A CB  
749  N  N   A LYS   A 28  ? 0.2372 0.2665 0.1463 -0.0556 0.0240  -0.0502 28  LYS   A N   
750  N  N   B LYS   A 28  ? 0.2783 0.3000 0.2060 -0.0071 0.0108  -0.0207 28  LYS   A N   
751  C  CA  A LYS   A 28  ? 0.2794 0.3080 0.2008 -0.0456 0.0294  -0.0686 28  LYS   A CA  
752  C  CA  B LYS   A 28  ? 0.3059 0.3265 0.2432 -0.0089 0.0087  -0.0308 28  LYS   A CA  
753  C  C   A LYS   A 28  ? 0.3011 0.3452 0.1823 -0.0498 0.0482  -0.0554 28  LYS   A C   
754  C  C   B LYS   A 28  ? 0.3242 0.3484 0.2437 -0.0161 0.0131  -0.0274 28  LYS   A C   
755  O  O   A LYS   A 28  ? 0.3132 0.3619 0.2287 -0.0481 0.0301  -0.0514 28  LYS   A O   
756  O  O   B LYS   A 28  ? 0.3311 0.3565 0.2587 -0.0155 0.0061  -0.0295 28  LYS   A O   
757  C  CB  A LYS   A 28  ? 0.3008 0.3208 0.2666 -0.0290 0.0321  -0.0885 28  LYS   A CB  
758  C  CB  B LYS   A 28  ? 0.3177 0.3345 0.2839 -0.0039 0.0086  -0.0403 28  LYS   A CB  
759  C  CG  A LYS   A 28  ? 0.3214 0.3336 0.3244 -0.0168 0.0364  -0.0954 28  LYS   A CG  
760  C  CG  B LYS   A 28  ? 0.3298 0.3423 0.3234 -0.0001 0.0095  -0.0454 28  LYS   A CG  
761  C  CD  A LYS   A 28  ? 0.3400 0.3517 0.3920 -0.0079 0.0302  -0.0879 28  LYS   A CD  
762  C  CD  B LYS   A 28  ? 0.3420 0.3524 0.3705 0.0032  0.0069  -0.0445 28  LYS   A CD  
763  C  CE  A LYS   A 28  ? 0.3533 0.3635 0.4363 -0.0040 0.0260  -0.0893 28  LYS   A CE  
764  C  CE  B LYS   A 28  ? 0.3513 0.3588 0.4030 0.0042  0.0060  -0.0470 28  LYS   A CE  
765  N  NZ  A LYS   A 28  ? 0.3627 0.3705 0.4680 -0.0001 0.0272  -0.0953 28  LYS   A NZ  
766  N  NZ  B LYS   A 28  ? 0.3573 0.3623 0.4234 0.0062  0.0080  -0.0509 28  LYS   A NZ  
793  N  N   A LYS   A 29  ? 0.3071 0.3661 0.1531 -0.0561 0.0791  -0.0284 29  LYS   A N   
794  N  N   B LYS   A 29  ? 0.3342 0.3616 0.2478 -0.0242 0.0253  -0.0168 29  LYS   A N   
795  C  CA  A LYS   A 29  ? 0.3232 0.3900 0.1776 -0.0608 0.1008  -0.0079 29  LYS   A CA  
796  C  CA  B LYS   A 29  ? 0.3468 0.3753 0.2600 -0.0322 0.0356  -0.0087 29  LYS   A CA  
797  C  C   A LYS   A 29  ? 0.3163 0.3828 0.1529 -0.0711 0.0902  0.0021  29  LYS   A C   
798  C  C   B LYS   A 29  ? 0.3397 0.3676 0.2253 -0.0448 0.0309  -0.0030 29  LYS   A C   
799  O  O   A LYS   A 29  ? 0.3273 0.3988 0.1688 -0.0603 0.0876  -0.0016 29  LYS   A O   
800  O  O   B LYS   A 29  ? 0.3434 0.3734 0.2226 -0.0418 0.0339  -0.0020 29  LYS   A O   
801  C  CB  A LYS   A 29  ? 0.3416 0.4186 0.2433 -0.0525 0.1300  -0.0032 29  LYS   A CB  
802  C  CB  B LYS   A 29  ? 0.3641 0.3947 0.3145 -0.0268 0.0483  -0.0070 29  LYS   A CB  
803  C  CG  A LYS   A 29  ? 0.3642 0.4440 0.3421 -0.0456 0.1286  0.0015  29  LYS   A CG  
804  C  CG  B LYS   A 29  ? 0.3811 0.4119 0.3769 -0.0224 0.0538  -0.0033 29  LYS   A CG  
805  C  CD  A LYS   A 29  ? 0.3839 0.4663 0.4305 -0.0397 0.1241  -0.0010 29  LYS   A CD  
806  C  CD  B LYS   A 29  ? 0.3946 0.4265 0.4345 -0.0191 0.0577  -0.0024 29  LYS   A CD  
807  C  CE  A LYS   A 29  ? 0.3964 0.4811 0.4834 -0.0363 0.1269  -0.0054 29  LYS   A CE  
808  C  CE  B LYS   A 29  ? 0.4035 0.4361 0.4733 -0.0170 0.0625  -0.0042 29  LYS   A CE  
809  N  NZ  A LYS   A 29  ? 0.4020 0.4891 0.5179 -0.0343 0.1279  -0.0099 29  LYS   A NZ  
810  N  NZ  B LYS   A 29  ? 0.4075 0.4411 0.4979 -0.0156 0.0644  -0.0060 29  LYS   A NZ  
837  N  N   A VAL   A 30  ? 0.2981 0.3569 0.1400 -0.0880 0.0687  0.0133  30  VAL   A N   
838  N  N   B VAL   A 30  ? 0.3283 0.3527 0.2044 -0.0594 0.0228  0.0029  30  VAL   A N   
839  C  CA  A VAL   A 30  ? 0.2939 0.3419 0.1472 -0.0983 0.0379  0.0329  30  VAL   A CA  
840  C  CA  B VAL   A 30  ? 0.3207 0.3403 0.1893 -0.0713 0.0131  0.0148  30  VAL   A CA  
841  C  C   A VAL   A 30  ? 0.2986 0.3271 0.1211 -0.0897 0.0274  0.0423  30  VAL   A C   
842  C  C   B VAL   A 30  ? 0.3130 0.3315 0.1496 -0.0789 0.0132  0.0236  30  VAL   A C   
843  O  O   A VAL   A 30  ? 0.3064 0.3262 0.1265 -0.0855 0.0204  0.0476  30  VAL   A O   
844  O  O   B VAL   A 30  ? 0.3168 0.3320 0.1574 -0.0766 0.0099  0.0218  30  VAL   A O   
845  C  CB  A VAL   A 30  ? 0.2850 0.3388 0.1893 -0.1104 0.0197  0.0401  30  VAL   A CB  
846  C  CB  B VAL   A 30  ? 0.3192 0.3360 0.2150 -0.0739 0.0041  0.0167  30  VAL   A CB  
847  C  CG1 A VAL   A 30  ? 0.2884 0.3359 0.1925 -0.1118 0.0119  0.0598  30  VAL   A CG1 
848  C  CG1 B VAL   A 30  ? 0.3214 0.3343 0.2231 -0.0720 -0.0028 0.0186  30  VAL   A CG1 
849  C  CG2 A VAL   A 30  ? 0.2803 0.3442 0.2251 -0.1171 0.0221  0.0364  30  VAL   A CG2 
850  C  CG2 B VAL   A 30  ? 0.3183 0.3362 0.2313 -0.0763 0.0076  0.0205  30  VAL   A CG2 
869  N  N   . LYS   A 31  ? 0.3002 0.3226 0.1270 -0.0886 0.0095  0.0293  31  LYS   A N   
870  C  CA  . LYS   A 31  ? 0.3137 0.3295 0.1336 -0.0790 -0.0216 0.0161  31  LYS   A CA  
871  C  C   . LYS   A 31  ? 0.2833 0.2958 0.1020 -0.0569 -0.0168 0.0514  31  LYS   A C   
872  O  O   . LYS   A 31  ? 0.2950 0.3104 0.1316 -0.0541 -0.0405 0.0593  31  LYS   A O   
873  C  CB  . LYS   A 31  ? 0.3667 0.3744 0.2242 -0.0840 -0.0398 -0.0043 31  LYS   A CB  
874  C  CG  . LYS   A 31  ? 0.4271 0.4266 0.3691 -0.0783 -0.0522 -0.0169 31  LYS   A CG  
875  C  CD  . LYS   A 31  ? 0.4734 0.4658 0.4831 -0.0700 -0.0586 -0.0282 31  LYS   A CD  
876  C  CE  . LYS   A 31  ? 0.5044 0.4925 0.5529 -0.0637 -0.0657 -0.0412 31  LYS   A CE  
877  N  NZ  . LYS   A 31  ? 0.5207 0.5131 0.5894 -0.0603 -0.0723 -0.0512 31  LYS   A NZ  
892  N  N   . PRO   A 32  ? 0.2451 0.2659 0.0850 -0.0537 -0.0044 0.0344  32  PRO   A N   
893  C  CA  . PRO   A 32  ? 0.2361 0.2397 0.1413 -0.0505 -0.0130 0.0498  32  PRO   A CA  
894  C  C   . PRO   A 32  ? 0.2279 0.2316 0.1563 -0.0409 -0.0225 0.0504  32  PRO   A C   
895  O  O   . PRO   A 32  ? 0.2265 0.2234 0.1582 -0.0469 -0.0326 0.0465  32  PRO   A O   
896  C  CB  . PRO   A 32  ? 0.2339 0.2470 0.1547 -0.0496 -0.0133 0.0369  32  PRO   A CB  
897  C  CG  . PRO   A 32  ? 0.2337 0.2559 0.0907 -0.0436 -0.0215 0.0275  32  PRO   A CG  
898  C  CD  . PRO   A 32  ? 0.2310 0.2591 0.0887 -0.0487 -0.0109 0.0297  32  PRO   A CD  
906  N  N   . THR   A 33  ? 0.2376 0.2308 0.1424 -0.0358 -0.0185 0.0554  33  THR   A N   
907  C  CA  . THR   A 33  ? 0.2360 0.2273 0.1560 -0.0220 -0.0292 0.0496  33  THR   A CA  
908  C  C   . THR   A 33  ? 0.2077 0.2131 0.1413 -0.0251 -0.0277 0.0371  33  THR   A C   
909  O  O   . THR   A 33  ? 0.1960 0.2149 0.1664 -0.0326 -0.0401 0.0391  33  THR   A O   
910  C  CB  . THR   A 33  ? 0.2597 0.2497 0.1793 -0.0107 -0.0338 0.0636  33  THR   A CB  
911  O  OG1 . THR   A 33  ? 0.2820 0.2685 0.2020 -0.0006 -0.0202 0.0751  33  THR   A OG1 
912  C  CG2 . THR   A 33  ? 0.2612 0.2599 0.2020 -0.0088 -0.0391 0.0573  33  THR   A CG2 
920  N  N   . VAL   A 34  ? 0.1889 0.1996 0.1318 -0.0280 -0.0184 0.0349  34  VAL   A N   
921  C  CA  . VAL   A 34  ? 0.1772 0.1833 0.1213 -0.0207 -0.0121 0.0302  34  VAL   A CA  
922  C  C   . VAL   A 34  ? 0.1598 0.1835 0.1147 -0.0223 -0.0043 0.0308  34  VAL   A C   
923  O  O   . VAL   A 34  ? 0.1595 0.1789 0.1508 -0.0284 -0.0107 0.0367  34  VAL   A O   
924  C  CB  . VAL   A 34  ? 0.1797 0.1772 0.1530 -0.0179 -0.0080 0.0189  34  VAL   A CB  
925  C  CG1 . VAL   A 34  ? 0.1813 0.1783 0.1457 -0.0104 -0.0096 0.0119  34  VAL   A CG1 
926  C  CG2 . VAL   A 34  ? 0.1839 0.1847 0.1787 -0.0072 -0.0142 0.0277  34  VAL   A CG2 
936  N  N   . VAL   A 35  ? 0.1508 0.1682 0.1089 -0.0241 -0.0124 0.0189  35  VAL   A N   
937  C  CA  . VAL   A 35  ? 0.1461 0.1597 0.1139 -0.0195 -0.0099 0.0160  35  VAL   A CA  
938  C  C   . VAL   A 35  ? 0.1427 0.1444 0.1124 -0.0137 -0.0020 0.0117  35  VAL   A C   
939  O  O   . VAL   A 35  ? 0.1322 0.1527 0.1399 -0.0211 0.0119  0.0107  35  VAL   A O   
940  C  CB  . VAL   A 35  ? 0.1544 0.1687 0.1213 -0.0146 0.0017  0.0052  35  VAL   A CB  
941  C  CG1 . VAL   A 35  ? 0.1604 0.1629 0.1502 -0.0088 -0.0077 -0.0050 35  VAL   A CG1 
942  C  CG2 . VAL   A 35  ? 0.1498 0.1726 0.1587 -0.0153 0.0077  0.0072  35  VAL   A CG2 
952  N  N   . VAL   A 36  ? 0.1321 0.1377 0.1010 -0.0176 0.0070  0.0234  36  VAL   A N   
953  C  CA  . VAL   A 36  ? 0.1258 0.1283 0.1175 -0.0130 0.0014  0.0083  36  VAL   A CA  
954  C  C   . VAL   A 36  ? 0.1212 0.1374 0.1241 -0.0157 0.0068  0.0084  36  VAL   A C   
955  O  O   . VAL   A 36  ? 0.1247 0.1299 0.1396 -0.0047 0.0136  0.0110  36  VAL   A O   
956  C  CB  . VAL   A 36  ? 0.1287 0.1215 0.1250 -0.0106 0.0022  0.0138  36  VAL   A CB  
957  C  CG1 . VAL   A 36  ? 0.1326 0.1274 0.1381 -0.0127 0.0027  0.0125  36  VAL   A CG1 
958  C  CG2 . VAL   A 36  ? 0.1397 0.1291 0.1570 -0.0061 0.0003  0.0248  36  VAL   A CG2 
968  N  N   . ASN   A 37  ? 0.1140 0.1324 0.1159 -0.0021 -0.0000 0.0188  37  ASN   A N   
969  C  CA  . ASN   A 37  ? 0.1169 0.1291 0.1212 -0.0004 0.0037  0.0122  37  ASN   A CA  
970  C  C   . ASN   A 37  ? 0.1162 0.1232 0.1160 -0.0031 0.0118  0.0247  37  ASN   A C   
971  O  O   . ASN   A 37  ? 0.1285 0.1293 0.1189 0.0060  0.0140  0.0053  37  ASN   A O   
972  C  CB  . ASN   A 37  ? 0.1192 0.1238 0.1309 -0.0065 0.0000  0.0080  37  ASN   A CB  
973  C  CG  . ASN   A 37  ? 0.1226 0.1227 0.1384 -0.0018 0.0081  0.0034  37  ASN   A CG  
974  O  OD1 . ASN   A 37  ? 0.1234 0.1228 0.1633 -0.0003 0.0017  0.0178  37  ASN   A OD1 
975  N  ND2 . ASN   A 37  ? 0.1276 0.1213 0.1402 -0.0010 -0.0004 0.0194  37  ASN   A ND2 
982  N  N   A ALA   A 38  ? 0.1192 0.1331 0.1206 0.0005  0.0147  0.0095  38  ALA   A N   
983  N  N   B ALA   A 38  ? 0.1221 0.1313 0.1310 -0.0067 0.0039  0.0227  38  ALA   A N   
984  C  CA  A ALA   A 38  ? 0.1258 0.1340 0.1112 0.0001  -0.0011 0.0021  38  ALA   A CA  
985  C  CA  B ALA   A 38  ? 0.1294 0.1368 0.1459 -0.0117 -0.0077 0.0225  38  ALA   A CA  
986  C  C   A ALA   A 38  ? 0.1241 0.1329 0.1081 0.0063  -0.0012 -0.0057 38  ALA   A C   
987  C  C   B ALA   A 38  ? 0.1282 0.1298 0.1479 -0.0047 -0.0164 0.0071  38  ALA   A C   
988  O  O   A ALA   A 38  ? 0.1195 0.1270 0.1134 0.0015  -0.0072 -0.0041 38  ALA   A O   
989  O  O   B ALA   A 38  ? 0.1181 0.1206 0.1629 -0.0064 -0.0236 0.0075  38  ALA   A O   
990  C  CB  A ALA   A 38  ? 0.1262 0.1451 0.1335 -0.0087 0.0013  0.0046  38  ALA   A CB  
991  C  CB  B ALA   A 38  ? 0.1331 0.1468 0.1629 -0.0180 -0.0094 0.0146  38  ALA   A CB  
1002 N  N   A ALA   A 39  ? 0.1229 0.1288 0.1245 0.0079  0.0037  0.0023  39  ALA   A N   
1003 N  N   B ALA   A 39  ? 0.1335 0.1318 0.1466 -0.0034 -0.0084 0.0106  39  ALA   A N   
1004 C  CA  A ALA   A 39  ? 0.1179 0.1199 0.1174 0.0041  0.0072  0.0078  39  ALA   A CA  
1005 C  CA  B ALA   A 39  ? 0.1372 0.1320 0.1374 -0.0082 0.0009  0.0125  39  ALA   A CA  
1006 C  C   A ALA   A 39  ? 0.1242 0.1253 0.1182 0.0038  -0.0069 0.0026  39  ALA   A C   
1007 C  C   B ALA   A 39  ? 0.1302 0.1278 0.1274 -0.0063 0.0076  0.0152  39  ALA   A C   
1008 O  O   A ALA   A 39  ? 0.1357 0.1258 0.1348 0.0031  0.0030  0.0089  39  ALA   A O   
1009 O  O   B ALA   A 39  ? 0.1355 0.1250 0.1234 -0.0121 0.0157  0.0117  39  ALA   A O   
1010 C  CB  A ALA   A 39  ? 0.1139 0.1220 0.1441 0.0147  -0.0023 -0.0006 39  ALA   A CB  
1011 C  CB  B ALA   A 39  ? 0.1512 0.1359 0.1530 -0.0051 -0.0052 0.0036  39  ALA   A CB  
1022 N  N   A ASN   A 40  ? 0.1220 0.1260 0.1209 -0.0040 0.0029  0.0003  40  ASN   A N   
1023 N  N   B ASN   A 40  ? 0.1264 0.1235 0.1275 -0.0007 0.0205  0.0266  40  ASN   A N   
1024 C  CA  A ASN   A 40  ? 0.1379 0.1203 0.1230 -0.0050 0.0022  -0.0059 40  ASN   A CA  
1025 C  CA  B ASN   A 40  ? 0.1293 0.1148 0.1323 0.0012  0.0092  0.0258  40  ASN   A CA  
1026 C  C   A ASN   A 40  ? 0.1349 0.1165 0.1118 -0.0030 0.0053  0.0078  40  ASN   A C   
1027 C  C   B ASN   A 40  ? 0.1268 0.1115 0.1304 -0.0043 0.0141  0.0345  40  ASN   A C   
1028 O  O   A ASN   A 40  ? 0.1358 0.1236 0.1229 -0.0066 0.0047  0.0026  40  ASN   A O   
1029 O  O   B ASN   A 40  ? 0.1149 0.1097 0.1313 -0.0126 0.0061  0.0399  40  ASN   A O   
1030 C  CB  A ASN   A 40  ? 0.1572 0.1324 0.1462 0.0041  -0.0103 -0.0016 40  ASN   A CB  
1031 C  CB  B ASN   A 40  ? 0.1411 0.1190 0.1432 0.0019  0.0078  0.0260  40  ASN   A CB  
1032 C  CG  A ASN   A 40  ? 0.1743 0.1377 0.1934 0.0094  -0.0132 0.0129  40  ASN   A CG  
1033 C  CG  B ASN   A 40  ? 0.1503 0.1277 0.1484 -0.0021 0.0136  0.0217  40  ASN   A CG  
1034 O  OD1 A ASN   A 40  ? 0.1770 0.1339 0.2224 0.0076  -0.0256 0.0055  40  ASN   A OD1 
1035 O  OD1 B ASN   A 40  ? 0.1516 0.1297 0.1334 -0.0136 0.0309  0.0127  40  ASN   A OD1 
1036 N  ND2 A ASN   A 40  ? 0.1808 0.1485 0.1902 0.0104  -0.0013 0.0034  40  ASN   A ND2 
1037 N  ND2 B ASN   A 40  ? 0.1507 0.1378 0.1594 -0.0028 0.0144  0.0050  40  ASN   A ND2 
1050 N  N   A VAL   A 41  ? 0.1382 0.1243 0.1055 -0.0013 0.0027  0.0040  41  VAL   A N   
1051 N  N   B VAL   A 41  ? 0.1250 0.1196 0.1330 -0.0004 0.0170  0.0313  41  VAL   A N   
1052 C  CA  A VAL   A 41  ? 0.1373 0.1265 0.1261 0.0019  0.0078  0.0104  41  VAL   A CA  
1053 C  CA  B VAL   A 41  ? 0.1274 0.1296 0.1256 0.0019  0.0218  0.0287  41  VAL   A CA  
1054 C  C   A VAL   A 41  ? 0.1345 0.1198 0.1339 0.0003  0.0158  0.0114  41  VAL   A C   
1055 C  C   B VAL   A 41  ? 0.1271 0.1323 0.1143 0.0001  0.0283  0.0261  41  VAL   A C   
1056 O  O   A VAL   A 41  ? 0.1468 0.1194 0.1512 0.0043  0.0023  0.0083  41  VAL   A O   
1057 O  O   B VAL   A 41  ? 0.1337 0.1265 0.1231 0.0034  0.0110  0.0215  41  VAL   A O   
1058 C  CB  A VAL   A 41  ? 0.1440 0.1356 0.1380 0.0027  0.0168  0.0026  41  VAL   A CB  
1059 C  CB  B VAL   A 41  ? 0.1345 0.1428 0.1298 0.0037  0.0291  0.0296  41  VAL   A CB  
1060 C  CG1 A VAL   A 41  ? 0.1492 0.1365 0.1482 0.0100  0.0015  -0.0120 41  VAL   A CG1 
1061 C  CG1 B VAL   A 41  ? 0.1538 0.1528 0.1366 -0.0068 0.0385  0.0238  41  VAL   A CG1 
1062 C  CG2 A VAL   A 41  ? 0.1488 0.1482 0.1274 0.0023  0.0264  0.0015  41  VAL   A CG2 
1063 C  CG2 B VAL   A 41  ? 0.1337 0.1493 0.1267 0.0031  0.0198  0.0247  41  VAL   A CG2 
1082 N  N   A TYR   A 42  ? 0.1236 0.1200 0.1545 0.0036  0.0267  0.0106  42  TYR   A N   
1083 N  N   B TYR   A 42  ? 0.1257 0.1345 0.1186 0.0043  0.0301  0.0283  42  TYR   A N   
1084 C  CA  A TYR   A 42  ? 0.1342 0.1181 0.1709 -0.0060 0.0116  0.0151  42  TYR   A CA  
1085 C  CA  B TYR   A 42  ? 0.1269 0.1339 0.1187 0.0026  0.0331  0.0335  42  TYR   A CA  
1086 C  C   A TYR   A 42  ? 0.1342 0.1135 0.1680 -0.0005 0.0087  0.0255  42  TYR   A C   
1087 C  C   B TYR   A 42  ? 0.1380 0.1277 0.1259 -0.0012 0.0212  0.0360  42  TYR   A C   
1088 O  O   A TYR   A 42  ? 0.1299 0.1168 0.1960 -0.0028 0.0099  0.0028  42  TYR   A O   
1089 O  O   B TYR   A 42  ? 0.1387 0.1274 0.1336 -0.0037 0.0181  0.0335  42  TYR   A O   
1090 C  CB  A TYR   A 42  ? 0.1506 0.1300 0.1631 -0.0042 0.0239  0.0211  42  TYR   A CB  
1091 C  CB  B TYR   A 42  ? 0.1304 0.1407 0.1222 0.0041  0.0246  0.0433  42  TYR   A CB  
1092 C  CG  A TYR   A 42  ? 0.1593 0.1398 0.1601 -0.0015 0.0151  0.0274  42  TYR   A CG  
1093 C  CG  B TYR   A 42  ? 0.1400 0.1516 0.1346 0.0098  0.0124  0.0453  42  TYR   A CG  
1094 C  CD1 A TYR   A 42  ? 0.1585 0.1534 0.1758 -0.0041 0.0056  0.0232  42  TYR   A CD1 
1095 C  CD1 B TYR   A 42  ? 0.1418 0.1545 0.1370 0.0045  0.0188  0.0485  42  TYR   A CD1 
1096 C  CD2 A TYR   A 42  ? 0.1627 0.1585 0.1823 0.0063  0.0114  0.0248  42  TYR   A CD2 
1097 C  CD2 B TYR   A 42  ? 0.1505 0.1660 0.1567 0.0163  0.0087  0.0367  42  TYR   A CD2 
1098 C  CE1 A TYR   A 42  ? 0.1652 0.1653 0.1814 -0.0017 0.0124  0.0156  42  TYR   A CE1 
1099 C  CE1 B TYR   A 42  ? 0.1424 0.1604 0.1349 0.0054  0.0352  0.0492  42  TYR   A CE1 
1100 C  CE2 A TYR   A 42  ? 0.1685 0.1681 0.1958 0.0010  0.0193  0.0341  42  TYR   A CE2 
1101 C  CE2 B TYR   A 42  ? 0.1555 0.1723 0.1582 0.0177  0.0250  0.0407  42  TYR   A CE2 
1102 C  CZ  A TYR   A 42  ? 0.1722 0.1754 0.1826 -0.0008 0.0272  0.0310  42  TYR   A CZ  
1103 C  CZ  B TYR   A 42  ? 0.1518 0.1710 0.1507 0.0137  0.0300  0.0388  42  TYR   A CZ  
1104 O  OH  A TYR   A 42  ? 0.1796 0.1947 0.2081 -0.0041 0.0227  0.0248  42  TYR   A OH  
1105 O  OH  B TYR   A 42  ? 0.1513 0.1844 0.1611 0.0116  0.0235  0.0277  42  TYR   A OH  
1124 N  N   . LEU   A 43  ? 0.1415 0.1241 0.1435 -0.0072 0.0191  0.0080  43  LEU   A N   
1125 C  CA  . LEU   A 43  ? 0.1325 0.1233 0.1460 -0.0073 0.0108  0.0114  43  LEU   A CA  
1126 C  C   . LEU   A 43  ? 0.1371 0.1325 0.1432 -0.0037 0.0087  0.0055  43  LEU   A C   
1127 O  O   . LEU   A 43  ? 0.1483 0.1377 0.1554 0.0037  0.0011  0.0072  43  LEU   A O   
1128 C  CB  . LEU   A 43  ? 0.1348 0.1227 0.1645 -0.0120 0.0169  0.0066  43  LEU   A CB  
1129 C  CG  . LEU   A 43  ? 0.1365 0.1224 0.1719 -0.0081 0.0050  0.0086  43  LEU   A CG  
1130 C  CD1 . LEU   A 43  ? 0.1422 0.1268 0.1933 -0.0029 0.0026  0.0161  43  LEU   A CD1 
1131 C  CD2 . LEU   A 43  ? 0.1476 0.1272 0.1567 -0.0099 -0.0018 0.0181  43  LEU   A CD2 
1144 N  N   A LYS   A 44  ? 0.1330 0.1209 0.1403 0.0024  0.0120  0.0167  44  LYS   A N   
1145 N  N   B LYS   A 44  ? 0.1464 0.1398 0.1550 -0.0048 0.0022  0.0076  44  LYS   A N   
1146 C  CA  A LYS   A 44  ? 0.1416 0.1159 0.1502 -0.0000 0.0207  0.0264  44  LYS   A CA  
1147 C  CA  B LYS   A 44  ? 0.1625 0.1504 0.1735 -0.0081 -0.0015 0.0068  44  LYS   A CA  
1148 C  C   A LYS   A 44  ? 0.1302 0.1181 0.1218 0.0047  0.0116  0.0117  44  LYS   A C   
1149 C  C   B LYS   A 44  ? 0.1598 0.1449 0.1523 -0.0097 -0.0115 0.0014  44  LYS   A C   
1150 O  O   A LYS   A 44  ? 0.1423 0.1318 0.1379 0.0049  0.0055  0.0039  44  LYS   A O   
1151 O  O   B LYS   A 44  ? 0.1639 0.1490 0.1496 -0.0147 -0.0141 -0.0043 44  LYS   A O   
1152 C  CB  A LYS   A 44  ? 0.1714 0.1275 0.1973 -0.0037 0.0323  0.0448  44  LYS   A CB  
1153 C  CB  B LYS   A 44  ? 0.1850 0.1735 0.2155 -0.0070 0.0062  0.0067  44  LYS   A CB  
1154 C  CG  A LYS   A 44  ? 0.2072 0.1576 0.2512 -0.0100 0.0522  0.0579  44  LYS   A CG  
1155 C  CG  B LYS   A 44  ? 0.2075 0.1979 0.2633 -0.0075 0.0169  0.0089  44  LYS   A CG  
1156 C  CD  A LYS   A 44  ? 0.2442 0.2126 0.3596 -0.0124 0.0443  0.0458  44  LYS   A CD  
1157 C  CD  B LYS   A 44  ? 0.2287 0.2267 0.3231 -0.0102 0.0144  0.0116  44  LYS   A CD  
1158 C  CE  A LYS   A 44  ? 0.2648 0.2451 0.4329 -0.0133 0.0417  0.0385  44  LYS   A CE  
1159 C  CE  B LYS   A 44  ? 0.2406 0.2443 0.3634 -0.0137 0.0130  0.0171  44  LYS   A CE  
1160 N  NZ  A LYS   A 44  ? 0.2765 0.2682 0.4683 -0.0140 0.0346  0.0352  44  LYS   A NZ  
1161 N  NZ  B LYS   A 44  ? 0.2488 0.2560 0.3843 -0.0186 0.0088  0.0199  44  LYS   A NZ  
1188 N  N   A HIS   A 45  ? 0.1141 0.1162 0.1167 0.0036  0.0012  0.0112  45  HIS   A N   
1189 N  N   B HIS   A 45  ? 0.1577 0.1371 0.1526 -0.0071 -0.0199 0.0032  45  HIS   A N   
1190 C  CA  A HIS   A 45  ? 0.1135 0.1230 0.1264 0.0029  -0.0058 0.0019  45  HIS   A CA  
1191 C  CA  B HIS   A 45  ? 0.1559 0.1348 0.1539 -0.0010 -0.0180 0.0045  45  HIS   A CA  
1192 C  C   A HIS   A 45  ? 0.1187 0.1304 0.1353 0.0064  0.0030  0.0148  45  HIS   A C   
1193 C  C   B HIS   A 45  ? 0.1573 0.1430 0.1533 -0.0037 -0.0139 0.0107  45  HIS   A C   
1194 O  O   A HIS   A 45  ? 0.1213 0.1270 0.1657 0.0123  0.0108  0.0061  45  HIS   A O   
1195 O  O   B HIS   A 45  ? 0.1578 0.1462 0.1565 -0.0001 -0.0145 0.0050  45  HIS   A O   
1196 C  CB  A HIS   A 45  ? 0.1074 0.1271 0.1312 -0.0048 0.0040  -0.0039 45  HIS   A CB  
1197 C  CB  B HIS   A 45  ? 0.1493 0.1237 0.1492 0.0100  -0.0223 0.0018  45  HIS   A CB  
1198 C  CG  A HIS   A 45  ? 0.1121 0.1304 0.1312 -0.0056 0.0042  0.0099  45  HIS   A CG  
1199 C  CG  B HIS   A 45  ? 0.1410 0.1100 0.1256 0.0071  -0.0062 0.0030  45  HIS   A CG  
1200 N  ND1 A HIS   A 45  ? 0.1157 0.1426 0.1569 -0.0054 0.0075  0.0203  45  HIS   A ND1 
1201 N  ND1 B HIS   A 45  ? 0.1341 0.1089 0.1159 0.0104  -0.0162 0.0114  45  HIS   A ND1 
1202 C  CD2 A HIS   A 45  ? 0.1122 0.1388 0.1449 -0.0143 -0.0054 0.0177  45  HIS   A CD2 
1203 C  CD2 B HIS   A 45  ? 0.1381 0.1098 0.1314 0.0091  -0.0001 0.0089  45  HIS   A CD2 
1204 C  CE1 A HIS   A 45  ? 0.1208 0.1447 0.1344 -0.0094 0.0027  0.0134  45  HIS   A CE1 
1205 C  CE1 B HIS   A 45  ? 0.1370 0.1113 0.1027 0.0091  -0.0100 0.0113  45  HIS   A CE1 
1206 N  NE2 A HIS   A 45  ? 0.1193 0.1416 0.1372 -0.0056 -0.0059 0.0183  45  HIS   A NE2 
1207 N  NE2 B HIS   A 45  ? 0.1380 0.1118 0.1193 0.0124  -0.0001 0.0101  45  HIS   A NE2 
1222 N  N   A GLY   A 46  ? 0.1245 0.1362 0.1471 0.0094  -0.0078 0.0214  46  GLY   A N   
1223 N  N   B GLY   A 46  ? 0.1571 0.1411 0.1648 -0.0116 -0.0109 0.0167  46  GLY   A N   
1224 C  CA  A GLY   A 46  ? 0.1268 0.1430 0.1666 0.0137  -0.0124 0.0250  46  GLY   A CA  
1225 C  CA  B GLY   A 46  ? 0.1503 0.1522 0.1645 -0.0080 0.0012  0.0213  46  GLY   A CA  
1226 C  C   A GLY   A 46  ? 0.1317 0.1400 0.1611 0.0161  -0.0098 0.0446  46  GLY   A C   
1227 C  C   B GLY   A 46  ? 0.1442 0.1561 0.1418 -0.0119 0.0140  0.0214  46  GLY   A C   
1228 O  O   A GLY   A 46  ? 0.1403 0.1408 0.1704 0.0147  -0.0074 0.0431  46  GLY   A O   
1229 O  O   B GLY   A 46  ? 0.1410 0.1633 0.1421 -0.0182 0.0178  0.0119  46  GLY   A O   
1236 N  N   A GLY   A 47  ? 0.1307 0.1375 0.1701 0.0179  -0.0065 0.0307  47  GLY   A N   
1237 N  N   B GLY   A 47  ? 0.1439 0.1565 0.1557 -0.0094 0.0240  0.0050  47  GLY   A N   
1238 C  CA  A GLY   A 47  ? 0.1398 0.1422 0.1655 0.0196  -0.0042 0.0252  47  GLY   A CA  
1239 C  CA  B GLY   A 47  ? 0.1409 0.1573 0.1659 -0.0070 0.0205  0.0089  47  GLY   A CA  
1240 C  C   A GLY   A 47  ? 0.1438 0.1283 0.1279 0.0201  -0.0139 0.0216  47  GLY   A C   
1241 C  C   B GLY   A 47  ? 0.1355 0.1487 0.1496 -0.0005 0.0227  0.0028  47  GLY   A C   
1242 O  O   A GLY   A 47  ? 0.1393 0.1261 0.1428 0.0212  -0.0114 0.0164  47  GLY   A O   
1243 O  O   B GLY   A 47  ? 0.1321 0.1399 0.1598 0.0019  0.0101  0.0061  47  GLY   A O   
1250 N  N   A GLY   A 48  ? 0.1351 0.1276 0.1182 0.0212  -0.0127 0.0208  48  GLY   A N   
1251 N  N   B GLY   A 48  ? 0.1406 0.1531 0.1370 -0.0055 0.0319  0.0026  48  GLY   A N   
1252 C  CA  A GLY   A 48  ? 0.1342 0.1319 0.1148 0.0128  -0.0099 0.0017  48  GLY   A CA  
1253 C  CA  B GLY   A 48  ? 0.1518 0.1516 0.1295 -0.0101 0.0282  -0.0100 48  GLY   A CA  
1254 C  C   A GLY   A 48  ? 0.1209 0.1337 0.0840 0.0033  -0.0071 -0.0063 48  GLY   A C   
1255 C  C   B GLY   A 48  ? 0.1578 0.1576 0.1285 -0.0077 0.0114  -0.0079 48  GLY   A C   
1256 O  O   A GLY   A 48  ? 0.1295 0.1348 0.1176 0.0067  -0.0161 -0.0195 48  GLY   A O   
1257 O  O   B GLY   A 48  ? 0.1582 0.1597 0.1285 -0.0050 0.0028  -0.0196 48  GLY   A O   
1264 N  N   A VAL   A 49  ? 0.1119 0.1244 0.0795 -0.0002 0.0044  -0.0018 49  VAL   A N   
1265 N  N   B VAL   A 49  ? 0.1564 0.1540 0.1253 -0.0068 0.0025  -0.0162 49  VAL   A N   
1266 C  CA  A VAL   A 49  ? 0.1176 0.1218 0.0827 -0.0001 0.0044  -0.0037 49  VAL   A CA  
1267 C  CA  B VAL   A 49  ? 0.1608 0.1590 0.1503 -0.0023 -0.0129 -0.0189 49  VAL   A CA  
1268 C  C   A VAL   A 49  ? 0.1146 0.1214 0.0622 0.0016  0.0086  0.0028  49  VAL   A C   
1269 C  C   B VAL   A 49  ? 0.1551 0.1475 0.1637 -0.0014 -0.0236 -0.0262 49  VAL   A C   
1270 O  O   A VAL   A 49  ? 0.1118 0.1250 0.0665 -0.0091 -0.0026 -0.0099 49  VAL   A O   
1271 O  O   B VAL   A 49  ? 0.1554 0.1515 0.1815 0.0031  -0.0362 -0.0331 49  VAL   A O   
1272 C  CB  A VAL   A 49  ? 0.1371 0.1143 0.0881 -0.0129 0.0003  -0.0082 49  VAL   A CB  
1273 C  CB  B VAL   A 49  ? 0.1722 0.1777 0.1883 0.0079  -0.0185 -0.0096 49  VAL   A CB  
1274 C  CG1 A VAL   A 49  ? 0.1461 0.1119 0.0990 -0.0069 -0.0131 -0.0071 49  VAL   A CG1 
1275 C  CG1 B VAL   A 49  ? 0.1755 0.1755 0.1944 0.0132  -0.0303 0.0010  49  VAL   A CG1 
1276 C  CG2 A VAL   A 49  ? 0.1538 0.1291 0.1128 -0.0285 0.0023  0.0037  49  VAL   A CG2 
1277 C  CG2 B VAL   A 49  ? 0.1810 0.1918 0.2131 0.0099  -0.0141 -0.0076 49  VAL   A CG2 
1296 N  N   A ALA   A 50  ? 0.1185 0.1175 0.0698 0.0017  -0.0021 -0.0015 50  ALA   A N   
1297 N  N   B ALA   A 50  ? 0.1477 0.1372 0.1804 -0.0028 -0.0178 -0.0056 50  ALA   A N   
1298 C  CA  A ALA   A 50  ? 0.1208 0.1187 0.0965 -0.0048 -0.0053 0.0139  50  ALA   A CA  
1299 C  CA  B ALA   A 50  ? 0.1406 0.1336 0.1745 -0.0040 -0.0112 0.0018  50  ALA   A CA  
1300 C  C   A ALA   A 50  ? 0.1221 0.1231 0.0993 -0.0069 0.0004  0.0034  50  ALA   A C   
1301 C  C   B ALA   A 50  ? 0.1314 0.1262 0.1513 -0.0020 -0.0047 0.0065  50  ALA   A C   
1302 O  O   A ALA   A 50  ? 0.1208 0.1220 0.1310 -0.0008 -0.0064 -0.0004 50  ALA   A O   
1303 O  O   B ALA   A 50  ? 0.1230 0.1211 0.1707 -0.0003 -0.0050 0.0120  50  ALA   A O   
1304 C  CB  A ALA   A 50  ? 0.1092 0.1202 0.0891 -0.0036 -0.0004 0.0072  50  ALA   A CB  
1305 C  CB  B ALA   A 50  ? 0.1398 0.1414 0.1857 -0.0029 -0.0089 -0.0054 50  ALA   A CB  
1316 N  N   . GLY   A 51  ? 0.1269 0.1174 0.1367 0.0052  -0.0141 0.0059  51  GLY   A N   
1317 C  CA  . GLY   A 51  ? 0.1350 0.1187 0.1389 0.0072  -0.0121 0.0032  51  GLY   A CA  
1318 C  C   . GLY   A 51  ? 0.1247 0.1333 0.1435 0.0108  -0.0037 -0.0114 51  GLY   A C   
1319 O  O   . GLY   A 51  ? 0.1369 0.1351 0.1539 0.0051  -0.0085 -0.0083 51  GLY   A O   
1324 N  N   A ALA   A 52  ? 0.1223 0.1388 0.1307 0.0110  -0.0118 -0.0073 52  ALA   A N   
1325 N  N   B ALA   A 52  ? 0.1216 0.1412 0.1440 0.0039  0.0020  -0.0065 52  ALA   A N   
1326 C  CA  A ALA   A 52  ? 0.1324 0.1528 0.1395 0.0076  -0.0099 0.0016  52  ALA   A CA  
1327 C  CA  B ALA   A 52  ? 0.1179 0.1480 0.1479 -0.0038 0.0044  -0.0035 52  ALA   A CA  
1328 C  C   A ALA   A 52  ? 0.1305 0.1486 0.1108 0.0032  -0.0005 -0.0149 52  ALA   A C   
1329 C  C   B ALA   A 52  ? 0.1128 0.1481 0.1431 -0.0142 0.0060  -0.0065 52  ALA   A C   
1330 O  O   A ALA   A 52  ? 0.1414 0.1512 0.1228 0.0104  -0.0088 -0.0128 52  ALA   A O   
1331 O  O   B ALA   A 52  ? 0.1123 0.1421 0.1648 -0.0094 0.0140  -0.0149 52  ALA   A O   
1332 C  CB  A ALA   A 52  ? 0.1410 0.1806 0.1524 0.0019  -0.0100 0.0045  52  ALA   A CB  
1333 C  CB  B ALA   A 52  ? 0.1190 0.1633 0.1529 -0.0074 0.0069  -0.0033 52  ALA   A CB  
1344 N  N   A LEU   A 53  ? 0.1269 0.1361 0.1248 -0.0041 -0.0043 -0.0095 53  LEU   A N   
1345 N  N   B LEU   A 53  ? 0.1155 0.1455 0.1376 -0.0126 -0.0037 -0.0017 53  LEU   A N   
1346 C  CA  A LEU   A 53  ? 0.1331 0.1414 0.1257 -0.0042 0.0028  -0.0013 53  LEU   A CA  
1347 C  CA  B LEU   A 53  ? 0.1182 0.1452 0.1284 -0.0035 -0.0050 0.0035  53  LEU   A CA  
1348 C  C   A LEU   A 53  ? 0.1291 0.1436 0.1050 0.0047  -0.0032 -0.0022 53  LEU   A C   
1349 C  C   B LEU   A 53  ? 0.1241 0.1429 0.1078 0.0052  -0.0028 -0.0032 53  LEU   A C   
1350 O  O   A LEU   A 53  ? 0.1381 0.1486 0.1349 -0.0037 -0.0060 -0.0035 53  LEU   A O   
1351 O  O   B LEU   A 53  ? 0.1323 0.1401 0.1076 0.0038  -0.0018 -0.0067 53  LEU   A O   
1352 C  CB  A LEU   A 53  ? 0.1330 0.1397 0.1188 -0.0058 -0.0026 -0.0006 53  LEU   A CB  
1353 C  CB  B LEU   A 53  ? 0.1172 0.1457 0.1308 -0.0047 -0.0079 0.0006  53  LEU   A CB  
1354 C  CG  A LEU   A 53  ? 0.1350 0.1325 0.1294 0.0014  0.0003  0.0017  53  LEU   A CG  
1355 C  CG  B LEU   A 53  ? 0.1220 0.1487 0.1347 0.0007  -0.0149 0.0036  53  LEU   A CG  
1356 C  CD1 A LEU   A 53  ? 0.1232 0.1376 0.1215 0.0093  -0.0107 0.0122  53  LEU   A CD1 
1357 C  CD1 B LEU   A 53  ? 0.1311 0.1543 0.1520 0.0143  -0.0157 -0.0060 53  LEU   A CD1 
1358 C  CD2 A LEU   A 53  ? 0.1601 0.1483 0.1529 0.0019  0.0021  0.0076  53  LEU   A CD2 
1359 C  CD2 B LEU   A 53  ? 0.1191 0.1510 0.1266 -0.0033 -0.0123 0.0141  53  LEU   A CD2 
1382 N  N   . ASN   A 54  ? 0.1270 0.1379 0.1230 -0.0005 -0.0067 0.0048  54  ASN   A N   
1383 C  CA  . ASN   A 54  ? 0.1198 0.1266 0.1335 -0.0011 -0.0079 -0.0039 54  ASN   A CA  
1384 C  C   . ASN   A 54  ? 0.1307 0.1383 0.1217 -0.0093 -0.0080 -0.0048 54  ASN   A C   
1385 O  O   . ASN   A 54  ? 0.1335 0.1458 0.1388 -0.0058 -0.0072 -0.0129 54  ASN   A O   
1386 C  CB  . ASN   A 54  ? 0.1193 0.1366 0.1304 -0.0014 -0.0073 -0.0071 54  ASN   A CB  
1387 C  CG  . ASN   A 54  ? 0.1199 0.1324 0.1432 -0.0046 -0.0001 -0.0081 54  ASN   A CG  
1388 O  OD1 . ASN   A 54  ? 0.1184 0.1322 0.1597 -0.0019 -0.0143 -0.0012 54  ASN   A OD1 
1389 N  ND2 . ASN   A 54  ? 0.1312 0.1318 0.1638 -0.0084 -0.0126 0.0055  54  ASN   A ND2 
1397 N  N   . LYS   A 55  ? 0.1275 0.1373 0.1377 -0.0019 0.0011  -0.0095 55  LYS   A N   
1398 C  CA  . LYS   A 55  ? 0.1376 0.1496 0.1400 0.0033  -0.0100 -0.0207 55  LYS   A CA  
1399 C  C   . LYS   A 55  ? 0.1314 0.1568 0.1514 0.0010  -0.0144 -0.0221 55  LYS   A C   
1400 O  O   . LYS   A 55  ? 0.1417 0.1623 0.1612 0.0071  -0.0155 -0.0301 55  LYS   A O   
1401 C  CB  . LYS   A 55  ? 0.1490 0.1537 0.1479 0.0160  -0.0074 -0.0191 55  LYS   A CB  
1402 C  CG  . LYS   A 55  ? 0.1679 0.1762 0.1714 0.0272  -0.0190 -0.0312 55  LYS   A CG  
1403 C  CD  . LYS   A 55  ? 0.1797 0.1928 0.1974 0.0458  -0.0116 -0.0183 55  LYS   A CD  
1404 C  CE  . LYS   A 55  ? 0.2074 0.2234 0.2379 0.0556  -0.0264 -0.0164 55  LYS   A CE  
1405 N  NZ  . LYS   A 55  ? 0.2139 0.2367 0.2423 0.0635  -0.0294 -0.0173 55  LYS   A NZ  
1419 N  N   . ALA   A 56  ? 0.1349 0.1611 0.1456 -0.0037 -0.0027 -0.0194 56  ALA   A N   
1420 C  CA  . ALA   A 56  ? 0.1465 0.1760 0.1422 -0.0085 0.0037  -0.0169 56  ALA   A CA  
1421 C  C   . ALA   A 56  ? 0.1519 0.1845 0.1202 -0.0106 0.0045  -0.0179 56  ALA   A C   
1422 O  O   . ALA   A 56  ? 0.1534 0.2187 0.1371 0.0021  0.0053  -0.0185 56  ALA   A O   
1423 C  CB  . ALA   A 56  ? 0.1520 0.1953 0.1539 -0.0127 0.0063  -0.0111 56  ALA   A CB  
1429 N  N   . THR   A 57  ? 0.1368 0.1609 0.1162 -0.0093 -0.0000 -0.0215 57  THR   A N   
1430 C  CA  . THR   A 57  ? 0.1457 0.1638 0.1271 -0.0083 -0.0036 -0.0117 57  THR   A CA  
1431 C  C   . THR   A 57  ? 0.1436 0.1690 0.1382 -0.0022 -0.0078 -0.0216 57  THR   A C   
1432 O  O   . THR   A 57  ? 0.1424 0.1686 0.1595 -0.0135 -0.0106 -0.0306 57  THR   A O   
1433 C  CB  . THR   A 57  ? 0.1411 0.1580 0.1394 -0.0066 -0.0065 -0.0100 57  THR   A CB  
1434 O  OG1 . THR   A 57  ? 0.1329 0.1567 0.1422 -0.0037 -0.0005 -0.0077 57  THR   A OG1 
1435 C  CG2 . THR   A 57  ? 0.1449 0.1535 0.1221 -0.0029 0.0032  0.0004  57  THR   A CG2 
1443 N  N   . ASN   A 58  ? 0.1462 0.1587 0.1538 -0.0044 0.0023  -0.0240 58  ASN   A N   
1444 C  CA  . ASN   A 58  ? 0.1643 0.1588 0.1761 -0.0031 0.0023  -0.0390 58  ASN   A CA  
1445 C  C   . ASN   A 58  ? 0.1447 0.1438 0.1563 0.0032  -0.0023 -0.0251 58  ASN   A C   
1446 O  O   . ASN   A 58  ? 0.1483 0.1535 0.1806 -0.0109 -0.0051 -0.0279 58  ASN   A O   
1447 C  CB  . ASN   A 58  ? 0.2133 0.1719 0.2008 -0.0134 0.0288  -0.0487 58  ASN   A CB  
1448 C  CG  . ASN   A 58  ? 0.2531 0.1987 0.2715 -0.0096 0.0325  -0.0259 58  ASN   A CG  
1449 O  OD1 . ASN   A 58  ? 0.2770 0.1925 0.3166 0.0258  0.0621  -0.0120 58  ASN   A OD1 
1450 N  ND2 . ASN   A 58  ? 0.2613 0.2074 0.2961 -0.0109 0.0128  -0.0344 58  ASN   A ND2 
1457 N  N   . ASN   A 59  ? 0.1315 0.1401 0.1445 -0.0046 -0.0121 -0.0190 59  ASN   A N   
1458 C  CA  . ASN   A 59  ? 0.1373 0.1270 0.1412 -0.0020 -0.0086 -0.0082 59  ASN   A CA  
1459 C  C   . ASN   A 59  ? 0.1370 0.1323 0.1409 -0.0091 -0.0020 0.0010  59  ASN   A C   
1460 O  O   . ASN   A 59  ? 0.1385 0.1367 0.1430 -0.0085 -0.0065 0.0076  59  ASN   A O   
1461 C  CB  . ASN   A 59  ? 0.1456 0.1326 0.1519 0.0041  -0.0207 -0.0168 59  ASN   A CB  
1462 C  CG  . ASN   A 59  ? 0.1443 0.1354 0.1513 0.0010  -0.0375 -0.0039 59  ASN   A CG  
1463 O  OD1 . ASN   A 59  ? 0.1524 0.1469 0.1527 -0.0062 -0.0276 -0.0020 59  ASN   A OD1 
1464 N  ND2 . ASN   A 59  ? 0.1555 0.1371 0.1739 -0.0157 -0.0239 0.0083  59  ASN   A ND2 
1471 N  N   . ALA   A 60  ? 0.1233 0.1380 0.1323 -0.0038 -0.0059 0.0040  60  ALA   A N   
1472 C  CA  . ALA   A 60  ? 0.1267 0.1411 0.1444 0.0006  -0.0145 -0.0020 60  ALA   A CA  
1473 C  C   . ALA   A 60  ? 0.1271 0.1362 0.1616 -0.0055 -0.0029 0.0019  60  ALA   A C   
1474 O  O   . ALA   A 60  ? 0.1213 0.1372 0.1830 -0.0082 -0.0105 -0.0010 60  ALA   A O   
1475 C  CB  . ALA   A 60  ? 0.1356 0.1493 0.1512 -0.0010 -0.0217 -0.0236 60  ALA   A CB  
1481 N  N   . MET   A 61  ? 0.1217 0.1288 0.1514 -0.0059 0.0033  -0.0056 61  MET   A N   
1482 C  CA  . MET   A 61  ? 0.1251 0.1236 0.1439 -0.0047 0.0017  0.0021  61  MET   A CA  
1483 C  C   . MET   A 61  ? 0.1248 0.1200 0.1485 -0.0099 -0.0042 -0.0058 61  MET   A C   
1484 O  O   . MET   A 61  ? 0.1315 0.1219 0.1559 -0.0030 0.0070  0.0060  61  MET   A O   
1485 C  CB  . MET   A 61  ? 0.1259 0.1290 0.1391 -0.0030 0.0009  -0.0010 61  MET   A CB  
1486 C  CG  . MET   A 61  ? 0.1297 0.1323 0.1479 -0.0008 -0.0044 0.0001  61  MET   A CG  
1487 S  SD  . MET   A 61  ? 0.1333 0.1370 0.1732 -0.0075 -0.0031 -0.0145 61  MET   A SD  
1488 C  CE  . MET   A 61  ? 0.1492 0.1546 0.1896 -0.0098 0.0055  -0.0126 61  MET   A CE  
1498 N  N   . GLN   A 62  ? 0.1287 0.1189 0.1460 -0.0074 -0.0118 0.0064  62  GLN   A N   
1499 C  CA  . GLN   A 62  ? 0.1384 0.1191 0.1578 -0.0069 -0.0039 0.0002  62  GLN   A CA  
1500 C  C   . GLN   A 62  ? 0.1373 0.1191 0.1473 0.0004  0.0028  0.0011  62  GLN   A C   
1501 O  O   . GLN   A 62  ? 0.1372 0.1289 0.1581 -0.0032 0.0030  -0.0029 62  GLN   A O   
1502 C  CB  . GLN   A 62  ? 0.1330 0.1173 0.1539 -0.0023 -0.0030 0.0035  62  GLN   A CB  
1503 C  CG  . GLN   A 62  ? 0.1330 0.1202 0.1480 -0.0008 -0.0102 0.0148  62  GLN   A CG  
1504 C  CD  . GLN   A 62  ? 0.1404 0.1213 0.1567 0.0049  0.0070  0.0139  62  GLN   A CD  
1505 O  OE1 . GLN   A 62  ? 0.1401 0.1314 0.1761 -0.0000 0.0024  0.0013  62  GLN   A OE1 
1506 N  NE2 . GLN   A 62  ? 0.1505 0.1267 0.1552 0.0017  0.0095  -0.0017 62  GLN   A NE2 
1515 N  N   . VAL   A 63  ? 0.1264 0.1276 0.1594 -0.0089 0.0083  -0.0180 63  VAL   A N   
1516 C  CA  . VAL   A 63  ? 0.1297 0.1324 0.1871 -0.0144 -0.0022 -0.0124 63  VAL   A CA  
1517 C  C   . VAL   A 63  ? 0.1198 0.1272 0.1788 -0.0123 -0.0104 -0.0125 63  VAL   A C   
1518 O  O   . VAL   A 63  ? 0.1222 0.1259 0.2016 -0.0152 -0.0064 -0.0033 63  VAL   A O   
1519 C  CB  . VAL   A 63  ? 0.1394 0.1519 0.2259 -0.0057 -0.0108 -0.0322 63  VAL   A CB  
1520 C  CG1 . VAL   A 63  ? 0.1503 0.1724 0.2685 -0.0055 -0.0046 -0.0639 63  VAL   A CG1 
1521 C  CG2 . VAL   A 63  ? 0.1520 0.1458 0.2354 -0.0091 0.0053  -0.0252 63  VAL   A CG2 
1531 N  N   . GLU   A 64  ? 0.1245 0.1355 0.1757 -0.0036 -0.0060 -0.0045 64  GLU   A N   
1532 C  CA  . GLU   A 64  ? 0.1219 0.1363 0.1568 -0.0088 -0.0102 -0.0030 64  GLU   A CA  
1533 C  C   . GLU   A 64  ? 0.1142 0.1348 0.1573 -0.0093 0.0047  0.0051  64  GLU   A C   
1534 O  O   . GLU   A 64  ? 0.1305 0.1352 0.1682 -0.0003 0.0065  0.0016  64  GLU   A O   
1535 C  CB  . GLU   A 64  ? 0.1356 0.1477 0.1704 -0.0061 -0.0022 -0.0094 64  GLU   A CB  
1536 C  CG  . GLU   A 64  ? 0.1378 0.1510 0.1767 -0.0135 -0.0061 -0.0064 64  GLU   A CG  
1537 C  CD  . GLU   A 64  ? 0.1496 0.1571 0.1859 -0.0161 -0.0030 0.0034  64  GLU   A CD  
1538 O  OE1 . GLU   A 64  ? 0.1458 0.1627 0.2116 -0.0188 0.0023  -0.0029 64  GLU   A OE1 
1539 O  OE2 . GLU   A 64  ? 0.1626 0.1605 0.1763 -0.0234 -0.0124 0.0064  64  GLU   A OE2 
1546 N  N   . SER   A 65  ? 0.1109 0.1354 0.1558 -0.0032 -0.0011 0.0062  65  SER   A N   
1547 C  CA  . SER   A 65  ? 0.1228 0.1271 0.1400 -0.0007 -0.0056 -0.0032 65  SER   A CA  
1548 C  C   . SER   A 65  ? 0.1243 0.1318 0.1560 -0.0050 0.0002  -0.0005 65  SER   A C   
1549 O  O   . SER   A 65  ? 0.1355 0.1367 0.1763 -0.0017 0.0100  0.0008  65  SER   A O   
1550 C  CB  . SER   A 65  ? 0.1242 0.1317 0.1587 -0.0099 -0.0004 0.0096  65  SER   A CB  
1551 O  OG  . SER   A 65  ? 0.1244 0.1364 0.1578 -0.0070 -0.0073 0.0093  65  SER   A OG  
1557 N  N   . ASP   A 66  ? 0.1280 0.1283 0.1777 -0.0048 0.0050  0.0117  66  ASP   A N   
1558 C  CA  . ASP   A 66  ? 0.1364 0.1336 0.1879 -0.0021 0.0082  0.0200  66  ASP   A CA  
1559 C  C   . ASP   A 66  ? 0.1310 0.1374 0.1955 -0.0031 0.0088  0.0235  66  ASP   A C   
1560 O  O   . ASP   A 66  ? 0.1373 0.1471 0.2050 -0.0019 0.0184  0.0267  66  ASP   A O   
1561 C  CB  . ASP   A 66  ? 0.1460 0.1498 0.2187 0.0060  0.0121  0.0386  66  ASP   A CB  
1562 C  CG  . ASP   A 66  ? 0.1633 0.1613 0.2334 0.0061  -0.0030 0.0470  66  ASP   A CG  
1563 O  OD1 . ASP   A 66  ? 0.1645 0.1933 0.2137 -0.0056 -0.0137 0.0477  66  ASP   A OD1 
1564 O  OD2 . ASP   A 66  ? 0.1786 0.1722 0.3079 0.0227  -0.0146 0.0273  66  ASP   A OD2 
1569 N  N   . ASP   A 67  ? 0.1244 0.1361 0.2014 -0.0023 0.0049  0.0234  67  ASP   A N   
1570 C  CA  . ASP   A 67  ? 0.1267 0.1579 0.2125 -0.0041 0.0102  0.0308  67  ASP   A CA  
1571 C  C   . ASP   A 67  ? 0.1297 0.1576 0.2165 -0.0030 0.0149  0.0315  67  ASP   A C   
1572 O  O   . ASP   A 67  ? 0.1259 0.1693 0.2392 -0.0007 0.0193  0.0410  67  ASP   A O   
1573 C  CB  . ASP   A 67  ? 0.1252 0.1721 0.2448 -0.0049 -0.0080 0.0406  67  ASP   A CB  
1574 C  CG  . ASP   A 67  ? 0.1287 0.1807 0.2835 -0.0100 -0.0218 0.0472  67  ASP   A CG  
1575 O  OD1 . ASP   A 67  ? 0.1390 0.1985 0.3688 -0.0132 -0.0385 0.0652  67  ASP   A OD1 
1576 O  OD2 . ASP   A 67  ? 0.1311 0.1831 0.2499 0.0010  -0.0121 0.0402  67  ASP   A OD2 
1581 N  N   . TYR   A 68  ? 0.1353 0.1369 0.2045 0.0050  0.0185  0.0353  68  TYR   A N   
1582 C  CA  . TYR   A 68  ? 0.1447 0.1364 0.1838 0.0028  0.0303  0.0279  68  TYR   A CA  
1583 C  C   . TYR   A 68  ? 0.1435 0.1376 0.1829 0.0002  0.0239  0.0231  68  TYR   A C   
1584 O  O   . TYR   A 68  ? 0.1504 0.1444 0.2074 0.0095  0.0299  0.0190  68  TYR   A O   
1585 C  CB  . TYR   A 68  ? 0.1524 0.1381 0.2025 0.0106  0.0387  0.0305  68  TYR   A CB  
1586 C  CG  . TYR   A 68  ? 0.1552 0.1563 0.2407 0.0097  0.0546  0.0277  68  TYR   A CG  
1587 C  CD1 . TYR   A 68  ? 0.1600 0.1642 0.2691 -0.0180 0.0522  -0.0064 68  TYR   A CD1 
1588 C  CD2 . TYR   A 68  ? 0.1755 0.1621 0.2848 0.0158  0.0678  0.0337  68  TYR   A CD2 
1589 C  CE1 . TYR   A 68  ? 0.1704 0.1817 0.3168 -0.0167 0.0623  -0.0170 68  TYR   A CE1 
1590 C  CE2 . TYR   A 68  ? 0.1777 0.1670 0.3016 0.0035  0.0817  0.0037  68  TYR   A CE2 
1591 C  CZ  . TYR   A 68  ? 0.1701 0.1657 0.3242 -0.0147 0.0677  -0.0210 68  TYR   A CZ  
1592 O  OH  . TYR   A 68  ? 0.2042 0.1657 0.3636 -0.0159 0.0499  -0.0450 68  TYR   A OH  
1602 N  N   . ILE   A 69  ? 0.1311 0.1330 0.1817 0.0042  0.0205  0.0189  69  ILE   A N   
1603 C  CA  . ILE   A 69  ? 0.1377 0.1349 0.1805 0.0065  0.0115  0.0014  69  ILE   A CA  
1604 C  C   . ILE   A 69  ? 0.1449 0.1339 0.1816 0.0097  0.0194  0.0243  69  ILE   A C   
1605 O  O   . ILE   A 69  ? 0.1434 0.1492 0.1889 0.0070  0.0212  0.0272  69  ILE   A O   
1606 C  CB  . ILE   A 69  ? 0.1381 0.1628 0.1919 0.0091  0.0233  -0.0104 69  ILE   A CB  
1607 C  CG1 . ILE   A 69  ? 0.1374 0.1765 0.1940 0.0112  0.0192  -0.0212 69  ILE   A CG1 
1608 C  CG2 . ILE   A 69  ? 0.1571 0.1791 0.2009 0.0169  0.0057  -0.0165 69  ILE   A CG2 
1609 C  CD1 . ILE   A 69  ? 0.1516 0.1829 0.2178 0.0043  0.0157  -0.0196 69  ILE   A CD1 
1621 N  N   . ALA   A 70  ? 0.1483 0.1367 0.1854 -0.0039 0.0173  0.0279  70  ALA   A N   
1622 C  CA  . ALA   A 70  ? 0.1502 0.1553 0.2095 -0.0083 0.0294  0.0244  70  ALA   A CA  
1623 C  C   . ALA   A 70  ? 0.1489 0.1705 0.2061 -0.0092 0.0260  0.0272  70  ALA   A C   
1624 O  O   . ALA   A 70  ? 0.1649 0.2049 0.2230 0.0115  0.0383  0.0380  70  ALA   A O   
1625 C  CB  . ALA   A 70  ? 0.1512 0.1486 0.2330 -0.0118 0.0240  0.0204  70  ALA   A CB  
1631 N  N   . THR   A 71  ? 0.1405 0.1697 0.1922 -0.0043 0.0141  0.0352  71  THR   A N   
1632 C  CA  . THR   A 71  ? 0.1558 0.1861 0.2280 0.0125  0.0194  0.0341  71  THR   A CA  
1633 C  C   . THR   A 71  ? 0.1442 0.1784 0.2508 0.0135  0.0381  0.0285  71  THR   A C   
1634 O  O   . THR   A 71  ? 0.1525 0.2028 0.2900 0.0130  0.0513  0.0003  71  THR   A O   
1635 C  CB  . THR   A 71  ? 0.1840 0.2150 0.2593 0.0213  -0.0142 0.0445  71  THR   A CB  
1636 O  OG1 . THR   A 71  ? 0.2093 0.2321 0.2797 0.0144  -0.0388 0.0354  71  THR   A OG1 
1637 C  CG2 . THR   A 71  ? 0.1911 0.2289 0.2834 0.0259  -0.0218 0.0617  71  THR   A CG2 
1645 N  N   . ASN   A 72  ? 0.1478 0.1630 0.2300 0.0172  0.0246  0.0260  72  ASN   A N   
1646 C  CA  . ASN   A 72  ? 0.1525 0.1580 0.2170 0.0241  0.0363  0.0354  72  ASN   A CA  
1647 C  C   . ASN   A 72  ? 0.1679 0.1552 0.2139 0.0146  0.0502  0.0186  72  ASN   A C   
1648 O  O   . ASN   A 72  ? 0.1824 0.1582 0.2382 0.0210  0.0461  0.0092  72  ASN   A O   
1649 C  CB  . ASN   A 72  ? 0.1805 0.1682 0.2310 0.0214  0.0424  0.0367  72  ASN   A CB  
1650 C  CG  . ASN   A 72  ? 0.2000 0.1864 0.2318 0.0272  0.0415  0.0360  72  ASN   A CG  
1651 O  OD1 . ASN   A 72  ? 0.2162 0.2132 0.2520 0.0236  0.0410  0.0276  72  ASN   A OD1 
1652 N  ND2 . ASN   A 72  ? 0.2144 0.1901 0.2414 0.0488  0.0301  0.0285  72  ASN   A ND2 
1659 N  N   . GLY   A 73  ? 0.1708 0.1519 0.2030 0.0081  0.0454  0.0097  73  GLY   A N   
1660 C  CA  . GLY   A 73  ? 0.1768 0.1505 0.1876 -0.0019 0.0442  0.0114  73  GLY   A CA  
1661 C  C   . GLY   A 73  ? 0.1741 0.1380 0.1746 0.0026  0.0508  0.0339  73  GLY   A C   
1662 O  O   . GLY   A 73  ? 0.1727 0.1471 0.1971 0.0095  0.0328  0.0260  73  GLY   A O   
1666 N  N   . PRO   A 74  ? 0.1826 0.1447 0.1825 -0.0065 0.0541  0.0211  74  PRO   A N   
1667 C  CA  . PRO   A 74  ? 0.1757 0.1459 0.1886 0.0011  0.0559  0.0183  74  PRO   A CA  
1668 C  C   . PRO   A 74  ? 0.1701 0.1330 0.1904 0.0021  0.0411  0.0126  74  PRO   A C   
1669 O  O   . PRO   A 74  ? 0.1811 0.1305 0.2120 0.0043  0.0430  0.0044  74  PRO   A O   
1670 C  CB  . PRO   A 74  ? 0.1868 0.1783 0.2248 0.0006  0.0458  0.0376  74  PRO   A CB  
1671 C  CG  . PRO   A 74  ? 0.2099 0.2097 0.2703 -0.0153 0.0313  0.0298  74  PRO   A CG  
1672 C  CD  . PRO   A 74  ? 0.1988 0.1856 0.2177 -0.0120 0.0365  0.0176  74  PRO   A CD  
1680 N  N   . LEU   A 75  ? 0.1581 0.1227 0.1743 0.0025  0.0275  0.0090  75  LEU   A N   
1681 C  CA  . LEU   A 75  ? 0.1624 0.1248 0.1554 -0.0013 0.0133  0.0128  75  LEU   A CA  
1682 C  C   . LEU   A 75  ? 0.1754 0.1397 0.1395 0.0020  0.0221  0.0212  75  LEU   A C   
1683 O  O   . LEU   A 75  ? 0.2083 0.1530 0.1565 0.0101  0.0069  0.0077  75  LEU   A O   
1684 C  CB  . LEU   A 75  ? 0.1704 0.1345 0.1425 -0.0015 0.0206  0.0165  75  LEU   A CB  
1685 C  CG  . LEU   A 75  ? 0.1872 0.1636 0.1599 -0.0312 0.0106  0.0103  75  LEU   A CG  
1686 C  CD1 . LEU   A 75  ? 0.1925 0.2154 0.1906 -0.0330 0.0113  -0.0035 75  LEU   A CD1 
1687 C  CD2 . LEU   A 75  ? 0.2165 0.2102 0.2157 -0.0096 0.0138  0.0095  75  LEU   A CD2 
1699 N  N   . LYS   A 76  ? 0.1761 0.1363 0.1617 -0.0053 0.0229  0.0070  76  LYS   A N   
1700 C  CA  . LYS   A 76  ? 0.1681 0.1551 0.1682 -0.0091 0.0147  -0.0055 76  LYS   A CA  
1701 C  C   . LYS   A 76  ? 0.1727 0.1371 0.1235 -0.0037 0.0076  0.0025  76  LYS   A C   
1702 O  O   . LYS   A 76  ? 0.1782 0.1296 0.1303 0.0012  0.0143  0.0087  76  LYS   A O   
1703 C  CB  . LYS   A 76  ? 0.1660 0.1773 0.2232 -0.0001 0.0210  -0.0236 76  LYS   A CB  
1704 C  CG  . LYS   A 76  ? 0.1793 0.1635 0.2723 0.0040  0.0108  -0.0143 76  LYS   A CG  
1705 C  CD  . LYS   A 76  ? 0.1881 0.1629 0.3137 0.0065  -0.0019 -0.0162 76  LYS   A CD  
1706 C  CE  . LYS   A 76  ? 0.1998 0.1833 0.3608 0.0039  0.0083  -0.0295 76  LYS   A CE  
1707 N  NZ  . LYS   A 76  ? 0.1981 0.1800 0.3995 -0.0067 -0.0003 -0.0455 76  LYS   A NZ  
1721 N  N   . VAL   A 77  ? 0.1811 0.1412 0.1238 -0.0011 0.0234  0.0138  77  VAL   A N   
1722 C  CA  . VAL   A 77  ? 0.1715 0.1424 0.1350 0.0085  0.0154  0.0170  77  VAL   A CA  
1723 C  C   . VAL   A 77  ? 0.1689 0.1379 0.1377 0.0105  0.0183  0.0086  77  VAL   A C   
1724 O  O   . VAL   A 77  ? 0.1741 0.1408 0.1456 0.0143  0.0325  0.0051  77  VAL   A O   
1725 C  CB  . VAL   A 77  ? 0.1877 0.1561 0.1568 0.0083  0.0164  0.0199  77  VAL   A CB  
1726 C  CG1 . VAL   A 77  ? 0.1856 0.1713 0.1830 0.0124  0.0071  0.0048  77  VAL   A CG1 
1727 C  CG2 . VAL   A 77  ? 0.2066 0.1657 0.1727 0.0016  0.0098  0.0219  77  VAL   A CG2 
1737 N  N   . GLY   A 78  ? 0.1635 0.1307 0.1349 0.0077  0.0225  0.0065  78  GLY   A N   
1738 C  CA  . GLY   A 78  ? 0.1607 0.1327 0.1449 0.0040  0.0255  0.0137  78  GLY   A CA  
1739 C  C   . GLY   A 78  ? 0.1499 0.1281 0.1525 0.0017  0.0247  0.0099  78  GLY   A C   
1740 O  O   . GLY   A 78  ? 0.1443 0.1326 0.1588 0.0041  0.0197  0.0247  78  GLY   A O   
1744 N  N   . GLY   A 79  ? 0.1579 0.1281 0.1389 0.0019  0.0171  0.0100  79  GLY   A N   
1745 C  CA  . GLY   A 79  ? 0.1504 0.1291 0.1401 -0.0028 0.0100  0.0087  79  GLY   A CA  
1746 C  C   . GLY   A 79  ? 0.1364 0.1262 0.1517 -0.0030 0.0127  0.0049  79  GLY   A C   
1747 O  O   . GLY   A 79  ? 0.1380 0.1322 0.1557 0.0171  0.0066  0.0019  79  GLY   A O   
1751 N  N   . SER   A 80  ? 0.1247 0.1405 0.1641 0.0006  0.0230  -0.0047 80  SER   A N   
1752 C  CA  . SER   A 80  ? 0.1274 0.1373 0.1477 0.0015  0.0058  0.0084  80  SER   A CA  
1753 C  C   . SER   A 80  ? 0.1268 0.1395 0.1389 -0.0022 0.0165  0.0177  80  SER   A C   
1754 O  O   . SER   A 80  ? 0.1228 0.1526 0.1947 0.0109  0.0179  0.0033  80  SER   A O   
1755 C  CB  . SER   A 80  ? 0.1413 0.1309 0.1754 -0.0105 0.0147  0.0108  80  SER   A CB  
1756 O  OG  . SER   A 80  ? 0.1616 0.1286 0.2191 0.0039  0.0003  0.0221  80  SER   A OG  
1762 N  N   . CYS   A 81  ? 0.1199 0.1303 0.1462 0.0025  0.0091  0.0095  81  CYS   A N   
1763 C  CA  . CYS   A 81  ? 0.1148 0.1421 0.1485 -0.0034 0.0005  0.0232  81  CYS   A CA  
1764 C  C   . CYS   A 81  ? 0.1207 0.1358 0.1550 -0.0107 -0.0014 0.0252  81  CYS   A C   
1765 O  O   . CYS   A 81  ? 0.1205 0.1560 0.1734 -0.0007 0.0024  0.0262  81  CYS   A O   
1766 C  CB  . CYS   A 81  ? 0.1286 0.1460 0.1788 -0.0056 0.0014  0.0269  81  CYS   A CB  
1767 S  SG  . CYS   A 81  ? 0.1434 0.1338 0.1684 -0.0112 0.0003  0.0156  81  CYS   A SG  
1773 N  N   . VAL   A 82  ? 0.1248 0.1421 0.1529 0.0009  -0.0133 0.0154  82  VAL   A N   
1774 C  CA  . VAL   A 82  ? 0.1402 0.1451 0.1569 0.0064  -0.0048 0.0192  82  VAL   A CA  
1775 C  C   . VAL   A 82  ? 0.1347 0.1418 0.1654 0.0009  -0.0016 0.0186  82  VAL   A C   
1776 O  O   . VAL   A 82  ? 0.1271 0.1558 0.1963 -0.0022 0.0004  -0.0027 82  VAL   A O   
1777 C  CB  . VAL   A 82  ? 0.1724 0.1499 0.1793 0.0109  0.0000  0.0217  82  VAL   A CB  
1778 C  CG1 . VAL   A 82  ? 0.1927 0.1651 0.1932 0.0136  0.0058  0.0299  82  VAL   A CG1 
1779 C  CG2 . VAL   A 82  ? 0.1836 0.1513 0.2070 0.0007  -0.0020 0.0299  82  VAL   A CG2 
1789 N  N   . LEU   A 83  ? 0.1305 0.1388 0.1626 -0.0058 -0.0131 0.0161  83  LEU   A N   
1790 C  CA  . LEU   A 83  ? 0.1362 0.1460 0.1424 -0.0100 -0.0123 0.0097  83  LEU   A CA  
1791 C  C   . LEU   A 83  ? 0.1411 0.1458 0.1421 -0.0077 -0.0175 0.0157  83  LEU   A C   
1792 O  O   . LEU   A 83  ? 0.1469 0.1496 0.1584 -0.0085 -0.0065 0.0292  83  LEU   A O   
1793 C  CB  . LEU   A 83  ? 0.1401 0.1507 0.1484 -0.0087 -0.0166 0.0145  83  LEU   A CB  
1794 C  CG  . LEU   A 83  ? 0.1510 0.1642 0.1621 -0.0134 0.0022  0.0064  83  LEU   A CG  
1795 C  CD1 . LEU   A 83  ? 0.1696 0.1615 0.1659 -0.0300 -0.0102 0.0183  83  LEU   A CD1 
1796 C  CD2 . LEU   A 83  ? 0.1515 0.1791 0.1795 -0.0116 0.0157  0.0197  83  LEU   A CD2 
1808 N  N   . SER   A 84  ? 0.1519 0.1499 0.1485 -0.0065 -0.0126 0.0169  84  SER   A N   
1809 C  CA  . SER   A 84  ? 0.1576 0.1558 0.1370 -0.0051 -0.0131 0.0141  84  SER   A CA  
1810 C  C   . SER   A 84  ? 0.1617 0.1578 0.1326 -0.0122 -0.0027 0.0109  84  SER   A C   
1811 O  O   . SER   A 84  ? 0.1547 0.1718 0.1284 -0.0092 -0.0098 0.0059  84  SER   A O   
1812 C  CB  . SER   A 84  ? 0.1714 0.1724 0.1536 -0.0022 -0.0169 0.0031  84  SER   A CB  
1813 O  OG  . SER   A 84  ? 0.1696 0.1962 0.1588 -0.0066 -0.0218 -0.0044 84  SER   A OG  
1819 N  N   . GLY   A 85  ? 0.1710 0.1655 0.1364 -0.0154 0.0032  0.0084  85  GLY   A N   
1820 C  CA  . GLY   A 85  ? 0.1690 0.1808 0.1492 -0.0193 0.0043  -0.0128 85  GLY   A CA  
1821 C  C   . GLY   A 85  ? 0.1669 0.1879 0.1245 -0.0113 -0.0130 0.0054  85  GLY   A C   
1822 O  O   . GLY   A 85  ? 0.1660 0.2065 0.1364 -0.0212 -0.0009 -0.0133 85  GLY   A O   
1826 N  N   . HIS   A 86  ? 0.1688 0.1766 0.1279 -0.0102 -0.0096 0.0018  86  HIS   A N   
1827 C  CA  . HIS   A 86  ? 0.1876 0.1850 0.1240 -0.0099 -0.0147 0.0030  86  HIS   A CA  
1828 C  C   . HIS   A 86  ? 0.2082 0.1991 0.1114 -0.0135 -0.0108 0.0065  86  HIS   A C   
1829 O  O   . HIS   A 86  ? 0.2192 0.2252 0.1284 -0.0167 0.0053  0.0040  86  HIS   A O   
1830 C  CB  . HIS   A 86  ? 0.1849 0.1776 0.1432 -0.0035 0.0047  0.0039  86  HIS   A CB  
1831 C  CG  . HIS   A 86  ? 0.1815 0.1713 0.1507 -0.0020 0.0091  0.0117  86  HIS   A CG  
1832 N  ND1 . HIS   A 86  ? 0.1949 0.1720 0.1875 -0.0143 0.0000  0.0094  86  HIS   A ND1 
1833 C  CD2 . HIS   A 86  ? 0.1861 0.1687 0.1317 0.0080  0.0148  0.0202  86  HIS   A CD2 
1834 C  CE1 . HIS   A 86  ? 0.1922 0.1752 0.1758 -0.0130 0.0213  0.0191  86  HIS   A CE1 
1835 N  NE2 . HIS   A 86  ? 0.1892 0.1671 0.1637 0.0077  0.0141  0.0308  86  HIS   A NE2 
1843 N  N   . ASN   A 87  ? 0.2147 0.2047 0.1344 0.0014  0.0111  -0.0051 87  ASN   A N   
1844 C  CA  . ASN   A 87  ? 0.2358 0.2172 0.1543 -0.0027 0.0294  -0.0098 87  ASN   A CA  
1845 C  C   . ASN   A 87  ? 0.2353 0.2320 0.1706 -0.0111 0.0444  -0.0029 87  ASN   A C   
1846 O  O   . ASN   A 87  ? 0.2632 0.2470 0.2252 -0.0307 0.0827  -0.0130 87  ASN   A O   
1847 C  CB  . ASN   A 87  ? 0.2516 0.2232 0.1634 0.0016  0.0318  -0.0113 87  ASN   A CB  
1848 C  CG  . ASN   A 87  ? 0.2647 0.2249 0.1714 0.0095  0.0440  0.0031  87  ASN   A CG  
1849 O  OD1 . ASN   A 87  ? 0.2804 0.2156 0.1776 0.0270  0.0395  0.0083  87  ASN   A OD1 
1850 N  ND2 . ASN   A 87  ? 0.2698 0.2473 0.1663 0.0078  0.0432  0.0138  87  ASN   A ND2 
1857 N  N   . LEU   A 88  ? 0.2044 0.2235 0.1693 -0.0149 0.0138  0.0199  88  LEU   A N   
1858 C  CA  . LEU   A 88  ? 0.1853 0.2205 0.1879 -0.0232 0.0264  0.0249  88  LEU   A CA  
1859 C  C   . LEU   A 88  ? 0.1795 0.2252 0.1707 -0.0230 0.0128  0.0327  88  LEU   A C   
1860 O  O   . LEU   A 88  ? 0.1859 0.2292 0.2090 -0.0188 0.0144  0.0599  88  LEU   A O   
1861 C  CB  . LEU   A 88  ? 0.1888 0.2239 0.2030 -0.0313 -0.0066 0.0349  88  LEU   A CB  
1862 C  CG  . LEU   A 88  ? 0.2087 0.2317 0.2226 -0.0265 -0.0184 0.0326  88  LEU   A CG  
1863 C  CD1 . LEU   A 88  ? 0.2209 0.2431 0.2110 -0.0249 -0.0160 0.0187  88  LEU   A CD1 
1864 C  CD2 . LEU   A 88  ? 0.2279 0.2375 0.2569 -0.0188 -0.0124 0.0192  88  LEU   A CD2 
1876 N  N   . ALA   A 89  ? 0.1824 0.2141 0.1478 -0.0184 0.0080  0.0080  89  ALA   A N   
1877 C  CA  . ALA   A 89  ? 0.1852 0.2109 0.1408 -0.0209 -0.0002 0.0222  89  ALA   A CA  
1878 C  C   . ALA   A 89  ? 0.1898 0.2140 0.1445 -0.0109 -0.0115 0.0183  89  ALA   A C   
1879 O  O   . ALA   A 89  ? 0.1896 0.2108 0.1845 -0.0252 -0.0100 -0.0092 89  ALA   A O   
1880 C  CB  . ALA   A 89  ? 0.1773 0.2138 0.1170 -0.0230 -0.0076 0.0188  89  ALA   A CB  
1886 N  N   . LYS   A 90  ? 0.2047 0.2252 0.1353 -0.0151 -0.0227 0.0218  90  LYS   A N   
1887 C  CA  . LYS   A 90  ? 0.2110 0.2371 0.1356 -0.0113 -0.0360 0.0145  90  LYS   A CA  
1888 C  C   . LYS   A 90  ? 0.1871 0.2246 0.1313 -0.0142 -0.0348 0.0081  90  LYS   A C   
1889 O  O   . LYS   A 90  ? 0.1921 0.2336 0.1785 -0.0258 -0.0433 -0.0063 90  LYS   A O   
1890 C  CB  . LYS   A 90  ? 0.2331 0.2676 0.1732 -0.0096 -0.0464 0.0448  90  LYS   A CB  
1891 C  CG  . LYS   A 90  ? 0.2721 0.3021 0.2702 -0.0111 -0.0489 0.0610  90  LYS   A CG  
1892 C  CD  . LYS   A 90  ? 0.3251 0.3427 0.3795 -0.0157 -0.0310 0.0706  90  LYS   A CD  
1893 C  CE  . LYS   A 90  ? 0.3671 0.3816 0.4610 -0.0187 -0.0140 0.0635  90  LYS   A CE  
1894 N  NZ  . LYS   A 90  ? 0.4010 0.4052 0.5179 -0.0221 -0.0050 0.0592  90  LYS   A NZ  
1908 N  N   . HIS   A 91  ? 0.1777 0.1906 0.1125 -0.0126 -0.0300 0.0130  91  HIS   A N   
1909 C  CA  . HIS   A 91  ? 0.1737 0.1754 0.1226 -0.0127 -0.0279 0.0138  91  HIS   A CA  
1910 C  C   . HIS   A 91  ? 0.1547 0.1678 0.1081 -0.0180 -0.0244 0.0193  91  HIS   A C   
1911 O  O   . HIS   A 91  ? 0.1466 0.1808 0.1360 -0.0215 -0.0078 0.0214  91  HIS   A O   
1912 C  CB  . HIS   A 91  ? 0.1877 0.2028 0.1839 0.0094  -0.0462 0.0149  91  HIS   A CB  
1913 C  CG  . HIS   A 91  ? 0.2170 0.2492 0.2405 0.0189  -0.0656 0.0056  91  HIS   A CG  
1914 N  ND1 . HIS   A 91  ? 0.2278 0.2782 0.2751 0.0167  -0.0726 -0.0185 91  HIS   A ND1 
1915 C  CD2 . HIS   A 91  ? 0.2411 0.2707 0.2737 0.0216  -0.0828 0.0150  91  HIS   A CD2 
1916 C  CE1 . HIS   A 91  ? 0.2390 0.2860 0.2982 0.0238  -0.0723 -0.0053 91  HIS   A CE1 
1917 N  NE2 . HIS   A 91  ? 0.2519 0.2846 0.2973 0.0288  -0.0863 0.0024  91  HIS   A NE2 
1925 N  N   . CYS   A 92  ? 0.1484 0.1599 0.1191 -0.0146 -0.0248 0.0196  92  CYS   A N   
1926 C  CA  . CYS   A 92  ? 0.1364 0.1483 0.1336 -0.0108 -0.0012 0.0128  92  CYS   A CA  
1927 C  C   . CYS   A 92  ? 0.1287 0.1439 0.1354 -0.0076 0.0005  0.0110  92  CYS   A C   
1928 O  O   . CYS   A 92  ? 0.1335 0.1506 0.1514 -0.0096 -0.0032 0.0085  92  CYS   A O   
1929 C  CB  . CYS   A 92  ? 0.1379 0.1515 0.1509 -0.0069 -0.0079 0.0125  92  CYS   A CB  
1930 S  SG  . CYS   A 92  ? 0.1404 0.1400 0.1373 -0.0105 -0.0043 0.0068  92  CYS   A SG  
1936 N  N   . LEU   A 93  ? 0.1289 0.1351 0.1390 -0.0082 0.0019  0.0128  93  LEU   A N   
1937 C  CA  . LEU   A 93  ? 0.1228 0.1321 0.1376 -0.0051 0.0064  0.0087  93  LEU   A CA  
1938 C  C   . LEU   A 93  ? 0.1225 0.1222 0.1321 0.0009  0.0082  0.0089  93  LEU   A C   
1939 O  O   . LEU   A 93  ? 0.1171 0.1306 0.1373 0.0010  0.0018  0.0130  93  LEU   A O   
1940 C  CB  . LEU   A 93  ? 0.1295 0.1308 0.1495 -0.0036 -0.0094 0.0168  93  LEU   A CB  
1941 C  CG  . LEU   A 93  ? 0.1345 0.1341 0.1506 -0.0049 -0.0011 0.0166  93  LEU   A CG  
1942 C  CD1 . LEU   A 93  ? 0.1416 0.1345 0.1846 -0.0031 0.0064  0.0155  93  LEU   A CD1 
1943 C  CD2 . LEU   A 93  ? 0.1515 0.1327 0.1834 -0.0094 0.0011  0.0176  93  LEU   A CD2 
1955 N  N   . HIS   A 94  ? 0.1168 0.1216 0.1401 -0.0012 0.0035  0.0169  94  HIS   A N   
1956 C  CA  . HIS   A 94  ? 0.1125 0.1160 0.1359 -0.0027 0.0004  0.0155  94  HIS   A CA  
1957 C  C   . HIS   A 94  ? 0.1166 0.1227 0.1373 -0.0039 0.0030  0.0106  94  HIS   A C   
1958 O  O   . HIS   A 94  ? 0.1165 0.1359 0.1769 0.0024  0.0095  -0.0060 94  HIS   A O   
1959 C  CB  . HIS   A 94  ? 0.1180 0.1185 0.1481 -0.0008 -0.0010 0.0153  94  HIS   A CB  
1960 C  CG  . HIS   A 94  ? 0.1206 0.1159 0.1365 -0.0007 -0.0064 0.0102  94  HIS   A CG  
1961 N  ND1 . HIS   A 94  ? 0.1235 0.1226 0.1511 -0.0098 -0.0056 0.0123  94  HIS   A ND1 
1962 C  CD2 . HIS   A 94  ? 0.1280 0.1283 0.1445 -0.0044 -0.0080 0.0048  94  HIS   A CD2 
1963 C  CE1 . HIS   A 94  ? 0.1318 0.1243 0.1462 -0.0052 -0.0160 0.0070  94  HIS   A CE1 
1964 N  NE2 . HIS   A 94  ? 0.1302 0.1266 0.1366 -0.0087 -0.0063 0.0077  94  HIS   A NE2 
1972 N  N   . VAL   A 95  ? 0.1181 0.1177 0.1290 -0.0015 0.0037  -0.0010 95  VAL   A N   
1973 C  CA  . VAL   A 95  ? 0.1204 0.1234 0.1098 -0.0035 0.0151  0.0108  95  VAL   A CA  
1974 C  C   . VAL   A 95  ? 0.1294 0.1223 0.1126 -0.0171 0.0032  0.0015  95  VAL   A C   
1975 O  O   . VAL   A 95  ? 0.1283 0.1280 0.1366 0.0109  0.0016  0.0030  95  VAL   A O   
1976 C  CB  . VAL   A 95  ? 0.1220 0.1299 0.1373 -0.0102 0.0178  0.0065  95  VAL   A CB  
1977 C  CG1 . VAL   A 95  ? 0.1418 0.1265 0.1556 -0.0119 0.0096  -0.0026 95  VAL   A CG1 
1978 C  CG2 . VAL   A 95  ? 0.1274 0.1318 0.1460 -0.0139 0.0048  0.0250  95  VAL   A CG2 
1988 N  N   . VAL   A 96  ? 0.1330 0.1224 0.1022 -0.0026 0.0071  0.0203  96  VAL   A N   
1989 C  CA  . VAL   A 96  ? 0.1387 0.1282 0.1304 -0.0026 0.0103  0.0224  96  VAL   A CA  
1990 C  C   . VAL   A 96  ? 0.1417 0.1325 0.1350 -0.0005 0.0119  0.0163  96  VAL   A C   
1991 O  O   . VAL   A 96  ? 0.1439 0.1346 0.1526 -0.0010 0.0178  0.0038  96  VAL   A O   
1992 C  CB  . VAL   A 96  ? 0.1440 0.1295 0.1296 -0.0050 0.0178  0.0212  96  VAL   A CB  
1993 C  CG1 . VAL   A 96  ? 0.1513 0.1341 0.1328 0.0006  0.0186  0.0128  96  VAL   A CG1 
1994 C  CG2 . VAL   A 96  ? 0.1356 0.1387 0.1556 -0.0128 0.0121  0.0049  96  VAL   A CG2 
2004 N  N   . GLY   A 97  ? 0.1363 0.1354 0.1239 -0.0065 0.0107  0.0101  97  GLY   A N   
2005 C  CA  . GLY   A 97  ? 0.1410 0.1413 0.1316 -0.0010 0.0050  0.0210  97  GLY   A CA  
2006 C  C   . GLY   A 97  ? 0.1504 0.1533 0.1325 -0.0037 0.0026  0.0091  97  GLY   A C   
2007 O  O   . GLY   A 97  ? 0.1616 0.1494 0.1522 -0.0078 -0.0032 0.0215  97  GLY   A O   
2011 N  N   A PRO   A 98  ? 0.1574 0.1591 0.1229 0.0024  -0.0016 0.0142  98  PRO   A N   
2012 N  N   B PRO   A 98  ? 0.1580 0.1548 0.1342 -0.0048 -0.0077 0.0221  98  PRO   A N   
2013 C  CA  A PRO   A 98  ? 0.1618 0.1826 0.1310 0.0037  0.0041  0.0043  98  PRO   A CA  
2014 C  CA  B PRO   A 98  ? 0.1675 0.1634 0.1465 -0.0070 -0.0178 0.0261  98  PRO   A CA  
2015 C  C   A PRO   A 98  ? 0.1665 0.1878 0.1092 -0.0006 0.0082  0.0116  98  PRO   A C   
2016 C  C   B PRO   A 98  ? 0.1877 0.1550 0.1470 -0.0118 -0.0239 0.0347  98  PRO   A C   
2017 O  O   A PRO   A 98  ? 0.1656 0.1739 0.1337 0.0037  0.0089  0.0112  98  PRO   A O   
2018 O  O   B PRO   A 98  ? 0.1857 0.1501 0.1765 -0.0077 -0.0166 0.0325  98  PRO   A O   
2019 C  CB  A PRO   A 98  ? 0.1653 0.1874 0.1264 0.0131  -0.0057 0.0004  98  PRO   A CB  
2020 C  CB  B PRO   A 98  ? 0.1657 0.1638 0.1371 -0.0014 -0.0168 0.0270  98  PRO   A CB  
2021 C  CG  A PRO   A 98  ? 0.1714 0.1726 0.1311 0.0108  -0.0127 -0.0046 98  PRO   A CG  
2022 C  CG  B PRO   A 98  ? 0.1709 0.1597 0.1420 -0.0046 -0.0194 0.0243  98  PRO   A CG  
2023 C  CD  A PRO   A 98  ? 0.1675 0.1568 0.1237 0.0097  -0.0074 0.0039  98  PRO   A CD  
2024 C  CD  B PRO   A 98  ? 0.1625 0.1525 0.1339 -0.0036 -0.0176 0.0268  98  PRO   A CD  
2039 N  N   A ASN   A 99  ? 0.1693 0.2048 0.1170 -0.0047 0.0159  0.0236  99  ASN   A N   
2040 N  N   B ASN   A 99  ? 0.2141 0.1496 0.1203 -0.0099 -0.0270 0.0448  99  ASN   A N   
2041 C  CA  A ASN   A 99  ? 0.1921 0.2156 0.1104 -0.0067 0.0148  0.0283  99  ASN   A CA  
2042 C  CA  B ASN   A 99  ? 0.2439 0.1535 0.1066 -0.0002 -0.0247 0.0512  99  ASN   A CA  
2043 C  C   A ASN   A 99  ? 0.2151 0.2422 0.1072 -0.0197 0.0114  0.0332  99  ASN   A C   
2044 C  C   B ASN   A 99  ? 0.2580 0.1588 0.1204 0.0015  -0.0311 0.0500  99  ASN   A C   
2045 O  O   A ASN   A 99  ? 0.2264 0.2592 0.1281 -0.0106 0.0096  0.0235  99  ASN   A O   
2046 O  O   B ASN   A 99  ? 0.2593 0.1370 0.1186 0.0093  -0.0415 0.0291  99  ASN   A O   
2047 C  CB  A ASN   A 99  ? 0.1874 0.2070 0.1193 -0.0079 0.0002  0.0386  99  ASN   A CB  
2048 C  CB  B ASN   A 99  ? 0.2541 0.1555 0.1303 0.0027  -0.0214 0.0451  99  ASN   A CB  
2049 C  CG  A ASN   A 99  ? 0.1850 0.2039 0.1375 -0.0068 -0.0109 0.0284  99  ASN   A CG  
2050 C  CG  B ASN   A 99  ? 0.2617 0.1648 0.1359 0.0030  -0.0159 0.0425  99  ASN   A CG  
2051 O  OD1 A ASN   A 99  ? 0.1931 0.2158 0.1399 0.0023  -0.0134 0.0193  99  ASN   A OD1 
2052 O  OD1 B ASN   A 99  ? 0.2611 0.1678 0.1081 -0.0008 -0.0134 0.0433  99  ASN   A OD1 
2053 N  ND2 A ASN   A 99  ? 0.1858 0.2041 0.1456 -0.0037 -0.0099 0.0321  99  ASN   A ND2 
2054 N  ND2 B ASN   A 99  ? 0.2652 0.1735 0.1647 0.0123  -0.0244 0.0275  99  ASN   A ND2 
2067 N  N   A VAL   A 100 ? 0.2296 0.2549 0.1238 -0.0398 -0.0109 0.0212  100 VAL   A N   
2068 N  N   B VAL   A 100 ? 0.2692 0.1881 0.1482 -0.0047 -0.0360 0.0487  100 VAL   A N   
2069 C  CA  A VAL   A 100 ? 0.2553 0.2743 0.1395 -0.0422 -0.0141 0.0294  100 VAL   A CA  
2070 C  CA  B VAL   A 100 ? 0.2819 0.2111 0.1961 -0.0063 -0.0397 0.0411  100 VAL   A CA  
2071 C  C   A VAL   A 100 ? 0.2595 0.2872 0.1349 -0.0409 -0.0130 0.0598  100 VAL   A C   
2072 C  C   B VAL   A 100 ? 0.2875 0.2171 0.2123 -0.0036 -0.0420 0.0359  100 VAL   A C   
2073 O  O   A VAL   A 100 ? 0.2661 0.2956 0.1560 -0.0339 0.0057  0.0550  100 VAL   A O   
2074 O  O   B VAL   A 100 ? 0.2887 0.2163 0.2239 -0.0034 -0.0404 0.0221  100 VAL   A O   
2075 C  CB  A VAL   A 100 ? 0.2768 0.2839 0.1856 -0.0497 -0.0216 0.0158  100 VAL   A CB  
2076 C  CB  B VAL   A 100 ? 0.2871 0.2250 0.2247 -0.0056 -0.0395 0.0347  100 VAL   A CB  
2077 C  CG1 A VAL   A 100 ? 0.2803 0.2853 0.2078 -0.0545 -0.0175 0.0124  100 VAL   A CG1 
2078 C  CG1 B VAL   A 100 ? 0.2859 0.2229 0.2360 -0.0054 -0.0378 0.0331  100 VAL   A CG1 
2079 C  CG2 A VAL   A 100 ? 0.2875 0.2893 0.1861 -0.0555 -0.0178 0.0161  100 VAL   A CG2 
2080 C  CG2 B VAL   A 100 ? 0.2896 0.2348 0.2323 -0.0064 -0.0373 0.0286  100 VAL   A CG2 
2099 N  N   A ASN   A 101 ? 0.2606 0.2942 0.1439 -0.0432 -0.0278 0.0853  101 ASN   A N   
2100 N  N   B ASN   A 101 ? 0.2947 0.2269 0.2198 -0.0045 -0.0455 0.0413  101 ASN   A N   
2101 C  CA  A ASN   A 101 ? 0.2815 0.3046 0.1658 -0.0407 -0.0269 0.0975  101 ASN   A CA  
2102 C  CA  B ASN   A 101 ? 0.3061 0.2393 0.2259 -0.0044 -0.0430 0.0429  101 ASN   A CA  
2103 C  C   A ASN   A 101 ? 0.3049 0.3351 0.1930 -0.0440 -0.0028 0.1221  101 ASN   A C   
2104 C  C   B ASN   A 101 ? 0.3182 0.2575 0.2161 0.0027  -0.0365 0.0654  101 ASN   A C   
2105 O  O   A ASN   A 101 ? 0.3194 0.3446 0.2487 -0.0432 0.0025  0.1086  101 ASN   A O   
2106 O  O   B ASN   A 101 ? 0.3240 0.2590 0.1908 0.0024  -0.0395 0.0805  101 ASN   A O   
2107 C  CB  A ASN   A 101 ? 0.2802 0.2803 0.1585 -0.0350 -0.0452 0.0796  101 ASN   A CB  
2108 C  CB  B ASN   A 101 ? 0.3054 0.2356 0.2447 -0.0146 -0.0357 0.0296  101 ASN   A CB  
2109 C  CG  A ASN   A 101 ? 0.2780 0.2551 0.1549 -0.0299 -0.0594 0.0376  101 ASN   A CG  
2110 C  CG  B ASN   A 101 ? 0.3057 0.2388 0.2656 -0.0257 -0.0318 0.0220  101 ASN   A CG  
2111 O  OD1 A ASN   A 101 ? 0.2655 0.2529 0.1529 -0.0128 -0.0477 -0.0027 101 ASN   A OD1 
2112 O  OD1 B ASN   A 101 ? 0.3073 0.2390 0.2815 -0.0316 -0.0318 0.0209  101 ASN   A OD1 
2113 N  ND2 A ASN   A 101 ? 0.2858 0.2397 0.1350 -0.0357 -0.0688 0.0513  101 ASN   A ND2 
2114 N  ND2 B ASN   A 101 ? 0.3088 0.2423 0.2790 -0.0280 -0.0267 0.0202  101 ASN   A ND2 
2127 N  N   A LYS   A 102 ? 0.3076 0.3595 0.2213 -0.0508 0.0128  0.1247  102 LYS   A N   
2128 N  N   B LYS   A 102 ? 0.3217 0.2765 0.2555 0.0073  -0.0213 0.0632  102 LYS   A N   
2129 C  CA  A LYS   A 102 ? 0.3212 0.3817 0.2423 -0.0548 0.0118  0.1189  102 LYS   A CA  
2130 C  CA  B LYS   A 102 ? 0.3281 0.2945 0.2697 0.0051  -0.0085 0.0628  102 LYS   A CA  
2131 C  C   A LYS   A 102 ? 0.3348 0.4030 0.2255 -0.0406 0.0019  0.1107  102 LYS   A C   
2132 C  C   B LYS   A 102 ? 0.3308 0.3007 0.2619 0.0082  -0.0122 0.0731  102 LYS   A C   
2133 O  O   A LYS   A 102 ? 0.3371 0.4161 0.2360 -0.0335 0.0047  0.1059  102 LYS   A O   
2134 O  O   B LYS   A 102 ? 0.3333 0.3022 0.2641 0.0100  -0.0067 0.0824  102 LYS   A O   
2135 C  CB  A LYS   A 102 ? 0.3266 0.3839 0.2873 -0.0699 0.0018  0.1065  102 LYS   A CB  
2136 C  CB  B LYS   A 102 ? 0.3322 0.3052 0.3012 0.0012  -0.0067 0.0497  102 LYS   A CB  
2137 C  CG  A LYS   A 102 ? 0.3334 0.3833 0.3231 -0.0826 -0.0135 0.0895  102 LYS   A CG  
2138 C  CG  B LYS   A 102 ? 0.3369 0.3163 0.3281 -0.0036 -0.0061 0.0379  102 LYS   A CG  
2139 C  CD  A LYS   A 102 ? 0.3461 0.3877 0.3614 -0.0880 -0.0235 0.0652  102 LYS   A CD  
2140 C  CD  B LYS   A 102 ? 0.3438 0.3298 0.3661 -0.0062 -0.0059 0.0250  102 LYS   A CD  
2141 C  CE  A LYS   A 102 ? 0.3581 0.3925 0.3905 -0.0866 -0.0264 0.0498  102 LYS   A CE  
2142 C  CE  B LYS   A 102 ? 0.3500 0.3401 0.3963 -0.0067 -0.0069 0.0191  102 LYS   A CE  
2143 N  NZ  A LYS   A 102 ? 0.3669 0.3952 0.4044 -0.0882 -0.0262 0.0379  102 LYS   A NZ  
2144 N  NZ  B LYS   A 102 ? 0.3535 0.3455 0.4102 -0.0075 -0.0060 0.0180  102 LYS   A NZ  
2171 N  N   A GLY   A 103 ? 0.3425 0.4148 0.2268 -0.0276 -0.0118 0.0868  103 GLY   A N   
2172 N  N   B GLY   A 103 ? 0.3295 0.3072 0.2535 0.0120  -0.0251 0.0647  103 GLY   A N   
2173 C  CA  A GLY   A 103 ? 0.3499 0.4202 0.2177 -0.0183 -0.0116 0.0653  103 GLY   A CA  
2174 C  CA  B GLY   A 103 ? 0.3278 0.3092 0.2512 0.0121  -0.0300 0.0576  103 GLY   A CA  
2175 C  C   A GLY   A 103 ? 0.3496 0.4242 0.2172 -0.0140 -0.0012 0.0423  103 GLY   A C   
2176 C  C   B GLY   A 103 ? 0.3208 0.3068 0.2323 0.0114  -0.0303 0.0466  103 GLY   A C   
2177 O  O   A GLY   A 103 ? 0.3617 0.4360 0.2554 -0.0083 0.0002  0.0261  103 GLY   A O   
2178 O  O   B GLY   A 103 ? 0.3266 0.3121 0.2389 0.0132  -0.0339 0.0457  103 GLY   A O   
2185 N  N   A GLU   A 104 ? 0.3289 0.4096 0.1604 -0.0190 0.0055  0.0342  104 GLU   A N   
2186 N  N   B GLU   A 104 ? 0.3031 0.2927 0.2031 0.0088  -0.0345 0.0484  104 GLU   A N   
2187 C  CA  A GLU   A 104 ? 0.3048 0.3932 0.1551 -0.0309 0.0172  0.0300  104 GLU   A CA  
2188 C  CA  B GLU   A 104 ? 0.2847 0.2771 0.1783 0.0028  -0.0319 0.0380  104 GLU   A CA  
2189 C  C   A GLU   A 104 ? 0.3049 0.4014 0.1760 -0.0334 0.0172  0.0066  104 GLU   A C   
2190 C  C   B GLU   A 104 ? 0.2738 0.2686 0.1691 0.0073  -0.0215 0.0195  104 GLU   A C   
2191 O  O   A GLU   A 104 ? 0.3008 0.4015 0.2001 -0.0390 0.0118  -0.0070 104 GLU   A O   
2192 O  O   B GLU   A 104 ? 0.2703 0.2636 0.1732 0.0082  -0.0275 0.0123  104 GLU   A O   
2193 C  CB  A GLU   A 104 ? 0.2759 0.3674 0.1437 -0.0425 0.0294  0.0554  104 GLU   A CB  
2194 C  CB  B GLU   A 104 ? 0.2774 0.2705 0.1747 -0.0057 -0.0328 0.0520  104 GLU   A CB  
2195 C  CG  A GLU   A 104 ? 0.2563 0.3488 0.1542 -0.0487 0.0215  0.0605  104 GLU   A CG  
2196 C  CG  B GLU   A 104 ? 0.2770 0.2733 0.1963 -0.0118 -0.0370 0.0543  104 GLU   A CG  
2197 C  CD  A GLU   A 104 ? 0.2364 0.3340 0.1606 -0.0513 0.0155  0.0657  104 GLU   A CD  
2198 C  CD  B GLU   A 104 ? 0.2774 0.2778 0.2053 -0.0116 -0.0441 0.0593  104 GLU   A CD  
2199 O  OE1 A GLU   A 104 ? 0.2221 0.3198 0.1259 -0.0501 0.0035  0.0561  104 GLU   A OE1 
2200 O  OE1 B GLU   A 104 ? 0.2798 0.2849 0.2117 -0.0098 -0.0465 0.0537  104 GLU   A OE1 
2201 O  OE2 A GLU   A 104 ? 0.2440 0.3327 0.1901 -0.0534 0.0182  0.0894  104 GLU   A OE2 
2202 O  OE2 B GLU   A 104 ? 0.2805 0.2769 0.2135 -0.0136 -0.0431 0.0658  104 GLU   A OE2 
2215 N  N   A ASP   A 105 ? 0.3061 0.4089 0.1838 -0.0332 0.0249  -0.0109 105 ASP   A N   
2216 N  N   B ASP   A 105 ? 0.2690 0.2657 0.1813 0.0100  -0.0084 0.0042  105 ASP   A N   
2217 C  CA  A ASP   A 105 ? 0.3059 0.4170 0.2109 -0.0272 0.0281  -0.0347 105 ASP   A CA  
2218 C  CA  B ASP   A 105 ? 0.2640 0.2646 0.2071 0.0200  0.0065  -0.0164 105 ASP   A CA  
2219 C  C   A ASP   A 105 ? 0.2735 0.4032 0.1792 -0.0351 0.0187  -0.0451 105 ASP   A C   
2220 C  C   B ASP   A 105 ? 0.2586 0.2576 0.1952 0.0101  0.0063  -0.0130 105 ASP   A C   
2221 O  O   A ASP   A 105 ? 0.2595 0.4002 0.1336 -0.0347 0.0167  -0.0572 105 ASP   A O   
2222 O  O   B ASP   A 105 ? 0.2487 0.2432 0.1742 0.0088  0.0059  -0.0037 105 ASP   A O   
2223 C  CB  A ASP   A 105 ? 0.3322 0.4372 0.2704 -0.0154 0.0422  -0.0456 105 ASP   A CB  
2224 C  CB  B ASP   A 105 ? 0.2614 0.2722 0.2496 0.0386  0.0192  -0.0347 105 ASP   A CB  
2225 C  CG  A ASP   A 105 ? 0.3538 0.4554 0.3312 -0.0044 0.0472  -0.0590 105 ASP   A CG  
2226 C  CG  B ASP   A 105 ? 0.2581 0.2777 0.2869 0.0566  0.0290  -0.0520 105 ASP   A CG  
2227 O  OD1 A ASP   A 105 ? 0.3585 0.4609 0.3384 -0.0031 0.0491  -0.0748 105 ASP   A OD1 
2228 O  OD1 B ASP   A 105 ? 0.2571 0.2749 0.2834 0.0581  0.0251  -0.0658 105 ASP   A OD1 
2229 O  OD2 A ASP   A 105 ? 0.3674 0.4646 0.3779 0.0002  0.0500  -0.0533 105 ASP   A OD2 
2230 O  OD2 B ASP   A 105 ? 0.2549 0.2833 0.3124 0.0657  0.0417  -0.0483 105 ASP   A OD2 
2239 N  N   A ILE   A 106 ? 0.2535 0.3920 0.1996 -0.0421 -0.0076 -0.0440 106 ILE   A N   
2240 N  N   B ILE   A 106 ? 0.2637 0.2707 0.2168 0.0048  -0.0061 -0.0148 106 ILE   A N   
2241 C  CA  A ILE   A 106 ? 0.2270 0.3725 0.2170 -0.0544 -0.0184 -0.0538 106 ILE   A CA  
2242 C  CA  B ILE   A 106 ? 0.2659 0.2814 0.2373 -0.0078 -0.0097 -0.0210 106 ILE   A CA  
2243 C  C   A ILE   A 106 ? 0.2064 0.3431 0.2064 -0.0701 -0.0062 -0.0680 106 ILE   A C   
2244 C  C   B ILE   A 106 ? 0.2661 0.2801 0.2421 -0.0173 0.0016  -0.0210 106 ILE   A C   
2245 O  O   A ILE   A 106 ? 0.1816 0.3282 0.2187 -0.0748 0.0063  -0.0675 106 ILE   A O   
2246 O  O   B ILE   A 106 ? 0.2602 0.2759 0.2457 -0.0166 0.0048  -0.0165 106 ILE   A O   
2247 C  CB  A ILE   A 106 ? 0.2380 0.3878 0.2698 -0.0431 -0.0349 -0.0334 106 ILE   A CB  
2248 C  CB  B ILE   A 106 ? 0.2731 0.2977 0.2660 -0.0095 -0.0232 -0.0180 106 ILE   A CB  
2249 C  CG1 A ILE   A 106 ? 0.2359 0.3912 0.2949 -0.0271 -0.0398 -0.0139 106 ILE   A CG1 
2250 C  CG1 B ILE   A 106 ? 0.2731 0.3044 0.2772 -0.0051 -0.0275 -0.0105 106 ILE   A CG1 
2251 C  CG2 A ILE   A 106 ? 0.2477 0.3946 0.2926 -0.0450 -0.0402 -0.0311 106 ILE   A CG2 
2252 C  CG2 B ILE   A 106 ? 0.2774 0.3035 0.2765 -0.0120 -0.0266 -0.0202 106 ILE   A CG2 
2253 C  CD1 A ILE   A 106 ? 0.2340 0.3890 0.3093 -0.0131 -0.0368 -0.0050 106 ILE   A CD1 
2254 C  CD1 B ILE   A 106 ? 0.2717 0.3049 0.2845 -0.0008 -0.0258 -0.0077 106 ILE   A CD1 
2277 N  N   A GLN   A 107 ? 0.2294 0.3283 0.2333 -0.0672 -0.0020 -0.0877 107 GLN   A N   
2278 N  N   B GLN   A 107 ? 0.2753 0.2807 0.2619 -0.0242 0.0088  -0.0295 107 GLN   A N   
2279 C  CA  A GLN   A 107 ? 0.2610 0.3159 0.3052 -0.0522 0.0151  -0.0903 107 GLN   A CA  
2280 C  CA  B GLN   A 107 ? 0.2855 0.2851 0.3048 -0.0292 0.0179  -0.0366 107 GLN   A CA  
2281 C  C   A GLN   A 107 ? 0.2342 0.2630 0.2860 -0.0401 0.0362  -0.0600 107 GLN   A C   
2282 C  C   B GLN   A 107 ? 0.2513 0.2531 0.2743 -0.0342 0.0325  -0.0325 107 GLN   A C   
2283 O  O   A GLN   A 107 ? 0.2357 0.2554 0.3335 -0.0257 0.0456  -0.0580 107 GLN   A O   
2284 O  O   B GLN   A 107 ? 0.2577 0.2529 0.3024 -0.0333 0.0343  -0.0265 107 GLN   A O   
2285 C  CB  A GLN   A 107 ? 0.3106 0.3550 0.4073 -0.0571 0.0071  -0.0984 107 GLN   A CB  
2286 C  CB  B GLN   A 107 ? 0.3237 0.3203 0.3794 -0.0337 0.0111  -0.0418 107 GLN   A CB  
2287 C  CG  A GLN   A 107 ? 0.3617 0.3952 0.5209 -0.0557 -0.0003 -0.0906 107 GLN   A CG  
2288 C  CG  B GLN   A 107 ? 0.3589 0.3523 0.4574 -0.0361 0.0041  -0.0411 107 GLN   A CG  
2289 C  CD  A GLN   A 107 ? 0.4038 0.4263 0.6191 -0.0543 -0.0035 -0.0809 107 GLN   A CD  
2290 C  CD  B GLN   A 107 ? 0.3881 0.3788 0.5264 -0.0370 0.0001  -0.0384 107 GLN   A CD  
2291 O  OE1 A GLN   A 107 ? 0.4220 0.4331 0.6571 -0.0566 -0.0029 -0.0779 107 GLN   A OE1 
2292 O  OE1 B GLN   A 107 ? 0.3979 0.3877 0.5511 -0.0390 0.0007  -0.0374 107 GLN   A OE1 
2293 N  NE2 A GLN   A 107 ? 0.4124 0.4364 0.6518 -0.0526 -0.0063 -0.0807 107 GLN   A NE2 
2294 N  NE2 B GLN   A 107 ? 0.3962 0.3890 0.5495 -0.0367 -0.0037 -0.0400 107 GLN   A NE2 
2311 N  N   . LEU   A 108 ? 0.2132 0.2247 0.2291 -0.0395 0.0389  -0.0399 108 LEU   A N   
2312 C  CA  . LEU   A 108 ? 0.1945 0.1809 0.1964 -0.0154 0.0289  -0.0065 108 LEU   A CA  
2313 C  C   . LEU   A 108 ? 0.1658 0.1536 0.1797 -0.0058 0.0147  0.0089  108 LEU   A C   
2314 O  O   . LEU   A 108 ? 0.1632 0.1540 0.1996 0.0013  0.0262  0.0062  108 LEU   A O   
2315 C  CB  . LEU   A 108 ? 0.1952 0.1936 0.1734 -0.0189 0.0349  -0.0090 108 LEU   A CB  
2316 C  CG  . LEU   A 108 ? 0.2099 0.2181 0.2084 -0.0141 0.0494  -0.0025 108 LEU   A CG  
2317 C  CD1 . LEU   A 108 ? 0.2329 0.2246 0.2230 -0.0185 0.0600  -0.0095 108 LEU   A CD1 
2318 C  CD2 . LEU   A 108 ? 0.2073 0.2451 0.2548 -0.0031 0.0544  0.0032  108 LEU   A CD2 
2331 N  N   . LEU   A 109 ? 0.1543 0.1525 0.1882 0.0060  0.0197  0.0188  109 LEU   A N   
2332 C  CA  . LEU   A 109 ? 0.1520 0.1463 0.1634 0.0052  0.0082  0.0139  109 LEU   A CA  
2333 C  C   . LEU   A 109 ? 0.1360 0.1371 0.1616 -0.0049 0.0181  0.0026  109 LEU   A C   
2334 O  O   . LEU   A 109 ? 0.1467 0.1263 0.1780 -0.0004 0.0084  -0.0027 109 LEU   A O   
2335 C  CB  . LEU   A 109 ? 0.1584 0.1574 0.1839 0.0080  0.0048  0.0218  109 LEU   A CB  
2336 C  CG  . LEU   A 109 ? 0.1500 0.1595 0.1922 0.0055  0.0064  0.0302  109 LEU   A CG  
2337 C  CD1 . LEU   A 109 ? 0.1597 0.1513 0.2068 0.0006  0.0162  0.0234  109 LEU   A CD1 
2338 C  CD2 . LEU   A 109 ? 0.1487 0.1782 0.2070 0.0047  0.0138  0.0270  109 LEU   A CD2 
2350 N  N   . LYS   A 110 ? 0.1350 0.1384 0.1602 -0.0066 0.0029  0.0069  110 LYS   A N   
2351 C  CA  . LYS   A 110 ? 0.1381 0.1284 0.1733 -0.0009 0.0064  0.0130  110 LYS   A CA  
2352 C  C   . LYS   A 110 ? 0.1369 0.1240 0.1532 -0.0042 0.0085  0.0071  110 LYS   A C   
2353 O  O   . LYS   A 110 ? 0.1330 0.1201 0.1660 -0.0019 0.0090  0.0020  110 LYS   A O   
2354 C  CB  . LYS   A 110 ? 0.1428 0.1399 0.1963 -0.0035 0.0038  -0.0053 110 LYS   A CB  
2355 C  CG  . LYS   A 110 ? 0.1416 0.1345 0.2037 -0.0005 0.0091  -0.0038 110 LYS   A CG  
2356 C  CD  . LYS   A 110 ? 0.1473 0.1399 0.2311 -0.0026 0.0057  -0.0106 110 LYS   A CD  
2357 C  CE  . LYS   A 110 ? 0.1541 0.1424 0.2454 -0.0057 0.0158  -0.0110 110 LYS   A CE  
2358 N  NZ  . LYS   A 110 ? 0.1546 0.1412 0.2541 -0.0102 0.0254  -0.0034 110 LYS   A NZ  
2372 N  N   . SER   A 111 ? 0.1424 0.1255 0.1543 0.0012  -0.0023 0.0028  111 SER   A N   
2373 C  CA  . SER   A 111 ? 0.1337 0.1352 0.1619 -0.0029 0.0063  0.0016  111 SER   A CA  
2374 C  C   . SER   A 111 ? 0.1278 0.1282 0.1623 -0.0076 0.0088  0.0082  111 SER   A C   
2375 O  O   . SER   A 111 ? 0.1452 0.1218 0.1724 -0.0052 0.0075  0.0041  111 SER   A O   
2376 C  CB  . SER   A 111 ? 0.1402 0.1531 0.1772 -0.0003 0.0183  -0.0114 111 SER   A CB  
2377 O  OG  . SER   A 111 ? 0.1936 0.1689 0.1873 0.0059  0.0301  -0.0128 111 SER   A OG  
2383 N  N   . ALA   A 112 ? 0.1353 0.1187 0.1658 0.0009  0.0105  0.0115  112 ALA   A N   
2384 C  CA  . ALA   A 112 ? 0.1342 0.1188 0.1514 -0.0011 0.0169  -0.0039 112 ALA   A CA  
2385 C  C   . ALA   A 112 ? 0.1307 0.1151 0.1590 0.0005  0.0121  0.0026  112 ALA   A C   
2386 O  O   . ALA   A 112 ? 0.1329 0.1158 0.1761 -0.0085 0.0169  0.0113  112 ALA   A O   
2387 C  CB  . ALA   A 112 ? 0.1453 0.1243 0.1522 -0.0012 0.0147  0.0015  112 ALA   A CB  
2393 N  N   . TYR   A 113 ? 0.1253 0.1189 0.1698 -0.0025 0.0118  0.0133  113 TYR   A N   
2394 C  CA  . TYR   A 113 ? 0.1242 0.1192 0.1521 -0.0034 0.0101  0.0144  113 TYR   A CA  
2395 C  C   . TYR   A 113 ? 0.1230 0.1214 0.1326 -0.0082 0.0074  0.0015  113 TYR   A C   
2396 O  O   . TYR   A 113 ? 0.1242 0.1211 0.1512 0.0012  0.0188  0.0051  113 TYR   A O   
2397 C  CB  . TYR   A 113 ? 0.1231 0.1243 0.1691 -0.0033 0.0026  0.0056  113 TYR   A CB  
2398 C  CG  . TYR   A 113 ? 0.1280 0.1331 0.1564 -0.0081 0.0066  0.0106  113 TYR   A CG  
2399 C  CD1 . TYR   A 113 ? 0.1241 0.1411 0.1489 -0.0046 0.0063  0.0118  113 TYR   A CD1 
2400 C  CD2 . TYR   A 113 ? 0.1349 0.1371 0.1524 -0.0106 0.0148  0.0130  113 TYR   A CD2 
2401 C  CE1 . TYR   A 113 ? 0.1299 0.1486 0.1481 -0.0032 0.0071  0.0167  113 TYR   A CE1 
2402 C  CE2 . TYR   A 113 ? 0.1341 0.1408 0.1474 -0.0089 0.0043  0.0216  113 TYR   A CE2 
2403 C  CZ  . TYR   A 113 ? 0.1293 0.1419 0.1542 0.0019  0.0029  0.0143  113 TYR   A CZ  
2404 O  OH  . TYR   A 113 ? 0.1289 0.1530 0.1727 0.0137  0.0028  0.0220  113 TYR   A OH  
2414 N  N   . GLU   A 114 ? 0.1277 0.1191 0.1483 -0.0008 0.0129  0.0066  114 GLU   A N   
2415 C  CA  . GLU   A 114 ? 0.1306 0.1152 0.1600 0.0032  0.0067  0.0109  114 GLU   A CA  
2416 C  C   . GLU   A 114 ? 0.1189 0.1201 0.1659 0.0025  0.0142  0.0098  114 GLU   A C   
2417 O  O   . GLU   A 114 ? 0.1299 0.1200 0.1700 0.0013  0.0041  0.0151  114 GLU   A O   
2418 C  CB  . GLU   A 114 ? 0.1293 0.1195 0.1719 0.0003  0.0135  0.0151  114 GLU   A CB  
2419 C  CG  . GLU   A 114 ? 0.1343 0.1242 0.1637 0.0026  0.0049  0.0030  114 GLU   A CG  
2420 C  CD  . GLU   A 114 ? 0.1451 0.1271 0.1802 0.0010  0.0044  0.0000  114 GLU   A CD  
2421 O  OE1 . GLU   A 114 ? 0.1421 0.1287 0.1905 -0.0057 0.0169  -0.0109 114 GLU   A OE1 
2422 O  OE2 . GLU   A 114 ? 0.1561 0.1307 0.2010 -0.0034 0.0094  -0.0173 114 GLU   A OE2 
2429 N  N   . ASN   A 115 ? 0.1249 0.1181 0.1593 -0.0055 0.0062  0.0065  115 ASN   A N   
2430 C  CA  . ASN   A 115 ? 0.1309 0.1266 0.1676 -0.0064 0.0185  0.0066  115 ASN   A CA  
2431 C  C   . ASN   A 115 ? 0.1327 0.1185 0.1454 -0.0025 0.0071  0.0074  115 ASN   A C   
2432 O  O   . ASN   A 115 ? 0.1401 0.1322 0.1538 -0.0086 0.0053  0.0150  115 ASN   A O   
2433 C  CB  . ASN   A 115 ? 0.1387 0.1293 0.1544 -0.0088 0.0123  0.0104  115 ASN   A CB  
2434 C  CG  . ASN   A 115 ? 0.1362 0.1473 0.1666 -0.0105 0.0185  0.0097  115 ASN   A CG  
2435 O  OD1 . ASN   A 115 ? 0.1311 0.2375 0.1954 -0.0131 0.0234  0.0338  115 ASN   A OD1 
2436 N  ND2 . ASN   A 115 ? 0.1398 0.1280 0.1610 -0.0143 0.0274  0.0142  115 ASN   A ND2 
2443 N  N   . PHE   A 116 ? 0.1202 0.1270 0.1540 -0.0063 0.0185  0.0160  116 PHE   A N   
2444 C  CA  . PHE   A 116 ? 0.1242 0.1296 0.1586 -0.0034 0.0077  0.0211  116 PHE   A CA  
2445 C  C   . PHE   A 116 ? 0.1243 0.1311 0.1572 -0.0106 0.0119  0.0264  116 PHE   A C   
2446 O  O   . PHE   A 116 ? 0.1265 0.1395 0.1672 0.0022  0.0111  0.0296  116 PHE   A O   
2447 C  CB  . PHE   A 116 ? 0.1279 0.1252 0.1724 -0.0027 0.0206  0.0130  116 PHE   A CB  
2448 C  CG  . PHE   A 116 ? 0.1275 0.1204 0.1641 -0.0083 0.0124  0.0109  116 PHE   A CG  
2449 C  CD1 . PHE   A 116 ? 0.1302 0.1251 0.1732 -0.0066 0.0053  0.0088  116 PHE   A CD1 
2450 C  CD2 . PHE   A 116 ? 0.1288 0.1298 0.1779 -0.0085 0.0113  0.0091  116 PHE   A CD2 
2451 C  CE1 . PHE   A 116 ? 0.1280 0.1253 0.1807 -0.0105 0.0025  0.0058  116 PHE   A CE1 
2452 C  CE2 . PHE   A 116 ? 0.1276 0.1231 0.1737 -0.0038 0.0197  0.0077  116 PHE   A CE2 
2453 C  CZ  . PHE   A 116 ? 0.1350 0.1193 0.1652 -0.0020 0.0030  0.0129  116 PHE   A CZ  
2463 N  N   . ASN   A 117 ? 0.1234 0.1301 0.1631 -0.0056 0.0109  0.0157  117 ASN   A N   
2464 C  CA  . ASN   A 117 ? 0.1289 0.1225 0.1761 -0.0022 0.0111  0.0196  117 ASN   A CA  
2465 C  C   . ASN   A 117 ? 0.1301 0.1330 0.1794 0.0027  0.0155  0.0210  117 ASN   A C   
2466 O  O   . ASN   A 117 ? 0.1378 0.1406 0.2104 0.0033  -0.0007 0.0358  117 ASN   A O   
2467 C  CB  . ASN   A 117 ? 0.1263 0.1292 0.1880 0.0050  0.0163  0.0274  117 ASN   A CB  
2468 C  CG  . ASN   A 117 ? 0.1230 0.1302 0.1894 -0.0023 0.0150  0.0242  117 ASN   A CG  
2469 O  OD1 . ASN   A 117 ? 0.1331 0.1419 0.2020 -0.0108 0.0169  0.0263  117 ASN   A OD1 
2470 N  ND2 . ASN   A 117 ? 0.1220 0.1270 0.1924 -0.0057 0.0095  0.0277  117 ASN   A ND2 
2477 N  N   . GLN   A 118 ? 0.1261 0.1375 0.1855 0.0006  0.0036  0.0278  118 GLN   A N   
2478 C  CA  . GLN   A 118 ? 0.1373 0.1543 0.1890 -0.0057 -0.0061 0.0269  118 GLN   A CA  
2479 C  C   . GLN   A 118 ? 0.1306 0.1598 0.1793 -0.0077 -0.0054 0.0245  118 GLN   A C   
2480 O  O   . GLN   A 118 ? 0.1371 0.1843 0.2055 0.0024  -0.0023 0.0070  118 GLN   A O   
2481 C  CB  . GLN   A 118 ? 0.1335 0.1570 0.2016 0.0003  0.0028  0.0214  118 GLN   A CB  
2482 C  CG  . GLN   A 118 ? 0.1282 0.1541 0.2043 0.0014  0.0040  0.0210  118 GLN   A CG  
2483 C  CD  . GLN   A 118 ? 0.1260 0.1483 0.2119 0.0067  0.0099  0.0229  118 GLN   A CD  
2484 O  OE1 . GLN   A 118 ? 0.1324 0.1628 0.2238 0.0102  0.0010  0.0129  118 GLN   A OE1 
2485 N  NE2 . GLN   A 118 ? 0.1323 0.1466 0.2292 0.0067  0.0095  0.0272  118 GLN   A NE2 
2494 N  N   . HIS   A 119 ? 0.1300 0.1505 0.1661 -0.0055 -0.0010 0.0245  119 HIS   A N   
2495 C  CA  . HIS   A 119 ? 0.1428 0.1603 0.1728 -0.0046 -0.0033 0.0240  119 HIS   A CA  
2496 C  C   . HIS   A 119 ? 0.1572 0.1612 0.1615 -0.0067 0.0108  0.0329  119 HIS   A C   
2497 O  O   . HIS   A 119 ? 0.1590 0.1682 0.1842 -0.0207 0.0031  0.0313  119 HIS   A O   
2498 C  CB  . HIS   A 119 ? 0.1471 0.1621 0.1963 0.0009  0.0200  0.0268  119 HIS   A CB  
2499 C  CG  . HIS   A 119 ? 0.1438 0.1632 0.2333 0.0017  0.0104  0.0352  119 HIS   A CG  
2500 N  ND1 . HIS   A 119 ? 0.1602 0.1745 0.2901 -0.0066 0.0115  0.0254  119 HIS   A ND1 
2501 C  CD2 . HIS   A 119 ? 0.1600 0.1687 0.2584 0.0101  0.0323  0.0504  119 HIS   A CD2 
2502 C  CE1 . HIS   A 119 ? 0.1572 0.1723 0.3116 -0.0139 0.0287  0.0472  119 HIS   A CE1 
2503 N  NE2 . HIS   A 119 ? 0.1671 0.1693 0.3080 0.0054  0.0377  0.0551  119 HIS   A NE2 
2511 N  N   . GLU   A 120 ? 0.1678 0.1783 0.1715 0.0001  -0.0099 0.0504  120 GLU   A N   
2512 C  CA  . GLU   A 120 ? 0.1781 0.2155 0.1970 0.0053  -0.0027 0.0754  120 GLU   A CA  
2513 C  C   . GLU   A 120 ? 0.1586 0.1949 0.1851 -0.0030 -0.0025 0.0647  120 GLU   A C   
2514 O  O   . GLU   A 120 ? 0.1547 0.1909 0.2023 -0.0060 0.0018  0.0661  120 GLU   A O   
2515 C  CB  . GLU   A 120 ? 0.2296 0.2798 0.2422 0.0276  -0.0069 0.1318  120 GLU   A CB  
2516 C  CG  . GLU   A 120 ? 0.3212 0.3543 0.3717 0.0422  -0.0051 0.1382  120 GLU   A CG  
2517 C  CD  . GLU   A 120 ? 0.4036 0.4165 0.4905 0.0568  0.0038  0.1385  120 GLU   A CD  
2518 O  OE1 . GLU   A 120 ? 0.4209 0.4295 0.5068 0.0594  0.0083  0.1376  120 GLU   A OE1 
2519 O  OE2 . GLU   A 120 ? 0.4445 0.4468 0.5514 0.0597  0.0066  0.1383  120 GLU   A OE2 
2526 N  N   . VAL   A 121 ? 0.1539 0.1909 0.1692 -0.0024 0.0018  0.0454  121 VAL   A N   
2527 C  CA  . VAL   A 121 ? 0.1644 0.2037 0.1327 -0.0023 0.0110  0.0547  121 VAL   A CA  
2528 C  C   . VAL   A 121 ? 0.1566 0.1914 0.1269 -0.0118 0.0080  0.0444  121 VAL   A C   
2529 O  O   . VAL   A 121 ? 0.1609 0.1980 0.1551 -0.0241 -0.0083 0.0302  121 VAL   A O   
2530 C  CB  . VAL   A 121 ? 0.2076 0.2455 0.1843 0.0126  0.0315  0.0609  121 VAL   A CB  
2531 C  CG1 . VAL   A 121 ? 0.2123 0.2636 0.1917 0.0221  0.0317  0.0722  121 VAL   A CG1 
2532 C  CG2 . VAL   A 121 ? 0.2380 0.2626 0.2379 0.0039  0.0280  0.0450  121 VAL   A CG2 
2542 N  N   . LEU   A 122 ? 0.1462 0.1661 0.1363 -0.0135 0.0106  0.0421  122 LEU   A N   
2543 C  CA  . LEU   A 122 ? 0.1533 0.1507 0.1519 -0.0178 0.0201  0.0388  122 LEU   A CA  
2544 C  C   . LEU   A 122 ? 0.1458 0.1519 0.1530 -0.0164 0.0037  0.0250  122 LEU   A C   
2545 O  O   . LEU   A 122 ? 0.1412 0.1607 0.1876 -0.0249 0.0024  0.0330  122 LEU   A O   
2546 C  CB  . LEU   A 122 ? 0.1734 0.1526 0.1744 -0.0108 0.0164  0.0417  122 LEU   A CB  
2547 C  CG  . LEU   A 122 ? 0.1757 0.1613 0.1717 -0.0083 0.0237  0.0277  122 LEU   A CG  
2548 C  CD1 . LEU   A 122 ? 0.1924 0.1638 0.1801 -0.0163 0.0221  0.0313  122 LEU   A CD1 
2549 C  CD2 . LEU   A 122 ? 0.1705 0.1502 0.1625 -0.0123 0.0369  0.0198  122 LEU   A CD2 
2561 N  N   A LEU   A 123 ? 0.1385 0.1461 0.1550 -0.0157 0.0020  0.0193  123 LEU   A N   
2562 N  N   B LEU   A 123 ? 0.1431 0.1470 0.1555 -0.0139 -0.0016 0.0160  123 LEU   A N   
2563 C  CA  A LEU   A 123 ? 0.1358 0.1473 0.1307 -0.0179 0.0176  0.0277  123 LEU   A CA  
2564 C  CA  B LEU   A 123 ? 0.1432 0.1466 0.1542 -0.0130 0.0031  0.0139  123 LEU   A CA  
2565 C  C   A LEU   A 123 ? 0.1339 0.1404 0.1164 -0.0071 0.0026  0.0180  123 LEU   A C   
2566 C  C   B LEU   A 123 ? 0.1433 0.1380 0.1437 -0.0093 -0.0026 0.0073  123 LEU   A C   
2567 O  O   A LEU   A 123 ? 0.1236 0.1462 0.1402 -0.0118 0.0084  0.0221  123 LEU   A O   
2568 O  O   B LEU   A 123 ? 0.1418 0.1394 0.1338 -0.0165 -0.0094 0.0111  123 LEU   A O   
2569 C  CB  A LEU   A 123 ? 0.1482 0.1594 0.1229 -0.0184 0.0273  0.0241  123 LEU   A CB  
2570 C  CB  B LEU   A 123 ? 0.1500 0.1561 0.1543 -0.0117 0.0060  0.0104  123 LEU   A CB  
2571 C  CG  A LEU   A 123 ? 0.1537 0.1707 0.1588 -0.0120 0.0208  0.0174  123 LEU   A CG  
2572 C  CG  B LEU   A 123 ? 0.1536 0.1633 0.1591 -0.0095 0.0077  0.0113  123 LEU   A CG  
2573 C  CD1 A LEU   A 123 ? 0.1633 0.1831 0.1750 -0.0037 0.0127  0.0036  123 LEU   A CD1 
2574 C  CD1 B LEU   A 123 ? 0.1594 0.1700 0.1543 -0.0057 0.0050  0.0076  123 LEU   A CD1 
2575 C  CD2 A LEU   A 123 ? 0.1590 0.1750 0.1637 -0.0043 0.0136  0.0162  123 LEU   A CD2 
2576 C  CD2 B LEU   A 123 ? 0.1568 0.1659 0.1618 -0.0055 0.0067  0.0108  123 LEU   A CD2 
2599 N  N   A ALA   A 124 ? 0.1306 0.1313 0.0994 -0.0079 0.0024  0.0154  124 ALA   A N   
2600 N  N   B ALA   A 124 ? 0.1392 0.1293 0.1547 -0.0061 0.0024  -0.0000 124 ALA   A N   
2601 C  CA  A ALA   A 124 ? 0.1152 0.1287 0.0976 -0.0022 -0.0010 0.0132  124 ALA   A CA  
2602 C  CA  B ALA   A 124 ? 0.1393 0.1289 0.1659 -0.0087 0.0031  0.0056  124 ALA   A CA  
2603 C  C   A ALA   A 124 ? 0.1147 0.1233 0.1103 -0.0012 0.0057  0.0176  124 ALA   A C   
2604 C  C   B ALA   A 124 ? 0.1347 0.1202 0.1495 -0.0037 -0.0046 0.0075  124 ALA   A C   
2605 O  O   A ALA   A 124 ? 0.1172 0.1367 0.1315 -0.0094 0.0173  0.0272  124 ALA   A O   
2606 O  O   B ALA   A 124 ? 0.1336 0.1128 0.1751 0.0029  0.0001  -0.0027 124 ALA   A O   
2607 C  CB  A ALA   A 124 ? 0.1185 0.1228 0.1217 0.0032  -0.0029 0.0185  124 ALA   A CB  
2608 C  CB  B ALA   A 124 ? 0.1491 0.1310 0.1818 -0.0119 0.0094  0.0128  124 ALA   A CB  
2619 N  N   A PRO   A 125 ? 0.1153 0.1238 0.1373 0.0035  0.0143  0.0273  125 PRO   A N   
2620 N  N   B PRO   A 125 ? 0.1228 0.1225 0.1126 0.0075  -0.0040 0.0237  125 PRO   A N   
2621 C  CA  A PRO   A 125 ? 0.1233 0.1308 0.1463 -0.0061 0.0052  0.0120  125 PRO   A CA  
2622 C  CA  B PRO   A 125 ? 0.1198 0.1277 0.1027 0.0015  0.0001  0.0196  125 PRO   A CA  
2623 C  C   A PRO   A 125 ? 0.1209 0.1391 0.1474 -0.0105 0.0072  0.0145  125 PRO   A C   
2624 C  C   B PRO   A 125 ? 0.1273 0.1439 0.1168 -0.0016 0.0090  0.0139  125 PRO   A C   
2625 O  O   A PRO   A 125 ? 0.1344 0.1299 0.1612 -0.0046 0.0057  0.0138  125 PRO   A O   
2626 O  O   B PRO   A 125 ? 0.1324 0.1469 0.1203 0.0013  0.0083  0.0054  125 PRO   A O   
2627 C  CB  A PRO   A 125 ? 0.1364 0.1264 0.1491 -0.0057 0.0060  0.0136  125 PRO   A CB  
2628 C  CB  B PRO   A 125 ? 0.1090 0.1185 0.1084 -0.0035 0.0025  0.0203  125 PRO   A CB  
2629 C  CG  A PRO   A 125 ? 0.1390 0.1347 0.1626 -0.0047 0.0080  0.0178  125 PRO   A CG  
2630 C  CG  B PRO   A 125 ? 0.1062 0.1178 0.1201 -0.0008 0.0106  0.0142  125 PRO   A CG  
2631 C  CD  A PRO   A 125 ? 0.1192 0.1354 0.1611 -0.0083 0.0138  0.0191  125 PRO   A CD  
2632 C  CD  B PRO   A 125 ? 0.1144 0.1164 0.1186 0.0038  0.0092  0.0173  125 PRO   A CD  
2647 N  N   A LEU   A 126 ? 0.1182 0.1492 0.1410 -0.0071 0.0118  0.0135  126 LEU   A N   
2648 N  N   B LEU   A 126 ? 0.1311 0.1491 0.1275 -0.0006 0.0076  0.0091  126 LEU   A N   
2649 C  CA  A LEU   A 126 ? 0.1250 0.1519 0.1504 -0.0077 0.0055  0.0155  126 LEU   A CA  
2650 C  CA  B LEU   A 126 ? 0.1318 0.1485 0.1373 -0.0096 0.0031  0.0121  126 LEU   A CA  
2651 C  C   A LEU   A 126 ? 0.1323 0.1440 0.1605 0.0042  -0.0017 0.0153  126 LEU   A C   
2652 C  C   B LEU   A 126 ? 0.1333 0.1439 0.1403 0.0003  0.0028  0.0070  126 LEU   A C   
2653 O  O   A LEU   A 126 ? 0.1448 0.1368 0.2011 0.0029  0.0097  0.0187  126 LEU   A O   
2654 O  O   B LEU   A 126 ? 0.1491 0.1434 0.1616 0.0042  0.0176  0.0018  126 LEU   A O   
2655 C  CB  A LEU   A 126 ? 0.1291 0.1559 0.1771 0.0004  -0.0052 0.0110  126 LEU   A CB  
2656 C  CB  B LEU   A 126 ? 0.1328 0.1530 0.1534 -0.0169 -0.0019 0.0058  126 LEU   A CB  
2657 C  CG  A LEU   A 126 ? 0.1313 0.1736 0.2062 -0.0031 0.0141  0.0053  126 LEU   A CG  
2658 C  CG  B LEU   A 126 ? 0.1275 0.1540 0.1664 -0.0128 0.0078  -0.0025 126 LEU   A CG  
2659 C  CD1 A LEU   A 126 ? 0.1382 0.1874 0.2253 -0.0036 0.0176  0.0002  126 LEU   A CD1 
2660 C  CD1 B LEU   A 126 ? 0.1288 0.1461 0.1760 -0.0178 0.0010  -0.0185 126 LEU   A CD1 
2661 C  CD2 A LEU   A 126 ? 0.1445 0.1670 0.2078 -0.0084 0.0119  0.0228  126 LEU   A CD2 
2662 C  CD2 B LEU   A 126 ? 0.1295 0.1568 0.1731 -0.0121 0.0031  0.0081  126 LEU   A CD2 
2685 N  N   A LEU   A 127 ? 0.1365 0.1412 0.1657 0.0020  0.0052  0.0213  127 LEU   A N   
2686 N  N   B LEU   A 127 ? 0.1272 0.1406 0.1375 -0.0021 0.0012  0.0209  127 LEU   A N   
2687 C  CA  A LEU   A 127 ? 0.1368 0.1399 0.1598 0.0013  0.0044  0.0078  127 LEU   A CA  
2688 C  CA  B LEU   A 127 ? 0.1212 0.1419 0.1305 -0.0019 -0.0062 0.0322  127 LEU   A CA  
2689 C  C   A LEU   A 127 ? 0.1303 0.1293 0.1311 0.0018  0.0161  0.0099  127 LEU   A C   
2690 C  C   B LEU   A 127 ? 0.1285 0.1483 0.1425 -0.0020 -0.0048 0.0245  127 LEU   A C   
2691 O  O   A LEU   A 127 ? 0.1389 0.1331 0.1480 -0.0090 0.0023  0.0164  127 LEU   A O   
2692 O  O   B LEU   A 127 ? 0.1364 0.1519 0.1535 -0.0073 -0.0055 0.0245  127 LEU   A O   
2693 C  CB  A LEU   A 127 ? 0.1462 0.1403 0.1674 0.0051  0.0094  0.0156  127 LEU   A CB  
2694 C  CB  B LEU   A 127 ? 0.1152 0.1509 0.1315 -0.0024 -0.0054 0.0220  127 LEU   A CB  
2695 C  CG  A LEU   A 127 ? 0.1509 0.1352 0.1783 0.0051  0.0012  0.0165  127 LEU   A CG  
2696 C  CG  B LEU   A 127 ? 0.1188 0.1568 0.1338 0.0031  -0.0038 0.0308  127 LEU   A CG  
2697 C  CD1 A LEU   A 127 ? 0.1548 0.1331 0.1825 0.0012  -0.0019 0.0063  127 LEU   A CD1 
2698 C  CD1 B LEU   A 127 ? 0.1193 0.1595 0.1406 0.0086  0.0088  0.0364  127 LEU   A CD1 
2699 C  CD2 A LEU   A 127 ? 0.1584 0.1295 0.1889 0.0118  -0.0141 0.0139  127 LEU   A CD2 
2700 C  CD2 B LEU   A 127 ? 0.1255 0.1706 0.1408 0.0026  -0.0126 0.0164  127 LEU   A CD2 
2723 N  N   A SER   A 128 ? 0.1367 0.1336 0.1245 -0.0014 0.0112  0.0073  128 SER   A N   
2724 N  N   B SER   A 128 ? 0.1383 0.1532 0.1384 -0.0051 -0.0006 0.0227  128 SER   A N   
2725 C  CA  A SER   A 128 ? 0.1424 0.1366 0.1170 -0.0010 0.0052  0.0055  128 SER   A CA  
2726 C  CA  B SER   A 128 ? 0.1418 0.1560 0.1410 -0.0076 -0.0058 0.0100  128 SER   A CA  
2727 C  C   A SER   A 128 ? 0.1515 0.1346 0.0981 0.0029  0.0040  0.0193  128 SER   A C   
2728 C  C   B SER   A 128 ? 0.1466 0.1583 0.1556 -0.0060 -0.0128 0.0152  128 SER   A C   
2729 O  O   A SER   A 128 ? 0.1579 0.1558 0.1261 0.0037  0.0135  0.0064  128 SER   A O   
2730 O  O   B SER   A 128 ? 0.1433 0.1589 0.1677 0.0015  -0.0257 0.0022  128 SER   A O   
2731 C  CB  A SER   A 128 ? 0.1452 0.1345 0.1328 -0.0027 -0.0034 0.0113  128 SER   A CB  
2732 C  CB  B SER   A 128 ? 0.1507 0.1547 0.1328 -0.0113 0.0017  0.0148  128 SER   A CB  
2733 O  OG  A SER   A 128 ? 0.1526 0.1373 0.1404 -0.0016 -0.0013 -0.0035 128 SER   A OG  
2734 O  OG  B SER   A 128 ? 0.1542 0.1534 0.1128 -0.0047 0.0133  0.0147  128 SER   A OG  
2745 N  N   A ALA   A 129 ? 0.1413 0.1321 0.1212 -0.0100 0.0038  0.0340  129 ALA   A N   
2746 N  N   B ALA   A 129 ? 0.1473 0.1611 0.1836 -0.0075 0.0049  0.0197  129 ALA   A N   
2747 C  CA  A ALA   A 129 ? 0.1372 0.1343 0.1526 -0.0066 0.0089  0.0212  129 ALA   A CA  
2748 C  CA  B ALA   A 129 ? 0.1525 0.1649 0.2002 -0.0073 0.0024  0.0174  129 ALA   A CA  
2749 C  C   A ALA   A 129 ? 0.1439 0.1401 0.1610 0.0002  -0.0100 0.0119  129 ALA   A C   
2750 C  C   B ALA   A 129 ? 0.1563 0.1650 0.1903 -0.0107 -0.0024 0.0108  129 ALA   A C   
2751 O  O   A ALA   A 129 ? 0.1574 0.1459 0.1531 0.0002  -0.0253 0.0303  129 ALA   A O   
2752 O  O   B ALA   A 129 ? 0.1611 0.1641 0.1892 -0.0186 -0.0044 0.0063  129 ALA   A O   
2753 C  CB  A ALA   A 129 ? 0.1429 0.1330 0.1561 0.0142  0.0125  0.0154  129 ALA   A CB  
2754 C  CB  B ALA   A 129 ? 0.1546 0.1701 0.2049 0.0025  -0.0016 0.0189  129 ALA   A CB  
2765 N  N   A GLY   A 130 ? 0.1559 0.1408 0.2104 0.0032  0.0005  0.0021  130 GLY   A N   
2766 N  N   B GLY   A 130 ? 0.1620 0.1659 0.1945 -0.0087 0.0068  0.0172  130 GLY   A N   
2767 C  CA  A GLY   A 130 ? 0.1826 0.1352 0.2211 0.0074  -0.0090 0.0002  130 GLY   A CA  
2768 C  CA  B GLY   A 130 ? 0.1743 0.1628 0.1790 -0.0054 0.0116  0.0186  130 GLY   A CA  
2769 C  C   A GLY   A 130 ? 0.1879 0.1331 0.2003 0.0070  -0.0204 0.0029  130 GLY   A C   
2770 C  C   B GLY   A 130 ? 0.1768 0.1564 0.1620 -0.0029 0.0220  0.0139  130 GLY   A C   
2771 O  O   A GLY   A 130 ? 0.1849 0.1328 0.2109 0.0136  -0.0293 0.0052  130 GLY   A O   
2772 O  O   B GLY   A 130 ? 0.1802 0.1509 0.1587 -0.0021 0.0264  0.0056  130 GLY   A O   
2779 N  N   A ILE   A 131 ? 0.1931 0.1326 0.1674 -0.0063 -0.0156 0.0099  131 ILE   A N   
2780 N  N   B ILE   A 131 ? 0.1783 0.1561 0.1647 -0.0051 0.0216  0.0157  131 ILE   A N   
2781 C  CA  A ILE   A 131 ? 0.2013 0.1404 0.1452 -0.0093 -0.0283 0.0109  131 ILE   A CA  
2782 C  CA  B ILE   A 131 ? 0.1838 0.1566 0.1623 -0.0051 0.0148  0.0147  131 ILE   A CA  
2783 C  C   A ILE   A 131 ? 0.1877 0.1465 0.1340 -0.0037 -0.0219 0.0148  131 ILE   A C   
2784 C  C   B ILE   A 131 ? 0.1767 0.1588 0.1530 -0.0034 0.0044  0.0130  131 ILE   A C   
2785 O  O   A ILE   A 131 ? 0.1846 0.1557 0.1606 0.0021  -0.0142 0.0215  131 ILE   A O   
2786 O  O   B ILE   A 131 ? 0.1702 0.1620 0.1630 0.0042  -0.0077 0.0210  131 ILE   A O   
2787 C  CB  A ILE   A 131 ? 0.2259 0.1522 0.1476 -0.0191 -0.0340 0.0114  131 ILE   A CB  
2788 C  CB  B ILE   A 131 ? 0.1959 0.1599 0.1664 -0.0108 0.0124  0.0189  131 ILE   A CB  
2789 C  CG1 A ILE   A 131 ? 0.2330 0.1702 0.1393 -0.0318 -0.0357 0.0139  131 ILE   A CG1 
2790 C  CG1 B ILE   A 131 ? 0.2058 0.1784 0.1710 -0.0172 -0.0028 0.0362  131 ILE   A CG1 
2791 C  CG2 A ILE   A 131 ? 0.2393 0.1491 0.1397 -0.0134 -0.0234 0.0100  131 ILE   A CG2 
2792 C  CG2 B ILE   A 131 ? 0.2025 0.1531 0.1859 -0.0084 0.0062  0.0016  131 ILE   A CG2 
2793 C  CD1 A ILE   A 131 ? 0.2352 0.1711 0.1482 -0.0308 -0.0307 0.0130  131 ILE   A CD1 
2794 C  CD1 B ILE   A 131 ? 0.2135 0.1853 0.1854 -0.0149 -0.0063 0.0468  131 ILE   A CD1 
2817 N  N   A PHE   A 132 ? 0.1766 0.1384 0.1460 0.0020  -0.0181 0.0195  132 PHE   A N   
2818 N  N   B PHE   A 132 ? 0.1746 0.1559 0.1600 -0.0054 0.0027  0.0153  132 PHE   A N   
2819 C  CA  A PHE   A 132 ? 0.1772 0.1456 0.1500 -0.0025 -0.0149 0.0088  132 PHE   A CA  
2820 C  CA  B PHE   A 132 ? 0.1833 0.1603 0.1568 -0.0091 -0.0028 0.0089  132 PHE   A CA  
2821 C  C   A PHE   A 132 ? 0.1778 0.1555 0.1630 -0.0100 -0.0248 0.0138  132 PHE   A C   
2822 C  C   B PHE   A 132 ? 0.1895 0.1662 0.1653 -0.0026 -0.0154 0.0049  132 PHE   A C   
2823 O  O   A PHE   A 132 ? 0.1816 0.1549 0.1683 -0.0175 -0.0302 0.0056  132 PHE   A O   
2824 O  O   B PHE   A 132 ? 0.2027 0.1717 0.1765 -0.0060 -0.0132 -0.0051 132 PHE   A O   
2825 C  CB  A PHE   A 132 ? 0.1702 0.1429 0.1370 0.0012  -0.0221 0.0144  132 PHE   A CB  
2826 C  CB  B PHE   A 132 ? 0.1837 0.1555 0.1449 -0.0122 -0.0061 0.0053  132 PHE   A CB  
2827 C  CG  A PHE   A 132 ? 0.1709 0.1463 0.1358 0.0025  -0.0200 0.0209  132 PHE   A CG  
2828 C  CG  B PHE   A 132 ? 0.1848 0.1619 0.1406 -0.0125 -0.0114 0.0050  132 PHE   A CG  
2829 C  CD1 A PHE   A 132 ? 0.1640 0.1509 0.1546 0.0063  -0.0195 0.0052  132 PHE   A CD1 
2830 C  CD1 B PHE   A 132 ? 0.1833 0.1649 0.1564 -0.0079 -0.0129 0.0016  132 PHE   A CD1 
2831 C  CD2 A PHE   A 132 ? 0.1735 0.1584 0.1546 0.0050  -0.0221 0.0064  132 PHE   A CD2 
2832 C  CD2 B PHE   A 132 ? 0.1888 0.1703 0.1548 -0.0123 -0.0135 -0.0042 132 PHE   A CD2 
2833 C  CE1 A PHE   A 132 ? 0.1633 0.1559 0.1487 0.0085  -0.0195 -0.0038 132 PHE   A CE1 
2834 C  CE1 B PHE   A 132 ? 0.1842 0.1705 0.1696 -0.0129 -0.0122 0.0002  132 PHE   A CE1 
2835 C  CE2 A PHE   A 132 ? 0.1647 0.1674 0.1453 0.0110  -0.0252 0.0094  132 PHE   A CE2 
2836 C  CE2 B PHE   A 132 ? 0.1866 0.1798 0.1740 -0.0083 -0.0106 -0.0040 132 PHE   A CE2 
2837 C  CZ  A PHE   A 132 ? 0.1639 0.1595 0.1405 0.0047  -0.0176 0.0143  132 PHE   A CZ  
2838 C  CZ  B PHE   A 132 ? 0.1861 0.1762 0.1838 -0.0131 -0.0130 -0.0027 132 PHE   A CZ  
2857 N  N   A GLY   A 133 ? 0.1825 0.1679 0.1612 -0.0095 -0.0310 0.0160  133 GLY   A N   
2858 N  N   B GLY   A 133 ? 0.1852 0.1682 0.1615 0.0039  -0.0307 0.0121  133 GLY   A N   
2859 C  CA  A GLY   A 133 ? 0.1877 0.1747 0.1654 -0.0138 -0.0363 0.0068  133 GLY   A CA  
2860 C  CA  B GLY   A 133 ? 0.1840 0.1702 0.1585 0.0063  -0.0336 0.0073  133 GLY   A CA  
2861 C  C   A GLY   A 133 ? 0.1861 0.1790 0.1666 -0.0100 -0.0449 0.0019  133 GLY   A C   
2862 C  C   B GLY   A 133 ? 0.1760 0.1742 0.1563 0.0119  -0.0323 -0.0015 133 GLY   A C   
2863 O  O   A GLY   A 133 ? 0.1968 0.1847 0.1737 -0.0062 -0.0350 -0.0096 133 GLY   A O   
2864 O  O   B GLY   A 133 ? 0.1735 0.1790 0.1582 0.0151  -0.0270 -0.0184 133 GLY   A O   
2871 N  N   A ALA   A 134 ? 0.1787 0.1700 0.1675 -0.0181 -0.0328 0.0105  134 ALA   A N   
2872 N  N   B ALA   A 134 ? 0.1726 0.1681 0.1548 0.0115  -0.0244 0.0054  134 ALA   A N   
2873 C  CA  A ALA   A 134 ? 0.1771 0.1764 0.1822 -0.0155 -0.0314 0.0037  134 ALA   A CA  
2874 C  CA  B ALA   A 134 ? 0.1706 0.1674 0.1629 0.0108  -0.0189 0.0024  134 ALA   A CA  
2875 C  C   A ALA   A 134 ? 0.1804 0.1909 0.1711 -0.0141 -0.0280 0.0075  134 ALA   A C   
2876 C  C   B ALA   A 134 ? 0.1705 0.1664 0.1551 0.0050  -0.0176 -0.0006 134 ALA   A C   
2877 O  O   A ALA   A 134 ? 0.1900 0.1989 0.1981 -0.0215 -0.0085 0.0142  134 ALA   A O   
2878 O  O   B ALA   A 134 ? 0.1741 0.1661 0.1779 -0.0039 -0.0034 -0.0055 134 ALA   A O   
2879 C  CB  A ALA   A 134 ? 0.1822 0.1750 0.2088 -0.0143 -0.0271 -0.0059 134 ALA   A CB  
2880 C  CB  B ALA   A 134 ? 0.1739 0.1685 0.1848 0.0137  -0.0151 0.0044  134 ALA   A CB  
2891 N  N   A ASP   A 135 ? 0.1825 0.1923 0.1823 -0.0135 -0.0218 0.0119  135 ASP   A N   
2892 N  N   B ASP   A 135 ? 0.1738 0.1702 0.1594 0.0010  -0.0185 0.0053  135 ASP   A N   
2893 C  CA  A ASP   A 135 ? 0.1838 0.1962 0.2070 -0.0232 -0.0364 0.0258  135 ASP   A CA  
2894 C  CA  B ASP   A 135 ? 0.1718 0.1722 0.1755 -0.0049 -0.0288 0.0047  135 ASP   A CA  
2895 C  C   A ASP   A 135 ? 0.1703 0.1854 0.2216 -0.0223 -0.0272 0.0410  135 ASP   A C   
2896 C  C   B ASP   A 135 ? 0.1634 0.1640 0.1830 -0.0018 -0.0295 0.0121  135 ASP   A C   
2897 O  O   A ASP   A 135 ? 0.1636 0.1793 0.2307 -0.0150 -0.0254 0.0405  135 ASP   A O   
2898 O  O   B ASP   A 135 ? 0.1629 0.1611 0.1923 -0.0062 -0.0253 0.0218  135 ASP   A O   
2899 C  CB  A ASP   A 135 ? 0.2009 0.2173 0.2387 -0.0363 -0.0571 0.0266  135 ASP   A CB  
2900 C  CB  B ASP   A 135 ? 0.1795 0.1829 0.1934 -0.0120 -0.0339 -0.0008 135 ASP   A CB  
2901 C  CG  A ASP   A 135 ? 0.2174 0.2383 0.2864 -0.0537 -0.0593 0.0186  135 ASP   A CG  
2902 C  CG  B ASP   A 135 ? 0.1878 0.1950 0.2172 -0.0177 -0.0306 0.0032  135 ASP   A CG  
2903 O  OD1 A ASP   A 135 ? 0.2101 0.2434 0.2765 -0.0635 -0.0689 0.0350  135 ASP   A OD1 
2904 O  OD1 B ASP   A 135 ? 0.1864 0.1923 0.2290 -0.0165 -0.0298 0.0112  135 ASP   A OD1 
2905 O  OD2 A ASP   A 135 ? 0.2533 0.2543 0.3404 -0.0528 -0.0254 0.0124  135 ASP   A OD2 
2906 O  OD2 B ASP   A 135 ? 0.1926 0.2100 0.2385 -0.0226 -0.0366 0.0041  135 ASP   A OD2 
2915 N  N   A PRO   A 136 ? 0.1580 0.1841 0.2323 -0.0158 -0.0108 0.0532  136 PRO   A N   
2916 N  N   B PRO   A 136 ? 0.1538 0.1576 0.1952 0.0087  -0.0274 0.0169  136 PRO   A N   
2917 C  CA  A PRO   A 136 ? 0.1547 0.1856 0.2369 -0.0133 -0.0019 0.0422  136 PRO   A CA  
2918 C  CA  B PRO   A 136 ? 0.1521 0.1604 0.2033 0.0045  -0.0248 0.0102  136 PRO   A CA  
2919 C  C   A PRO   A 136 ? 0.1387 0.1754 0.2248 -0.0051 0.0079  0.0383  136 PRO   A C   
2920 C  C   B PRO   A 136 ? 0.1396 0.1620 0.1968 0.0028  -0.0215 0.0074  136 PRO   A C   
2921 O  O   A PRO   A 136 ? 0.1364 0.1716 0.2119 -0.0016 0.0085  0.0339  136 PRO   A O   
2922 O  O   B PRO   A 136 ? 0.1385 0.1546 0.1900 0.0088  -0.0143 0.0064  136 PRO   A O   
2923 C  CB  A PRO   A 136 ? 0.1736 0.1876 0.2620 -0.0133 -0.0064 0.0405  136 PRO   A CB  
2924 C  CB  B PRO   A 136 ? 0.1650 0.1566 0.2144 0.0075  -0.0294 0.0079  136 PRO   A CB  
2925 C  CG  A PRO   A 136 ? 0.1796 0.1975 0.2751 -0.0150 -0.0071 0.0312  136 PRO   A CG  
2926 C  CG  B PRO   A 136 ? 0.1745 0.1561 0.2251 0.0102  -0.0302 0.0086  136 PRO   A CG  
2927 C  CD  A PRO   A 136 ? 0.1697 0.1902 0.2529 -0.0104 -0.0060 0.0479  136 PRO   A CD  
2928 C  CD  B PRO   A 136 ? 0.1556 0.1537 0.2115 0.0104  -0.0282 0.0181  136 PRO   A CD  
2943 N  N   A ILE   A 137 ? 0.1379 0.1738 0.2377 -0.0043 -0.0038 0.0425  137 ILE   A N   
2944 N  N   B ILE   A 137 ? 0.1404 0.1650 0.2118 -0.0026 -0.0217 0.0066  137 ILE   A N   
2945 C  CA  A ILE   A 137 ? 0.1400 0.1808 0.2360 -0.0138 -0.0180 0.0428  137 ILE   A CA  
2946 C  CA  B ILE   A 137 ? 0.1526 0.1784 0.2224 -0.0053 -0.0187 0.0105  137 ILE   A CA  
2947 C  C   A ILE   A 137 ? 0.1387 0.1754 0.2160 -0.0235 -0.0179 0.0320  137 ILE   A C   
2948 C  C   B ILE   A 137 ? 0.1544 0.1847 0.2201 -0.0085 -0.0136 0.0158  137 ILE   A C   
2949 O  O   A ILE   A 137 ? 0.1430 0.1643 0.2082 -0.0206 -0.0073 0.0114  137 ILE   A O   
2950 O  O   B ILE   A 137 ? 0.1564 0.1892 0.2291 -0.0094 -0.0113 0.0170  137 ILE   A O   
2951 C  CB  A ILE   A 137 ? 0.1393 0.2059 0.2651 -0.0249 -0.0392 0.0377  137 ILE   A CB  
2952 C  CB  B ILE   A 137 ? 0.1615 0.1873 0.2429 -0.0112 -0.0250 0.0118  137 ILE   A CB  
2953 C  CG1 A ILE   A 137 ? 0.1520 0.2297 0.3064 -0.0217 -0.0282 0.0510  137 ILE   A CG1 
2954 C  CG1 B ILE   A 137 ? 0.1728 0.1941 0.2661 -0.0069 -0.0217 0.0296  137 ILE   A CG1 
2955 C  CG2 A ILE   A 137 ? 0.1454 0.2026 0.2701 -0.0228 -0.0487 0.0257  137 ILE   A CG2 
2956 C  CG2 B ILE   A 137 ? 0.1679 0.1886 0.2480 -0.0054 -0.0267 0.0095  137 ILE   A CG2 
2957 C  CD1 A ILE   A 137 ? 0.1710 0.2386 0.3298 -0.0175 -0.0114 0.0637  137 ILE   A CD1 
2958 C  CD1 B ILE   A 137 ? 0.1808 0.2012 0.2864 -0.0052 -0.0139 0.0379  137 ILE   A CD1 
2981 N  N   A HIS   A 138 ? 0.1353 0.1920 0.2130 -0.0155 -0.0152 0.0289  138 HIS   A N   
2982 N  N   B HIS   A 138 ? 0.1552 0.1937 0.2117 -0.0067 -0.0055 0.0161  138 HIS   A N   
2983 C  CA  A HIS   A 138 ? 0.1400 0.1982 0.1917 -0.0126 -0.0183 0.0201  138 HIS   A CA  
2984 C  CA  B HIS   A 138 ? 0.1573 0.1945 0.1960 -0.0096 -0.0045 0.0166  138 HIS   A CA  
2985 C  C   A HIS   A 138 ? 0.1351 0.1863 0.1837 -0.0104 -0.0169 0.0243  138 HIS   A C   
2986 C  C   B HIS   A 138 ? 0.1462 0.1845 0.1858 -0.0090 -0.0044 0.0245  138 HIS   A C   
2987 O  O   A HIS   A 138 ? 0.1473 0.1846 0.1929 -0.0063 -0.0046 0.0183  138 HIS   A O   
2988 O  O   B HIS   A 138 ? 0.1540 0.1849 0.1915 -0.0082 0.0049  0.0250  138 HIS   A O   
2989 C  CB  A HIS   A 138 ? 0.1648 0.2183 0.1768 -0.0119 -0.0310 0.0135  138 HIS   A CB  
2990 C  CB  B HIS   A 138 ? 0.1691 0.2074 0.1880 -0.0116 -0.0077 0.0101  138 HIS   A CB  
2991 C  CG  A HIS   A 138 ? 0.1877 0.2369 0.1958 -0.0181 -0.0144 0.0151  138 HIS   A CG  
2992 C  CG  B HIS   A 138 ? 0.1796 0.2201 0.1958 -0.0174 -0.0026 0.0123  138 HIS   A CG  
2993 N  ND1 A HIS   A 138 ? 0.1980 0.2484 0.2221 -0.0210 -0.0123 0.0037  138 HIS   A ND1 
2994 N  ND1 B HIS   A 138 ? 0.1839 0.2268 0.2112 -0.0202 -0.0045 0.0065  138 HIS   A ND1 
2995 C  CD2 A HIS   A 138 ? 0.1946 0.2478 0.1984 -0.0166 -0.0208 0.0171  138 HIS   A CD2 
2996 C  CD2 B HIS   A 138 ? 0.1825 0.2272 0.1951 -0.0170 -0.0036 0.0151  138 HIS   A CD2 
2997 C  CE1 A HIS   A 138 ? 0.2031 0.2545 0.2233 -0.0172 -0.0155 0.0046  138 HIS   A CE1 
2998 C  CE1 B HIS   A 138 ? 0.1869 0.2313 0.2154 -0.0170 -0.0020 0.0080  138 HIS   A CE1 
2999 N  NE2 A HIS   A 138 ? 0.2029 0.2537 0.2052 -0.0164 -0.0059 0.0120  138 HIS   A NE2 
3000 N  NE2 B HIS   A 138 ? 0.1866 0.2312 0.2009 -0.0168 0.0076  0.0131  138 HIS   A NE2 
3015 N  N   . SER   A 139 ? 0.1323 0.1734 0.1849 -0.0054 -0.0083 0.0305  139 SER   A N   
3016 C  CA  . SER   A 139 ? 0.1321 0.1657 0.1802 -0.0084 0.0008  0.0324  139 SER   A CA  
3017 C  C   . SER   A 139 ? 0.1229 0.1592 0.1807 -0.0103 -0.0029 0.0176  139 SER   A C   
3018 O  O   . SER   A 139 ? 0.1266 0.1540 0.2001 -0.0102 0.0010  0.0308  139 SER   A O   
3019 C  CB  . SER   A 139 ? 0.1307 0.1622 0.1934 -0.0109 -0.0046 0.0331  139 SER   A CB  
3020 O  OG  . SER   A 139 ? 0.1347 0.1584 0.2097 -0.0195 -0.0160 0.0339  139 SER   A OG  
3027 N  N   . LEU   A 140 ? 0.1232 0.1644 0.1893 -0.0032 0.0004  0.0222  140 LEU   A N   
3028 C  CA  . LEU   A 140 ? 0.1186 0.1545 0.1757 -0.0046 -0.0017 0.0260  140 LEU   A CA  
3029 C  C   . LEU   A 140 ? 0.1232 0.1603 0.1834 -0.0110 0.0069  0.0282  140 LEU   A C   
3030 O  O   . LEU   A 140 ? 0.1256 0.1585 0.1995 -0.0059 0.0000  0.0284  140 LEU   A O   
3031 C  CB  . LEU   A 140 ? 0.1238 0.1629 0.1794 -0.0084 0.0015  0.0151  140 LEU   A CB  
3032 C  CG  . LEU   A 140 ? 0.1319 0.1703 0.1963 -0.0213 0.0122  0.0295  140 LEU   A CG  
3033 C  CD1 . LEU   A 140 ? 0.1333 0.1746 0.2222 -0.0108 0.0098  0.0317  140 LEU   A CD1 
3034 C  CD2 . LEU   A 140 ? 0.1396 0.1865 0.1997 -0.0164 0.0111  0.0384  140 LEU   A CD2 
3046 N  N   A ARG   A 141 ? 0.1274 0.1657 0.1925 -0.0131 -0.0041 0.0202  141 ARG   A N   
3047 N  N   B ARG   A 141 ? 0.1251 0.1632 0.1773 -0.0116 0.0104  0.0292  141 ARG   A N   
3048 C  CA  A ARG   A 141 ? 0.1403 0.1777 0.2214 -0.0245 -0.0120 -0.0041 141 ARG   A CA  
3049 C  CA  B ARG   A 141 ? 0.1319 0.1687 0.1871 -0.0169 0.0141  0.0238  141 ARG   A CA  
3050 C  C   A ARG   A 141 ? 0.1399 0.1663 0.2004 -0.0179 -0.0082 -0.0010 141 ARG   A C   
3051 C  C   B ARG   A 141 ? 0.1391 0.1621 0.1851 -0.0100 0.0056  0.0179  141 ARG   A C   
3052 O  O   A ARG   A 141 ? 0.1307 0.1585 0.2001 -0.0140 0.0117  -0.0043 141 ARG   A O   
3053 O  O   B ARG   A 141 ? 0.1354 0.1568 0.1916 -0.0109 0.0102  0.0100  141 ARG   A O   
3054 C  CB  A ARG   A 141 ? 0.1568 0.1998 0.2602 -0.0281 -0.0213 -0.0182 141 ARG   A CB  
3055 C  CB  B ARG   A 141 ? 0.1337 0.1808 0.1929 -0.0173 0.0279  0.0251  141 ARG   A CB  
3056 C  CG  A ARG   A 141 ? 0.1942 0.2291 0.2926 -0.0213 -0.0332 -0.0188 141 ARG   A CG  
3057 C  CG  B ARG   A 141 ? 0.1440 0.1909 0.1943 -0.0126 0.0325  0.0305  141 ARG   A CG  
3058 C  CD  A ARG   A 141 ? 0.2136 0.2503 0.3088 -0.0252 -0.0439 -0.0095 141 ARG   A CD  
3059 C  CD  B ARG   A 141 ? 0.1533 0.1881 0.2000 -0.0170 0.0091  0.0322  141 ARG   A CD  
3060 N  NE  A ARG   A 141 ? 0.2140 0.2640 0.3214 -0.0259 -0.0390 -0.0049 141 ARG   A NE  
3061 N  NE  B ARG   A 141 ? 0.1586 0.2027 0.1956 -0.0177 0.0055  0.0239  141 ARG   A NE  
3062 C  CZ  A ARG   A 141 ? 0.2067 0.2766 0.3194 -0.0364 -0.0376 -0.0027 141 ARG   A CZ  
3063 C  CZ  B ARG   A 141 ? 0.1686 0.2082 0.1841 -0.0252 0.0161  0.0287  141 ARG   A CZ  
3064 N  NH1 A ARG   A 141 ? 0.2024 0.2779 0.3280 -0.0281 -0.0507 0.0041  141 ARG   A NH1 
3065 N  NH1 B ARG   A 141 ? 0.1720 0.2147 0.1697 -0.0295 0.0224  0.0156  141 ARG   A NH1 
3066 N  NH2 A ARG   A 141 ? 0.2020 0.2808 0.3191 -0.0377 -0.0242 -0.0025 141 ARG   A NH2 
3067 N  NH2 B ARG   A 141 ? 0.1697 0.2121 0.1911 -0.0240 0.0257  0.0420  141 ARG   A NH2 
3094 N  N   A VAL   A 142 ? 0.1262 0.1623 0.1835 -0.0161 -0.0052 -0.0032 142 VAL   A N   
3095 N  N   B VAL   A 142 ? 0.1381 0.1614 0.1779 -0.0013 0.0047  0.0161  142 VAL   A N   
3096 C  CA  A VAL   A 142 ? 0.1236 0.1520 0.1867 -0.0161 0.0123  -0.0039 142 VAL   A CA  
3097 C  CA  B VAL   A 142 ? 0.1430 0.1582 0.1753 0.0069  0.0067  0.0143  142 VAL   A CA  
3098 C  C   A VAL   A 142 ? 0.1155 0.1457 0.1681 -0.0186 0.0057  0.0082  142 VAL   A C   
3099 C  C   B VAL   A 142 ? 0.1343 0.1500 0.1641 -0.0022 0.0054  0.0154  142 VAL   A C   
3100 O  O   A VAL   A 142 ? 0.1190 0.1500 0.1869 -0.0064 0.0068  0.0139  142 VAL   A O   
3101 O  O   B VAL   A 142 ? 0.1389 0.1516 0.1715 0.0053  0.0046  0.0193  142 VAL   A O   
3102 C  CB  A VAL   A 142 ? 0.1326 0.1506 0.1846 -0.0129 0.0141  0.0007  142 VAL   A CB  
3103 C  CB  B VAL   A 142 ? 0.1565 0.1644 0.1642 0.0203  -0.0009 0.0224  142 VAL   A CB  
3104 C  CG1 A VAL   A 142 ? 0.1318 0.1400 0.1916 -0.0216 0.0090  -0.0058 142 VAL   A CG1 
3105 C  CG1 B VAL   A 142 ? 0.1623 0.1656 0.1673 0.0275  -0.0101 0.0148  142 VAL   A CG1 
3106 C  CG2 A VAL   A 142 ? 0.1401 0.1640 0.2134 -0.0124 0.0190  -0.0026 142 VAL   A CG2 
3107 C  CG2 B VAL   A 142 ? 0.1643 0.1682 0.1675 0.0254  -0.0033 0.0283  142 VAL   A CG2 
3126 N  N   . CYS   A 143 ? 0.1289 0.1456 0.1607 -0.0118 0.0097  0.0097  143 CYS   A N   
3127 C  CA  . CYS   A 143 ? 0.1301 0.1449 0.1693 -0.0081 0.0100  0.0113  143 CYS   A CA  
3128 C  C   . CYS   A 143 ? 0.1294 0.1463 0.1747 -0.0080 0.0048  0.0193  143 CYS   A C   
3129 O  O   . CYS   A 143 ? 0.1277 0.1431 0.1871 -0.0067 0.0105  0.0172  143 CYS   A O   
3130 C  CB  . CYS   A 143 ? 0.1360 0.1473 0.1886 0.0019  0.0193  0.0238  143 CYS   A CB  
3131 S  SG  . CYS   A 143 ? 0.1540 0.1562 0.1751 0.0044  0.0108  0.0136  143 CYS   A SG  
3138 N  N   . VAL   A 144 ? 0.1246 0.1490 0.1914 -0.0045 0.0111  0.0221  144 VAL   A N   
3139 C  CA  . VAL   A 144 ? 0.1351 0.1537 0.2231 -0.0118 0.0298  0.0327  144 VAL   A CA  
3140 C  C   . VAL   A 144 ? 0.1365 0.1446 0.2228 -0.0198 0.0014  0.0208  144 VAL   A C   
3141 O  O   . VAL   A 144 ? 0.1548 0.1509 0.2297 -0.0023 0.0048  0.0288  144 VAL   A O   
3142 C  CB  . VAL   A 144 ? 0.1574 0.1724 0.2910 0.0005  0.0471  0.0257  144 VAL   A CB  
3143 C  CG1 . VAL   A 144 ? 0.1673 0.1947 0.3398 -0.0143 0.0291  0.0128  144 VAL   A CG1 
3144 C  CG2 . VAL   A 144 ? 0.1451 0.1764 0.3060 -0.0060 0.0565  0.0313  144 VAL   A CG2 
3154 N  N   . ASP   A 145 ? 0.1404 0.1381 0.2338 -0.0140 0.0046  0.0083  145 ASP   A N   
3155 C  CA  . ASP   A 145 ? 0.1515 0.1397 0.2296 -0.0173 0.0055  0.0029  145 ASP   A CA  
3156 C  C   . ASP   A 145 ? 0.1581 0.1431 0.2316 -0.0121 0.0067  -0.0038 145 ASP   A C   
3157 O  O   . ASP   A 145 ? 0.1644 0.1536 0.2929 -0.0144 0.0005  -0.0387 145 ASP   A O   
3158 C  CB  . ASP   A 145 ? 0.1599 0.1755 0.2455 -0.0254 0.0008  -0.0064 145 ASP   A CB  
3159 C  CG  . ASP   A 145 ? 0.1777 0.2183 0.2643 -0.0469 -0.0071 -0.0050 145 ASP   A CG  
3160 O  OD1 . ASP   A 145 ? 0.1808 0.2348 0.2949 -0.0542 -0.0091 0.0017  145 ASP   A OD1 
3161 O  OD2 . ASP   A 145 ? 0.2035 0.2439 0.2819 -0.0521 -0.0275 -0.0124 145 ASP   A OD2 
3166 N  N   . THR   A 146 ? 0.1371 0.1390 0.1908 -0.0080 0.0120  0.0052  146 THR   A N   
3167 C  CA  . THR   A 146 ? 0.1333 0.1311 0.1917 0.0001  0.0070  0.0080  146 THR   A CA  
3168 C  C   . THR   A 146 ? 0.1345 0.1289 0.1922 0.0015  0.0046  0.0092  146 THR   A C   
3169 O  O   . THR   A 146 ? 0.1406 0.1406 0.2129 0.0028  0.0028  0.0084  146 THR   A O   
3170 C  CB  . THR   A 146 ? 0.1348 0.1387 0.1909 0.0041  0.0136  0.0168  146 THR   A CB  
3171 O  OG1 . THR   A 146 ? 0.1309 0.1530 0.1935 0.0016  0.0089  0.0101  146 THR   A OG1 
3172 C  CG2 . THR   A 146 ? 0.1319 0.1439 0.2183 -0.0009 0.0108  0.0139  146 THR   A CG2 
3180 N  N   . VAL   A 147 ? 0.1291 0.1325 0.1733 -0.0038 0.0146  0.0118  147 VAL   A N   
3181 C  CA  . VAL   A 147 ? 0.1293 0.1385 0.1753 -0.0093 0.0217  0.0196  147 VAL   A CA  
3182 C  C   . VAL   A 147 ? 0.1295 0.1366 0.2042 -0.0101 0.0169  0.0247  147 VAL   A C   
3183 O  O   . VAL   A 147 ? 0.1266 0.1408 0.2266 -0.0109 0.0074  0.0225  147 VAL   A O   
3184 C  CB  . VAL   A 147 ? 0.1463 0.1341 0.1725 -0.0075 0.0193  0.0199  147 VAL   A CB  
3185 C  CG1 . VAL   A 147 ? 0.1809 0.1459 0.1749 -0.0001 0.0119  0.0346  147 VAL   A CG1 
3186 C  CG2 . VAL   A 147 ? 0.1464 0.1385 0.1663 -0.0120 0.0100  0.0212  147 VAL   A CG2 
3196 N  N   . ARG   A 148 ? 0.1300 0.1435 0.2091 -0.0044 0.0185  0.0458  148 ARG   A N   
3197 C  CA  . ARG   A 148 ? 0.1345 0.1387 0.2024 -0.0035 0.0164  0.0451  148 ARG   A CA  
3198 C  C   . ARG   A 148 ? 0.1538 0.1437 0.2069 -0.0088 0.0119  0.0540  148 ARG   A C   
3199 O  O   . ARG   A 148 ? 0.1809 0.1519 0.2267 -0.0179 0.0134  0.0453  148 ARG   A O   
3200 C  CB  . ARG   A 148 ? 0.1420 0.1410 0.2248 -0.0017 0.0251  0.0387  148 ARG   A CB  
3201 C  CG  . ARG   A 148 ? 0.1565 0.1422 0.2570 -0.0005 0.0380  0.0220  148 ARG   A CG  
3202 C  CD  . ARG   A 148 ? 0.1721 0.1445 0.2832 0.0001  0.0464  0.0467  148 ARG   A CD  
3203 N  NE  . ARG   A 148 ? 0.1680 0.1475 0.2738 0.0113  0.0485  0.0569  148 ARG   A NE  
3204 C  CZ  . ARG   A 148 ? 0.1663 0.1336 0.2549 0.0134  0.0433  0.0523  148 ARG   A CZ  
3205 N  NH1 . ARG   A 148 ? 0.1727 0.1374 0.2596 -0.0007 0.0430  0.0205  148 ARG   A NH1 
3206 N  NH2 . ARG   A 148 ? 0.1574 0.1533 0.2526 0.0221  0.0386  0.0500  148 ARG   A NH2 
3220 N  N   . THR   A 149 ? 0.1516 0.1464 0.1965 -0.0114 0.0042  0.0414  149 THR   A N   
3221 C  CA  . THR   A 149 ? 0.1471 0.1541 0.1971 -0.0118 0.0130  0.0358  149 THR   A CA  
3222 C  C   . THR   A 149 ? 0.1379 0.1504 0.1831 -0.0199 0.0120  0.0407  149 THR   A C   
3223 O  O   . THR   A 149 ? 0.1402 0.1599 0.1998 -0.0204 0.0199  0.0373  149 THR   A O   
3224 C  CB  . THR   A 149 ? 0.1432 0.1624 0.2048 -0.0150 0.0116  0.0312  149 THR   A CB  
3225 O  OG1 . THR   A 149 ? 0.1533 0.1510 0.2098 -0.0184 0.0111  0.0311  149 THR   A OG1 
3226 C  CG2 . THR   A 149 ? 0.1418 0.1791 0.2075 0.0043  0.0043  0.0277  149 THR   A CG2 
3234 N  N   . ASN   A 150 ? 0.1422 0.1562 0.1854 -0.0083 0.0042  0.0411  150 ASN   A N   
3235 C  CA  . ASN   A 150 ? 0.1553 0.1701 0.1840 -0.0102 0.0063  0.0357  150 ASN   A CA  
3236 C  C   . ASN   A 150 ? 0.1415 0.1577 0.1909 -0.0171 0.0030  0.0416  150 ASN   A C   
3237 O  O   . ASN   A 150 ? 0.1504 0.1688 0.2271 -0.0140 -0.0076 0.0406  150 ASN   A O   
3238 C  CB  . ASN   A 150 ? 0.1984 0.2019 0.2136 -0.0145 0.0284  0.0611  150 ASN   A CB  
3239 C  CG  . ASN   A 150 ? 0.2554 0.2431 0.2762 -0.0125 0.0129  0.0687  150 ASN   A CG  
3240 O  OD1 . ASN   A 150 ? 0.2766 0.2541 0.2887 -0.0245 0.0169  0.0855  150 ASN   A OD1 
3241 N  ND2 . ASN   A 150 ? 0.2904 0.2689 0.3203 -0.0074 0.0058  0.0794  150 ASN   A ND2 
3248 N  N   . VAL   A 151 ? 0.1435 0.1447 0.1914 -0.0173 0.0051  0.0361  151 VAL   A N   
3249 C  CA  . VAL   A 151 ? 0.1505 0.1463 0.1781 -0.0187 0.0111  0.0366  151 VAL   A CA  
3250 C  C   . VAL   A 151 ? 0.1422 0.1453 0.1704 -0.0224 0.0128  0.0363  151 VAL   A C   
3251 O  O   . VAL   A 151 ? 0.1473 0.1540 0.2158 -0.0148 0.0125  0.0304  151 VAL   A O   
3252 C  CB  . VAL   A 151 ? 0.1701 0.1718 0.1824 -0.0078 0.0096  0.0308  151 VAL   A CB  
3253 C  CG1 . VAL   A 151 ? 0.1632 0.1933 0.2107 -0.0123 0.0115  0.0334  151 VAL   A CG1 
3254 C  CG2 . VAL   A 151 ? 0.1807 0.1758 0.1754 -0.0052 0.0205  0.0254  151 VAL   A CG2 
3264 N  N   . TYR   A 152 ? 0.1316 0.1507 0.1718 -0.0173 0.0047  0.0261  152 TYR   A N   
3265 C  CA  . TYR   A 152 ? 0.1325 0.1539 0.1583 -0.0225 0.0076  0.0224  152 TYR   A CA  
3266 C  C   . TYR   A 152 ? 0.1348 0.1454 0.1582 -0.0170 0.0081  0.0272  152 TYR   A C   
3267 O  O   . TYR   A 152 ? 0.1513 0.1437 0.1622 -0.0256 0.0155  0.0257  152 TYR   A O   
3268 C  CB  . TYR   A 152 ? 0.1462 0.1597 0.1556 -0.0167 0.0166  0.0232  152 TYR   A CB  
3269 C  CG  . TYR   A 152 ? 0.1675 0.1848 0.1655 -0.0240 0.0260  0.0356  152 TYR   A CG  
3270 C  CD1 . TYR   A 152 ? 0.1860 0.2036 0.1978 -0.0076 0.0310  0.0498  152 TYR   A CD1 
3271 C  CD2 . TYR   A 152 ? 0.1702 0.2054 0.1564 -0.0378 0.0180  0.0303  152 TYR   A CD2 
3272 C  CE1 . TYR   A 152 ? 0.2169 0.2198 0.2131 -0.0006 0.0184  0.0604  152 TYR   A CE1 
3273 C  CE2 . TYR   A 152 ? 0.1973 0.2179 0.1729 -0.0409 0.0191  0.0367  152 TYR   A CE2 
3274 C  CZ  . TYR   A 152 ? 0.2313 0.2191 0.2030 -0.0200 0.0229  0.0645  152 TYR   A CZ  
3275 O  OH  . TYR   A 152 ? 0.2641 0.2348 0.2429 -0.0169 0.0239  0.0796  152 TYR   A OH  
3285 N  N   . LEU   A 153 ? 0.1318 0.1418 0.1631 -0.0187 0.0170  0.0289  153 LEU   A N   
3286 C  CA  . LEU   A 153 ? 0.1297 0.1447 0.1733 -0.0083 0.0119  0.0268  153 LEU   A CA  
3287 C  C   . LEU   A 153 ? 0.1323 0.1457 0.1890 -0.0050 0.0216  0.0239  153 LEU   A C   
3288 O  O   . LEU   A 153 ? 0.1386 0.1596 0.2235 -0.0084 0.0316  0.0151  153 LEU   A O   
3289 C  CB  . LEU   A 153 ? 0.1321 0.1457 0.1817 -0.0127 0.0041  0.0356  153 LEU   A CB  
3290 C  CG  . LEU   A 153 ? 0.1397 0.1450 0.1782 -0.0094 0.0071  0.0210  153 LEU   A CG  
3291 C  CD1 . LEU   A 153 ? 0.1482 0.1493 0.1923 -0.0044 -0.0014 0.0208  153 LEU   A CD1 
3292 C  CD2 . LEU   A 153 ? 0.1502 0.1540 0.1734 -0.0127 0.0206  0.0059  153 LEU   A CD2 
3304 N  N   A ALA   A 154 ? 0.1317 0.1434 0.1861 -0.0050 0.0228  0.0349  154 ALA   A N   
3305 N  N   B ALA   A 154 ? 0.1335 0.1437 0.1778 -0.0022 0.0225  0.0271  154 ALA   A N   
3306 C  CA  A ALA   A 154 ? 0.1434 0.1476 0.2019 -0.0031 0.0254  0.0337  154 ALA   A CA  
3307 C  CA  B ALA   A 154 ? 0.1416 0.1446 0.1789 0.0010  0.0216  0.0210  154 ALA   A CA  
3308 C  C   A ALA   A 154 ? 0.1457 0.1484 0.2086 0.0000  0.0202  0.0331  154 ALA   A C   
3309 C  C   B ALA   A 154 ? 0.1428 0.1435 0.1820 0.0039  0.0183  0.0177  154 ALA   A C   
3310 O  O   A ALA   A 154 ? 0.1490 0.1575 0.2015 -0.0025 0.0164  0.0342  154 ALA   A O   
3311 O  O   B ALA   A 154 ? 0.1451 0.1449 0.1805 0.0082  0.0138  0.0133  154 ALA   A O   
3312 C  CB  A ALA   A 154 ? 0.1519 0.1468 0.2087 0.0081  0.0091  0.0190  154 ALA   A CB  
3313 C  CB  B ALA   A 154 ? 0.1475 0.1432 0.1786 0.0071  0.0123  0.0110  154 ALA   A CB  
3324 N  N   A VAL   A 155 ? 0.1501 0.1466 0.2091 0.0073  0.0146  0.0417  155 VAL   A N   
3325 N  N   B VAL   A 155 ? 0.1457 0.1480 0.1855 0.0077  0.0115  0.0277  155 VAL   A N   
3326 C  CA  A VAL   A 155 ? 0.1535 0.1566 0.2269 0.0019  0.0167  0.0419  155 VAL   A CA  
3327 C  CA  B VAL   A 155 ? 0.1476 0.1524 0.1934 0.0030  0.0094  0.0328  155 VAL   A CA  
3328 C  C   A VAL   A 155 ? 0.1646 0.1593 0.2601 0.0130  0.0006  0.0451  155 VAL   A C   
3329 C  C   B VAL   A 155 ? 0.1536 0.1519 0.2011 0.0062  0.0039  0.0263  155 VAL   A C   
3330 O  O   A VAL   A 155 ? 0.1592 0.1604 0.2767 0.0165  0.0058  0.0434  155 VAL   A O   
3331 O  O   B VAL   A 155 ? 0.1464 0.1494 0.2185 0.0028  0.0034  0.0140  155 VAL   A O   
3332 C  CB  A VAL   A 155 ? 0.1530 0.1618 0.2203 0.0021  0.0047  0.0296  155 VAL   A CB  
3333 C  CB  B VAL   A 155 ? 0.1481 0.1582 0.1887 0.0029  0.0035  0.0334  155 VAL   A CB  
3334 C  CG1 A VAL   A 155 ? 0.1710 0.1785 0.2365 0.0007  -0.0045 0.0335  155 VAL   A CG1 
3335 C  CG1 B VAL   A 155 ? 0.1556 0.1672 0.1954 0.0045  -0.0022 0.0397  155 VAL   A CG1 
3336 C  CG2 A VAL   A 155 ? 0.1557 0.1645 0.2248 0.0053  0.0013  0.0255  155 VAL   A CG2 
3337 C  CG2 B VAL   A 155 ? 0.1524 0.1592 0.1951 0.0001  0.0066  0.0285  155 VAL   A CG2 
3356 N  N   A PHE   A 156 ? 0.1802 0.1614 0.2806 0.0143  -0.0115 0.0642  156 PHE   A N   
3357 N  N   B PHE   A 156 ? 0.1631 0.1568 0.1868 0.0151  -0.0024 0.0284  156 PHE   A N   
3358 C  CA  A PHE   A 156 ? 0.2052 0.1706 0.3109 0.0204  -0.0198 0.0718  156 PHE   A CA  
3359 C  CA  B PHE   A 156 ? 0.1633 0.1641 0.1843 0.0250  -0.0015 0.0413  156 PHE   A CA  
3360 C  C   A PHE   A 156 ? 0.2067 0.1765 0.3180 0.0287  -0.0119 0.0747  156 PHE   A C   
3361 C  C   B PHE   A 156 ? 0.1658 0.1771 0.2070 0.0262  0.0039  0.0424  156 PHE   A C   
3362 O  O   A PHE   A 156 ? 0.2156 0.1881 0.3445 0.0359  0.0023  0.0526  156 PHE   A O   
3363 O  O   B PHE   A 156 ? 0.1632 0.1812 0.2193 0.0279  0.0098  0.0550  156 PHE   A O   
3364 C  CB  A PHE   A 156 ? 0.2360 0.1764 0.3253 0.0166  -0.0333 0.0884  156 PHE   A CB  
3365 C  CB  B PHE   A 156 ? 0.1670 0.1694 0.1989 0.0247  0.0015  0.0310  156 PHE   A CB  
3366 C  CG  A PHE   A 156 ? 0.2676 0.1939 0.3424 0.0244  -0.0418 0.0808  156 PHE   A CG  
3367 C  CG  B PHE   A 156 ? 0.1784 0.1720 0.2083 0.0227  0.0146  0.0152  156 PHE   A CG  
3368 C  CD1 A PHE   A 156 ? 0.2860 0.2042 0.3589 0.0263  -0.0431 0.0652  156 PHE   A CD1 
3369 C  CD1 B PHE   A 156 ? 0.1866 0.1797 0.2111 0.0183  0.0237  0.0045  156 PHE   A CD1 
3370 C  CD2 A PHE   A 156 ? 0.2824 0.2093 0.3588 0.0313  -0.0414 0.0795  156 PHE   A CD2 
3371 C  CD2 B PHE   A 156 ? 0.1858 0.1685 0.2181 0.0257  0.0214  0.0152  156 PHE   A CD2 
3372 C  CE1 A PHE   A 156 ? 0.3009 0.2158 0.3791 0.0285  -0.0383 0.0538  156 PHE   A CE1 
3373 C  CE1 B PHE   A 156 ? 0.1948 0.1810 0.2164 0.0230  0.0278  0.0025  156 PHE   A CE1 
3374 C  CE2 A PHE   A 156 ? 0.2987 0.2217 0.3716 0.0317  -0.0399 0.0667  156 PHE   A CE2 
3375 C  CE2 B PHE   A 156 ? 0.1935 0.1670 0.2134 0.0294  0.0233  0.0129  156 PHE   A CE2 
3376 C  CZ  A PHE   A 156 ? 0.3054 0.2231 0.3838 0.0328  -0.0385 0.0473  156 PHE   A CZ  
3377 C  CZ  B PHE   A 156 ? 0.1954 0.1778 0.2201 0.0286  0.0291  0.0122  156 PHE   A CZ  
3396 N  N   A ASP   A 157 ? 0.2096 0.1830 0.3091 0.0209  -0.0190 0.0888  157 ASP   A N   
3397 N  N   B ASP   A 157 ? 0.1723 0.1893 0.2047 0.0244  -0.0091 0.0327  157 ASP   A N   
3398 C  CA  A ASP   A 157 ? 0.2178 0.1939 0.3144 0.0240  -0.0275 0.0948  157 ASP   A CA  
3399 C  CA  B ASP   A 157 ? 0.1798 0.2072 0.2149 0.0132  -0.0086 0.0306  157 ASP   A CA  
3400 C  C   A ASP   A 157 ? 0.2018 0.2019 0.3203 0.0283  -0.0094 0.1084  157 ASP   A C   
3401 C  C   B ASP   A 157 ? 0.1780 0.2155 0.2362 0.0044  0.0006  0.0302  157 ASP   A C   
3402 O  O   A ASP   A 157 ? 0.1950 0.1954 0.3174 0.0303  0.0058  0.1151  157 ASP   A O   
3403 O  O   B ASP   A 157 ? 0.1749 0.2179 0.2376 0.0012  0.0002  0.0250  157 ASP   A O   
3404 C  CB  A ASP   A 157 ? 0.2406 0.1998 0.3317 0.0289  -0.0418 0.0901  157 ASP   A CB  
3405 C  CB  B ASP   A 157 ? 0.1882 0.2188 0.2151 0.0113  -0.0059 0.0344  157 ASP   A CB  
3406 C  CG  A ASP   A 157 ? 0.2677 0.2155 0.3674 0.0391  -0.0538 0.0741  157 ASP   A CG  
3407 C  CG  B ASP   A 157 ? 0.2027 0.2324 0.2292 0.0138  -0.0104 0.0334  157 ASP   A CG  
3408 O  OD1 A ASP   A 157 ? 0.3022 0.2255 0.3884 0.0374  -0.0767 0.0600  157 ASP   A OD1 
3409 O  OD1 B ASP   A 157 ? 0.2059 0.2463 0.2470 0.0123  -0.0107 0.0302  157 ASP   A OD1 
3410 O  OD2 A ASP   A 157 ? 0.2576 0.2096 0.3847 0.0404  -0.0451 0.0816  157 ASP   A OD2 
3411 O  OD2 B ASP   A 157 ? 0.2145 0.2353 0.2389 0.0167  -0.0201 0.0313  157 ASP   A OD2 
3420 N  N   A LYS   A 158 ? 0.1968 0.2260 0.3463 0.0272  -0.0045 0.0923  158 LYS   A N   
3421 N  N   B LYS   A 158 ? 0.1855 0.2248 0.2639 -0.0028 0.0029  0.0241  158 LYS   A N   
3422 C  CA  A LYS   A 158 ? 0.1919 0.2487 0.3652 0.0384  0.0141  0.0867  158 LYS   A CA  
3423 C  CA  B LYS   A 158 ? 0.2009 0.2344 0.2850 -0.0103 0.0077  0.0224  158 LYS   A CA  
3424 C  C   A LYS   A 158 ? 0.1754 0.2619 0.3585 0.0439  0.0102  0.0976  158 LYS   A C   
3425 C  C   B LYS   A 158 ? 0.1963 0.2371 0.2866 -0.0169 -0.0089 0.0294  158 LYS   A C   
3426 O  O   A LYS   A 158 ? 0.1733 0.2584 0.3582 0.0370  0.0227  0.0942  158 LYS   A O   
3427 O  O   B LYS   A 158 ? 0.1923 0.2293 0.2846 -0.0230 -0.0162 0.0337  158 LYS   A O   
3428 C  CB  A LYS   A 158 ? 0.2031 0.2614 0.3816 0.0397  0.0376  0.0867  158 LYS   A CB  
3429 C  CB  B LYS   A 158 ? 0.2211 0.2451 0.3055 -0.0072 0.0201  0.0171  158 LYS   A CB  
3430 C  CG  A LYS   A 158 ? 0.2240 0.2788 0.4053 0.0315  0.0594  0.0964  158 LYS   A CG  
3431 C  CG  B LYS   A 158 ? 0.2408 0.2544 0.3290 -0.0030 0.0234  0.0198  158 LYS   A CG  
3432 C  CD  A LYS   A 158 ? 0.2262 0.2914 0.4116 0.0307  0.0896  0.1088  158 LYS   A CD  
3433 C  CD  B LYS   A 158 ? 0.2495 0.2619 0.3426 0.0008  0.0303  0.0225  158 LYS   A CD  
3434 C  CE  A LYS   A 158 ? 0.2289 0.3007 0.4284 0.0254  0.1079  0.1175  158 LYS   A CE  
3435 C  CE  B LYS   A 158 ? 0.2521 0.2654 0.3495 0.0011  0.0343  0.0250  158 LYS   A CE  
3436 N  NZ  A LYS   A 158 ? 0.2280 0.3065 0.4284 0.0270  0.1128  0.1295  158 LYS   A NZ  
3437 N  NZ  B LYS   A 158 ? 0.2567 0.2702 0.3615 0.0037  0.0367  0.0189  158 LYS   A NZ  
3464 N  N   A ASN   A 159 ? 0.1680 0.2817 0.3691 0.0518  -0.0035 0.0966  159 ASN   A N   
3465 N  N   B ASN   A 159 ? 0.2024 0.2514 0.3003 -0.0134 -0.0134 0.0296  159 ASN   A N   
3466 C  CA  A ASN   A 159 ? 0.1710 0.2993 0.3658 0.0573  -0.0114 0.1059  159 ASN   A CA  
3467 C  CA  B ASN   A 159 ? 0.2131 0.2653 0.3113 -0.0078 -0.0147 0.0364  159 ASN   A CA  
3468 C  C   A ASN   A 159 ? 0.1488 0.2953 0.3185 0.0405  -0.0032 0.1059  159 ASN   A C   
3469 C  C   B ASN   A 159 ? 0.1975 0.2585 0.2778 -0.0137 -0.0105 0.0388  159 ASN   A C   
3470 O  O   A ASN   A 159 ? 0.1380 0.3127 0.3053 0.0254  -0.0175 0.0937  159 ASN   A O   
3471 O  O   B ASN   A 159 ? 0.1947 0.2682 0.2777 -0.0214 -0.0145 0.0353  159 ASN   A O   
3472 C  CB  A ASN   A 159 ? 0.2004 0.3217 0.4158 0.0637  -0.0205 0.1133  159 ASN   A CB  
3473 C  CB  B ASN   A 159 ? 0.2408 0.2856 0.3603 0.0008  -0.0177 0.0398  159 ASN   A CB  
3474 C  CG  A ASN   A 159 ? 0.2265 0.3432 0.4654 0.0613  -0.0161 0.1075  159 ASN   A CG  
3475 C  CG  B ASN   A 159 ? 0.2654 0.3032 0.4021 0.0030  -0.0199 0.0411  159 ASN   A CG  
3476 O  OD1 A ASN   A 159 ? 0.2257 0.3520 0.4793 0.0584  -0.0059 0.1021  159 ASN   A OD1 
3477 O  OD1 B ASN   A 159 ? 0.2743 0.3087 0.4136 0.0030  -0.0215 0.0402  159 ASN   A OD1 
3478 N  ND2 A ASN   A 159 ? 0.2320 0.3522 0.4890 0.0625  -0.0179 0.1019  159 ASN   A ND2 
3479 N  ND2 B ASN   A 159 ? 0.2738 0.3098 0.4188 0.0029  -0.0244 0.0414  159 ASN   A ND2 
3492 N  N   A LEU   A 160 ? 0.1398 0.2761 0.3053 0.0334  -0.0203 0.1073  160 LEU   A N   
3493 N  N   B LEU   A 160 ? 0.1875 0.2446 0.2596 -0.0129 -0.0164 0.0441  160 LEU   A N   
3494 C  CA  A LEU   A 160 ? 0.1396 0.2596 0.2911 0.0195  -0.0097 0.1026  160 LEU   A CA  
3495 C  CA  B LEU   A 160 ? 0.1876 0.2367 0.2518 -0.0117 -0.0028 0.0470  160 LEU   A CA  
3496 C  C   A LEU   A 160 ? 0.1230 0.2525 0.2802 0.0105  0.0137  0.0923  160 LEU   A C   
3497 C  C   B LEU   A 160 ? 0.1772 0.2263 0.2398 -0.0123 0.0056  0.0503  160 LEU   A C   
3498 O  O   A LEU   A 160 ? 0.1218 0.2665 0.3029 0.0031  0.0138  0.0811  160 LEU   A O   
3499 O  O   B LEU   A 160 ? 0.1765 0.2286 0.2474 -0.0163 0.0101  0.0440  160 LEU   A O   
3500 C  CB  A LEU   A 160 ? 0.1561 0.2515 0.2798 0.0033  -0.0082 0.1036  160 LEU   A CB  
3501 C  CB  B LEU   A 160 ? 0.1962 0.2392 0.2526 -0.0114 0.0006  0.0460  160 LEU   A CB  
3502 C  CG  A LEU   A 160 ? 0.1658 0.2507 0.2773 -0.0169 -0.0000 0.0915  160 LEU   A CG  
3503 C  CG  B LEU   A 160 ? 0.2028 0.2433 0.2558 -0.0130 0.0063  0.0392  160 LEU   A CG  
3504 C  CD1 A LEU   A 160 ? 0.1835 0.2640 0.2891 -0.0200 0.0059  0.0733  160 LEU   A CD1 
3505 C  CD1 B LEU   A 160 ? 0.2098 0.2496 0.2590 -0.0139 0.0124  0.0313  160 LEU   A CD1 
3506 C  CD2 A LEU   A 160 ? 0.1667 0.2403 0.2655 -0.0237 0.0028  0.0910  160 LEU   A CD2 
3507 C  CD2 B LEU   A 160 ? 0.2034 0.2427 0.2551 -0.0110 0.0082  0.0350  160 LEU   A CD2 
3530 N  N   A TYR   A 161 ? 0.1248 0.2398 0.2822 0.0129  0.0125  0.0842  161 TYR   A N   
3531 N  N   B TYR   A 161 ? 0.1719 0.2179 0.2288 -0.0079 0.0021  0.0595  161 TYR   A N   
3532 C  CA  A TYR   A 161 ? 0.1321 0.2295 0.2650 0.0158  0.0165  0.0747  161 TYR   A CA  
3533 C  CA  B TYR   A 161 ? 0.1688 0.2123 0.2164 -0.0041 0.0021  0.0626  161 TYR   A CA  
3534 C  C   A TYR   A 161 ? 0.1305 0.2423 0.2704 0.0128  0.0187  0.0627  161 TYR   A C   
3535 C  C   B TYR   A 161 ? 0.1696 0.2171 0.2153 -0.0054 0.0073  0.0642  161 TYR   A C   
3536 O  O   A TYR   A 161 ? 0.1277 0.2430 0.2792 0.0055  0.0177  0.0537  161 TYR   A O   
3537 O  O   B TYR   A 161 ? 0.1676 0.2134 0.2008 -0.0056 0.0065  0.0671  161 TYR   A O   
3538 C  CB  A TYR   A 161 ? 0.1477 0.2099 0.2724 0.0155  0.0128  0.0625  161 TYR   A CB  
3539 C  CB  B TYR   A 161 ? 0.1686 0.2020 0.2225 0.0001  0.0006  0.0548  161 TYR   A CB  
3540 C  CG  A TYR   A 161 ? 0.1574 0.1963 0.2570 0.0139  0.0143  0.0461  161 TYR   A CG  
3541 C  CG  B TYR   A 161 ? 0.1667 0.1961 0.2240 0.0025  0.0035  0.0439  161 TYR   A CG  
3542 C  CD1 A TYR   A 161 ? 0.1596 0.1948 0.2624 0.0078  0.0097  0.0444  161 TYR   A CD1 
3543 C  CD1 B TYR   A 161 ? 0.1656 0.1916 0.2243 0.0014  0.0045  0.0440  161 TYR   A CD1 
3544 C  CD2 A TYR   A 161 ? 0.1617 0.2058 0.2538 0.0117  0.0028  0.0321  161 TYR   A CD2 
3545 C  CD2 B TYR   A 161 ? 0.1651 0.2043 0.2263 0.0035  0.0016  0.0315  161 TYR   A CD2 
3546 C  CE1 A TYR   A 161 ? 0.1668 0.1959 0.2716 -0.0065 0.0026  0.0498  161 TYR   A CE1 
3547 C  CE1 B TYR   A 161 ? 0.1680 0.1944 0.2274 -0.0028 0.0102  0.0421  161 TYR   A CE1 
3548 C  CE2 A TYR   A 161 ? 0.1696 0.1998 0.2600 -0.0027 -0.0008 0.0452  161 TYR   A CE2 
3549 C  CE2 B TYR   A 161 ? 0.1636 0.1988 0.2260 0.0003  0.0126  0.0331  161 TYR   A CE2 
3550 C  CZ  A TYR   A 161 ? 0.1810 0.1998 0.2759 -0.0149 -0.0072 0.0583  161 TYR   A CZ  
3551 C  CZ  B TYR   A 161 ? 0.1683 0.1964 0.2276 0.0001  0.0165  0.0403  161 TYR   A CZ  
3552 O  OH  A TYR   A 161 ? 0.1977 0.2055 0.3055 -0.0350 -0.0318 0.0744  161 TYR   A OH  
3553 O  OH  B TYR   A 161 ? 0.1674 0.1999 0.2241 -0.0038 0.0266  0.0467  161 TYR   A OH  
3572 N  N   A ASP   A 162 ? 0.1286 0.2525 0.2842 0.0130  0.0152  0.0628  162 ASP   A N   
3573 N  N   B ASP   A 162 ? 0.1702 0.2257 0.2345 -0.0062 0.0131  0.0645  162 ASP   A N   
3574 C  CA  A ASP   A 162 ? 0.1284 0.2743 0.2979 0.0081  0.0202  0.0646  162 ASP   A CA  
3575 C  CA  B ASP   A 162 ? 0.1726 0.2436 0.2479 -0.0079 0.0157  0.0611  162 ASP   A CA  
3576 C  C   A ASP   A 162 ? 0.1162 0.2876 0.2993 -0.0038 0.0249  0.0652  162 ASP   A C   
3577 C  C   B ASP   A 162 ? 0.1857 0.2594 0.2567 -0.0087 0.0185  0.0606  162 ASP   A C   
3578 O  O   A ASP   A 162 ? 0.1195 0.2835 0.3140 -0.0113 0.0354  0.0586  162 ASP   A O   
3579 O  O   B ASP   A 162 ? 0.1881 0.2569 0.2618 -0.0125 0.0193  0.0627  162 ASP   A O   
3580 C  CB  A ASP   A 162 ? 0.1450 0.2879 0.3091 0.0103  0.0344  0.0563  162 ASP   A CB  
3581 C  CB  B ASP   A 162 ? 0.1647 0.2511 0.2657 -0.0113 0.0206  0.0475  162 ASP   A CB  
3582 C  CG  A ASP   A 162 ? 0.1690 0.3039 0.3357 0.0174  0.0419  0.0417  162 ASP   A CG  
3583 C  CG  B ASP   A 162 ? 0.1606 0.2618 0.2812 -0.0114 0.0238  0.0307  162 ASP   A CG  
3584 O  OD1 A ASP   A 162 ? 0.1865 0.3108 0.3296 0.0100  0.0667  0.0455  162 ASP   A OD1 
3585 O  OD1 B ASP   A 162 ? 0.1675 0.2653 0.2802 -0.0153 0.0325  0.0305  162 ASP   A OD1 
3586 O  OD2 A ASP   A 162 ? 0.1882 0.3115 0.3670 0.0243  0.0384  0.0218  162 ASP   A OD2 
3587 O  OD2 B ASP   A 162 ? 0.1494 0.2666 0.2882 -0.0134 0.0292  0.0202  162 ASP   A OD2 
3596 N  N   A LYS   A 163 ? 0.1231 0.3085 0.3110 -0.0080 0.0041  0.0665  163 LYS   A N   
3597 N  N   B LYS   A 163 ? 0.2017 0.2789 0.2737 -0.0059 0.0152  0.0556  163 LYS   A N   
3598 C  CA  A LYS   A 163 ? 0.1389 0.3246 0.3021 -0.0176 -0.0055 0.0618  163 LYS   A CA  
3599 C  CA  B LYS   A 163 ? 0.2174 0.2950 0.2798 -0.0027 0.0186  0.0472  163 LYS   A CA  
3600 C  C   A LYS   A 163 ? 0.1336 0.3042 0.2853 -0.0234 0.0163  0.0571  163 LYS   A C   
3601 C  C   B LYS   A 163 ? 0.2115 0.2849 0.2531 -0.0012 0.0251  0.0420  163 LYS   A C   
3602 O  O   A LYS   A 163 ? 0.1299 0.3189 0.3066 -0.0269 0.0170  0.0528  163 LYS   A O   
3603 O  O   B LYS   A 163 ? 0.2159 0.2908 0.2622 -0.0032 0.0244  0.0394  163 LYS   A O   
3604 C  CB  A LYS   A 163 ? 0.1858 0.3609 0.3445 -0.0067 -0.0236 0.0648  163 LYS   A CB  
3605 C  CB  B LYS   A 163 ? 0.2455 0.3198 0.3256 0.0030  0.0134  0.0440  163 LYS   A CB  
3606 C  CG  A LYS   A 163 ? 0.2390 0.3920 0.3945 -0.0036 -0.0145 0.0688  163 LYS   A CG  
3607 C  CG  B LYS   A 163 ? 0.2701 0.3411 0.3724 0.0041  0.0180  0.0424  163 LYS   A CG  
3608 C  CD  A LYS   A 163 ? 0.2998 0.4183 0.4549 -0.0016 -0.0067 0.0679  163 LYS   A CD  
3609 C  CD  B LYS   A 163 ? 0.2931 0.3585 0.4227 0.0048  0.0213  0.0398  163 LYS   A CD  
3610 C  CE  A LYS   A 163 ? 0.3458 0.4359 0.5019 -0.0024 -0.0007 0.0707  163 LYS   A CE  
3611 C  CE  B LYS   A 163 ? 0.3079 0.3704 0.4605 0.0047  0.0248  0.0419  163 LYS   A CE  
3612 N  NZ  A LYS   A 163 ? 0.3719 0.4436 0.5292 -0.0047 0.0050  0.0755  163 LYS   A NZ  
3613 N  NZ  B LYS   A 163 ? 0.3158 0.3758 0.4839 0.0056  0.0260  0.0426  163 LYS   A NZ  
3640 N  N   A LEU   A 164 ? 0.1236 0.2701 0.2571 -0.0344 0.0134  0.0527  164 LEU   A N   
3641 N  N   B LEU   A 164 ? 0.1992 0.2708 0.2275 -0.0002 0.0208  0.0399  164 LEU   A N   
3642 C  CA  A LEU   A 164 ? 0.1276 0.2404 0.2483 -0.0329 0.0281  0.0439  164 LEU   A CA  
3643 C  CA  B LEU   A 164 ? 0.1875 0.2576 0.2116 0.0048  0.0252  0.0355  164 LEU   A CA  
3644 C  C   A LEU   A 164 ? 0.1302 0.2281 0.2497 -0.0285 0.0325  0.0429  164 LEU   A C   
3645 C  C   B LEU   A 164 ? 0.1858 0.2541 0.2049 0.0043  0.0303  0.0374  164 LEU   A C   
3646 O  O   A LEU   A 164 ? 0.1398 0.2381 0.2648 -0.0267 0.0550  0.0193  164 LEU   A O   
3647 O  O   B LEU   A 164 ? 0.1891 0.2599 0.2125 0.0025  0.0483  0.0255  164 LEU   A O   
3648 C  CB  A LEU   A 164 ? 0.1325 0.2346 0.2563 -0.0346 0.0301  0.0452  164 LEU   A CB  
3649 C  CB  B LEU   A 164 ? 0.1789 0.2529 0.2134 0.0087  0.0184  0.0333  164 LEU   A CB  
3650 C  CG  A LEU   A 164 ? 0.1422 0.2336 0.2578 -0.0309 0.0232  0.0483  164 LEU   A CG  
3651 C  CG  B LEU   A 164 ? 0.1719 0.2492 0.2112 0.0113  0.0075  0.0342  164 LEU   A CG  
3652 C  CD1 A LEU   A 164 ? 0.1368 0.2319 0.2570 -0.0262 0.0137  0.0495  164 LEU   A CD1 
3653 C  CD1 B LEU   A 164 ? 0.1680 0.2471 0.2155 0.0133  0.0041  0.0343  164 LEU   A CD1 
3654 C  CD2 A LEU   A 164 ? 0.1513 0.2303 0.2584 -0.0289 0.0219  0.0519  164 LEU   A CD2 
3655 C  CD2 B LEU   A 164 ? 0.1694 0.2464 0.2097 0.0137  0.0027  0.0340  164 LEU   A CD2 
3678 N  N   A VAL   A 165 ? 0.1355 0.2219 0.2522 -0.0223 0.0359  0.0453  165 VAL   A N   
3679 N  N   B VAL   A 165 ? 0.1837 0.2497 0.2014 0.0054  0.0262  0.0407  165 VAL   A N   
3680 C  CA  A VAL   A 165 ? 0.1386 0.2194 0.2462 -0.0218 0.0424  0.0478  165 VAL   A CA  
3681 C  CA  B VAL   A 165 ? 0.1843 0.2480 0.1996 0.0074  0.0214  0.0417  165 VAL   A CA  
3682 C  C   A VAL   A 165 ? 0.1277 0.2265 0.2541 -0.0194 0.0373  0.0440  165 VAL   A C   
3683 C  C   B VAL   A 165 ? 0.1737 0.2549 0.2029 0.0141  0.0209  0.0321  165 VAL   A C   
3684 O  O   A VAL   A 165 ? 0.1225 0.2250 0.2421 -0.0231 0.0340  0.0409  165 VAL   A O   
3685 O  O   B VAL   A 165 ? 0.1696 0.2542 0.2094 0.0203  0.0207  0.0269  165 VAL   A O   
3686 C  CB  A VAL   A 165 ? 0.1628 0.2196 0.2510 -0.0210 0.0491  0.0353  165 VAL   A CB  
3687 C  CB  B VAL   A 165 ? 0.1977 0.2414 0.2015 0.0043  0.0150  0.0422  165 VAL   A CB  
3688 C  CG1 A VAL   A 165 ? 0.1671 0.2260 0.2520 -0.0200 0.0551  0.0239  165 VAL   A CG1 
3689 C  CG1 B VAL   A 165 ? 0.2012 0.2427 0.2062 0.0046  0.0156  0.0368  165 VAL   A CG1 
3690 C  CG2 A VAL   A 165 ? 0.1804 0.2148 0.2623 -0.0199 0.0534  0.0407  165 VAL   A CG2 
3691 C  CG2 B VAL   A 165 ? 0.2055 0.2413 0.2122 0.0038  0.0076  0.0425  165 VAL   A CG2 
3710 N  N   A SER   A 166 ? 0.1296 0.2372 0.2740 -0.0219 0.0412  0.0446  166 SER   A N   
3711 N  N   B SER   A 166 ? 0.1640 0.2639 0.2093 0.0185  0.0174  0.0266  166 SER   A N   
3712 C  CA  A SER   A 166 ? 0.1357 0.2632 0.2965 -0.0229 0.0301  0.0459  166 SER   A CA  
3713 C  CA  B SER   A 166 ? 0.1617 0.2793 0.2281 0.0175  0.0027  0.0086  166 SER   A CA  
3714 C  C   A SER   A 166 ? 0.1372 0.2943 0.3010 -0.0319 0.0152  0.0246  166 SER   A C   
3715 C  C   B SER   A 166 ? 0.1699 0.2851 0.2461 0.0091  0.0090  0.0040  166 SER   A C   
3716 O  O   A SER   A 166 ? 0.1570 0.3022 0.3466 -0.0446 0.0140  -0.0057 166 SER   A O   
3717 O  O   B SER   A 166 ? 0.1715 0.2856 0.2599 0.0056  0.0187  -0.0116 166 SER   A O   
3718 C  CB  A SER   A 166 ? 0.1632 0.2723 0.3273 -0.0085 0.0187  0.0617  166 SER   A CB  
3719 C  CB  B SER   A 166 ? 0.1450 0.2912 0.2354 0.0315  -0.0313 -0.0075 166 SER   A CB  
3720 O  OG  A SER   A 166 ? 0.2056 0.2887 0.3851 0.0028  -0.0019 0.0740  166 SER   A OG  
3721 O  OG  B SER   A 166 ? 0.1647 0.3045 0.2417 0.0367  -0.0438 0.0046  166 SER   A OG  
3732 N  N   A SER   A 167 ? 0.1472 0.3109 0.2555 -0.0173 -0.0023 0.0284  167 SER   A N   
3733 N  N   B SER   A 167 ? 0.1843 0.2908 0.2474 0.0050  0.0088  0.0144  167 SER   A N   
3734 C  CA  A SER   A 167 ? 0.1669 0.3212 0.2316 -0.0170 -0.0198 0.0063  167 SER   A CA  
3735 C  CA  B SER   A 167 ? 0.2053 0.2925 0.2550 -0.0013 0.0114  0.0154  167 SER   A CA  
3736 C  C   A SER   A 167 ? 0.1716 0.3119 0.2255 -0.0083 -0.0094 -0.0060 167 SER   A C   
3737 C  C   B SER   A 167 ? 0.2092 0.2936 0.2734 0.0027  0.0204  0.0186  167 SER   A C   
3738 O  O   A SER   A 167 ? 0.1733 0.3107 0.2076 -0.0043 -0.0077 -0.0218 167 SER   A O   
3739 O  O   B SER   A 167 ? 0.2308 0.3012 0.3041 0.0056  0.0253  0.0215  167 SER   A O   
3740 C  CB  A SER   A 167 ? 0.1716 0.3385 0.2183 -0.0186 -0.0129 -0.0031 167 SER   A CB  
3741 C  CB  B SER   A 167 ? 0.2154 0.2930 0.2480 -0.0072 0.0202  0.0108  167 SER   A CB  
3742 O  OG  A SER   A 167 ? 0.1814 0.3477 0.2099 -0.0200 -0.0022 -0.0109 167 SER   A OG  
3743 O  OG  B SER   A 167 ? 0.2223 0.2928 0.2373 -0.0080 0.0290  0.0096  167 SER   A OG  
3754 N  N   A PHE   A 168 ? 0.1603 0.3005 0.2135 -0.0058 -0.0071 -0.0034 168 PHE   A N   
3755 N  N   B PHE   A 168 ? 0.1878 0.2835 0.2465 0.0026  0.0330  0.0199  168 PHE   A N   
3756 C  CA  A PHE   A 168 ? 0.1633 0.2946 0.2377 -0.0123 0.0189  -0.0171 168 PHE   A CA  
3757 C  CA  B PHE   A 168 ? 0.1768 0.2794 0.2211 0.0030  0.0529  0.0187  168 PHE   A CA  
3758 C  C   A PHE   A 168 ? 0.1884 0.3095 0.2913 -0.0174 0.0456  -0.0239 168 PHE   A C   
3759 C  C   B PHE   A 168 ? 0.1805 0.2863 0.2267 -0.0080 0.0660  0.0155  168 PHE   A C   
3760 O  O   A PHE   A 168 ? 0.1943 0.3143 0.3259 -0.0297 0.0558  -0.0118 168 PHE   A O   
3761 O  O   B PHE   A 168 ? 0.1638 0.2849 0.2136 -0.0067 0.0750  0.0165  168 PHE   A O   
3762 C  CB  A PHE   A 168 ? 0.1640 0.2801 0.2210 -0.0169 0.0052  -0.0175 168 PHE   A CB  
3763 C  CB  B PHE   A 168 ? 0.1748 0.2749 0.2176 0.0021  0.0465  0.0240  168 PHE   A CB  
3764 C  CG  A PHE   A 168 ? 0.1654 0.2666 0.2082 -0.0242 -0.0033 -0.0194 168 PHE   A CG  
3765 C  CG  B PHE   A 168 ? 0.1845 0.2703 0.2123 0.0031  0.0314  0.0340  168 PHE   A CG  
3766 C  CD1 A PHE   A 168 ? 0.1655 0.2667 0.2141 -0.0251 -0.0114 -0.0017 168 PHE   A CD1 
3767 C  CD1 B PHE   A 168 ? 0.1867 0.2712 0.2110 0.0041  0.0260  0.0432  168 PHE   A CD1 
3768 C  CD2 A PHE   A 168 ? 0.1635 0.2580 0.1872 -0.0226 0.0106  -0.0253 168 PHE   A CD2 
3769 C  CD2 B PHE   A 168 ? 0.1907 0.2666 0.2107 0.0046  0.0254  0.0375  168 PHE   A CD2 
3770 C  CE1 A PHE   A 168 ? 0.1587 0.2643 0.2043 -0.0267 -0.0037 0.0013  168 PHE   A CE1 
3771 C  CE1 B PHE   A 168 ? 0.1885 0.2708 0.2106 0.0031  0.0246  0.0478  168 PHE   A CE1 
3772 C  CE2 A PHE   A 168 ? 0.1650 0.2523 0.1896 -0.0270 0.0175  -0.0087 168 PHE   A CE2 
3773 C  CE2 B PHE   A 168 ? 0.1931 0.2655 0.2123 0.0019  0.0215  0.0471  168 PHE   A CE2 
3774 C  CZ  A PHE   A 168 ? 0.1624 0.2586 0.1970 -0.0303 0.0075  -0.0002 168 PHE   A CZ  
3775 C  CZ  B PHE   A 168 ? 0.1933 0.2683 0.2116 -0.0007 0.0219  0.0480  168 PHE   A CZ  
3794 N  N   A LEU   A 169 ? 0.2217 0.3189 0.3314 -0.0130 0.0474  -0.0371 169 LEU   A N   
3795 N  N   B LEU   A 169 ? 0.2104 0.2989 0.2594 -0.0127 0.0554  0.0102  169 LEU   A N   
3796 C  CA  A LEU   A 169 ? 0.2609 0.3356 0.3873 -0.0016 0.0309  -0.0470 169 LEU   A CA  
3797 C  CA  B LEU   A 169 ? 0.2421 0.3123 0.2974 -0.0142 0.0256  0.0018  169 LEU   A CA  
3798 C  C   A LEU   A 169 ? 0.2627 0.3388 0.4140 0.0019  0.0350  -0.0381 169 LEU   A C   
3799 C  C   B LEU   A 169 ? 0.2564 0.3213 0.3068 -0.0130 0.0120  -0.0158 169 LEU   A C   
3800 O  O   A LEU   A 169 ? 0.2696 0.3448 0.4244 0.0046  0.0326  -0.0323 169 LEU   A O   
3801 O  O   B LEU   A 169 ? 0.2603 0.3271 0.3142 -0.0129 -0.0085 -0.0246 169 LEU   A O   
3802 C  CB  A LEU   A 169 ? 0.2926 0.3502 0.3989 0.0033  0.0196  -0.0532 169 LEU   A CB  
3803 C  CB  B LEU   A 169 ? 0.2564 0.3157 0.3236 -0.0173 0.0134  0.0092  169 LEU   A CB  
3804 C  CG  A LEU   A 169 ? 0.3171 0.3595 0.4091 0.0038  0.0112  -0.0675 169 LEU   A CG  
3805 C  CG  B LEU   A 169 ? 0.2696 0.3208 0.3415 -0.0213 0.0015  0.0156  169 LEU   A CG  
3806 C  CD1 A LEU   A 169 ? 0.3255 0.3637 0.4162 0.0070  0.0088  -0.0700 169 LEU   A CD1 
3807 C  CD1 B LEU   A 169 ? 0.2726 0.3223 0.3471 -0.0229 -0.0016 0.0189  169 LEU   A CD1 
3808 C  CD2 A LEU   A 169 ? 0.3241 0.3619 0.4039 0.0011  0.0119  -0.0754 169 LEU   A CD2 
3809 C  CD2 B LEU   A 169 ? 0.2701 0.3221 0.3528 -0.0228 -0.0005 0.0154  169 LEU   A CD2 
3810 O  OXT A LEU   A 169 ? 0.2446 0.3373 0.4166 0.0037  0.0529  -0.0460 169 LEU   A OXT 
3811 O  OXT B LEU   A 169 ? 0.2650 0.3268 0.3143 -0.0151 0.0142  -0.0196 169 LEU   A OXT 
3834 N  N   A SER   B 1   ? 0.3567 0.3466 0.3716 -0.1245 -0.0921 0.0351  1   SER   B N   
3835 N  N   B SER   B 1   ? 0.3428 0.3165 0.3211 -0.0812 -0.0336 0.0110  1   SER   B N   
3836 C  CA  A SER   B 1   ? 0.3428 0.3482 0.3720 -0.1324 -0.0992 0.0336  1   SER   B CA  
3837 C  CA  B SER   B 1   ? 0.3372 0.3203 0.3269 -0.0842 -0.0355 0.0101  1   SER   B CA  
3838 C  C   A SER   B 1   ? 0.3094 0.3458 0.3477 -0.1371 -0.1068 0.0594  1   SER   B C   
3839 C  C   B SER   B 1   ? 0.3227 0.3254 0.3248 -0.0827 -0.0404 0.0311  1   SER   B C   
3840 O  O   A SER   B 1   ? 0.3185 0.3446 0.3183 -0.1307 -0.1037 0.0547  1   SER   B O   
3841 O  O   B SER   B 1   ? 0.3263 0.3246 0.3082 -0.0794 -0.0366 0.0283  1   SER   B O   
3842 C  CB  A SER   B 1   ? 0.3618 0.3504 0.3947 -0.1300 -0.0845 0.0154  1   SER   B CB  
3843 C  CB  B SER   B 1   ? 0.3451 0.3166 0.3311 -0.0856 -0.0261 -0.0093 1   SER   B CB  
3844 O  OG  A SER   B 1   ? 0.3795 0.3608 0.4413 -0.1246 -0.0742 0.0120  1   SER   B OG  
3845 O  OG  B SER   B 1   ? 0.3522 0.3167 0.3499 -0.0864 -0.0237 -0.0209 1   SER   B OG  
3860 N  N   A MET   B 2   ? 0.2807 0.3490 0.3404 -0.1306 -0.1060 0.1058  2   MET   B N   
3861 N  N   B MET   B 2   ? 0.3093 0.3317 0.3288 -0.0779 -0.0444 0.0625  2   MET   B N   
3862 C  CA  A MET   B 2   ? 0.2664 0.3538 0.3668 -0.1068 -0.0967 0.1235  2   MET   B CA  
3863 C  CA  B MET   B 2   ? 0.2987 0.3365 0.3404 -0.0659 -0.0446 0.0807  2   MET   B CA  
3864 C  C   A MET   B 2   ? 0.2283 0.3358 0.3369 -0.0887 -0.1059 0.1420  2   MET   B C   
3865 C  C   B MET   B 2   ? 0.2749 0.3242 0.3142 -0.0624 -0.0405 0.0911  2   MET   B C   
3866 O  O   A MET   B 2   ? 0.2186 0.3486 0.3311 -0.0692 -0.1173 0.1528  2   MET   B O   
3867 O  O   B MET   B 2   ? 0.2755 0.3310 0.3137 -0.0575 -0.0334 0.0906  2   MET   B O   
3868 C  CB  A MET   B 2   ? 0.2991 0.3868 0.4541 -0.0843 -0.0755 0.0972  2   MET   B CB  
3869 C  CB  B MET   B 2   ? 0.3153 0.3569 0.3889 -0.0512 -0.0482 0.0772  2   MET   B CB  
3870 C  CG  A MET   B 2   ? 0.3324 0.4175 0.5369 -0.0607 -0.0451 0.0784  2   MET   B CG  
3871 C  CG  B MET   B 2   ? 0.3311 0.3761 0.4309 -0.0375 -0.0455 0.0811  2   MET   B CG  
3872 S  SD  A MET   B 2   ? 0.3639 0.4479 0.6151 -0.0399 -0.0219 0.0618  2   MET   B SD  
3873 S  SD  B MET   B 2   ? 0.3467 0.3972 0.4671 -0.0240 -0.0447 0.0827  2   MET   B SD  
3874 C  CE  A MET   B 2   ? 0.3676 0.4521 0.6137 -0.0372 -0.0166 0.0643  2   MET   B CE  
3875 C  CE  B MET   B 2   ? 0.3486 0.4009 0.4708 -0.0231 -0.0457 0.0805  2   MET   B CE  
3894 N  N   A VAL   B 3   ? 0.2069 0.3009 0.3198 -0.0921 -0.0936 0.1472  3   VAL   B N   
3895 N  N   B VAL   B 3   ? 0.2515 0.3033 0.2950 -0.0649 -0.0432 0.0986  3   VAL   B N   
3896 C  CA  A VAL   B 3   ? 0.2051 0.2704 0.3059 -0.0798 -0.0864 0.1318  3   VAL   B CA  
3897 C  CA  B VAL   B 3   ? 0.2317 0.2815 0.2755 -0.0616 -0.0479 0.0956  3   VAL   B CA  
3898 C  C   A VAL   B 3   ? 0.1966 0.2575 0.2640 -0.0688 -0.0755 0.1163  3   VAL   B C   
3899 C  C   B VAL   B 3   ? 0.2081 0.2654 0.2423 -0.0597 -0.0525 0.0963  3   VAL   B C   
3900 O  O   A VAL   B 3   ? 0.1931 0.2597 0.2652 -0.0703 -0.0726 0.1228  3   VAL   B O   
3901 O  O   B VAL   B 3   ? 0.2053 0.2711 0.2317 -0.0500 -0.0513 0.1026  3   VAL   B O   
3902 C  CB  A VAL   B 3   ? 0.2185 0.2648 0.3635 -0.0775 -0.0783 0.1128  3   VAL   B CB  
3903 C  CB  B VAL   B 3   ? 0.2383 0.2786 0.3037 -0.0608 -0.0452 0.0867  3   VAL   B CB  
3904 C  CG1 A VAL   B 3   ? 0.2275 0.2609 0.3856 -0.0800 -0.0774 0.1065  3   VAL   B CG1 
3905 C  CG1 B VAL   B 3   ? 0.2421 0.2765 0.3128 -0.0614 -0.0453 0.0814  3   VAL   B CG1 
3906 C  CG2 A VAL   B 3   ? 0.2167 0.2639 0.3813 -0.0736 -0.0702 0.1258  3   VAL   B CG2 
3907 C  CG2 B VAL   B 3   ? 0.2385 0.2778 0.3117 -0.0599 -0.0443 0.0923  3   VAL   B CG2 
3926 N  N   . ASN   B 4   ? 0.1874 0.2423 0.2343 -0.0675 -0.0625 0.0909  4   ASN   B N   
3927 C  CA  . ASN   B 4   ? 0.1833 0.2367 0.1863 -0.0647 -0.0517 0.0511  4   ASN   B CA  
3928 C  C   . ASN   B 4   ? 0.1882 0.2492 0.1676 -0.0586 -0.0382 0.0360  4   ASN   B C   
3929 O  O   . ASN   B 4   ? 0.1841 0.2444 0.1908 -0.0530 -0.0265 0.0209  4   ASN   B O   
3930 C  CB  . ASN   B 4   ? 0.1797 0.2246 0.1770 -0.0598 -0.0479 0.0420  4   ASN   B CB  
3931 C  CG  . ASN   B 4   ? 0.1813 0.2042 0.1670 -0.0553 -0.0470 0.0372  4   ASN   B CG  
3932 O  OD1 . ASN   B 4   ? 0.1809 0.1900 0.1654 -0.0502 -0.0479 0.0320  4   ASN   B OD1 
3933 N  ND2 . ASN   B 4   ? 0.2079 0.2086 0.1883 -0.0298 -0.0358 0.0371  4   ASN   B ND2 
3941 N  N   . SER   B 5   ? 0.1958 0.2693 0.1768 -0.0596 -0.0384 0.0341  5   SER   B N   
3942 C  CA  . SER   B 5   ? 0.2122 0.3009 0.1992 -0.0435 -0.0243 0.0380  5   SER   B CA  
3943 C  C   . SER   B 5   ? 0.2343 0.3042 0.2427 -0.0546 0.0046  0.0383  5   SER   B C   
3944 O  O   . SER   B 5   ? 0.2474 0.3024 0.3437 -0.0506 0.0539  0.0411  5   SER   B O   
3945 C  CB  . SER   B 5   ? 0.2211 0.3180 0.2243 -0.0283 -0.0199 0.0489  5   SER   B CB  
3946 O  OG  . SER   B 5   ? 0.2439 0.3419 0.2840 -0.0138 -0.0071 0.0544  5   SER   B OG  
3952 N  N   . PHE   B 6   ? 0.2566 0.3113 0.2120 -0.0598 0.0280  0.0270  6   PHE   B N   
3953 C  CA  . PHE   B 6   ? 0.2755 0.3095 0.1890 -0.0805 0.0395  0.0010  6   PHE   B CA  
3954 C  C   . PHE   B 6   ? 0.3303 0.3363 0.2481 -0.0929 0.0699  -0.0253 6   PHE   B C   
3955 O  O   . PHE   B 6   ? 0.3472 0.3620 0.2767 -0.0878 0.0463  -0.0311 6   PHE   B O   
3956 C  CB  . PHE   B 6   ? 0.2474 0.2866 0.1751 -0.0719 0.0197  0.0016  6   PHE   B CB  
3957 C  CG  . PHE   B 6   ? 0.2169 0.2572 0.1534 -0.0637 0.0116  0.0004  6   PHE   B CG  
3958 C  CD1 . PHE   B 6   ? 0.2188 0.2220 0.1350 -0.0577 0.0039  -0.0026 6   PHE   B CD1 
3959 C  CD2 . PHE   B 6   ? 0.1888 0.2540 0.1664 -0.0530 0.0083  0.0299  6   PHE   B CD2 
3960 C  CE1 . PHE   B 6   ? 0.2124 0.2069 0.1573 -0.0418 -0.0004 -0.0050 6   PHE   B CE1 
3961 C  CE2 . PHE   B 6   ? 0.1875 0.2374 0.1991 -0.0390 0.0120  0.0303  6   PHE   B CE2 
3962 C  CZ  . PHE   B 6   ? 0.1965 0.2163 0.1730 -0.0339 0.0053  0.0070  6   PHE   B CZ  
3972 N  N   A SER   B 7   ? 0.3532 0.3262 0.2608 -0.1079 0.1139  -0.0451 7   SER   B N   
3973 N  N   B SER   B 7   ? 0.3430 0.3277 0.2688 -0.0988 0.0859  -0.0421 7   SER   B N   
3974 C  CA  A SER   B 7   ? 0.3816 0.3356 0.3146 -0.1000 0.1288  -0.0577 7   SER   B CA  
3975 C  CA  B SER   B 7   ? 0.3567 0.3272 0.3062 -0.0933 0.0900  -0.0537 7   SER   B CA  
3976 C  C   A SER   B 7   ? 0.3770 0.3248 0.3159 -0.0975 0.1495  -0.0718 7   SER   B C   
3977 C  C   B SER   B 7   ? 0.3551 0.3182 0.3159 -0.0910 0.1011  -0.0617 7   SER   B C   
3978 O  O   A SER   B 7   ? 0.3807 0.3228 0.3401 -0.1032 0.1508  -0.0706 7   SER   B O   
3979 O  O   B SER   B 7   ? 0.3577 0.3181 0.3317 -0.0938 0.0991  -0.0608 7   SER   B O   
3980 C  CB  A SER   B 7   ? 0.3994 0.3487 0.3604 -0.0966 0.1322  -0.0520 7   SER   B CB  
3981 C  CB  B SER   B 7   ? 0.3639 0.3310 0.3307 -0.0914 0.0872  -0.0528 7   SER   B CB  
3982 O  OG  A SER   B 7   ? 0.4087 0.3592 0.4021 -0.0952 0.1321  -0.0411 7   SER   B OG  
3983 O  OG  B SER   B 7   ? 0.3671 0.3333 0.3513 -0.0905 0.0837  -0.0462 7   SER   B OG  
3994 N  N   A GLY   B 8   ? 0.3730 0.3171 0.3227 -0.0819 0.1597  -0.0802 8   GLY   B N   
3995 N  N   B GLY   B 8   ? 0.3530 0.3091 0.3205 -0.0820 0.1107  -0.0682 8   GLY   B N   
3996 C  CA  A GLY   B 8   ? 0.3555 0.3018 0.3178 -0.0786 0.1618  -0.0877 8   GLY   B CA  
3997 C  CA  B GLY   B 8   ? 0.3430 0.2960 0.3164 -0.0791 0.1193  -0.0749 8   GLY   B CA  
3998 C  C   A GLY   B 8   ? 0.3347 0.2830 0.3158 -0.0787 0.1527  -0.0839 8   GLY   B C   
3999 C  C   B GLY   B 8   ? 0.3299 0.2803 0.3116 -0.0781 0.1252  -0.0773 8   GLY   B C   
4000 O  O   A GLY   B 8   ? 0.3453 0.2937 0.3522 -0.0661 0.1513  -0.0953 8   GLY   B O   
4001 O  O   B GLY   B 8   ? 0.3370 0.2861 0.3327 -0.0720 0.1243  -0.0805 8   GLY   B O   
4008 N  N   . TYR   B 9   ? 0.3135 0.2625 0.2903 -0.0764 0.1227  -0.0848 9   TYR   B N   
4009 C  CA  . TYR   B 9   ? 0.2791 0.2237 0.2378 -0.0668 0.0811  -0.0680 9   TYR   B CA  
4010 C  C   . TYR   B 9   ? 0.2774 0.2192 0.2314 -0.0580 0.0460  -0.0486 9   TYR   B C   
4011 O  O   . TYR   B 9   ? 0.2929 0.2394 0.2748 -0.0623 0.0526  -0.0287 9   TYR   B O   
4012 C  CB  . TYR   B 9   ? 0.2675 0.2052 0.2312 -0.0564 0.0616  -0.0612 9   TYR   B CB  
4013 C  CG  . TYR   B 9   ? 0.2541 0.1936 0.2298 -0.0593 0.0590  -0.0581 9   TYR   B CG  
4014 C  CD1 . TYR   B 9   ? 0.2546 0.1978 0.2476 -0.0718 0.0671  -0.0461 9   TYR   B CD1 
4015 C  CD2 . TYR   B 9   ? 0.2400 0.1920 0.2139 -0.0519 0.0549  -0.0597 9   TYR   B CD2 
4016 C  CE1 . TYR   B 9   ? 0.2491 0.2048 0.2525 -0.0748 0.0677  -0.0568 9   TYR   B CE1 
4017 C  CE2 . TYR   B 9   ? 0.2429 0.1944 0.2403 -0.0447 0.0504  -0.0580 9   TYR   B CE2 
4018 C  CZ  . TYR   B 9   ? 0.2450 0.2086 0.2516 -0.0632 0.0556  -0.0692 9   TYR   B CZ  
4019 O  OH  . TYR   B 9   ? 0.2466 0.2231 0.2645 -0.0742 0.0587  -0.0820 9   TYR   B OH  
4030 N  N   . LEU   B 10  ? 0.2560 0.1964 0.2069 -0.0526 0.0314  -0.0395 10  LEU   B N   
4031 C  CA  . LEU   B 10  ? 0.2650 0.1943 0.2152 -0.0627 -0.0028 -0.0365 10  LEU   B CA  
4032 C  C   . LEU   B 10  ? 0.2521 0.1993 0.2232 -0.0607 -0.0116 -0.0333 10  LEU   B C   
4033 O  O   . LEU   B 10  ? 0.2360 0.1973 0.2212 -0.0540 -0.0002 -0.0282 10  LEU   B O   
4034 C  CB  . LEU   B 10  ? 0.2963 0.1908 0.2392 -0.0716 -0.0171 -0.0090 10  LEU   B CB  
4035 C  CG  . LEU   B 10  ? 0.3237 0.1993 0.2708 -0.0664 -0.0536 0.0047  10  LEU   B CG  
4036 C  CD1 . LEU   B 10  ? 0.3399 0.2065 0.3052 -0.0654 -0.0553 -0.0026 10  LEU   B CD1 
4037 C  CD2 . LEU   B 10  ? 0.3312 0.2124 0.2899 -0.0662 -0.0588 0.0243  10  LEU   B CD2 
4049 N  N   . LYS   B 11  ? 0.2665 0.2266 0.2234 -0.0577 -0.0205 -0.0293 11  LYS   B N   
4050 C  CA  . LYS   B 11  ? 0.2960 0.2541 0.2598 -0.0464 -0.0184 -0.0357 11  LYS   B CA  
4051 C  C   . LYS   B 11  ? 0.2805 0.2256 0.2550 -0.0663 -0.0025 -0.0479 11  LYS   B C   
4052 O  O   . LYS   B 11  ? 0.2996 0.2418 0.2860 -0.0875 -0.0040 -0.0809 11  LYS   B O   
4053 C  CB  . LYS   B 11  ? 0.3374 0.3085 0.3221 -0.0189 -0.0298 -0.0367 11  LYS   B CB  
4054 C  CG  . LYS   B 11  ? 0.3731 0.3425 0.3904 -0.0036 -0.0369 -0.0380 11  LYS   B CG  
4055 C  CD  . LYS   B 11  ? 0.4019 0.3618 0.4511 -0.0004 -0.0417 -0.0448 11  LYS   B CD  
4056 C  CE  . LYS   B 11  ? 0.4237 0.3740 0.4999 -0.0030 -0.0460 -0.0515 11  LYS   B CE  
4057 N  NZ  . LYS   B 11  ? 0.4349 0.3829 0.5248 -0.0061 -0.0506 -0.0531 11  LYS   B NZ  
4071 N  N   . LEU   B 12  ? 0.2390 0.1999 0.2315 -0.0530 -0.0011 -0.0460 12  LEU   B N   
4072 C  CA  . LEU   B 12  ? 0.2214 0.1764 0.2487 -0.0459 -0.0008 -0.0398 12  LEU   B CA  
4073 C  C   . LEU   B 12  ? 0.2057 0.1803 0.2699 -0.0427 -0.0316 -0.0389 12  LEU   B C   
4074 O  O   . LEU   B 12  ? 0.2049 0.1808 0.3098 -0.0477 -0.0455 -0.0338 12  LEU   B O   
4075 C  CB  . LEU   B 12  ? 0.2253 0.1577 0.2473 -0.0354 0.0065  -0.0337 12  LEU   B CB  
4076 C  CG  . LEU   B 12  ? 0.2274 0.1507 0.2577 -0.0364 0.0058  -0.0272 12  LEU   B CG  
4077 C  CD1 . LEU   B 12  ? 0.2310 0.1597 0.2439 -0.0192 -0.0026 -0.0084 12  LEU   B CD1 
4078 C  CD2 . LEU   B 12  ? 0.2385 0.1544 0.2812 -0.0354 0.0072  -0.0377 12  LEU   B CD2 
4090 N  N   . THR   B 13  ? 0.1944 0.1858 0.2675 -0.0461 -0.0323 -0.0426 13  THR   B N   
4091 C  CA  . THR   B 13  ? 0.2009 0.1961 0.2507 -0.0551 -0.0450 -0.0268 13  THR   B CA  
4092 C  C   . THR   B 13  ? 0.2502 0.2181 0.2734 -0.0680 -0.0587 -0.0215 13  THR   B C   
4093 O  O   . THR   B 13  ? 0.2721 0.2204 0.2850 -0.0702 -0.0259 -0.0265 13  THR   B O   
4094 C  CB  . THR   B 13  ? 0.1904 0.1953 0.2487 -0.0512 -0.0398 -0.0112 13  THR   B CB  
4095 O  OG1 . THR   B 13  ? 0.1784 0.1810 0.2559 -0.0480 -0.0273 -0.0138 13  THR   B OG1 
4096 C  CG2 . THR   B 13  ? 0.2003 0.1991 0.2660 -0.0404 -0.0200 -0.0018 13  THR   B CG2 
4104 N  N   A ASP   B 14  ? 0.2661 0.2321 0.2891 -0.0774 -0.0872 -0.0060 14  ASP   B N   
4105 N  N   B ASP   B 14  ? 0.2608 0.2290 0.2851 -0.0679 -0.0731 -0.0070 14  ASP   B N   
4106 C  CA  A ASP   B 14  ? 0.2836 0.2494 0.3182 -0.0807 -0.0987 0.0095  14  ASP   B CA  
4107 C  CA  B ASP   B 14  ? 0.2722 0.2405 0.3034 -0.0655 -0.0788 0.0047  14  ASP   B CA  
4108 C  C   A ASP   B 14  ? 0.2705 0.2288 0.2800 -0.0847 -0.0798 0.0174  14  ASP   B C   
4109 C  C   B ASP   B 14  ? 0.2579 0.2223 0.2721 -0.0664 -0.0762 0.0098  14  ASP   B C   
4110 O  O   A ASP   B 14  ? 0.2985 0.2422 0.2725 -0.0856 -0.0723 0.0384  14  ASP   B O   
4111 O  O   B ASP   B 14  ? 0.2712 0.2266 0.2664 -0.0563 -0.0772 0.0180  14  ASP   B O   
4112 C  CB  A ASP   B 14  ? 0.3080 0.2857 0.3955 -0.0765 -0.1139 0.0142  14  ASP   B CB  
4113 C  CB  B ASP   B 14  ? 0.2941 0.2686 0.3571 -0.0607 -0.0806 0.0092  14  ASP   B CB  
4114 C  CG  A ASP   B 14  ? 0.3340 0.3162 0.4629 -0.0695 -0.1114 0.0032  14  ASP   B CG  
4115 C  CG  B ASP   B 14  ? 0.3157 0.2930 0.4021 -0.0545 -0.0771 0.0040  14  ASP   B CG  
4116 O  OD1 A ASP   B 14  ? 0.3501 0.3256 0.4778 -0.0712 -0.1114 -0.0089 14  ASP   B OD1 
4117 O  OD1 B ASP   B 14  ? 0.3264 0.3048 0.4123 -0.0538 -0.0727 -0.0000 14  ASP   B OD1 
4118 O  OD2 A ASP   B 14  ? 0.3375 0.3301 0.4974 -0.0672 -0.1071 0.0042  14  ASP   B OD2 
4119 O  OD2 B ASP   B 14  ? 0.3203 0.3003 0.4190 -0.0544 -0.0800 0.0021  14  ASP   B OD2 
4128 N  N   . ASN   B 15  ? 0.2339 0.2011 0.2547 -0.0663 -0.0739 0.0135  15  ASN   B N   
4129 C  CA  . ASN   B 15  ? 0.1882 0.1700 0.2352 -0.0426 -0.0505 0.0009  15  ASN   B CA  
4130 C  C   . ASN   B 15  ? 0.1666 0.1569 0.2116 -0.0244 -0.0381 -0.0072 15  ASN   B C   
4131 O  O   . ASN   B 15  ? 0.1643 0.1553 0.2280 -0.0203 -0.0446 -0.0229 15  ASN   B O   
4132 C  CB  . ASN   B 15  ? 0.1838 0.1686 0.2577 -0.0178 -0.0455 -0.0032 15  ASN   B CB  
4133 C  CG  . ASN   B 15  ? 0.1687 0.1670 0.2468 -0.0184 -0.0245 0.0015  15  ASN   B CG  
4134 O  OD1 . ASN   B 15  ? 0.1708 0.2007 0.2784 -0.0408 -0.0340 0.0021  15  ASN   B OD1 
4135 N  ND2 . ASN   B 15  ? 0.1672 0.1379 0.2403 -0.0087 0.0047  -0.0091 15  ASN   B ND2 
4143 N  N   . VAL   B 16  ? 0.1629 0.1565 0.2127 -0.0303 -0.0496 -0.0050 16  VAL   B N   
4144 C  CA  . VAL   B 16  ? 0.1650 0.1581 0.2001 -0.0276 -0.0242 -0.0301 16  VAL   B CA  
4145 C  C   . VAL   B 16  ? 0.1623 0.1648 0.1979 -0.0305 -0.0280 -0.0210 16  VAL   B C   
4146 O  O   . VAL   B 16  ? 0.1659 0.1783 0.2210 -0.0216 -0.0200 -0.0336 16  VAL   B O   
4147 C  CB  . VAL   B 16  ? 0.1698 0.1478 0.2044 -0.0095 -0.0120 -0.0317 16  VAL   B CB  
4148 C  CG1 . VAL   B 16  ? 0.1767 0.1518 0.2170 0.0005  -0.0116 -0.0207 16  VAL   B CG1 
4149 C  CG2 . VAL   B 16  ? 0.1735 0.1490 0.2337 -0.0035 -0.0136 -0.0233 16  VAL   B CG2 
4159 N  N   . TYR   B 17  ? 0.1653 0.1796 0.1946 -0.0262 -0.0142 -0.0271 17  TYR   B N   
4160 C  CA  . TYR   B 17  ? 0.1722 0.1968 0.1824 -0.0279 -0.0183 -0.0011 17  TYR   B CA  
4161 C  C   . TYR   B 17  ? 0.1697 0.1656 0.1783 -0.0303 -0.0104 -0.0235 17  TYR   B C   
4162 O  O   . TYR   B 17  ? 0.1705 0.1744 0.1977 -0.0328 -0.0178 -0.0439 17  TYR   B O   
4163 C  CB  . TYR   B 17  ? 0.2063 0.2468 0.2385 -0.0184 -0.0234 0.0340  17  TYR   B CB  
4164 C  CG  . TYR   B 17  ? 0.2426 0.3007 0.2871 -0.0096 -0.0402 0.0501  17  TYR   B CG  
4165 C  CD1 . TYR   B 17  ? 0.2661 0.3209 0.3160 -0.0039 -0.0558 0.0613  17  TYR   B CD1 
4166 C  CD2 . TYR   B 17  ? 0.2715 0.3319 0.3174 -0.0030 -0.0550 0.0508  17  TYR   B CD2 
4167 C  CE1 . TYR   B 17  ? 0.2874 0.3495 0.3381 0.0060  -0.0697 0.0525  17  TYR   B CE1 
4168 C  CE2 . TYR   B 17  ? 0.2912 0.3557 0.3458 0.0107  -0.0700 0.0581  17  TYR   B CE2 
4169 C  CZ  . TYR   B 17  ? 0.3010 0.3708 0.3572 0.0147  -0.0760 0.0520  17  TYR   B CZ  
4170 O  OH  . TYR   B 17  ? 0.3186 0.3905 0.3774 0.0229  -0.0804 0.0511  17  TYR   B OH  
4180 N  N   . ILE   B 18  ? 0.1780 0.1676 0.1753 -0.0291 -0.0062 -0.0245 18  ILE   B N   
4181 C  CA  . ILE   B 18  ? 0.1796 0.1628 0.1879 -0.0341 0.0054  -0.0242 18  ILE   B CA  
4182 C  C   . ILE   B 18  ? 0.1913 0.1652 0.1999 -0.0452 0.0003  -0.0405 18  ILE   B C   
4183 O  O   . ILE   B 18  ? 0.2089 0.1860 0.1964 -0.0439 0.0183  -0.0489 18  ILE   B O   
4184 C  CB  . ILE   B 18  ? 0.1854 0.1601 0.1984 -0.0372 0.0028  -0.0262 18  ILE   B CB  
4185 C  CG1 . ILE   B 18  ? 0.1850 0.1653 0.2091 -0.0404 0.0048  -0.0219 18  ILE   B CG1 
4186 C  CG2 . ILE   B 18  ? 0.1930 0.1698 0.1853 -0.0395 -0.0076 -0.0187 18  ILE   B CG2 
4187 C  CD1 . ILE   B 18  ? 0.1958 0.1877 0.2453 -0.0343 -0.0143 0.0094  18  ILE   B CD1 
4199 N  N   . LYS   B 19  ? 0.1943 0.1691 0.2092 -0.0247 0.0340  -0.0466 19  LYS   B N   
4200 C  CA  . LYS   B 19  ? 0.2031 0.1754 0.2318 -0.0311 0.0351  -0.0550 19  LYS   B CA  
4201 C  C   . LYS   B 19  ? 0.1874 0.1692 0.2448 -0.0246 0.0390  -0.0689 19  LYS   B C   
4202 O  O   . LYS   B 19  ? 0.1830 0.1713 0.2274 -0.0165 0.0319  -0.0514 19  LYS   B O   
4203 C  CB  . LYS   B 19  ? 0.2284 0.1957 0.2433 -0.0421 0.0522  -0.0437 19  LYS   B CB  
4204 C  CG  . LYS   B 19  ? 0.2581 0.2232 0.2876 -0.0462 0.0783  -0.0476 19  LYS   B CG  
4205 C  CD  . LYS   B 19  ? 0.2915 0.2547 0.3159 -0.0490 0.1013  -0.0455 19  LYS   B CD  
4206 C  CE  . LYS   B 19  ? 0.3223 0.2837 0.3585 -0.0517 0.0976  -0.0464 19  LYS   B CE  
4207 N  NZ  . LYS   B 19  ? 0.3402 0.3027 0.3784 -0.0582 0.0913  -0.0441 19  LYS   B NZ  
4221 N  N   . ASN   B 20  ? 0.1852 0.1787 0.2731 -0.0176 0.0445  -0.0749 20  ASN   B N   
4222 C  CA  . ASN   B 20  ? 0.1948 0.1938 0.2937 -0.0125 0.0527  -0.0851 20  ASN   B CA  
4223 C  C   . ASN   B 20  ? 0.1902 0.2164 0.2992 -0.0148 0.0601  -0.0978 20  ASN   B C   
4224 O  O   . ASN   B 20  ? 0.2106 0.2529 0.3282 -0.0303 0.0473  -0.0964 20  ASN   B O   
4225 C  CB  . ASN   B 20  ? 0.2294 0.1895 0.3360 0.0089  0.0401  -0.0928 20  ASN   B CB  
4226 C  CG  . ASN   B 20  ? 0.2568 0.2015 0.3706 0.0424  0.0346  -0.0923 20  ASN   B CG  
4227 O  OD1 . ASN   B 20  ? 0.2871 0.2302 0.3924 0.0567  0.0259  -0.0962 20  ASN   B OD1 
4228 N  ND2 . ASN   B 20  ? 0.2474 0.1997 0.3672 0.0432  0.0260  -0.0838 20  ASN   B ND2 
4235 N  N   . ALA   B 21  ? 0.1875 0.2034 0.2850 -0.0187 0.0638  -0.0873 21  ALA   B N   
4236 C  CA  . ALA   B 21  ? 0.1962 0.2048 0.3003 -0.0241 0.0362  -0.0666 21  ALA   B CA  
4237 C  C   . ALA   B 21  ? 0.1982 0.1747 0.2843 -0.0201 0.0483  -0.0504 21  ALA   B C   
4238 O  O   . ALA   B 21  ? 0.2067 0.1668 0.2804 -0.0282 0.0516  -0.0351 21  ALA   B O   
4239 C  CB  . ALA   B 21  ? 0.2105 0.2329 0.3083 -0.0365 0.0382  -0.0493 21  ALA   B CB  
4245 N  N   . ASP   B 22  ? 0.1877 0.1678 0.2836 -0.0228 0.0311  -0.0383 22  ASP   B N   
4246 C  CA  . ASP   B 22  ? 0.1823 0.1599 0.2584 -0.0110 0.0239  -0.0239 22  ASP   B CA  
4247 C  C   . ASP   B 22  ? 0.1859 0.1585 0.2105 -0.0138 0.0225  -0.0170 22  ASP   B C   
4248 O  O   . ASP   B 22  ? 0.1870 0.1623 0.2112 -0.0111 0.0151  -0.0105 22  ASP   B O   
4249 C  CB  . ASP   B 22  ? 0.1895 0.1639 0.2945 -0.0059 0.0271  -0.0198 22  ASP   B CB  
4250 C  CG  . ASP   B 22  ? 0.1873 0.1873 0.3359 0.0061  0.0068  -0.0138 22  ASP   B CG  
4251 O  OD1 . ASP   B 22  ? 0.1970 0.1790 0.3376 0.0081  -0.0117 -0.0045 22  ASP   B OD1 
4252 O  OD2 . ASP   B 22  ? 0.1954 0.2149 0.4038 0.0157  -0.0144 -0.0336 22  ASP   B OD2 
4257 N  N   . ILE   B 23  ? 0.1895 0.1431 0.2004 -0.0103 0.0107  0.0013  23  ILE   B N   
4258 C  CA  . ILE   B 23  ? 0.1772 0.1408 0.1892 -0.0109 -0.0000 0.0053  23  ILE   B CA  
4259 C  C   . ILE   B 23  ? 0.1651 0.1427 0.1720 -0.0092 -0.0040 0.0048  23  ILE   B C   
4260 O  O   . ILE   B 23  ? 0.1562 0.1454 0.1667 -0.0074 -0.0037 0.0050  23  ILE   B O   
4261 C  CB  . ILE   B 23  ? 0.1675 0.1452 0.2010 -0.0195 0.0044  0.0067  23  ILE   B CB  
4262 C  CG1 . ILE   B 23  ? 0.1690 0.1556 0.2058 -0.0091 0.0138  0.0144  23  ILE   B CG1 
4263 C  CG2 . ILE   B 23  ? 0.1742 0.1598 0.2012 -0.0130 0.0039  0.0080  23  ILE   B CG2 
4264 C  CD1 . ILE   B 23  ? 0.1798 0.1724 0.2099 -0.0017 0.0060  0.0169  23  ILE   B CD1 
4276 N  N   . VAL   B 24  ? 0.1679 0.1506 0.1851 -0.0095 -0.0029 0.0008  24  VAL   B N   
4277 C  CA  . VAL   B 24  ? 0.1638 0.1533 0.1945 -0.0049 -0.0166 -0.0026 24  VAL   B CA  
4278 C  C   . VAL   B 24  ? 0.1618 0.1519 0.2121 -0.0088 -0.0099 -0.0022 24  VAL   B C   
4279 O  O   . VAL   B 24  ? 0.1602 0.1620 0.2262 -0.0123 -0.0035 0.0131  24  VAL   B O   
4280 C  CB  . VAL   B 24  ? 0.1719 0.1677 0.2054 -0.0015 -0.0188 -0.0041 24  VAL   B CB  
4281 C  CG1 . VAL   B 24  ? 0.1740 0.1686 0.2440 -0.0107 -0.0217 0.0008  24  VAL   B CG1 
4282 C  CG2 . VAL   B 24  ? 0.1872 0.1986 0.2088 0.0054  -0.0205 -0.0049 24  VAL   B CG2 
4292 N  N   . GLU   B 25  ? 0.1780 0.1662 0.2113 -0.0081 0.0078  -0.0037 25  GLU   B N   
4293 C  CA  . GLU   B 25  ? 0.1880 0.1961 0.2257 0.0059  0.0148  0.0021  25  GLU   B CA  
4294 C  C   . GLU   B 25  ? 0.1835 0.1903 0.1972 -0.0073 0.0085  0.0059  25  GLU   B C   
4295 O  O   . GLU   B 25  ? 0.1870 0.2097 0.2202 -0.0070 0.0240  0.0066  25  GLU   B O   
4296 C  CB  . GLU   B 25  ? 0.2282 0.2473 0.3107 0.0253  0.0259  0.0023  25  GLU   B CB  
4297 C  CG  . GLU   B 25  ? 0.2727 0.3145 0.4241 0.0307  0.0297  -0.0065 25  GLU   B CG  
4298 C  CD  . GLU   B 25  ? 0.3079 0.3772 0.5140 0.0258  0.0248  -0.0154 25  GLU   B CD  
4299 O  OE1 . GLU   B 25  ? 0.3365 0.3997 0.5377 0.0306  0.0307  -0.0198 25  GLU   B OE1 
4300 O  OE2 . GLU   B 25  ? 0.3286 0.3953 0.5463 0.0228  0.0147  -0.0227 25  GLU   B OE2 
4307 N  N   A GLU   B 26  ? 0.1851 0.1844 0.1870 -0.0215 0.0119  0.0044  26  GLU   B N   
4308 N  N   B GLU   B 26  ? 0.1809 0.1836 0.1951 -0.0171 0.0045  0.0061  26  GLU   B N   
4309 C  CA  A GLU   B 26  ? 0.1888 0.1960 0.1901 -0.0323 0.0031  0.0036  26  GLU   B CA  
4310 C  CA  B GLU   B 26  ? 0.1770 0.1861 0.2013 -0.0259 -0.0052 0.0063  26  GLU   B CA  
4311 C  C   A GLU   B 26  ? 0.1698 0.1903 0.1744 -0.0257 0.0055  0.0139  26  GLU   B C   
4312 C  C   B GLU   B 26  ? 0.1646 0.1831 0.1824 -0.0232 0.0031  0.0135  26  GLU   B C   
4313 O  O   A GLU   B 26  ? 0.1861 0.2080 0.1852 -0.0208 0.0058  0.0227  26  GLU   B O   
4314 O  O   B GLU   B 26  ? 0.1736 0.1939 0.1882 -0.0211 0.0045  0.0193  26  GLU   B O   
4315 C  CB  A GLU   B 26  ? 0.2249 0.2143 0.2141 -0.0403 0.0162  0.0196  26  GLU   B CB  
4316 C  CB  B GLU   B 26  ? 0.1906 0.1918 0.2293 -0.0313 -0.0121 0.0122  26  GLU   B CB  
4317 C  CG  A GLU   B 26  ? 0.2613 0.2447 0.2710 -0.0420 0.0350  0.0030  26  GLU   B CG  
4318 C  CG  B GLU   B 26  ? 0.2034 0.2042 0.2749 -0.0339 -0.0122 -0.0029 26  GLU   B CG  
4319 C  CD  A GLU   B 26  ? 0.2783 0.2616 0.2766 -0.0566 0.0622  -0.0120 26  GLU   B CD  
4320 C  CD  B GLU   B 26  ? 0.1966 0.2010 0.2811 -0.0445 -0.0150 -0.0226 26  GLU   B CD  
4321 O  OE1 A GLU   B 26  ? 0.2891 0.2522 0.2636 -0.0569 0.1083  -0.0097 26  GLU   B OE1 
4322 O  OE1 B GLU   B 26  ? 0.1874 0.1991 0.3139 -0.0625 -0.0008 -0.0412 26  GLU   B OE1 
4323 O  OE2 A GLU   B 26  ? 0.2744 0.2793 0.3094 -0.0685 0.0683  0.0003  26  GLU   B OE2 
4324 O  OE2 B GLU   B 26  ? 0.1969 0.1949 0.2797 -0.0375 -0.0114 -0.0217 26  GLU   B OE2 
4337 N  N   . ALA   B 27  ? 0.1523 0.1720 0.1731 -0.0203 0.0120  0.0137  27  ALA   B N   
4338 C  CA  . ALA   B 27  ? 0.1560 0.1691 0.1956 -0.0142 0.0069  0.0245  27  ALA   B CA  
4339 C  C   . ALA   B 27  ? 0.1538 0.1832 0.2166 -0.0135 0.0150  0.0419  27  ALA   B C   
4340 O  O   . ALA   B 27  ? 0.1635 0.1919 0.2254 -0.0119 0.0101  0.0457  27  ALA   B O   
4341 C  CB  . ALA   B 27  ? 0.1670 0.1519 0.1951 -0.0141 0.0132  0.0179  27  ALA   B CB  
4348 N  N   . LYS   B 28  ? 0.1463 0.2097 0.2637 -0.0159 0.0212  0.0609  28  LYS   B N   
4349 C  CA  . LYS   B 28  ? 0.1634 0.2429 0.2788 -0.0056 0.0487  0.0999  28  LYS   B CA  
4350 C  C   . LYS   B 28  ? 0.1903 0.2622 0.2493 0.0095  0.0670  0.0904  28  LYS   B C   
4351 O  O   . LYS   B 28  ? 0.2218 0.2790 0.2665 0.0041  0.0617  0.0832  28  LYS   B O   
4352 C  CB  . LYS   B 28  ? 0.1858 0.2839 0.3513 0.0110  0.0705  0.1128  28  LYS   B CB  
4353 C  CG  . LYS   B 28  ? 0.2092 0.3311 0.3928 0.0239  0.0793  0.1224  28  LYS   B CG  
4354 C  CD  . LYS   B 28  ? 0.2588 0.3916 0.4518 0.0332  0.0969  0.1209  28  LYS   B CD  
4355 C  CE  . LYS   B 28  ? 0.3066 0.4381 0.5016 0.0440  0.1059  0.1231  28  LYS   B CE  
4356 N  NZ  . LYS   B 28  ? 0.3251 0.4602 0.5168 0.0522  0.1080  0.1265  28  LYS   B NZ  
4370 N  N   . LYS   B 29  ? 0.2132 0.2845 0.2518 0.0272  0.0745  0.0717  29  LYS   B N   
4371 C  CA  . LYS   B 29  ? 0.2572 0.3195 0.2824 0.0283  0.0616  0.0699  29  LYS   B CA  
4372 C  C   . LYS   B 29  ? 0.2570 0.3193 0.2491 0.0224  0.0453  0.0803  29  LYS   B C   
4373 O  O   . LYS   B 29  ? 0.2809 0.3430 0.2635 0.0335  0.0460  0.0817  29  LYS   B O   
4374 C  CB  . LYS   B 29  ? 0.3078 0.3551 0.3582 0.0263  0.0608  0.0509  29  LYS   B CB  
4375 C  CG  . LYS   B 29  ? 0.3486 0.3830 0.4499 0.0234  0.0593  0.0457  29  LYS   B CG  
4376 C  CD  . LYS   B 29  ? 0.3838 0.4030 0.5202 0.0170  0.0674  0.0396  29  LYS   B CD  
4377 C  CE  . LYS   B 29  ? 0.4136 0.4156 0.5638 0.0108  0.0783  0.0348  29  LYS   B CE  
4378 N  NZ  . LYS   B 29  ? 0.4276 0.4234 0.5974 0.0068  0.0802  0.0307  29  LYS   B NZ  
4392 N  N   . VAL   B 30  ? 0.2278 0.2974 0.2318 0.0013  0.0308  0.0716  30  VAL   B N   
4393 C  CA  . VAL   B 30  ? 0.2149 0.2856 0.2654 -0.0132 -0.0009 0.0758  30  VAL   B CA  
4394 C  C   . VAL   B 30  ? 0.1841 0.2721 0.2361 -0.0162 0.0005  0.0905  30  VAL   B C   
4395 O  O   . VAL   B 30  ? 0.1933 0.2946 0.2385 -0.0127 0.0059  0.0967  30  VAL   B O   
4396 C  CB  . VAL   B 30  ? 0.2225 0.2855 0.3371 -0.0318 -0.0385 0.0736  30  VAL   B CB  
4397 C  CG1 . VAL   B 30  ? 0.2287 0.2939 0.3346 -0.0310 -0.0339 0.0703  30  VAL   B CG1 
4398 C  CG2 . VAL   B 30  ? 0.2368 0.2875 0.3688 -0.0370 -0.0512 0.0577  30  VAL   B CG2 
4408 N  N   . LYS   B 31  ? 0.1740 0.2285 0.2755 -0.0231 -0.0002 0.0876  31  LYS   B N   
4409 C  CA  . LYS   B 31  ? 0.1604 0.2267 0.3065 -0.0323 -0.0052 0.0971  31  LYS   B CA  
4410 C  C   . LYS   B 31  ? 0.1548 0.1989 0.2619 -0.0365 -0.0248 0.0831  31  LYS   B C   
4411 O  O   . LYS   B 31  ? 0.1630 0.2153 0.2769 -0.0267 -0.0167 0.0973  31  LYS   B O   
4412 C  CB  . LYS   B 31  ? 0.1760 0.2758 0.3739 -0.0251 0.0328  0.1126  31  LYS   B CB  
4413 C  CG  . LYS   B 31  ? 0.2088 0.3188 0.4222 -0.0223 0.0548  0.1113  31  LYS   B CG  
4414 C  CD  . LYS   B 31  ? 0.2503 0.3667 0.4696 -0.0141 0.0562  0.0999  31  LYS   B CD  
4415 C  CE  . LYS   B 31  ? 0.2812 0.3958 0.5163 -0.0088 0.0513  0.0857  31  LYS   B CE  
4416 N  NZ  . LYS   B 31  ? 0.3078 0.4191 0.5276 -0.0022 0.0467  0.0734  31  LYS   B NZ  
4430 N  N   . PRO   B 32  ? 0.1731 0.1632 0.2035 -0.0378 -0.0400 0.0517  32  PRO   B N   
4431 C  CA  . PRO   B 32  ? 0.1792 0.1594 0.1605 -0.0362 -0.0393 0.0229  32  PRO   B CA  
4432 C  C   . PRO   B 32  ? 0.1873 0.1484 0.1694 -0.0366 -0.0429 0.0322  32  PRO   B C   
4433 O  O   . PRO   B 32  ? 0.1975 0.1531 0.2223 -0.0344 -0.0625 0.0261  32  PRO   B O   
4434 C  CB  . PRO   B 32  ? 0.1943 0.1495 0.1682 -0.0425 -0.0260 0.0089  32  PRO   B CB  
4435 C  CG  . PRO   B 32  ? 0.2099 0.1390 0.1698 -0.0334 -0.0403 0.0188  32  PRO   B CG  
4436 C  CD  . PRO   B 32  ? 0.1993 0.1479 0.2096 -0.0280 -0.0424 0.0315  32  PRO   B CD  
4444 N  N   . THR   B 33  ? 0.1915 0.1398 0.1693 -0.0331 -0.0379 0.0203  33  THR   B N   
4445 C  CA  . THR   B 33  ? 0.1947 0.1499 0.1729 -0.0389 -0.0407 0.0260  33  THR   B CA  
4446 C  C   . THR   B 33  ? 0.1968 0.1395 0.1581 -0.0365 -0.0416 0.0160  33  THR   B C   
4447 O  O   . THR   B 33  ? 0.2092 0.1500 0.1737 -0.0423 -0.0527 0.0215  33  THR   B O   
4448 C  CB  . THR   B 33  ? 0.2072 0.1577 0.1638 -0.0236 -0.0529 0.0240  33  THR   B CB  
4449 O  OG1 . THR   B 33  ? 0.2008 0.1671 0.1694 -0.0273 -0.0512 0.0358  33  THR   B OG1 
4450 C  CG2 . THR   B 33  ? 0.2277 0.1641 0.1639 -0.0137 -0.0406 0.0129  33  THR   B CG2 
4458 N  N   . VAL   B 34  ? 0.1802 0.1401 0.1329 -0.0341 -0.0408 0.0134  34  VAL   B N   
4459 C  CA  . VAL   B 34  ? 0.1637 0.1345 0.1399 -0.0256 -0.0368 0.0082  34  VAL   B CA  
4460 C  C   . VAL   B 34  ? 0.1582 0.1347 0.1141 -0.0287 -0.0183 0.0065  34  VAL   B C   
4461 O  O   . VAL   B 34  ? 0.1795 0.1372 0.1241 -0.0285 -0.0280 0.0105  34  VAL   B O   
4462 C  CB  . VAL   B 34  ? 0.1690 0.1387 0.1782 -0.0125 -0.0214 0.0040  34  VAL   B CB  
4463 C  CG1 . VAL   B 34  ? 0.1709 0.1532 0.1808 -0.0093 -0.0073 0.0002  34  VAL   B CG1 
4464 C  CG2 . VAL   B 34  ? 0.1757 0.1489 0.2044 -0.0097 -0.0270 0.0021  34  VAL   B CG2 
4474 N  N   . VAL   B 35  ? 0.1506 0.1267 0.1172 -0.0275 -0.0114 0.0057  35  VAL   B N   
4475 C  CA  . VAL   B 35  ? 0.1412 0.1249 0.1143 -0.0178 -0.0082 0.0005  35  VAL   B CA  
4476 C  C   . VAL   B 35  ? 0.1323 0.1205 0.1087 -0.0120 -0.0091 -0.0009 35  VAL   B C   
4477 O  O   . VAL   B 35  ? 0.1366 0.1304 0.1228 -0.0189 0.0022  -0.0070 35  VAL   B O   
4478 C  CB  . VAL   B 35  ? 0.1381 0.1457 0.1458 -0.0194 0.0006  0.0055  35  VAL   B CB  
4479 C  CG1 . VAL   B 35  ? 0.1293 0.1604 0.1752 -0.0215 0.0054  0.0004  35  VAL   B CG1 
4480 C  CG2 . VAL   B 35  ? 0.1453 0.1445 0.1671 -0.0078 -0.0069 0.0108  35  VAL   B CG2 
4490 N  N   . VAL   B 36  ? 0.1327 0.1193 0.1149 -0.0165 -0.0135 0.0120  36  VAL   B N   
4491 C  CA  . VAL   B 36  ? 0.1375 0.1181 0.1139 -0.0112 -0.0040 0.0072  36  VAL   B CA  
4492 C  C   . VAL   B 36  ? 0.1262 0.1221 0.0882 -0.0084 0.0048  0.0035  36  VAL   B C   
4493 O  O   . VAL   B 36  ? 0.1373 0.1287 0.1348 -0.0090 0.0022  -0.0064 36  VAL   B O   
4494 C  CB  . VAL   B 36  ? 0.1300 0.1255 0.1285 -0.0158 -0.0071 -0.0013 36  VAL   B CB  
4495 C  CG1 . VAL   B 36  ? 0.1302 0.1395 0.1431 -0.0153 -0.0101 0.0192  36  VAL   B CG1 
4496 C  CG2 . VAL   B 36  ? 0.1392 0.1342 0.1375 -0.0115 -0.0076 0.0098  36  VAL   B CG2 
4506 N  N   . ASN   B 37  ? 0.1299 0.1226 0.1143 0.0031  -0.0035 0.0088  37  ASN   B N   
4507 C  CA  . ASN   B 37  ? 0.1325 0.1255 0.1203 0.0017  -0.0033 0.0082  37  ASN   B CA  
4508 C  C   . ASN   B 37  ? 0.1274 0.1312 0.1215 0.0042  -0.0131 0.0092  37  ASN   B C   
4509 O  O   . ASN   B 37  ? 0.1379 0.1330 0.1265 0.0011  -0.0013 0.0123  37  ASN   B O   
4510 C  CB  . ASN   B 37  ? 0.1328 0.1324 0.1203 0.0045  -0.0023 0.0027  37  ASN   B CB  
4511 C  CG  . ASN   B 37  ? 0.1328 0.1286 0.1373 -0.0017 -0.0049 -0.0003 37  ASN   B CG  
4512 O  OD1 . ASN   B 37  ? 0.1420 0.1302 0.1527 0.0051  -0.0076 -0.0009 37  ASN   B OD1 
4513 N  ND2 . ASN   B 37  ? 0.1382 0.1246 0.1476 0.0015  -0.0116 0.0021  37  ASN   B ND2 
4520 N  N   . ALA   B 38  ? 0.1396 0.1247 0.1253 0.0076  0.0026  -0.0014 38  ALA   B N   
4521 C  CA  . ALA   B 38  ? 0.1455 0.1328 0.1360 0.0015  0.0070  0.0125  38  ALA   B CA  
4522 C  C   . ALA   B 38  ? 0.1452 0.1278 0.1303 -0.0005 0.0075  0.0141  38  ALA   B C   
4523 O  O   . ALA   B 38  ? 0.1586 0.1331 0.1519 0.0066  0.0015  0.0155  38  ALA   B O   
4524 C  CB  . ALA   B 38  ? 0.1624 0.1381 0.1583 -0.0081 0.0126  0.0077  38  ALA   B CB  
4530 N  N   . ALA   B 39  ? 0.1456 0.1260 0.1253 0.0061  -0.0005 0.0063  39  ALA   B N   
4531 C  CA  . ALA   B 39  ? 0.1564 0.1343 0.1298 0.0069  -0.0047 0.0031  39  ALA   B CA  
4532 C  C   . ALA   B 39  ? 0.1648 0.1425 0.1160 0.0081  -0.0021 0.0062  39  ALA   B C   
4533 O  O   . ALA   B 39  ? 0.1600 0.1413 0.1456 0.0011  0.0049  0.0066  39  ALA   B O   
4534 C  CB  . ALA   B 39  ? 0.1546 0.1361 0.1439 -0.0027 -0.0067 0.0024  39  ALA   B CB  
4540 N  N   . ASN   B 40  ? 0.1698 0.1604 0.1178 0.0001  -0.0007 -0.0056 40  ASN   B N   
4541 C  CA  . ASN   B 40  ? 0.1776 0.1641 0.1415 0.0094  -0.0065 -0.0016 40  ASN   B CA  
4542 C  C   . ASN   B 40  ? 0.1787 0.1642 0.1051 0.0138  -0.0107 -0.0065 40  ASN   B C   
4543 O  O   . ASN   B 40  ? 0.1713 0.1578 0.1225 0.0123  -0.0138 0.0101  40  ASN   B O   
4544 C  CB  . ASN   B 40  ? 0.1866 0.1673 0.1663 0.0163  -0.0118 0.0193  40  ASN   B CB  
4545 C  CG  . ASN   B 40  ? 0.1848 0.1670 0.1935 0.0108  -0.0240 0.0244  40  ASN   B CG  
4546 O  OD1 . ASN   B 40  ? 0.1801 0.1630 0.2759 0.0025  -0.0300 0.0192  40  ASN   B OD1 
4547 N  ND2 . ASN   B 40  ? 0.1917 0.1690 0.1948 0.0124  -0.0181 0.0144  40  ASN   B ND2 
4554 N  N   . VAL   B 41  ? 0.1837 0.1680 0.1159 0.0183  -0.0011 0.0006  41  VAL   B N   
4555 C  CA  . VAL   B 41  ? 0.1877 0.1833 0.1218 0.0101  0.0064  -0.0029 41  VAL   B CA  
4556 C  C   . VAL   B 41  ? 0.1797 0.1831 0.1172 0.0158  -0.0032 -0.0068 41  VAL   B C   
4557 O  O   . VAL   B 41  ? 0.1799 0.1751 0.1466 0.0169  -0.0115 -0.0067 41  VAL   B O   
4558 C  CB  . VAL   B 41  ? 0.2016 0.2020 0.1477 -0.0062 0.0244  -0.0243 41  VAL   B CB  
4559 C  CG1 . VAL   B 41  ? 0.1966 0.2080 0.1698 -0.0135 0.0422  -0.0255 41  VAL   B CG1 
4560 C  CG2 . VAL   B 41  ? 0.2203 0.2240 0.1591 -0.0098 0.0299  -0.0147 41  VAL   B CG2 
4570 N  N   . TYR   B 42  ? 0.1874 0.1834 0.1317 0.0172  -0.0195 -0.0015 42  TYR   B N   
4571 C  CA  . TYR   B 42  ? 0.1968 0.1843 0.1339 0.0184  -0.0241 -0.0163 42  TYR   B CA  
4572 C  C   . TYR   B 42  ? 0.1827 0.1672 0.1449 0.0227  -0.0205 -0.0188 42  TYR   B C   
4573 O  O   . TYR   B 42  ? 0.1784 0.1712 0.1769 0.0200  -0.0257 -0.0211 42  TYR   B O   
4574 C  CB  . TYR   B 42  ? 0.2175 0.2167 0.1537 0.0129  -0.0276 -0.0149 42  TYR   B CB  
4575 C  CG  . TYR   B 42  ? 0.2157 0.2375 0.1469 0.0045  -0.0274 0.0026  42  TYR   B CG  
4576 C  CD1 . TYR   B 42  ? 0.2070 0.2376 0.1217 -0.0004 -0.0088 0.0020  42  TYR   B CD1 
4577 C  CD2 . TYR   B 42  ? 0.2297 0.2462 0.1874 -0.0022 -0.0107 0.0130  42  TYR   B CD2 
4578 C  CE1 . TYR   B 42  ? 0.2233 0.2523 0.1182 -0.0013 -0.0064 0.0003  42  TYR   B CE1 
4579 C  CE2 . TYR   B 42  ? 0.2357 0.2593 0.1805 0.0003  0.0164  0.0291  42  TYR   B CE2 
4580 C  CZ  . TYR   B 42  ? 0.2432 0.2740 0.1487 0.0128  0.0208  0.0069  42  TYR   B CZ  
4581 O  OH  . TYR   B 42  ? 0.2786 0.3028 0.1946 0.0311  0.0287  0.0170  42  TYR   B OH  
4591 N  N   . LEU   B 43  ? 0.1643 0.1530 0.1303 0.0086  -0.0158 -0.0146 43  LEU   B N   
4592 C  CA  . LEU   B 43  ? 0.1560 0.1551 0.1140 0.0063  -0.0113 -0.0018 43  LEU   B CA  
4593 C  C   . LEU   B 43  ? 0.1644 0.1517 0.1262 0.0027  -0.0120 -0.0076 43  LEU   B C   
4594 O  O   . LEU   B 43  ? 0.1570 0.1586 0.1712 0.0035  -0.0218 0.0144  43  LEU   B O   
4595 C  CB  . LEU   B 43  ? 0.1532 0.1519 0.1384 0.0011  -0.0196 -0.0099 43  LEU   B CB  
4596 C  CG  . LEU   B 43  ? 0.1677 0.1443 0.1443 0.0058  -0.0189 -0.0042 43  LEU   B CG  
4597 C  CD1 . LEU   B 43  ? 0.1794 0.1532 0.1737 0.0006  -0.0307 -0.0115 43  LEU   B CD1 
4598 C  CD2 . LEU   B 43  ? 0.1620 0.1439 0.1692 -0.0007 -0.0258 -0.0168 43  LEU   B CD2 
4610 N  N   . LYS   B 44  ? 0.1585 0.1476 0.1442 0.0102  -0.0055 -0.0062 44  LYS   B N   
4611 C  CA  . LYS   B 44  ? 0.1704 0.1652 0.1420 0.0105  -0.0094 0.0041  44  LYS   B CA  
4612 C  C   . LYS   B 44  ? 0.1693 0.1518 0.1375 0.0180  -0.0104 -0.0066 44  LYS   B C   
4613 O  O   . LYS   B 44  ? 0.1921 0.1523 0.1736 0.0082  0.0036  0.0001  44  LYS   B O   
4614 C  CB  . LYS   B 44  ? 0.1915 0.1948 0.1626 0.0199  -0.0228 0.0048  44  LYS   B CB  
4615 C  CG  . LYS   B 44  ? 0.2263 0.2212 0.1910 0.0198  -0.0396 0.0038  44  LYS   B CG  
4616 C  CD  . LYS   B 44  ? 0.2627 0.2393 0.2585 0.0076  -0.0507 0.0021  44  LYS   B CD  
4617 C  CE  . LYS   B 44  ? 0.2987 0.2623 0.3039 -0.0024 -0.0555 0.0249  44  LYS   B CE  
4618 N  NZ  . LYS   B 44  ? 0.3081 0.2724 0.3301 -0.0024 -0.0700 0.0445  44  LYS   B NZ  
4632 N  N   . HIS   B 45  ? 0.1618 0.1624 0.1331 0.0104  0.0000  0.0088  45  HIS   B N   
4633 C  CA  . HIS   B 45  ? 0.1607 0.1621 0.1316 0.0112  0.0008  -0.0044 45  HIS   B CA  
4634 C  C   . HIS   B 45  ? 0.1831 0.1791 0.1763 0.0190  -0.0124 -0.0060 45  HIS   B C   
4635 O  O   . HIS   B 45  ? 0.1994 0.2073 0.2398 0.0438  0.0128  0.0010  45  HIS   B O   
4636 C  CB  . HIS   B 45  ? 0.1528 0.1628 0.1439 0.0066  -0.0086 -0.0069 45  HIS   B CB  
4637 C  CG  . HIS   B 45  ? 0.1517 0.1527 0.1445 0.0032  -0.0090 -0.0043 45  HIS   B CG  
4638 N  ND1 . HIS   B 45  ? 0.1577 0.1482 0.1517 0.0049  -0.0221 -0.0011 45  HIS   B ND1 
4639 C  CD2 . HIS   B 45  ? 0.1640 0.1544 0.1638 0.0016  -0.0159 -0.0034 45  HIS   B CD2 
4640 C  CE1 . HIS   B 45  ? 0.1663 0.1408 0.1398 0.0013  -0.0195 -0.0040 45  HIS   B CE1 
4641 N  NE2 . HIS   B 45  ? 0.1697 0.1488 0.1579 0.0029  -0.0139 -0.0044 45  HIS   B NE2 
4649 N  N   A GLY   B 46  ? 0.1908 0.1732 0.2084 0.0244  -0.0263 0.0105  46  GLY   B N   
4650 N  N   B GLY   B 46  ? 0.1924 0.1829 0.1984 0.0194  -0.0199 0.0070  46  GLY   B N   
4651 C  CA  A GLY   B 46  ? 0.2095 0.1856 0.2516 0.0226  -0.0211 0.0132  46  GLY   B CA  
4652 C  CA  B GLY   B 46  ? 0.2073 0.1950 0.2252 0.0170  -0.0187 0.0131  46  GLY   B CA  
4653 C  C   A GLY   B 46  ? 0.2167 0.2045 0.3016 0.0254  -0.0250 0.0114  46  GLY   B C   
4654 C  C   B GLY   B 46  ? 0.2174 0.2113 0.2586 0.0178  -0.0212 0.0172  46  GLY   B C   
4655 O  O   A GLY   B 46  ? 0.2205 0.2127 0.3832 0.0293  -0.0181 -0.0080 46  GLY   B O   
4656 O  O   B GLY   B 46  ? 0.2234 0.2223 0.2778 0.0192  -0.0200 0.0230  46  GLY   B O   
4663 N  N   . GLY   B 47  ? 0.2198 0.2140 0.2700 0.0062  -0.0155 0.0033  47  GLY   B N   
4664 C  CA  . GLY   B 47  ? 0.2077 0.1807 0.2185 -0.0032 -0.0098 -0.0073 47  GLY   B CA  
4665 C  C   . GLY   B 47  ? 0.1821 0.1556 0.1839 -0.0026 0.0046  -0.0000 47  GLY   B C   
4666 O  O   . GLY   B 47  ? 0.1948 0.1508 0.1933 0.0021  0.0025  0.0093  47  GLY   B O   
4671 N  N   . GLY   B 48  ? 0.1549 0.1450 0.1773 0.0032  -0.0092 0.0178  48  GLY   B N   
4672 C  CA  . GLY   B 48  ? 0.1594 0.1446 0.1954 0.0016  -0.0004 0.0065  48  GLY   B CA  
4673 C  C   . GLY   B 48  ? 0.1484 0.1393 0.1816 0.0003  0.0044  0.0091  48  GLY   B C   
4674 O  O   . GLY   B 48  ? 0.1430 0.1411 0.2010 0.0039  -0.0058 0.0043  48  GLY   B O   
4678 N  N   . VAL   B 49  ? 0.1454 0.1458 0.1684 0.0092  -0.0031 0.0092  49  VAL   B N   
4679 C  CA  . VAL   B 49  ? 0.1515 0.1605 0.1450 0.0092  -0.0049 -0.0087 49  VAL   B CA  
4680 C  C   . VAL   B 49  ? 0.1394 0.1490 0.1443 0.0070  -0.0018 0.0007  49  VAL   B C   
4681 O  O   . VAL   B 49  ? 0.1493 0.1515 0.1536 0.0072  0.0019  -0.0014 49  VAL   B O   
4682 C  CB  . VAL   B 49  ? 0.1551 0.1701 0.1755 0.0028  -0.0130 0.0003  49  VAL   B CB  
4683 C  CG1 . VAL   B 49  ? 0.1463 0.1829 0.1784 0.0030  -0.0238 -0.0014 49  VAL   B CG1 
4684 C  CG2 . VAL   B 49  ? 0.1771 0.1771 0.1968 -0.0057 -0.0342 0.0011  49  VAL   B CG2 
4694 N  N   . ALA   B 50  ? 0.1419 0.1366 0.1442 0.0000  -0.0029 0.0067  50  ALA   B N   
4695 C  CA  . ALA   B 50  ? 0.1401 0.1273 0.1440 0.0124  -0.0036 -0.0002 50  ALA   B CA  
4696 C  C   . ALA   B 50  ? 0.1471 0.1349 0.1436 0.0056  -0.0004 0.0089  50  ALA   B C   
4697 O  O   . ALA   B 50  ? 0.1443 0.1387 0.1472 0.0051  0.0081  0.0007  50  ALA   B O   
4698 C  CB  . ALA   B 50  ? 0.1558 0.1295 0.1547 -0.0038 -0.0050 0.0061  50  ALA   B CB  
4704 N  N   . GLY   B 51  ? 0.1457 0.1442 0.1575 0.0143  -0.0030 0.0050  51  GLY   B N   
4705 C  CA  . GLY   B 51  ? 0.1510 0.1530 0.1886 0.0216  -0.0039 0.0081  51  GLY   B CA  
4706 C  C   . GLY   B 51  ? 0.1495 0.1466 0.1692 0.0219  -0.0060 0.0106  51  GLY   B C   
4707 O  O   . GLY   B 51  ? 0.1463 0.1627 0.1904 0.0101  -0.0053 -0.0055 51  GLY   B O   
4711 N  N   . ALA   B 52  ? 0.1529 0.1409 0.1626 0.0200  -0.0117 -0.0053 52  ALA   B N   
4712 C  CA  . ALA   B 52  ? 0.1579 0.1491 0.1665 0.0146  -0.0058 -0.0140 52  ALA   B CA  
4713 C  C   . ALA   B 52  ? 0.1455 0.1470 0.1579 0.0085  0.0032  -0.0095 52  ALA   B C   
4714 O  O   . ALA   B 52  ? 0.1413 0.1528 0.1756 0.0129  0.0065  0.0037  52  ALA   B O   
4715 C  CB  . ALA   B 52  ? 0.1699 0.1534 0.1835 0.0067  0.0072  -0.0109 52  ALA   B CB  
4721 N  N   . LEU   B 53  ? 0.1385 0.1436 0.1518 0.0150  0.0030  -0.0039 53  LEU   B N   
4722 C  CA  . LEU   B 53  ? 0.1375 0.1573 0.1383 0.0147  0.0012  0.0029  53  LEU   B CA  
4723 C  C   . LEU   B 53  ? 0.1414 0.1452 0.1433 0.0100  0.0051  -0.0040 53  LEU   B C   
4724 O  O   . LEU   B 53  ? 0.1476 0.1526 0.1684 0.0009  0.0044  0.0153  53  LEU   B O   
4725 C  CB  . LEU   B 53  ? 0.1354 0.1568 0.1672 0.0132  0.0024  0.0081  53  LEU   B CB  
4726 C  CG  . LEU   B 53  ? 0.1338 0.1726 0.1717 0.0059  0.0046  0.0177  53  LEU   B CG  
4727 C  CD1 . LEU   B 53  ? 0.1370 0.1940 0.1961 0.0136  0.0036  0.0102  53  LEU   B CD1 
4728 C  CD2 . LEU   B 53  ? 0.1405 0.2009 0.1917 -0.0007 -0.0069 -0.0110 53  LEU   B CD2 
4740 N  N   . ASN   B 54  ? 0.1462 0.1333 0.1415 0.0065  0.0034  0.0031  54  ASN   B N   
4741 C  CA  . ASN   B 54  ? 0.1474 0.1476 0.1476 0.0016  -0.0017 -0.0104 54  ASN   B CA  
4742 C  C   . ASN   B 54  ? 0.1414 0.1524 0.1827 -0.0019 0.0050  -0.0007 54  ASN   B C   
4743 O  O   . ASN   B 54  ? 0.1407 0.1572 0.1952 -0.0027 0.0027  -0.0080 54  ASN   B O   
4744 C  CB  . ASN   B 54  ? 0.1495 0.1565 0.1756 0.0031  0.0067  -0.0079 54  ASN   B CB  
4745 C  CG  . ASN   B 54  ? 0.1466 0.1671 0.1629 0.0075  -0.0031 -0.0001 54  ASN   B CG  
4746 O  OD1 . ASN   B 54  ? 0.1413 0.1685 0.1839 0.0072  -0.0039 -0.0169 54  ASN   B OD1 
4747 N  ND2 . ASN   B 54  ? 0.1616 0.1858 0.1939 0.0031  -0.0257 0.0082  54  ASN   B ND2 
4754 N  N   . LYS   B 55  ? 0.1462 0.1528 0.2071 0.0086  0.0066  0.0038  55  LYS   B N   
4755 C  CA  . LYS   B 55  ? 0.1482 0.1696 0.2125 0.0154  0.0093  -0.0080 55  LYS   B CA  
4756 C  C   . LYS   B 55  ? 0.1408 0.1682 0.2064 0.0115  0.0065  -0.0135 55  LYS   B C   
4757 O  O   . LYS   B 55  ? 0.1412 0.1877 0.2233 0.0144  0.0111  -0.0042 55  LYS   B O   
4758 C  CB  . LYS   B 55  ? 0.1692 0.1797 0.2602 0.0264  0.0264  -0.0084 55  LYS   B CB  
4759 C  CG  . LYS   B 55  ? 0.2152 0.2152 0.3484 0.0345  0.0395  0.0036  55  LYS   B CG  
4760 C  CD  . LYS   B 55  ? 0.2529 0.2403 0.4140 0.0478  0.0534  0.0139  55  LYS   B CD  
4761 C  CE  . LYS   B 55  ? 0.2780 0.2612 0.4731 0.0510  0.0668  0.0162  55  LYS   B CE  
4762 N  NZ  . LYS   B 55  ? 0.2882 0.2793 0.5100 0.0479  0.0525  0.0276  55  LYS   B NZ  
4776 N  N   . ALA   B 56  ? 0.1427 0.1685 0.1924 0.0131  0.0020  -0.0180 56  ALA   B N   
4777 C  CA  . ALA   B 56  ? 0.1593 0.1854 0.1889 0.0093  0.0122  -0.0109 56  ALA   B CA  
4778 C  C   . ALA   B 56  ? 0.1650 0.1817 0.1937 0.0053  0.0291  -0.0022 56  ALA   B C   
4779 O  O   . ALA   B 56  ? 0.1691 0.1896 0.2098 0.0065  0.0393  -0.0054 56  ALA   B O   
4780 C  CB  . ALA   B 56  ? 0.1730 0.2059 0.1824 -0.0093 0.0074  -0.0114 56  ALA   B CB  
4786 N  N   . THR   B 57  ? 0.1518 0.1710 0.1985 0.0052  0.0301  -0.0041 57  THR   B N   
4787 C  CA  . THR   B 57  ? 0.1495 0.1722 0.1840 0.0012  0.0263  -0.0027 57  THR   B CA  
4788 C  C   . THR   B 57  ? 0.1560 0.1823 0.2114 -0.0016 0.0318  -0.0067 57  THR   B C   
4789 O  O   . THR   B 57  ? 0.1661 0.1801 0.2238 -0.0157 0.0224  0.0058  57  THR   B O   
4790 C  CB  . THR   B 57  ? 0.1599 0.1570 0.1592 -0.0006 0.0178  0.0020  57  THR   B CB  
4791 O  OG1 . THR   B 57  ? 0.1615 0.1512 0.1760 -0.0040 0.0228  0.0008  57  THR   B OG1 
4792 C  CG2 . THR   B 57  ? 0.1583 0.1607 0.1700 -0.0024 0.0253  0.0022  57  THR   B CG2 
4800 N  N   . ASN   B 58  ? 0.1397 0.2028 0.2426 -0.0160 0.0154  -0.0272 58  ASN   B N   
4801 C  CA  . ASN   B 58  ? 0.1591 0.2540 0.2763 -0.0333 0.0498  -0.0210 58  ASN   B CA  
4802 C  C   . ASN   B 58  ? 0.1400 0.2267 0.2304 -0.0161 0.0091  -0.0201 58  ASN   B C   
4803 O  O   . ASN   B 58  ? 0.1499 0.2371 0.2370 -0.0172 0.0025  -0.0221 58  ASN   B O   
4804 C  CB  . ASN   B 58  ? 0.2725 0.3478 0.3996 -0.0471 0.0913  -0.0175 58  ASN   B CB  
4805 C  CG  . ASN   B 58  ? 0.4159 0.4483 0.5520 -0.0495 0.1159  0.0040  58  ASN   B CG  
4806 O  OD1 . ASN   B 58  ? 0.4457 0.4676 0.6038 -0.0505 0.1219  0.0088  58  ASN   B OD1 
4807 N  ND2 . ASN   B 58  ? 0.5137 0.5137 0.6072 -0.0497 0.1234  0.0086  58  ASN   B ND2 
4814 N  N   . ASN   B 59  ? 0.1482 0.2101 0.2043 -0.0103 0.0046  -0.0049 59  ASN   B N   
4815 C  CA  . ASN   B 59  ? 0.1498 0.2045 0.1980 -0.0120 -0.0053 0.0062  59  ASN   B CA  
4816 C  C   . ASN   B 59  ? 0.1420 0.1982 0.1930 -0.0115 -0.0060 0.0001  59  ASN   B C   
4817 O  O   . ASN   B 59  ? 0.1445 0.1967 0.1868 -0.0076 -0.0076 0.0011  59  ASN   B O   
4818 C  CB  . ASN   B 59  ? 0.1569 0.2237 0.2147 -0.0034 -0.0249 0.0067  59  ASN   B CB  
4819 C  CG  . ASN   B 59  ? 0.1698 0.2389 0.2281 0.0059  -0.0351 0.0008  59  ASN   B CG  
4820 O  OD1 . ASN   B 59  ? 0.1710 0.2385 0.2406 0.0094  -0.0173 0.0219  59  ASN   B OD1 
4821 N  ND2 . ASN   B 59  ? 0.1759 0.2478 0.2260 -0.0046 -0.0226 -0.0013 59  ASN   B ND2 
4828 N  N   . ALA   B 60  ? 0.1442 0.1877 0.1931 -0.0150 0.0058  -0.0058 60  ALA   B N   
4829 C  CA  . ALA   B 60  ? 0.1571 0.1754 0.1896 -0.0236 0.0029  0.0010  60  ALA   B CA  
4830 C  C   . ALA   B 60  ? 0.1540 0.1601 0.1720 -0.0104 0.0005  0.0019  60  ALA   B C   
4831 O  O   . ALA   B 60  ? 0.1564 0.1594 0.1962 -0.0097 0.0035  0.0000  60  ALA   B O   
4832 C  CB  . ALA   B 60  ? 0.1644 0.1719 0.2118 -0.0186 0.0058  -0.0006 60  ALA   B CB  
4838 N  N   . MET   B 61  ? 0.1469 0.1548 0.1664 -0.0047 0.0020  0.0074  61  MET   B N   
4839 C  CA  . MET   B 61  ? 0.1428 0.1471 0.1548 -0.0046 -0.0077 0.0024  61  MET   B CA  
4840 C  C   . MET   B 61  ? 0.1502 0.1494 0.1477 -0.0118 -0.0051 0.0076  61  MET   B C   
4841 O  O   . MET   B 61  ? 0.1506 0.1450 0.1564 -0.0032 0.0035  -0.0101 61  MET   B O   
4842 C  CB  . MET   B 61  ? 0.1355 0.1452 0.1595 0.0045  -0.0039 -0.0110 61  MET   B CB  
4843 C  CG  . MET   B 61  ? 0.1415 0.1423 0.1595 -0.0028 -0.0077 0.0036  61  MET   B CG  
4844 S  SD  . MET   B 61  ? 0.1400 0.1488 0.1721 0.0002  -0.0027 -0.0093 61  MET   B SD  
4845 C  CE  . MET   B 61  ? 0.1386 0.1738 0.1998 -0.0019 0.0017  -0.0236 61  MET   B CE  
4855 N  N   . GLN   B 62  ? 0.1462 0.1569 0.1495 -0.0045 -0.0144 0.0049  62  GLN   B N   
4856 C  CA  . GLN   B 62  ? 0.1489 0.1605 0.1629 0.0018  -0.0184 0.0022  62  GLN   B CA  
4857 C  C   . GLN   B 62  ? 0.1506 0.1647 0.1632 0.0031  -0.0213 -0.0072 62  GLN   B C   
4858 O  O   . GLN   B 62  ? 0.1662 0.1647 0.1593 -0.0008 -0.0232 -0.0076 62  GLN   B O   
4859 C  CB  . GLN   B 62  ? 0.1467 0.1632 0.1676 0.0018  -0.0180 0.0002  62  GLN   B CB  
4860 C  CG  . GLN   B 62  ? 0.1514 0.1687 0.1693 0.0046  -0.0240 -0.0058 62  GLN   B CG  
4861 C  CD  . GLN   B 62  ? 0.1563 0.1636 0.1607 0.0093  -0.0231 0.0037  62  GLN   B CD  
4862 O  OE1 . GLN   B 62  ? 0.1548 0.1614 0.1712 0.0070  -0.0256 -0.0046 62  GLN   B OE1 
4863 N  NE2 . GLN   B 62  ? 0.1614 0.1634 0.1663 0.0075  -0.0282 -0.0020 62  GLN   B NE2 
4872 N  N   . VAL   B 63  ? 0.1480 0.1623 0.1820 -0.0021 -0.0187 -0.0192 63  VAL   B N   
4873 C  CA  . VAL   B 63  ? 0.1555 0.1682 0.2050 -0.0065 -0.0228 -0.0094 63  VAL   B CA  
4874 C  C   . VAL   B 63  ? 0.1572 0.1589 0.1800 -0.0094 -0.0196 -0.0190 63  VAL   B C   
4875 O  O   . VAL   B 63  ? 0.1663 0.1571 0.1978 -0.0032 -0.0357 -0.0149 63  VAL   B O   
4876 C  CB  . VAL   B 63  ? 0.1546 0.1791 0.2554 -0.0101 -0.0209 -0.0132 63  VAL   B CB  
4877 C  CG1 . VAL   B 63  ? 0.1701 0.1859 0.2683 -0.0205 -0.0163 -0.0072 63  VAL   B CG1 
4878 C  CG2 . VAL   B 63  ? 0.1508 0.2020 0.2773 -0.0048 -0.0312 -0.0188 63  VAL   B CG2 
4888 N  N   . GLU   B 64  ? 0.1550 0.1466 0.1738 -0.0032 -0.0160 -0.0116 64  GLU   B N   
4889 C  CA  . GLU   B 64  ? 0.1543 0.1437 0.1667 -0.0046 -0.0269 -0.0033 64  GLU   B CA  
4890 C  C   . GLU   B 64  ? 0.1503 0.1481 0.1600 0.0032  -0.0235 -0.0093 64  GLU   B C   
4891 O  O   . GLU   B 64  ? 0.1592 0.1551 0.1665 -0.0067 -0.0280 -0.0189 64  GLU   B O   
4892 C  CB  . GLU   B 64  ? 0.1523 0.1521 0.1705 -0.0103 -0.0172 0.0005  64  GLU   B CB  
4893 C  CG  . GLU   B 64  ? 0.1626 0.1474 0.1723 -0.0179 -0.0240 -0.0104 64  GLU   B CG  
4894 C  CD  . GLU   B 64  ? 0.1637 0.1696 0.1758 -0.0267 -0.0307 -0.0067 64  GLU   B CD  
4895 O  OE1 . GLU   B 64  ? 0.1671 0.1886 0.1798 -0.0325 -0.0140 -0.0310 64  GLU   B OE1 
4896 O  OE2 . GLU   B 64  ? 0.1788 0.1757 0.1813 -0.0295 -0.0301 -0.0145 64  GLU   B OE2 
4903 N  N   . SER   B 65  ? 0.1483 0.1475 0.1536 -0.0021 -0.0107 -0.0147 65  SER   B N   
4904 C  CA  . SER   B 65  ? 0.1500 0.1483 0.1612 -0.0026 -0.0092 -0.0207 65  SER   B CA  
4905 C  C   . SER   B 65  ? 0.1539 0.1434 0.1612 -0.0004 -0.0178 -0.0228 65  SER   B C   
4906 O  O   . SER   B 65  ? 0.1603 0.1542 0.1648 0.0002  -0.0132 -0.0260 65  SER   B O   
4907 C  CB  . SER   B 65  ? 0.1532 0.1489 0.1727 -0.0068 -0.0159 -0.0158 65  SER   B CB  
4908 O  OG  . SER   B 65  ? 0.1557 0.1498 0.1721 -0.0067 -0.0112 -0.0236 65  SER   B OG  
4914 N  N   . ASP   B 66  ? 0.1632 0.1506 0.1660 -0.0011 -0.0295 -0.0260 66  ASP   B N   
4915 C  CA  . ASP   B 66  ? 0.1756 0.1650 0.1581 0.0006  -0.0332 -0.0174 66  ASP   B CA  
4916 C  C   . ASP   B 66  ? 0.1782 0.1712 0.1545 -0.0052 -0.0272 -0.0200 66  ASP   B C   
4917 O  O   . ASP   B 66  ? 0.1833 0.1782 0.1684 0.0029  -0.0288 -0.0215 66  ASP   B O   
4918 C  CB  . ASP   B 66  ? 0.1874 0.1807 0.1872 0.0079  -0.0473 -0.0168 66  ASP   B CB  
4919 C  CG  . ASP   B 66  ? 0.2068 0.2015 0.2129 0.0157  -0.0550 -0.0083 66  ASP   B CG  
4920 O  OD1 . ASP   B 66  ? 0.2332 0.1907 0.2078 0.0147  -0.0481 -0.0014 66  ASP   B OD1 
4921 O  OD2 . ASP   B 66  ? 0.2217 0.2240 0.2772 0.0391  -0.0457 -0.0109 66  ASP   B OD2 
4926 N  N   . ASP   B 67  ? 0.1702 0.1611 0.1512 -0.0059 -0.0230 -0.0205 67  ASP   B N   
4927 C  CA  . ASP   B 67  ? 0.1855 0.1587 0.1709 -0.0110 -0.0240 -0.0116 67  ASP   B CA  
4928 C  C   . ASP   B 67  ? 0.1846 0.1558 0.1702 -0.0007 -0.0229 -0.0170 67  ASP   B C   
4929 O  O   . ASP   B 67  ? 0.1918 0.1599 0.1885 0.0014  -0.0222 -0.0274 67  ASP   B O   
4930 C  CB  . ASP   B 67  ? 0.2096 0.1643 0.1791 -0.0167 -0.0460 -0.0076 67  ASP   B CB  
4931 C  CG  . ASP   B 67  ? 0.2498 0.1698 0.1799 -0.0065 -0.0716 -0.0177 67  ASP   B CG  
4932 O  OD1 . ASP   B 67  ? 0.2696 0.1799 0.2003 -0.0078 -0.0681 -0.0094 67  ASP   B OD1 
4933 O  OD2 . ASP   B 67  ? 0.2667 0.1720 0.2200 0.0081  -0.0749 -0.0173 67  ASP   B OD2 
4938 N  N   . TYR   B 68  ? 0.1771 0.1564 0.1587 0.0041  -0.0344 -0.0257 68  TYR   B N   
4939 C  CA  . TYR   B 68  ? 0.1722 0.1709 0.1814 0.0083  -0.0303 -0.0354 68  TYR   B CA  
4940 C  C   . TYR   B 68  ? 0.1668 0.1644 0.1709 0.0012  -0.0280 -0.0372 68  TYR   B C   
4941 O  O   . TYR   B 68  ? 0.1742 0.1767 0.1813 0.0078  -0.0256 -0.0511 68  TYR   B O   
4942 C  CB  . TYR   B 68  ? 0.1709 0.1906 0.1952 0.0128  -0.0267 -0.0475 68  TYR   B CB  
4943 C  CG  . TYR   B 68  ? 0.1831 0.1981 0.2063 0.0208  -0.0259 -0.0654 68  TYR   B CG  
4944 C  CD1 . TYR   B 68  ? 0.1882 0.2062 0.2271 -0.0012 -0.0196 -0.0769 68  TYR   B CD1 
4945 C  CD2 . TYR   B 68  ? 0.1927 0.2175 0.2143 0.0234  -0.0354 -0.0601 68  TYR   B CD2 
4946 C  CE1 . TYR   B 68  ? 0.1972 0.2189 0.2424 -0.0005 -0.0229 -0.0769 68  TYR   B CE1 
4947 C  CE2 . TYR   B 68  ? 0.1949 0.2258 0.2140 0.0206  -0.0355 -0.0708 68  TYR   B CE2 
4948 C  CZ  . TYR   B 68  ? 0.1909 0.2281 0.2378 0.0029  -0.0323 -0.0653 68  TYR   B CZ  
4949 O  OH  . TYR   B 68  ? 0.1847 0.2424 0.2714 -0.0021 -0.0237 -0.0386 68  TYR   B OH  
4959 N  N   . ILE   B 69  ? 0.1675 0.1600 0.1703 0.0044  -0.0256 -0.0354 69  ILE   B N   
4960 C  CA  . ILE   B 69  ? 0.1763 0.1675 0.1741 -0.0007 -0.0243 -0.0379 69  ILE   B CA  
4961 C  C   . ILE   B 69  ? 0.1728 0.1673 0.1706 0.0076  -0.0299 -0.0241 69  ILE   B C   
4962 O  O   . ILE   B 69  ? 0.1792 0.1729 0.1719 0.0067  -0.0223 -0.0320 69  ILE   B O   
4963 C  CB  . ILE   B 69  ? 0.1801 0.1684 0.1927 -0.0000 -0.0008 -0.0329 69  ILE   B CB  
4964 C  CG1 . ILE   B 69  ? 0.1850 0.1739 0.1939 -0.0025 0.0176  -0.0338 69  ILE   B CG1 
4965 C  CG2 . ILE   B 69  ? 0.1885 0.1851 0.2140 -0.0010 0.0026  -0.0298 69  ILE   B CG2 
4966 C  CD1 . ILE   B 69  ? 0.1854 0.1786 0.2136 -0.0131 0.0210  -0.0371 69  ILE   B CD1 
4978 N  N   . ALA   B 70  ? 0.1609 0.1693 0.1781 0.0160  -0.0367 -0.0318 70  ALA   B N   
4979 C  CA  . ALA   B 70  ? 0.1679 0.1758 0.1630 0.0104  -0.0348 -0.0318 70  ALA   B CA  
4980 C  C   . ALA   B 70  ? 0.1755 0.1711 0.1756 -0.0037 -0.0341 -0.0366 70  ALA   B C   
4981 O  O   . ALA   B 70  ? 0.1872 0.1708 0.1822 0.0023  -0.0307 -0.0371 70  ALA   B O   
4982 C  CB  . ALA   B 70  ? 0.1716 0.1933 0.1662 0.0086  -0.0342 -0.0270 70  ALA   B CB  
4988 N  N   . THR   B 71  ? 0.1884 0.1688 0.1822 0.0024  -0.0448 -0.0411 71  THR   B N   
4989 C  CA  . THR   B 71  ? 0.1988 0.1659 0.2100 0.0100  -0.0651 -0.0310 71  THR   B CA  
4990 C  C   . THR   B 71  ? 0.1996 0.1655 0.2444 0.0303  -0.0570 -0.0385 71  THR   B C   
4991 O  O   . THR   B 71  ? 0.2131 0.1766 0.2857 0.0242  -0.0594 -0.0624 71  THR   B O   
4992 C  CB  . THR   B 71  ? 0.2228 0.1956 0.2381 -0.0001 -0.0654 -0.0100 71  THR   B CB  
4993 O  OG1 . THR   B 71  ? 0.2459 0.2235 0.2637 -0.0181 -0.0586 0.0093  71  THR   B OG1 
4994 C  CG2 . THR   B 71  ? 0.2347 0.1901 0.2668 0.0034  -0.0551 0.0013  71  THR   B CG2 
5002 N  N   . ASN   B 72  ? 0.1843 0.1699 0.2336 0.0174  -0.0523 -0.0631 72  ASN   B N   
5003 C  CA  . ASN   B 72  ? 0.1847 0.1852 0.2418 0.0219  -0.0391 -0.0782 72  ASN   B CA  
5004 C  C   . ASN   B 72  ? 0.1813 0.1976 0.2413 0.0077  -0.0236 -0.0743 72  ASN   B C   
5005 O  O   . ASN   B 72  ? 0.1779 0.2182 0.2817 0.0104  -0.0123 -0.0675 72  ASN   B O   
5006 C  CB  . ASN   B 72  ? 0.1892 0.2006 0.2455 0.0193  -0.0556 -0.0656 72  ASN   B CB  
5007 C  CG  . ASN   B 72  ? 0.2044 0.2139 0.2512 0.0335  -0.0633 -0.0406 72  ASN   B CG  
5008 O  OD1 . ASN   B 72  ? 0.2307 0.2323 0.2626 0.0147  -0.0371 -0.0532 72  ASN   B OD1 
5009 N  ND2 . ASN   B 72  ? 0.2136 0.2212 0.2928 0.0471  -0.0521 -0.0061 72  ASN   B ND2 
5016 N  N   . GLY   B 73  ? 0.1916 0.2051 0.2054 0.0035  -0.0243 -0.0611 73  GLY   B N   
5017 C  CA  . GLY   B 73  ? 0.1882 0.2107 0.1742 0.0018  -0.0214 -0.0558 73  GLY   B CA  
5018 C  C   . GLY   B 73  ? 0.1782 0.2048 0.1430 0.0061  -0.0084 -0.0491 73  GLY   B C   
5019 O  O   . GLY   B 73  ? 0.1771 0.1910 0.1657 0.0059  -0.0150 -0.0357 73  GLY   B O   
5023 N  N   . PRO   B 74  ? 0.1791 0.2132 0.1305 0.0042  -0.0231 -0.0390 74  PRO   B N   
5024 C  CA  . PRO   B 74  ? 0.1706 0.2155 0.1049 0.0063  -0.0190 -0.0286 74  PRO   B CA  
5025 C  C   . PRO   B 74  ? 0.1521 0.2037 0.1341 0.0041  -0.0099 -0.0224 74  PRO   B C   
5026 O  O   . PRO   B 74  ? 0.1618 0.2021 0.1786 0.0051  -0.0072 -0.0371 74  PRO   B O   
5027 C  CB  . PRO   B 74  ? 0.1846 0.2411 0.1208 -0.0030 -0.0140 -0.0178 74  PRO   B CB  
5028 C  CG  . PRO   B 74  ? 0.2098 0.2493 0.1548 -0.0028 -0.0121 -0.0081 74  PRO   B CG  
5029 C  CD  . PRO   B 74  ? 0.2018 0.2363 0.1371 0.0030  -0.0098 -0.0316 74  PRO   B CD  
5037 N  N   . LEU   B 75  ? 0.1525 0.1959 0.1205 0.0167  -0.0157 -0.0298 75  LEU   B N   
5038 C  CA  . LEU   B 75  ? 0.1575 0.1955 0.1275 0.0073  -0.0108 -0.0071 75  LEU   B CA  
5039 C  C   . LEU   B 75  ? 0.1616 0.2001 0.1348 0.0096  -0.0067 -0.0038 75  LEU   B C   
5040 O  O   . LEU   B 75  ? 0.1772 0.2029 0.1564 0.0013  -0.0058 0.0059  75  LEU   B O   
5041 C  CB  . LEU   B 75  ? 0.1687 0.1938 0.1103 -0.0084 -0.0143 -0.0028 75  LEU   B CB  
5042 C  CG  . LEU   B 75  ? 0.1965 0.2085 0.1467 -0.0324 -0.0045 0.0015  75  LEU   B CG  
5043 C  CD1 . LEU   B 75  ? 0.2319 0.2236 0.1502 -0.0422 0.0245  -0.0042 75  LEU   B CD1 
5044 C  CD2 . LEU   B 75  ? 0.2362 0.2257 0.2316 -0.0244 0.0044  0.0056  75  LEU   B CD2 
5056 N  N   . LYS   B 76  ? 0.1587 0.2109 0.1749 0.0029  0.0007  0.0083  76  LYS   B N   
5057 C  CA  . LYS   B 76  ? 0.1685 0.2183 0.1917 0.0008  0.0220  0.0048  76  LYS   B CA  
5058 C  C   . LYS   B 76  ? 0.1663 0.2036 0.1564 0.0021  0.0078  0.0258  76  LYS   B C   
5059 O  O   . LYS   B 76  ? 0.1715 0.1856 0.1579 -0.0001 0.0105  0.0225  76  LYS   B O   
5060 C  CB  . LYS   B 76  ? 0.1876 0.2242 0.2501 -0.0004 0.0442  -0.0259 76  LYS   B CB  
5061 C  CG  . LYS   B 76  ? 0.1976 0.2406 0.2844 0.0066  0.0380  -0.0367 76  LYS   B CG  
5062 C  CD  . LYS   B 76  ? 0.2013 0.2518 0.3331 0.0129  0.0253  -0.0431 76  LYS   B CD  
5063 C  CE  . LYS   B 76  ? 0.2095 0.2614 0.3873 0.0145  0.0039  -0.0491 76  LYS   B CE  
5064 N  NZ  . LYS   B 76  ? 0.2047 0.2574 0.4109 0.0117  -0.0110 -0.0668 76  LYS   B NZ  
5078 N  N   . VAL   B 77  ? 0.1712 0.2142 0.1552 0.0140  0.0122  0.0215  77  VAL   B N   
5079 C  CA  . VAL   B 77  ? 0.1761 0.2041 0.1732 0.0150  0.0201  0.0500  77  VAL   B CA  
5080 C  C   . VAL   B 77  ? 0.1620 0.1853 0.1677 0.0104  0.0294  0.0269  77  VAL   B C   
5081 O  O   . VAL   B 77  ? 0.1679 0.1804 0.1606 0.0190  0.0353  0.0191  77  VAL   B O   
5082 C  CB  . VAL   B 77  ? 0.1936 0.2128 0.2134 0.0186  0.0336  0.0672  77  VAL   B CB  
5083 C  CG1 . VAL   B 77  ? 0.1984 0.2070 0.2438 0.0087  0.0437  0.0889  77  VAL   B CG1 
5084 C  CG2 . VAL   B 77  ? 0.2074 0.2334 0.2342 0.0117  0.0008  0.0730  77  VAL   B CG2 
5094 N  N   . GLY   B 78  ? 0.1599 0.1656 0.1661 0.0121  0.0144  0.0262  78  GLY   B N   
5095 C  CA  . GLY   B 78  ? 0.1647 0.1673 0.1649 0.0135  0.0265  0.0129  78  GLY   B CA  
5096 C  C   . GLY   B 78  ? 0.1550 0.1658 0.1502 0.0144  0.0227  0.0193  78  GLY   B C   
5097 O  O   . GLY   B 78  ? 0.1557 0.1582 0.1690 0.0132  0.0159  0.0215  78  GLY   B O   
5101 N  N   . GLY   B 79  ? 0.1442 0.1675 0.1572 0.0132  0.0185  0.0135  79  GLY   B N   
5102 C  CA  . GLY   B 79  ? 0.1428 0.1581 0.1619 0.0081  0.0120  0.0039  79  GLY   B CA  
5103 C  C   . GLY   B 79  ? 0.1388 0.1474 0.1515 0.0153  0.0133  0.0017  79  GLY   B C   
5104 O  O   . GLY   B 79  ? 0.1449 0.1516 0.1644 0.0143  0.0135  0.0147  79  GLY   B O   
5108 N  N   . SER   B 80  ? 0.1432 0.1398 0.1571 0.0074  0.0216  0.0008  80  SER   B N   
5109 C  CA  . SER   B 80  ? 0.1357 0.1377 0.1605 0.0047  0.0053  0.0053  80  SER   B CA  
5110 C  C   . SER   B 80  ? 0.1378 0.1370 0.1560 0.0061  0.0006  -0.0001 80  SER   B C   
5111 O  O   . SER   B 80  ? 0.1550 0.1368 0.1842 0.0105  0.0110  -0.0071 80  SER   B O   
5112 C  CB  . SER   B 80  ? 0.1477 0.1421 0.1610 -0.0055 0.0056  0.0103  80  SER   B CB  
5113 O  OG  . SER   B 80  ? 0.1548 0.1481 0.1861 0.0009  -0.0084 0.0139  80  SER   B OG  
5119 N  N   . CYS   B 81  ? 0.1395 0.1276 0.1624 0.0045  -0.0072 0.0009  81  CYS   B N   
5120 C  CA  . CYS   B 81  ? 0.1410 0.1220 0.1597 0.0040  -0.0123 -0.0009 81  CYS   B CA  
5121 C  C   . CYS   B 81  ? 0.1448 0.1214 0.1303 -0.0003 -0.0089 -0.0022 81  CYS   B C   
5122 O  O   . CYS   B 81  ? 0.1661 0.1227 0.1496 0.0090  -0.0006 -0.0053 81  CYS   B O   
5123 C  CB  . CYS   B 81  ? 0.1509 0.1312 0.1536 -0.0015 -0.0140 0.0015  81  CYS   B CB  
5124 S  SG  . CYS   B 81  ? 0.1539 0.1557 0.1511 -0.0028 -0.0181 -0.0095 81  CYS   B SG  
5130 N  N   . VAL   B 82  ? 0.1499 0.1274 0.1431 0.0085  -0.0123 -0.0029 82  VAL   B N   
5131 C  CA  . VAL   B 82  ? 0.1495 0.1328 0.1391 -0.0037 -0.0043 0.0126  82  VAL   B CA  
5132 C  C   . VAL   B 82  ? 0.1565 0.1180 0.1482 -0.0030 -0.0091 -0.0029 82  VAL   B C   
5133 O  O   . VAL   B 82  ? 0.1590 0.1200 0.1953 -0.0030 0.0000  -0.0191 82  VAL   B O   
5134 C  CB  . VAL   B 82  ? 0.1571 0.1504 0.1576 -0.0004 -0.0043 0.0108  82  VAL   B CB  
5135 C  CG1 . VAL   B 82  ? 0.1700 0.1745 0.1621 0.0012  -0.0094 0.0184  82  VAL   B CG1 
5136 C  CG2 . VAL   B 82  ? 0.1631 0.1623 0.1759 -0.0108 -0.0272 0.0108  82  VAL   B CG2 
5146 N  N   . LEU   B 83  ? 0.1425 0.1253 0.1518 -0.0129 -0.0167 -0.0006 83  LEU   B N   
5147 C  CA  . LEU   B 83  ? 0.1476 0.1268 0.1495 -0.0093 -0.0164 -0.0061 83  LEU   B CA  
5148 C  C   . LEU   B 83  ? 0.1478 0.1249 0.1495 -0.0184 -0.0197 0.0031  83  LEU   B C   
5149 O  O   . LEU   B 83  ? 0.1523 0.1332 0.1376 -0.0205 -0.0134 0.0060  83  LEU   B O   
5150 C  CB  . LEU   B 83  ? 0.1497 0.1397 0.1482 -0.0149 -0.0178 -0.0157 83  LEU   B CB  
5151 C  CG  . LEU   B 83  ? 0.1703 0.1594 0.1566 -0.0167 -0.0102 -0.0065 83  LEU   B CG  
5152 C  CD1 . LEU   B 83  ? 0.1828 0.1644 0.1515 -0.0171 -0.0158 0.0025  83  LEU   B CD1 
5153 C  CD2 . LEU   B 83  ? 0.1896 0.1611 0.1938 -0.0077 -0.0104 -0.0282 83  LEU   B CD2 
5165 N  N   . SER   B 84  ? 0.1508 0.1381 0.1771 -0.0228 -0.0139 0.0028  84  SER   B N   
5166 C  CA  . SER   B 84  ? 0.1511 0.1564 0.1589 -0.0232 -0.0098 0.0176  84  SER   B CA  
5167 C  C   . SER   B 84  ? 0.1369 0.1756 0.1130 -0.0145 -0.0112 0.0168  84  SER   B C   
5168 O  O   . SER   B 84  ? 0.1480 0.1550 0.1314 -0.0164 -0.0118 -0.0030 84  SER   B O   
5169 C  CB  . SER   B 84  ? 0.1695 0.1620 0.2033 -0.0222 0.0170  0.0183  84  SER   B CB  
5170 O  OG  . SER   B 84  ? 0.1632 0.1755 0.2473 -0.0311 0.0117  0.0269  84  SER   B OG  
5176 N  N   . GLY   B 85  ? 0.1405 0.1897 0.1269 -0.0163 -0.0129 0.0233  85  GLY   B N   
5177 C  CA  . GLY   B 85  ? 0.1444 0.1945 0.1523 -0.0247 0.0038  -0.0099 85  GLY   B CA  
5178 C  C   . GLY   B 85  ? 0.1450 0.1822 0.1416 -0.0378 -0.0020 0.0025  85  GLY   B C   
5179 O  O   . GLY   B 85  ? 0.1612 0.1836 0.1402 -0.0515 0.0211  -0.0178 85  GLY   B O   
5183 N  N   . HIS   B 86  ? 0.1404 0.1699 0.1619 -0.0266 -0.0086 0.0024  86  HIS   B N   
5184 C  CA  . HIS   B 86  ? 0.1464 0.1681 0.1694 -0.0340 -0.0121 0.0124  86  HIS   B CA  
5185 C  C   . HIS   B 86  ? 0.1480 0.1820 0.1504 -0.0408 -0.0037 0.0206  86  HIS   B C   
5186 O  O   . HIS   B 86  ? 0.1593 0.1921 0.1569 -0.0317 0.0089  0.0196  86  HIS   B O   
5187 C  CB  . HIS   B 86  ? 0.1543 0.1712 0.1630 -0.0155 -0.0134 0.0018  86  HIS   B CB  
5188 C  CG  . HIS   B 86  ? 0.1509 0.1758 0.1529 -0.0079 -0.0104 0.0064  86  HIS   B CG  
5189 N  ND1 . HIS   B 86  ? 0.1653 0.2005 0.1836 -0.0225 -0.0120 -0.0086 86  HIS   B ND1 
5190 C  CD2 . HIS   B 86  ? 0.1528 0.1813 0.1652 -0.0032 -0.0185 0.0084  86  HIS   B CD2 
5191 C  CE1 . HIS   B 86  ? 0.1703 0.1943 0.1650 -0.0144 -0.0063 -0.0235 86  HIS   B CE1 
5192 N  NE2 . HIS   B 86  ? 0.1659 0.1854 0.1623 0.0040  -0.0004 -0.0023 86  HIS   B NE2 
5200 N  N   . ASN   B 87  ? 0.1492 0.1767 0.1585 -0.0278 0.0029  0.0181  87  ASN   B N   
5201 C  CA  . ASN   B 87  ? 0.1642 0.1946 0.1611 -0.0223 0.0184  0.0073  87  ASN   B CA  
5202 C  C   . ASN   B 87  ? 0.1773 0.1808 0.1535 -0.0299 0.0279  0.0009  87  ASN   B C   
5203 O  O   . ASN   B 87  ? 0.2035 0.1849 0.1852 -0.0271 0.0510  -0.0056 87  ASN   B O   
5204 C  CB  . ASN   B 87  ? 0.1640 0.2210 0.1910 -0.0133 0.0248  0.0087  87  ASN   B CB  
5205 C  CG  . ASN   B 87  ? 0.1768 0.2378 0.1957 0.0145  0.0369  0.0208  87  ASN   B CG  
5206 O  OD1 . ASN   B 87  ? 0.1700 0.2180 0.1857 0.0190  0.0464  0.0355  87  ASN   B OD1 
5207 N  ND2 . ASN   B 87  ? 0.2097 0.2507 0.2413 0.0221  0.0522  0.0162  87  ASN   B ND2 
5214 N  N   . LEU   B 88  ? 0.1621 0.1758 0.1457 -0.0277 0.0194  0.0025  88  LEU   B N   
5215 C  CA  . LEU   B 88  ? 0.1783 0.1698 0.1587 -0.0301 0.0028  -0.0049 88  LEU   B CA  
5216 C  C   . LEU   B 88  ? 0.1793 0.1562 0.1536 -0.0381 -0.0005 -0.0063 88  LEU   B C   
5217 O  O   . LEU   B 88  ? 0.2020 0.1641 0.1693 -0.0253 -0.0179 -0.0062 88  LEU   B O   
5218 C  CB  . LEU   B 88  ? 0.1872 0.1727 0.1698 -0.0321 -0.0061 0.0127  88  LEU   B CB  
5219 C  CG  . LEU   B 88  ? 0.2192 0.2028 0.1884 -0.0250 -0.0243 0.0327  88  LEU   B CG  
5220 C  CD1 . LEU   B 88  ? 0.2294 0.2373 0.2121 -0.0418 -0.0201 0.0462  88  LEU   B CD1 
5221 C  CD2 . LEU   B 88  ? 0.2498 0.2245 0.2551 0.0104  -0.0552 0.0120  88  LEU   B CD2 
5233 N  N   . ALA   B 89  ? 0.1590 0.1565 0.1573 -0.0375 0.0237  -0.0069 89  ALA   B N   
5234 C  CA  . ALA   B 89  ? 0.1572 0.1511 0.1273 -0.0325 0.0033  0.0108  89  ALA   B CA  
5235 C  C   . ALA   B 89  ? 0.1657 0.1533 0.1326 -0.0364 0.0101  0.0015  89  ALA   B C   
5236 O  O   . ALA   B 89  ? 0.1505 0.1611 0.1729 -0.0356 0.0101  -0.0251 89  ALA   B O   
5237 C  CB  . ALA   B 89  ? 0.1498 0.1478 0.1476 -0.0256 0.0075  0.0115  89  ALA   B CB  
5243 N  N   . LYS   B 90  ? 0.1996 0.1473 0.1369 -0.0455 -0.0035 0.0035  90  LYS   B N   
5244 C  CA  . LYS   B 90  ? 0.2093 0.1440 0.1289 -0.0391 -0.0064 0.0110  90  LYS   B CA  
5245 C  C   . LYS   B 90  ? 0.1896 0.1272 0.1442 -0.0296 -0.0065 0.0045  90  LYS   B C   
5246 O  O   . LYS   B 90  ? 0.1939 0.1487 0.1587 -0.0420 0.0012  0.0035  90  LYS   B O   
5247 C  CB  . LYS   B 90  ? 0.2247 0.1537 0.1593 -0.0342 -0.0037 0.0172  90  LYS   B CB  
5248 C  CG  . LYS   B 90  ? 0.2134 0.1642 0.1682 -0.0213 0.0072  0.0110  90  LYS   B CG  
5249 C  CD  . LYS   B 90  ? 0.2371 0.1863 0.2128 -0.0056 0.0215  0.0051  90  LYS   B CD  
5250 C  CE  . LYS   B 90  ? 0.2391 0.2011 0.2688 -0.0156 0.0314  -0.0007 90  LYS   B CE  
5251 N  NZ  . LYS   B 90  ? 0.2496 0.1913 0.2493 -0.0285 0.0477  -0.0011 90  LYS   B NZ  
5265 N  N   . HIS   B 91  ? 0.1701 0.1261 0.1271 -0.0271 -0.0087 0.0120  91  HIS   B N   
5266 C  CA  . HIS   B 91  ? 0.1593 0.1295 0.1443 -0.0232 -0.0070 0.0024  91  HIS   B CA  
5267 C  C   . HIS   B 91  ? 0.1461 0.1256 0.1217 -0.0202 -0.0069 0.0085  91  HIS   B C   
5268 O  O   . HIS   B 91  ? 0.1615 0.1325 0.1250 -0.0244 -0.0135 0.0019  91  HIS   B O   
5269 C  CB  . HIS   B 91  ? 0.1696 0.1321 0.1783 -0.0058 -0.0085 0.0126  91  HIS   B CB  
5270 C  CG  . HIS   B 91  ? 0.2111 0.1525 0.2437 0.0040  0.0226  0.0154  91  HIS   B CG  
5271 N  ND1 . HIS   B 91  ? 0.2425 0.1553 0.3113 0.0025  0.0303  0.0020  91  HIS   B ND1 
5272 C  CD2 . HIS   B 91  ? 0.2240 0.1792 0.3000 0.0191  0.0126  0.0514  91  HIS   B CD2 
5273 C  CE1 . HIS   B 91  ? 0.2470 0.1684 0.3302 0.0228  0.0320  0.0127  91  HIS   B CE1 
5274 N  NE2 . HIS   B 91  ? 0.2421 0.1819 0.3375 0.0331  0.0275  0.0533  91  HIS   B NE2 
5282 N  N   . CYS   B 92  ? 0.1417 0.1250 0.1271 -0.0189 -0.0004 0.0040  92  CYS   B N   
5283 C  CA  . CYS   B 92  ? 0.1389 0.1323 0.1119 -0.0174 -0.0017 -0.0003 92  CYS   B CA  
5284 C  C   . CYS   B 92  ? 0.1360 0.1222 0.1154 -0.0121 -0.0062 -0.0026 92  CYS   B C   
5285 O  O   . CYS   B 92  ? 0.1418 0.1307 0.1329 -0.0124 -0.0020 0.0023  92  CYS   B O   
5286 C  CB  . CYS   B 92  ? 0.1389 0.1326 0.1298 -0.0108 0.0016  -0.0076 92  CYS   B CB  
5287 S  SG  . CYS   B 92  ? 0.1401 0.1329 0.1363 -0.0095 -0.0054 0.0051  92  CYS   B SG  
5293 N  N   . LEU   B 93  ? 0.1279 0.1221 0.1216 -0.0120 -0.0023 -0.0025 93  LEU   B N   
5294 C  CA  . LEU   B 93  ? 0.1291 0.1249 0.1170 -0.0028 -0.0093 0.0003  93  LEU   B CA  
5295 C  C   . LEU   B 93  ? 0.1256 0.1264 0.1079 -0.0031 -0.0149 0.0106  93  LEU   B C   
5296 O  O   . LEU   B 93  ? 0.1314 0.1224 0.1348 -0.0035 -0.0058 0.0029  93  LEU   B O   
5297 C  CB  . LEU   B 93  ? 0.1329 0.1210 0.1377 0.0065  -0.0014 0.0064  93  LEU   B CB  
5298 C  CG  . LEU   B 93  ? 0.1281 0.1398 0.1532 -0.0040 0.0006  0.0176  93  LEU   B CG  
5299 C  CD1 . LEU   B 93  ? 0.1329 0.1493 0.1586 0.0064  0.0043  0.0014  93  LEU   B CD1 
5300 C  CD2 . LEU   B 93  ? 0.1313 0.1375 0.1685 -0.0020 -0.0069 0.0039  93  LEU   B CD2 
5312 N  N   . HIS   B 94  ? 0.1268 0.1235 0.1026 -0.0092 -0.0138 0.0109  94  HIS   B N   
5313 C  CA  . HIS   B 94  ? 0.1327 0.1257 0.1135 0.0002  -0.0046 0.0085  94  HIS   B CA  
5314 C  C   . HIS   B 94  ? 0.1275 0.1257 0.1301 -0.0000 0.0010  0.0165  94  HIS   B C   
5315 O  O   . HIS   B 94  ? 0.1309 0.1297 0.1891 -0.0011 0.0203  -0.0113 94  HIS   B O   
5316 C  CB  . HIS   B 94  ? 0.1304 0.1308 0.1206 0.0052  0.0022  0.0100  94  HIS   B CB  
5317 C  CG  . HIS   B 94  ? 0.1370 0.1233 0.1214 -0.0009 -0.0175 0.0033  94  HIS   B CG  
5318 N  ND1 . HIS   B 94  ? 0.1364 0.1323 0.1239 -0.0018 -0.0172 -0.0029 94  HIS   B ND1 
5319 C  CD2 . HIS   B 94  ? 0.1394 0.1230 0.1261 -0.0008 -0.0097 0.0050  94  HIS   B CD2 
5320 C  CE1 . HIS   B 94  ? 0.1356 0.1298 0.1284 -0.0071 -0.0135 0.0044  94  HIS   B CE1 
5321 N  NE2 . HIS   B 94  ? 0.1285 0.1333 0.1334 -0.0112 -0.0142 -0.0041 94  HIS   B NE2 
5329 N  N   . VAL   B 95  ? 0.1272 0.1244 0.1434 0.0016  0.0027  0.0155  95  VAL   B N   
5330 C  CA  . VAL   B 95  ? 0.1257 0.1314 0.1323 0.0052  0.0082  0.0162  95  VAL   B CA  
5331 C  C   . VAL   B 95  ? 0.1389 0.1265 0.1126 0.0001  0.0206  0.0086  95  VAL   B C   
5332 O  O   . VAL   B 95  ? 0.1413 0.1243 0.1551 0.0134  0.0078  0.0086  95  VAL   B O   
5333 C  CB  . VAL   B 95  ? 0.1332 0.1304 0.1296 -0.0011 -0.0053 0.0053  95  VAL   B CB  
5334 C  CG1 . VAL   B 95  ? 0.1404 0.1406 0.1671 -0.0043 0.0027  0.0135  95  VAL   B CG1 
5335 C  CG2 . VAL   B 95  ? 0.1366 0.1276 0.1352 0.0043  -0.0060 0.0061  95  VAL   B CG2 
5345 N  N   . VAL   B 96  ? 0.1446 0.1377 0.1308 0.0088  0.0181  0.0127  96  VAL   B N   
5346 C  CA  . VAL   B 96  ? 0.1523 0.1486 0.1156 0.0062  0.0197  0.0204  96  VAL   B CA  
5347 C  C   . VAL   B 96  ? 0.1545 0.1482 0.1374 0.0079  0.0161  0.0189  96  VAL   B C   
5348 O  O   . VAL   B 96  ? 0.1564 0.1569 0.1504 0.0032  0.0180  0.0094  96  VAL   B O   
5349 C  CB  . VAL   B 96  ? 0.1544 0.1685 0.1223 0.0143  0.0153  0.0185  96  VAL   B CB  
5350 C  CG1 . VAL   B 96  ? 0.1614 0.1780 0.1350 0.0142  0.0206  0.0020  96  VAL   B CG1 
5351 C  CG2 . VAL   B 96  ? 0.1713 0.1701 0.1367 0.0089  0.0134  -0.0000 96  VAL   B CG2 
5361 N  N   . GLY   B 97  ? 0.1572 0.1468 0.1417 0.0039  0.0113  0.0222  97  GLY   B N   
5362 C  CA  . GLY   B 97  ? 0.1738 0.1518 0.1336 0.0050  0.0074  0.0183  97  GLY   B CA  
5363 C  C   . GLY   B 97  ? 0.1940 0.1587 0.1589 0.0136  0.0164  0.0152  97  GLY   B C   
5364 O  O   . GLY   B 97  ? 0.2045 0.1703 0.1698 0.0156  0.0053  0.0150  97  GLY   B O   
5368 N  N   . PRO   B 98  ? 0.2092 0.1649 0.1751 0.0160  0.0433  0.0350  98  PRO   B N   
5369 C  CA  . PRO   B 98  ? 0.2260 0.1865 0.1836 0.0351  0.0637  0.0334  98  PRO   B CA  
5370 C  C   . PRO   B 98  ? 0.2315 0.1904 0.1617 0.0470  0.0625  0.0526  98  PRO   B C   
5371 O  O   . PRO   B 98  ? 0.2215 0.1810 0.1889 0.0375  0.0557  0.0483  98  PRO   B O   
5372 C  CB  . PRO   B 98  ? 0.2244 0.1870 0.1997 0.0331  0.0797  0.0381  98  PRO   B CB  
5373 C  CG  . PRO   B 98  ? 0.2111 0.1760 0.2054 0.0237  0.0642  0.0449  98  PRO   B CG  
5374 C  CD  . PRO   B 98  ? 0.1965 0.1592 0.2100 0.0198  0.0519  0.0441  98  PRO   B CD  
5382 N  N   . ASN   B 99  ? 0.2535 0.2085 0.1647 0.0696  0.0514  0.0376  99  ASN   B N   
5383 C  CA  . ASN   B 99  ? 0.2788 0.2198 0.1652 0.0825  0.0465  0.0574  99  ASN   B CA  
5384 C  C   . ASN   B 99  ? 0.3040 0.2534 0.2008 0.0803  0.0823  0.0829  99  ASN   B C   
5385 O  O   . ASN   B 99  ? 0.3227 0.2637 0.2068 0.0811  0.0776  0.0822  99  ASN   B O   
5386 C  CB  . ASN   B 99  ? 0.2858 0.2130 0.1692 0.0815  0.0356  0.0548  99  ASN   B CB  
5387 C  CG  . ASN   B 99  ? 0.2881 0.2242 0.2004 0.0729  0.0361  0.0413  99  ASN   B CG  
5388 O  OD1 . ASN   B 99  ? 0.2879 0.2188 0.2352 0.0787  0.0408  0.0470  99  ASN   B OD1 
5389 N  ND2 . ASN   B 99  ? 0.2897 0.2245 0.2031 0.0743  0.0121  0.0265  99  ASN   B ND2 
5396 N  N   A VAL   B 100 ? 0.3186 0.2648 0.2555 0.0618  0.0915  0.1111  100 VAL   B N   
5397 N  N   B VAL   B 100 ? 0.3227 0.2659 0.2521 0.0647  0.0771  0.0969  100 VAL   B N   
5398 C  CA  A VAL   B 100 ? 0.3412 0.2812 0.3154 0.0496  0.0855  0.1264  100 VAL   B CA  
5399 C  CA  B VAL   B 100 ? 0.3448 0.2796 0.3026 0.0529  0.0654  0.1068  100 VAL   B CA  
5400 C  C   A VAL   B 100 ? 0.3640 0.2868 0.2953 0.0520  0.0861  0.1456  100 VAL   B C   
5401 C  C   B VAL   B 100 ? 0.3650 0.2853 0.2967 0.0534  0.0661  0.1278  100 VAL   B C   
5402 O  O   A VAL   B 100 ? 0.3747 0.3064 0.3173 0.0495  0.1022  0.1341  100 VAL   B O   
5403 O  O   B VAL   B 100 ? 0.3710 0.2945 0.3096 0.0504  0.0722  0.1188  100 VAL   B O   
5404 C  CB  A VAL   B 100 ? 0.3473 0.2953 0.3913 0.0274  0.0786  0.1257  100 VAL   B CB  
5405 C  CB  B VAL   B 100 ? 0.3493 0.2887 0.3553 0.0380  0.0550  0.0981  100 VAL   B CB  
5406 C  CG1 A VAL   B 100 ? 0.3518 0.3008 0.4162 0.0251  0.0778  0.1259  100 VAL   B CG1 
5407 C  CG1 B VAL   B 100 ? 0.3517 0.2916 0.3719 0.0353  0.0522  0.0967  100 VAL   B CG1 
5408 C  CG2 A VAL   B 100 ? 0.3467 0.2981 0.4096 0.0152  0.0787  0.1293  100 VAL   B CG2 
5409 C  CG2 B VAL   B 100 ? 0.3500 0.2914 0.3703 0.0310  0.0522  0.0951  100 VAL   B CG2 
5428 N  N   . ASN   B 101 ? 0.3808 0.2885 0.2930 0.0568  0.0599  0.1439  101 ASN   B N   
5429 C  CA  . ASN   B 101 ? 0.4218 0.3068 0.3163 0.0573  0.0247  0.1377  101 ASN   B CA  
5430 C  C   . ASN   B 101 ? 0.4791 0.3595 0.3372 0.0518  0.0166  0.1302  101 ASN   B C   
5431 O  O   . ASN   B 101 ? 0.4804 0.3666 0.3527 0.0594  0.0266  0.1082  101 ASN   B O   
5432 C  CB  . ASN   B 101 ? 0.4071 0.2819 0.3289 0.0497  0.0158  0.1212  101 ASN   B CB  
5433 C  CG  . ASN   B 101 ? 0.3938 0.2583 0.3291 0.0408  0.0229  0.1229  101 ASN   B CG  
5434 O  OD1 . ASN   B 101 ? 0.3923 0.2580 0.3534 0.0309  0.0469  0.1161  101 ASN   B OD1 
5435 N  ND2 . ASN   B 101 ? 0.3870 0.2547 0.3227 0.0371  0.0163  0.1041  101 ASN   B ND2 
5443 N  N   A LYS   B 102 ? 0.5081 0.3835 0.3595 0.0424  0.0161  0.1216  102 LYS   B N   
5444 N  N   B LYS   B 102 ? 0.5033 0.3852 0.3658 0.0433  0.0128  0.1193  102 LYS   B N   
5445 C  CA  A LYS   B 102 ? 0.5344 0.4131 0.3879 0.0292  0.0156  0.1033  102 LYS   B CA  
5446 C  CA  B LYS   B 102 ? 0.5250 0.4124 0.3950 0.0331  0.0119  0.1032  102 LYS   B CA  
5447 C  C   A LYS   B 102 ? 0.5356 0.4162 0.3667 0.0304  0.0205  0.1107  102 LYS   B C   
5448 C  C   B LYS   B 102 ? 0.5285 0.4160 0.3776 0.0315  0.0206  0.1103  102 LYS   B C   
5449 O  O   A LYS   B 102 ? 0.5447 0.4180 0.3670 0.0315  0.0091  0.1091  102 LYS   B O   
5450 O  O   B LYS   B 102 ? 0.5337 0.4182 0.3811 0.0316  0.0125  0.1109  102 LYS   B O   
5451 C  CB  A LYS   B 102 ? 0.5546 0.4375 0.4504 0.0162  0.0207  0.0670  102 LYS   B CB  
5452 C  CB  B LYS   B 102 ? 0.5398 0.4337 0.4474 0.0258  0.0095  0.0738  102 LYS   B CB  
5453 C  CG  A LYS   B 102 ? 0.5715 0.4592 0.5066 0.0059  0.0286  0.0347  102 LYS   B CG  
5454 C  CG  B LYS   B 102 ? 0.5516 0.4518 0.4925 0.0206  0.0101  0.0469  102 LYS   B CG  
5455 C  CD  A LYS   B 102 ? 0.5873 0.4771 0.5680 -0.0017 0.0379  0.0100  102 LYS   B CD  
5456 C  CD  B LYS   B 102 ? 0.5619 0.4664 0.5395 0.0169  0.0127  0.0250  102 LYS   B CD  
5457 C  CE  A LYS   B 102 ? 0.5994 0.4896 0.6123 -0.0072 0.0430  -0.0106 102 LYS   B CE  
5458 C  CE  B LYS   B 102 ? 0.5692 0.4764 0.5725 0.0143  0.0135  0.0074  102 LYS   B CE  
5459 N  NZ  A LYS   B 102 ? 0.6065 0.4966 0.6375 -0.0095 0.0437  -0.0236 102 LYS   B NZ  
5460 N  NZ  B LYS   B 102 ? 0.5735 0.4820 0.5916 0.0132  0.0130  -0.0032 102 LYS   B NZ  
5487 N  N   . GLY   B 103 ? 0.5240 0.4143 0.3658 0.0304  0.0409  0.1089  103 GLY   B N   
5488 C  CA  . GLY   B 103 ? 0.5052 0.4104 0.3735 0.0345  0.0747  0.0867  103 GLY   B CA  
5489 C  C   . GLY   B 103 ? 0.4810 0.4004 0.3639 0.0365  0.1061  0.0674  103 GLY   B C   
5490 O  O   . GLY   B 103 ? 0.4868 0.4072 0.3783 0.0373  0.1149  0.0643  103 GLY   B O   
5495 N  N   A GLU   B 104 ? 0.4611 0.3865 0.3416 0.0442  0.1301  0.0567  104 GLU   B N   
5496 N  N   B GLU   B 104 ? 0.4684 0.3940 0.3621 0.0304  0.1019  0.0534  104 GLU   B N   
5497 C  CA  A GLU   B 104 ? 0.4396 0.3728 0.3148 0.0539  0.1433  0.0511  104 GLU   B CA  
5498 C  CA  B GLU   B 104 ? 0.4543 0.3867 0.3535 0.0249  0.0953  0.0410  104 GLU   B CA  
5499 C  C   A GLU   B 104 ? 0.4417 0.3804 0.3299 0.0348  0.1823  0.0591  104 GLU   B C   
5500 C  C   B GLU   B 104 ? 0.4525 0.3878 0.3697 0.0161  0.1149  0.0402  104 GLU   B C   
5501 O  O   A GLU   B 104 ? 0.4469 0.3865 0.3588 0.0255  0.1816  0.0605  104 GLU   B O   
5502 O  O   B GLU   B 104 ? 0.4550 0.3912 0.3827 0.0123  0.1135  0.0384  104 GLU   B O   
5503 C  CB  A GLU   B 104 ? 0.4221 0.3510 0.3025 0.0850  0.1010  0.0247  104 GLU   B CB  
5504 C  CB  B GLU   B 104 ? 0.4444 0.3773 0.3367 0.0288  0.0667  0.0235  104 GLU   B CB  
5505 C  CG  A GLU   B 104 ? 0.4058 0.3342 0.2826 0.1143  0.0561  -0.0072 104 GLU   B CG  
5506 C  CG  B GLU   B 104 ? 0.4361 0.3699 0.3194 0.0324  0.0380  0.0026  104 GLU   B CG  
5507 C  CD  A GLU   B 104 ? 0.3929 0.3240 0.2631 0.1365  0.0194  -0.0269 104 GLU   B CD  
5508 C  CD  B GLU   B 104 ? 0.4305 0.3646 0.3052 0.0343  0.0148  -0.0131 104 GLU   B CD  
5509 O  OE1 A GLU   B 104 ? 0.3818 0.3118 0.2206 0.1506  0.0226  -0.0229 104 GLU   B OE1 
5510 O  OE1 B GLU   B 104 ? 0.4271 0.3602 0.2877 0.0342  0.0117  -0.0145 104 GLU   B OE1 
5511 O  OE2 A GLU   B 104 ? 0.3923 0.3300 0.2717 0.1360  -0.0105 -0.0420 104 GLU   B OE2 
5512 O  OE2 B GLU   B 104 ? 0.4297 0.3652 0.3057 0.0342  -0.0011 -0.0241 104 GLU   B OE2 
5525 N  N   A ASP   B 105 ? 0.4336 0.3808 0.3199 0.0249  0.2102  0.0662  105 ASP   B N   
5526 N  N   B ASP   B 105 ? 0.4457 0.3844 0.3709 0.0110  0.1340  0.0422  105 ASP   B N   
5527 C  CA  A ASP   B 105 ? 0.4330 0.3836 0.3475 0.0179  0.2149  0.0523  105 ASP   B CA  
5528 C  CA  B ASP   B 105 ? 0.4405 0.3799 0.3804 0.0069  0.1472  0.0387  105 ASP   B CA  
5529 C  C   A ASP   B 105 ? 0.4147 0.3556 0.3241 0.0124  0.2116  0.0499  105 ASP   B C   
5530 C  C   B ASP   B 105 ? 0.4248 0.3582 0.3535 0.0064  0.1756  0.0435  105 ASP   B C   
5531 O  O   A ASP   B 105 ? 0.3947 0.3459 0.3120 0.0143  0.2036  0.0460  105 ASP   B O   
5532 O  O   B ASP   B 105 ? 0.4214 0.3569 0.3428 0.0069  0.1827  0.0441  105 ASP   B O   
5533 C  CB  A ASP   B 105 ? 0.4494 0.4100 0.4233 0.0199  0.2121  0.0340  105 ASP   B CB  
5534 C  CB  B ASP   B 105 ? 0.4477 0.3934 0.4179 0.0047  0.1335  0.0293  105 ASP   B CB  
5535 C  CG  A ASP   B 105 ? 0.4613 0.4316 0.4923 0.0189  0.2193  0.0212  105 ASP   B CG  
5536 C  CG  B ASP   B 105 ? 0.4536 0.4033 0.4542 0.0014  0.1263  0.0237  105 ASP   B CG  
5537 O  OD1 A ASP   B 105 ? 0.4614 0.4372 0.4971 0.0102  0.2361  0.0314  105 ASP   B OD1 
5538 O  OD1 B ASP   B 105 ? 0.4551 0.4074 0.4628 -0.0026 0.1264  0.0259  105 ASP   B OD1 
5539 O  OD2 A ASP   B 105 ? 0.4684 0.4435 0.5362 0.0246  0.2059  0.0064  105 ASP   B OD2 
5540 O  OD2 B ASP   B 105 ? 0.4540 0.4068 0.4655 0.0010  0.1252  0.0218  105 ASP   B OD2 
5549 N  N   . ILE   B 106 ? 0.4087 0.3334 0.3464 0.0085  0.1910  0.0501  106 ILE   B N   
5550 C  CA  . ILE   B 106 ? 0.3764 0.2893 0.3683 0.0048  0.1933  0.0411  106 ILE   B CA  
5551 C  C   . ILE   B 106 ? 0.3301 0.2740 0.3616 0.0059  0.1944  0.0239  106 ILE   B C   
5552 O  O   . ILE   B 106 ? 0.3226 0.2419 0.3825 0.0025  0.1956  0.0238  106 ILE   B O   
5553 C  CB  . ILE   B 106 ? 0.3967 0.2767 0.3947 -0.0008 0.1858  0.0494  106 ILE   B CB  
5554 C  CG1 . ILE   B 106 ? 0.4029 0.2706 0.4026 0.0170  0.1728  0.0385  106 ILE   B CG1 
5555 C  CG2 . ILE   B 106 ? 0.4061 0.2829 0.4231 -0.0130 0.1832  0.0526  106 ILE   B CG2 
5556 C  CD1 . ILE   B 106 ? 0.4050 0.2690 0.4022 0.0299  0.1627  0.0401  106 ILE   B CD1 
5569 N  N   A GLN   B 107 ? 0.3105 0.2845 0.3745 -0.0028 0.1917  0.0276  107 GLN   B N   
5570 N  N   B GLN   B 107 ? 0.3202 0.2859 0.3679 0.0008  0.1721  0.0201  107 GLN   B N   
5571 C  CA  A GLN   B 107 ? 0.2887 0.2942 0.3719 -0.0134 0.1865  0.0305  107 GLN   B CA  
5572 C  CA  B GLN   B 107 ? 0.3085 0.2951 0.3670 -0.0036 0.1477  0.0182  107 GLN   B CA  
5573 C  C   A GLN   B 107 ? 0.2628 0.2731 0.3436 -0.0041 0.1467  0.0201  107 GLN   B C   
5574 C  C   B GLN   B 107 ? 0.2774 0.2770 0.3336 0.0017  0.1315  0.0140  107 GLN   B C   
5575 O  O   A GLN   B 107 ? 0.2531 0.2732 0.3935 0.0085  0.1049  -0.0057 107 GLN   B O   
5576 O  O   B GLN   B 107 ? 0.2762 0.2806 0.3552 0.0056  0.1088  -0.0013 107 GLN   B O   
5577 C  CB  A GLN   B 107 ? 0.3183 0.3342 0.4362 -0.0209 0.1692  0.0337  107 GLN   B CB  
5578 C  CB  B GLN   B 107 ? 0.3347 0.3244 0.4149 -0.0090 0.1234  0.0190  107 GLN   B CB  
5579 C  CG  A GLN   B 107 ? 0.3531 0.3706 0.4987 -0.0217 0.1331  0.0336  107 GLN   B CG  
5580 C  CG  B GLN   B 107 ? 0.3596 0.3498 0.4599 -0.0122 0.0946  0.0200  107 GLN   B CG  
5581 C  CD  A GLN   B 107 ? 0.3783 0.3977 0.5461 -0.0268 0.1069  0.0387  107 GLN   B CD  
5582 C  CD  B GLN   B 107 ? 0.3781 0.3688 0.4964 -0.0173 0.0731  0.0231  107 GLN   B CD  
5583 O  OE1 A GLN   B 107 ? 0.3887 0.4081 0.5619 -0.0300 0.1065  0.0360  107 GLN   B OE1 
5584 O  OE1 B GLN   B 107 ? 0.3855 0.3762 0.5075 -0.0207 0.0709  0.0221  107 GLN   B OE1 
5585 N  NE2 A GLN   B 107 ? 0.3885 0.4064 0.5640 -0.0241 0.0907  0.0436  107 GLN   B NE2 
5586 N  NE2 B GLN   B 107 ? 0.3849 0.3754 0.5111 -0.0166 0.0628  0.0254  107 GLN   B NE2 
5603 N  N   . LEU   B 108 ? 0.2449 0.2547 0.3023 0.0109  0.1277  0.0183  108 LEU   B N   
5604 C  CA  . LEU   B 108 ? 0.2290 0.2366 0.2564 0.0252  0.0832  0.0260  108 LEU   B CA  
5605 C  C   . LEU   B 108 ? 0.1954 0.1887 0.2432 0.0251  0.0494  0.0256  108 LEU   B C   
5606 O  O   . LEU   B 108 ? 0.1892 0.1771 0.2251 0.0217  0.0345  0.0150  108 LEU   B O   
5607 C  CB  . LEU   B 108 ? 0.2478 0.2635 0.2405 0.0263  0.0873  0.0315  108 LEU   B CB  
5608 C  CG  . LEU   B 108 ? 0.2630 0.2969 0.2401 0.0305  0.0719  0.0091  108 LEU   B CG  
5609 C  CD1 . LEU   B 108 ? 0.2720 0.3140 0.2291 0.0258  0.0667  0.0091  108 LEU   B CD1 
5610 C  CD2 . LEU   B 108 ? 0.2759 0.3093 0.2522 0.0386  0.0560  -0.0030 108 LEU   B CD2 
5623 N  N   . LEU   B 109 ? 0.1773 0.1620 0.2359 0.0168  0.0465  0.0248  109 LEU   B N   
5624 C  CA  . LEU   B 109 ? 0.1579 0.1435 0.2469 0.0089  0.0460  0.0250  109 LEU   B CA  
5625 C  C   . LEU   B 109 ? 0.1452 0.1312 0.2405 0.0008  0.0422  0.0131  109 LEU   B C   
5626 O  O   . LEU   B 109 ? 0.1459 0.1352 0.2309 0.0063  0.0308  0.0266  109 LEU   B O   
5627 C  CB  . LEU   B 109 ? 0.1679 0.1356 0.2513 0.0004  0.0332  0.0335  109 LEU   B CB  
5628 C  CG  . LEU   B 109 ? 0.1665 0.1332 0.2423 0.0037  0.0172  0.0208  109 LEU   B CG  
5629 C  CD1 . LEU   B 109 ? 0.1692 0.1450 0.2225 0.0057  0.0159  0.0154  109 LEU   B CD1 
5630 C  CD2 . LEU   B 109 ? 0.1803 0.1374 0.2509 0.0038  0.0159  0.0137  109 LEU   B CD2 
5642 N  N   . LYS   B 110 ? 0.1481 0.1308 0.2370 -0.0063 0.0328  0.0175  110 LYS   B N   
5643 C  CA  . LYS   B 110 ? 0.1490 0.1326 0.2239 0.0016  0.0331  0.0168  110 LYS   B CA  
5644 C  C   . LYS   B 110 ? 0.1382 0.1317 0.2216 0.0006  0.0304  0.0115  110 LYS   B C   
5645 O  O   . LYS   B 110 ? 0.1339 0.1351 0.2138 -0.0008 0.0216  0.0046  110 LYS   B O   
5646 C  CB  . LYS   B 110 ? 0.1506 0.1344 0.2390 -0.0018 0.0270  0.0171  110 LYS   B CB  
5647 C  CG  . LYS   B 110 ? 0.1523 0.1374 0.2498 -0.0113 0.0180  0.0206  110 LYS   B CG  
5648 C  CD  . LYS   B 110 ? 0.1563 0.1362 0.2460 -0.0088 0.0176  0.0141  110 LYS   B CD  
5649 C  CE  . LYS   B 110 ? 0.1433 0.1493 0.2640 -0.0044 0.0127  0.0053  110 LYS   B CE  
5650 N  NZ  . LYS   B 110 ? 0.1490 0.1621 0.2660 0.0040  0.0069  0.0022  110 LYS   B NZ  
5664 N  N   . SER   B 111 ? 0.1417 0.1311 0.2287 0.0013  0.0255  0.0146  111 SER   B N   
5665 C  CA  . SER   B 111 ? 0.1494 0.1377 0.2053 0.0015  0.0152  0.0163  111 SER   B CA  
5666 C  C   . SER   B 111 ? 0.1441 0.1329 0.1929 0.0020  0.0172  0.0057  111 SER   B C   
5667 O  O   . SER   B 111 ? 0.1428 0.1359 0.2029 -0.0006 0.0224  0.0039  111 SER   B O   
5668 C  CB  . SER   B 111 ? 0.1620 0.1556 0.2071 0.0090  0.0317  0.0253  111 SER   B CB  
5669 O  OG  . SER   B 111 ? 0.1833 0.1918 0.2114 0.0098  0.0391  0.0299  111 SER   B OG  
5675 N  N   . ALA   B 112 ? 0.1364 0.1386 0.2024 0.0049  0.0266  0.0175  112 ALA   B N   
5676 C  CA  . ALA   B 112 ? 0.1348 0.1423 0.1799 0.0004  0.0114  0.0032  112 ALA   B CA  
5677 C  C   . ALA   B 112 ? 0.1316 0.1369 0.1740 0.0032  0.0145  -0.0016 112 ALA   B C   
5678 O  O   . ALA   B 112 ? 0.1278 0.1374 0.1980 -0.0029 0.0139  0.0040  112 ALA   B O   
5679 C  CB  . ALA   B 112 ? 0.1451 0.1445 0.1808 0.0050  0.0092  0.0101  112 ALA   B CB  
5685 N  N   . TYR   B 113 ? 0.1318 0.1208 0.1875 0.0003  0.0129  0.0023  113 TYR   B N   
5686 C  CA  . TYR   B 113 ? 0.1200 0.1223 0.1829 -0.0008 0.0262  -0.0016 113 TYR   B CA  
5687 C  C   . TYR   B 113 ? 0.1210 0.1219 0.1766 -0.0100 0.0173  -0.0017 113 TYR   B C   
5688 O  O   . TYR   B 113 ? 0.1293 0.1194 0.1751 -0.0052 0.0130  -0.0041 113 TYR   B O   
5689 C  CB  . TYR   B 113 ? 0.1322 0.1094 0.1994 -0.0024 0.0152  0.0092  113 TYR   B CB  
5690 C  CG  . TYR   B 113 ? 0.1318 0.1175 0.2110 -0.0068 0.0079  0.0121  113 TYR   B CG  
5691 C  CD1 . TYR   B 113 ? 0.1355 0.1183 0.2211 -0.0038 0.0153  0.0188  113 TYR   B CD1 
5692 C  CD2 . TYR   B 113 ? 0.1451 0.1152 0.2102 0.0004  0.0024  0.0094  113 TYR   B CD2 
5693 C  CE1 . TYR   B 113 ? 0.1439 0.1265 0.2180 0.0004  0.0269  0.0068  113 TYR   B CE1 
5694 C  CE2 . TYR   B 113 ? 0.1505 0.1139 0.2057 0.0014  0.0083  0.0148  113 TYR   B CE2 
5695 C  CZ  . TYR   B 113 ? 0.1385 0.1207 0.2214 0.0103  0.0109  0.0035  113 TYR   B CZ  
5696 O  OH  . TYR   B 113 ? 0.1533 0.1150 0.2555 0.0079  0.0152  0.0043  113 TYR   B OH  
5706 N  N   . GLU   B 114 ? 0.1297 0.1157 0.1959 -0.0028 0.0216  0.0001  114 GLU   B N   
5707 C  CA  . GLU   B 114 ? 0.1213 0.1154 0.1896 0.0031  0.0100  0.0054  114 GLU   B CA  
5708 C  C   . GLU   B 114 ? 0.1196 0.1150 0.1870 0.0030  0.0164  0.0003  114 GLU   B C   
5709 O  O   . GLU   B 114 ? 0.1177 0.1201 0.1952 0.0037  -0.0000 0.0045  114 GLU   B O   
5710 C  CB  . GLU   B 114 ? 0.1239 0.1228 0.2044 -0.0017 0.0161  0.0062  114 GLU   B CB  
5711 C  CG  . GLU   B 114 ? 0.1298 0.1225 0.2034 -0.0010 0.0151  -0.0008 114 GLU   B CG  
5712 C  CD  . GLU   B 114 ? 0.1251 0.1248 0.2183 -0.0074 0.0101  0.0022  114 GLU   B CD  
5713 O  OE1 . GLU   B 114 ? 0.1248 0.1394 0.2156 -0.0041 0.0204  0.0070  114 GLU   B OE1 
5714 O  OE2 . GLU   B 114 ? 0.1206 0.1438 0.2352 -0.0115 0.0117  0.0078  114 GLU   B OE2 
5721 N  N   . ASN   B 115 ? 0.1220 0.1124 0.1896 0.0005  0.0083  0.0093  115 ASN   B N   
5722 C  CA  . ASN   B 115 ? 0.1262 0.1196 0.1742 -0.0114 0.0060  0.0068  115 ASN   B CA  
5723 C  C   . ASN   B 115 ? 0.1225 0.1190 0.1681 -0.0094 0.0007  0.0043  115 ASN   B C   
5724 O  O   . ASN   B 115 ? 0.1308 0.1224 0.1760 -0.0084 0.0069  0.0011  115 ASN   B O   
5725 C  CB  . ASN   B 115 ? 0.1302 0.1341 0.1715 -0.0084 0.0177  0.0055  115 ASN   B CB  
5726 C  CG  . ASN   B 115 ? 0.1383 0.1378 0.1750 0.0088  0.0010  0.0062  115 ASN   B CG  
5727 O  OD1 . ASN   B 115 ? 0.1867 0.1431 0.1908 0.0020  0.0074  -0.0122 115 ASN   B OD1 
5728 N  ND2 . ASN   B 115 ? 0.1372 0.1445 0.1709 0.0023  0.0024  0.0082  115 ASN   B ND2 
5735 N  N   . PHE   B 116 ? 0.1268 0.1169 0.1615 -0.0020 0.0059  0.0038  116 PHE   B N   
5736 C  CA  . PHE   B 116 ? 0.1288 0.1235 0.1641 -0.0106 -0.0016 -0.0019 116 PHE   B CA  
5737 C  C   . PHE   B 116 ? 0.1252 0.1129 0.1569 -0.0122 0.0020  0.0004  116 PHE   B C   
5738 O  O   . PHE   B 116 ? 0.1328 0.1230 0.1681 -0.0029 -0.0004 0.0051  116 PHE   B O   
5739 C  CB  . PHE   B 116 ? 0.1199 0.1190 0.1556 -0.0036 0.0001  0.0054  116 PHE   B CB  
5740 C  CG  . PHE   B 116 ? 0.1197 0.1184 0.1710 -0.0030 -0.0020 -0.0000 116 PHE   B CG  
5741 C  CD1 . PHE   B 116 ? 0.1364 0.1249 0.1798 0.0003  0.0010  0.0015  116 PHE   B CD1 
5742 C  CD2 . PHE   B 116 ? 0.1309 0.1267 0.1657 -0.0028 0.0096  -0.0101 116 PHE   B CD2 
5743 C  CE1 . PHE   B 116 ? 0.1361 0.1299 0.1774 -0.0035 -0.0063 0.0026  116 PHE   B CE1 
5744 C  CE2 . PHE   B 116 ? 0.1324 0.1238 0.1693 0.0045  0.0070  -0.0083 116 PHE   B CE2 
5745 C  CZ  . PHE   B 116 ? 0.1250 0.1292 0.1778 -0.0015 -0.0050 0.0013  116 PHE   B CZ  
5755 N  N   . ASN   B 117 ? 0.1256 0.1151 0.1838 -0.0019 -0.0049 0.0040  117 ASN   B N   
5756 C  CA  . ASN   B 117 ? 0.1349 0.1196 0.1781 0.0025  -0.0081 0.0032  117 ASN   B CA  
5757 C  C   . ASN   B 117 ? 0.1398 0.1234 0.1890 0.0009  -0.0095 0.0062  117 ASN   B C   
5758 O  O   . ASN   B 117 ? 0.1426 0.1303 0.2139 -0.0060 -0.0308 0.0073  117 ASN   B O   
5759 C  CB  . ASN   B 117 ? 0.1307 0.1232 0.1911 0.0010  -0.0053 0.0034  117 ASN   B CB  
5760 C  CG  . ASN   B 117 ? 0.1264 0.1310 0.1927 0.0059  0.0026  -0.0071 117 ASN   B CG  
5761 O  OD1 . ASN   B 117 ? 0.1492 0.1276 0.2088 -0.0121 0.0114  -0.0024 117 ASN   B OD1 
5762 N  ND2 . ASN   B 117 ? 0.1328 0.1378 0.1783 -0.0019 0.0084  -0.0028 117 ASN   B ND2 
5769 N  N   . GLN   B 118 ? 0.1386 0.1132 0.1839 0.0007  -0.0142 -0.0006 118 GLN   B N   
5770 C  CA  . GLN   B 118 ? 0.1456 0.1190 0.1906 0.0067  -0.0070 0.0010  118 GLN   B CA  
5771 C  C   . GLN   B 118 ? 0.1402 0.1139 0.2016 -0.0003 -0.0074 -0.0035 118 GLN   B C   
5772 O  O   . GLN   B 118 ? 0.1555 0.1157 0.2389 -0.0040 0.0049  0.0017  118 GLN   B O   
5773 C  CB  . GLN   B 118 ? 0.1532 0.1248 0.1958 0.0113  -0.0119 -0.0083 118 GLN   B CB  
5774 C  CG  . GLN   B 118 ? 0.1586 0.1330 0.1888 0.0156  -0.0086 -0.0126 118 GLN   B CG  
5775 C  CD  . GLN   B 118 ? 0.1596 0.1272 0.2063 0.0096  -0.0072 -0.0149 118 GLN   B CD  
5776 O  OE1 . GLN   B 118 ? 0.1686 0.1208 0.2158 0.0094  0.0040  -0.0021 118 GLN   B OE1 
5777 N  NE2 . GLN   B 118 ? 0.1585 0.1314 0.2131 0.0069  -0.0228 -0.0030 118 GLN   B NE2 
5786 N  N   . HIS   B 119 ? 0.1481 0.1155 0.1839 -0.0076 -0.0136 0.0104  119 HIS   B N   
5787 C  CA  . HIS   B 119 ? 0.1546 0.1340 0.1609 -0.0036 -0.0128 0.0037  119 HIS   B CA  
5788 C  C   . HIS   B 119 ? 0.1554 0.1432 0.1569 -0.0041 -0.0246 0.0110  119 HIS   B C   
5789 O  O   . HIS   B 119 ? 0.1596 0.1344 0.1846 -0.0298 -0.0123 0.0125  119 HIS   B O   
5790 C  CB  . HIS   B 119 ? 0.1549 0.1441 0.1726 -0.0002 -0.0117 0.0017  119 HIS   B CB  
5791 C  CG  . HIS   B 119 ? 0.1608 0.1648 0.1859 0.0106  -0.0344 -0.0162 119 HIS   B CG  
5792 N  ND1 . HIS   B 119 ? 0.1804 0.1804 0.2297 0.0053  -0.0475 -0.0313 119 HIS   B ND1 
5793 C  CD2 . HIS   B 119 ? 0.1792 0.1914 0.1844 0.0329  -0.0365 -0.0199 119 HIS   B CD2 
5794 C  CE1 . HIS   B 119 ? 0.1991 0.1975 0.2217 0.0153  -0.0611 -0.0427 119 HIS   B CE1 
5795 N  NE2 . HIS   B 119 ? 0.2032 0.2104 0.2033 0.0324  -0.0467 -0.0288 119 HIS   B NE2 
5803 N  N   A GLU   B 120 ? 0.1793 0.1381 0.1442 -0.0111 -0.0300 0.0186  120 GLU   B N   
5804 N  N   B GLU   B 120 ? 0.1787 0.1557 0.1692 -0.0078 -0.0229 0.0139  120 GLU   B N   
5805 C  CA  A GLU   B 120 ? 0.2101 0.1480 0.1584 -0.0034 -0.0418 0.0299  120 GLU   B CA  
5806 C  CA  B GLU   B 120 ? 0.2047 0.1719 0.1900 -0.0048 -0.0254 0.0190  120 GLU   B CA  
5807 C  C   A GLU   B 120 ? 0.1873 0.1451 0.1594 -0.0128 -0.0334 0.0218  120 GLU   B C   
5808 C  C   B GLU   B 120 ? 0.1878 0.1575 0.1703 -0.0119 -0.0238 0.0173  120 GLU   B C   
5809 O  O   A GLU   B 120 ? 0.1765 0.1528 0.1634 -0.0136 -0.0283 0.0097  120 GLU   B O   
5810 O  O   B GLU   B 120 ? 0.1832 0.1621 0.1645 -0.0112 -0.0213 0.0115  120 GLU   B O   
5811 C  CB  A GLU   B 120 ? 0.2662 0.1828 0.2315 0.0104  -0.0679 0.0528  120 GLU   B CB  
5812 C  CB  B GLU   B 120 ? 0.2485 0.2081 0.2555 0.0054  -0.0349 0.0304  120 GLU   B CB  
5813 C  CG  A GLU   B 120 ? 0.3132 0.2529 0.3414 0.0187  -0.0799 0.0738  120 GLU   B CG  
5814 C  CG  B GLU   B 120 ? 0.2870 0.2547 0.3347 0.0116  -0.0390 0.0454  120 GLU   B CG  
5815 C  CD  A GLU   B 120 ? 0.3480 0.3150 0.4426 0.0177  -0.0834 0.0864  120 GLU   B CD  
5816 C  CD  B GLU   B 120 ? 0.3195 0.2981 0.4074 0.0135  -0.0388 0.0561  120 GLU   B CD  
5817 O  OE1 A GLU   B 120 ? 0.3625 0.3334 0.4770 0.0101  -0.0760 0.1003  120 GLU   B OE1 
5818 O  OE1 B GLU   B 120 ? 0.3302 0.3053 0.4322 0.0115  -0.0380 0.0626  120 GLU   B OE1 
5819 O  OE2 A GLU   B 120 ? 0.3618 0.3425 0.4928 0.0154  -0.0839 0.0777  120 GLU   B OE2 
5820 O  OE2 B GLU   B 120 ? 0.3295 0.3130 0.4333 0.0133  -0.0406 0.0589  120 GLU   B OE2 
5833 N  N   . VAL   B 121 ? 0.1732 0.1387 0.1667 -0.0193 -0.0232 0.0192  121 VAL   B N   
5834 C  CA  . VAL   B 121 ? 0.1696 0.1479 0.1484 -0.0178 -0.0185 0.0165  121 VAL   B CA  
5835 C  C   . VAL   B 121 ? 0.1589 0.1460 0.1432 -0.0209 -0.0203 0.0163  121 VAL   B C   
5836 O  O   . VAL   B 121 ? 0.1650 0.1434 0.1712 -0.0322 -0.0255 0.0075  121 VAL   B O   
5837 C  CB  . VAL   B 121 ? 0.1913 0.1863 0.1648 -0.0086 -0.0230 0.0169  121 VAL   B CB  
5838 C  CG1 . VAL   B 121 ? 0.1965 0.1986 0.2007 -0.0204 -0.0124 0.0088  121 VAL   B CG1 
5839 C  CG2 . VAL   B 121 ? 0.2197 0.2148 0.1582 0.0032  -0.0131 0.0027  121 VAL   B CG2 
5850 N  N   . LEU   B 122 ? 0.1486 0.1397 0.1460 -0.0167 -0.0142 0.0074  122 LEU   B N   
5851 C  CA  . LEU   B 122 ? 0.1435 0.1414 0.1304 -0.0212 -0.0148 0.0033  122 LEU   B CA  
5852 C  C   . LEU   B 122 ? 0.1447 0.1351 0.1341 -0.0272 -0.0080 0.0072  122 LEU   B C   
5853 O  O   . LEU   B 122 ? 0.1562 0.1368 0.1720 -0.0332 -0.0143 -0.0018 122 LEU   B O   
5854 C  CB  . LEU   B 122 ? 0.1633 0.1559 0.1736 -0.0042 -0.0218 0.0062  122 LEU   B CB  
5855 C  CG  . LEU   B 122 ? 0.1453 0.1678 0.1758 -0.0172 -0.0037 0.0079  122 LEU   B CG  
5856 C  CD1 . LEU   B 122 ? 0.1552 0.1967 0.1723 -0.0244 -0.0087 0.0097  122 LEU   B CD1 
5857 C  CD2 . LEU   B 122 ? 0.1469 0.1659 0.1543 -0.0098 0.0035  0.0055  122 LEU   B CD2 
5869 N  N   . LEU   B 123 ? 0.1428 0.1263 0.1300 -0.0253 -0.0091 0.0083  123 LEU   B N   
5870 C  CA  . LEU   B 123 ? 0.1450 0.1300 0.1291 -0.0206 -0.0134 -0.0012 123 LEU   B CA  
5871 C  C   . LEU   B 123 ? 0.1377 0.1299 0.1253 -0.0253 -0.0063 -0.0035 123 LEU   B C   
5872 O  O   . LEU   B 123 ? 0.1473 0.1339 0.1339 -0.0262 -0.0101 0.0017  123 LEU   B O   
5873 C  CB  . LEU   B 123 ? 0.1515 0.1306 0.1361 -0.0234 -0.0042 -0.0003 123 LEU   B CB  
5874 C  CG  . LEU   B 123 ? 0.1510 0.1339 0.1597 -0.0160 -0.0035 0.0092  123 LEU   B CG  
5875 C  CD1 . LEU   B 123 ? 0.1561 0.1382 0.1801 -0.0153 -0.0001 -0.0077 123 LEU   B CD1 
5876 C  CD2 . LEU   B 123 ? 0.1566 0.1467 0.1854 -0.0141 0.0086  0.0084  123 LEU   B CD2 
5888 N  N   . ALA   B 124 ? 0.1358 0.1226 0.1406 -0.0166 0.0033  -0.0066 124 ALA   B N   
5889 C  CA  . ALA   B 124 ? 0.1288 0.1238 0.1535 -0.0137 -0.0023 -0.0117 124 ALA   B CA  
5890 C  C   . ALA   B 124 ? 0.1229 0.1217 0.1367 -0.0148 -0.0052 -0.0087 124 ALA   B C   
5891 O  O   . ALA   B 124 ? 0.1405 0.1265 0.1461 -0.0148 -0.0014 -0.0041 124 ALA   B O   
5892 C  CB  . ALA   B 124 ? 0.1347 0.1287 0.1704 -0.0077 0.0006  -0.0004 124 ALA   B CB  
5898 N  N   . PRO   B 125 ? 0.1395 0.1249 0.1350 -0.0093 -0.0102 0.0044  125 PRO   B N   
5899 C  CA  . PRO   B 125 ? 0.1468 0.1234 0.1613 -0.0128 -0.0042 0.0177  125 PRO   B CA  
5900 C  C   . PRO   B 125 ? 0.1446 0.1213 0.1783 -0.0130 -0.0035 0.0031  125 PRO   B C   
5901 O  O   . PRO   B 125 ? 0.1425 0.1241 0.1922 -0.0136 0.0083  0.0091  125 PRO   B O   
5902 C  CB  . PRO   B 125 ? 0.1511 0.1475 0.1769 -0.0202 -0.0193 0.0254  125 PRO   B CB  
5903 C  CG  . PRO   B 125 ? 0.1642 0.1529 0.1603 -0.0260 -0.0165 0.0141  125 PRO   B CG  
5904 C  CD  . PRO   B 125 ? 0.1534 0.1339 0.1380 -0.0238 -0.0110 0.0027  125 PRO   B CD  
5912 N  N   . LEU   B 126 ? 0.1484 0.1210 0.1902 -0.0134 0.0150  0.0075  126 LEU   B N   
5913 C  CA  . LEU   B 126 ? 0.1553 0.1287 0.1876 -0.0105 0.0226  0.0132  126 LEU   B CA  
5914 C  C   . LEU   B 126 ? 0.1486 0.1416 0.1898 0.0029  0.0248  0.0169  126 LEU   B C   
5915 O  O   . LEU   B 126 ? 0.1747 0.1675 0.2106 0.0168  -0.0005 -0.0097 126 LEU   B O   
5916 C  CB  . LEU   B 126 ? 0.1724 0.1282 0.2304 -0.0182 0.0319  0.0143  126 LEU   B CB  
5917 C  CG  . LEU   B 126 ? 0.1925 0.1401 0.2402 -0.0231 0.0310  -0.0056 126 LEU   B CG  
5918 C  CD1 . LEU   B 126 ? 0.2113 0.1425 0.2826 -0.0192 0.0180  -0.0104 126 LEU   B CD1 
5919 C  CD2 . LEU   B 126 ? 0.1955 0.1462 0.2300 -0.0367 0.0128  -0.0030 126 LEU   B CD2 
5931 N  N   . LEU   B 127 ? 0.1488 0.1312 0.1966 0.0055  0.0338  0.0062  127 LEU   B N   
5932 C  CA  . LEU   B 127 ? 0.1491 0.1353 0.2020 -0.0016 0.0359  0.0152  127 LEU   B CA  
5933 C  C   . LEU   B 127 ? 0.1472 0.1276 0.2135 0.0011  0.0244  0.0145  127 LEU   B C   
5934 O  O   . LEU   B 127 ? 0.1450 0.1337 0.2234 -0.0154 0.0145  0.0097  127 LEU   B O   
5935 C  CB  . LEU   B 127 ? 0.1608 0.1336 0.2143 0.0006  0.0315  0.0169  127 LEU   B CB  
5936 C  CG  . LEU   B 127 ? 0.1712 0.1313 0.2363 0.0013  0.0277  0.0127  127 LEU   B CG  
5937 C  CD1 . LEU   B 127 ? 0.1695 0.1272 0.2400 0.0040  0.0153  0.0032  127 LEU   B CD1 
5938 C  CD2 . LEU   B 127 ? 0.1741 0.1376 0.2428 -0.0041 0.0324  0.0211  127 LEU   B CD2 
5950 N  N   . SER   B 128 ? 0.1511 0.1289 0.2040 0.0024  0.0088  0.0156  128 SER   B N   
5951 C  CA  . SER   B 128 ? 0.1591 0.1366 0.1991 0.0068  0.0001  0.0141  128 SER   B CA  
5952 C  C   . SER   B 128 ? 0.1767 0.1379 0.2399 0.0122  -0.0181 0.0162  128 SER   B C   
5953 O  O   . SER   B 128 ? 0.1856 0.1419 0.2822 0.0136  -0.0231 0.0297  128 SER   B O   
5954 C  CB  . SER   B 128 ? 0.1636 0.1382 0.2040 0.0036  0.0123  0.0266  128 SER   B CB  
5955 O  OG  . SER   B 128 ? 0.1792 0.1555 0.2065 0.0104  0.0168  0.0290  128 SER   B OG  
5961 N  N   . ALA   B 129 ? 0.1911 0.1409 0.2658 0.0271  -0.0118 -0.0056 129 ALA   B N   
5962 C  CA  . ALA   B 129 ? 0.2084 0.1530 0.2667 0.0306  -0.0094 -0.0173 129 ALA   B CA  
5963 C  C   . ALA   B 129 ? 0.1910 0.1519 0.2589 0.0228  0.0104  -0.0085 129 ALA   B C   
5964 O  O   . ALA   B 129 ? 0.1760 0.1532 0.2515 0.0151  0.0021  0.0054  129 ALA   B O   
5965 C  CB  . ALA   B 129 ? 0.2345 0.1739 0.2946 0.0392  0.0019  -0.0189 129 ALA   B CB  
5971 N  N   . GLY   B 130 ? 0.1878 0.1456 0.2542 0.0255  0.0132  -0.0090 130 GLY   B N   
5972 C  CA  . GLY   B 130 ? 0.1906 0.1554 0.2507 0.0234  0.0351  -0.0008 130 GLY   B CA  
5973 C  C   . GLY   B 130 ? 0.1909 0.1561 0.2539 0.0176  0.0173  0.0084  130 GLY   B C   
5974 O  O   . GLY   B 130 ? 0.2020 0.1654 0.2743 0.0207  0.0101  0.0092  130 GLY   B O   
5978 N  N   . ILE   B 131 ? 0.1816 0.1703 0.2715 0.0372  0.0198  0.0101  131 ILE   B N   
5979 C  CA  . ILE   B 131 ? 0.2043 0.1877 0.2719 0.0322  0.0140  0.0244  131 ILE   B CA  
5980 C  C   . ILE   B 131 ? 0.2178 0.1796 0.2361 0.0161  0.0090  0.0331  131 ILE   B C   
5981 O  O   . ILE   B 131 ? 0.2402 0.1917 0.2519 0.0142  -0.0060 0.0362  131 ILE   B O   
5982 C  CB  . ILE   B 131 ? 0.2060 0.2244 0.2984 0.0334  0.0012  0.0313  131 ILE   B CB  
5983 C  CG1 . ILE   B 131 ? 0.2113 0.2441 0.3045 0.0031  0.0081  0.0340  131 ILE   B CG1 
5984 C  CG2 . ILE   B 131 ? 0.2071 0.2430 0.3202 0.0425  -0.0011 0.0220  131 ILE   B CG2 
5985 C  CD1 . ILE   B 131 ? 0.2202 0.2655 0.3212 -0.0229 0.0103  0.0378  131 ILE   B CD1 
5997 N  N   . PHE   B 132 ? 0.2072 0.1619 0.2194 0.0113  0.0219  0.0193  132 PHE   B N   
5998 C  CA  . PHE   B 132 ? 0.2179 0.1629 0.2200 0.0016  0.0389  0.0164  132 PHE   B CA  
5999 C  C   . PHE   B 132 ? 0.2342 0.1775 0.2517 0.0013  0.0550  0.0145  132 PHE   B C   
6000 O  O   . PHE   B 132 ? 0.2527 0.2024 0.2803 0.0010  0.0752  0.0108  132 PHE   B O   
6001 C  CB  . PHE   B 132 ? 0.2006 0.1575 0.1976 0.0121  0.0354  0.0296  132 PHE   B CB  
6002 C  CG  . PHE   B 132 ? 0.1922 0.1590 0.1902 0.0186  0.0281  0.0252  132 PHE   B CG  
6003 C  CD1 . PHE   B 132 ? 0.2038 0.1626 0.2428 0.0112  0.0312  0.0194  132 PHE   B CD1 
6004 C  CD2 . PHE   B 132 ? 0.1954 0.1640 0.1867 0.0255  0.0194  0.0247  132 PHE   B CD2 
6005 C  CE1 . PHE   B 132 ? 0.2085 0.1678 0.2528 0.0062  0.0200  0.0228  132 PHE   B CE1 
6006 C  CE2 . PHE   B 132 ? 0.2015 0.1693 0.1873 0.0209  0.0096  0.0175  132 PHE   B CE2 
6007 C  CZ  . PHE   B 132 ? 0.2083 0.1669 0.2168 0.0126  0.0049  0.0254  132 PHE   B CZ  
6017 N  N   . GLY   B 133 ? 0.2287 0.1608 0.2531 0.0018  0.0470  0.0331  133 GLY   B N   
6018 C  CA  . GLY   B 133 ? 0.2441 0.1771 0.2652 -0.0166 0.0430  0.0429  133 GLY   B CA  
6019 C  C   . GLY   B 133 ? 0.2463 0.1911 0.2725 -0.0288 0.0523  0.0457  133 GLY   B C   
6020 O  O   . GLY   B 133 ? 0.2623 0.2049 0.3255 -0.0424 0.0442  0.0568  133 GLY   B O   
6024 N  N   . ALA   B 134 ? 0.2213 0.1848 0.2584 -0.0240 0.0513  0.0197  134 ALA   B N   
6025 C  CA  . ALA   B 134 ? 0.2180 0.1808 0.2712 -0.0126 0.0501  0.0063  134 ALA   B CA  
6026 C  C   . ALA   B 134 ? 0.2285 0.1676 0.2645 -0.0075 0.0419  0.0283  134 ALA   B C   
6027 O  O   . ALA   B 134 ? 0.2372 0.1883 0.2700 0.0014  0.0255  0.0228  134 ALA   B O   
6028 C  CB  . ALA   B 134 ? 0.2161 0.1823 0.2967 -0.0081 0.0485  -0.0069 134 ALA   B CB  
6034 N  N   . ASP   B 135 ? 0.2439 0.1658 0.2650 -0.0131 0.0225  0.0330  135 ASP   B N   
6035 C  CA  . ASP   B 135 ? 0.2650 0.1562 0.2918 -0.0080 0.0126  0.0394  135 ASP   B CA  
6036 C  C   . ASP   B 135 ? 0.2455 0.1420 0.2722 -0.0031 0.0109  0.0354  135 ASP   B C   
6037 O  O   . ASP   B 135 ? 0.2371 0.1388 0.2943 -0.0043 0.0110  0.0362  135 ASP   B O   
6038 C  CB  . ASP   B 135 ? 0.3006 0.1723 0.3207 -0.0329 0.0148  0.0350  135 ASP   B CB  
6039 C  CG  . ASP   B 135 ? 0.3307 0.1702 0.3645 -0.0539 0.0209  0.0337  135 ASP   B CG  
6040 O  OD1 . ASP   B 135 ? 0.3370 0.1509 0.3553 -0.0337 0.0136  0.0245  135 ASP   B OD1 
6041 O  OD2 . ASP   B 135 ? 0.3527 0.2093 0.4136 -0.0740 0.0184  0.0150  135 ASP   B OD2 
6046 N  N   . PRO   B 136 ? 0.2387 0.1511 0.2848 0.0202  -0.0083 0.0227  136 PRO   B N   
6047 C  CA  . PRO   B 136 ? 0.2139 0.1410 0.2903 0.0177  -0.0076 0.0085  136 PRO   B CA  
6048 C  C   . PRO   B 136 ? 0.1905 0.1313 0.2975 0.0149  -0.0063 -0.0020 136 PRO   B C   
6049 O  O   . PRO   B 136 ? 0.1716 0.1298 0.2834 0.0066  -0.0102 0.0129  136 PRO   B O   
6050 C  CB  . PRO   B 136 ? 0.2212 0.1628 0.3003 0.0342  -0.0085 -0.0057 136 PRO   B CB  
6051 C  CG  . PRO   B 136 ? 0.2396 0.1726 0.3197 0.0331  -0.0077 -0.0065 136 PRO   B CG  
6052 C  CD  . PRO   B 136 ? 0.2451 0.1671 0.3014 0.0469  -0.0116 0.0102  136 PRO   B CD  
6060 N  N   . ILE   B 137 ? 0.2004 0.1243 0.3056 0.0107  -0.0087 -0.0020 137 ILE   B N   
6061 C  CA  . ILE   B 137 ? 0.2087 0.1180 0.3181 -0.0062 0.0014  0.0011  137 ILE   B CA  
6062 C  C   . ILE   B 137 ? 0.1991 0.1279 0.3065 -0.0094 0.0169  0.0146  137 ILE   B C   
6063 O  O   . ILE   B 137 ? 0.1870 0.1365 0.2946 -0.0081 0.0089  0.0105  137 ILE   B O   
6064 C  CB  . ILE   B 137 ? 0.2374 0.1283 0.3548 -0.0037 -0.0014 0.0059  137 ILE   B CB  
6065 C  CG1 . ILE   B 137 ? 0.2663 0.1472 0.4004 0.0014  -0.0012 -0.0011 137 ILE   B CG1 
6066 C  CG2 . ILE   B 137 ? 0.2451 0.1325 0.3623 -0.0313 -0.0019 0.0125  137 ILE   B CG2 
6067 C  CD1 . ILE   B 137 ? 0.2880 0.1772 0.4339 0.0127  -0.0060 -0.0012 137 ILE   B CD1 
6079 N  N   . HIS   B 138 ? 0.2089 0.1238 0.3092 -0.0088 0.0208  0.0146  138 HIS   B N   
6080 C  CA  . HIS   B 138 ? 0.2132 0.1321 0.2952 -0.0043 0.0314  0.0134  138 HIS   B CA  
6081 C  C   . HIS   B 138 ? 0.1909 0.1317 0.2800 0.0007  0.0285  0.0283  138 HIS   B C   
6082 O  O   . HIS   B 138 ? 0.1829 0.1421 0.2917 0.0022  0.0397  0.0348  138 HIS   B O   
6083 C  CB  . HIS   B 138 ? 0.2426 0.1445 0.3068 -0.0084 0.0525  0.0103  138 HIS   B CB  
6084 C  CG  . HIS   B 138 ? 0.2721 0.1673 0.3093 -0.0086 0.0752  0.0347  138 HIS   B CG  
6085 N  ND1 . HIS   B 138 ? 0.2860 0.1885 0.3311 -0.0052 0.0866  0.0303  138 HIS   B ND1 
6086 C  CD2 . HIS   B 138 ? 0.2892 0.1811 0.3024 -0.0092 0.0881  0.0264  138 HIS   B CD2 
6087 C  CE1 . HIS   B 138 ? 0.2942 0.1929 0.3252 -0.0017 0.0962  0.0275  138 HIS   B CE1 
6088 N  NE2 . HIS   B 138 ? 0.2985 0.1762 0.3057 0.0015  0.0971  0.0250  138 HIS   B NE2 
6096 N  N   . SER   B 139 ? 0.1860 0.1223 0.2719 0.0024  0.0245  0.0126  139 SER   B N   
6097 C  CA  . SER   B 139 ? 0.1814 0.1196 0.2547 0.0018  0.0184  -0.0022 139 SER   B CA  
6098 C  C   . SER   B 139 ? 0.1517 0.1144 0.2538 -0.0004 0.0205  0.0043  139 SER   B C   
6099 O  O   . SER   B 139 ? 0.1583 0.1186 0.2521 -0.0021 0.0133  0.0029  139 SER   B O   
6100 C  CB  . SER   B 139 ? 0.1869 0.1170 0.2626 0.0046  0.0024  -0.0039 139 SER   B CB  
6101 O  OG  . SER   B 139 ? 0.1838 0.1230 0.2497 -0.0025 -0.0177 0.0079  139 SER   B OG  
6107 N  N   . LEU   B 140 ? 0.1544 0.1114 0.2660 -0.0015 0.0204  0.0038  140 LEU   B N   
6108 C  CA  . LEU   B 140 ? 0.1503 0.1156 0.2627 -0.0006 0.0161  0.0045  140 LEU   B CA  
6109 C  C   . LEU   B 140 ? 0.1473 0.1146 0.2668 -0.0066 0.0089  -0.0089 140 LEU   B C   
6110 O  O   . LEU   B 140 ? 0.1505 0.1265 0.2553 -0.0040 0.0024  -0.0023 140 LEU   B O   
6111 C  CB  . LEU   B 140 ? 0.1486 0.1157 0.2608 -0.0052 0.0210  0.0009  140 LEU   B CB  
6112 C  CG  . LEU   B 140 ? 0.1607 0.1180 0.2596 -0.0088 0.0061  0.0108  140 LEU   B CG  
6113 C  CD1 . LEU   B 140 ? 0.1678 0.1341 0.2765 -0.0156 0.0156  0.0009  140 LEU   B CD1 
6114 C  CD2 . LEU   B 140 ? 0.1811 0.1293 0.2565 -0.0044 0.0071  -0.0093 140 LEU   B CD2 
6126 N  N   . ARG   B 141 ? 0.1437 0.1223 0.2714 -0.0130 0.0133  -0.0076 141 ARG   B N   
6127 C  CA  . ARG   B 141 ? 0.1492 0.1229 0.3029 -0.0167 0.0291  -0.0108 141 ARG   B CA  
6128 C  C   . ARG   B 141 ? 0.1499 0.1233 0.2822 -0.0149 0.0284  -0.0001 141 ARG   B C   
6129 O  O   . ARG   B 141 ? 0.1515 0.1310 0.2753 -0.0158 0.0093  -0.0155 141 ARG   B O   
6130 C  CB  . ARG   B 141 ? 0.1689 0.1293 0.3260 -0.0199 0.0399  -0.0176 141 ARG   B CB  
6131 C  CG  . ARG   B 141 ? 0.1933 0.1590 0.3449 -0.0200 0.0370  -0.0048 141 ARG   B CG  
6132 C  CD  . ARG   B 141 ? 0.2296 0.1857 0.3547 -0.0107 0.0118  -0.0185 141 ARG   B CD  
6133 N  NE  . ARG   B 141 ? 0.2415 0.1822 0.3464 -0.0206 0.0127  -0.0223 141 ARG   B NE  
6134 C  CZ  . ARG   B 141 ? 0.2508 0.1635 0.3233 -0.0072 0.0170  -0.0347 141 ARG   B CZ  
6135 N  NH1 . ARG   B 141 ? 0.2636 0.1571 0.3126 -0.0019 0.0089  -0.0216 141 ARG   B NH1 
6136 N  NH2 . ARG   B 141 ? 0.2630 0.1801 0.3377 0.0024  0.0007  -0.0233 141 ARG   B NH2 
6150 N  N   . VAL   B 142 ? 0.1487 0.1191 0.2753 -0.0100 0.0217  -0.0112 142 VAL   B N   
6151 C  CA  . VAL   B 142 ? 0.1435 0.1212 0.2737 -0.0054 0.0181  -0.0108 142 VAL   B CA  
6152 C  C   . VAL   B 142 ? 0.1409 0.1197 0.2752 -0.0064 0.0163  -0.0098 142 VAL   B C   
6153 O  O   . VAL   B 142 ? 0.1456 0.1182 0.2750 -0.0000 0.0227  -0.0002 142 VAL   B O   
6154 C  CB  . VAL   B 142 ? 0.1561 0.1293 0.2751 -0.0011 0.0283  0.0030  142 VAL   B CB  
6155 C  CG1 . VAL   B 142 ? 0.1485 0.1294 0.2709 0.0060  0.0283  0.0066  142 VAL   B CG1 
6156 C  CG2 . VAL   B 142 ? 0.1812 0.1286 0.2888 0.0030  0.0356  0.0180  142 VAL   B CG2 
6166 N  N   . CYS   B 143 ? 0.1377 0.1218 0.2364 -0.0043 0.0124  0.0055  143 CYS   B N   
6167 C  CA  . CYS   B 143 ? 0.1269 0.1276 0.2457 -0.0113 0.0063  -0.0035 143 CYS   B CA  
6168 C  C   . CYS   B 143 ? 0.1281 0.1264 0.2399 -0.0125 0.0138  0.0006  143 CYS   B C   
6169 O  O   . CYS   B 143 ? 0.1336 0.1245 0.2529 -0.0041 -0.0017 -0.0057 143 CYS   B O   
6170 C  CB  . CYS   B 143 ? 0.1434 0.1306 0.2418 -0.0088 0.0082  0.0022  143 CYS   B CB  
6171 S  SG  . CYS   B 143 ? 0.1414 0.1455 0.2357 -0.0036 0.0142  0.0048  143 CYS   B SG  
6177 N  N   . VAL   B 144 ? 0.1380 0.1263 0.2634 -0.0079 0.0052  -0.0121 144 VAL   B N   
6178 C  CA  . VAL   B 144 ? 0.1456 0.1365 0.2882 -0.0163 -0.0022 -0.0201 144 VAL   B CA  
6179 C  C   . VAL   B 144 ? 0.1395 0.1367 0.2799 -0.0129 0.0048  -0.0084 144 VAL   B C   
6180 O  O   . VAL   B 144 ? 0.1450 0.1650 0.2860 0.0015  0.0032  0.0194  144 VAL   B O   
6181 C  CB  . VAL   B 144 ? 0.1672 0.1498 0.3510 -0.0109 -0.0117 -0.0279 144 VAL   B CB  
6182 C  CG1 . VAL   B 144 ? 0.1952 0.1918 0.3817 -0.0051 -0.0162 -0.0256 144 VAL   B CG1 
6183 C  CG2 . VAL   B 144 ? 0.1796 0.1507 0.3520 -0.0034 -0.0213 -0.0352 144 VAL   B CG2 
6193 N  N   . ASP   B 145 ? 0.1365 0.1300 0.2903 -0.0128 0.0102  -0.0216 145 ASP   B N   
6194 C  CA  . ASP   B 145 ? 0.1373 0.1324 0.3073 -0.0073 0.0132  -0.0151 145 ASP   B CA  
6195 C  C   . ASP   B 145 ? 0.1302 0.1423 0.2970 -0.0055 0.0136  -0.0085 145 ASP   B C   
6196 O  O   . ASP   B 145 ? 0.1352 0.1557 0.3603 -0.0105 0.0182  -0.0245 145 ASP   B O   
6197 C  CB  . ASP   B 145 ? 0.1546 0.1449 0.3420 -0.0145 0.0287  -0.0060 145 ASP   B CB  
6198 C  CG  . ASP   B 145 ? 0.1751 0.1459 0.3822 -0.0208 0.0375  0.0008  145 ASP   B CG  
6199 O  OD1 . ASP   B 145 ? 0.1745 0.1448 0.3995 -0.0244 0.0065  -0.0163 145 ASP   B OD1 
6200 O  OD2 . ASP   B 145 ? 0.2079 0.1532 0.4239 -0.0298 0.0474  0.0124  145 ASP   B OD2 
6205 N  N   . THR   B 146 ? 0.1253 0.1235 0.2700 -0.0081 0.0071  -0.0075 146 THR   B N   
6206 C  CA  . THR   B 146 ? 0.1370 0.1205 0.2502 -0.0018 0.0094  -0.0069 146 THR   B CA  
6207 C  C   . THR   B 146 ? 0.1333 0.1226 0.2416 -0.0119 0.0046  0.0027  146 THR   B C   
6208 O  O   . THR   B 146 ? 0.1409 0.1193 0.2345 -0.0067 0.0010  0.0011  146 THR   B O   
6209 C  CB  . THR   B 146 ? 0.1386 0.1224 0.2624 -0.0021 0.0216  0.0024  146 THR   B CB  
6210 O  OG1 . THR   B 146 ? 0.1423 0.1233 0.2636 -0.0046 0.0259  0.0104  146 THR   B OG1 
6211 C  CG2 . THR   B 146 ? 0.1487 0.1279 0.2406 0.0018  0.0132  -0.0053 146 THR   B CG2 
6219 N  N   . VAL   B 147 ? 0.1388 0.1264 0.2315 -0.0034 0.0158  -0.0009 147 VAL   B N   
6220 C  CA  . VAL   B 147 ? 0.1377 0.1246 0.2228 -0.0145 0.0041  -0.0075 147 VAL   B CA  
6221 C  C   . VAL   B 147 ? 0.1382 0.1223 0.2293 -0.0120 0.0015  -0.0056 147 VAL   B C   
6222 O  O   . VAL   B 147 ? 0.1488 0.1304 0.2456 -0.0177 -0.0189 -0.0091 147 VAL   B O   
6223 C  CB  . VAL   B 147 ? 0.1396 0.1351 0.1951 -0.0086 -0.0005 -0.0006 147 VAL   B CB  
6224 C  CG1 . VAL   B 147 ? 0.1427 0.1479 0.1966 -0.0075 -0.0021 0.0044  147 VAL   B CG1 
6225 C  CG2 . VAL   B 147 ? 0.1464 0.1328 0.2104 -0.0109 -0.0020 0.0028  147 VAL   B CG2 
6235 N  N   . ARG   B 148 ? 0.1373 0.1289 0.2207 -0.0070 -0.0175 -0.0077 148 ARG   B N   
6236 C  CA  . ARG   B 148 ? 0.1400 0.1368 0.2056 -0.0047 -0.0200 -0.0101 148 ARG   B CA  
6237 C  C   . ARG   B 148 ? 0.1426 0.1509 0.1946 -0.0059 -0.0228 -0.0058 148 ARG   B C   
6238 O  O   . ARG   B 148 ? 0.1643 0.1752 0.1883 -0.0224 -0.0329 -0.0002 148 ARG   B O   
6239 C  CB  . ARG   B 148 ? 0.1421 0.1488 0.2111 0.0028  -0.0216 -0.0183 148 ARG   B CB  
6240 C  CG  . ARG   B 148 ? 0.1473 0.1556 0.2319 -0.0059 -0.0179 -0.0387 148 ARG   B CG  
6241 C  CD  . ARG   B 148 ? 0.1592 0.1747 0.2347 0.0041  -0.0214 -0.0427 148 ARG   B CD  
6242 N  NE  . ARG   B 148 ? 0.1613 0.1737 0.2303 0.0186  -0.0242 -0.0294 148 ARG   B NE  
6243 C  CZ  . ARG   B 148 ? 0.1491 0.1622 0.2142 0.0201  -0.0159 -0.0277 148 ARG   B CZ  
6244 N  NH1 . ARG   B 148 ? 0.1388 0.1683 0.2146 0.0093  -0.0058 -0.0212 148 ARG   B NH1 
6245 N  NH2 . ARG   B 148 ? 0.1735 0.1493 0.2095 0.0190  -0.0192 -0.0196 148 ARG   B NH2 
6259 N  N   . THR   B 149 ? 0.1460 0.1433 0.2000 -0.0086 -0.0193 0.0071  149 THR   B N   
6260 C  CA  . THR   B 149 ? 0.1536 0.1413 0.1882 -0.0149 -0.0219 0.0104  149 THR   B CA  
6261 C  C   . THR   B 149 ? 0.1547 0.1387 0.1745 -0.0132 -0.0235 0.0084  149 THR   B C   
6262 O  O   . THR   B 149 ? 0.1630 0.1440 0.2028 -0.0200 -0.0086 0.0033  149 THR   B O   
6263 C  CB  . THR   B 149 ? 0.1583 0.1396 0.1908 -0.0137 -0.0250 -0.0049 149 THR   B CB  
6264 O  OG1 . THR   B 149 ? 0.1585 0.1400 0.1773 -0.0231 -0.0248 -0.0003 149 THR   B OG1 
6265 C  CG2 . THR   B 149 ? 0.1653 0.1426 0.2047 -0.0110 -0.0171 0.0072  149 THR   B CG2 
6273 N  N   . ASN   B 150 ? 0.1561 0.1368 0.1744 -0.0126 -0.0276 0.0042  150 ASN   B N   
6274 C  CA  . ASN   B 150 ? 0.1612 0.1553 0.1817 -0.0257 -0.0230 -0.0028 150 ASN   B CA  
6275 C  C   . ASN   B 150 ? 0.1545 0.1522 0.1825 -0.0167 -0.0209 -0.0014 150 ASN   B C   
6276 O  O   . ASN   B 150 ? 0.1583 0.1505 0.2013 -0.0277 -0.0340 -0.0012 150 ASN   B O   
6277 C  CB  . ASN   B 150 ? 0.1880 0.1939 0.1928 -0.0251 -0.0247 0.0156  150 ASN   B CB  
6278 C  CG  . ASN   B 150 ? 0.2168 0.2375 0.2330 -0.0269 -0.0328 0.0257  150 ASN   B CG  
6279 O  OD1 . ASN   B 150 ? 0.2247 0.2567 0.2429 -0.0364 -0.0491 0.0240  150 ASN   B OD1 
6280 N  ND2 . ASN   B 150 ? 0.2275 0.2628 0.2789 -0.0165 -0.0424 0.0618  150 ASN   B ND2 
6287 N  N   . VAL   B 151 ? 0.1492 0.1472 0.1669 -0.0207 -0.0239 -0.0047 151 VAL   B N   
6288 C  CA  . VAL   B 151 ? 0.1532 0.1492 0.1673 -0.0280 -0.0178 -0.0022 151 VAL   B CA  
6289 C  C   . VAL   B 151 ? 0.1537 0.1398 0.1575 -0.0290 -0.0199 -0.0096 151 VAL   B C   
6290 O  O   . VAL   B 151 ? 0.1588 0.1488 0.1970 -0.0222 -0.0106 -0.0152 151 VAL   B O   
6291 C  CB  . VAL   B 151 ? 0.1676 0.1551 0.1793 -0.0126 -0.0110 -0.0033 151 VAL   B CB  
6292 C  CG1 . VAL   B 151 ? 0.1739 0.1579 0.2073 -0.0173 0.0096  -0.0189 151 VAL   B CG1 
6293 C  CG2 . VAL   B 151 ? 0.1827 0.1728 0.1749 0.0012  -0.0156 0.0039  151 VAL   B CG2 
6303 N  N   . TYR   B 152 ? 0.1510 0.1322 0.1599 -0.0256 -0.0061 -0.0073 152 TYR   B N   
6304 C  CA  . TYR   B 152 ? 0.1544 0.1531 0.1534 -0.0215 -0.0042 -0.0071 152 TYR   B CA  
6305 C  C   . TYR   B 152 ? 0.1506 0.1441 0.1421 -0.0174 -0.0070 -0.0100 152 TYR   B C   
6306 O  O   . TYR   B 152 ? 0.1559 0.1379 0.1664 -0.0223 -0.0071 -0.0030 152 TYR   B O   
6307 C  CB  . TYR   B 152 ? 0.1642 0.1686 0.1640 -0.0265 -0.0074 0.0025  152 TYR   B CB  
6308 C  CG  . TYR   B 152 ? 0.1816 0.1785 0.1549 -0.0449 -0.0077 -0.0024 152 TYR   B CG  
6309 C  CD1 . TYR   B 152 ? 0.1935 0.1898 0.1575 -0.0295 -0.0168 0.0023  152 TYR   B CD1 
6310 C  CD2 . TYR   B 152 ? 0.2003 0.1974 0.1599 -0.0380 -0.0040 -0.0131 152 TYR   B CD2 
6311 C  CE1 . TYR   B 152 ? 0.2091 0.2098 0.1743 -0.0268 -0.0225 0.0126  152 TYR   B CE1 
6312 C  CE2 . TYR   B 152 ? 0.2147 0.2231 0.1635 -0.0327 -0.0092 -0.0188 152 TYR   B CE2 
6313 C  CZ  . TYR   B 152 ? 0.2203 0.2318 0.1485 -0.0330 -0.0307 0.0095  152 TYR   B CZ  
6314 O  OH  . TYR   B 152 ? 0.2515 0.2739 0.1719 -0.0244 -0.0359 0.0178  152 TYR   B OH  
6324 N  N   . LEU   B 153 ? 0.1520 0.1347 0.1646 -0.0239 -0.0069 -0.0131 153 LEU   B N   
6325 C  CA  . LEU   B 153 ? 0.1537 0.1343 0.1509 -0.0189 0.0016  -0.0103 153 LEU   B CA  
6326 C  C   . LEU   B 153 ? 0.1509 0.1344 0.1511 -0.0236 -0.0017 -0.0151 153 LEU   B C   
6327 O  O   . LEU   B 153 ? 0.1580 0.1548 0.1887 -0.0197 -0.0043 -0.0346 153 LEU   B O   
6328 C  CB  . LEU   B 153 ? 0.1541 0.1288 0.1771 -0.0278 0.0067  -0.0099 153 LEU   B CB  
6329 C  CG  . LEU   B 153 ? 0.1489 0.1365 0.1913 -0.0191 0.0069  -0.0121 153 LEU   B CG  
6330 C  CD1 . LEU   B 153 ? 0.1551 0.1475 0.1991 -0.0241 0.0195  -0.0012 153 LEU   B CD1 
6331 C  CD2 . LEU   B 153 ? 0.1490 0.1576 0.1978 -0.0232 0.0051  -0.0014 153 LEU   B CD2 
6343 N  N   . ALA   B 154 ? 0.1482 0.1310 0.1685 -0.0082 -0.0088 -0.0139 154 ALA   B N   
6344 C  CA  . ALA   B 154 ? 0.1591 0.1433 0.1825 -0.0013 -0.0096 -0.0227 154 ALA   B CA  
6345 C  C   . ALA   B 154 ? 0.1788 0.1391 0.1895 0.0026  -0.0311 -0.0345 154 ALA   B C   
6346 O  O   . ALA   B 154 ? 0.2182 0.1425 0.2151 0.0075  -0.0196 -0.0149 154 ALA   B O   
6347 C  CB  . ALA   B 154 ? 0.1482 0.1605 0.2225 -0.0013 -0.0068 -0.0274 154 ALA   B CB  
6353 N  N   . VAL   B 155 ? 0.1466 0.1348 0.2225 -0.0050 -0.0018 -0.0240 155 VAL   B N   
6354 C  CA  . VAL   B 155 ? 0.1377 0.1338 0.2342 -0.0046 -0.0078 -0.0219 155 VAL   B CA  
6355 C  C   . VAL   B 155 ? 0.1373 0.1391 0.2319 0.0016  -0.0007 -0.0330 155 VAL   B C   
6356 O  O   . VAL   B 155 ? 0.1593 0.1559 0.2692 0.0116  -0.0016 -0.0422 155 VAL   B O   
6357 C  CB  . VAL   B 155 ? 0.1413 0.1530 0.2711 -0.0015 -0.0089 -0.0113 155 VAL   B CB  
6358 C  CG1 . VAL   B 155 ? 0.1454 0.1496 0.2729 -0.0108 -0.0096 -0.0046 155 VAL   B CG1 
6359 C  CG2 . VAL   B 155 ? 0.1373 0.1695 0.3081 0.0001  -0.0138 0.0248  155 VAL   B CG2 
6369 N  N   . PHE   B 156 ? 0.1315 0.1463 0.2584 0.0069  0.0001  -0.0253 156 PHE   B N   
6370 C  CA  . PHE   B 156 ? 0.1378 0.1505 0.2872 0.0091  -0.0044 -0.0283 156 PHE   B CA  
6371 C  C   . PHE   B 156 ? 0.1426 0.1682 0.3123 0.0165  -0.0075 -0.0510 156 PHE   B C   
6372 O  O   . PHE   B 156 ? 0.1675 0.1863 0.3185 0.0256  -0.0029 -0.0548 156 PHE   B O   
6373 C  CB  . PHE   B 156 ? 0.1440 0.1491 0.2727 0.0035  -0.0089 -0.0138 156 PHE   B CB  
6374 C  CG  . PHE   B 156 ? 0.1469 0.1647 0.2697 0.0054  -0.0139 -0.0075 156 PHE   B CG  
6375 C  CD1 . PHE   B 156 ? 0.1539 0.1902 0.3148 0.0111  -0.0001 0.0289  156 PHE   B CD1 
6376 C  CD2 . PHE   B 156 ? 0.1520 0.1710 0.2624 0.0132  -0.0253 -0.0123 156 PHE   B CD2 
6377 C  CE1 . PHE   B 156 ? 0.1561 0.2009 0.3314 0.0109  -0.0055 0.0302  156 PHE   B CE1 
6378 C  CE2 . PHE   B 156 ? 0.1540 0.1923 0.2938 0.0156  -0.0214 0.0087  156 PHE   B CE2 
6379 C  CZ  . PHE   B 156 ? 0.1471 0.1975 0.3193 0.0224  -0.0137 0.0191  156 PHE   B CZ  
6389 N  N   . ASP   B 157 ? 0.1454 0.1535 0.3339 0.0123  -0.0238 -0.0412 157 ASP   B N   
6390 C  CA  . ASP   B 157 ? 0.1629 0.1587 0.3743 0.0091  -0.0193 -0.0445 157 ASP   B CA  
6391 C  C   . ASP   B 157 ? 0.1594 0.1597 0.3614 0.0040  -0.0235 -0.0699 157 ASP   B C   
6392 O  O   . ASP   B 157 ? 0.1404 0.1546 0.3683 0.0056  -0.0214 -0.0425 157 ASP   B O   
6393 C  CB  . ASP   B 157 ? 0.1784 0.1713 0.3926 0.0060  -0.0393 -0.0275 157 ASP   B CB  
6394 C  CG  . ASP   B 157 ? 0.2164 0.1880 0.4148 0.0015  -0.0348 -0.0286 157 ASP   B CG  
6395 O  OD1 . ASP   B 157 ? 0.2188 0.1837 0.4228 0.0167  -0.0293 -0.0154 157 ASP   B OD1 
6396 O  OD2 . ASP   B 157 ? 0.2587 0.2079 0.4447 -0.0064 -0.0226 -0.0268 157 ASP   B OD2 
6401 N  N   A LYS   B 158 ? 0.1561 0.1856 0.3724 0.0066  -0.0100 -0.0891 158 LYS   B N   
6402 N  N   B LYS   B 158 ? 0.1747 0.1859 0.3428 0.0072  -0.0153 -0.0756 158 LYS   B N   
6403 C  CA  A LYS   B 158 ? 0.1661 0.2036 0.3918 0.0081  0.0010  -0.0981 158 LYS   B CA  
6404 C  CA  B LYS   B 158 ? 0.1964 0.2088 0.3368 0.0111  -0.0098 -0.0767 158 LYS   B CA  
6405 C  C   A LYS   B 158 ? 0.1667 0.1839 0.4101 0.0055  -0.0134 -0.0925 158 LYS   B C   
6406 C  C   B LYS   B 158 ? 0.1985 0.2049 0.3270 0.0129  -0.0169 -0.0689 158 LYS   B C   
6407 O  O   A LYS   B 158 ? 0.1660 0.1765 0.4258 -0.0032 -0.0143 -0.1119 158 LYS   B O   
6408 O  O   B LYS   B 158 ? 0.2004 0.2061 0.3217 0.0103  -0.0138 -0.0725 158 LYS   B O   
6409 C  CB  A LYS   B 158 ? 0.1891 0.2422 0.3863 0.0158  0.0101  -0.1106 158 LYS   B CB  
6410 C  CB  B LYS   B 158 ? 0.2180 0.2343 0.3401 0.0152  -0.0029 -0.0851 158 LYS   B CB  
6411 C  CG  A LYS   B 158 ? 0.2211 0.2781 0.3838 0.0165  0.0168  -0.1177 158 LYS   B CG  
6412 C  CG  B LYS   B 158 ? 0.2410 0.2574 0.3459 0.0157  0.0032  -0.0884 158 LYS   B CG  
6413 C  CD  A LYS   B 158 ? 0.2475 0.3162 0.3960 0.0155  0.0173  -0.1072 158 LYS   B CD  
6414 C  CD  B LYS   B 158 ? 0.2617 0.2834 0.3608 0.0158  0.0074  -0.0836 158 LYS   B CD  
6415 C  CE  A LYS   B 158 ? 0.2653 0.3408 0.4074 0.0164  0.0114  -0.0988 158 LYS   B CE  
6416 C  CE  B LYS   B 158 ? 0.2760 0.3004 0.3727 0.0178  0.0069  -0.0807 158 LYS   B CE  
6417 N  NZ  A LYS   B 158 ? 0.2651 0.3512 0.4052 0.0105  0.0062  -0.0953 158 LYS   B NZ  
6418 N  NZ  B LYS   B 158 ? 0.2800 0.3087 0.3754 0.0157  0.0055  -0.0801 158 LYS   B NZ  
6445 N  N   A ASN   B 159 ? 0.1669 0.1704 0.4193 0.0089  -0.0350 -0.0721 159 ASN   B N   
6446 N  N   B ASN   B 159 ? 0.1964 0.1976 0.3303 0.0143  -0.0313 -0.0585 159 ASN   B N   
6447 C  CA  A ASN   B 159 ? 0.1866 0.1613 0.4317 0.0254  -0.0472 -0.0603 159 ASN   B CA  
6448 C  CA  B ASN   B 159 ? 0.1997 0.1880 0.3428 0.0211  -0.0393 -0.0551 159 ASN   B CA  
6449 C  C   A ASN   B 159 ? 0.1741 0.1495 0.4171 0.0224  -0.0543 -0.0541 159 ASN   B C   
6450 C  C   B ASN   B 159 ? 0.1832 0.1684 0.3632 0.0214  -0.0442 -0.0563 159 ASN   B C   
6451 O  O   A ASN   B 159 ? 0.1758 0.1411 0.4291 -0.0027 -0.0594 -0.0373 159 ASN   B O   
6452 O  O   B ASN   B 159 ? 0.1832 0.1630 0.3616 0.0149  -0.0413 -0.0553 159 ASN   B O   
6453 C  CB  A ASN   B 159 ? 0.2113 0.1747 0.4525 0.0360  -0.0501 -0.0561 159 ASN   B CB  
6454 C  CB  B ASN   B 159 ? 0.2139 0.1982 0.3366 0.0255  -0.0413 -0.0510 159 ASN   B CB  
6455 C  CG  A ASN   B 159 ? 0.2377 0.1936 0.4710 0.0336  -0.0628 -0.0554 159 ASN   B CG  
6456 C  CG  B ASN   B 159 ? 0.2284 0.2104 0.3379 0.0260  -0.0465 -0.0471 159 ASN   B CG  
6457 O  OD1 A ASN   B 159 ? 0.2555 0.2078 0.4750 0.0393  -0.0651 -0.0596 159 ASN   B OD1 
6458 O  OD1 B ASN   B 159 ? 0.2368 0.2166 0.3364 0.0312  -0.0506 -0.0426 159 ASN   B OD1 
6459 N  ND2 A ASN   B 159 ? 0.2402 0.2027 0.4777 0.0255  -0.0720 -0.0458 159 ASN   B ND2 
6460 N  ND2 B ASN   B 159 ? 0.2310 0.2165 0.3412 0.0232  -0.0472 -0.0414 159 ASN   B ND2 
6473 N  N   . LEU   B 160 ? 0.1678 0.1580 0.3854 0.0185  -0.0506 -0.0467 160 LEU   B N   
6474 C  CA  . LEU   B 160 ? 0.1624 0.1586 0.3542 0.0171  -0.0423 -0.0360 160 LEU   B CA  
6475 C  C   . LEU   B 160 ? 0.1591 0.1457 0.3493 0.0038  -0.0222 -0.0428 160 LEU   B C   
6476 O  O   . LEU   B 160 ? 0.1452 0.1476 0.3528 0.0034  -0.0337 -0.0318 160 LEU   B O   
6477 C  CB  . LEU   B 160 ? 0.1577 0.1627 0.3373 0.0073  -0.0490 -0.0316 160 LEU   B CB  
6478 C  CG  . LEU   B 160 ? 0.1629 0.1714 0.3198 0.0134  -0.0403 -0.0147 160 LEU   B CG  
6479 C  CD1 . LEU   B 160 ? 0.1843 0.1899 0.3220 0.0023  -0.0183 -0.0114 160 LEU   B CD1 
6480 C  CD2 . LEU   B 160 ? 0.1683 0.1729 0.3116 0.0306  -0.0394 -0.0213 160 LEU   B CD2 
6493 N  N   A TYR   B 161 ? 0.1608 0.1447 0.3514 -0.0040 0.0028  -0.0470 161 TYR   B N   
6494 N  N   B TYR   B 161 ? 0.1641 0.1500 0.3347 0.0004  -0.0042 -0.0453 161 TYR   B N   
6495 C  CA  A TYR   B 161 ? 0.1606 0.1454 0.3376 -0.0148 0.0206  -0.0496 161 TYR   B CA  
6496 C  CA  B TYR   B 161 ? 0.1683 0.1544 0.3146 -0.0046 0.0094  -0.0473 161 TYR   B CA  
6497 C  C   A TYR   B 161 ? 0.1602 0.1398 0.3324 -0.0157 0.0224  -0.0475 161 TYR   B C   
6498 C  C   B TYR   B 161 ? 0.1659 0.1488 0.3187 -0.0073 0.0113  -0.0508 161 TYR   B C   
6499 O  O   A TYR   B 161 ? 0.1589 0.1436 0.3377 -0.0168 0.0258  -0.0447 161 TYR   B O   
6500 O  O   B TYR   B 161 ? 0.1665 0.1522 0.3157 -0.0066 0.0118  -0.0507 161 TYR   B O   
6501 C  CB  A TYR   B 161 ? 0.1746 0.1572 0.3338 -0.0245 0.0376  -0.0572 161 TYR   B CB  
6502 C  CB  B TYR   B 161 ? 0.1817 0.1667 0.2973 -0.0065 0.0217  -0.0467 161 TYR   B CB  
6503 C  CG  A TYR   B 161 ? 0.1965 0.1579 0.3207 -0.0321 0.0443  -0.0664 161 TYR   B CG  
6504 C  CG  B TYR   B 161 ? 0.1995 0.1756 0.2806 -0.0108 0.0267  -0.0446 161 TYR   B CG  
6505 C  CD1 A TYR   B 161 ? 0.2029 0.1507 0.3168 -0.0476 0.0382  -0.0739 161 TYR   B CD1 
6506 C  CD1 B TYR   B 161 ? 0.2057 0.1770 0.2766 -0.0162 0.0254  -0.0453 161 TYR   B CD1 
6507 C  CD2 A TYR   B 161 ? 0.2196 0.1684 0.3123 -0.0312 0.0365  -0.0646 161 TYR   B CD2 
6508 C  CD2 B TYR   B 161 ? 0.2126 0.1833 0.2697 -0.0108 0.0232  -0.0403 161 TYR   B CD2 
6509 C  CE1 A TYR   B 161 ? 0.2186 0.1743 0.3255 -0.0492 0.0450  -0.0660 161 TYR   B CE1 
6510 C  CE1 B TYR   B 161 ? 0.2152 0.1893 0.2775 -0.0182 0.0292  -0.0410 161 TYR   B CE1 
6511 C  CE2 A TYR   B 161 ? 0.2352 0.1838 0.3278 -0.0371 0.0402  -0.0566 161 TYR   B CE2 
6512 C  CE2 B TYR   B 161 ? 0.2230 0.1921 0.2759 -0.0130 0.0261  -0.0366 161 TYR   B CE2 
6513 C  CZ  A TYR   B 161 ? 0.2360 0.1837 0.3301 -0.0519 0.0349  -0.0558 161 TYR   B CZ  
6514 C  CZ  B TYR   B 161 ? 0.2255 0.1935 0.2770 -0.0188 0.0240  -0.0365 161 TYR   B CZ  
6515 O  OH  A TYR   B 161 ? 0.2654 0.2039 0.3537 -0.0499 0.0326  -0.0525 161 TYR   B OH  
6516 O  OH  B TYR   B 161 ? 0.2430 0.2034 0.2899 -0.0193 0.0250  -0.0366 161 TYR   B OH  
6535 N  N   . ASP   B 162 ? 0.1635 0.1465 0.3399 -0.0073 0.0047  -0.0561 162 ASP   B N   
6536 C  CA  . ASP   B 162 ? 0.1715 0.1516 0.3337 -0.0044 0.0011  -0.0533 162 ASP   B CA  
6537 C  C   . ASP   B 162 ? 0.1731 0.1425 0.3240 -0.0069 -0.0055 -0.0489 162 ASP   B C   
6538 O  O   . ASP   B 162 ? 0.1780 0.1445 0.3427 -0.0121 -0.0206 -0.0336 162 ASP   B O   
6539 C  CB  . ASP   B 162 ? 0.1922 0.1686 0.3590 0.0008  0.0038  -0.0669 162 ASP   B CB  
6540 C  CG  . ASP   B 162 ? 0.1935 0.1898 0.3774 0.0021  -0.0025 -0.0839 162 ASP   B CG  
6541 O  OD1 . ASP   B 162 ? 0.1906 0.2085 0.3729 -0.0064 0.0166  -0.0816 162 ASP   B OD1 
6542 O  OD2 . ASP   B 162 ? 0.2136 0.2147 0.4032 0.0225  -0.0075 -0.0852 162 ASP   B OD2 
6548 N  N   A LYS   B 163 ? 0.1719 0.1304 0.3148 -0.0031 -0.0212 -0.0446 163 LYS   B N   
6549 N  N   B LYS   B 163 ? 0.1779 0.1496 0.3155 -0.0073 -0.0122 -0.0365 163 LYS   B N   
6550 C  CA  A LYS   B 163 ? 0.1824 0.1398 0.3271 -0.0055 -0.0099 -0.0275 163 LYS   B CA  
6551 C  CA  B LYS   B 163 ? 0.1885 0.1661 0.3213 -0.0091 -0.0062 -0.0211 163 LYS   B CA  
6552 C  C   A LYS   B 163 ? 0.1545 0.1351 0.3265 -0.0087 -0.0072 -0.0110 163 LYS   B C   
6553 C  C   B LYS   B 163 ? 0.1640 0.1501 0.3133 -0.0106 -0.0052 -0.0115 163 LYS   B C   
6554 O  O   A LYS   B 163 ? 0.1542 0.1418 0.3533 -0.0171 -0.0118 -0.0014 163 LYS   B O   
6555 O  O   B LYS   B 163 ? 0.1652 0.1541 0.3225 -0.0150 -0.0074 -0.0069 163 LYS   B O   
6556 C  CB  A LYS   B 163 ? 0.2293 0.1677 0.3554 0.0012  -0.0074 -0.0184 163 LYS   B CB  
6557 C  CB  B LYS   B 163 ? 0.2261 0.2026 0.3476 -0.0073 -0.0051 -0.0140 163 LYS   B CB  
6558 C  CG  A LYS   B 163 ? 0.2914 0.2272 0.3962 -0.0010 0.0027  -0.0128 163 LYS   B CG  
6559 C  CG  B LYS   B 163 ? 0.2674 0.2454 0.3818 -0.0072 -0.0013 -0.0088 163 LYS   B CG  
6560 C  CD  A LYS   B 163 ? 0.3469 0.2830 0.4438 -0.0105 0.0002  -0.0156 163 LYS   B CD  
6561 C  CD  B LYS   B 163 ? 0.3045 0.2857 0.4206 -0.0105 -0.0029 -0.0086 163 LYS   B CD  
6562 C  CE  A LYS   B 163 ? 0.3900 0.3251 0.4723 -0.0162 0.0019  -0.0149 163 LYS   B CE  
6563 C  CE  B LYS   B 163 ? 0.3330 0.3204 0.4480 -0.0136 -0.0019 -0.0062 163 LYS   B CE  
6564 N  NZ  A LYS   B 163 ? 0.4171 0.3476 0.4942 -0.0188 0.0028  -0.0195 163 LYS   B NZ  
6565 N  NZ  B LYS   B 163 ? 0.3488 0.3306 0.4664 -0.0150 -0.0015 -0.0067 163 LYS   B NZ  
6592 N  N   . LEU   B 164 ? 0.1474 0.1350 0.3037 -0.0111 -0.0042 -0.0095 164 LEU   B N   
6593 C  CA  . LEU   B 164 ? 0.1449 0.1320 0.2862 -0.0128 -0.0158 -0.0041 164 LEU   B CA  
6594 C  C   . LEU   B 164 ? 0.1547 0.1309 0.2801 -0.0156 -0.0305 -0.0007 164 LEU   B C   
6595 O  O   . LEU   B 164 ? 0.1553 0.1561 0.2956 -0.0184 -0.0290 0.0046  164 LEU   B O   
6596 C  CB  . LEU   B 164 ? 0.1425 0.1323 0.2685 -0.0112 -0.0116 -0.0047 164 LEU   B CB  
6597 C  CG  . LEU   B 164 ? 0.1544 0.1478 0.2664 -0.0094 -0.0078 -0.0059 164 LEU   B CG  
6598 C  CD1 . LEU   B 164 ? 0.1597 0.1469 0.2668 -0.0125 -0.0189 -0.0090 164 LEU   B CD1 
6599 C  CD2 . LEU   B 164 ? 0.1697 0.1887 0.2837 -0.0066 -0.0020 -0.0135 164 LEU   B CD2 
6612 N  N   . VAL   B 165 ? 0.1826 0.1410 0.3110 -0.0181 -0.0380 -0.0191 165 VAL   B N   
6613 C  CA  . VAL   B 165 ? 0.2177 0.1484 0.3189 -0.0329 -0.0588 -0.0012 165 VAL   B CA  
6614 C  C   . VAL   B 165 ? 0.2426 0.1643 0.3558 -0.0467 -0.0882 0.0040  165 VAL   B C   
6615 O  O   . VAL   B 165 ? 0.2612 0.1817 0.3657 -0.0509 -0.0955 0.0085  165 VAL   B O   
6616 C  CB  . VAL   B 165 ? 0.2456 0.1700 0.3159 -0.0229 -0.0269 -0.0328 165 VAL   B CB  
6617 C  CG1 . VAL   B 165 ? 0.2632 0.1747 0.3367 -0.0209 -0.0177 -0.0301 165 VAL   B CG1 
6618 C  CG2 . VAL   B 165 ? 0.2439 0.1819 0.3012 -0.0229 -0.0175 -0.0282 165 VAL   B CG2 
6628 N  N   . SER   B 166 ? 0.2537 0.1567 0.3876 -0.0394 -0.0980 -0.0313 166 SER   B N   
6629 C  CA  . SER   B 166 ? 0.2488 0.1614 0.4457 -0.0399 -0.0721 -0.0376 166 SER   B CA  
6630 C  C   . SER   B 166 ? 0.2334 0.1757 0.4579 -0.0402 -0.0640 -0.0067 166 SER   B C   
6631 O  O   . SER   B 166 ? 0.2294 0.1911 0.4851 -0.0481 -0.0708 -0.0374 166 SER   B O   
6632 C  CB  . SER   B 166 ? 0.2457 0.1677 0.4803 -0.0288 -0.0678 -0.0506 166 SER   B CB  
6633 O  OG  . SER   B 166 ? 0.2298 0.1665 0.4970 -0.0185 -0.0716 -0.0334 166 SER   B OG  
6639 N  N   . SER   B 167 ? 0.2212 0.1596 0.4266 -0.0383 -0.0682 0.0370  167 SER   B N   
6640 C  CA  . SER   B 167 ? 0.2178 0.1723 0.4086 -0.0296 -0.0455 0.0390  167 SER   B CA  
6641 C  C   . SER   B 167 ? 0.2049 0.1837 0.3849 -0.0451 -0.0370 0.0613  167 SER   B C   
6642 O  O   . SER   B 167 ? 0.2052 0.1945 0.3659 -0.0539 -0.0347 0.0619  167 SER   B O   
6643 C  CB  . SER   B 167 ? 0.2059 0.1761 0.4056 -0.0339 -0.0162 0.0241  167 SER   B CB  
6644 O  OG  . SER   B 167 ? 0.2002 0.1839 0.3890 -0.0273 0.0002  0.0235  167 SER   B OG  
6650 N  N   . PHE   B 168 ? 0.2012 0.1836 0.3712 -0.0446 -0.0330 0.0657  168 PHE   B N   
6651 C  CA  . PHE   B 168 ? 0.2081 0.1728 0.3306 -0.0471 -0.0307 0.0423  168 PHE   B CA  
6652 C  C   . PHE   B 168 ? 0.1835 0.1618 0.2669 -0.0257 -0.0085 0.0154  168 PHE   B C   
6653 O  O   . PHE   B 168 ? 0.2099 0.1498 0.2795 -0.0056 -0.0074 0.0011  168 PHE   B O   
6654 C  CB  . PHE   B 168 ? 0.2194 0.1706 0.3457 -0.0577 -0.0417 0.0493  168 PHE   B CB  
6655 C  CG  . PHE   B 168 ? 0.2401 0.1571 0.3451 -0.0544 -0.0366 0.0259  168 PHE   B CG  
6656 C  CD1 . PHE   B 168 ? 0.2663 0.1700 0.3620 -0.0555 -0.0400 0.0155  168 PHE   B CD1 
6657 C  CD2 . PHE   B 168 ? 0.2256 0.1465 0.3400 -0.0445 -0.0382 0.0293  168 PHE   B CD2 
6658 C  CE1 . PHE   B 168 ? 0.2785 0.1744 0.3566 -0.0386 -0.0408 0.0205  168 PHE   B CE1 
6659 C  CE2 . PHE   B 168 ? 0.2539 0.1611 0.3482 -0.0286 -0.0428 0.0228  168 PHE   B CE2 
6660 C  CZ  . PHE   B 168 ? 0.2688 0.1550 0.3457 -0.0233 -0.0451 0.0396  168 PHE   B CZ  
6670 N  N   A LEU   B 169 ? 0.1919 0.1699 0.2571 -0.0055 0.0076  0.0029  169 LEU   B N   
6671 N  N   B LEU   B 169 ? 0.1928 0.1753 0.2633 -0.0092 0.0015  0.0106  169 LEU   B N   
6672 C  CA  A LEU   B 169 ? 0.2271 0.1981 0.2903 -0.0074 0.0033  -0.0294 169 LEU   B CA  
6673 C  CA  B LEU   B 169 ? 0.2152 0.1980 0.2821 -0.0025 0.0033  -0.0055 169 LEU   B CA  
6674 C  C   A LEU   B 169 ? 0.2531 0.2256 0.3481 0.0029  0.0047  -0.0532 169 LEU   B C   
6675 C  C   B LEU   B 169 ? 0.2294 0.2080 0.3068 0.0171  0.0060  -0.0187 169 LEU   B C   
6676 O  O   A LEU   B 169 ? 0.2694 0.2455 0.3976 -0.0057 0.0078  -0.0722 169 LEU   B O   
6677 O  O   B LEU   B 169 ? 0.2446 0.2199 0.3257 0.0168  0.0177  -0.0275 169 LEU   B O   
6678 C  CB  A LEU   B 169 ? 0.2540 0.2318 0.2978 -0.0092 -0.0093 -0.0051 169 LEU   B CB  
6679 C  CB  B LEU   B 169 ? 0.2332 0.2248 0.2918 -0.0092 -0.0026 0.0075  169 LEU   B CB  
6680 C  CG  A LEU   B 169 ? 0.2932 0.2674 0.3371 -0.0035 -0.0057 0.0053  169 LEU   B CG  
6681 C  CG  B LEU   B 169 ? 0.2576 0.2519 0.3186 -0.0092 0.0012  0.0122  169 LEU   B CG  
6682 C  CD1 A LEU   B 169 ? 0.3059 0.2832 0.3385 -0.0044 -0.0067 0.0200  169 LEU   B CD1 
6683 C  CD1 B LEU   B 169 ? 0.2647 0.2631 0.3196 -0.0110 0.0023  0.0201  169 LEU   B CD1 
6684 C  CD2 A LEU   B 169 ? 0.2968 0.2737 0.3458 0.0032  0.0039  -0.0051 169 LEU   B CD2 
6685 C  CD2 B LEU   B 169 ? 0.2598 0.2574 0.3248 -0.0051 0.0081  0.0051  169 LEU   B CD2 
6686 O  OXT A LEU   B 169 ? 0.2662 0.2412 0.3486 0.0325  0.0123  -0.0511 169 LEU   B OXT 
6687 O  OXT B LEU   B 169 ? 0.2328 0.2116 0.3100 0.0457  0.0033  -0.0191 169 LEU   B OXT 
6710 S  S   B DMS   C .   ? 0.1921 0.1752 0.1975 0.0172  0.0035  0.0322  301 DMS   A S   
6711 O  O   B DMS   C .   ? 0.1884 0.1803 0.1816 0.0054  -0.0157 0.0241  301 DMS   A O   
6712 C  C1  B DMS   C .   ? 0.2014 0.1807 0.2206 0.0132  -0.0064 0.0285  301 DMS   A C1  
6713 C  C2  B DMS   C .   ? 0.1997 0.1860 0.2238 0.0192  0.0003  0.0375  301 DMS   A C2  
6720 N  N2  B A1A58 D .   ? 0.1211 0.1754 0.0889 0.0036  0.0006  0.0455  302 A1A58 A N2  
6721 C  C3  B A1A58 D .   ? 0.1484 0.1702 0.1329 0.0198  0.0107  0.0184  302 A1A58 A C3  
6722 C  C6  B A1A58 D .   ? 0.1296 0.1689 0.0744 0.0219  -0.0109 0.0447  302 A1A58 A C6  
6723 C  C9  B A1A58 D .   ? 0.1360 0.1625 0.0992 0.0304  0.0029  0.0452  302 A1A58 A C9  
6724 C  C1  B A1A58 D .   ? 0.1237 0.1526 0.1303 0.0134  -0.0079 0.0288  302 A1A58 A C1  
6725 C  C10 B A1A58 D .   ? 0.1323 0.1685 0.1194 0.0305  0.0114  0.0352  302 A1A58 A C10 
6726 C  C11 B A1A58 D .   ? 0.1259 0.1602 0.1385 0.0269  0.0224  0.0308  302 A1A58 A C11 
6727 C  C2  B A1A58 D .   ? 0.1363 0.1600 0.1188 0.0197  -0.0039 0.0266  302 A1A58 A C2  
6728 C  C4  B A1A58 D .   ? 0.1473 0.1712 0.1136 0.0181  0.0119  0.0269  302 A1A58 A C4  
6729 C  C5  B A1A58 D .   ? 0.1405 0.1666 0.1079 0.0304  0.0049  0.0398  302 A1A58 A C5  
6730 C  C7  B A1A58 D .   ? 0.1194 0.1700 0.0628 0.0055  0.0259  0.0337  302 A1A58 A C7  
6731 C  C8  B A1A58 D .   ? 0.1397 0.1607 0.0973 0.0211  0.0046  0.0308  302 A1A58 A C8  
6732 F  F1  B A1A58 D .   ? 0.1455 0.1728 0.1235 0.0014  0.0196  0.0212  302 A1A58 A F1  
6733 N  N1  B A1A58 D .   ? 0.1291 0.1624 0.1003 0.0202  -0.0092 0.0321  302 A1A58 A N1  
6734 N  N3  B A1A58 D .   ? 0.1296 0.1668 0.0871 0.0124  0.0164  0.0312  302 A1A58 A N3  
6735 N  N4  B A1A58 D .   ? 0.1351 0.1548 0.1197 0.0293  0.0060  0.0108  302 A1A58 A N4  
6736 O  O1  B A1A58 D .   ? 0.1221 0.1466 0.1531 0.0100  0.0043  0.0374  302 A1A58 A O1  
6750 CL CL  B CL    E .   ? 0.1525 0.1274 0.1512 -0.0019 -0.0052 0.0181  303 CL    A CL  
6751 O  O   B HOH   F .   ? 0.5258 0.5770 0.5846 0.0350  0.1034  0.0429  401 HOH   A O   
6752 O  O   . HOH   F .   ? 0.4207 0.7740 0.4271 -0.1298 0.0335  0.0504  402 HOH   A O   
6753 O  O   . HOH   F .   ? 0.6326 0.4020 0.6225 -0.0359 -0.1330 0.0369  403 HOH   A O   
6754 O  O   . HOH   F .   ? 0.7488 0.5422 0.3679 -0.1289 -0.0072 0.1953  404 HOH   A O   
6755 O  O   . HOH   F .   ? 0.3930 0.3711 0.5311 -0.0038 0.1651  -0.0659 405 HOH   A O   
6756 O  O   . HOH   F .   ? 0.5356 0.6010 0.4718 -0.1008 -0.1048 -0.1054 406 HOH   A O   
6757 O  O   . HOH   F .   ? 0.4398 0.2446 0.3838 0.0640  0.0651  0.0600  407 HOH   A O   
6758 O  O   B HOH   F .   ? 0.2582 0.2088 0.3104 0.0620  -0.0661 0.0113  408 HOH   A O   
6759 O  O   . HOH   F .   ? 0.6153 0.4478 0.6551 -0.0716 0.1642  0.2100  409 HOH   A O   
6760 O  O   . HOH   F .   ? 0.6947 0.4788 0.3277 0.2027  -0.1208 0.0583  410 HOH   A O   
6761 O  O   . HOH   F .   ? 0.2072 0.1659 0.2406 0.0265  -0.0334 -0.0052 411 HOH   A O   
6762 O  O   . HOH   F .   ? 0.4905 0.1831 0.5665 0.0532  -0.0166 -0.0194 412 HOH   A O   
6763 O  O   . HOH   F .   ? 0.6721 0.4686 0.4205 -0.1471 0.1319  0.1539  413 HOH   A O   
6764 O  O   . HOH   F .   ? 0.2325 0.6136 0.3944 -0.0087 -0.0250 0.0881  414 HOH   A O   
6765 O  O   . HOH   F .   ? 0.3471 0.3481 0.1813 -0.0708 0.0586  0.0465  415 HOH   A O   
6766 O  O   B HOH   F .   ? 0.1579 0.1380 0.1640 -0.0006 -0.0143 0.0158  416 HOH   A O   
6767 O  O   . HOH   F .   ? 0.4795 0.6116 0.4048 0.2175  -0.0176 -0.0677 417 HOH   A O   
6768 O  O   . HOH   F .   ? 0.2725 0.6896 0.5517 -0.0128 -0.0423 0.2449  418 HOH   A O   
6769 O  O   . HOH   F .   ? 0.3179 0.4407 0.5292 0.1482  0.0278  -0.1266 419 HOH   A O   
6770 O  O   . HOH   F .   ? 0.5771 0.5808 0.3593 -0.0979 -0.0592 0.0743  420 HOH   A O   
6771 O  O   B HOH   F .   ? 0.1428 0.2142 0.2041 -0.0446 0.0380  -0.0009 421 HOH   A O   
6772 O  O   . HOH   F .   ? 0.1553 0.3964 0.2407 -0.0276 0.0237  0.0289  422 HOH   A O   
6773 O  O   . HOH   F .   ? 0.1736 0.4248 0.3257 0.0763  0.0080  0.0602  423 HOH   A O   
6774 O  O   . HOH   F .   ? 0.2002 0.1930 0.3692 -0.0473 0.0031  -0.0184 424 HOH   A O   
6775 O  O   . HOH   F .   ? 0.4286 0.3266 0.3329 -0.1130 0.0172  0.0900  425 HOH   A O   
6776 O  O   . HOH   F .   ? 0.3217 0.2574 0.4552 -0.0469 -0.0953 0.1161  426 HOH   A O   
6777 O  O   A HOH   F .   ? 0.3510 0.4783 0.3394 0.1752  -0.1145 -0.0935 427 HOH   A O   
6778 O  O   A HOH   F .   ? 0.2702 0.4621 0.5065 -0.0201 0.1049  0.2183  428 HOH   A O   
6779 O  O   . HOH   F .   ? 0.3509 0.3489 0.3747 -0.0382 0.1459  0.0257  429 HOH   A O   
6780 O  O   . HOH   F .   ? 0.3326 0.3562 0.5167 0.0077  0.1437  -0.0521 430 HOH   A O   
6781 O  O   . HOH   F .   ? 0.1671 0.1668 0.2208 -0.0086 0.0218  0.0252  431 HOH   A O   
6782 O  O   . HOH   F .   ? 0.4321 0.5221 0.3486 0.1356  0.0696  -0.0791 432 HOH   A O   
6783 O  O   . HOH   F .   ? 0.2155 0.3338 0.3625 -0.0351 -0.0544 0.1045  433 HOH   A O   
6784 O  O   B HOH   F .   ? 0.1529 0.1614 0.1648 0.0176  0.0515  0.0706  434 HOH   A O   
6785 O  O   . HOH   F .   ? 0.6681 0.5297 0.4856 0.0806  -0.0658 -0.0451 435 HOH   A O   
6786 O  O   . HOH   F .   ? 0.1982 0.3495 0.4364 -0.0314 0.0499  -0.0974 436 HOH   A O   
6787 O  O   . HOH   F .   ? 0.4803 0.4100 0.2741 -0.1712 -0.0915 0.0197  437 HOH   A O   
6788 O  O   . HOH   F .   ? 0.2392 0.2921 0.3774 -0.0217 0.0702  -0.0666 438 HOH   A O   
6789 O  O   . HOH   F .   ? 0.4016 0.3435 0.3225 -0.1594 0.0198  0.0442  439 HOH   A O   
6790 O  O   . HOH   F .   ? 0.1468 0.1552 0.2262 -0.0180 0.0089  0.0040  440 HOH   A O   
6791 O  O   . HOH   F .   ? 0.4765 0.5759 0.3126 -0.1464 0.1380  0.0941  441 HOH   A O   
6792 O  O   . HOH   F .   ? 0.2282 0.2185 0.2689 0.0340  0.0285  0.0304  442 HOH   A O   
6793 O  O   . HOH   F .   ? 0.1479 0.1620 0.2441 0.0029  -0.0221 -0.0292 443 HOH   A O   
6794 O  O   . HOH   F .   ? 0.3249 0.4186 0.2611 -0.0500 0.0403  0.0531  444 HOH   A O   
6795 O  O   . HOH   F .   ? 0.2159 0.1636 0.1683 0.0022  0.0303  0.0128  445 HOH   A O   
6796 O  O   B HOH   F .   ? 0.1475 0.3085 0.3345 0.0019  0.0192  0.1392  446 HOH   A O   
6797 O  O   . HOH   F .   ? 0.5252 0.4013 0.3033 0.0548  0.0947  0.1075  447 HOH   A O   
6798 O  O   . HOH   F .   ? 0.5186 0.2042 0.4624 0.0716  -0.0141 0.0840  448 HOH   A O   
6799 O  O   . HOH   F .   ? 0.2124 0.1669 0.2702 -0.0121 -0.0369 -0.0012 449 HOH   A O   
6800 O  O   . HOH   F .   ? 0.4795 0.3697 0.4612 -0.1591 0.0641  0.1687  450 HOH   A O   
6801 O  O   . HOH   F .   ? 0.1469 0.2153 0.2152 -0.0020 -0.0096 0.0455  451 HOH   A O   
6802 O  O   . HOH   F .   ? 0.2675 0.1804 0.2640 0.0009  0.0215  0.0114  452 HOH   A O   
6803 O  O   . HOH   F .   ? 0.3144 0.3410 0.2423 -0.0871 -0.0206 -0.0657 453 HOH   A O   
6804 O  O   . HOH   F .   ? 0.1770 0.1646 0.2097 0.0101  -0.0159 0.0221  454 HOH   A O   
6805 O  O   A HOH   F .   ? 0.2508 0.2124 0.2995 -0.0022 0.0917  0.0400  455 HOH   A O   
6806 O  O   . HOH   F .   ? 0.5812 0.5642 0.4937 0.0104  0.2516  -0.0812 456 HOH   A O   
6807 O  O   . HOH   F .   ? 0.1972 0.2252 0.2710 -0.0193 -0.0127 0.0751  457 HOH   A O   
6808 O  O   . HOH   F .   ? 0.2587 0.3782 0.3816 -0.0786 -0.0509 -0.0551 458 HOH   A O   
6809 O  O   . HOH   F .   ? 0.3172 0.6181 0.7283 0.0975  0.1460  0.0871  459 HOH   A O   
6810 O  O   . HOH   F .   ? 0.1754 0.2160 0.1989 -0.0189 0.0023  0.0640  460 HOH   A O   
6811 O  O   . HOH   F .   ? 0.2405 0.4138 0.3594 0.0894  -0.0822 -0.0041 461 HOH   A O   
6812 O  O   . HOH   F .   ? 0.6207 0.5512 0.7307 -0.1210 -0.0497 0.1187  462 HOH   A O   
6813 O  O   . HOH   F .   ? 0.1400 0.1943 0.2640 0.0034  -0.0121 0.0132  463 HOH   A O   
6814 O  O   . HOH   F .   ? 0.3813 0.5028 0.4411 0.2023  0.0282  0.0534  464 HOH   A O   
6815 O  O   . HOH   F .   ? 0.1865 0.2267 0.3665 0.0141  0.0723  -0.0622 465 HOH   A O   
6816 O  O   B HOH   F .   ? 0.1792 0.1174 0.2531 -0.0312 -0.0310 0.0166  466 HOH   A O   
6817 O  O   . HOH   F .   ? 0.1991 0.2045 0.3539 0.0167  0.0860  0.0046  467 HOH   A O   
6818 O  O   . HOH   F .   ? 0.5032 0.2579 0.3621 -0.1653 0.1623  -0.0704 468 HOH   A O   
6819 O  O   . HOH   F .   ? 0.2854 0.3113 0.4503 -0.0515 -0.0798 -0.0684 469 HOH   A O   
6820 O  O   . HOH   F .   ? 0.2656 0.1954 0.2365 -0.0404 0.0277  -0.0282 470 HOH   A O   
6821 O  O   . HOH   F .   ? 0.3764 0.3119 0.3767 -0.1115 -0.0070 -0.0280 471 HOH   A O   
6822 O  O   . HOH   F .   ? 0.3299 0.4351 0.5744 0.0436  -0.0725 0.1106  472 HOH   A O   
6823 O  O   . HOH   F .   ? 0.1329 0.1255 0.1608 0.0010  0.0136  0.0126  473 HOH   A O   
6824 O  O   . HOH   F .   ? 0.3202 0.4807 0.4363 0.0205  -0.0579 0.0802  474 HOH   A O   
6825 O  O   . HOH   F .   ? 0.2438 0.4092 0.3442 -0.0465 0.0410  -0.0306 475 HOH   A O   
6826 O  O   . HOH   F .   ? 0.1791 0.1891 0.2555 -0.0304 0.0181  0.0316  476 HOH   A O   
6827 O  O   . HOH   F .   ? 0.7573 0.3648 0.6353 -0.0346 -0.1231 0.0523  477 HOH   A O   
6828 O  O   A HOH   F .   ? 0.3640 0.1593 0.1976 0.0451  0.0154  0.0086  478 HOH   A O   
6829 O  O   . HOH   F .   ? 0.1419 0.1645 0.1554 -0.0042 -0.0121 -0.0097 479 HOH   A O   
6830 O  O   . HOH   F .   ? 0.4160 0.2197 0.2921 0.1172  0.0563  0.0234  480 HOH   A O   
6831 O  O   . HOH   F .   ? 0.2711 0.3103 0.3420 -0.0940 0.1020  -0.0362 481 HOH   A O   
6832 O  O   . HOH   F .   ? 0.4156 0.6788 0.5969 -0.0887 -0.1365 0.0630  482 HOH   A O   
6833 O  O   B HOH   F .   ? 0.2650 0.2629 0.2431 0.0284  0.0307  -0.0129 483 HOH   A O   
6834 O  O   . HOH   F .   ? 0.1603 0.1333 0.2291 -0.0112 0.0245  -0.0077 484 HOH   A O   
6835 O  O   A HOH   F .   ? 0.2155 0.3221 0.2454 0.0652  0.0602  0.1140  485 HOH   A O   
6836 O  O   . HOH   F .   ? 0.3119 0.3309 0.2881 -0.0147 -0.0967 0.0515  486 HOH   A O   
6837 O  O   . HOH   F .   ? 0.1916 0.2192 0.2237 -0.0244 -0.0442 0.0387  487 HOH   A O   
6838 O  O   A HOH   F .   ? 0.1970 0.3365 0.2641 0.0881  0.0470  0.0836  488 HOH   A O   
6839 O  O   . HOH   F .   ? 0.2842 0.6189 0.3655 0.1259  0.0285  -0.1195 489 HOH   A O   
6840 O  O   . HOH   F .   ? 0.4031 0.2166 0.4729 -0.0963 0.1194  -0.0030 490 HOH   A O   
6841 O  O   . HOH   F .   ? 0.1972 0.1756 0.1878 -0.0038 0.0144  0.0184  491 HOH   A O   
6842 O  O   B HOH   F .   ? 0.1706 0.2137 0.1594 0.0542  0.0055  0.0211  492 HOH   A O   
6843 O  O   . HOH   F .   ? 1.0324 0.9198 0.8089 0.0037  -0.0889 -0.1203 493 HOH   A O   
6844 O  O   . HOH   F .   ? 0.2951 0.2976 0.2239 0.0191  0.0567  0.0054  494 HOH   A O   
6845 O  O   . HOH   F .   ? 0.3127 0.2533 0.3264 -0.0039 -0.0453 0.0774  495 HOH   A O   
6846 O  O   . HOH   F .   ? 0.2333 0.1992 0.1903 -0.0466 0.0250  0.0232  496 HOH   A O   
6847 O  O   . HOH   F .   ? 0.3002 0.4384 0.3380 0.0646  0.0792  0.1987  497 HOH   A O   
6848 O  O   . HOH   F .   ? 0.2703 0.4041 0.3694 -0.0487 0.1181  -0.0795 498 HOH   A O   
6849 O  O   . HOH   F .   ? 0.3468 0.6026 0.4228 -0.0849 0.0243  0.1140  499 HOH   A O   
6850 O  O   . HOH   F .   ? 0.1852 0.1839 0.3830 0.0360  0.0967  0.0792  500 HOH   A O   
6851 O  O   . HOH   F .   ? 0.3126 0.2363 0.4872 -0.0403 -0.0056 -0.0425 501 HOH   A O   
6852 O  O   A HOH   F .   ? 0.4631 0.5251 0.4483 -0.1429 0.1652  0.0264  502 HOH   A O   
6853 O  O   . HOH   F .   ? 0.3105 0.2486 0.2253 -0.0552 -0.1088 0.0233  503 HOH   A O   
6854 O  O   . HOH   F .   ? 0.1628 0.1448 0.1672 -0.0241 0.0137  -0.0036 504 HOH   A O   
6855 O  O   . HOH   F .   ? 0.5747 0.6622 0.5823 0.0815  -0.1223 0.1423  505 HOH   A O   
6856 O  O   . HOH   F .   ? 0.2119 0.1750 0.2989 0.0071  -0.0302 0.0069  506 HOH   A O   
6857 O  O   . HOH   F .   ? 0.2491 0.2749 0.3904 -0.0085 -0.0039 -0.0656 507 HOH   A O   
6858 O  O   . HOH   F .   ? 0.1424 0.1418 0.1794 0.0062  -0.0216 0.0047  508 HOH   A O   
6859 O  O   . HOH   F .   ? 0.2224 0.2239 0.3023 0.0137  -0.0565 0.0146  509 HOH   A O   
6860 O  O   . HOH   F .   ? 0.4569 0.4889 0.2147 0.0429  0.0871  0.0941  510 HOH   A O   
6861 O  O   . HOH   F .   ? 0.2275 0.2355 0.4442 0.0072  -0.0358 -0.0451 511 HOH   A O   
6862 O  O   . HOH   F .   ? 0.4342 0.4709 0.5505 0.0057  0.0456  0.2549  512 HOH   A O   
6863 O  O   A HOH   F .   ? 0.1210 0.1217 0.1588 0.0020  -0.0126 0.0074  513 HOH   A O   
6864 O  O   . HOH   F .   ? 0.1969 0.2760 0.3802 -0.0268 -0.0301 0.0182  514 HOH   A O   
6865 O  O   . HOH   F .   ? 0.5143 0.3843 0.3627 0.1733  -0.0862 -0.1300 515 HOH   A O   
6866 O  O   B HOH   F .   ? 0.1877 0.2507 0.1605 0.0992  0.0514  0.0982  516 HOH   A O   
6867 O  O   . HOH   F .   ? 0.3713 0.2262 0.5878 0.0585  0.1434  0.0611  517 HOH   A O   
6868 O  O   . HOH   F .   ? 0.4572 0.6588 0.5388 0.2606  0.0201  0.1204  518 HOH   A O   
6869 O  O   . HOH   F .   ? 0.3171 0.1293 0.2154 -0.0034 -0.0376 0.0130  519 HOH   A O   
6870 O  O   . HOH   F .   ? 0.2459 0.2134 0.2801 -0.0461 -0.0019 0.0502  520 HOH   A O   
6871 O  O   . HOH   F .   ? 0.3767 0.2251 0.5534 -0.0628 -0.2250 0.0938  521 HOH   A O   
6872 O  O   . HOH   F .   ? 0.7999 0.7806 0.6560 -0.1317 -0.0469 0.0068  522 HOH   A O   
6873 O  O   . HOH   F .   ? 0.1547 0.1722 0.2882 0.0029  0.0127  0.0186  523 HOH   A O   
6874 O  O   A HOH   F .   ? 0.2276 0.2560 0.3039 0.0195  0.0624  0.1105  524 HOH   A O   
6875 O  O   . HOH   F .   ? 0.2144 0.2662 0.2844 -0.0146 -0.0587 0.0444  525 HOH   A O   
6876 O  O   . HOH   F .   ? 0.3502 0.3779 0.2632 -0.0346 -0.0422 0.0045  526 HOH   A O   
6877 O  O   . HOH   F .   ? 0.2709 0.3506 0.6943 -0.0233 0.0500  -0.0768 527 HOH   A O   
6878 O  O   . HOH   F .   ? 0.4001 0.6659 0.3862 -0.1033 -0.0126 0.1845  528 HOH   A O   
6879 O  O   A HOH   F .   ? 0.1330 0.2302 0.3906 -0.0176 0.0591  0.0381  529 HOH   A O   
6880 O  O   A HOH   F .   ? 0.1431 0.1359 0.1397 -0.0109 -0.0074 0.0260  530 HOH   A O   
6881 O  O   . HOH   F .   ? 0.2843 0.5886 0.1712 -0.0013 0.0478  0.0257  531 HOH   A O   
6882 O  O   . HOH   F .   ? 0.2282 0.4007 0.2743 0.1351  -0.0079 0.0181  532 HOH   A O   
6883 O  O   . HOH   F .   ? 0.5138 0.3308 0.4205 0.0706  -0.0029 0.0140  533 HOH   A O   
6884 O  O   . HOH   F .   ? 0.1690 0.2245 0.2700 -0.0212 0.0094  0.0423  534 HOH   A O   
6885 O  O   . HOH   F .   ? 0.5089 0.6609 0.3304 0.0176  0.2317  -0.0365 535 HOH   A O   
6886 O  O   . HOH   F .   ? 0.6831 0.4253 0.5735 0.1439  -0.0446 0.1644  536 HOH   A O   
6887 O  O   . HOH   F .   ? 0.5014 0.6094 0.7218 -0.0070 -0.0590 -0.0966 537 HOH   A O   
6888 O  O   . HOH   F .   ? 0.4620 0.4650 0.3698 -0.0323 -0.1730 0.0199  538 HOH   A O   
6889 O  O   . HOH   F .   ? 0.5549 0.6231 0.6508 -0.1686 0.0329  -0.1336 539 HOH   A O   
6890 O  O   A HOH   F .   ? 0.1450 0.1435 0.1416 0.0092  -0.0347 -0.0092 540 HOH   A O   
6891 O  O   . HOH   F .   ? 0.6761 0.5071 0.8442 -0.1495 0.0472  -0.0025 541 HOH   A O   
6892 O  O   B HOH   F .   ? 0.1047 0.1293 0.2612 -0.0036 0.0290  0.0789  542 HOH   A O   
6893 O  O   A HOH   F .   ? 0.1831 0.1621 0.2237 0.0380  -0.0470 0.0067  543 HOH   A O   
6894 O  O   . HOH   F .   ? 0.3612 0.2608 0.1872 -0.0935 0.0289  0.0193  544 HOH   A O   
6895 O  O   . HOH   F .   ? 0.6622 0.6168 0.5945 0.0522  -0.0843 0.0196  545 HOH   A O   
6896 O  O   . HOH   F .   ? 0.1831 0.2016 0.4615 -0.0129 -0.0708 0.0556  546 HOH   A O   
6897 O  O   A HOH   F .   ? 0.5545 0.2505 0.6273 -0.0174 0.0304  -0.0957 547 HOH   A O   
6898 O  O   . HOH   F .   ? 0.2591 0.1665 0.2852 0.0169  0.0245  0.0192  548 HOH   A O   
6899 O  O   . HOH   F .   ? 0.2399 0.2135 0.2634 0.0175  0.0251  0.0356  549 HOH   A O   
6900 O  O   . HOH   F .   ? 0.3865 0.3477 0.3302 0.2137  -0.0610 -0.0635 550 HOH   A O   
6901 O  O   . HOH   F .   ? 0.7271 0.7909 0.4562 0.2597  -0.1148 0.1736  551 HOH   A O   
6902 O  O   A HOH   F .   ? 0.2815 0.1893 0.2537 -0.0021 -0.0763 -0.0148 552 HOH   A O   
6903 O  O   . HOH   F .   ? 0.4467 0.4442 0.5289 -0.0548 -0.1034 -0.1337 553 HOH   A O   
6904 O  O   . HOH   F .   ? 0.2507 0.2826 0.4387 0.0209  0.0518  -0.0696 554 HOH   A O   
6905 O  O   . HOH   F .   ? 0.2061 0.2784 0.2502 0.0100  -0.0010 -0.0416 555 HOH   A O   
6906 O  O   A HOH   F .   ? 0.5384 0.2619 0.4591 0.1543  0.1460  0.1156  556 HOH   A O   
6907 O  O   . HOH   F .   ? 0.6118 0.5818 0.8230 0.0512  -0.1129 0.1626  557 HOH   A O   
6908 O  O   . HOH   F .   ? 0.4558 0.4391 0.4910 0.0330  -0.0427 0.1150  558 HOH   A O   
6909 O  O   . HOH   F .   ? 0.6642 0.6705 0.5516 -0.0573 0.1619  0.1283  559 HOH   A O   
6910 O  O   . HOH   F .   ? 0.4980 0.4117 0.3732 0.0521  0.0762  0.0062  560 HOH   A O   
6911 O  O   . HOH   F .   ? 0.4881 0.3116 0.4744 0.0744  0.1191  0.0231  561 HOH   A O   
6912 O  O   . HOH   F .   ? 0.2897 0.2746 0.3451 0.0477  -0.0653 0.0158  562 HOH   A O   
6913 O  O   . HOH   F .   ? 0.2800 0.2893 0.3383 -0.0567 0.0300  -0.0780 563 HOH   A O   
6914 O  O   . HOH   F .   ? 0.7357 0.7463 0.4926 -0.0321 -0.1111 -0.0438 564 HOH   A O   
6915 O  O   . HOH   F .   ? 0.3118 0.4956 0.5479 -0.1639 0.1190  -0.1711 565 HOH   A O   
6916 O  O   B HOH   F .   ? 0.4207 0.4220 0.5305 -0.0110 -0.0048 -0.0240 566 HOH   A O   
6917 O  O   . HOH   F .   ? 0.3928 0.5362 0.4629 0.1081  -0.1030 0.1592  567 HOH   A O   
6918 O  O   . HOH   F .   ? 0.3844 0.4380 0.3385 -0.0871 -0.0344 0.0200  568 HOH   A O   
6919 O  O   . HOH   F .   ? 0.2494 0.2498 0.3292 -0.0600 0.0472  -0.0303 569 HOH   A O   
6920 O  O   B HOH   F .   ? 0.1245 0.1047 0.2020 -0.0133 -0.0143 -0.0068 570 HOH   A O   
6921 O  O   . HOH   F .   ? 0.6165 0.3767 0.8036 0.0810  0.1078  0.2684  571 HOH   A O   
6922 O  O   B HOH   F .   ? 0.1264 0.2224 0.2894 0.0026  -0.0151 0.0525  572 HOH   A O   
6923 O  O   . HOH   F .   ? 0.3121 0.3949 0.4765 0.0613  0.0111  -0.1872 573 HOH   A O   
6924 O  O   A HOH   F .   ? 0.2038 0.2786 0.5130 0.0213  -0.0864 -0.0741 574 HOH   A O   
6925 O  O   . HOH   F .   ? 0.4284 0.6266 0.4022 -0.0589 -0.0717 0.2183  575 HOH   A O   
6926 O  O   B HOH   F .   ? 0.3251 0.4776 0.3573 0.1107  0.0148  0.1314  576 HOH   A O   
6927 O  O   . HOH   F .   ? 0.2745 0.2533 0.3488 0.0029  0.0519  -0.0018 577 HOH   A O   
6928 O  O   . HOH   F .   ? 0.2861 0.1738 0.2698 0.0411  -0.0803 -0.0262 578 HOH   A O   
6929 O  O   . HOH   F .   ? 0.5786 0.4688 0.4487 0.0758  0.1177  0.0398  579 HOH   A O   
6930 O  O   . HOH   F .   ? 0.7603 0.6373 0.5946 0.1241  0.2366  0.1692  580 HOH   A O   
6931 O  O   . HOH   F .   ? 0.4341 0.5348 0.3482 0.0488  -0.0674 -0.0494 581 HOH   A O   
6932 O  O   B HOH   F .   ? 0.1858 0.1708 0.2556 0.0004  0.0124  0.0505  582 HOH   A O   
6933 O  O   . HOH   F .   ? 0.4019 0.4718 0.4331 -0.2276 -0.0129 -0.0118 583 HOH   A O   
6934 O  O   . HOH   F .   ? 0.2500 0.2593 0.2604 0.0360  0.0068  0.0095  584 HOH   A O   
6935 O  O   . HOH   F .   ? 0.4630 0.2751 0.3693 -0.0476 -0.1103 0.0603  585 HOH   A O   
6936 O  O   . HOH   F .   ? 0.6056 0.7036 0.5779 -0.1468 -0.1395 0.0432  586 HOH   A O   
6937 O  O   . HOH   F .   ? 0.5878 0.5837 0.4149 0.1684  -0.1185 -0.0709 587 HOH   A O   
6938 O  O   . HOH   F .   ? 0.5814 0.4693 0.3947 -0.0178 0.0336  -0.1325 588 HOH   A O   
6939 O  O   B HOH   F .   ? 0.3949 0.2203 0.2195 0.0013  -0.0358 0.0162  589 HOH   A O   
6940 O  O   B HOH   F .   ? 0.1363 0.1834 0.2308 0.0098  -0.0158 0.0642  590 HOH   A O   
6941 O  O   . HOH   F .   ? 0.8233 0.4210 0.3306 -0.0741 -0.1099 0.0055  591 HOH   A O   
6942 O  O   . HOH   F .   ? 0.7447 0.7588 0.5126 -0.1189 0.1381  0.1639  592 HOH   A O   
6943 O  O   . HOH   F .   ? 0.4147 0.5004 0.3046 0.0231  -0.0178 0.0335  593 HOH   A O   
6944 O  O   . HOH   F .   ? 0.6502 0.4084 0.4397 0.0012  0.1410  0.0233  594 HOH   A O   
6945 O  O   . HOH   F .   ? 0.4783 0.4439 0.3526 -0.0645 -0.0354 -0.0286 595 HOH   A O   
6946 O  O   . HOH   F .   ? 0.6877 0.4737 0.6646 -0.1108 0.1238  -0.0164 596 HOH   A O   
6947 O  O   . HOH   F .   ? 0.3212 0.4920 0.4853 0.0450  0.1439  0.1485  597 HOH   A O   
6948 O  O   . HOH   F .   ? 0.6293 0.4830 0.5213 -0.1023 -0.0525 -0.0748 598 HOH   A O   
6949 O  O   . HOH   F .   ? 0.2766 0.3070 0.5071 0.0111  0.1070  -0.0596 599 HOH   A O   
6950 O  O   . HOH   F .   ? 0.3710 0.1997 0.6089 0.0257  0.1403  0.0797  600 HOH   A O   
6951 O  O   . HOH   F .   ? 0.2530 0.5440 0.3774 0.0940  0.0999  0.2359  601 HOH   A O   
6952 O  O   B HOH   F .   ? 0.1912 0.3965 0.1705 -0.0078 -0.0049 0.0494  602 HOH   A O   
6953 O  O   . HOH   F .   ? 0.2593 0.2382 0.6791 -0.0052 -0.1191 0.0177  603 HOH   A O   
6954 O  O   . HOH   F .   ? 0.4929 0.3110 0.4930 -0.1203 0.1203  0.0546  604 HOH   A O   
6955 O  O   . HOH   F .   ? 0.5051 0.7043 0.5319 -0.0130 -0.1304 0.0679  605 HOH   A O   
6956 O  O   . HOH   F .   ? 0.5811 0.2726 0.5080 -0.0798 0.1131  0.0529  606 HOH   A O   
6957 O  O   . HOH   F .   ? 0.5185 0.5431 0.6387 0.0537  0.2091  -0.1107 607 HOH   A O   
6958 O  O   . HOH   F .   ? 0.3916 0.3266 0.2451 -0.0416 0.1095  -0.0163 608 HOH   A O   
6959 O  O   B HOH   F .   ? 0.1547 0.1774 0.2236 -0.0204 -0.0169 0.0605  609 HOH   A O   
6960 O  O   . HOH   F .   ? 0.4606 0.3078 0.4522 0.0113  0.2336  0.0390  610 HOH   A O   
6961 O  O   B HOH   F .   ? 0.1551 0.1903 0.2063 -0.0091 -0.0183 0.0819  611 HOH   A O   
6962 O  O   B HOH   F .   ? 0.2883 0.1635 0.3203 0.0594  -0.0451 0.0859  612 HOH   A O   
6963 O  O   . HOH   F .   ? 0.3821 0.8658 0.5531 -0.1330 -0.0357 0.2496  613 HOH   A O   
6964 O  O   . HOH   F .   ? 0.5970 0.7151 0.5937 0.0930  0.0603  0.1662  614 HOH   A O   
6965 O  O   . HOH   F .   ? 0.2807 0.5017 0.3430 -0.0064 -0.0379 -0.0663 615 HOH   A O   
6966 O  O   . HOH   F .   ? 0.2298 0.3086 0.4229 0.0354  -0.0417 0.0572  616 HOH   A O   
6967 O  O   . HOH   F .   ? 0.6943 0.6604 0.4784 0.2583  -0.1174 0.0917  617 HOH   A O   
6968 O  O   . HOH   F .   ? 0.4633 0.2895 0.4856 -0.1494 0.0020  0.0396  618 HOH   A O   
6969 O  O   . HOH   F .   ? 0.3051 0.3987 0.3869 0.0614  -0.0109 0.0013  619 HOH   A O   
6970 O  O   B HOH   F .   ? 0.2522 0.1616 0.2379 0.0348  -0.0297 0.0255  620 HOH   A O   
6971 O  O   . HOH   F .   ? 0.6647 0.3753 0.5093 -0.0270 -0.0015 0.0994  621 HOH   A O   
6972 O  O   . HOH   F .   ? 0.3310 0.2223 0.4468 0.0309  0.0240  0.0501  622 HOH   A O   
6973 O  O   . HOH   F .   ? 0.4771 0.6845 0.5467 0.3014  0.0016  0.1231  623 HOH   A O   
6974 O  O   . HOH   F .   ? 0.5043 0.5650 0.4447 0.0373  -0.1107 -0.1058 624 HOH   A O   
6975 O  O   B HOH   F .   ? 0.2405 0.1683 0.3134 0.0113  0.0459  0.0823  625 HOH   A O   
6976 O  O   A HOH   F .   ? 0.2737 0.4362 0.3021 0.0473  0.0454  -0.0139 626 HOH   A O   
6977 O  O   . HOH   F .   ? 0.2500 0.8083 0.3362 0.0896  0.0179  0.0876  627 HOH   A O   
6978 O  O   . HOH   F .   ? 0.5058 0.4543 0.3841 0.0781  0.0242  0.1117  628 HOH   A O   
6979 O  O   . HOH   F .   ? 0.4931 0.6699 0.5250 -0.0717 -0.0622 0.0900  629 HOH   A O   
6980 O  O   B HOH   F .   ? 0.2983 0.2789 0.3547 0.0116  0.0960  0.0956  630 HOH   A O   
6981 O  O   B HOH   F .   ? 0.2466 0.2967 0.3793 0.1343  0.0241  0.0491  631 HOH   A O   
6982 O  O   B HOH   F .   ? 0.2081 0.2111 0.3683 -0.0365 -0.0280 0.0799  632 HOH   A O   
6983 O  O   . HOH   F .   ? 0.3970 0.4036 0.5122 -0.0486 -0.0897 0.2056  633 HOH   A O   
6984 O  O   . HOH   G .   ? 0.2381 0.2046 0.2879 0.0250  0.0547  0.0281  201 HOH   B O   
6985 O  O   . HOH   G .   ? 0.2928 0.5849 0.4511 0.0042  0.1321  -0.1986 202 HOH   B O   
6986 O  O   . HOH   G .   ? 0.3711 0.2566 0.6637 -0.0119 0.0938  0.0352  203 HOH   B O   
6987 O  O   . HOH   G .   ? 0.4998 0.3719 0.3767 -0.0031 0.0204  -0.1852 204 HOH   B O   
6988 O  O   . HOH   G .   ? 0.2983 0.6936 0.3959 0.1284  0.0395  0.2234  205 HOH   B O   
6989 O  O   . HOH   G .   ? 0.7310 0.3555 0.5589 0.0413  0.1782  -0.0505 206 HOH   B O   
6990 O  O   . HOH   G .   ? 0.2924 0.1882 0.5171 0.0070  0.1756  0.0561  207 HOH   B O   
6991 O  O   . HOH   G .   ? 0.3425 0.4222 0.5582 -0.0979 0.0098  -0.1593 208 HOH   B O   
6992 O  O   . HOH   G .   ? 0.5633 0.6571 0.5171 0.1779  0.0096  -0.0180 209 HOH   B O   
6993 O  O   . HOH   G .   ? 0.4733 0.5502 0.4274 0.2802  -0.1219 -0.0365 210 HOH   B O   
6994 O  O   . HOH   G .   ? 0.1607 0.1957 0.2839 -0.0158 0.0018  0.0174  211 HOH   B O   
6995 O  O   . HOH   G .   ? 0.3969 0.5418 0.2324 0.0403  -0.0265 -0.1066 212 HOH   B O   
6996 O  O   . HOH   G .   ? 0.2050 0.2179 0.3118 0.0027  0.0308  -0.0307 213 HOH   B O   
6997 O  O   . HOH   G .   ? 0.3925 0.5340 0.4406 0.2261  -0.0032 0.0212  214 HOH   B O   
6998 O  O   . HOH   G .   ? 0.2592 0.2539 0.5984 0.0523  -0.0783 0.0462  215 HOH   B O   
6999 O  O   . HOH   G .   ? 0.3672 0.3410 0.3950 0.0235  -0.1052 0.0210  216 HOH   B O   
7000 O  O   . HOH   G .   ? 0.3789 0.5342 0.5589 0.2383  0.0257  -0.0909 217 HOH   B O   
7001 O  O   . HOH   G .   ? 0.4280 0.4729 0.4475 0.0452  0.0900  -0.1915 218 HOH   B O   
7002 O  O   . HOH   G .   ? 0.4226 0.3682 0.6478 -0.0190 -0.1566 -0.0882 219 HOH   B O   
7003 O  O   . HOH   G .   ? 0.5108 0.2044 0.2701 0.0054  -0.0752 0.0090  220 HOH   B O   
7004 O  O   . HOH   G .   ? 0.4920 0.3241 0.3351 -0.1683 0.0280  -0.0154 221 HOH   B O   
7005 O  O   . HOH   G .   ? 0.3483 0.2493 0.4912 0.0576  -0.1286 -0.0708 222 HOH   B O   
7006 O  O   . HOH   G .   ? 0.1829 0.2290 0.3084 -0.0156 0.0223  -0.0331 223 HOH   B O   
7007 O  O   . HOH   G .   ? 0.2123 0.2120 0.3917 -0.0264 0.0121  -0.0525 224 HOH   B O   
7008 O  O   . HOH   G .   ? 0.5855 0.4842 0.6337 0.0932  -0.0708 0.2964  225 HOH   B O   
7009 O  O   . HOH   G .   ? 0.3454 0.3184 0.2308 0.0352  0.0607  0.0539  226 HOH   B O   
7010 O  O   . HOH   G .   ? 0.3902 0.3826 0.5064 -0.1435 0.0037  0.0776  227 HOH   B O   
7011 O  O   . HOH   G .   ? 0.2649 0.1761 0.2728 -0.0309 0.1059  0.0039  228 HOH   B O   
7012 O  O   . HOH   G .   ? 0.2131 0.2845 0.3376 -0.0574 0.0010  -0.0066 229 HOH   B O   
7013 O  O   . HOH   G .   ? 0.3615 0.2324 0.4207 0.0727  -0.0655 -0.0676 230 HOH   B O   
7014 O  O   . HOH   G .   ? 0.4510 0.3302 0.3072 0.0687  0.0099  -0.0853 231 HOH   B O   
7015 O  O   . HOH   G .   ? 0.2541 0.2591 0.3296 0.0265  0.0094  -0.0945 232 HOH   B O   
7016 O  O   . HOH   G .   ? 0.2759 0.3286 0.3296 -0.0847 0.0320  -0.0079 233 HOH   B O   
7017 O  O   . HOH   G .   ? 0.3629 0.2418 0.4486 0.0420  -0.0820 -0.1148 234 HOH   B O   
7018 O  O   . HOH   G .   ? 0.3633 0.1969 0.2024 0.0223  -0.0743 -0.0212 235 HOH   B O   
7019 O  O   . HOH   G .   ? 0.2930 0.1764 0.6160 -0.0030 -0.1280 -0.0297 236 HOH   B O   
7020 O  O   . HOH   G .   ? 0.3137 0.2294 0.5065 0.0024  0.1834  0.0222  237 HOH   B O   
7021 O  O   . HOH   G .   ? 0.6767 0.5014 0.4610 0.1635  -0.0038 -0.1314 238 HOH   B O   
7022 O  O   . HOH   G .   ? 0.1494 0.1424 0.1537 -0.0109 -0.0006 -0.0010 239 HOH   B O   
7023 O  O   . HOH   G .   ? 0.2431 0.2068 0.2501 0.0694  -0.0754 -0.0528 240 HOH   B O   
7024 O  O   . HOH   G .   ? 0.5110 0.7451 0.4137 0.2944  0.0797  0.0470  241 HOH   B O   
7025 O  O   . HOH   G .   ? 0.6092 0.3368 0.2769 0.0078  0.0678  -0.0607 242 HOH   B O   
7026 O  O   . HOH   G .   ? 0.2056 0.1323 0.3676 0.0158  -0.0594 -0.0205 243 HOH   B O   
7027 O  O   . HOH   G .   ? 0.1969 0.3482 0.2377 -0.0153 -0.0073 0.0395  244 HOH   B O   
7028 O  O   . HOH   G .   ? 0.2719 0.2189 0.2971 0.0755  0.0779  0.0072  245 HOH   B O   
7029 O  O   . HOH   G .   ? 0.2283 0.2916 0.2261 -0.0496 0.0264  0.0449  246 HOH   B O   
7030 O  O   . HOH   G .   ? 0.5010 0.3031 0.4374 -0.2196 0.0170  -0.0028 247 HOH   B O   
7031 O  O   . HOH   G .   ? 0.2034 0.1542 0.2208 -0.0218 -0.0366 0.0215  248 HOH   B O   
7032 O  O   . HOH   G .   ? 0.1441 0.1354 0.1694 -0.0030 -0.0064 0.0078  249 HOH   B O   
7033 O  O   . HOH   G .   ? 0.5202 0.5925 0.3450 -0.0615 -0.0565 -0.0167 250 HOH   B O   
7034 O  O   . HOH   G .   ? 0.3081 0.4567 0.5335 -0.0268 -0.0044 -0.1326 251 HOH   B O   
7035 O  O   . HOH   G .   ? 0.2678 0.2109 0.2016 0.0077  -0.0072 0.0108  252 HOH   B O   
7036 O  O   . HOH   G .   ? 0.2204 0.3717 0.3365 -0.0394 -0.0466 -0.0713 253 HOH   B O   
7037 O  O   . HOH   G .   ? 0.2061 0.4333 0.5029 -0.0332 -0.0245 -0.1364 254 HOH   B O   
7038 O  O   . HOH   G .   ? 0.1531 0.1500 0.2454 -0.0090 0.0078  -0.0117 255 HOH   B O   
7039 O  O   . HOH   G .   ? 0.3568 0.2440 0.3281 -0.0176 0.0425  -0.0693 256 HOH   B O   
7040 O  O   . HOH   G .   ? 0.2225 0.1880 0.2177 -0.0251 -0.0294 0.0132  257 HOH   B O   
7041 O  O   . HOH   G .   ? 0.4296 0.4209 0.6108 0.0899  0.0316  -0.0333 258 HOH   B O   
7042 O  O   . HOH   G .   ? 0.1792 0.2637 0.2761 0.0396  0.0329  0.0857  259 HOH   B O   
7043 O  O   . HOH   G .   ? 0.3239 0.4028 0.2487 0.0431  0.0815  -0.0017 260 HOH   B O   
7044 O  O   . HOH   G .   ? 0.4119 0.2746 0.4871 -0.0589 0.0400  -0.0314 261 HOH   B O   
7045 O  O   . HOH   G .   ? 0.1346 0.1703 0.2147 -0.0105 0.0095  0.0215  262 HOH   B O   
7046 O  O   . HOH   G .   ? 0.1571 0.1664 0.2906 -0.0199 -0.0119 0.0049  263 HOH   B O   
7047 O  O   . HOH   G .   ? 0.2779 0.4526 0.3329 -0.0905 -0.0478 -0.0828 264 HOH   B O   
7048 O  O   . HOH   G .   ? 0.2354 0.5286 0.5209 0.1308  -0.0203 0.0123  265 HOH   B O   
7049 O  O   . HOH   G .   ? 0.5197 0.5911 0.2772 0.0819  -0.1035 0.0699  266 HOH   B O   
7050 O  O   . HOH   G .   ? 0.2427 0.1925 0.3010 -0.0469 0.0216  -0.0055 267 HOH   B O   
7051 O  O   . HOH   G .   ? 0.2907 0.4971 0.3680 -0.0233 -0.0879 0.1250  268 HOH   B O   
7052 O  O   . HOH   G .   ? 0.2034 0.1551 0.2373 -0.0281 -0.0218 0.0033  269 HOH   B O   
7053 O  O   . HOH   G .   ? 0.2413 0.2142 0.2075 0.0102  -0.0084 -0.0054 270 HOH   B O   
7054 O  O   . HOH   G .   ? 0.1811 0.1804 0.1780 -0.0392 -0.0401 0.0156  271 HOH   B O   
7055 O  O   . HOH   G .   ? 0.2570 0.2641 0.2602 -0.0383 -0.0721 0.0276  272 HOH   B O   
7056 O  O   . HOH   G .   ? 0.2414 0.2740 0.2342 -0.0410 -0.0610 -0.0480 273 HOH   B O   
7057 O  O   . HOH   G .   ? 0.1956 0.2010 0.3765 0.0018  -0.0185 -0.0404 274 HOH   B O   
7058 O  O   . HOH   G .   ? 0.2597 0.3910 0.2445 0.1411  -0.0700 -0.0589 275 HOH   B O   
7059 O  O   . HOH   G .   ? 0.3423 0.3407 0.4550 0.1182  -0.0692 -0.1074 276 HOH   B O   
7060 O  O   . HOH   G .   ? 0.2336 0.3487 0.3321 -0.0456 0.0460  -0.1285 277 HOH   B O   
7061 O  O   . HOH   G .   ? 0.4132 0.5495 0.4631 -0.0096 -0.1533 -0.0028 278 HOH   B O   
7062 O  O   . HOH   G .   ? 0.2602 0.3987 0.3743 0.0268  0.1166  0.0063  279 HOH   B O   
7063 O  O   . HOH   G .   ? 0.2988 0.2047 0.4591 0.0191  0.0389  0.0531  280 HOH   B O   
7064 O  O   . HOH   G .   ? 0.2986 0.4570 0.5256 -0.0949 -0.1257 0.1013  281 HOH   B O   
7065 O  O   . HOH   G .   ? 0.1780 0.1414 0.4072 -0.0065 -0.0167 -0.0249 282 HOH   B O   
7066 O  O   . HOH   G .   ? 0.1671 0.1489 0.1991 0.0062  0.0093  0.0031  283 HOH   B O   
7067 O  O   . HOH   G .   ? 0.1581 0.1576 0.3282 -0.0114 0.0103  -0.0060 284 HOH   B O   
7068 O  O   . HOH   G .   ? 0.3670 0.2275 0.4581 -0.1024 -0.2088 0.0920  285 HOH   B O   
7069 O  O   . HOH   G .   ? 0.5732 0.4952 0.4551 0.2314  -0.0135 0.0612  286 HOH   B O   
7070 O  O   . HOH   G .   ? 0.3920 0.2605 0.2124 0.0572  -0.0862 -0.0143 287 HOH   B O   
7071 O  O   . HOH   G .   ? 0.3811 0.3314 0.4773 -0.0305 -0.1067 -0.0869 288 HOH   B O   
7072 O  O   . HOH   G .   ? 0.3048 0.3296 0.3024 -0.0221 0.0243  -0.1532 289 HOH   B O   
7073 O  O   . HOH   G .   ? 0.1584 0.2065 0.1749 -0.0120 -0.0154 0.0085  290 HOH   B O   
7074 O  O   . HOH   G .   ? 0.2538 0.2621 0.2942 0.0095  -0.0751 0.0386  291 HOH   B O   
7075 O  O   . HOH   G .   ? 0.1805 0.1924 0.3440 0.0255  0.0101  0.0052  292 HOH   B O   
7076 O  O   . HOH   G .   ? 0.4002 0.4297 0.4321 -0.1016 0.1444  -0.1090 293 HOH   B O   
7077 O  O   . HOH   G .   ? 0.1631 0.1528 0.2985 0.0072  0.0021  -0.0072 294 HOH   B O   
7078 O  O   . HOH   G .   ? 0.2445 0.5594 0.2801 0.0694  -0.0296 -0.0733 295 HOH   B O   
7079 O  O   . HOH   G .   ? 0.3594 0.4062 0.4257 -0.1595 0.1261  -0.0485 296 HOH   B O   
7080 O  O   . HOH   G .   ? 0.1746 0.3334 0.4144 0.0392  -0.0153 -0.1377 297 HOH   B O   
7081 O  O   . HOH   G .   ? 0.3065 0.6016 0.7306 0.1050  -0.0462 -0.0754 298 HOH   B O   
7082 O  O   . HOH   G .   ? 0.7305 0.6388 0.3356 0.0253  0.0034  0.1321  299 HOH   B O   
7083 O  O   . HOH   G .   ? 0.4115 0.3894 0.2469 0.0959  -0.0589 0.0914  300 HOH   B O   
7084 O  O   . HOH   G .   ? 0.1706 0.1551 0.2529 0.0144  0.0055  0.0178  301 HOH   B O   
7085 O  O   . HOH   G .   ? 0.1990 0.1549 0.3489 0.0286  -0.0842 0.0001  302 HOH   B O   
7086 O  O   . HOH   G .   ? 0.2231 0.3587 0.5777 0.0910  -0.0489 -0.1570 303 HOH   B O   
7087 O  O   . HOH   G .   ? 0.5152 0.4715 0.6084 0.0726  0.0030  -0.0057 304 HOH   B O   
7088 O  O   . HOH   G .   ? 0.2147 0.1716 0.2715 -0.0235 -0.0231 -0.0125 305 HOH   B O   
7089 O  O   . HOH   G .   ? 0.2445 0.1491 0.2683 -0.0159 -0.0245 0.0269  306 HOH   B O   
7090 O  O   . HOH   G .   ? 0.2865 0.2918 0.3472 -0.0228 0.0952  -0.0710 307 HOH   B O   
7091 O  O   . HOH   G .   ? 0.1667 0.1949 0.2854 -0.0307 -0.0060 0.0064  308 HOH   B O   
7092 O  O   . HOH   G .   ? 0.3136 0.1963 0.3573 0.0686  0.0989  0.0387  309 HOH   B O   
7093 O  O   . HOH   G .   ? 0.3149 0.2929 0.5454 -0.0312 -0.0896 0.1240  310 HOH   B O   
7094 O  O   . HOH   G .   ? 0.4550 0.4963 0.2455 0.0356  0.1095  0.0874  311 HOH   B O   
7095 O  O   . HOH   G .   ? 0.2214 0.1905 0.1754 -0.0081 0.0191  0.0136  312 HOH   B O   
7096 O  O   . HOH   G .   ? 0.3892 0.1950 0.3105 0.1098  0.1091  0.0236  313 HOH   B O   
7097 O  O   . HOH   G .   ? 0.4103 0.5148 0.7197 0.0118  -0.0335 0.0103  314 HOH   B O   
7098 O  O   . HOH   G .   ? 0.4869 0.2847 0.2671 -0.1703 0.0759  -0.0222 315 HOH   B O   
7099 O  O   . HOH   G .   ? 0.2095 0.3269 0.3078 0.0692  -0.0118 -0.0833 316 HOH   B O   
7100 O  O   . HOH   G .   ? 0.4754 0.3772 0.4863 -0.0674 0.0442  0.1230  317 HOH   B O   
7101 O  O   . HOH   G .   ? 0.1650 0.2662 0.2250 -0.0090 -0.0259 0.0606  318 HOH   B O   
7102 O  O   . HOH   G .   ? 0.2088 0.3056 0.5019 -0.0043 -0.0714 -0.0226 319 HOH   B O   
7103 O  O   . HOH   G .   ? 0.1593 0.1608 0.2807 -0.0095 -0.0081 -0.0147 320 HOH   B O   
7104 O  O   . HOH   G .   ? 0.5174 0.3551 0.2664 -0.0033 -0.0370 -0.0422 321 HOH   B O   
7105 O  O   . HOH   G .   ? 0.6128 0.3803 0.3885 0.2588  0.1534  0.0865  322 HOH   B O   
7106 O  O   . HOH   G .   ? 0.5449 0.2700 0.3574 0.0933  0.0245  0.0862  323 HOH   B O   
7107 O  O   . HOH   G .   ? 0.6960 0.4438 0.5573 0.1890  0.1571  0.0810  324 HOH   B O   
7108 O  O   . HOH   G .   ? 0.2199 0.4669 0.5041 -0.0643 -0.0022 -0.0923 325 HOH   B O   
7109 O  O   . HOH   G .   ? 0.3078 0.6734 0.3569 0.1557  -0.0204 0.0807  326 HOH   B O   
7110 O  O   . HOH   G .   ? 0.5903 0.3610 0.4953 -0.0054 0.1619  -0.1565 327 HOH   B O   
7111 O  O   . HOH   G .   ? 0.2822 0.2239 0.2634 0.0131  -0.0406 0.0272  328 HOH   B O   
7112 O  O   . HOH   G .   ? 0.1891 0.1995 0.3032 0.0325  0.0452  0.0248  329 HOH   B O   
7113 O  O   . HOH   G .   ? 0.6387 0.3766 0.3902 0.0450  0.1368  0.1497  330 HOH   B O   
7114 O  O   . HOH   G .   ? 0.2913 0.1934 0.4584 -0.0123 -0.0059 0.0334  331 HOH   B O   
7115 O  O   . HOH   G .   ? 0.5114 0.4252 0.2784 0.1652  -0.1112 -0.0303 332 HOH   B O   
7116 O  O   . HOH   G .   ? 0.2311 0.2415 0.5603 -0.0518 0.0071  0.1421  333 HOH   B O   
7117 O  O   . HOH   G .   ? 0.4383 0.3388 0.5953 0.1482  0.2360  0.2006  334 HOH   B O   
7118 O  O   . HOH   G .   ? 0.3617 0.4669 0.8251 -0.0313 -0.1080 0.2410  335 HOH   B O   
7119 O  O   . HOH   G .   ? 0.2820 0.3166 0.5270 -0.0638 -0.1692 0.1272  336 HOH   B O   
7120 O  O   . HOH   G .   ? 0.6360 0.4022 0.5733 -0.0958 -0.1089 -0.1328 337 HOH   B O   
7121 O  O   . HOH   G .   ? 0.5661 0.5177 0.6426 0.1234  -0.0701 0.2400  338 HOH   B O   
7122 O  O   . HOH   G .   ? 0.1732 0.1588 0.2447 0.0094  -0.0140 0.0180  339 HOH   B O   
7123 O  O   . HOH   G .   ? 0.5283 0.5553 0.6088 -0.1077 -0.0557 0.1697  340 HOH   B O   
7124 O  O   . HOH   G .   ? 0.8640 0.2563 0.3687 0.0804  -0.1140 -0.0580 341 HOH   B O   
7125 O  O   . HOH   G .   ? 0.4223 0.6918 0.3819 -0.0288 -0.0829 0.1310  342 HOH   B O   
7126 O  O   . HOH   G .   ? 0.5268 0.3236 0.3294 0.0478  -0.0902 -0.0740 343 HOH   B O   
7127 O  O   . HOH   G .   ? 0.4875 0.6170 0.3794 -0.0059 -0.1108 0.0525  344 HOH   B O   
7128 O  O   . HOH   G .   ? 0.3890 0.5746 0.3979 -0.0645 -0.0729 -0.0698 345 HOH   B O   
7129 O  O   . HOH   G .   ? 0.2610 0.1804 0.4022 0.0291  -0.0893 -0.0350 346 HOH   B O   
7130 O  O   . HOH   G .   ? 0.2310 0.1947 0.2975 -0.0022 0.0717  -0.0055 347 HOH   B O   
7131 O  O   . HOH   G .   ? 0.4520 0.5848 0.6073 0.0346  -0.1120 -0.0896 348 HOH   B O   
7132 O  O   . HOH   G .   ? 0.2430 0.6261 0.2934 0.1599  -0.0573 -0.1454 349 HOH   B O   
7133 O  O   . HOH   G .   ? 0.5064 0.5799 0.5917 -0.1519 0.1289  0.0975  350 HOH   B O   
7134 O  O   . HOH   G .   ? 0.2739 0.2266 0.5280 -0.0374 -0.0598 -0.0477 351 HOH   B O   
7135 O  O   . HOH   G .   ? 0.3527 0.4684 0.5197 -0.1867 0.0369  0.0038  352 HOH   B O   
7136 O  O   . HOH   G .   ? 0.3534 0.2325 0.3529 -0.0557 0.0060  -0.0758 353 HOH   B O   
7137 O  O   . HOH   G .   ? 0.4089 0.6100 0.6245 0.0353  0.0981  -0.0244 354 HOH   B O   
7138 O  O   . HOH   G .   ? 0.2217 0.4079 0.4842 0.0084  0.0458  0.0016  355 HOH   B O   
7139 O  O   . HOH   G .   ? 0.4604 0.2506 0.5843 -0.0604 0.1954  -0.0032 356 HOH   B O   
7140 O  O   . HOH   G .   ? 0.4905 0.5671 0.5126 0.2128  -0.1217 0.1171  357 HOH   B O   
7141 O  O   . HOH   G .   ? 0.3659 0.2751 0.4331 -0.0787 0.0006  -0.0671 358 HOH   B O   
7142 O  O   . HOH   G .   ? 0.5168 0.3126 0.4832 -0.0013 0.1508  -0.0631 359 HOH   B O   
7143 O  O   . HOH   G .   ? 0.4731 0.4652 0.5520 0.0159  -0.0437 0.0797  360 HOH   B O   
7144 O  O   . HOH   G .   ? 0.4303 0.3887 0.4979 0.0213  -0.1571 -0.0561 361 HOH   B O   
7145 O  O   . HOH   G .   ? 0.5626 0.4090 0.6011 0.0512  0.1114  0.0825  362 HOH   B O   
7146 O  O   . HOH   G .   ? 0.2121 0.3494 0.6934 -0.0615 -0.0482 -0.0768 363 HOH   B O   
7147 O  O   . HOH   G .   ? 0.3812 0.6218 0.3255 0.1950  -0.0427 -0.0087 364 HOH   B O   
7148 O  O   . HOH   G .   ? 0.6586 0.2500 0.3006 -0.0062 0.0490  0.0600  365 HOH   B O   
7149 O  O   . HOH   G .   ? 0.5307 0.5977 0.4429 -0.0763 -0.0572 -0.1256 366 HOH   B O   
7150 O  O   . HOH   G .   ? 0.5724 0.3267 0.5856 -0.1485 0.0468  0.0072  367 HOH   B O   
7151 O  O   . HOH   G .   ? 0.6061 0.6094 0.3566 0.1883  -0.1601 0.0619  368 HOH   B O   
7152 O  O   . HOH   G .   ? 0.6399 0.4832 0.4781 0.1609  0.1202  0.0762  369 HOH   B O   
7153 O  O   . HOH   G .   ? 0.4792 0.3245 0.4888 0.0697  -0.1718 0.0075  370 HOH   B O   
7154 O  O   . HOH   G .   ? 0.3983 0.5872 0.5806 0.2509  0.0449  0.1216  371 HOH   B O   
7155 O  O   . HOH   G .   ? 0.7747 0.8350 0.5783 0.3058  -0.1441 0.1393  372 HOH   B O   
7156 O  O   . HOH   G .   ? 0.6405 0.4091 0.3387 -0.0863 -0.1148 -0.0943 373 HOH   B O   
7157 O  O   . HOH   G .   ? 0.3725 0.3756 0.3924 0.0739  -0.1113 -0.0559 374 HOH   B O   
7158 O  O   . HOH   G .   ? 0.4351 0.4650 0.5120 -0.0539 -0.0638 0.0138  375 HOH   B O   
7159 O  O   . HOH   G .   ? 0.4958 0.7234 0.3738 -0.1303 0.0342  -0.1679 376 HOH   B O   
7160 O  O   . HOH   G .   ? 0.4670 0.8010 0.6029 0.1530  0.0612  0.2935  377 HOH   B O   
7161 O  O   . HOH   G .   ? 0.2361 0.3737 0.4787 0.0120  -0.0559 -0.0970 378 HOH   B O   
7162 O  O   . HOH   G .   ? 0.2876 0.4791 0.2251 0.0554  -0.0078 -0.0000 379 HOH   B O   
7163 O  O   . HOH   G .   ? 0.3799 0.5941 0.6395 0.1398  -0.0632 0.0046  380 HOH   B O   
7164 O  O   . HOH   G .   ? 0.5821 0.6640 0.6674 -0.0156 0.2554  0.1295  381 HOH   B O   
7165 O  O   . HOH   G .   ? 0.6530 0.3558 0.4916 -0.0676 -0.0478 -0.0014 382 HOH   B O   
7166 O  O   . HOH   G .   ? 0.4413 0.8432 0.5579 0.1191  0.2063  0.0653  383 HOH   B O   
7167 O  O   . HOH   G .   ? 0.2719 0.2679 0.3244 0.0088  0.0309  0.0398  384 HOH   B O   
7168 O  O   . HOH   G .   ? 0.2266 0.4396 0.4264 -0.0517 -0.0977 -0.0618 385 HOH   B O   
7169 O  O   . HOH   G .   ? 0.4733 0.5467 0.4315 -0.0002 -0.0268 -0.0579 386 HOH   B O   
7170 O  O   . HOH   G .   ? 0.6993 0.4265 0.4500 0.0824  0.1262  -0.0858 387 HOH   B O   
7171 O  O   . HOH   G .   ? 0.7593 0.5850 0.4178 0.1806  -0.0458 0.0110  388 HOH   B O   
7172 O  O   . HOH   G .   ? 0.6335 0.3959 0.5502 -0.0476 0.0813  -0.0111 389 HOH   B O   
7173 O  O   . HOH   G .   ? 0.4700 0.4331 0.3111 0.0299  0.0801  0.0180  390 HOH   B O   
7174 O  O   . HOH   G .   ? 0.4092 0.2473 0.3093 0.0867  -0.0272 0.0119  391 HOH   B O   
7175 O  O   . HOH   G .   ? 0.5028 0.4254 0.4351 0.0295  0.0165  0.0536  392 HOH   B O   
7176 O  O   . HOH   G .   ? 0.4486 0.2318 0.4673 -0.0800 -0.0168 0.0480  393 HOH   B O   
7177 O  O   . HOH   G .   ? 0.2361 0.5273 0.6535 -0.1450 -0.0521 -0.0469 394 HOH   B O   
7178 O  O   . HOH   G .   ? 0.4989 0.5755 0.4003 0.1621  -0.0206 -0.1087 395 HOH   B O   
7179 O  O   . HOH   G .   ? 0.3352 0.3888 0.3897 0.0057  0.0228  -0.1028 396 HOH   B O   
7180 O  O   . HOH   G .   ? 0.4124 0.4654 0.4673 0.0605  0.0814  0.0608  397 HOH   B O   
7181 O  O   . HOH   G .   ? 0.2060 0.2805 0.5315 -0.0404 -0.0576 -0.0098 398 HOH   B O   
7182 O  O   . HOH   G .   ? 0.5368 0.4620 0.5853 -0.0086 -0.1141 0.2327  399 HOH   B O   
7183 O  O   . HOH   G .   ? 0.4786 0.4037 0.3075 -0.1938 -0.0510 0.0878  400 HOH   B O   
7184 O  O   . HOH   G .   ? 0.6567 0.6327 0.3986 0.1097  -0.1174 0.0065  401 HOH   B O   
# 
