data_7HF4
# 
_entry.id   7HF4 
# 
_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   7HF4         pdb_00007hf4 10.2210/pdb7hf4/pdb 
WWPDB D_1001407394 ?            ?                   
# 
_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                        7HF4 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                  18178.766 2   '3.4.19.121, 3.4.22.-' 
? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'trifluoroacetic acid'                                                      114.023   1   ?                      
? ? ?                                                                                    
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                        78.133    2   ?                      
? ? ?                                                                                    
4 non-polymer syn '4-{(2S)-3-hydroxy-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propyl}phenol' 284.313   1   ?                      
? ? ?                                                                                    
5 non-polymer syn 'CHLORIDE ION'                                                              35.453    1   ?                      
? ? ?                                                                                    
6 water       nat water                                                                       18.015    425 ?                      
? ? ?                                                                                    
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                                      TFA   
3 'DIMETHYL SULFOXIDE'                                                        DMS   
4 '4-{(2S)-3-hydroxy-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propyl}phenol' A1BAO 
5 'CHLORIDE ION'                                                              CL    
6 water                                                                       HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BAO non-polymer         . '4-{(2S)-3-hydroxy-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propyl}phenol' ? 'C15 H16 N4 O2'  284.313 
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 
TFA   non-polymer         . 'trifluoroacetic acid'                                                      ? 'C2 H F3 O2'     114.023 
THR   'L-peptide linking' y THREONINE                                                                   ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                                    ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                      ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TFA   1   201  201  TFA   TFA A . 
D 3 DMS   1   202  301  DMS   DMS A . 
E 3 DMS   1   203  401  DMS   DMS A . 
F 4 A1BAO 1   204  201  A1BAO LA1 A . 
G 5 CL    1   205  1    CL    CL  A . 
H 6 HOH   1   1301 1301 HOH   HOH A . 
H 6 HOH   2   1302 1289 HOH   HOH A . 
H 6 HOH   3   1303 292  HOH   HOH A . 
H 6 HOH   4   1304 105  HOH   HOH A . 
H 6 HOH   5   1305 196  HOH   HOH A . 
H 6 HOH   6   1306 1    HOH   HOH A . 
H 6 HOH   7   1307 209  HOH   HOH A . 
H 6 HOH   8   1308 964  HOH   HOH A . 
H 6 HOH   9   1309 5    HOH   HOH A . 
H 6 HOH   10  1310 625  HOH   HOH A . 
H 6 HOH   11  1311 192  HOH   HOH A . 
H 6 HOH   12  1312 109  HOH   HOH A . 
H 6 HOH   13  1313 136  HOH   HOH A . 
H 6 HOH   14  1314 124  HOH   HOH A . 
H 6 HOH   15  1315 1283 HOH   HOH A . 
H 6 HOH   16  1316 76   HOH   HOH A . 
H 6 HOH   17  1317 661  HOH   HOH A . 
H 6 HOH   18  1318 155  HOH   HOH A . 
H 6 HOH   19  1319 236  HOH   HOH A . 
H 6 HOH   20  1320 229  HOH   HOH A . 
H 6 HOH   21  1321 393  HOH   HOH A . 
H 6 HOH   22  1322 493  HOH   HOH A . 
H 6 HOH   23  1323 151  HOH   HOH A . 
H 6 HOH   24  1324 33   HOH   HOH A . 
H 6 HOH   25  1325 9    HOH   HOH A . 
H 6 HOH   26  1326 1295 HOH   HOH A . 
H 6 HOH   27  1327 15   HOH   HOH A . 
H 6 HOH   28  1328 281  HOH   HOH A . 
H 6 HOH   29  1329 247  HOH   HOH A . 
H 6 HOH   30  1330 140  HOH   HOH A . 
H 6 HOH   31  1331 630  HOH   HOH A . 
H 6 HOH   32  1332 469  HOH   HOH A . 
H 6 HOH   33  1333 1290 HOH   HOH A . 
H 6 HOH   34  1334 164  HOH   HOH A . 
H 6 HOH   35  1335 1300 HOH   HOH A . 
H 6 HOH   36  1336 26   HOH   HOH A . 
H 6 HOH   37  1337 165  HOH   HOH A . 
H 6 HOH   38  1338 241  HOH   HOH A . 
H 6 HOH   39  1339 153  HOH   HOH A . 
H 6 HOH   40  1340 92   HOH   HOH A . 
H 6 HOH   41  1341 102  HOH   HOH A . 
H 6 HOH   42  1342 320  HOH   HOH A . 
H 6 HOH   43  1343 337  HOH   HOH A . 
H 6 HOH   44  1344 21   HOH   HOH A . 
H 6 HOH   45  1345 16   HOH   HOH A . 
H 6 HOH   46  1346 42   HOH   HOH A . 
H 6 HOH   47  1347 225  HOH   HOH A . 
H 6 HOH   48  1348 139  HOH   HOH A . 
H 6 HOH   49  1349 39   HOH   HOH A . 
H 6 HOH   50  1350 169  HOH   HOH A . 
H 6 HOH   51  1351 18   HOH   HOH A . 
H 6 HOH   52  1352 93   HOH   HOH A . 
H 6 HOH   53  1353 354  HOH   HOH A . 
H 6 HOH   54  1354 17   HOH   HOH A . 
H 6 HOH   55  1355 36   HOH   HOH A . 
H 6 HOH   56  1356 66   HOH   HOH A . 
H 6 HOH   57  1357 8    HOH   HOH A . 
H 6 HOH   58  1358 2    HOH   HOH A . 
H 6 HOH   59  1359 5    HOH   HOH A . 
H 6 HOH   60  1360 461  HOH   HOH A . 
H 6 HOH   61  1361 56   HOH   HOH A . 
H 6 HOH   62  1362 396  HOH   HOH A . 
H 6 HOH   63  1363 409  HOH   HOH A . 
H 6 HOH   64  1364 45   HOH   HOH A . 
H 6 HOH   65  1365 162  HOH   HOH A . 
H 6 HOH   66  1366 19   HOH   HOH A . 
H 6 HOH   67  1367 96   HOH   HOH A . 
H 6 HOH   68  1368 296  HOH   HOH A . 
H 6 HOH   69  1369 218  HOH   HOH A . 
H 6 HOH   70  1370 159  HOH   HOH A . 
H 6 HOH   71  1371 138  HOH   HOH A . 
H 6 HOH   72  1372 49   HOH   HOH A . 
H 6 HOH   73  1373 939  HOH   HOH A . 
H 6 HOH   74  1374 46   HOH   HOH A . 
H 6 HOH   75  1375 115  HOH   HOH A . 
H 6 HOH   76  1376 195  HOH   HOH A . 
H 6 HOH   77  1377 140  HOH   HOH A . 
H 6 HOH   78  1378 86   HOH   HOH A . 
H 6 HOH   79  1379 81   HOH   HOH A . 
H 6 HOH   80  1380 57   HOH   HOH A . 
H 6 HOH   81  1381 366  HOH   HOH A . 
H 6 HOH   82  1382 35   HOH   HOH A . 
H 6 HOH   83  1383 134  HOH   HOH A . 
H 6 HOH   84  1384 85   HOH   HOH A . 
H 6 HOH   85  1385 148  HOH   HOH A . 
H 6 HOH   86  1386 186  HOH   HOH A . 
H 6 HOH   87  1387 2    HOH   HOH A . 
H 6 HOH   88  1388 662  HOH   HOH A . 
H 6 HOH   89  1389 10   HOH   HOH A . 
H 6 HOH   90  1390 1275 HOH   HOH A . 
H 6 HOH   91  1391 405  HOH   HOH A . 
H 6 HOH   92  1392 154  HOH   HOH A . 
H 6 HOH   93  1393 27   HOH   HOH A . 
H 6 HOH   94  1394 116  HOH   HOH A . 
H 6 HOH   95  1395 17   HOH   HOH A . 
H 6 HOH   96  1396 1315 HOH   HOH A . 
H 6 HOH   97  1397 12   HOH   HOH A . 
H 6 HOH   98  1398 58   HOH   HOH A . 
H 6 HOH   99  1399 121  HOH   HOH A . 
H 6 HOH   100 1400 74   HOH   HOH A . 
H 6 HOH   101 1401 1310 HOH   HOH A . 
H 6 HOH   102 1402 67   HOH   HOH A . 
H 6 HOH   103 1403 1308 HOH   HOH A . 
H 6 HOH   104 1404 4    HOH   HOH A . 
H 6 HOH   105 1405 34   HOH   HOH A . 
H 6 HOH   106 1406 199  HOH   HOH A . 
H 6 HOH   107 1407 83   HOH   HOH A . 
H 6 HOH   108 1408 351  HOH   HOH A . 
H 6 HOH   109 1409 25   HOH   HOH A . 
H 6 HOH   110 1410 68   HOH   HOH A . 
H 6 HOH   111 1411 3    HOH   HOH A . 
H 6 HOH   112 1412 156  HOH   HOH A . 
H 6 HOH   113 1413 1068 HOH   HOH A . 
H 6 HOH   114 1414 123  HOH   HOH A . 
H 6 HOH   115 1415 78   HOH   HOH A . 
H 6 HOH   116 1416 6    HOH   HOH A . 
H 6 HOH   117 1417 303  HOH   HOH A . 
H 6 HOH   118 1418 212  HOH   HOH A . 
H 6 HOH   119 1419 125  HOH   HOH A . 
H 6 HOH   120 1420 53   HOH   HOH A . 
H 6 HOH   121 1421 122  HOH   HOH A . 
H 6 HOH   122 1422 24   HOH   HOH A . 
H 6 HOH   123 1423 1313 HOH   HOH A . 
H 6 HOH   124 1424 95   HOH   HOH A . 
H 6 HOH   125 1425 51   HOH   HOH A . 
H 6 HOH   126 1426 8    HOH   HOH A . 
H 6 HOH   127 1427 582  HOH   HOH A . 
H 6 HOH   128 1428 381  HOH   HOH A . 
H 6 HOH   129 1429 397  HOH   HOH A . 
H 6 HOH   130 1430 278  HOH   HOH A . 
H 6 HOH   131 1431 1222 HOH   HOH A . 
H 6 HOH   132 1432 132  HOH   HOH A . 
H 6 HOH   133 1433 333  HOH   HOH A . 
H 6 HOH   134 1434 7    HOH   HOH A . 
H 6 HOH   135 1435 1309 HOH   HOH A . 
H 6 HOH   136 1436 70   HOH   HOH A . 
H 6 HOH   137 1437 1279 HOH   HOH A . 
H 6 HOH   138 1438 1238 HOH   HOH A . 
H 6 HOH   139 1439 71   HOH   HOH A . 
H 6 HOH   140 1440 1296 HOH   HOH A . 
H 6 HOH   141 1441 40   HOH   HOH A . 
H 6 HOH   142 1442 944  HOH   HOH A . 
H 6 HOH   143 1443 80   HOH   HOH A . 
H 6 HOH   144 1444 16   HOH   HOH A . 
H 6 HOH   145 1445 1094 HOH   HOH A . 
H 6 HOH   146 1446 188  HOH   HOH A . 
H 6 HOH   147 1447 1286 HOH   HOH A . 
H 6 HOH   148 1448 73   HOH   HOH A . 
H 6 HOH   149 1449 1134 HOH   HOH A . 
H 6 HOH   150 1450 1189 HOH   HOH A . 
H 6 HOH   151 1451 94   HOH   HOH A . 
H 6 HOH   152 1452 952  HOH   HOH A . 
H 6 HOH   153 1453 79   HOH   HOH A . 
H 6 HOH   154 1454 576  HOH   HOH A . 
H 6 HOH   155 1455 104  HOH   HOH A . 
H 6 HOH   156 1456 97   HOH   HOH A . 
H 6 HOH   157 1457 11   HOH   HOH A . 
H 6 HOH   158 1458 4    HOH   HOH A . 
H 6 HOH   159 1459 14   HOH   HOH A . 
H 6 HOH   160 1460 330  HOH   HOH A . 
H 6 HOH   161 1461 1119 HOH   HOH A . 
H 6 HOH   162 1462 7    HOH   HOH A . 
H 6 HOH   163 1463 509  HOH   HOH A . 
H 6 HOH   164 1464 726  HOH   HOH A . 
H 6 HOH   165 1465 107  HOH   HOH A . 
H 6 HOH   166 1466 163  HOH   HOH A . 
H 6 HOH   167 1467 3    HOH   HOH A . 
H 6 HOH   168 1468 756  HOH   HOH A . 
H 6 HOH   169 1469 408  HOH   HOH A . 
H 6 HOH   170 1470 556  HOH   HOH A . 
H 6 HOH   171 1471 126  HOH   HOH A . 
H 6 HOH   172 1472 319  HOH   HOH A . 
H 6 HOH   173 1473 361  HOH   HOH A . 
H 6 HOH   174 1474 801  HOH   HOH A . 
H 6 HOH   175 1475 280  HOH   HOH A . 
H 6 HOH   176 1476 1276 HOH   HOH A . 
H 6 HOH   177 1477 63   HOH   HOH A . 
H 6 HOH   178 1478 342  HOH   HOH A . 
H 6 HOH   179 1479 370  HOH   HOH A . 
H 6 HOH   180 1480 250  HOH   HOH A . 
H 6 HOH   181 1481 1307 HOH   HOH A . 
H 6 HOH   182 1482 224  HOH   HOH A . 
H 6 HOH   183 1483 267  HOH   HOH A . 
H 6 HOH   184 1484 15   HOH   HOH A . 
H 6 HOH   185 1485 521  HOH   HOH A . 
H 6 HOH   186 1486 1306 HOH   HOH A . 
H 6 HOH   187 1487 326  HOH   HOH A . 
H 6 HOH   188 1488 1287 HOH   HOH A . 
H 6 HOH   189 1489 695  HOH   HOH A . 
H 6 HOH   190 1490 674  HOH   HOH A . 
H 6 HOH   191 1491 1299 HOH   HOH A . 
H 6 HOH   192 1492 919  HOH   HOH A . 
H 6 HOH   193 1493 135  HOH   HOH A . 
H 6 HOH   194 1494 711  HOH   HOH A . 
H 6 HOH   195 1495 202  HOH   HOH A . 
H 6 HOH   196 1496 318  HOH   HOH A . 
H 6 HOH   197 1497 309  HOH   HOH A . 
H 6 HOH   198 1498 356  HOH   HOH A . 
H 6 HOH   199 1499 1284 HOH   HOH A . 
H 6 HOH   200 1500 331  HOH   HOH A . 
H 6 HOH   201 1501 1314 HOH   HOH A . 
H 6 HOH   202 1502 315  HOH   HOH A . 
H 6 HOH   203 1503 263  HOH   HOH A . 
H 6 HOH   204 1504 941  HOH   HOH A . 
H 6 HOH   205 1505 152  HOH   HOH A . 
H 6 HOH   206 1506 805  HOH   HOH A . 
H 6 HOH   207 1507 208  HOH   HOH A . 
H 6 HOH   208 1508 1071 HOH   HOH A . 
H 6 HOH   209 1509 180  HOH   HOH A . 
H 6 HOH   210 1510 350  HOH   HOH A . 
H 6 HOH   211 1511 363  HOH   HOH A . 
H 6 HOH   212 1512 371  HOH   HOH A . 
H 6 HOH   213 1513 313  HOH   HOH A . 
H 6 HOH   214 1514 429  HOH   HOH A . 
H 6 HOH   215 1515 185  HOH   HOH A . 
H 6 HOH   216 1516 772  HOH   HOH A . 
H 6 HOH   217 1517 70   HOH   HOH A . 
H 6 HOH   218 1518 13   HOH   HOH A . 
H 6 HOH   219 1519 12   HOH   HOH A . 
H 6 HOH   220 1520 376  HOH   HOH A . 
H 6 HOH   221 1521 1074 HOH   HOH A . 
H 6 HOH   222 1522 1292 HOH   HOH A . 
H 6 HOH   223 1523 346  HOH   HOH A . 
H 6 HOH   224 1524 1078 HOH   HOH A . 
I 6 HOH   1   201  64   HOH   HOH B . 
I 6 HOH   2   202  240  HOH   HOH B . 
I 6 HOH   3   203  549  HOH   HOH B . 
I 6 HOH   4   204  531  HOH   HOH B . 
I 6 HOH   5   205  398  HOH   HOH B . 
I 6 HOH   6   206  358  HOH   HOH B . 
I 6 HOH   7   207  758  HOH   HOH B . 
I 6 HOH   8   208  444  HOH   HOH B . 
I 6 HOH   9   209  120  HOH   HOH B . 
I 6 HOH   10  210  1249 HOH   HOH B . 
I 6 HOH   11  211  654  HOH   HOH B . 
I 6 HOH   12  212  50   HOH   HOH B . 
I 6 HOH   13  213  364  HOH   HOH B . 
I 6 HOH   14  214  232  HOH   HOH B . 
I 6 HOH   15  215  332  HOH   HOH B . 
I 6 HOH   16  216  343  HOH   HOH B . 
I 6 HOH   17  217  205  HOH   HOH B . 
I 6 HOH   18  218  743  HOH   HOH B . 
I 6 HOH   19  219  452  HOH   HOH B . 
I 6 HOH   20  220  353  HOH   HOH B . 
I 6 HOH   21  221  264  HOH   HOH B . 
I 6 HOH   22  222  1278 HOH   HOH B . 
I 6 HOH   23  223  1140 HOH   HOH B . 
I 6 HOH   24  224  75   HOH   HOH B . 
I 6 HOH   25  225  172  HOH   HOH B . 
I 6 HOH   26  226  82   HOH   HOH B . 
I 6 HOH   27  227  131  HOH   HOH B . 
I 6 HOH   28  228  54   HOH   HOH B . 
I 6 HOH   29  229  282  HOH   HOH B . 
I 6 HOH   30  230  723  HOH   HOH B . 
I 6 HOH   31  231  60   HOH   HOH B . 
I 6 HOH   32  232  900  HOH   HOH B . 
I 6 HOH   33  233  127  HOH   HOH B . 
I 6 HOH   34  234  166  HOH   HOH B . 
I 6 HOH   35  235  276  HOH   HOH B . 
I 6 HOH   36  236  128  HOH   HOH B . 
I 6 HOH   37  237  69   HOH   HOH B . 
I 6 HOH   38  238  41   HOH   HOH B . 
I 6 HOH   39  239  325  HOH   HOH B . 
I 6 HOH   40  240  133  HOH   HOH B . 
I 6 HOH   41  241  110  HOH   HOH B . 
I 6 HOH   42  242  14   HOH   HOH B . 
I 6 HOH   43  243  300  HOH   HOH B . 
I 6 HOH   44  244  1    HOH   HOH B . 
I 6 HOH   45  245  181  HOH   HOH B . 
I 6 HOH   46  246  347  HOH   HOH B . 
I 6 HOH   47  247  30   HOH   HOH B . 
I 6 HOH   48  248  272  HOH   HOH B . 
I 6 HOH   49  249  72   HOH   HOH B . 
I 6 HOH   50  250  9    HOH   HOH B . 
I 6 HOH   51  251  129  HOH   HOH B . 
I 6 HOH   52  252  391  HOH   HOH B . 
I 6 HOH   53  253  144  HOH   HOH B . 
I 6 HOH   54  254  62   HOH   HOH B . 
I 6 HOH   55  255  52   HOH   HOH B . 
I 6 HOH   56  256  31   HOH   HOH B . 
I 6 HOH   57  257  150  HOH   HOH B . 
I 6 HOH   58  258  47   HOH   HOH B . 
I 6 HOH   59  259  231  HOH   HOH B . 
I 6 HOH   60  260  143  HOH   HOH B . 
I 6 HOH   61  261  10   HOH   HOH B . 
I 6 HOH   62  262  1312 HOH   HOH B . 
I 6 HOH   63  263  103  HOH   HOH B . 
I 6 HOH   64  264  59   HOH   HOH B . 
I 6 HOH   65  265  302  HOH   HOH B . 
I 6 HOH   66  266  11   HOH   HOH B . 
I 6 HOH   67  267  242  HOH   HOH B . 
I 6 HOH   68  268  117  HOH   HOH B . 
I 6 HOH   69  269  20   HOH   HOH B . 
I 6 HOH   70  270  243  HOH   HOH B . 
I 6 HOH   71  271  61   HOH   HOH B . 
I 6 HOH   72  272  84   HOH   HOH B . 
I 6 HOH   73  273  1106 HOH   HOH B . 
I 6 HOH   74  274  1277 HOH   HOH B . 
I 6 HOH   75  275  114  HOH   HOH B . 
I 6 HOH   76  276  271  HOH   HOH B . 
I 6 HOH   77  277  77   HOH   HOH B . 
I 6 HOH   78  278  175  HOH   HOH B . 
I 6 HOH   79  279  147  HOH   HOH B . 
I 6 HOH   80  280  287  HOH   HOH B . 
I 6 HOH   81  281  252  HOH   HOH B . 
I 6 HOH   82  282  43   HOH   HOH B . 
I 6 HOH   83  283  22   HOH   HOH B . 
I 6 HOH   84  284  235  HOH   HOH B . 
I 6 HOH   85  285  88   HOH   HOH B . 
I 6 HOH   86  286  137  HOH   HOH B . 
I 6 HOH   87  287  13   HOH   HOH B . 
I 6 HOH   88  288  216  HOH   HOH B . 
I 6 HOH   89  289  1305 HOH   HOH B . 
I 6 HOH   90  290  1285 HOH   HOH B . 
I 6 HOH   91  291  89   HOH   HOH B . 
I 6 HOH   92  292  1066 HOH   HOH B . 
I 6 HOH   93  293  160  HOH   HOH B . 
I 6 HOH   94  294  106  HOH   HOH B . 
I 6 HOH   95  295  311  HOH   HOH B . 
I 6 HOH   96  296  316  HOH   HOH B . 
I 6 HOH   97  297  220  HOH   HOH B . 
I 6 HOH   98  298  221  HOH   HOH B . 
I 6 HOH   99  299  416  HOH   HOH B . 
I 6 HOH   100 300  112  HOH   HOH B . 
I 6 HOH   101 301  38   HOH   HOH B . 
I 6 HOH   102 302  99   HOH   HOH B . 
I 6 HOH   103 303  32   HOH   HOH B . 
I 6 HOH   104 304  299  HOH   HOH B . 
I 6 HOH   105 305  215  HOH   HOH B . 
I 6 HOH   106 306  142  HOH   HOH B . 
I 6 HOH   107 307  297  HOH   HOH B . 
I 6 HOH   108 308  387  HOH   HOH B . 
I 6 HOH   109 309  101  HOH   HOH B . 
I 6 HOH   110 310  118  HOH   HOH B . 
I 6 HOH   111 311  23   HOH   HOH B . 
I 6 HOH   112 312  177  HOH   HOH B . 
I 6 HOH   113 313  37   HOH   HOH B . 
I 6 HOH   114 314  170  HOH   HOH B . 
I 6 HOH   115 315  635  HOH   HOH B . 
I 6 HOH   116 316  91   HOH   HOH B . 
I 6 HOH   117 317  48   HOH   HOH B . 
I 6 HOH   118 318  704  HOH   HOH B . 
I 6 HOH   119 319  141  HOH   HOH B . 
I 6 HOH   120 320  197  HOH   HOH B . 
I 6 HOH   121 321  1274 HOH   HOH B . 
I 6 HOH   122 322  28   HOH   HOH B . 
I 6 HOH   123 323  44   HOH   HOH B . 
I 6 HOH   124 324  100  HOH   HOH B . 
I 6 HOH   125 325  341  HOH   HOH B . 
I 6 HOH   126 326  29   HOH   HOH B . 
I 6 HOH   127 327  161  HOH   HOH B . 
I 6 HOH   128 328  98   HOH   HOH B . 
I 6 HOH   129 329  1294 HOH   HOH B . 
I 6 HOH   130 330  334  HOH   HOH B . 
I 6 HOH   131 331  55   HOH   HOH B . 
I 6 HOH   132 332  1291 HOH   HOH B . 
I 6 HOH   133 333  207  HOH   HOH B . 
I 6 HOH   134 334  1126 HOH   HOH B . 
I 6 HOH   135 335  445  HOH   HOH B . 
I 6 HOH   136 336  717  HOH   HOH B . 
I 6 HOH   137 337  182  HOH   HOH B . 
I 6 HOH   138 338  234  HOH   HOH B . 
I 6 HOH   139 339  65   HOH   HOH B . 
I 6 HOH   140 340  339  HOH   HOH B . 
I 6 HOH   141 341  619  HOH   HOH B . 
I 6 HOH   142 342  1293 HOH   HOH B . 
I 6 HOH   143 343  362  HOH   HOH B . 
I 6 HOH   144 344  960  HOH   HOH B . 
I 6 HOH   145 345  90   HOH   HOH B . 
I 6 HOH   146 346  463  HOH   HOH B . 
I 6 HOH   147 347  1304 HOH   HOH B . 
I 6 HOH   148 348  178  HOH   HOH B . 
I 6 HOH   149 349  1046 HOH   HOH B . 
I 6 HOH   150 350  191  HOH   HOH B . 
I 6 HOH   151 351  304  HOH   HOH B . 
I 6 HOH   152 352  623  HOH   HOH B . 
I 6 HOH   153 353  335  HOH   HOH B . 
I 6 HOH   154 354  1280 HOH   HOH B . 
I 6 HOH   155 355  87   HOH   HOH B . 
I 6 HOH   156 356  290  HOH   HOH B . 
I 6 HOH   157 357  203  HOH   HOH B . 
I 6 HOH   158 358  541  HOH   HOH B . 
I 6 HOH   159 359  1077 HOH   HOH B . 
I 6 HOH   160 360  389  HOH   HOH B . 
I 6 HOH   161 361  718  HOH   HOH B . 
I 6 HOH   162 362  479  HOH   HOH B . 
I 6 HOH   163 363  283  HOH   HOH B . 
I 6 HOH   164 364  1072 HOH   HOH B . 
I 6 HOH   165 365  898  HOH   HOH B . 
I 6 HOH   166 366  373  HOH   HOH B . 
I 6 HOH   167 367  1316 HOH   HOH B . 
I 6 HOH   168 368  291  HOH   HOH B . 
I 6 HOH   169 369  615  HOH   HOH B . 
I 6 HOH   170 370  340  HOH   HOH B . 
I 6 HOH   171 371  667  HOH   HOH B . 
I 6 HOH   172 372  190  HOH   HOH B . 
I 6 HOH   173 373  1303 HOH   HOH B . 
I 6 HOH   174 374  310  HOH   HOH B . 
I 6 HOH   175 375  1173 HOH   HOH B . 
I 6 HOH   176 376  431  HOH   HOH B . 
I 6 HOH   177 377  149  HOH   HOH B . 
I 6 HOH   178 378  183  HOH   HOH B . 
I 6 HOH   179 379  418  HOH   HOH B . 
I 6 HOH   180 380  1000 HOH   HOH B . 
I 6 HOH   181 381  1163 HOH   HOH B . 
I 6 HOH   182 382  1311 HOH   HOH B . 
I 6 HOH   183 383  176  HOH   HOH B . 
I 6 HOH   184 384  491  HOH   HOH B . 
I 6 HOH   185 385  424  HOH   HOH B . 
I 6 HOH   186 386  470  HOH   HOH B . 
I 6 HOH   187 387  981  HOH   HOH B . 
I 6 HOH   188 388  265  HOH   HOH B . 
I 6 HOH   189 389  248  HOH   HOH B . 
I 6 HOH   190 390  1298 HOH   HOH B . 
I 6 HOH   191 391  360  HOH   HOH B . 
I 6 HOH   192 392  184  HOH   HOH B . 
I 6 HOH   193 393  410  HOH   HOH B . 
I 6 HOH   194 394  355  HOH   HOH B . 
I 6 HOH   195 395  274  HOH   HOH B . 
I 6 HOH   196 396  314  HOH   HOH B . 
I 6 HOH   197 397  566  HOH   HOH B . 
I 6 HOH   198 398  157  HOH   HOH B . 
I 6 HOH   199 399  321  HOH   HOH B . 
I 6 HOH   200 400  792  HOH   HOH B . 
I 6 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           7HF4 
_cell.length_a           88.713 
_cell.length_b           88.713 
_cell.length_c           39.418 
_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                         7HF4 
_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          7HF4 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.44 
_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   2023-07-01 
_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                     7HF4 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.360 
_reflns.d_resolution_high            0.970 
_reflns.number_obs                   180570 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.600 
_reflns.pdbx_Rmerge_I_obs            0.046 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.500 
_reflns.B_iso_Wilson_estimate        11.230 
_reflns.pdbx_redundancy              6.100 
_reflns.pdbx_Rrim_I_all              0.050 
_reflns.pdbx_Rpim_I_all              0.020 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1106557 
_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 0.970 0.990  ? 26688 8393 ? 1.088 ? ? ? 3.200 ? 0.700  ? ? ? ? ? ? 93.600 1.297 0.687 0.544 
1 2 5.310 44.360 ? 8275  1195 ? 0.027 ? ? ? 6.900 ? 51.700 ? ? ? ? ? ? 99.800 0.029 0.011 0.999 
# 
_refine.entry_id                                 7HF4 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9700 
_refine.ls_d_res_low                             44.3600 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.5700 
_refine.ls_number_reflns_obs                     180487 
_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                          0.1432 
_refine.ls_R_factor_R_work                       0.1426 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1540 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8100 
_refine.ls_number_reflns_R_free                  8681 
_refine.ls_number_reflns_R_work                  171806 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               17.6956 
_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                            0.1100 
_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                                65.240 
_refine.B_iso_min                                8.100 
_refine.pdbx_overall_phase_error                 16.6500 
_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                       0.9700 
_refine_hist.d_res_low                        44.3600 
_refine_hist.pdbx_number_atoms_ligand         65 
_refine_hist.number_atoms_solvent             425 
_refine_hist.number_atoms_total               3032 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           20.55 
_refine_hist.pdbx_B_iso_mean_solvent          28.73 
_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 
0.9700 0.9800  30 92.0000  5326 . 0.4098 0.4195 . 255 0.0000 5581 . 'X-RAY DIFFRACTION' 
0.9800 0.9900  30 97.0000  5461 . 0.3622 0.3538 . 294 0.0000 5755 . 'X-RAY DIFFRACTION' 
0.9900 1.0000  30 99.0000  5690 . 0.3185 0.3195 . 270 0.0000 5960 . 'X-RAY DIFFRACTION' 
1.0000 1.0200  30 100.0000 5723 . 0.2688 0.2531 . 283 0.0000 6006 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 100.0000 5775 . 0.2303 0.2388 . 242 0.0000 6017 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5722 . 0.2079 0.2179 . 318 0.0000 6040 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 5651 . 0.1895 0.1991 . 338 0.0000 5989 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5714 . 0.1746 0.1866 . 285 0.0000 5999 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5733 . 0.1550 0.1798 . 286 0.0000 6019 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5720 . 0.1451 0.1679 . 284 0.0000 6004 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5766 . 0.1417 0.1589 . 279 0.0000 6045 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 5718 . 0.1365 0.1486 . 270 0.0000 5988 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 5725 . 0.1275 0.1476 . 307 0.0000 6032 . 'X-RAY DIFFRACTION' 
1.1700 1.2000  30 100.0000 5753 . 0.1258 0.1500 . 284 0.0000 6037 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 100.0000 5678 . 0.1168 0.1405 . 305 0.0000 5983 . 'X-RAY DIFFRACTION' 
1.2200 1.2500  30 100.0000 5753 . 0.1190 0.1332 . 280 0.0000 6033 . 'X-RAY DIFFRACTION' 
1.2500 1.2800  30 100.0000 5746 . 0.1194 0.1339 . 278 0.0000 6024 . 'X-RAY DIFFRACTION' 
1.2800 1.3200  30 100.0000 5721 . 0.1190 0.1349 . 313 0.0000 6034 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5730 . 0.1205 0.1400 . 300 0.0000 6030 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5754 . 0.1211 0.1500 . 279 0.0000 6033 . 'X-RAY DIFFRACTION' 
1.4000 1.4500  30 100.0000 5783 . 0.1216 0.1394 . 279 0.0000 6062 . 'X-RAY DIFFRACTION' 
1.4500 1.5100  30 100.0000 5743 . 0.1181 0.1188 . 279 0.0000 6022 . 'X-RAY DIFFRACTION' 
1.5100 1.5800  30 100.0000 5742 . 0.1161 0.1343 . 308 0.0000 6050 . 'X-RAY DIFFRACTION' 
1.5800 1.6600  30 100.0000 5738 . 0.1185 0.1309 . 295 0.0000 6033 . 'X-RAY DIFFRACTION' 
1.6600 1.7600  30 100.0000 5809 . 0.1263 0.1368 . 261 0.0000 6070 . 'X-RAY DIFFRACTION' 
1.7600 1.9000  30 100.0000 5755 . 0.1305 0.1406 . 311 0.0000 6066 . 'X-RAY DIFFRACTION' 
1.9000 2.0900  30 100.0000 5793 . 0.1360 0.1346 . 291 0.0000 6084 . 'X-RAY DIFFRACTION' 
2.0900 2.3900  30 100.0000 5771 . 0.1380 0.1353 . 322 0.0000 6093 . 'X-RAY DIFFRACTION' 
2.3900 3.0100  30 100.0000 5842 . 0.1459 0.1665 . 294 0.0000 6136 . 'X-RAY DIFFRACTION' 
3.0100 44.3600 30 100.0000 5971 . 0.1503 0.1642 . 291 0.0000 6262 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HF4 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0004066' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HF4 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HF4 A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HF4 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 7HF4 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HF4 MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HF4 SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HF4 MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H 
2 1 B,I           
# 
_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 HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HF4 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    1380 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    1388 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
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  ? ? 54.90   -133.03 
2 1 SER A 128 ? B 70.46   -10.98  
3 1 SER A 167 ? B -101.51 64.62   
4 1 PHE A 168 ? B -120.29 -50.96  
5 1 HIS B 86  ? ? 57.57   -128.17 
# 
_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 1522 ? 5.94 . 
2 1 O ? A HOH 1523 ? 5.98 . 
3 1 O ? A HOH 1524 ? 7.60 . 
4 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 
A1BAO N2   N  Y N 1   
A1BAO C3   C  N N 2   
A1BAO C6   C  Y N 3   
A1BAO C9   C  Y N 4   
A1BAO C12  C  Y N 5   
A1BAO C14  C  Y N 6   
A1BAO C1   C  N N 7   
A1BAO C10  C  Y N 8   
A1BAO C11  C  Y N 9   
A1BAO C13  C  Y N 10  
A1BAO C15  C  Y N 11  
A1BAO C2   C  N S 12  
A1BAO C4   C  Y N 13  
A1BAO C5   C  Y N 14  
A1BAO C7   C  Y N 15  
A1BAO C8   C  Y N 16  
A1BAO N1   N  N N 17  
A1BAO N3   N  Y N 18  
A1BAO N4   N  Y N 19  
A1BAO O1   O  N N 20  
A1BAO O2   O  N N 21  
A1BAO H6   H  N N 22  
A1BAO H5   H  N N 23  
A1BAO H8   H  N N 24  
A1BAO H11  H  N N 25  
A1BAO H14  H  N N 26  
A1BAO H4   H  N N 27  
A1BAO H3   H  N N 28  
A1BAO H13  H  N N 29  
A1BAO H15  H  N N 30  
A1BAO H1   H  N N 31  
A1BAO H7   H  N N 32  
A1BAO H10  H  N N 33  
A1BAO H12  H  N N 34  
A1BAO H16  H  N N 35  
A1BAO H2   H  N N 36  
A1BAO H9   H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CL    CL   CL N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
DMS   S    S  N N 126 
DMS   O    O  N N 127 
DMS   C1   C  N N 128 
DMS   C2   C  N N 129 
DMS   H11  H  N N 130 
DMS   H12  H  N N 131 
DMS   H13  H  N N 132 
DMS   H21  H  N N 133 
DMS   H22  H  N N 134 
DMS   H23  H  N N 135 
GLN   N    N  N N 136 
GLN   CA   C  N S 137 
GLN   C    C  N N 138 
GLN   O    O  N N 139 
GLN   CB   C  N N 140 
GLN   CG   C  N N 141 
GLN   CD   C  N N 142 
GLN   OE1  O  N N 143 
GLN   NE2  N  N N 144 
GLN   OXT  O  N N 145 
GLN   H    H  N N 146 
GLN   H2   H  N N 147 
GLN   HA   H  N N 148 
GLN   HB2  H  N N 149 
GLN   HB3  H  N N 150 
GLN   HG2  H  N N 151 
GLN   HG3  H  N N 152 
GLN   HE21 H  N N 153 
GLN   HE22 H  N N 154 
GLN   HXT  H  N N 155 
GLU   N    N  N N 156 
GLU   CA   C  N S 157 
GLU   C    C  N N 158 
GLU   O    O  N N 159 
GLU   CB   C  N N 160 
GLU   CG   C  N N 161 
GLU   CD   C  N N 162 
GLU   OE1  O  N N 163 
GLU   OE2  O  N N 164 
GLU   OXT  O  N N 165 
GLU   H    H  N N 166 
GLU   H2   H  N N 167 
GLU   HA   H  N N 168 
GLU   HB2  H  N N 169 
GLU   HB3  H  N N 170 
GLU   HG2  H  N N 171 
GLU   HG3  H  N N 172 
GLU   HE2  H  N N 173 
GLU   HXT  H  N N 174 
GLY   N    N  N N 175 
GLY   CA   C  N N 176 
GLY   C    C  N N 177 
GLY   O    O  N N 178 
GLY   OXT  O  N N 179 
GLY   H    H  N N 180 
GLY   H2   H  N N 181 
GLY   HA2  H  N N 182 
GLY   HA3  H  N N 183 
GLY   HXT  H  N N 184 
HIS   N    N  N N 185 
HIS   CA   C  N S 186 
HIS   C    C  N N 187 
HIS   O    O  N N 188 
HIS   CB   C  N N 189 
HIS   CG   C  Y N 190 
HIS   ND1  N  Y N 191 
HIS   CD2  C  Y N 192 
HIS   CE1  C  Y N 193 
HIS   NE2  N  Y N 194 
HIS   OXT  O  N N 195 
HIS   H    H  N N 196 
HIS   H2   H  N N 197 
HIS   HA   H  N N 198 
HIS   HB2  H  N N 199 
HIS   HB3  H  N N 200 
HIS   HD1  H  N N 201 
HIS   HD2  H  N N 202 
HIS   HE1  H  N N 203 
HIS   HE2  H  N N 204 
HIS   HXT  H  N N 205 
HOH   O    O  N N 206 
HOH   H1   H  N N 207 
HOH   H2   H  N N 208 
ILE   N    N  N N 209 
ILE   CA   C  N S 210 
ILE   C    C  N N 211 
ILE   O    O  N N 212 
ILE   CB   C  N S 213 
ILE   CG1  C  N N 214 
ILE   CG2  C  N N 215 
ILE   CD1  C  N N 216 
ILE   OXT  O  N N 217 
ILE   H    H  N N 218 
ILE   H2   H  N N 219 
ILE   HA   H  N N 220 
ILE   HB   H  N N 221 
ILE   HG12 H  N N 222 
ILE   HG13 H  N N 223 
ILE   HG21 H  N N 224 
ILE   HG22 H  N N 225 
ILE   HG23 H  N N 226 
ILE   HD11 H  N N 227 
ILE   HD12 H  N N 228 
ILE   HD13 H  N N 229 
ILE   HXT  H  N N 230 
LEU   N    N  N N 231 
LEU   CA   C  N S 232 
LEU   C    C  N N 233 
LEU   O    O  N N 234 
LEU   CB   C  N N 235 
LEU   CG   C  N N 236 
LEU   CD1  C  N N 237 
LEU   CD2  C  N N 238 
LEU   OXT  O  N N 239 
LEU   H    H  N N 240 
LEU   H2   H  N N 241 
LEU   HA   H  N N 242 
LEU   HB2  H  N N 243 
LEU   HB3  H  N N 244 
LEU   HG   H  N N 245 
LEU   HD11 H  N N 246 
LEU   HD12 H  N N 247 
LEU   HD13 H  N N 248 
LEU   HD21 H  N N 249 
LEU   HD22 H  N N 250 
LEU   HD23 H  N N 251 
LEU   HXT  H  N N 252 
LYS   N    N  N N 253 
LYS   CA   C  N S 254 
LYS   C    C  N N 255 
LYS   O    O  N N 256 
LYS   CB   C  N N 257 
LYS   CG   C  N N 258 
LYS   CD   C  N N 259 
LYS   CE   C  N N 260 
LYS   NZ   N  N N 261 
LYS   OXT  O  N N 262 
LYS   H    H  N N 263 
LYS   H2   H  N N 264 
LYS   HA   H  N N 265 
LYS   HB2  H  N N 266 
LYS   HB3  H  N N 267 
LYS   HG2  H  N N 268 
LYS   HG3  H  N N 269 
LYS   HD2  H  N N 270 
LYS   HD3  H  N N 271 
LYS   HE2  H  N N 272 
LYS   HE3  H  N N 273 
LYS   HZ1  H  N N 274 
LYS   HZ2  H  N N 275 
LYS   HZ3  H  N N 276 
LYS   HXT  H  N N 277 
MET   N    N  N N 278 
MET   CA   C  N S 279 
MET   C    C  N N 280 
MET   O    O  N N 281 
MET   CB   C  N N 282 
MET   CG   C  N N 283 
MET   SD   S  N N 284 
MET   CE   C  N N 285 
MET   OXT  O  N N 286 
MET   H    H  N N 287 
MET   H2   H  N N 288 
MET   HA   H  N N 289 
MET   HB2  H  N N 290 
MET   HB3  H  N N 291 
MET   HG2  H  N N 292 
MET   HG3  H  N N 293 
MET   HE1  H  N N 294 
MET   HE2  H  N N 295 
MET   HE3  H  N N 296 
MET   HXT  H  N N 297 
PHE   N    N  N N 298 
PHE   CA   C  N S 299 
PHE   C    C  N N 300 
PHE   O    O  N N 301 
PHE   CB   C  N N 302 
PHE   CG   C  Y N 303 
PHE   CD1  C  Y N 304 
PHE   CD2  C  Y N 305 
PHE   CE1  C  Y N 306 
PHE   CE2  C  Y N 307 
PHE   CZ   C  Y N 308 
PHE   OXT  O  N N 309 
PHE   H    H  N N 310 
PHE   H2   H  N N 311 
PHE   HA   H  N N 312 
PHE   HB2  H  N N 313 
PHE   HB3  H  N N 314 
PHE   HD1  H  N N 315 
PHE   HD2  H  N N 316 
PHE   HE1  H  N N 317 
PHE   HE2  H  N N 318 
PHE   HZ   H  N N 319 
PHE   HXT  H  N N 320 
PRO   N    N  N N 321 
PRO   CA   C  N S 322 
PRO   C    C  N N 323 
PRO   O    O  N N 324 
PRO   CB   C  N N 325 
PRO   CG   C  N N 326 
PRO   CD   C  N N 327 
PRO   OXT  O  N N 328 
PRO   H    H  N N 329 
PRO   HA   H  N N 330 
PRO   HB2  H  N N 331 
PRO   HB3  H  N N 332 
PRO   HG2  H  N N 333 
PRO   HG3  H  N N 334 
PRO   HD2  H  N N 335 
PRO   HD3  H  N N 336 
PRO   HXT  H  N N 337 
SER   N    N  N N 338 
SER   CA   C  N S 339 
SER   C    C  N N 340 
SER   O    O  N N 341 
SER   CB   C  N N 342 
SER   OG   O  N N 343 
SER   OXT  O  N N 344 
SER   H    H  N N 345 
SER   H2   H  N N 346 
SER   HA   H  N N 347 
SER   HB2  H  N N 348 
SER   HB3  H  N N 349 
SER   HG   H  N N 350 
SER   HXT  H  N N 351 
TFA   C1   C  N N 352 
TFA   C2   C  N N 353 
TFA   O    O  N N 354 
TFA   F1   F  N N 355 
TFA   F2   F  N N 356 
TFA   F3   F  N N 357 
TFA   OXT  O  N N 358 
TFA   HXT  H  N N 359 
THR   N    N  N N 360 
THR   CA   C  N S 361 
THR   C    C  N N 362 
THR   O    O  N N 363 
THR   CB   C  N R 364 
THR   OG1  O  N N 365 
THR   CG2  C  N N 366 
THR   OXT  O  N N 367 
THR   H    H  N N 368 
THR   H2   H  N N 369 
THR   HA   H  N N 370 
THR   HB   H  N N 371 
THR   HG1  H  N N 372 
THR   HG21 H  N N 373 
THR   HG22 H  N N 374 
THR   HG23 H  N N 375 
THR   HXT  H  N N 376 
TYR   N    N  N N 377 
TYR   CA   C  N S 378 
TYR   C    C  N N 379 
TYR   O    O  N N 380 
TYR   CB   C  N N 381 
TYR   CG   C  Y N 382 
TYR   CD1  C  Y N 383 
TYR   CD2  C  Y N 384 
TYR   CE1  C  Y N 385 
TYR   CE2  C  Y N 386 
TYR   CZ   C  Y N 387 
TYR   OH   O  N N 388 
TYR   OXT  O  N N 389 
TYR   H    H  N N 390 
TYR   H2   H  N N 391 
TYR   HA   H  N N 392 
TYR   HB2  H  N N 393 
TYR   HB3  H  N N 394 
TYR   HD1  H  N N 395 
TYR   HD2  H  N N 396 
TYR   HE1  H  N N 397 
TYR   HE2  H  N N 398 
TYR   HH   H  N N 399 
TYR   HXT  H  N N 400 
VAL   N    N  N N 401 
VAL   CA   C  N S 402 
VAL   C    C  N N 403 
VAL   O    O  N N 404 
VAL   CB   C  N N 405 
VAL   CG1  C  N N 406 
VAL   CG2  C  N N 407 
VAL   OXT  O  N N 408 
VAL   H    H  N N 409 
VAL   H2   H  N N 410 
VAL   HA   H  N N 411 
VAL   HB   H  N N 412 
VAL   HG11 H  N N 413 
VAL   HG12 H  N N 414 
VAL   HG13 H  N N 415 
VAL   HG21 H  N N 416 
VAL   HG22 H  N N 417 
VAL   HG23 H  N N 418 
VAL   HXT  H  N N 419 
# 
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 
A1BAO O2  C7   sing N N 1   
A1BAO C6  C7   doub Y N 2   
A1BAO C6  C5   sing Y N 3   
A1BAO C7  C8   sing Y N 4   
A1BAO C5  C4   doub Y N 5   
A1BAO C8  C9   doub Y N 6   
A1BAO C4  C9   sing Y N 7   
A1BAO C4  C3   sing N N 8   
A1BAO C3  C2   sing N N 9   
A1BAO O1  C1   sing N N 10  
A1BAO C1  C2   sing N N 11  
A1BAO C2  N1   sing N N 12  
A1BAO N1  C10  sing N N 13  
A1BAO C10 C13  doub Y N 14  
A1BAO C10 N2   sing Y N 15  
A1BAO C14 C13  sing Y N 16  
A1BAO C14 C15  doub Y N 17  
A1BAO C13 C12  sing Y N 18  
A1BAO N2  C11  doub Y N 19  
A1BAO C15 N4   sing Y N 20  
A1BAO C12 N4   sing Y N 21  
A1BAO C12 N3   doub Y N 22  
A1BAO C11 N3   sing Y N 23  
A1BAO C3  H6   sing N N 24  
A1BAO C3  H5   sing N N 25  
A1BAO C6  H8   sing N N 26  
A1BAO C9  H11  sing N N 27  
A1BAO C14 H14  sing N N 28  
A1BAO C1  H4   sing N N 29  
A1BAO C1  H3   sing N N 30  
A1BAO C11 H13  sing N N 31  
A1BAO C15 H15  sing N N 32  
A1BAO C2  H1   sing N N 33  
A1BAO C5  H7   sing N N 34  
A1BAO C8  H10  sing N N 35  
A1BAO N1  H12  sing N N 36  
A1BAO N4  H16  sing N N 37  
A1BAO O1  H2   sing N N 38  
A1BAO O2  H9   sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
DMS   S   O    doub N N 122 
DMS   S   C1   sing N N 123 
DMS   S   C2   sing N N 124 
DMS   C1  H11  sing N N 125 
DMS   C1  H12  sing N N 126 
DMS   C1  H13  sing N N 127 
DMS   C2  H21  sing N N 128 
DMS   C2  H22  sing N N 129 
DMS   C2  H23  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
HIS   N   CA   sing N N 177 
HIS   N   H    sing N N 178 
HIS   N   H2   sing N N 179 
HIS   CA  C    sing N N 180 
HIS   CA  CB   sing N N 181 
HIS   CA  HA   sing N N 182 
HIS   C   O    doub N N 183 
HIS   C   OXT  sing N N 184 
HIS   CB  CG   sing N N 185 
HIS   CB  HB2  sing N N 186 
HIS   CB  HB3  sing N N 187 
HIS   CG  ND1  sing Y N 188 
HIS   CG  CD2  doub Y N 189 
HIS   ND1 CE1  doub Y N 190 
HIS   ND1 HD1  sing N N 191 
HIS   CD2 NE2  sing Y N 192 
HIS   CD2 HD2  sing N N 193 
HIS   CE1 NE2  sing Y N 194 
HIS   CE1 HE1  sing N N 195 
HIS   NE2 HE2  sing N N 196 
HIS   OXT HXT  sing N N 197 
HOH   O   H1   sing N N 198 
HOH   O   H2   sing N N 199 
ILE   N   CA   sing N N 200 
ILE   N   H    sing N N 201 
ILE   N   H2   sing N N 202 
ILE   CA  C    sing N N 203 
ILE   CA  CB   sing N N 204 
ILE   CA  HA   sing N N 205 
ILE   C   O    doub N N 206 
ILE   C   OXT  sing N N 207 
ILE   CB  CG1  sing N N 208 
ILE   CB  CG2  sing N N 209 
ILE   CB  HB   sing N N 210 
ILE   CG1 CD1  sing N N 211 
ILE   CG1 HG12 sing N N 212 
ILE   CG1 HG13 sing N N 213 
ILE   CG2 HG21 sing N N 214 
ILE   CG2 HG22 sing N N 215 
ILE   CG2 HG23 sing N N 216 
ILE   CD1 HD11 sing N N 217 
ILE   CD1 HD12 sing N N 218 
ILE   CD1 HD13 sing N N 219 
ILE   OXT HXT  sing N N 220 
LEU   N   CA   sing N N 221 
LEU   N   H    sing N N 222 
LEU   N   H2   sing N N 223 
LEU   CA  C    sing N N 224 
LEU   CA  CB   sing N N 225 
LEU   CA  HA   sing N N 226 
LEU   C   O    doub N N 227 
LEU   C   OXT  sing N N 228 
LEU   CB  CG   sing N N 229 
LEU   CB  HB2  sing N N 230 
LEU   CB  HB3  sing N N 231 
LEU   CG  CD1  sing N N 232 
LEU   CG  CD2  sing N N 233 
LEU   CG  HG   sing N N 234 
LEU   CD1 HD11 sing N N 235 
LEU   CD1 HD12 sing N N 236 
LEU   CD1 HD13 sing N N 237 
LEU   CD2 HD21 sing N N 238 
LEU   CD2 HD22 sing N N 239 
LEU   CD2 HD23 sing N N 240 
LEU   OXT HXT  sing N N 241 
LYS   N   CA   sing N N 242 
LYS   N   H    sing N N 243 
LYS   N   H2   sing N N 244 
LYS   CA  C    sing N N 245 
LYS   CA  CB   sing N N 246 
LYS   CA  HA   sing N N 247 
LYS   C   O    doub N N 248 
LYS   C   OXT  sing N N 249 
LYS   CB  CG   sing N N 250 
LYS   CB  HB2  sing N N 251 
LYS   CB  HB3  sing N N 252 
LYS   CG  CD   sing N N 253 
LYS   CG  HG2  sing N N 254 
LYS   CG  HG3  sing N N 255 
LYS   CD  CE   sing N N 256 
LYS   CD  HD2  sing N N 257 
LYS   CD  HD3  sing N N 258 
LYS   CE  NZ   sing N N 259 
LYS   CE  HE2  sing N N 260 
LYS   CE  HE3  sing N N 261 
LYS   NZ  HZ1  sing N N 262 
LYS   NZ  HZ2  sing N N 263 
LYS   NZ  HZ3  sing N N 264 
LYS   OXT HXT  sing N N 265 
MET   N   CA   sing N N 266 
MET   N   H    sing N N 267 
MET   N   H2   sing N N 268 
MET   CA  C    sing N N 269 
MET   CA  CB   sing N N 270 
MET   CA  HA   sing N N 271 
MET   C   O    doub N N 272 
MET   C   OXT  sing N N 273 
MET   CB  CG   sing N N 274 
MET   CB  HB2  sing N N 275 
MET   CB  HB3  sing N N 276 
MET   CG  SD   sing N N 277 
MET   CG  HG2  sing N N 278 
MET   CG  HG3  sing N N 279 
MET   SD  CE   sing N N 280 
MET   CE  HE1  sing N N 281 
MET   CE  HE2  sing N N 282 
MET   CE  HE3  sing N N 283 
MET   OXT HXT  sing N N 284 
PHE   N   CA   sing N N 285 
PHE   N   H    sing N N 286 
PHE   N   H2   sing N N 287 
PHE   CA  C    sing N N 288 
PHE   CA  CB   sing N N 289 
PHE   CA  HA   sing N N 290 
PHE   C   O    doub N N 291 
PHE   C   OXT  sing N N 292 
PHE   CB  CG   sing N N 293 
PHE   CB  HB2  sing N N 294 
PHE   CB  HB3  sing N N 295 
PHE   CG  CD1  doub Y N 296 
PHE   CG  CD2  sing Y N 297 
PHE   CD1 CE1  sing Y N 298 
PHE   CD1 HD1  sing N N 299 
PHE   CD2 CE2  doub Y N 300 
PHE   CD2 HD2  sing N N 301 
PHE   CE1 CZ   doub Y N 302 
PHE   CE1 HE1  sing N N 303 
PHE   CE2 CZ   sing Y N 304 
PHE   CE2 HE2  sing N N 305 
PHE   CZ  HZ   sing N N 306 
PHE   OXT HXT  sing N N 307 
PRO   N   CA   sing N N 308 
PRO   N   CD   sing N N 309 
PRO   N   H    sing N N 310 
PRO   CA  C    sing N N 311 
PRO   CA  CB   sing N N 312 
PRO   CA  HA   sing N N 313 
PRO   C   O    doub N N 314 
PRO   C   OXT  sing N N 315 
PRO   CB  CG   sing N N 316 
PRO   CB  HB2  sing N N 317 
PRO   CB  HB3  sing N N 318 
PRO   CG  CD   sing N N 319 
PRO   CG  HG2  sing N N 320 
PRO   CG  HG3  sing N N 321 
PRO   CD  HD2  sing N N 322 
PRO   CD  HD3  sing N N 323 
PRO   OXT HXT  sing N N 324 
SER   N   CA   sing N N 325 
SER   N   H    sing N N 326 
SER   N   H2   sing N N 327 
SER   CA  C    sing N N 328 
SER   CA  CB   sing N N 329 
SER   CA  HA   sing N N 330 
SER   C   O    doub N N 331 
SER   C   OXT  sing N N 332 
SER   CB  OG   sing N N 333 
SER   CB  HB2  sing N N 334 
SER   CB  HB3  sing N N 335 
SER   OG  HG   sing N N 336 
SER   OXT HXT  sing N N 337 
TFA   C1  C2   sing N N 338 
TFA   C1  O    doub N N 339 
TFA   C1  OXT  sing N N 340 
TFA   C2  F1   sing N N 341 
TFA   C2  F2   sing N N 342 
TFA   C2  F3   sing N N 343 
TFA   OXT HXT  sing N N 344 
THR   N   CA   sing N N 345 
THR   N   H    sing N N 346 
THR   N   H2   sing N N 347 
THR   CA  C    sing N N 348 
THR   CA  CB   sing N N 349 
THR   CA  HA   sing N N 350 
THR   C   O    doub N N 351 
THR   C   OXT  sing N N 352 
THR   CB  OG1  sing N N 353 
THR   CB  CG2  sing N N 354 
THR   CB  HB   sing N N 355 
THR   OG1 HG1  sing N N 356 
THR   CG2 HG21 sing N N 357 
THR   CG2 HG22 sing N N 358 
THR   CG2 HG23 sing N N 359 
THR   OXT HXT  sing N N 360 
TYR   N   CA   sing N N 361 
TYR   N   H    sing N N 362 
TYR   N   H2   sing N N 363 
TYR   CA  C    sing N N 364 
TYR   CA  CB   sing N N 365 
TYR   CA  HA   sing N N 366 
TYR   C   O    doub N N 367 
TYR   C   OXT  sing N N 368 
TYR   CB  CG   sing N N 369 
TYR   CB  HB2  sing N N 370 
TYR   CB  HB3  sing N N 371 
TYR   CG  CD1  doub Y N 372 
TYR   CG  CD2  sing Y N 373 
TYR   CD1 CE1  sing Y N 374 
TYR   CD1 HD1  sing N N 375 
TYR   CD2 CE2  doub Y N 376 
TYR   CD2 HD2  sing N N 377 
TYR   CE1 CZ   doub Y N 378 
TYR   CE1 HE1  sing N N 379 
TYR   CE2 CZ   sing Y N 380 
TYR   CE2 HE2  sing N N 381 
TYR   CZ  OH   sing N N 382 
TYR   OH  HH   sing N N 383 
TYR   OXT HXT  sing N N 384 
VAL   N   CA   sing N N 385 
VAL   N   H    sing N N 386 
VAL   N   H2   sing N N 387 
VAL   CA  C    sing N N 388 
VAL   CA  CB   sing N N 389 
VAL   CA  HA   sing N N 390 
VAL   C   O    doub N N 391 
VAL   C   OXT  sing N N 392 
VAL   CB  CG1  sing N N 393 
VAL   CB  CG2  sing N N 394 
VAL   CB  HB   sing N N 395 
VAL   CG1 HG11 sing N N 396 
VAL   CG1 HG12 sing N N 397 
VAL   CG1 HG13 sing N N 398 
VAL   CG2 HG21 sing N N 399 
VAL   CG2 HG22 sing N N 400 
VAL   CG2 HG23 sing N N 401 
VAL   OXT HXT  sing N N 402 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171110 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         
'PanDDA analysis group deposition of SARS-CoV-2 NSP3 macrodomain ligand screen - FrankenROCS hits and analogues of AVI-313' 
_pdbx_deposit_group.group_description   
'SARS-CoV-2 NSP3 macrodomain in complex with ligands identified by X-ray diffraction using ALS 8.3.1,  SSRL 9-2, and SSRL 12-2' 
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002304 
# 
_atom_sites.entry_id                    7HF4 
_atom_sites.fract_transf_matrix[1][1]   0.011272 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011272 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.025369 
_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   ? 19.624 -16.234 22.231  0.50 46.98 ?  3    VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.621 -16.241 22.248  0.50 46.83 ?  3    VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.653 -15.159 22.391  0.50 46.69 ?  3    VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.690 -15.132 22.418  0.50 46.55 ?  3    VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.306 -13.811 22.109  0.50 45.48 ?  3    VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.365 -13.815 22.054  0.50 45.35 ?  3    VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.403 -13.531 22.594  0.50 45.86 ?  3    VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.508 -13.567 22.438  0.50 45.68 ?  3    VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.011 -15.189 23.794  0.50 47.41 ?  3    VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.123 -15.092 23.853  0.50 47.23 ?  3    VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 16.994 -14.065 23.941  0.50 47.57 ?  3    VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.139 -13.940 24.008  0.50 47.37 ?  3    VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.360 -16.540 24.054  0.50 47.56 ?  3    VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.458 -16.416 24.201  0.50 47.40 ?  3    VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.943 -15.281 21.745  0.50 56.06 ?  3    VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.944 -15.255 21.815  0.50 55.88 ?  3    VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.701 -15.056 24.463  0.50 56.91 ?  3    VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.850 -14.951 24.480  0.50 56.70 ?  3    VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.477 -14.212 24.748  0.50 57.10 ?  3    VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.667 -14.040 24.850  0.50 56.87 ?  3    VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.463 -13.218 24.000  0.50 57.10 ?  3    VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.627 -13.102 24.003  0.50 56.87 ?  3    VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.407 -14.068 23.169  0.50 57.10 ?  3    VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.508 -13.963 23.272  0.50 56.87 ?  3    VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.905 -16.512 24.910  0.50 57.10 ?  3    VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 17.047 -16.343 25.077  0.50 56.90 ?  3    VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.722 -16.724 23.347  0.50 57.10 ?  3    VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.782 -16.613 23.534  0.50 56.90 ?  3    VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.047 -17.225 24.066  0.50 57.10 ?  3    VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.130 -17.115 24.208  0.50 56.90 ?  3    VAL   A HG23 1 
ATOM   31   N  N    A ASN   A 1 4   ? 18.631 -12.982 21.315  0.50 43.54 ?  4    ASN   A N    1 
ATOM   32   N  N    B ASN   A 1 4   ? 18.654 -12.975 21.302  0.50 43.49 ?  4    ASN   A N    1 
ATOM   33   C  CA   A ASN   A 1 4   ? 19.081 -11.626 21.027  0.50 41.32 ?  4    ASN   A CA   1 
ATOM   34   C  CA   B ASN   A 1 4   ? 19.113 -11.632 20.973  0.50 41.36 ?  4    ASN   A CA   1 
ATOM   35   C  C    A ASN   A 1 4   ? 17.935 -10.652 21.285  0.50 39.50 ?  4    ASN   A C    1 
ATOM   36   C  C    B ASN   A 1 4   ? 17.977 -10.642 21.219  0.50 39.58 ?  4    ASN   A C    1 
ATOM   37   O  O    A ASN   A 1 4   ? 16.825 -11.048 21.654  0.50 39.47 ?  4    ASN   A O    1 
ATOM   38   O  O    B ASN   A 1 4   ? 16.857 -11.023 21.574  0.50 39.59 ?  4    ASN   A O    1 
ATOM   39   C  CB   A ASN   A 1 4   ? 19.640 -11.499 19.602  0.50 40.63 ?  4    ASN   A CB   1 
ATOM   40   C  CB   B ASN   A 1 4   ? 19.670 -11.549 19.543  0.50 40.68 ?  4    ASN   A CB   1 
ATOM   41   C  CG   A ASN   A 1 4   ? 18.635 -11.884 18.538  0.50 39.82 ?  4    ASN   A CG   1 
ATOM   42   C  CG   B ASN   A 1 4   ? 18.652 -11.938 18.491  0.50 39.89 ?  4    ASN   A CG   1 
ATOM   43   O  OD1  A ASN   A 1 4   ? 17.504 -11.399 18.527  0.50 39.55 ?  4    ASN   A OD1  1 
ATOM   44   O  OD1  B ASN   A 1 4   ? 17.542 -11.408 18.456  0.50 39.64 ?  4    ASN   A OD1  1 
ATOM   45   N  ND2  A ASN   A 1 4   ? 19.046 -12.764 17.631  0.50 39.59 ?  4    ASN   A ND2  1 
ATOM   46   N  ND2  B ASN   A 1 4   ? 19.028 -12.873 17.624  0.50 39.64 ?  4    ASN   A ND2  1 
ATOM   47   H  H    A ASN   A 1 4   ? 17.891 -13.190 20.928  0.50 52.27 ?  4    ASN   A H    1 
ATOM   48   H  H    B ASN   A 1 4   ? 17.885 -13.170 20.967  0.50 52.21 ?  4    ASN   A H    1 
ATOM   49   H  HA   A ASN   A 1 4   ? 19.798 -11.407 21.636  0.50 49.61 ?  4    ASN   A HA   1 
ATOM   50   H  HA   B ASN   A 1 4   ? 19.837 -11.405 21.572  0.50 49.65 ?  4    ASN   A HA   1 
ATOM   51   H  HB2  A ASN   A 1 4   ? 19.903 -10.576 19.449  0.50 48.78 ?  4    ASN   A HB2  1 
ATOM   52   H  HB2  B ASN   A 1 4   ? 19.952 -10.636 19.367  0.50 48.84 ?  4    ASN   A HB2  1 
ATOM   53   H  HB3  A ASN   A 1 4   ? 20.410 -12.080 19.513  0.50 48.78 ?  4    ASN   A HB3  1 
ATOM   54   H  HB3  B ASN   A 1 4   ? 20.428 -12.149 19.464  0.50 48.84 ?  4    ASN   A HB3  1 
ATOM   55   H  HD21 A ASN   A 1 4   ? 18.517 -13.015 17.002  0.50 47.53 ?  4    ASN   A HD21 1 
ATOM   56   H  HD21 B ASN   A 1 4   ? 18.490 -13.128 17.004  0.50 47.60 ?  4    ASN   A HD21 1 
ATOM   57   H  HD22 A ASN   A 1 4   ? 19.845 -13.082 17.673  0.50 47.53 ?  4    ASN   A HD22 1 
ATOM   58   H  HD22 B ASN   A 1 4   ? 19.813 -13.223 17.682  0.50 47.60 ?  4    ASN   A HD22 1 
ATOM   59   N  N    A SER   A 1 5   ? 18.211 -9.364  21.085  0.50 37.33 ?  5    SER   A N    1 
ATOM   60   N  N    B SER   A 1 5   ? 18.272 -9.357  21.024  0.50 37.37 ?  5    SER   A N    1 
ATOM   61   C  CA   A SER   A 1 5   ? 17.290 -8.298  21.457  0.50 35.13 ?  5    SER   A CA   1 
ATOM   62   C  CA   B SER   A 1 5   ? 17.377 -8.276  21.418  0.50 35.10 ?  5    SER   A CA   1 
ATOM   63   C  C    A SER   A 1 5   ? 16.434 -7.807  20.295  0.50 32.48 ?  5    SER   A C    1 
ATOM   64   C  C    B SER   A 1 5   ? 16.473 -7.796  20.286  0.50 32.50 ?  5    SER   A C    1 
ATOM   65   O  O    A SER   A 1 5   ? 15.750 -6.788  20.435  0.50 32.55 ?  5    SER   A O    1 
ATOM   66   O  O    B SER   A 1 5   ? 15.792 -6.778  20.444  0.50 32.61 ?  5    SER   A O    1 
ATOM   67   C  CB   A SER   A 1 5   ? 18.055 -7.125  22.075  0.50 35.81 ?  5    SER   A CB   1 
ATOM   68   C  CB   B SER   A 1 5   ? 18.183 -7.099  21.972  0.50 35.68 ?  5    SER   A CB   1 
ATOM   69   O  OG   A SER   A 1 5   ? 18.985 -6.579  21.156  0.50 36.06 ?  5    SER   A OG   1 
ATOM   70   O  OG   B SER   A 1 5   ? 19.065 -6.581  20.992  0.50 35.80 ?  5    SER   A OG   1 
ATOM   71   H  H    A SER   A 1 5   ? 18.937 -9.081  20.723  0.50 44.82 ?  5    SER   A H    1 
ATOM   72   H  H    B SER   A 1 5   ? 18.998 -9.087  20.653  0.50 44.87 ?  5    SER   A H    1 
ATOM   73   H  HA   A SER   A 1 5   ? 16.691 -8.638  22.139  0.50 42.18 ?  5    SER   A HA   1 
ATOM   74   H  HA   B SER   A 1 5   ? 16.809 -8.597  22.135  0.50 42.14 ?  5    SER   A HA   1 
ATOM   75   H  HB2  A SER   A 1 5   ? 17.420 -6.434  22.329  0.50 42.99 ?  5    SER   A HB2  1 
ATOM   76   H  HB2  B SER   A 1 5   ? 17.569 -6.398  22.247  0.50 42.83 ?  5    SER   A HB2  1 
ATOM   77   H  HB3  A SER   A 1 5   ? 18.532 -7.436  22.861  0.50 42.99 ?  5    SER   A HB3  1 
ATOM   78   H  HB3  B SER   A 1 5   ? 18.701 -7.400  22.736  0.50 42.83 ?  5    SER   A HB3  1 
ATOM   79   H  HG   A SER   A 1 5   ? 19.395 -5.936  21.510  0.50 43.30 ?  5    SER   A HG   1 
ATOM   80   H  HG   B SER   A 1 5   ? 19.500 -5.935  21.308  0.50 42.99 ?  5    SER   A HG   1 
ATOM   81   N  N    . PHE   A 1 6   ? 16.452 -8.494  19.155  1.00 29.28 ?  6    PHE   A N    1 
ATOM   82   C  CA   . PHE   A 1 6   ? 15.562 -8.121  18.062  1.00 23.49 ?  6    PHE   A CA   1 
ATOM   83   C  C    . PHE   A 1 6   ? 14.127 -8.491  18.424  1.00 23.13 ?  6    PHE   A C    1 
ATOM   84   O  O    . PHE   A 1 6   ? 13.865 -9.606  18.882  1.00 24.67 ?  6    PHE   A O    1 
ATOM   85   C  CB   . PHE   A 1 6   ? 15.973 -8.831  16.777  1.00 19.78 ?  6    PHE   A CB   1 
ATOM   86   C  CG   . PHE   A 1 6   ? 17.235 -8.288  16.158  1.00 17.22 ?  6    PHE   A CG   1 
ATOM   87   C  CD1  . PHE   A 1 6   ? 17.232 -7.073  15.492  1.00 16.44 ?  6    PHE   A CD1  1 
ATOM   88   C  CD2  . PHE   A 1 6   ? 18.415 -9.006  16.227  1.00 18.02 ?  6    PHE   A CD2  1 
ATOM   89   C  CE1  . PHE   A 1 6   ? 18.389 -6.578  14.913  1.00 16.73 ?  6    PHE   A CE1  1 
ATOM   90   C  CE2  . PHE   A 1 6   ? 19.571 -8.521  15.653  1.00 18.20 ?  6    PHE   A CE2  1 
ATOM   91   C  CZ   . PHE   A 1 6   ? 19.560 -7.303  14.995  1.00 17.46 ?  6    PHE   A CZ   1 
ATOM   92   H  H    A PHE   A 1 6   ? 16.961 -9.169  18.994  0.50 35.16 ?  6    PHE   A H    1 
ATOM   93   H  H    B PHE   A 1 6   ? 16.940 -9.185  18.997  0.50 35.16 ?  6    PHE   A H    1 
ATOM   94   H  HA   . PHE   A 1 6   ? 15.605 -7.168  17.921  1.00 28.21 ?  6    PHE   A HA   1 
ATOM   95   H  HB2  . PHE   A 1 6   ? 16.117 -9.773  16.974  1.00 23.76 ?  6    PHE   A HB2  1 
ATOM   96   H  HB3  . PHE   A 1 6   ? 15.258 -8.740  16.129  1.00 23.76 ?  6    PHE   A HB3  1 
ATOM   97   H  HD1  . PHE   A 1 6   ? 16.442 -6.583  15.438  1.00 19.75 ?  6    PHE   A HD1  1 
ATOM   98   H  HD2  . PHE   A 1 6   ? 18.428 -9.826  16.671  1.00 21.64 ?  6    PHE   A HD2  1 
ATOM   99   H  HE1  . PHE   A 1 6   ? 18.377 -5.758  14.472  1.00 20.09 ?  6    PHE   A HE1  1 
ATOM   100  H  HE2  . PHE   A 1 6   ? 20.363 -9.008  15.710  1.00 21.86 ?  6    PHE   A HE2  1 
ATOM   101  H  HZ   . PHE   A 1 6   ? 20.339 -6.971  14.609  1.00 20.97 ?  6    PHE   A HZ   1 
ATOM   102  N  N    . SER   A 1 7   ? 13.192 -7.563  18.209  1.00 21.83 ?  7    SER   A N    1 
ATOM   103  C  CA   . SER   A 1 7   ? 11.828 -7.698  18.707  1.00 21.88 ?  7    SER   A CA   1 
ATOM   104  C  C    . SER   A 1 7   ? 10.814 -7.460  17.594  1.00 19.87 ?  7    SER   A C    1 
ATOM   105  O  O    . SER   A 1 7   ? 10.998 -6.579  16.751  1.00 19.97 ?  7    SER   A O    1 
ATOM   106  C  CB   . SER   A 1 7   ? 11.580 -6.695  19.842  1.00 24.17 ?  7    SER   A CB   1 
ATOM   107  O  OG   . SER   A 1 7   ? 10.225 -6.705  20.245  1.00 26.30 ?  7    SER   A OG   1 
ATOM   108  H  H    . SER   A 1 7   ? 13.329 -6.843  17.758  1.00 26.21 ?  7    SER   A H    1 
ATOM   109  H  HA   . SER   A 1 7   ? 11.695 -8.592  19.056  1.00 26.28 ?  7    SER   A HA   1 
ATOM   110  H  HB2  . SER   A 1 7   ? 12.134 -6.936  20.603  1.00 29.03 ?  7    SER   A HB2  1 
ATOM   111  H  HB3  . SER   A 1 7   ? 11.818 -5.804  19.533  1.00 29.03 ?  7    SER   A HB3  1 
ATOM   112  H  HG   . SER   A 1 7   ? 10.104 -6.144  20.860  1.00 31.58 ?  7    SER   A HG   1 
ATOM   113  N  N    . GLY   A 1 8   ? 9.732  -8.240  17.607  1.00 18.38 ?  8    GLY   A N    1 
ATOM   114  C  CA   . GLY   A 1 8   ? 8.635  -8.015  16.689  1.00 17.74 ?  8    GLY   A CA   1 
ATOM   115  C  C    . GLY   A 1 8   ? 8.841  -8.520  15.281  1.00 16.03 ?  8    GLY   A C    1 
ATOM   116  O  O    . GLY   A 1 8   ? 8.079  -8.134  14.387  1.00 16.93 ?  8    GLY   A O    1 
ATOM   117  H  H    . GLY   A 1 8   ? 9.616  -8.903  18.143  1.00 22.08 ?  8    GLY   A H    1 
ATOM   118  H  HA2  . GLY   A 1 8   ? 7.839  -8.441  17.046  1.00 21.31 ?  8    GLY   A HA2  1 
ATOM   119  H  HA3  . GLY   A 1 8   ? 8.461  -7.063  16.636  1.00 21.31 ?  8    GLY   A HA3  1 
ATOM   120  N  N    . TYR   A 1 9   ? 9.839  -9.369  15.048  1.00 15.02 ?  9    TYR   A N    1 
ATOM   121  C  CA   . TYR   A 1 9   ? 10.094 -9.897  13.718  1.00 13.75 ?  9    TYR   A CA   1 
ATOM   122  C  C    . TYR   A 1 9   ? 9.228  -11.119 13.446  1.00 13.74 ?  9    TYR   A C    1 
ATOM   123  O  O    . TYR   A 1 9   ? 8.972  -11.936 14.339  1.00 15.48 ?  9    TYR   A O    1 
ATOM   124  C  CB   . TYR   A 1 9   ? 11.571 -10.280 13.552  1.00 13.87 ?  9    TYR   A CB   1 
ATOM   125  C  CG   . TYR   A 1 9   ? 12.477 -9.078  13.378  1.00 13.48 ?  9    TYR   A CG   1 
ATOM   126  C  CD1  . TYR   A 1 9   ? 12.802 -8.272  14.456  1.00 14.20 ?  9    TYR   A CD1  1 
ATOM   127  C  CD2  . TYR   A 1 9   ? 12.978 -8.735  12.130  1.00 13.31 ?  9    TYR   A CD2  1 
ATOM   128  C  CE1  . TYR   A 1 9   ? 13.602 -7.158  14.300  1.00 14.69 ?  9    TYR   A CE1  1 
ATOM   129  C  CE2  . TYR   A 1 9   ? 13.776 -7.629  11.962  1.00 13.39 ?  9    TYR   A CE2  1 
ATOM   130  C  CZ   . TYR   A 1 9   ? 14.083 -6.839  13.045  1.00 14.51 ?  9    TYR   A CZ   1 
ATOM   131  O  OH   . TYR   A 1 9   ? 14.871 -5.734  12.867  1.00 15.80 ?  9    TYR   A OH   1 
ATOM   132  H  H    . TYR   A 1 9   ? 10.381 -9.663  15.653  1.00 18.05 ?  9    TYR   A H    1 
ATOM   133  H  HA   . TYR   A 1 9   ? 9.882  -9.214  13.060  1.00 16.53 ?  9    TYR   A HA   1 
ATOM   134  H  HB2  . TYR   A 1 9   ? 11.863 -10.775 14.333  1.00 16.66 ?  9    TYR   A HB2  1 
ATOM   135  H  HB3  . TYR   A 1 9   ? 11.651 -10.836 12.759  1.00 16.66 ?  9    TYR   A HB3  1 
ATOM   136  H  HD1  . TYR   A 1 9   ? 12.458 -8.486  15.300  1.00 17.07 ?  9    TYR   A HD1  1 
ATOM   137  H  HD2  . TYR   A 1 9   ? 12.769 -9.264  11.392  1.00 16.00 ?  9    TYR   A HD2  1 
ATOM   138  H  HE1  . TYR   A 1 9   ? 13.804 -6.630  15.037  1.00 17.66 ?  9    TYR   A HE1  1 
ATOM   139  H  HE2  . TYR   A 1 9   ? 14.111 -7.417  11.121  1.00 16.09 ?  9    TYR   A HE2  1 
ATOM   140  H  HH   . TYR   A 1 9   ? 14.999 -5.357  13.606  1.00 18.98 ?  9    TYR   A HH   1 
ATOM   141  N  N    . LEU   A 1 10  ? 8.799  -11.245 12.194  1.00 12.99 ?  10   LEU   A N    1 
ATOM   142  C  CA   . LEU   A 1 10  ? 8.194  -12.472 11.704  1.00 12.93 ?  10   LEU   A CA   1 
ATOM   143  C  C    . LEU   A 1 10  ? 9.311  -13.410 11.263  1.00 12.24 ?  10   LEU   A C    1 
ATOM   144  O  O    . LEU   A 1 10  ? 10.239 -12.991 10.568  1.00 12.28 ?  10   LEU   A O    1 
ATOM   145  C  CB   . LEU   A 1 10  ? 7.287  -12.151 10.518  1.00 14.26 ?  10   LEU   A CB   1 
ATOM   146  C  CG   . LEU   A 1 10  ? 6.612  -13.350 9.852   1.00 16.25 ?  10   LEU   A CG   1 
ATOM   147  C  CD1  . LEU   A 1 10  ? 5.537  -13.929 10.747  1.00 17.76 ?  10   LEU   A CD1  1 
ATOM   148  C  CD2  . LEU   A 1 10  ? 6.059  -12.985 8.483   1.00 18.00 ?  10   LEU   A CD2  1 
ATOM   149  H  H    . LEU   A 1 10  ? 8.866  -10.626 11.589  1.00 15.61 ?  10   LEU   A H    1 
ATOM   150  H  HA   . LEU   A 1 10  ? 7.670  -12.888 12.406  1.00 15.53 ?  10   LEU   A HA   1 
ATOM   151  H  HB2  . LEU   A 1 10  ? 6.584  -11.550 10.818  1.00 17.13 ?  10   LEU   A HB2  1 
ATOM   152  H  HB3  . LEU   A 1 10  ? 7.818  -11.705 9.838   1.00 17.13 ?  10   LEU   A HB3  1 
ATOM   153  H  HG   . LEU   A 1 10  ? 7.276  -14.042 9.721   1.00 19.53 ?  10   LEU   A HG   1 
ATOM   154  H  HD11 . LEU   A 1 10  ? 5.213  -14.761 10.359  1.00 21.34 ?  10   LEU   A HD11 1 
ATOM   155  H  HD12 . LEU   A 1 10  ? 5.905  -14.103 11.628  1.00 21.34 ?  10   LEU   A HD12 1 
ATOM   156  H  HD13 . LEU   A 1 10  ? 4.803  -13.297 10.819  1.00 21.34 ?  10   LEU   A HD13 1 
ATOM   157  H  HD21 . LEU   A 1 10  ? 5.431  -13.671 8.209   1.00 21.62 ?  10   LEU   A HD21 1 
ATOM   158  H  HD22 . LEU   A 1 10  ? 5.616  -12.129 8.542   1.00 21.62 ?  10   LEU   A HD22 1 
ATOM   159  H  HD23 . LEU   A 1 10  ? 6.796  -12.937 7.856   1.00 21.62 ?  10   LEU   A HD23 1 
ATOM   160  N  N    . LYS   A 1 11  ? 9.230  -14.669 11.668  1.00 12.75 ?  11   LYS   A N    1 
ATOM   161  C  CA   . LYS   A 1 11  ? 10.226 -15.665 11.305  1.00 12.39 ?  11   LYS   A CA   1 
ATOM   162  C  C    . LYS   A 1 11  ? 9.859  -16.236 9.944   1.00 12.57 ?  11   LYS   A C    1 
ATOM   163  O  O    . LYS   A 1 11  ? 8.762  -16.772 9.779   1.00 14.17 ?  11   LYS   A O    1 
ATOM   164  C  CB   . LYS   A 1 11  ? 10.256 -16.755 12.373  1.00 12.50 ?  11   LYS   A CB   1 
ATOM   165  C  CG   . LYS   A 1 11  ? 11.273 -17.857 12.146  1.00 12.42 ?  11   LYS   A CG   1 
ATOM   166  C  CD   . LYS   A 1 11  ? 11.356 -18.737 13.394  1.00 12.93 ?  11   LYS   A CD   1 
ATOM   167  C  CE   . LYS   A 1 11  ? 12.378 -19.868 13.269  1.00 13.12 ?  11   LYS   A CE   1 
ATOM   168  N  NZ   . LYS   A 1 11  ? 13.751 -19.363 13.007  1.00 13.13 ?  11   LYS   A NZ   1 
ATOM   169  H  H    . LYS   A 1 11  ? 8.588  -14.973 12.158  1.00 15.33 ?  11   LYS   A H    1 
ATOM   170  H  HA   . LYS   A 1 11  ? 11.097 -15.246 11.245  1.00 14.89 ?  11   LYS   A HA   1 
ATOM   171  H  HB2  . LYS   A 1 11  ? 10.457 -16.333 13.224  1.00 15.02 ?  11   LYS   A HB2  1 
ATOM   172  H  HB3  . LYS   A 1 11  ? 9.375  -17.161 12.414  1.00 15.02 ?  11   LYS   A HB3  1 
ATOM   173  H  HG2  . LYS   A 1 11  ? 10.994 -18.410 11.397  1.00 14.92 ?  11   LYS   A HG2  1 
ATOM   174  H  HG3  . LYS   A 1 11  ? 12.144 -17.472 11.981  1.00 14.92 ?  11   LYS   A HG3  1 
ATOM   175  H  HD2  . LYS   A 1 11  ? 11.603 -18.188 14.152  1.00 15.54 ?  11   LYS   A HD2  1 
ATOM   176  H  HD3  . LYS   A 1 11  ? 10.484 -19.142 13.552  1.00 15.54 ?  11   LYS   A HD3  1 
ATOM   177  H  HE2  . LYS   A 1 11  ? 12.403 -20.373 14.099  1.00 15.76 ?  11   LYS   A HE2  1 
ATOM   178  H  HE3  . LYS   A 1 11  ? 12.130 -20.450 12.535  1.00 15.76 ?  11   LYS   A HE3  1 
ATOM   179  H  HZ1  . LYS   A 1 11  ? 14.299 -20.042 12.831  1.00 15.77 ?  11   LYS   A HZ1  1 
ATOM   180  H  HZ2  . LYS   A 1 11  ? 13.743 -18.811 12.307  1.00 15.77 ?  11   LYS   A HZ2  1 
ATOM   181  H  HZ3  . LYS   A 1 11  ? 14.056 -18.923 13.717  1.00 15.77 ?  11   LYS   A HZ3  1 
ATOM   182  N  N    . LEU   A 1 12  ? 10.756 -16.112 8.962   1.00 11.91 ?  12   LEU   A N    1 
ATOM   183  C  CA   . LEU   A 1 12  ? 10.492 -16.673 7.639   1.00 12.38 ?  12   LEU   A CA   1 
ATOM   184  C  C    . LEU   A 1 12  ? 11.079 -18.069 7.478   1.00 12.07 ?  12   LEU   A C    1 
ATOM   185  O  O    . LEU   A 1 12  ? 10.448 -18.937 6.865   1.00 12.71 ?  12   LEU   A O    1 
ATOM   186  C  CB   . LEU   A 1 12  ? 11.050 -15.771 6.533   1.00 12.63 ?  12   LEU   A CB   1 
ATOM   187  C  CG   . LEU   A 1 12  ? 10.386 -14.409 6.365   1.00 13.80 ?  12   LEU   A CG   1 
ATOM   188  C  CD1  . LEU   A 1 12  ? 11.081 -13.651 5.258   1.00 14.50 ?  12   LEU   A CD1  1 
ATOM   189  C  CD2  . LEU   A 1 12  ? 8.903  -14.564 6.069   1.00 14.97 ?  12   LEU   A CD2  1 
ATOM   190  H  H    . LEU   A 1 12  ? 11.520 -15.716 9.034   1.00 14.32 ?  12   LEU   A H    1 
ATOM   191  H  HA   . LEU   A 1 12  ? 9.531  -16.745 7.515   1.00 14.88 ?  12   LEU   A HA   1 
ATOM   192  H  HB2  . LEU   A 1 12  ? 11.987 -15.620 6.715   1.00 15.18 ?  12   LEU   A HB2  1 
ATOM   193  H  HB3  . LEU   A 1 12  ? 10.958 -16.246 5.689   1.00 15.18 ?  12   LEU   A HB3  1 
ATOM   194  H  HG   . LEU   A 1 12  ? 10.481 -13.908 7.187   1.00 16.58 ?  12   LEU   A HG   1 
ATOM   195  H  HD11 . LEU   A 1 12  ? 10.643 -12.799 5.133   1.00 17.42 ?  12   LEU   A HD11 1 
ATOM   196  H  HD12 . LEU   A 1 12  ? 12.012 -13.513 5.509   1.00 17.42 ?  12   LEU   A HD12 1 
ATOM   197  H  HD13 . LEU   A 1 12  ? 11.038 -14.173 4.440   1.00 17.42 ?  12   LEU   A HD13 1 
ATOM   198  H  HD21 . LEU   A 1 12  ? 8.545  -13.707 5.796   1.00 17.98 ?  12   LEU   A HD21 1 
ATOM   199  H  HD22 . LEU   A 1 12  ? 8.788  -15.214 5.356   1.00 17.98 ?  12   LEU   A HD22 1 
ATOM   200  H  HD23 . LEU   A 1 12  ? 8.450  -14.873 6.870   1.00 17.98 ?  12   LEU   A HD23 1 
ATOM   201  N  N    . THR   A 1 13  ? 12.294 -18.278 7.976   1.00 11.96 ?  13   THR   A N    1 
ATOM   202  C  CA   . THR   A 1 13  ? 12.986 -19.554 7.876   1.00 12.34 ?  13   THR   A CA   1 
ATOM   203  C  C    . THR   A 1 13  ? 13.757 -19.775 9.169   1.00 12.36 ?  13   THR   A C    1 
ATOM   204  O  O    . THR   A 1 13  ? 13.661 -18.994 10.122  1.00 12.40 ?  13   THR   A O    1 
ATOM   205  C  CB   . THR   A 1 13  ? 13.951 -19.590 6.685   1.00 13.02 ?  13   THR   A CB   1 
ATOM   206  O  OG1  . THR   A 1 13  ? 15.012 -18.670 6.935   1.00 13.10 ?  13   THR   A OG1  1 
ATOM   207  C  CG2  . THR   A 1 13  ? 13.266 -19.230 5.370   1.00 13.95 ?  13   THR   A CG2  1 
ATOM   208  H  H    . THR   A 1 13  ? 12.754 -17.669 8.372   1.00 14.38 ?  13   THR   A H    1 
ATOM   209  H  HA   . THR   A 1 13  ? 12.341 -20.268 7.764   1.00 14.83 ?  13   THR   A HA   1 
ATOM   210  H  HB   . THR   A 1 13  ? 14.326 -20.478 6.593   1.00 15.65 ?  13   THR   A HB   1 
ATOM   211  H  HG1  . THR   A 1 13  ? 15.556 -18.667 6.279   1.00 15.75 ?  13   THR   A HG1  1 
ATOM   212  H  HG21 . THR   A 1 13  ? 13.891 -19.344 4.629   1.00 16.76 ?  13   THR   A HG21 1 
ATOM   213  H  HG22 . THR   A 1 13  ? 12.506 -19.812 5.226   1.00 16.76 ?  13   THR   A HG22 1 
ATOM   214  H  HG23 . THR   A 1 13  ? 12.968 -18.311 5.388   1.00 16.76 ?  13   THR   A HG23 1 
ATOM   215  N  N    . ASP   A 1 14  ? 14.562 -20.836 9.182   1.00 12.72 ?  14   ASP   A N    1 
ATOM   216  C  CA   . ASP   A 1 14  ? 15.413 -21.106 10.329  1.00 13.61 ?  14   ASP   A CA   1 
ATOM   217  C  C    . ASP   A 1 14  ? 16.241 -19.884 10.724  1.00 13.37 ?  14   ASP   A C    1 
ATOM   218  O  O    . ASP   A 1 14  ? 16.476 -19.652 11.914  1.00 14.26 ?  14   ASP   A O    1 
ATOM   219  C  CB   . ASP   A 1 14  ? 16.342 -22.270 10.015  1.00 16.20 ?  14   ASP   A CB   1 
ATOM   220  C  CG   . ASP   A 1 14  ? 17.234 -22.603 11.174  1.00 19.78 ?  14   ASP   A CG   1 
ATOM   221  O  OD1  . ASP   A 1 14  ? 16.696 -23.016 12.225  1.00 21.36 ?  14   ASP   A OD1  1 
ATOM   222  O  OD2  . ASP   A 1 14  ? 18.458 -22.432 11.039  1.00 22.66 -1 14   ASP   A OD2  1 
ATOM   223  H  H    . ASP   A 1 14  ? 14.636 -21.404 8.538   1.00 15.29 ?  14   ASP   A H    1 
ATOM   224  H  HA   . ASP   A 1 14  ? 14.859 -21.356 11.083  1.00 16.35 ?  14   ASP   A HA   1 
ATOM   225  H  HB2  . ASP   A 1 14  ? 15.804 -23.056 9.803   1.00 19.46 ?  14   ASP   A HB2  1 
ATOM   226  H  HB3  . ASP   A 1 14  ? 16.896 -22.041 9.251   1.00 19.46 ?  14   ASP   A HB3  1 
ATOM   227  N  N    . ASN   A 1 15  ? 16.689 -19.086 9.745   1.00 12.30 ?  15   ASN   A N    1 
ATOM   228  C  CA   . ASN   A 1 15  ? 17.676 -18.046 10.007  1.00 12.44 ?  15   ASN   A CA   1 
ATOM   229  C  C    . ASN   A 1 15  ? 17.302 -16.658 9.507   1.00 12.74 ?  15   ASN   A C    1 
ATOM   230  O  O    . ASN   A 1 15  ? 18.073 -15.726 9.743   1.00 14.20 ?  15   ASN   A O    1 
ATOM   231  C  CB   . ASN   A 1 15  ? 19.047 -18.443 9.424   1.00 12.11 ?  15   ASN   A CB   1 
ATOM   232  C  CG   . ASN   A 1 15  ? 19.032 -18.534 7.918   1.00 12.51 ?  15   ASN   A CG   1 
ATOM   233  O  OD1  . ASN   A 1 15  ? 18.319 -19.359 7.338   1.00 13.69 ?  15   ASN   A OD1  1 
ATOM   234  N  ND2  . ASN   A 1 15  ? 19.813 -17.674 7.266   1.00 12.60 ?  15   ASN   A ND2  1 
ATOM   235  H  H    . ASN   A 1 15  ? 16.428 -19.127 8.934   1.00 14.78 ?  15   ASN   A H    1 
ATOM   236  H  HA   . ASN   A 1 15  ? 17.799 -17.975 10.967  1.00 14.94 ?  15   ASN   A HA   1 
ATOM   237  H  HB2  . ASN   A 1 15  ? 19.711 -17.774 9.683   1.00 14.55 ?  15   ASN   A HB2  1 
ATOM   238  H  HB3  . ASN   A 1 15  ? 19.309 -19.310 9.773   1.00 14.55 ?  15   ASN   A HB3  1 
ATOM   239  H  HD21 . ASN   A 1 15  ? 19.841 -17.675 6.406   1.00 15.15 ?  15   ASN   A HD21 1 
ATOM   240  H  HD22 . ASN   A 1 15  ? 20.296 -17.099 7.702   1.00 15.15 ?  15   ASN   A HD22 1 
ATOM   241  N  N    . VAL   A 1 16  ? 16.162 -16.486 8.838   1.00 12.29 ?  16   VAL   A N    1 
ATOM   242  C  CA   . VAL   A 1 16  ? 15.766 -15.206 8.263   1.00 11.76 ?  16   VAL   A CA   1 
ATOM   243  C  C    . VAL   A 1 16  ? 14.488 -14.723 8.932   1.00 11.39 ?  16   VAL   A C    1 
ATOM   244  O  O    . VAL   A 1 16  ? 13.499 -15.461 9.019   1.00 11.98 ?  16   VAL   A O    1 
ATOM   245  C  CB   . VAL   A 1 16  ? 15.591 -15.289 6.737   1.00 12.26 ?  16   VAL   A CB   1 
ATOM   246  C  CG1  . VAL   A 1 16  ? 15.156 -13.934 6.170   1.00 13.37 ?  16   VAL   A CG1  1 
ATOM   247  C  CG2  . VAL   A 1 16  ? 16.871 -15.763 6.072   1.00 13.29 ?  16   VAL   A CG2  1 
ATOM   248  H  H    . VAL   A 1 16  ? 15.586 -17.114 8.715   1.00 14.78 ?  16   VAL   A H    1 
ATOM   249  H  HA   . VAL   A 1 16  ? 16.464 -14.557 8.445   1.00 14.14 ?  16   VAL   A HA   1 
ATOM   250  H  HB   . VAL   A 1 16  ? 14.901 -15.933 6.536   1.00 14.74 ?  16   VAL   A HB   1 
ATOM   251  H  HG11 . VAL   A 1 16  ? 15.245 -13.955 5.204   1.00 16.07 ?  16   VAL   A HG11 1 
ATOM   252  H  HG12 . VAL   A 1 16  ? 14.228 -13.776 6.409   1.00 16.07 ?  16   VAL   A HG12 1 
ATOM   253  H  HG13 . VAL   A 1 16  ? 15.718 -13.238 6.539   1.00 16.07 ?  16   VAL   A HG13 1 
ATOM   254  H  HG21 . VAL   A 1 16  ? 16.760 -15.732 5.109   1.00 15.97 ?  16   VAL   A HG21 1 
ATOM   255  H  HG22 . VAL   A 1 16  ? 17.603 -15.180 6.336   1.00 15.97 ?  16   VAL   A HG22 1 
ATOM   256  H  HG23 . VAL   A 1 16  ? 17.059 -16.671 6.355   1.00 15.97 ?  16   VAL   A HG23 1 
ATOM   257  N  N    . TYR   A 1 17  ? 14.515 -13.463 9.364   1.00 11.22 ?  17   TYR   A N    1 
ATOM   258  C  CA   . TYR   A 1 17  ? 13.438 -12.780 10.067  1.00 11.04 ?  17   TYR   A CA   1 
ATOM   259  C  C    . TYR   A 1 17  ? 13.162 -11.457 9.363   1.00 11.43 ?  17   TYR   A C    1 
ATOM   260  O  O    . TYR   A 1 17  ? 14.067 -10.882 8.749   1.00 11.87 ?  17   TYR   A O    1 
ATOM   261  C  CB   . TYR   A 1 17  ? 13.877 -12.510 11.507  1.00 11.79 ?  17   TYR   A CB   1 
ATOM   262  C  CG   . TYR   A 1 17  ? 14.093 -13.772 12.312  1.00 12.42 ?  17   TYR   A CG   1 
ATOM   263  C  CD1  . TYR   A 1 17  ? 15.274 -14.508 12.210  1.00 13.33 ?  17   TYR   A CD1  1 
ATOM   264  C  CD2  . TYR   A 1 17  ? 13.106 -14.239 13.163  1.00 12.90 ?  17   TYR   A CD2  1 
ATOM   265  C  CE1  . TYR   A 1 17  ? 15.455 -15.684 12.939  1.00 13.99 ?  17   TYR   A CE1  1 
ATOM   266  C  CE2  . TYR   A 1 17  ? 13.281 -15.408 13.896  1.00 13.77 ?  17   TYR   A CE2  1 
ATOM   267  C  CZ   . TYR   A 1 17  ? 14.453 -16.127 13.787  1.00 14.12 ?  17   TYR   A CZ   1 
ATOM   268  O  OH   . TYR   A 1 17  ? 14.617 -17.282 14.522  1.00 14.87 ?  17   TYR   A OH   1 
ATOM   269  H  H    . TYR   A 1 17  ? 15.201 -12.951 9.240   1.00 13.49 ?  17   TYR   A H    1 
ATOM   270  H  HA   . TYR   A 1 17  ? 12.635 -13.329 10.057  1.00 13.28 ?  17   TYR   A HA   1 
ATOM   271  H  HB2  . TYR   A 1 17  ? 14.709 -12.019 11.486  1.00 14.17 ?  17   TYR   A HB2  1 
ATOM   272  H  HB3  . TYR   A 1 17  ? 13.191 -11.990 11.941  1.00 14.17 ?  17   TYR   A HB3  1 
ATOM   273  H  HD1  . TYR   A 1 17  ? 15.950 -14.215 11.634  1.00 16.02 ?  17   TYR   A HD1  1 
ATOM   274  H  HD2  . TYR   A 1 17  ? 12.309 -13.770 13.242  1.00 15.51 ?  17   TYR   A HD2  1 
ATOM   275  H  HE1  . TYR   A 1 17  ? 16.259 -16.159 12.862  1.00 16.81 ?  17   TYR   A HE1  1 
ATOM   276  H  HE2  . TYR   A 1 17  ? 12.612 -15.704 14.466  1.00 16.55 ?  17   TYR   A HE2  1 
ATOM   277  H  HH   . TYR   A 1 17  ? 13.888 -17.487 14.882  1.00 17.87 ?  17   TYR   A HH   1 
ATOM   278  N  N    A ILE   A 1 18  ? 11.906 -11.007 9.374   0.50 11.32 ?  18   ILE   A N    1 
ATOM   279  N  N    B ILE   A 1 18  ? 11.944 -10.918 9.538   0.50 11.21 ?  18   ILE   A N    1 
ATOM   280  C  CA   A ILE   A 1 18  ? 11.517 -9.843  8.579   0.50 11.09 ?  18   ILE   A CA   1 
ATOM   281  C  CA   B ILE   A 1 18  ? 11.543 -9.684  8.862   0.50 10.69 ?  18   ILE   A CA   1 
ATOM   282  C  C    A ILE   A 1 18  ? 10.524 -8.985  9.355   0.50 11.40 ?  18   ILE   A C    1 
ATOM   283  C  C    B ILE   A 1 18  ? 10.633 -8.834  9.745   0.50 10.52 ?  18   ILE   A C    1 
ATOM   284  O  O    A ILE   A 1 18  ? 9.682  -9.505  10.094  0.50 11.50 ?  18   ILE   A O    1 
ATOM   285  O  O    B ILE   A 1 18  ? 9.810  -9.351  10.509  0.50 11.14 ?  18   ILE   A O    1 
ATOM   286  C  CB   A ILE   A 1 18  ? 10.982 -10.274 7.194   0.50 10.66 ?  18   ILE   A CB   1 
ATOM   287  C  CB   B ILE   A 1 18  ? 10.885 -9.993  7.499   0.50 10.81 ?  18   ILE   A CB   1 
ATOM   288  C  CG1  A ILE   A 1 18  ? 10.892 -9.078  6.248   0.50 10.02 ?  18   ILE   A CG1  1 
ATOM   289  C  CG1  B ILE   A 1 18  ? 10.771 -8.731  6.646   0.50 11.90 ?  18   ILE   A CG1  1 
ATOM   290  C  CG2  A ILE   A 1 18  ? 9.651  -11.008 7.320   0.50 10.43 ?  18   ILE   A CG2  1 
ATOM   291  C  CG2  B ILE   A 1 18  ? 9.527  -10.649 7.691   0.50 11.14 ?  18   ILE   A CG2  1 
ATOM   292  C  CD1  A ILE   A 1 18  ? 10.675 -9.483  4.820   0.50 10.97 ?  18   ILE   A CD1  1 
ATOM   293  C  CD1  B ILE   A 1 18  ? 10.382 -9.016  5.213   0.50 13.20 ?  18   ILE   A CD1  1 
ATOM   294  H  H    A ILE   A 1 18  ? 11.265 -11.373 9.818   0.50 13.60 ?  18   ILE   A H    1 
ATOM   295  H  H    B ILE   A 1 18  ? 11.337 -11.254 10.048  0.50 13.47 ?  18   ILE   A H    1 
ATOM   296  H  HA   A ILE   A 1 18  ? 12.310 -9.312  8.421   0.50 13.33 ?  18   ILE   A HA   1 
ATOM   297  H  HA   B ILE   A 1 18  ? 12.340 -9.162  8.690   0.50 12.86 ?  18   ILE   A HA   1 
ATOM   298  H  HB   A ILE   A 1 18  ? 11.619 -10.901 6.808   0.50 12.82 ?  18   ILE   A HB   1 
ATOM   299  H  HB   B ILE   A 1 18  ? 11.457 -10.616 7.034   0.50 13.00 ?  18   ILE   A HB   1 
ATOM   300  H  HG12 A ILE   A 1 18  ? 10.149 -8.520  6.516   0.50 12.05 ?  18   ILE   A HG12 1 
ATOM   301  H  HG12 B ILE   A 1 18  ? 10.095 -8.150  7.028   0.50 14.31 ?  18   ILE   A HG12 1 
ATOM   302  H  HG13 A ILE   A 1 18  ? 11.721 -8.579  6.292   0.50 12.05 ?  18   ILE   A HG13 1 
ATOM   303  H  HG13 B ILE   A 1 18  ? 11.629 -8.278  6.636   0.50 14.31 ?  18   ILE   A HG13 1 
ATOM   304  H  HG21 A ILE   A 1 18  ? 9.415  -11.390 6.456   0.50 12.54 ?  18   ILE   A HG21 1 
ATOM   305  H  HG21 B ILE   A 1 18  ? 9.231  -11.007 6.838   0.50 13.39 ?  18   ILE   A HG21 1 
ATOM   306  H  HG22 A ILE   A 1 18  ? 9.742  -11.716 7.976   0.50 12.54 ?  18   ILE   A HG22 1 
ATOM   307  H  HG22 B ILE   A 1 18  ? 9.611  -11.364 8.338   0.50 13.39 ?  18   ILE   A HG22 1 
ATOM   308  H  HG23 A ILE   A 1 18  ? 8.968  -10.381 7.599   0.50 12.54 ?  18   ILE   A HG23 1 
ATOM   309  H  HG23 B ILE   A 1 18  ? 8.894  -9.986  8.008   0.50 13.39 ?  18   ILE   A HG23 1 
ATOM   310  H  HD11 A ILE   A 1 18  ? 10.704 -8.688  4.262   0.50 13.19 ?  18   ILE   A HD11 1 
ATOM   311  H  HD11 B ILE   A 1 18  ? 10.390 -8.184  4.713   0.50 15.87 ?  18   ILE   A HD11 1 
ATOM   312  H  HD12 A ILE   A 1 18  ? 11.374 -10.099 4.556   0.50 13.19 ?  18   ILE   A HD12 1 
ATOM   313  H  HD12 B ILE   A 1 18  ? 11.021 -9.637  4.829   0.50 15.87 ?  18   ILE   A HD12 1 
ATOM   314  H  HD13 A ILE   A 1 18  ? 9.807  -9.909  4.740   0.50 13.19 ?  18   ILE   A HD13 1 
ATOM   315  H  HD13 B ILE   A 1 18  ? 9.493  -9.402  5.196   0.50 15.87 ?  18   ILE   A HD13 1 
ATOM   316  N  N    A LYS   A 1 19  ? 10.620 -7.667  9.177   0.50 11.05 ?  19   LYS   A N    1 
ATOM   317  N  N    B LYS   A 1 19  ? 10.772 -7.510  9.614   0.50 10.52 ?  19   LYS   A N    1 
ATOM   318  C  CA   A LYS   A 1 19  ? 9.801  -6.713  9.913   0.50 11.65 ?  19   LYS   A CA   1 
ATOM   319  C  CA   B LYS   A 1 19  ? 9.997  -6.561  10.403  0.50 12.07 ?  19   LYS   A CA   1 
ATOM   320  C  C    A LYS   A 1 19  ? 9.631  -5.451  9.077   0.50 11.57 ?  19   LYS   A C    1 
ATOM   321  C  C    B LYS   A 1 19  ? 9.715  -5.326  9.564   0.50 13.00 ?  19   LYS   A C    1 
ATOM   322  O  O    A LYS   A 1 19  ? 10.535 -5.060  8.332   0.50 11.10 ?  19   LYS   A O    1 
ATOM   323  O  O    B LYS   A 1 19  ? 10.561 -4.891  8.779   0.50 13.10 ?  19   LYS   A O    1 
ATOM   324  C  CB   A LYS   A 1 19  ? 10.496 -6.353  11.234  0.50 12.62 ?  19   LYS   A CB   1 
ATOM   325  C  CB   B LYS   A 1 19  ? 10.753 -6.152  11.673  0.50 13.05 ?  19   LYS   A CB   1 
ATOM   326  C  CG   A LYS   A 1 19  ? 9.757  -5.396  12.162  0.50 14.19 ?  19   LYS   A CG   1 
ATOM   327  C  CG   B LYS   A 1 19  ? 9.997  -5.265  12.642  0.50 14.80 ?  19   LYS   A CG   1 
ATOM   328  C  CD   A LYS   A 1 19  ? 10.634 -5.105  13.382  0.50 15.49 ?  19   LYS   A CD   1 
ATOM   329  C  CD   B LYS   A 1 19  ? 10.905 -4.890  13.803  0.50 15.98 ?  19   LYS   A CD   1 
ATOM   330  C  CE   A LYS   A 1 19  ? 9.977  -4.174  14.389  0.50 16.43 ?  19   LYS   A CE   1 
ATOM   331  C  CE   B LYS   A 1 19  ? 10.185 -4.052  14.840  0.50 17.28 ?  19   LYS   A CE   1 
ATOM   332  N  NZ   A LYS   A 1 19  ? 10.888 -3.914  15.547  0.50 16.76 ?  19   LYS   A NZ   1 
ATOM   333  N  NZ   B LYS   A 1 19  ? 11.067 -3.784  16.007  0.50 18.15 ?  19   LYS   A NZ   1 
ATOM   334  H  H    A LYS   A 1 19  ? 11.174 -7.310  8.630   0.50 13.29 ?  19   LYS   A H    1 
ATOM   335  H  H    B LYS   A 1 19  ? 11.321 -7.127  9.060   0.50 12.65 ?  19   LYS   A H    1 
ATOM   336  H  HA   A LYS   A 1 19  ? 8.933  -7.111  10.103  0.50 14.00 ?  19   LYS   A HA   1 
ATOM   337  H  HA   B LYS   A 1 19  ? 9.153  -6.954  10.656  0.50 14.51 ?  19   LYS   A HA   1 
ATOM   338  H  HB2  A LYS   A 1 19  ? 10.647 -7.174  11.729  0.50 15.17 ?  19   LYS   A HB2  1 
ATOM   339  H  HB2  B LYS   A 1 19  ? 10.987 -6.957  12.158  0.50 15.68 ?  19   LYS   A HB2  1 
ATOM   340  H  HB3  A LYS   A 1 19  ? 11.348 -5.948  11.019  0.50 15.17 ?  19   LYS   A HB3  1 
ATOM   341  H  HB3  B LYS   A 1 19  ? 11.562 -5.679  11.419  0.50 15.68 ?  19   LYS   A HB3  1 
ATOM   342  H  HG2  A LYS   A 1 19  ? 9.580  -4.562  11.701  0.50 17.05 ?  19   LYS   A HG2  1 
ATOM   343  H  HG2  B LYS   A 1 19  ? 9.719  -4.453  12.193  0.50 17.79 ?  19   LYS   A HG2  1 
ATOM   344  H  HG3  A LYS   A 1 19  ? 8.930  -5.803  12.465  0.50 17.05 ?  19   LYS   A HG3  1 
ATOM   345  H  HG3  B LYS   A 1 19  ? 9.230  -5.745  12.991  0.50 17.79 ?  19   LYS   A HG3  1 
ATOM   346  H  HD2  A LYS   A 1 19  ? 10.833 -5.939  13.838  0.50 18.61 ?  19   LYS   A HD2  1 
ATOM   347  H  HD2  B LYS   A 1 19  ? 11.218 -5.703  14.234  0.50 19.20 ?  19   LYS   A HD2  1 
ATOM   348  H  HD3  A LYS   A 1 19  ? 11.460 -4.688  13.088  0.50 18.61 ?  19   LYS   A HD3  1 
ATOM   349  H  HD3  B LYS   A 1 19  ? 11.658 -4.381  13.466  0.50 19.20 ?  19   LYS   A HD3  1 
ATOM   350  H  HE2  A LYS   A 1 19  ? 9.778  -3.324  13.965  0.50 19.73 ?  19   LYS   A HE2  1 
ATOM   351  H  HE2  B LYS   A 1 19  ? 9.930  -3.204  14.444  0.50 20.76 ?  19   LYS   A HE2  1 
ATOM   352  H  HE3  A LYS   A 1 19  ? 9.165  -4.580  14.729  0.50 19.73 ?  19   LYS   A HE3  1 
ATOM   353  H  HE3  B LYS   A 1 19  ? 9.399  -4.530  15.149  0.50 20.76 ?  19   LYS   A HE3  1 
ATOM   354  H  HZ1  A LYS   A 1 19  ? 10.493 -3.373  16.135  0.50 20.14 ?  19   LYS   A HZ1  1 
ATOM   355  H  HZ1  B LYS   A 1 19  ? 10.629 -3.301  16.612  0.50 21.80 ?  19   LYS   A HZ1  1 
ATOM   356  H  HZ2  A LYS   A 1 19  ? 11.093 -4.680  15.953  0.50 20.14 ?  19   LYS   A HZ2  1 
ATOM   357  H  HZ2  B LYS   A 1 19  ? 11.320 -4.553  16.377  0.50 21.80 ?  19   LYS   A HZ2  1 
ATOM   358  H  HZ3  A LYS   A 1 19  ? 11.640 -3.529  15.265  0.50 20.14 ?  19   LYS   A HZ3  1 
ATOM   359  H  HZ3  B LYS   A 1 19  ? 11.789 -3.337  15.745  0.50 21.80 ?  19   LYS   A HZ3  1 
ATOM   360  N  N    A ASN   A 1 20  ? 8.469  -4.810  9.208   0.50 12.41 ?  20   ASN   A N    1 
ATOM   361  N  N    B ASN   A 1 20  ? 8.518  -4.771  9.736   0.50 14.26 ?  20   ASN   A N    1 
ATOM   362  C  CA   A ASN   A 1 20  ? 8.277  -3.472  8.651   0.50 13.63 ?  20   ASN   A CA   1 
ATOM   363  C  CA   B ASN   A 1 20  ? 8.123  -3.524  9.089   0.50 15.51 ?  20   ASN   A CA   1 
ATOM   364  C  C    A ASN   A 1 20  ? 8.911  -2.481  9.620   0.50 14.21 ?  20   ASN   A C    1 
ATOM   365  C  C    B ASN   A 1 20  ? 8.713  -2.371  9.890   0.50 16.17 ?  20   ASN   A C    1 
ATOM   366  O  O    A ASN   A 1 20  ? 8.421  -2.293  10.738  0.50 14.52 ?  20   ASN   A O    1 
ATOM   367  O  O    B ASN   A 1 20  ? 8.096  -1.856  10.825  0.50 16.98 ?  20   ASN   A O    1 
ATOM   368  C  CB   A ASN   A 1 20  ? 6.791  -3.184  8.432   0.50 14.52 ?  20   ASN   A CB   1 
ATOM   369  C  CB   B ASN   A 1 20  ? 6.602  -3.438  9.025   0.50 16.60 ?  20   ASN   A CB   1 
ATOM   370  C  CG   A ASN   A 1 20  ? 6.506  -1.716  8.097   0.50 16.14 ?  20   ASN   A CG   1 
ATOM   371  C  CG   B ASN   A 1 20  ? 6.102  -2.205  8.288   0.50 17.92 ?  20   ASN   A CG   1 
ATOM   372  O  OD1  A ASN   A 1 20  ? 5.582  -1.116  8.648   0.50 18.19 ?  20   ASN   A OD1  1 
ATOM   373  O  OD1  B ASN   A 1 20  ? 4.959  -1.790  8.466   0.50 18.87 ?  20   ASN   A OD1  1 
ATOM   374  N  ND2  A ASN   A 1 20  ? 7.295  -1.140  7.196   0.50 16.45 ?  20   ASN   A ND2  1 
ATOM   375  N  ND2  B ASN   A 1 20  ? 6.950  -1.614  7.463   0.50 18.67 ?  20   ASN   A ND2  1 
ATOM   376  H  H    A ASN   A 1 20  ? 7.780  -5.124  9.623   0.50 14.91 ?  20   ASN   A H    1 
ATOM   377  H  H    B ASN   A 1 20  ? 7.900  -5.115  10.216  0.50 17.14 ?  20   ASN   A H    1 
ATOM   378  H  HA   A ASN   A 1 20  ? 8.729  -3.412  7.797   0.50 16.38 ?  20   ASN   A HA   1 
ATOM   379  H  HA   B ASN   A 1 20  ? 8.483  -3.511  8.194   0.50 18.64 ?  20   ASN   A HA   1 
ATOM   380  H  HB2  A ASN   A 1 20  ? 6.469  -3.722  7.691   0.50 17.45 ?  20   ASN   A HB2  1 
ATOM   381  H  HB2  B ASN   A 1 20  ? 6.266  -4.223  8.570   0.50 19.95 ?  20   ASN   A HB2  1 
ATOM   382  H  HB3  A ASN   A 1 20  ? 6.302  -3.410  9.238   0.50 17.45 ?  20   ASN   A HB3  1 
ATOM   383  H  HB3  B ASN   A 1 20  ? 6.256  -3.409  9.935   0.50 19.95 ?  20   ASN   A HB3  1 
ATOM   384  H  HD21 A ASN   A 1 20  ? 7.166  -0.319  6.976   0.50 19.76 ?  20   ASN   A HD21 1 
ATOM   385  H  HD21 B ASN   A 1 20  ? 6.699  -0.919  7.038   0.50 22.43 ?  20   ASN   A HD21 1 
ATOM   386  H  HD22 A ASN   A 1 20  ? 7.928  -1.591  6.829   0.50 19.76 ?  20   ASN   A HD22 1 
ATOM   387  H  HD22 B ASN   A 1 20  ? 7.746  -1.920  7.353   0.50 22.43 ?  20   ASN   A HD22 1 
ATOM   388  N  N    A ALA   A 1 21  ? 10.028 -1.875  9.222   0.50 14.39 ?  21   ALA   A N    1 
ATOM   389  N  N    B ALA   A 1 21  ? 9.921  -1.952  9.515   0.50 15.90 ?  21   ALA   A N    1 
ATOM   390  C  CA   A ALA   A 1 21  ? 10.726 -0.983  10.136  0.50 14.77 ?  21   ALA   A CA   1 
ATOM   391  C  CA   B ALA   A 1 21  ? 10.618 -0.914  10.261  0.50 15.50 ?  21   ALA   A CA   1 
ATOM   392  C  C    A ALA   A 1 21  ? 11.694 -0.093  9.370   0.50 14.98 ?  21   ALA   A C    1 
ATOM   393  C  C    B ALA   A 1 21  ? 11.670 -0.258  9.378   0.50 13.86 ?  21   ALA   A C    1 
ATOM   394  O  O    A ALA   A 1 21  ? 12.156 -0.442  8.280   0.50 15.48 ?  21   ALA   A O    1 
ATOM   395  O  O    B ALA   A 1 21  ? 12.173 -0.864  8.428   0.50 13.88 ?  21   ALA   A O    1 
ATOM   396  C  CB   A ALA   A 1 21  ? 11.484 -1.771  11.208  0.50 15.43 ?  21   ALA   A CB   1 
ATOM   397  C  CB   B ALA   A 1 21  ? 11.272 -1.473  11.531  0.50 16.96 ?  21   ALA   A CB   1 
ATOM   398  H  H    A ALA   A 1 21  ? 10.391 -1.967  8.450   0.50 17.29 ?  21   ALA   A H    1 
ATOM   399  H  H    B ALA   A 1 21  ? 10.349 -2.240  8.826   0.50 19.11 ?  21   ALA   A H    1 
ATOM   400  H  HA   A ALA   A 1 21  ? 10.074 -0.414  10.580  0.50 17.74 ?  21   ALA   A HA   1 
ATOM   401  H  HA   B ALA   A 1 21  ? 9.979  -0.233  10.529  0.50 18.62 ?  21   ALA   A HA   1 
ATOM   402  H  HB1  A ALA   A 1 21  ? 11.907 -1.143  11.812  0.50 18.54 ?  21   ALA   A HB1  1 
ATOM   403  H  HB1  B ALA   A 1 21  ? 11.719 -0.751  12.002  0.50 20.38 ?  21   ALA   A HB1  1 
ATOM   404  H  HB2  A ALA   A 1 21  ? 10.851 -2.323  11.695  0.50 18.54 ?  21   ALA   A HB2  1 
ATOM   405  H  HB2  B ALA   A 1 21  ? 10.585 -1.860  12.098  0.50 20.38 ?  21   ALA   A HB2  1 
ATOM   406  H  HB3  A ALA   A 1 21  ? 12.148 -2.326  10.778  0.50 18.54 ?  21   ALA   A HB3  1 
ATOM   407  H  HB3  B ALA   A 1 21  ? 11.916 -2.153  11.282  0.50 20.38 ?  21   ALA   A HB3  1 
ATOM   408  N  N    A ASP   A 1 22  ? 11.981 1.066   9.963   0.50 15.15 ?  22   ASP   A N    1 
ATOM   409  N  N    B ASP   A 1 22  ? 11.959 1.004   9.694   0.50 12.84 ?  22   ASP   A N    1 
ATOM   410  C  CA   A ASP   A 1 22  ? 13.017 1.969   9.478   0.50 15.24 ?  22   ASP   A CA   1 
ATOM   411  C  CA   B ASP   A 1 22  ? 13.092 1.719   9.120   0.50 12.55 ?  22   ASP   A CA   1 
ATOM   412  C  C    A ASP   A 1 22  ? 14.355 1.506   10.042  0.50 14.21 ?  22   ASP   A C    1 
ATOM   413  C  C    B ASP   A 1 22  ? 14.381 1.170   9.725   0.50 11.11 ?  22   ASP   A C    1 
ATOM   414  O  O    A ASP   A 1 22  ? 14.559 1.527   11.261  0.50 14.57 ?  22   ASP   A O    1 
ATOM   415  O  O    B ASP   A 1 22  ? 14.525 1.119   10.951  0.50 11.12 ?  22   ASP   A O    1 
ATOM   416  C  CB   A ASP   A 1 22  ? 12.701 3.389   9.946   0.50 16.47 ?  22   ASP   A CB   1 
ATOM   417  C  CB   B ASP   A 1 22  ? 12.942 3.203   9.474   0.50 14.06 ?  22   ASP   A CB   1 
ATOM   418  C  CG   A ASP   A 1 22  ? 13.751 4.408   9.521   0.50 17.89 ?  22   ASP   A CG   1 
ATOM   419  C  CG   B ASP   A 1 22  ? 13.973 4.092   8.795   0.50 15.23 ?  22   ASP   A CG   1 
ATOM   420  O  OD1  A ASP   A 1 22  ? 14.769 4.028   8.904   0.50 18.18 ?  22   ASP   A OD1  1 
ATOM   421  O  OD1  B ASP   A 1 22  ? 15.050 3.596   8.403   0.50 13.88 ?  22   ASP   A OD1  1 
ATOM   422  O  OD2  A ASP   A 1 22  ? 13.550 5.608   9.807   0.50 19.25 -1 22   ASP   A OD2  1 
ATOM   423  O  OD2  B ASP   A 1 22  ? 13.707 5.305   8.657   0.50 17.77 -1 22   ASP   A OD2  1 
ATOM   424  H  H    A ASP   A 1 22  ? 11.568 1.361   10.661  0.50 18.20 ?  22   ASP   A H    1 
ATOM   425  H  H    B ASP   A 1 22  ? 11.487 1.478   10.238  0.50 15.43 ?  22   ASP   A H    1 
ATOM   426  H  HA   A ASP   A 1 22  ? 13.051 1.953   8.507   0.50 18.31 ?  22   ASP   A HA   1 
ATOM   427  H  HA   B ASP   A 1 22  ? 13.109 1.614   8.154   0.50 15.09 ?  22   ASP   A HA   1 
ATOM   428  H  HB2  A ASP   A 1 22  ? 11.853 3.667   9.568   0.50 19.79 ?  22   ASP   A HB2  1 
ATOM   429  H  HB2  B ASP   A 1 22  ? 12.067 3.508   9.195   0.50 16.89 ?  22   ASP   A HB2  1 
ATOM   430  H  HB3  A ASP   A 1 22  ? 12.643 3.392   10.917  0.50 19.79 ?  22   ASP   A HB3  1 
ATOM   431  H  HB3  B ASP   A 1 22  ? 13.034 3.299   10.438  0.50 16.89 ?  22   ASP   A HB3  1 
ATOM   432  N  N    A ILE   A 1 23  ? 15.262 1.080   9.158   0.50 13.30 ?  23   ILE   A N    1 
ATOM   433  N  N    B ILE   A 1 23  ? 15.316 0.743   8.868   0.50 11.02 ?  23   ILE   A N    1 
ATOM   434  C  CA   A ILE   A 1 23  ? 16.520 0.484   9.603   0.50 12.47 ?  23   ILE   A CA   1 
ATOM   435  C  CA   B ILE   A 1 23  ? 16.565 0.159   9.361   0.50 10.78 ?  23   ILE   A CA   1 
ATOM   436  C  C    A ILE   A 1 23  ? 17.306 1.447   10.479  0.50 12.51 ?  23   ILE   A C    1 
ATOM   437  C  C    B ILE   A 1 23  ? 17.302 1.130   10.271  0.50 11.18 ?  23   ILE   A C    1 
ATOM   438  O  O    A ILE   A 1 23  ? 18.040 1.021   11.380  0.50 12.97 ?  23   ILE   A O    1 
ATOM   439  O  O    B ILE   A 1 23  ? 17.971 0.712   11.225  0.50 11.44 ?  23   ILE   A O    1 
ATOM   440  C  CB   A ILE   A 1 23  ? 17.337 -0.024  8.396   0.50 12.02 ?  23   ILE   A CB   1 
ATOM   441  C  CB   B ILE   A 1 23  ? 17.455 -0.360  8.208   0.50 11.00 ?  23   ILE   A CB   1 
ATOM   442  C  CG1  A ILE   A 1 23  ? 18.482 -0.922  8.868   0.50 12.23 ?  23   ILE   A CG1  1 
ATOM   443  C  CG1  B ILE   A 1 23  ? 18.552 -1.271  8.770   0.50 11.41 ?  23   ILE   A CG1  1 
ATOM   444  C  CG2  A ILE   A 1 23  ? 17.851 1.140   7.554   0.50 12.16 ?  23   ILE   A CG2  1 
ATOM   445  C  CG2  B ILE   A 1 23  ? 18.052 0.792   7.402   0.50 10.98 ?  23   ILE   A CG2  1 
ATOM   446  C  CD1  A ILE   A 1 23  ? 19.195 -1.627  7.736   0.50 12.71 ?  23   ILE   A CD1  1 
ATOM   447  C  CD1  B ILE   A 1 23  ? 19.419 -1.926  7.712   0.50 11.88 ?  23   ILE   A CD1  1 
ATOM   448  H  H    A ILE   A 1 23  ? 15.170 1.128   8.306   0.50 15.99 ?  23   ILE   A H    1 
ATOM   449  H  H    B ILE   A 1 23  ? 15.249 0.770   8.017   0.50 13.24 ?  23   ILE   A H    1 
ATOM   450  H  HA   A ILE   A 1 23  ? 16.312 -0.285  10.151  0.50 14.99 ?  23   ILE   A HA   1 
ATOM   451  H  HA   B ILE   A 1 23  ? 16.334 -0.614  9.898   0.50 12.95 ?  23   ILE   A HA   1 
ATOM   452  H  HB   A ILE   A 1 23  ? 16.747 -0.558  7.841   0.50 14.45 ?  23   ILE   A HB   1 
ATOM   453  H  HB   B ILE   A 1 23  ? 16.903 -0.892  7.611   0.50 13.23 ?  23   ILE   A HB   1 
ATOM   454  H  HG12 A ILE   A 1 23  ? 19.134 -0.381  9.338   0.50 14.70 ?  23   ILE   A HG12 1 
ATOM   455  H  HG12 B ILE   A 1 23  ? 19.133 -0.746  9.341   0.50 13.71 ?  23   ILE   A HG12 1 
ATOM   456  H  HG13 A ILE   A 1 23  ? 18.125 -1.601  9.462   0.50 14.70 ?  23   ILE   A HG13 1 
ATOM   457  H  HG13 B ILE   A 1 23  ? 18.136 -1.979  9.288   0.50 13.71 ?  23   ILE   A HG13 1 
ATOM   458  H  HG21 A ILE   A 1 23  ? 18.197 0.793   6.715   0.50 14.61 ?  23   ILE   A HG21 1 
ATOM   459  H  HG21 B ILE   A 1 23  ? 18.444 0.437   6.586   0.50 13.20 ?  23   ILE   A HG21 1 
ATOM   460  H  HG22 A ILE   A 1 23  ? 17.117 1.750   7.378   0.50 14.61 ?  23   ILE   A HG22 1 
ATOM   461  H  HG22 B ILE   A 1 23  ? 17.348 1.419   7.182   0.50 13.20 ?  23   ILE   A HG22 1 
ATOM   462  H  HG23 A ILE   A 1 23  ? 18.553 1.597   8.038   0.50 14.61 ?  23   ILE   A HG23 1 
ATOM   463  H  HG23 B ILE   A 1 23  ? 18.735 1.229   7.932   0.50 13.20 ?  23   ILE   A HG23 1 
ATOM   464  H  HD11 A ILE   A 1 23  ? 19.851 -2.236  8.108   0.50 15.28 ?  23   ILE   A HD11 1 
ATOM   465  H  HD11 B ILE   A 1 23  ? 20.023 -2.552  8.143   0.50 14.28 ?  23   ILE   A HD11 1 
ATOM   466  H  HD12 A ILE   A 1 23  ? 18.543 -2.121  7.213   0.50 15.28 ?  23   ILE   A HD12 1 
ATOM   467  H  HD12 B ILE   A 1 23  ? 18.848 -2.397  7.085   0.50 14.28 ?  23   ILE   A HD12 1 
ATOM   468  H  HD13 A ILE   A 1 23  ? 19.634 -0.966  7.179   0.50 15.28 ?  23   ILE   A HD13 1 
ATOM   469  H  HD13 B ILE   A 1 23  ? 19.926 -1.242  7.251   0.50 14.28 ?  23   ILE   A HD13 1 
ATOM   470  N  N    A VAL   A 1 24  ? 17.162 2.753   10.245  0.50 12.85 ?  24   VAL   A N    1 
ATOM   471  N  N    B VAL   A 1 24  ? 17.192 2.433   10.002  0.50 11.73 ?  24   VAL   A N    1 
ATOM   472  C  CA   A VAL   A 1 24  ? 17.841 3.730   11.091  0.50 13.70 ?  24   VAL   A CA   1 
ATOM   473  C  CA   B VAL   A 1 24  ? 17.862 3.423   10.838  0.50 12.64 ?  24   VAL   A CA   1 
ATOM   474  C  C    A VAL   A 1 24  ? 17.326 3.640   12.520  0.50 14.07 ?  24   VAL   A C    1 
ATOM   475  C  C    B VAL   A 1 24  ? 17.272 3.424   12.243  0.50 13.24 ?  24   VAL   A C    1 
ATOM   476  O  O    A VAL   A 1 24  ? 18.102 3.519   13.477  0.50 14.62 ?  24   VAL   A O    1 
ATOM   477  O  O    B VAL   A 1 24  ? 18.002 3.499   13.238  0.50 14.01 ?  24   VAL   A O    1 
ATOM   478  C  CB   A VAL   A 1 24  ? 17.673 5.147   10.518  0.50 14.53 ?  24   VAL   A CB   1 
ATOM   479  C  CB   B VAL   A 1 24  ? 17.788 4.810   10.174  0.50 13.64 ?  24   VAL   A CB   1 
ATOM   480  C  CG1  A VAL   A 1 24  ? 18.130 6.184   11.534  0.50 15.11 ?  24   VAL   A CG1  1 
ATOM   481  C  CG1  B VAL   A 1 24  ? 18.451 5.854   11.051  0.50 15.13 ?  24   VAL   A CG1  1 
ATOM   482  C  CG2  A VAL   A 1 24  ? 18.444 5.288   9.218   0.50 15.08 ?  24   VAL   A CG2  1 
ATOM   483  C  CG2  B VAL   A 1 24  ? 18.433 4.768   8.795   0.50 14.13 ?  24   VAL   A CG2  1 
ATOM   484  H  H    A VAL   A 1 24  ? 16.680 3.094   9.616   0.50 15.45 ?  24   VAL   A H    1 
ATOM   485  H  H    B VAL   A 1 24  ? 16.735 2.762   9.353   0.50 14.10 ?  24   VAL   A H    1 
ATOM   486  H  HA   A VAL   A 1 24  ? 18.787 3.531   11.103  0.50 16.46 ?  24   VAL   A HA   1 
ATOM   487  H  HA   B VAL   A 1 24  ? 18.796 3.182   10.914  0.50 15.19 ?  24   VAL   A HA   1 
ATOM   488  H  HB   A VAL   A 1 24  ? 16.734 5.309   10.326  0.50 17.46 ?  24   VAL   A HB   1 
ATOM   489  H  HB   B VAL   A 1 24  ? 16.856 5.057   10.060  0.50 16.39 ?  24   VAL   A HB   1 
ATOM   490  H  HG11 A VAL   A 1 24  ? 18.302 7.020   11.074  0.50 18.16 ?  24   VAL   A HG11 1 
ATOM   491  H  HG11 B VAL   A 1 24  ? 18.567 6.666   10.535  0.50 18.17 ?  24   VAL   A HG11 1 
ATOM   492  H  HG12 A VAL   A 1 24  ? 17.433 6.309   12.196  0.50 18.16 ?  24   VAL   A HG12 1 
ATOM   493  H  HG12 B VAL   A 1 24  ? 17.883 6.029   11.818  0.50 18.17 ?  24   VAL   A HG12 1 
ATOM   494  H  HG13 A VAL   A 1 24  ? 18.943 5.868   11.958  0.50 18.16 ?  24   VAL   A HG13 1 
ATOM   495  H  HG13 B VAL   A 1 24  ? 19.312 5.519   11.342  0.50 18.17 ?  24   VAL   A HG13 1 
ATOM   496  H  HG21 A VAL   A 1 24  ? 18.205 6.127   8.795   0.50 18.12 ?  24   VAL   A HG21 1 
ATOM   497  H  HG21 B VAL   A 1 24  ? 18.484 5.668   8.443   0.50 16.98 ?  24   VAL   A HG21 1 
ATOM   498  H  HG22 A VAL   A 1 24  ? 19.395 5.279   9.414   0.50 18.12 ?  24   VAL   A HG22 1 
ATOM   499  H  HG22 B VAL   A 1 24  ? 19.325 4.393   8.877   0.50 16.98 ?  24   VAL   A HG22 1 
ATOM   500  H  HG23 A VAL   A 1 24  ? 18.219 4.548   8.633   0.50 18.12 ?  24   VAL   A HG23 1 
ATOM   501  H  HG23 B VAL   A 1 24  ? 17.896 4.211   8.209   0.50 16.98 ?  24   VAL   A HG23 1 
ATOM   502  N  N    A GLU   A 1 25  ? 16.003 3.704   12.685  0.50 14.53 ?  25   GLU   A N    1 
ATOM   503  N  N    B GLU   A 1 25  ? 15.944 3.332   12.349  0.50 13.77 ?  25   GLU   A N    1 
ATOM   504  C  CA   A GLU   A 1 25  ? 15.426 3.640   14.021  0.50 15.73 ?  25   GLU   A CA   1 
ATOM   505  C  CA   B GLU   A 1 25  ? 15.308 3.276   13.662  0.50 14.64 ?  25   GLU   A CA   1 
ATOM   506  C  C    A GLU   A 1 25  ? 15.653 2.281   14.666  0.50 14.26 ?  25   GLU   A C    1 
ATOM   507  C  C    B GLU   A 1 25  ? 15.592 1.948   14.359  0.50 14.32 ?  25   GLU   A C    1 
ATOM   508  O  O    A GLU   A 1 25  ? 15.847 2.204   15.885  0.50 14.64 ?  25   GLU   A O    1 
ATOM   509  O  O    B GLU   A 1 25  ? 15.840 1.920   15.569  0.50 14.87 ?  25   GLU   A O    1 
ATOM   510  C  CB   A GLU   A 1 25  ? 13.938 3.987   13.972  0.50 18.44 ?  25   GLU   A CB   1 
ATOM   511  C  CB   B GLU   A 1 25  ? 13.804 3.531   13.531  0.50 16.65 ?  25   GLU   A CB   1 
ATOM   512  C  CG   A GLU   A 1 25  ? 13.678 5.451   13.654  0.50 21.31 ?  25   GLU   A CG   1 
ATOM   513  C  CG   B GLU   A 1 25  ? 13.467 4.922   13.013  0.50 19.88 ?  25   GLU   A CG   1 
ATOM   514  C  CD   A GLU   A 1 25  ? 14.482 6.401   14.531  0.50 23.56 ?  25   GLU   A CD   1 
ATOM   515  C  CD   B GLU   A 1 25  ? 13.987 6.015   13.921  0.50 22.88 ?  25   GLU   A CD   1 
ATOM   516  O  OE1  A GLU   A 1 25  ? 14.552 6.168   15.756  0.50 24.08 ?  25   GLU   A OE1  1 
ATOM   517  O  OE1  B GLU   A 1 25  ? 13.962 5.820   15.156  0.50 24.14 ?  25   GLU   A OE1  1 
ATOM   518  O  OE2  A GLU   A 1 25  ? 15.060 7.367   13.989  0.50 24.64 -1 25   GLU   A OE2  1 
ATOM   519  O  OE2  B GLU   A 1 25  ? 14.427 7.061   13.401  0.50 24.06 -1 25   GLU   A OE2  1 
ATOM   520  H  H    A GLU   A 1 25  ? 15.429 3.789   12.047  0.50 17.45 ?  25   GLU   A H    1 
ATOM   521  H  H    B GLU   A 1 25  ? 15.399 3.301   11.685  0.50 16.54 ?  25   GLU   A H    1 
ATOM   522  H  HA   A GLU   A 1 25  ? 15.872 4.289   14.581  0.50 18.90 ?  25   GLU   A HA   1 
ATOM   523  H  HA   B GLU   A 1 25  ? 15.679 3.977   14.216  0.50 17.59 ?  25   GLU   A HA   1 
ATOM   524  H  HB2  A GLU   A 1 25  ? 13.509 3.451   13.281  0.50 22.15 ?  25   GLU   A HB2  1 
ATOM   525  H  HB2  B GLU   A 1 25  ? 13.426 2.890   12.913  0.50 20.01 ?  25   GLU   A HB2  1 
ATOM   526  H  HB3  A GLU   A 1 25  ? 13.537 3.792   14.833  0.50 22.15 ?  25   GLU   A HB3  1 
ATOM   527  H  HB3  B GLU   A 1 25  ? 13.391 3.435   14.403  0.50 20.01 ?  25   GLU   A HB3  1 
ATOM   528  H  HG2  A GLU   A 1 25  ? 13.926 5.618   12.734  0.50 25.59 ?  25   GLU   A HG2  1 
ATOM   529  H  HG2  B GLU   A 1 25  ? 13.863 5.044   12.136  0.50 23.88 ?  25   GLU   A HG2  1 
ATOM   530  H  HG3  A GLU   A 1 25  ? 12.736 5.636   13.790  0.50 25.59 ?  25   GLU   A HG3  1 
ATOM   531  H  HG3  B GLU   A 1 25  ? 12.504 5.022   12.960  0.50 23.88 ?  25   GLU   A HG3  1 
ATOM   532  N  N    A GLU   A 1 26  ? 15.644 1.207   13.874  0.50 13.98 ?  26   GLU   A N    1 
ATOM   533  N  N    B GLU   A 1 26  ? 15.571 0.839   13.614  0.50 14.11 ?  26   GLU   A N    1 
ATOM   534  C  CA   A GLU   A 1 26  ? 15.923 -0.117  14.423  0.50 13.92 ?  26   GLU   A CA   1 
ATOM   535  C  CA   B GLU   A 1 26  ? 15.956 -0.445  14.197  0.50 14.48 ?  26   GLU   A CA   1 
ATOM   536  C  C    A GLU   A 1 26  ? 17.343 -0.191  14.972  0.50 13.54 ?  26   GLU   A C    1 
ATOM   537  C  C    B GLU   A 1 26  ? 17.382 -0.394  14.728  0.50 13.44 ?  26   GLU   A C    1 
ATOM   538  O  O    A GLU   A 1 26  ? 17.564 -0.643  16.101  0.50 13.57 ?  26   GLU   A O    1 
ATOM   539  O  O    B GLU   A 1 26  ? 17.681 -0.947  15.792  0.50 13.55 ?  26   GLU   A O    1 
ATOM   540  C  CB   A GLU   A 1 26  ? 15.718 -1.186  13.349  0.50 15.07 ?  26   GLU   A CB   1 
ATOM   541  C  CB   B GLU   A 1 26  ? 15.828 -1.561  13.157  0.50 16.30 ?  26   GLU   A CB   1 
ATOM   542  C  CG   A GLU   A 1 26  ? 14.293 -1.646  13.158  0.50 17.90 ?  26   GLU   A CG   1 
ATOM   543  C  CG   B GLU   A 1 26  ? 14.444 -2.169  13.041  0.50 18.11 ?  26   GLU   A CG   1 
ATOM   544  C  CD   A GLU   A 1 26  ? 13.782 -2.474  14.312  0.50 19.25 ?  26   GLU   A CD   1 
ATOM   545  C  CD   B GLU   A 1 26  ? 13.969 -2.804  14.337  0.50 18.67 ?  26   GLU   A CD   1 
ATOM   546  O  OE1  A GLU   A 1 26  ? 14.520 -3.362  14.788  0.50 19.19 ?  26   GLU   A OE1  1 
ATOM   547  O  OE1  B GLU   A 1 26  ? 14.302 -3.980  14.625  0.50 18.46 ?  26   GLU   A OE1  1 
ATOM   548  O  OE2  A GLU   A 1 26  ? 12.641 -2.220  14.745  0.50 19.75 -1 26   GLU   A OE2  1 
ATOM   549  O  OE2  B GLU   A 1 26  ? 13.268 -2.108  15.082  0.50 18.91 -1 26   GLU   A OE2  1 
ATOM   550  H  H    A GLU   A 1 26  ? 15.489 1.223   13.027  0.50 16.80 ?  26   GLU   A H    1 
ATOM   551  H  H    B GLU   A 1 26  ? 15.345 0.803   12.786  0.50 16.96 ?  26   GLU   A H    1 
ATOM   552  H  HA   A GLU   A 1 26  ? 15.307 -0.292  15.148  0.50 16.73 ?  26   GLU   A HA   1 
ATOM   553  H  HA   B GLU   A 1 26  ? 15.368 -0.646  14.940  0.50 17.40 ?  26   GLU   A HA   1 
ATOM   554  H  HB2  A GLU   A 1 26  ? 16.020 -0.833  12.497  0.50 18.11 ?  26   GLU   A HB2  1 
ATOM   555  H  HB2  B GLU   A 1 26  ? 16.064 -1.203  12.286  0.50 19.58 ?  26   GLU   A HB2  1 
ATOM   556  H  HB3  A GLU   A 1 26  ? 16.250 -1.963  13.584  0.50 18.11 ?  26   GLU   A HB3  1 
ATOM   557  H  HB3  B GLU   A 1 26  ? 16.440 -2.277  13.391  0.50 19.58 ?  26   GLU   A HB3  1 
ATOM   558  H  HG2  A GLU   A 1 26  ? 13.715 -0.878  13.099  0.50 21.50 ?  26   GLU   A HG2  1 
ATOM   559  H  HG2  B GLU   A 1 26  ? 13.821 -1.471  12.769  0.50 21.75 ?  26   GLU   A HG2  1 
ATOM   560  H  HG3  A GLU   A 1 26  ? 14.234 -2.176  12.346  0.50 21.50 ?  26   GLU   A HG3  1 
ATOM   561  H  HG3  B GLU   A 1 26  ? 14.459 -2.875  12.386  0.50 21.75 ?  26   GLU   A HG3  1 
ATOM   562  N  N    A ALA   A 1 27  ? 18.325 0.246   14.179  0.50 13.38 ?  27   ALA   A N    1 
ATOM   563  N  N    B ALA   A 1 27  ? 18.282 0.261   13.996  0.50 12.48 ?  27   ALA   A N    1 
ATOM   564  C  CA   A ALA   A 1 27  ? 19.716 0.163   14.617  0.50 13.56 ?  27   ALA   A CA   1 
ATOM   565  C  CA   B ALA   A 1 27  ? 19.665 0.356   14.446  0.50 12.13 ?  27   ALA   A CA   1 
ATOM   566  C  C    A ALA   A 1 27  ? 19.944 0.965   15.893  0.50 14.97 ?  27   ALA   A C    1 
ATOM   567  C  C    B ALA   A 1 27  ? 19.769 1.198   15.713  0.50 12.27 ?  27   ALA   A C    1 
ATOM   568  O  O    A ALA   A 1 27  ? 20.647 0.512   16.804  0.50 15.27 ?  27   ALA   A O    1 
ATOM   569  O  O    B ALA   A 1 27  ? 20.399 0.788   16.695  0.50 12.39 ?  27   ALA   A O    1 
ATOM   570  C  CB   A ALA   A 1 27  ? 20.654 0.635   13.503  0.50 13.13 ?  27   ALA   A CB   1 
ATOM   571  C  CB   B ALA   A 1 27  ? 20.535 0.936   13.331  0.50 12.05 ?  27   ALA   A CB   1 
ATOM   572  H  H    A ALA   A 1 27  ? 18.213 0.592   13.398  0.50 16.08 ?  27   ALA   A H    1 
ATOM   573  H  H    B ALA   A 1 27  ? 18.112 0.656   13.251  0.50 15.00 ?  27   ALA   A H    1 
ATOM   574  H  HA   A ALA   A 1 27  ? 19.928 -0.761  14.805  0.50 16.30 ?  27   ALA   A HA   1 
ATOM   575  H  HA   B ALA   A 1 27  ? 19.988 -0.531  14.647  0.50 14.58 ?  27   ALA   A HA   1 
ATOM   576  H  HB1  A ALA   A 1 27  ? 21.573 0.571   13.813  0.50 15.78 ?  27   ALA   A HB1  1 
ATOM   577  H  HB1  B ALA   A 1 27  ? 21.450 0.986   13.640  0.50 14.48 ?  27   ALA   A HB1  1 
ATOM   578  H  HB2  A ALA   A 1 27  ? 20.532 0.068   12.723  0.50 15.78 ?  27   ALA   A HB2  1 
ATOM   579  H  HB2  B ALA   A 1 27  ? 20.477 0.358   12.553  0.50 14.48 ?  27   ALA   A HB2  1 
ATOM   580  H  HB3  A ALA   A 1 27  ? 20.446 1.555   13.276  0.50 15.78 ?  27   ALA   A HB3  1 
ATOM   581  H  HB3  B ALA   A 1 27  ? 20.211 1.824   13.105  0.50 14.48 ?  27   ALA   A HB3  1 
ATOM   582  N  N    A LYS   A 1 28  ? 19.353 2.159   15.982  0.50 16.93 ?  28   LYS   A N    1 
ATOM   583  N  N    B LYS   A 1 28  ? 19.139 2.375   15.717  0.50 13.81 ?  28   LYS   A N    1 
ATOM   584  C  CA   A LYS   A 1 28  ? 19.518 2.966   17.188  0.50 19.39 ?  28   LYS   A CA   1 
ATOM   585  C  CA   B LYS   A 1 28  ? 19.218 3.248   16.885  0.50 15.99 ?  28   LYS   A CA   1 
ATOM   586  C  C    A LYS   A 1 28  ? 18.970 2.253   18.418  0.50 19.99 ?  28   LYS   A C    1 
ATOM   587  C  C    B LYS   A 1 28  ? 18.704 2.553   18.138  0.50 16.78 ?  28   LYS   A C    1 
ATOM   588  O  O    A LYS   A 1 28  ? 19.539 2.377   19.509  0.50 21.25 ?  28   LYS   A O    1 
ATOM   589  O  O    B LYS   A 1 28  ? 19.278 2.714   19.221  0.50 17.46 ?  28   LYS   A O    1 
ATOM   590  C  CB   A LYS   A 1 28  ? 18.875 4.345   17.004  0.50 21.29 ?  28   LYS   A CB   1 
ATOM   591  C  CB   B LYS   A 1 28  ? 18.432 4.533   16.639  0.50 17.96 ?  28   LYS   A CB   1 
ATOM   592  C  CG   A LYS   A 1 28  ? 19.698 5.292   16.138  0.50 23.14 ?  28   LYS   A CG   1 
ATOM   593  C  CG   B LYS   A 1 28  ? 19.096 5.479   15.666  0.50 20.16 ?  28   LYS   A CG   1 
ATOM   594  C  CD   A LYS   A 1 28  ? 19.205 6.730   16.218  0.50 25.06 ?  28   LYS   A CD   1 
ATOM   595  C  CD   B LYS   A 1 28  ? 18.457 6.854   15.724  0.50 23.25 ?  28   LYS   A CD   1 
ATOM   596  C  CE   A LYS   A 1 28  ? 17.885 6.912   15.492  0.50 26.41 ?  28   LYS   A CE   1 
ATOM   597  C  CE   B LYS   A 1 28  ? 17.780 7.216   14.416  0.50 25.48 ?  28   LYS   A CE   1 
ATOM   598  N  NZ   A LYS   A 1 28  ? 17.498 8.349   15.420  0.50 27.37 ?  28   LYS   A NZ   1 
ATOM   599  N  NZ   B LYS   A 1 28  ? 17.039 8.503   14.524  0.50 26.38 ?  28   LYS   A NZ   1 
ATOM   600  H  H    A LYS   A 1 28  ? 18.867 2.515   15.372  0.50 20.33 ?  28   LYS   A H    1 
ATOM   601  H  H    B LYS   A 1 28  ? 18.669 2.686   15.071  0.50 16.60 ?  28   LYS   A H    1 
ATOM   602  H  HA   A LYS   A 1 28  ? 20.462 3.107   17.343  0.50 23.29 ?  28   LYS   A HA   1 
ATOM   603  H  HA   B LYS   A 1 28  ? 20.140 3.487   17.043  0.50 19.21 ?  28   LYS   A HA   1 
ATOM   604  H  HB2  A LYS   A 1 28  ? 18.011 4.239   16.580  0.50 25.57 ?  28   LYS   A HB2  1 
ATOM   605  H  HB2  B LYS   A 1 28  ? 17.559 4.307   16.280  0.50 21.58 ?  28   LYS   A HB2  1 
ATOM   606  H  HB3  A LYS   A 1 28  ? 18.768 4.764   17.872  0.50 25.57 ?  28   LYS   A HB3  1 
ATOM   607  H  HB3  B LYS   A 1 28  ? 18.327 5.003   17.482  0.50 21.58 ?  28   LYS   A HB3  1 
ATOM   608  H  HG2  A LYS   A 1 28  ? 20.621 5.275   16.435  0.50 27.79 ?  28   LYS   A HG2  1 
ATOM   609  H  HG2  B LYS   A 1 28  ? 20.034 5.566   15.893  0.50 24.22 ?  28   LYS   A HG2  1 
ATOM   610  H  HG3  A LYS   A 1 28  ? 19.641 5.008   15.212  0.50 27.79 ?  28   LYS   A HG3  1 
ATOM   611  H  HG3  B LYS   A 1 28  ? 18.997 5.134   14.765  0.50 24.22 ?  28   LYS   A HG3  1 
ATOM   612  H  HD2  A LYS   A 1 28  ? 19.075 6.973   17.148  0.50 30.10 ?  28   LYS   A HD2  1 
ATOM   613  H  HD2  B LYS   A 1 28  ? 17.786 6.869   16.426  0.50 27.92 ?  28   LYS   A HD2  1 
ATOM   614  H  HD3  A LYS   A 1 28  ? 19.860 7.317   15.808  0.50 30.10 ?  28   LYS   A HD3  1 
ATOM   615  H  HD3  B LYS   A 1 28  ? 19.143 7.516   15.905  0.50 27.92 ?  28   LYS   A HD3  1 
ATOM   616  H  HE2  A LYS   A 1 28  ? 17.968 6.574   14.587  0.50 31.72 ?  28   LYS   A HE2  1 
ATOM   617  H  HE2  B LYS   A 1 28  ? 18.454 7.308   13.724  0.50 30.60 ?  28   LYS   A HE2  1 
ATOM   618  H  HE3  A LYS   A 1 28  ? 17.189 6.434   15.968  0.50 31.72 ?  28   LYS   A HE3  1 
ATOM   619  H  HE3  B LYS   A 1 28  ? 17.149 6.519   14.180  0.50 30.60 ?  28   LYS   A HE3  1 
ATOM   620  H  HZ1  A LYS   A 1 28  ? 16.723 8.435   14.991  0.50 32.87 ?  28   LYS   A HZ1  1 
ATOM   621  H  HZ1  B LYS   A 1 28  ? 16.651 8.696   13.747  0.50 31.68 ?  28   LYS   A HZ1  1 
ATOM   622  H  HZ2  A LYS   A 1 28  ? 17.413 8.683   16.241  0.50 32.87 ?  28   LYS   A HZ2  1 
ATOM   623  H  HZ2  B LYS   A 1 28  ? 16.412 8.441   15.153  0.50 31.68 ?  28   LYS   A HZ2  1 
ATOM   624  H  HZ3  A LYS   A 1 28  ? 18.122 8.811   14.984  0.50 32.87 ?  28   LYS   A HZ3  1 
ATOM   625  H  HZ3  B LYS   A 1 28  ? 17.600 9.160   14.738  0.50 31.68 ?  28   LYS   A HZ3  1 
ATOM   626  N  N    A LYS   A 1 29  ? 17.890 1.485   18.260  0.50 20.06 ?  29   LYS   A N    1 
ATOM   627  N  N    B LYS   A 1 29  ? 17.618 1.789   18.012  0.50 17.57 ?  29   LYS   A N    1 
ATOM   628  C  CA   A LYS   A 1 29  ? 17.290 0.792   19.397  0.50 21.35 ?  29   LYS   A CA   1 
ATOM   629  C  CA   B LYS   A 1 29  ? 17.023 1.134   19.172  0.50 19.42 ?  29   LYS   A CA   1 
ATOM   630  C  C    A LYS   A 1 29  ? 18.093 -0.447  19.783  0.50 20.36 ?  29   LYS   A C    1 
ATOM   631  C  C    B LYS   A 1 29  ? 17.834 -0.084  19.595  0.50 18.88 ?  29   LYS   A C    1 
ATOM   632  O  O    A LYS   A 1 29  ? 18.365 -0.680  20.967  0.50 20.90 ?  29   LYS   A O    1 
ATOM   633  O  O    B LYS   A 1 29  ? 18.145 -0.250  20.780  0.50 19.95 ?  29   LYS   A O    1 
ATOM   634  C  CB   A LYS   A 1 29  ? 15.848 0.403   19.060  0.50 24.41 ?  29   LYS   A CB   1 
ATOM   635  C  CB   B LYS   A 1 29  ? 15.583 0.726   18.855  0.50 22.40 ?  29   LYS   A CB   1 
ATOM   636  C  CG   A LYS   A 1 29  ? 15.106 -0.306  20.185  0.50 27.54 ?  29   LYS   A CG   1 
ATOM   637  C  CG   B LYS   A 1 29  ? 14.858 0.038   20.004  0.50 25.62 ?  29   LYS   A CG   1 
ATOM   638  C  CD   A LYS   A 1 29  ? 14.759 0.648   21.318  0.50 30.32 ?  29   LYS   A CD   1 
ATOM   639  C  CD   B LYS   A 1 29  ? 14.580 1.006   21.142  0.50 28.63 ?  29   LYS   A CD   1 
ATOM   640  C  CE   A LYS   A 1 29  ? 13.874 -0.025  22.357  0.50 32.18 ?  29   LYS   A CE   1 
ATOM   641  C  CE   B LYS   A 1 29  ? 13.743 0.355   22.230  0.50 30.69 ?  29   LYS   A CE   1 
ATOM   642  N  NZ   A LYS   A 1 29  ? 13.407 0.933   23.397  0.50 33.34 ?  29   LYS   A NZ   1 
ATOM   643  N  NZ   B LYS   A 1 29  ? 13.414 1.313   23.319  0.50 31.94 ?  29   LYS   A NZ   1 
ATOM   644  H  H    A LYS   A 1 29  ? 17.490 1.348   17.509  0.50 24.10 ?  29   LYS   A H    1 
ATOM   645  H  H    B LYS   A 1 29  ? 17.203 1.636   17.273  0.50 21.11 ?  29   LYS   A H    1 
ATOM   646  H  HA   A LYS   A 1 29  ? 17.267 1.393   20.158  0.50 25.64 ?  29   LYS   A HA   1 
ATOM   647  H  HA   B LYS   A 1 29  ? 17.003 1.751   19.918  0.50 23.33 ?  29   LYS   A HA   1 
ATOM   648  H  HB2  A LYS   A 1 29  ? 15.349 1.207   18.844  0.50 29.31 ?  29   LYS   A HB2  1 
ATOM   649  H  HB2  B LYS   A 1 29  ? 15.076 1.522   18.629  0.50 26.90 ?  29   LYS   A HB2  1 
ATOM   650  H  HB3  A LYS   A 1 29  ? 15.856 -0.192  18.296  0.50 29.31 ?  29   LYS   A HB3  1 
ATOM   651  H  HB3  B LYS   A 1 29  ? 15.585 0.114   18.104  0.50 26.90 ?  29   LYS   A HB3  1 
ATOM   652  H  HG2  A LYS   A 1 29  ? 14.278 -0.672  19.838  0.50 33.07 ?  29   LYS   A HG2  1 
ATOM   653  H  HG2  B LYS   A 1 29  ? 14.007 -0.304  19.686  0.50 30.76 ?  29   LYS   A HG2  1 
ATOM   654  H  HG3  A LYS   A 1 29  ? 15.657 -1.018  20.546  0.50 33.07 ?  29   LYS   A HG3  1 
ATOM   655  H  HG3  B LYS   A 1 29  ? 15.399 -0.692  20.348  0.50 30.76 ?  29   LYS   A HG3  1 
ATOM   656  H  HD2  A LYS   A 1 29  ? 15.575 0.939   21.755  0.50 36.41 ?  29   LYS   A HD2  1 
ATOM   657  H  HD2  B LYS   A 1 29  ? 15.421 1.289   21.534  0.50 34.38 ?  29   LYS   A HD2  1 
ATOM   658  H  HD3  A LYS   A 1 29  ? 14.280 1.412   20.959  0.50 36.41 ?  29   LYS   A HD3  1 
ATOM   659  H  HD3  B LYS   A 1 29  ? 14.094 1.771   20.798  0.50 34.38 ?  29   LYS   A HD3  1 
ATOM   660  H  HE2  A LYS   A 1 29  ? 13.094 -0.399  21.917  0.50 38.64 ?  29   LYS   A HE2  1 
ATOM   661  H  HE2  B LYS   A 1 29  ? 12.912 0.035   21.844  0.50 36.85 ?  29   LYS   A HE2  1 
ATOM   662  H  HE3  A LYS   A 1 29  ? 14.378 -0.728  22.797  0.50 38.64 ?  29   LYS   A HE3  1 
ATOM   663  H  HE3  B LYS   A 1 29  ? 14.239 -0.385  22.615  0.50 36.85 ?  29   LYS   A HE3  1 
ATOM   664  H  HZ1  A LYS   A 1 29  ? 12.893 0.512   23.990  0.50 40.03 ?  29   LYS   A HZ1  1 
ATOM   665  H  HZ1  B LYS   A 1 29  ? 12.924 0.908   23.942  0.50 38.35 ?  29   LYS   A HZ1  1 
ATOM   666  H  HZ2  A LYS   A 1 29  ? 14.106 1.287   23.820  0.50 40.03 ?  29   LYS   A HZ2  1 
ATOM   667  H  HZ2  B LYS   A 1 29  ? 14.162 1.618   23.692  0.50 38.35 ?  29   LYS   A HZ2  1 
ATOM   668  H  HZ3  A LYS   A 1 29  ? 12.936 1.587   23.018  0.50 40.03 ?  29   LYS   A HZ3  1 
ATOM   669  H  HZ3  B LYS   A 1 29  ? 12.954 2.000   22.990  0.50 38.35 ?  29   LYS   A HZ3  1 
ATOM   670  N  N    A VAL   A 1 30  ? 18.460 -1.264  18.797  0.50 19.12 ?  30   VAL   A N    1 
ATOM   671  N  N    B VAL   A 1 30  ? 18.176 -0.949  18.640  0.50 18.25 ?  30   VAL   A N    1 
ATOM   672  C  CA   A VAL   A 1 30  ? 19.103 -2.543  19.079  0.50 18.06 ?  30   VAL   A CA   1 
ATOM   673  C  CA   B VAL   A 1 30  ? 18.814 -2.217  18.977  0.50 17.40 ?  30   VAL   A CA   1 
ATOM   674  C  C    A VAL   A 1 30  ? 20.607 -2.393  19.289  0.50 16.71 ?  30   VAL   A C    1 
ATOM   675  C  C    B VAL   A 1 30  ? 20.308 -2.048  19.231  0.50 17.02 ?  30   VAL   A C    1 
ATOM   676  O  O    A VAL   A 1 30  ? 21.201 -3.136  20.080  0.50 17.33 ?  30   VAL   A O    1 
ATOM   677  O  O    B VAL   A 1 30  ? 20.880 -2.753  20.070  0.50 17.33 ?  30   VAL   A O    1 
ATOM   678  C  CB   A VAL   A 1 30  ? 18.785 -3.537  17.947  0.50 18.79 ?  30   VAL   A CB   1 
ATOM   679  C  CB   B VAL   A 1 30  ? 18.534 -3.256  17.874  0.50 17.52 ?  30   VAL   A CB   1 
ATOM   680  C  CG1  A VAL   A 1 30  ? 19.548 -4.842  18.139  0.50 19.36 ?  30   VAL   A CG1  1 
ATOM   681  C  CG1  B VAL   A 1 30  ? 19.285 -4.554  18.144  0.50 18.08 ?  30   VAL   A CG1  1 
ATOM   682  C  CG2  A VAL   A 1 30  ? 17.286 -3.796  17.873  0.50 19.46 ?  30   VAL   A CG2  1 
ATOM   683  C  CG2  B VAL   A 1 30  ? 17.038 -3.519  17.758  0.50 18.07 ?  30   VAL   A CG2  1 
ATOM   684  H  H    A VAL   A 1 30  ? 18.329 -1.110  17.962  0.50 22.96 ?  30   VAL   A H    1 
ATOM   685  H  H    B VAL   A 1 30  ? 18.040 -0.830  17.798  0.50 21.92 ?  30   VAL   A H    1 
ATOM   686  H  HA   A VAL   A 1 30  ? 18.725 -2.903  19.895  0.50 21.69 ?  30   VAL   A HA   1 
ATOM   687  H  HA   B VAL   A 1 30  ? 18.412 -2.554  19.791  0.50 20.91 ?  30   VAL   A HA   1 
ATOM   688  H  HB   A VAL   A 1 30  ? 19.063 -3.153  17.101  0.50 22.58 ?  30   VAL   A HB   1 
ATOM   689  H  HB   B VAL   A 1 30  ? 18.841 -2.909  17.022  0.50 21.05 ?  30   VAL   A HB   1 
ATOM   690  H  HG11 A VAL   A 1 30  ? 19.164 -5.518  17.558  0.50 23.25 ?  30   VAL   A HG11 1 
ATOM   691  H  HG11 B VAL   A 1 30  ? 18.927 -5.251  17.569  0.50 21.72 ?  30   VAL   A HG11 1 
ATOM   692  H  HG12 A VAL   A 1 30  ? 20.479 -4.702  17.911  0.50 23.25 ?  30   VAL   A HG12 1 
ATOM   693  H  HG12 B VAL   A 1 30  ? 20.226 -4.423  17.953  0.50 21.72 ?  30   VAL   A HG12 1 
ATOM   694  H  HG13 A VAL   A 1 30  ? 19.468 -5.120  19.065  0.50 23.25 ?  30   VAL   A HG13 1 
ATOM   695  H  HG13 B VAL   A 1 30  ? 19.163 -4.801  19.074  0.50 21.72 ?  30   VAL   A HG13 1 
ATOM   696  H  HG21 A VAL   A 1 30  ? 17.112 -4.459  17.185  0.50 23.37 ?  30   VAL   A HG21 1 
ATOM   697  H  HG21 B VAL   A 1 30  ? 16.886 -4.208  17.091  0.50 21.71 ?  30   VAL   A HG21 1 
ATOM   698  H  HG22 A VAL   A 1 30  ? 16.979 -4.125  18.733  0.50 23.37 ?  30   VAL   A HG22 1 
ATOM   699  H  HG22 B VAL   A 1 30  ? 16.702 -3.815  18.619  0.50 21.71 ?  30   VAL   A HG22 1 
ATOM   700  H  HG23 A VAL   A 1 30  ? 16.832 -2.968  17.655  0.50 23.37 ?  30   VAL   A HG23 1 
ATOM   701  H  HG23 B VAL   A 1 30  ? 16.593 -2.700  17.493  0.50 21.71 ?  30   VAL   A HG23 1 
ATOM   702  N  N    A LYS   A 1 31  ? 21.244 -1.451  18.602  0.50 15.54 ?  31   LYS   A N    1 
ATOM   703  N  N    B LYS   A 1 31  ? 20.957 -1.122  18.534  0.50 16.93 ?  31   LYS   A N    1 
ATOM   704  C  CA   A LYS   A 1 31  ? 22.697 -1.347  18.557  0.50 16.08 ?  31   LYS   A CA   1 
ATOM   705  C  CA   B LYS   A 1 31  ? 22.412 -1.026  18.503  0.50 17.49 ?  31   LYS   A CA   1 
ATOM   706  C  C    A LYS   A 1 31  ? 23.300 -2.710  18.203  0.50 14.68 ?  31   LYS   A C    1 
ATOM   707  C  C    B LYS   A 1 31  ? 23.030 -2.401  18.234  0.50 16.38 ?  31   LYS   A C    1 
ATOM   708  O  O    A LYS   A 1 31  ? 24.063 -3.283  18.987  0.50 15.25 ?  31   LYS   A O    1 
ATOM   709  O  O    B LYS   A 1 31  ? 23.785 -2.922  19.060  0.50 17.24 ?  31   LYS   A O    1 
ATOM   710  C  CB   A LYS   A 1 31  ? 23.274 -0.813  19.861  0.50 20.02 ?  31   LYS   A CB   1 
ATOM   711  C  CB   B LYS   A 1 31  ? 22.974 -0.415  19.778  0.50 20.28 ?  31   LYS   A CB   1 
ATOM   712  C  CG   A LYS   A 1 31  ? 22.579 0.443   20.380  0.50 24.89 ?  31   LYS   A CG   1 
ATOM   713  C  CG   B LYS   A 1 31  ? 22.318 0.890   20.176  0.50 24.64 ?  31   LYS   A CG   1 
ATOM   714  C  CD   A LYS   A 1 31  ? 23.580 1.509   20.812  0.50 28.53 ?  31   LYS   A CD   1 
ATOM   715  C  CD   B LYS   A 1 31  ? 23.317 1.818   20.837  0.50 28.08 ?  31   LYS   A CD   1 
ATOM   716  C  CE   A LYS   A 1 31  ? 22.935 2.558   21.711  0.50 30.76 ?  31   LYS   A CE   1 
ATOM   717  C  CE   B LYS   A 1 31  ? 22.620 2.851   21.698  0.50 30.48 ?  31   LYS   A CE   1 
ATOM   718  N  NZ   A LYS   A 1 31  ? 21.770 3.234   21.075  0.50 32.00 ?  31   LYS   A NZ   1 
ATOM   719  N  NZ   B LYS   A 1 31  ? 21.494 3.505   20.982  0.50 31.95 ?  31   LYS   A NZ   1 
ATOM   720  H  H    A LYS   A 1 31  ? 20.847 -0.848  18.138  0.50 18.67 ?  31   LYS   A H    1 
ATOM   721  H  H    B LYS   A 1 31  ? 20.563 -0.518  18.065  0.50 20.34 ?  31   LYS   A H    1 
ATOM   722  H  HA   A LYS   A 1 31  ? 22.938 -0.724  17.856  0.50 19.32 ?  31   LYS   A HA   1 
ATOM   723  H  HA   B LYS   A 1 31  ? 22.659 -0.443  17.773  0.50 21.01 ?  31   LYS   A HA   1 
ATOM   724  H  HB2  A LYS   A 1 31  ? 23.197 -1.501  20.538  0.50 24.05 ?  31   LYS   A HB2  1 
ATOM   725  H  HB2  B LYS   A 1 31  ? 22.853 -1.039  20.507  0.50 24.36 ?  31   LYS   A HB2  1 
ATOM   726  H  HB3  A LYS   A 1 31  ? 24.211 -0.597  19.720  0.50 24.05 ?  31   LYS   A HB3  1 
ATOM   727  H  HB3  B LYS   A 1 31  ? 23.921 -0.239  19.648  0.50 24.36 ?  31   LYS   A HB3  1 
ATOM   728  H  HG2  A LYS   A 1 31  ? 22.025 0.817   19.676  0.50 29.89 ?  31   LYS   A HG2  1 
ATOM   729  H  HG2  B LYS   A 1 31  ? 21.967 1.330   19.385  0.50 29.59 ?  31   LYS   A HG2  1 
ATOM   730  H  HG3  A LYS   A 1 31  ? 22.034 0.212   21.148  0.50 29.89 ?  31   LYS   A HG3  1 
ATOM   731  H  HG3  B LYS   A 1 31  ? 21.603 0.711   20.808  0.50 29.59 ?  31   LYS   A HG3  1 
ATOM   732  H  HD2  A LYS   A 1 31  ? 24.302 1.091   21.306  0.50 34.26 ?  31   LYS   A HD2  1 
ATOM   733  H  HD2  B LYS   A 1 31  ? 23.913 1.299   21.401  0.50 33.72 ?  31   LYS   A HD2  1 
ATOM   734  H  HD3  A LYS   A 1 31  ? 23.930 1.959   20.026  0.50 34.26 ?  31   LYS   A HD3  1 
ATOM   735  H  HD3  B LYS   A 1 31  ? 23.825 2.282   20.152  0.50 33.72 ?  31   LYS   A HD3  1 
ATOM   736  H  HE2  A LYS   A 1 31  ? 22.625 2.130   22.524  0.50 36.94 ?  31   LYS   A HE2  1 
ATOM   737  H  HE2  B LYS   A 1 31  ? 22.267 2.415   22.488  0.50 36.60 ?  31   LYS   A HE2  1 
ATOM   738  H  HE3  A LYS   A 1 31  ? 23.593 3.239   21.927  0.50 36.94 ?  31   LYS   A HE3  1 
ATOM   739  H  HE3  B LYS   A 1 31  ? 23.258 3.536   21.951  0.50 36.60 ?  31   LYS   A HE3  1 
ATOM   740  H  HZ1  A LYS   A 1 31  ? 21.429 3.841   21.632  0.50 38.42 ?  31   LYS   A HZ1  1 
ATOM   741  H  HZ1  B LYS   A 1 31  ? 21.160 4.162   21.479  0.50 38.36 ?  31   LYS   A HZ1  1 
ATOM   742  H  HZ2  A LYS   A 1 31  ? 22.025 3.641   20.326  0.50 38.42 ?  31   LYS   A HZ2  1 
ATOM   743  H  HZ2  B LYS   A 1 31  ? 21.780 3.842   20.210  0.50 38.36 ?  31   LYS   A HZ2  1 
ATOM   744  H  HZ3  A LYS   A 1 31  ? 21.140 2.636   20.881  0.50 38.42 ?  31   LYS   A HZ3  1 
ATOM   745  H  HZ3  B LYS   A 1 31  ? 20.851 2.911   20.817  0.50 38.36 ?  31   LYS   A HZ3  1 
ATOM   746  N  N    A PRO   A 1 32  ? 22.972 -3.251  17.034  0.50 13.47 ?  32   PRO   A N    1 
ATOM   747  N  N    B PRO   A 1 32  ? 22.734 -3.003  17.086  0.50 14.52 ?  32   PRO   A N    1 
ATOM   748  C  CA   A PRO   A 1 32  ? 23.438 -4.593  16.684  0.50 13.93 ?  32   PRO   A CA   1 
ATOM   749  C  CA   B PRO   A 1 32  ? 23.213 -4.359  16.810  0.50 14.34 ?  32   PRO   A CA   1 
ATOM   750  C  C    A PRO   A 1 32  ? 24.938 -4.617  16.459  0.50 13.74 ?  32   PRO   A C    1 
ATOM   751  C  C    B PRO   A 1 32  ? 24.720 -4.380  16.621  0.50 14.26 ?  32   PRO   A C    1 
ATOM   752  O  O    A PRO   A 1 32  ? 25.572 -3.600  16.169  0.50 13.25 ?  32   PRO   A O    1 
ATOM   753  O  O    B PRO   A 1 32  ? 25.385 -3.349  16.501  0.50 14.35 ?  32   PRO   A O    1 
ATOM   754  C  CB   A PRO   A 1 32  ? 22.700 -4.883  15.374  0.50 14.62 ?  32   PRO   A CB   1 
ATOM   755  C  CB   B PRO   A 1 32  ? 22.501 -4.702  15.500  0.50 14.46 ?  32   PRO   A CB   1 
ATOM   756  C  CG   A PRO   A 1 32  ? 22.543 -3.532  14.756  0.50 13.62 ?  32   PRO   A CG   1 
ATOM   757  C  CG   B PRO   A 1 32  ? 22.390 -3.380  14.811  0.50 13.80 ?  32   PRO   A CG   1 
ATOM   758  C  CD   A PRO   A 1 32  ? 22.250 -2.619  15.918  0.50 13.26 ?  32   PRO   A CD   1 
ATOM   759  C  CD   B PRO   A 1 32  ? 22.054 -2.418  15.918  0.50 14.04 ?  32   PRO   A CD   1 
ATOM   760  H  HA   A PRO   A 1 32  ? 23.184 -5.241  17.363  0.50 16.74 ?  32   PRO   A HA   1 
ATOM   761  H  HA   B PRO   A 1 32  ? 22.946 -4.976  17.510  0.50 17.23 ?  32   PRO   A HA   1 
ATOM   762  H  HB2  A PRO   A 1 32  ? 23.240 -5.465  14.812  0.50 17.56 ?  32   PRO   A HB2  1 
ATOM   763  H  HB2  B PRO   A 1 32  ? 23.039 -5.322  14.983  0.50 17.37 ?  32   PRO   A HB2  1 
ATOM   764  H  HB3  A PRO   A 1 32  ? 21.837 -5.287  15.560  0.50 17.56 ?  32   PRO   A HB3  1 
ATOM   765  H  HB3  B PRO   A 1 32  ? 21.623 -5.074  15.685  0.50 17.37 ?  32   PRO   A HB3  1 
ATOM   766  H  HG2  A PRO   A 1 32  ? 23.368 -3.279  14.312  0.50 16.37 ?  32   PRO   A HG2  1 
ATOM   767  H  HG2  B PRO   A 1 32  ? 23.238 -3.152  14.398  0.50 16.58 ?  32   PRO   A HG2  1 
ATOM   768  H  HG3  A PRO   A 1 32  ? 21.804 -3.545  14.127  0.50 16.37 ?  32   PRO   A HG3  1 
ATOM   769  H  HG3  B PRO   A 1 32  ? 21.681 -3.412  14.149  0.50 16.58 ?  32   PRO   A HG3  1 
ATOM   770  H  HD2  A PRO   A 1 32  ? 22.602 -1.733  15.737  0.50 15.93 ?  32   PRO   A HD2  1 
ATOM   771  H  HD2  B PRO   A 1 32  ? 22.411 -1.539  15.716  0.50 16.87 ?  32   PRO   A HD2  1 
ATOM   772  H  HD3  A PRO   A 1 32  ? 21.300 -2.599  16.093  0.50 15.93 ?  32   PRO   A HD3  1 
ATOM   773  H  HD3  B PRO   A 1 32  ? 21.094 -2.389  16.057  0.50 16.87 ?  32   PRO   A HD3  1 
ATOM   774  N  N    A THR   A 1 33  ? 25.501 -5.818  16.576  0.50 13.55 ?  33   THR   A N    1 
ATOM   775  N  N    B THR   A 1 33  ? 25.258 -5.598  16.579  0.50 14.17 ?  33   THR   A N    1 
ATOM   776  C  CA   A THR   A 1 33  ? 26.908 -5.995  16.246  0.50 14.23 ?  33   THR   A CA   1 
ATOM   777  C  CA   B THR   A 1 33  ? 26.680 -5.769  16.304  0.50 14.30 ?  33   THR   A CA   1 
ATOM   778  C  C    A THR   A 1 33  ? 27.188 -5.544  14.818  0.50 13.14 ?  33   THR   A C    1 
ATOM   779  C  C    B THR   A 1 33  ? 27.025 -5.323  14.886  0.50 13.22 ?  33   THR   A C    1 
ATOM   780  O  O    A THR   A 1 33  ? 28.254 -4.979  14.536  0.50 12.96 ?  33   THR   A O    1 
ATOM   781  O  O    B THR   A 1 33  ? 28.010 -4.604  14.672  0.50 13.00 ?  33   THR   A O    1 
ATOM   782  C  CB   A THR   A 1 33  ? 27.311 -7.457  16.452  0.50 16.03 ?  33   THR   A CB   1 
ATOM   783  C  CB   B THR   A 1 33  ? 27.064 -7.232  16.518  0.50 15.76 ?  33   THR   A CB   1 
ATOM   784  O  OG1  A THR   A 1 33  ? 27.055 -7.841  17.808  0.50 17.71 ?  33   THR   A OG1  1 
ATOM   785  O  OG1  B THR   A 1 33  ? 26.700 -7.622  17.847  0.50 16.78 ?  33   THR   A OG1  1 
ATOM   786  C  CG2  A THR   A 1 33  ? 28.787 -7.661  16.161  0.50 16.46 ?  33   THR   A CG2  1 
ATOM   787  C  CG2  B THR   A 1 33  ? 28.563 -7.435  16.308  0.50 16.47 ?  33   THR   A CG2  1 
ATOM   788  H  H    A THR   A 1 33  ? 25.097 -6.534  16.826  0.50 16.28 ?  33   THR   A H    1 
ATOM   789  H  H    B THR   A 1 33  ? 24.825 -6.331  16.714  0.50 17.02 ?  33   THR   A H    1 
ATOM   790  H  HA   A THR   A 1 33  ? 27.444 -5.449  16.843  0.50 17.10 ?  33   THR   A HA   1 
ATOM   791  H  HA   B THR   A 1 33  ? 27.191 -5.233  16.932  0.50 17.18 ?  33   THR   A HA   1 
ATOM   792  H  HB   A THR   A 1 33  ? 26.791 -8.021  15.855  0.50 19.26 ?  33   THR   A HB   1 
ATOM   793  H  HB   B THR   A 1 33  ? 26.588 -7.790  15.880  0.50 18.94 ?  33   THR   A HB   1 
ATOM   794  H  HG1  A THR   A 1 33  ? 27.481 -7.342  18.334  0.50 21.27 ?  33   THR   A HG1  1 
ATOM   795  H  HG1  B THR   A 1 33  ? 27.127 -7.162  18.408  0.50 20.16 ?  33   THR   A HG1  1 
ATOM   796  H  HG21 A THR   A 1 33  ? 29.056 -8.547  16.449  0.50 19.78 ?  33   THR   A HG21 1 
ATOM   797  H  HG21 B THR   A 1 33  ? 28.822 -8.323  16.598  0.50 19.78 ?  33   THR   A HG21 1 
ATOM   798  H  HG22 A THR   A 1 33  ? 28.954 -7.572  15.212  0.50 19.78 ?  33   THR   A HG22 1 
ATOM   799  H  HG22 B THR   A 1 33  ? 28.784 -7.336  15.367  0.50 19.78 ?  33   THR   A HG22 1 
ATOM   800  H  HG23 A THR   A 1 33  ? 29.310 -7.001  16.642  0.50 19.78 ?  33   THR   A HG23 1 
ATOM   801  H  HG23 B THR   A 1 33  ? 29.060 -6.779  16.819  0.50 19.78 ?  33   THR   A HG23 1 
ATOM   802  N  N    . VAL   A 1 34  ? 26.232 -5.754  13.907  1.00 12.39 ?  34   VAL   A N    1 
ATOM   803  C  CA   . VAL   A 1 34  ? 26.426 -5.424  12.498  1.00 11.41 ?  34   VAL   A CA   1 
ATOM   804  C  C    . VAL   A 1 34  ? 25.128 -4.876  11.920  1.00 10.82 ?  34   VAL   A C    1 
ATOM   805  O  O    . VAL   A 1 34  ? 24.091 -5.552  11.955  1.00 11.72 ?  34   VAL   A O    1 
ATOM   806  C  CB   . VAL   A 1 34  ? 26.882 -6.635  11.663  1.00 12.30 ?  34   VAL   A CB   1 
ATOM   807  C  CG1  . VAL   A 1 34  ? 27.076 -6.227  10.209  1.00 12.73 ?  34   VAL   A CG1  1 
ATOM   808  C  CG2  . VAL   A 1 34  ? 28.157 -7.262  12.226  1.00 13.54 ?  34   VAL   A CG2  1 
ATOM   809  H  H    A VAL   A 1 34  ? 25.462 -6.088  14.088  0.50 14.89 ?  34   VAL   A H    1 
ATOM   810  H  H    B VAL   A 1 34  ? 25.553 -6.262  14.044  0.50 14.89 ?  34   VAL   A H    1 
ATOM   811  H  HA   . VAL   A 1 34  ? 27.107 -4.730  12.424  1.00 13.72 ?  34   VAL   A HA   1 
ATOM   812  H  HB   . VAL   A 1 34  ? 26.186 -7.305  11.695  1.00 14.78 ?  34   VAL   A HB   1 
ATOM   813  H  HG11 . VAL   A 1 34  ? 27.579 -6.920  9.757   1.00 15.30 ?  34   VAL   A HG11 1 
ATOM   814  H  HG12 . VAL   A 1 34  ? 26.209 -6.119  9.793   1.00 15.30 ?  34   VAL   A HG12 1 
ATOM   815  H  HG13 . VAL   A 1 34  ? 27.568 -5.390  10.180  1.00 15.30 ?  34   VAL   A HG13 1 
ATOM   816  H  HG21 . VAL   A 1 34  ? 28.439 -7.981  11.635  1.00 16.27 ?  34   VAL   A HG21 1 
ATOM   817  H  HG22 . VAL   A 1 34  ? 28.849 -6.587  12.278  1.00 16.27 ?  34   VAL   A HG22 1 
ATOM   818  H  HG23 . VAL   A 1 34  ? 27.972 -7.619  13.110  1.00 16.27 ?  34   VAL   A HG23 1 
ATOM   819  N  N    . VAL   A 1 35  ? 25.195 -3.669  11.355  1.00 10.29 ?  35   VAL   A N    1 
ATOM   820  C  CA   . VAL   A 1 35  ? 24.166 -3.160  10.459  1.00 9.99  ?  35   VAL   A CA   1 
ATOM   821  C  C    . VAL   A 1 35  ? 24.727 -3.171  9.046   1.00 9.38  ?  35   VAL   A C    1 
ATOM   822  O  O    . VAL   A 1 35  ? 25.873 -2.766  8.817   1.00 10.08 ?  35   VAL   A O    1 
ATOM   823  C  CB   . VAL   A 1 35  ? 23.641 -1.763  10.857  1.00 10.53 ?  35   VAL   A CB   1 
ATOM   824  C  CG1  . VAL   A 1 35  ? 24.710 -0.675  10.730  1.00 11.24 ?  35   VAL   A CG1  1 
ATOM   825  C  CG2  . VAL   A 1 35  ? 22.413 -1.409  10.023  1.00 11.22 ?  35   VAL   A CG2  1 
ATOM   826  H  H    . VAL   A 1 35  ? 25.844 -3.112  11.480  1.00 12.38 ?  35   VAL   A H    1 
ATOM   827  H  HA   . VAL   A 1 35  ? 23.413 -3.769  10.480  1.00 12.01 ?  35   VAL   A HA   1 
ATOM   828  H  HB   . VAL   A 1 35  ? 23.357 -1.790  11.781  1.00 12.66 ?  35   VAL   A HB   1 
ATOM   829  H  HG11 . VAL   A 1 35  ? 24.360 0.154   11.093  1.00 13.52 ?  35   VAL   A HG11 1 
ATOM   830  H  HG12 . VAL   A 1 35  ? 25.494 -0.950  11.226  1.00 13.52 ?  35   VAL   A HG12 1 
ATOM   831  H  HG13 . VAL   A 1 35  ? 24.933 -0.556  9.793   1.00 13.52 ?  35   VAL   A HG13 1 
ATOM   832  H  HG21 . VAL   A 1 35  ? 22.051 -0.565  10.325  1.00 13.49 ?  35   VAL   A HG21 1 
ATOM   833  H  HG22 . VAL   A 1 35  ? 22.673 -1.339  9.086   1.00 13.49 ?  35   VAL   A HG22 1 
ATOM   834  H  HG23 . VAL   A 1 35  ? 21.747 -2.111  10.122  1.00 13.49 ?  35   VAL   A HG23 1 
ATOM   835  N  N    . VAL   A 1 36  ? 23.920 -3.641  8.097   1.00 8.99  ?  36   VAL   A N    1 
ATOM   836  C  CA   . VAL   A 1 36  ? 24.298 -3.652  6.692   1.00 8.73  ?  36   VAL   A CA   1 
ATOM   837  C  C    . VAL   A 1 36  ? 23.841 -2.361  6.027   1.00 8.80  ?  36   VAL   A C    1 
ATOM   838  O  O    . VAL   A 1 36  ? 22.672 -1.968  6.141   1.00 9.49  ?  36   VAL   A O    1 
ATOM   839  C  CB   . VAL   A 1 36  ? 23.698 -4.867  5.972   1.00 9.02  ?  36   VAL   A CB   1 
ATOM   840  C  CG1  . VAL   A 1 36  ? 23.976 -4.794  4.487   1.00 9.72  ?  36   VAL   A CG1  1 
ATOM   841  C  CG2  . VAL   A 1 36  ? 24.229 -6.155  6.561   1.00 9.63  ?  36   VAL   A CG2  1 
ATOM   842  H  H    . VAL   A 1 36  ? 23.129 -3.965  8.249   1.00 10.81 ?  36   VAL   A H    1 
ATOM   843  H  HA   . VAL   A 1 36  ? 25.265 -3.708  6.627   1.00 10.50 ?  36   VAL   A HA   1 
ATOM   844  H  HB   . VAL   A 1 36  ? 22.737 -4.856  6.090   1.00 10.84 ?  36   VAL   A HB   1 
ATOM   845  H  HG11 . VAL   A 1 36  ? 23.842 -5.669  4.096   1.00 11.69 ?  36   VAL   A HG11 1 
ATOM   846  H  HG12 . VAL   A 1 36  ? 23.369 -4.154  4.078   1.00 11.69 ?  36   VAL   A HG12 1 
ATOM   847  H  HG13 . VAL   A 1 36  ? 24.895 -4.509  4.350   1.00 11.69 ?  36   VAL   A HG13 1 
ATOM   848  H  HG21 . VAL   A 1 36  ? 23.848 -6.905  6.073   1.00 11.57 ?  36   VAL   A HG21 1 
ATOM   849  H  HG22 . VAL   A 1 36  ? 25.195 -6.167  6.481   1.00 11.57 ?  36   VAL   A HG22 1 
ATOM   850  H  HG23 . VAL   A 1 36  ? 23.971 -6.206  7.494   1.00 11.57 ?  36   VAL   A HG23 1 
ATOM   851  N  N    . ASN   A 1 37  ? 24.767 -1.722  5.306   1.00 8.39  ?  37   ASN   A N    1 
ATOM   852  C  CA   . ASN   A 1 37  ? 24.439 -0.608  4.434   1.00 8.73  ?  37   ASN   A CA   1 
ATOM   853  C  C    . ASN   A 1 37  ? 24.309 -1.089  2.998   1.00 8.38  ?  37   ASN   A C    1 
ATOM   854  O  O    . ASN   A 1 37  ? 25.099 -1.918  2.525   1.00 8.97  ?  37   ASN   A O    1 
ATOM   855  C  CB   . ASN   A 1 37  ? 25.513 0.473   4.515   1.00 8.88  ?  37   ASN   A CB   1 
ATOM   856  C  CG   . ASN   A 1 37  ? 25.194 1.666   3.654   1.00 8.70  ?  37   ASN   A CG   1 
ATOM   857  O  OD1  . ASN   A 1 37  ? 24.023 1.998   3.458   1.00 9.47  ?  37   ASN   A OD1  1 
ATOM   858  N  ND2  . ASN   A 1 37  ? 26.230 2.318   3.135   1.00 9.26  ?  37   ASN   A ND2  1 
ATOM   859  H  H    . ASN   A 1 37  ? 25.604 -1.921  5.315   1.00 10.09 ?  37   ASN   A H    1 
ATOM   860  H  HA   . ASN   A 1 37  ? 23.596 -0.218  4.711   1.00 10.50 ?  37   ASN   A HA   1 
ATOM   861  H  HB2  . ASN   A 1 37  ? 25.589 0.780   5.434   1.00 10.68 ?  37   ASN   A HB2  1 
ATOM   862  H  HB3  . ASN   A 1 37  ? 26.361 0.105   4.219   1.00 10.68 ?  37   ASN   A HB3  1 
ATOM   863  H  HD21 . ASN   A 1 37  ? 26.098 3.001   2.632   1.00 11.13 ?  37   ASN   A HD21 1 
ATOM   864  H  HD22 . ASN   A 1 37  ? 27.027 2.053   3.293   1.00 11.13 ?  37   ASN   A HD22 1 
ATOM   865  N  N    A ALA   A 1 38  ? 23.289 -0.561  2.317   0.50 8.58  ?  38   ALA   A N    1 
ATOM   866  N  N    B ALA   A 1 38  ? 23.303 -0.557  2.297   0.50 8.83  ?  38   ALA   A N    1 
ATOM   867  C  CA   A ALA   A 1 38  ? 23.117 -0.706  0.875   0.50 8.76  ?  38   ALA   A CA   1 
ATOM   868  C  CA   B ALA   A 1 38  ? 23.142 -0.779  0.859   0.50 9.25  ?  38   ALA   A CA   1 
ATOM   869  C  C    A ALA   A 1 38  ? 24.034 0.309   0.198   0.50 9.01  ?  38   ALA   A C    1 
ATOM   870  C  C    B ALA   A 1 38  ? 24.007 0.234   0.110   0.50 9.09  ?  38   ALA   A C    1 
ATOM   871  O  O    A ALA   A 1 38  ? 23.637 1.424   -0.147  0.50 8.65  ?  38   ALA   A O    1 
ATOM   872  O  O    B ALA   A 1 38  ? 23.545 1.266   -0.386  0.50 9.18  ?  38   ALA   A O    1 
ATOM   873  C  CB   A ALA   A 1 38  ? 21.658 -0.483  0.494   0.50 9.58  ?  38   ALA   A CB   1 
ATOM   874  C  CB   B ALA   A 1 38  ? 21.674 -0.688  0.460   0.50 10.37 ?  38   ALA   A CB   1 
ATOM   875  H  H    A ALA   A 1 38  ? 22.673 -0.085  2.687   0.50 10.32 ?  38   ALA   A H    1 
ATOM   876  H  H    B ALA   A 1 38  ? 22.693 -0.055  2.644   0.50 10.61 ?  38   ALA   A H    1 
ATOM   877  H  HA   A ALA   A 1 38  ? 23.379 -1.595  0.603   0.50 10.53 ?  38   ALA   A HA   1 
ATOM   878  H  HA   B ALA   A 1 38  ? 23.461 -1.669  0.642   0.50 11.13 ?  38   ALA   A HA   1 
ATOM   879  H  HB1  A ALA   A 1 38  ? 21.562 -0.585  -0.465  0.50 11.52 ?  38   ALA   A HB1  1 
ATOM   880  H  HB1  B ALA   A 1 38  ? 21.600 -0.843  -0.494  0.50 12.46 ?  38   ALA   A HB1  1 
ATOM   881  H  HB2  A ALA   A 1 38  ? 21.108 -1.138  0.954   0.50 11.52 ?  38   ALA   A HB2  1 
ATOM   882  H  HB2  B ALA   A 1 38  ? 21.170 -1.362  0.945   0.50 12.46 ?  38   ALA   A HB2  1 
ATOM   883  H  HB3  A ALA   A 1 38  ? 21.393 0.413   0.759   0.50 11.52 ?  38   ALA   A HB3  1 
ATOM   884  H  HB3  B ALA   A 1 38  ? 21.342 0.195   0.680   0.50 12.46 ?  38   ALA   A HB3  1 
ATOM   885  N  N    . ALA   A 1 39  ? 25.294 -0.080  0.030   1.00 9.38  ?  39   ALA   A N    1 
ATOM   886  C  CA   . ALA   A 1 39  ? 26.322 0.818   -0.465  1.00 9.33  ?  39   ALA   A CA   1 
ATOM   887  C  C    . ALA   A 1 39  ? 26.454 0.759   -1.981  1.00 9.31  ?  39   ALA   A C    1 
ATOM   888  O  O    . ALA   A 1 39  ? 25.975 -0.168  -2.642  1.00 9.66  ?  39   ALA   A O    1 
ATOM   889  C  CB   . ALA   A 1 39  ? 27.662 0.442   0.173   1.00 10.50 ?  39   ALA   A CB   1 
ATOM   890  H  H    A ALA   A 1 39  ? 25.579 -0.873  0.211   0.50 11.28 ?  39   ALA   A H    1 
ATOM   891  H  H    B ALA   A 1 39  ? 25.605 -0.849  0.266   0.50 11.28 ?  39   ALA   A H    1 
ATOM   892  H  HA   . ALA   A 1 39  ? 26.096 1.730   -0.207  1.00 11.22 ?  39   ALA   A HA   1 
ATOM   893  H  HB1  . ALA   A 1 39  ? 28.341 1.050   -0.155  1.00 12.62 ?  39   ALA   A HB1  1 
ATOM   894  H  HB2  . ALA   A 1 39  ? 27.583 0.528   1.140   1.00 12.62 ?  39   ALA   A HB2  1 
ATOM   895  H  HB3  . ALA   A 1 39  ? 27.877 -0.467  -0.063  1.00 12.62 ?  39   ALA   A HB3  1 
ATOM   896  N  N    A ASN   A 1 40  ? 27.162 1.755   -2.517  0.50 9.62  ?  40   ASN   A N    1 
ATOM   897  N  N    B ASN   A 1 40  ? 27.079 1.788   -2.546  0.50 9.59  ?  40   ASN   A N    1 
ATOM   898  C  CA   A ASN   A 1 40  ? 27.741 1.714   -3.852  0.50 9.39  ?  40   ASN   A CA   1 
ATOM   899  C  CA   B ASN   A 1 40  ? 27.542 1.744   -3.927  0.50 9.38  ?  40   ASN   A CA   1 
ATOM   900  C  C    A ASN   A 1 40  ? 29.260 1.610   -3.746  0.50 9.11  ?  40   ASN   A C    1 
ATOM   901  C  C    B ASN   A 1 40  ? 29.063 1.623   -3.932  0.50 8.79  ?  40   ASN   A C    1 
ATOM   902  O  O    A ASN   A 1 40  ? 29.838 1.727   -2.661  0.50 9.13  ?  40   ASN   A O    1 
ATOM   903  O  O    B ASN   A 1 40  ? 29.712 1.703   -2.886  0.50 9.23  ?  40   ASN   A O    1 
ATOM   904  C  CB   A ASN   A 1 40  ? 27.282 2.898   -4.723  0.50 9.95  ?  40   ASN   A CB   1 
ATOM   905  C  CB   B ASN   A 1 40  ? 27.045 2.954   -4.734  0.50 10.05 ?  40   ASN   A CB   1 
ATOM   906  C  CG   A ASN   A 1 40  ? 27.603 4.249   -4.118  0.50 10.70 ?  40   ASN   A CG   1 
ATOM   907  C  CG   B ASN   A 1 40  ? 27.475 4.271   -4.141  0.50 11.09 ?  40   ASN   A CG   1 
ATOM   908  O  OD1  A ASN   A 1 40  ? 28.737 4.506   -3.709  0.50 11.23 ?  40   ASN   A OD1  1 
ATOM   909  O  OD1  B ASN   A 1 40  ? 28.665 4.584   -4.100  0.50 11.30 ?  40   ASN   A OD1  1 
ATOM   910  N  ND2  A ASN   A 1 40  ? 26.597 5.125   -4.063  0.50 11.18 ?  40   ASN   A ND2  1 
ATOM   911  N  ND2  B ASN   A 1 40  ? 26.505 5.060   -3.686  0.50 12.08 ?  40   ASN   A ND2  1 
ATOM   912  H  H    A ASN   A 1 40  ? 27.335 2.482   -2.097  0.50 11.57 ?  40   ASN   A H    1 
ATOM   913  H  H    B ASN   A 1 40  ? 27.243 2.528   -2.145  0.50 11.54 ?  40   ASN   A H    1 
ATOM   914  H  HA   A ASN   A 1 40  ? 27.443 0.909   -4.286  0.50 11.29 ?  40   ASN   A HA   1 
ATOM   915  H  HA   B ASN   A 1 40  ? 27.173 0.944   -4.349  0.50 11.28 ?  40   ASN   A HA   1 
ATOM   916  H  HB2  A ASN   A 1 40  ? 27.725 2.838   -5.588  0.50 11.97 ?  40   ASN   A HB2  1 
ATOM   917  H  HB2  B ASN   A 1 40  ? 27.402 2.896   -5.630  0.50 12.09 ?  40   ASN   A HB2  1 
ATOM   918  H  HB3  A ASN   A 1 40  ? 26.325 2.845   -4.837  0.50 11.97 ?  40   ASN   A HB3  1 
ATOM   919  H  HB3  B ASN   A 1 40  ? 26.073 2.937   -4.761  0.50 12.09 ?  40   ASN   A HB3  1 
ATOM   920  H  HD21 A ASN   A 1 40  ? 26.727 5.913   -3.737  0.50 13.44 ?  40   ASN   A HD21 1 
ATOM   921  H  HD21 B ASN   A 1 40  ? 26.700 5.821   -3.336  0.50 14.52 ?  40   ASN   A HD21 1 
ATOM   922  H  HD22 A ASN   A 1 40  ? 25.818 4.901   -4.345  0.50 13.44 ?  40   ASN   A HD22 1 
ATOM   923  H  HD22 B ASN   A 1 40  ? 25.684 4.810   -3.739  0.50 14.52 ?  40   ASN   A HD22 1 
ATOM   924  N  N    A VAL   A 1 41  ? 29.904 1.355   -4.890  0.50 9.18  ?  41   VAL   A N    1 
ATOM   925  N  N    B VAL   A 1 41  ? 29.637 1.405   -5.118  0.50 9.26  ?  41   VAL   A N    1 
ATOM   926  C  CA   A VAL   A 1 41  ? 31.333 1.042   -4.891  0.50 9.20  ?  41   VAL   A CA   1 
ATOM   927  C  CA   B VAL   A 1 41  ? 31.062 1.084   -5.191  0.50 10.02 ?  41   VAL   A CA   1 
ATOM   928  C  C    A VAL   A 1 41  ? 32.160 2.211   -4.392  0.50 9.12  ?  41   VAL   A C    1 
ATOM   929  C  C    B VAL   A 1 41  ? 31.954 2.214   -4.696  0.50 9.92  ?  41   VAL   A C    1 
ATOM   930  O  O    A VAL   A 1 41  ? 33.263 2.016   -3.865  0.50 9.30  ?  41   VAL   A O    1 
ATOM   931  O  O    B VAL   A 1 41  ? 33.128 1.974   -4.382  0.50 9.30  ?  41   VAL   A O    1 
ATOM   932  C  CB   A VAL   A 1 41  ? 31.828 0.542   -6.269  0.50 9.25  ?  41   VAL   A CB   1 
ATOM   933  C  CB   B VAL   A 1 41  ? 31.494 0.639   -6.606  0.50 10.88 ?  41   VAL   A CB   1 
ATOM   934  C  CG1  A VAL   A 1 41  ? 31.119 -0.739  -6.672  0.50 9.88  ?  41   VAL   A CG1  1 
ATOM   935  C  CG1  B VAL   A 1 41  ? 30.830 -0.676  -6.985  0.50 12.00 ?  41   VAL   A CG1  1 
ATOM   936  C  CG2  A VAL   A 1 41  ? 31.703 1.613   -7.353  0.50 8.99  ?  41   VAL   A CG2  1 
ATOM   937  C  CG2  B VAL   A 1 41  ? 31.200 1.724   -7.637  0.50 11.19 ?  41   VAL   A CG2  1 
ATOM   938  H  H    A VAL   A 1 41  ? 29.546 1.355   -5.664  0.50 11.04 ?  41   VAL   A H    1 
ATOM   939  H  H    B VAL   A 1 41  ? 29.223 1.421   -5.874  0.50 11.13 ?  41   VAL   A H    1 
ATOM   940  H  HA   A VAL   A 1 41  ? 31.492 0.324   -4.268  0.50 11.07 ?  41   VAL   A HA   1 
ATOM   941  H  HA   B VAL   A 1 41  ? 31.215 0.330   -4.602  0.50 12.05 ?  41   VAL   A HA   1 
ATOM   942  H  HB   A VAL   A 1 41  ? 32.773 0.334   -6.200  0.50 11.13 ?  41   VAL   A HB   1 
ATOM   943  H  HB   B VAL   A 1 41  ? 32.452 0.495   -6.596  0.50 13.08 ?  41   VAL   A HB   1 
ATOM   944  H  HG11 A VAL   A 1 41  ? 31.460 -1.042  -7.530  0.50 11.88 ?  41   VAL   A HG11 1 
ATOM   945  H  HG11 B VAL   A 1 41  ? 31.117 -0.928  -7.876  0.50 14.42 ?  41   VAL   A HG11 1 
ATOM   946  H  HG12 A VAL   A 1 41  ? 31.280 -1.415  -5.996  0.50 11.88 ?  41   VAL   A HG12 1 
ATOM   947  H  HG12 B VAL   A 1 41  ? 31.096 -1.360  -6.348  0.50 14.42 ?  41   VAL   A HG12 1 
ATOM   948  H  HG13 A VAL   A 1 41  ? 30.165 -0.565  -6.743  0.50 11.88 ?  41   VAL   A HG13 1 
ATOM   949  H  HG13 B VAL   A 1 41  ? 29.867 -0.565  -6.965  0.50 14.42 ?  41   VAL   A HG13 1 
ATOM   950  H  HG21 A VAL   A 1 41  ? 31.932 1.219   -8.215  0.50 10.81 ?  41   VAL   A HG21 1 
ATOM   951  H  HG21 B VAL   A 1 41  ? 31.495 1.413   -8.508  0.50 13.45 ?  41   VAL   A HG21 1 
ATOM   952  H  HG22 A VAL   A 1 41  ? 30.794 1.939   -7.373  0.50 10.81 ?  41   VAL   A HG22 1 
ATOM   953  H  HG22 B VAL   A 1 41  ? 30.246 1.895   -7.654  0.50 13.45 ?  41   VAL   A HG22 1 
ATOM   954  H  HG23 A VAL   A 1 41  ? 32.317 2.338   -7.155  0.50 10.81 ?  41   VAL   A HG23 1 
ATOM   955  H  HG23 B VAL   A 1 41  ? 31.678 2.531   -7.395  0.50 13.45 ?  41   VAL   A HG23 1 
ATOM   956  N  N    A TYR   A 1 42  ? 31.668 3.436   -4.571  0.50 9.84  ?  42   TYR   A N    1 
ATOM   957  N  N    B TYR   A 1 42  ? 31.446 3.450   -4.655  0.50 10.45 ?  42   TYR   A N    1 
ATOM   958  C  CA   A TYR   A 1 42  ? 32.380 4.636   -4.158  0.50 9.97  ?  42   TYR   A CA   1 
ATOM   959  C  CA   B TYR   A 1 42  ? 32.221 4.608   -4.222  0.50 10.47 ?  42   TYR   A CA   1 
ATOM   960  C  C    A TYR   A 1 42  ? 32.079 5.015   -2.720  0.50 9.74  ?  42   TYR   A C    1 
ATOM   961  C  C    B TYR   A 1 42  ? 31.990 4.973   -2.764  0.50 10.39 ?  42   TYR   A C    1 
ATOM   962  O  O    A TYR   A 1 42  ? 32.618 6.016   -2.230  0.50 10.27 ?  42   TYR   A O    1 
ATOM   963  O  O    B TYR   A 1 42  ? 32.589 5.942   -2.281  0.50 11.09 ?  42   TYR   A O    1 
ATOM   964  C  CB   A TYR   A 1 42  ? 32.026 5.806   -5.092  0.50 10.58 ?  42   TYR   A CB   1 
ATOM   965  C  CB   B TYR   A 1 42  ? 31.895 5.826   -5.100  0.50 10.98 ?  42   TYR   A CB   1 
ATOM   966  C  CG   A TYR   A 1 42  ? 32.245 5.474   -6.551  0.50 11.02 ?  42   TYR   A CG   1 
ATOM   967  C  CG   B TYR   A 1 42  ? 32.033 5.542   -6.573  0.50 11.50 ?  42   TYR   A CG   1 
ATOM   968  C  CD1  A TYR   A 1 42  ? 33.523 5.273   -7.046  0.50 11.64 ?  42   TYR   A CD1  1 
ATOM   969  C  CD1  B TYR   A 1 42  ? 33.279 5.333   -7.141  0.50 11.76 ?  42   TYR   A CD1  1 
ATOM   970  C  CD2  A TYR   A 1 42  ? 31.176 5.332   -7.426  0.50 11.86 ?  42   TYR   A CD2  1 
ATOM   971  C  CD2  B TYR   A 1 42  ? 30.918 5.463   -7.393  0.50 13.00 ?  42   TYR   A CD2  1 
ATOM   972  C  CE1  A TYR   A 1 42  ? 33.734 4.950   -8.375  0.50 11.86 ?  42   TYR   A CE1  1 
ATOM   973  C  CE1  B TYR   A 1 42  ? 33.413 5.061   -8.489  0.50 12.09 ?  42   TYR   A CE1  1 
ATOM   974  C  CE2  A TYR   A 1 42  ? 31.379 5.016   -8.760  0.50 12.55 ?  42   TYR   A CE2  1 
ATOM   975  C  CE2  B TYR   A 1 42  ? 31.040 5.201   -8.740  0.50 13.48 ?  42   TYR   A CE2  1 
ATOM   976  C  CZ   A TYR   A 1 42  ? 32.661 4.827   -9.228  0.50 12.28 ?  42   TYR   A CZ   1 
ATOM   977  C  CZ   B TYR   A 1 42  ? 32.289 4.995   -9.285  0.50 13.14 ?  42   TYR   A CZ   1 
ATOM   978  O  OH   A TYR   A 1 42  ? 32.869 4.504   -10.550 0.50 13.31 ?  42   TYR   A OH   1 
ATOM   979  O  OH   B TYR   A 1 42  ? 32.418 4.730   -10.629 0.50 13.97 ?  42   TYR   A OH   1 
ATOM   980  H  H    A TYR   A 1 42  ? 30.908 3.599   -4.930  0.50 11.84 ?  42   TYR   A H    1 
ATOM   981  H  H    B TYR   A 1 42  ? 30.640 3.647   -4.894  0.50 12.56 ?  42   TYR   A H    1 
ATOM   982  H  HA   A TYR   A 1 42  ? 33.336 4.486   -4.232  0.50 11.99 ?  42   TYR   A HA   1 
ATOM   983  H  HA   B TYR   A 1 42  ? 33.162 4.414   -4.335  0.50 12.59 ?  42   TYR   A HA   1 
ATOM   984  H  HB2  A TYR   A 1 42  ? 31.090 6.034   -4.973  0.50 12.72 ?  42   TYR   A HB2  1 
ATOM   985  H  HB2  B TYR   A 1 42  ? 30.980 6.105   -4.932  0.50 13.20 ?  42   TYR   A HB2  1 
ATOM   986  H  HB3  A TYR   A 1 42  ? 32.583 6.571   -4.872  0.50 12.72 ?  42   TYR   A HB3  1 
ATOM   987  H  HB3  B TYR   A 1 42  ? 32.504 6.551   -4.876  0.50 13.20 ?  42   TYR   A HB3  1 
ATOM   988  H  HD1  A TYR   A 1 42  ? 34.255 5.355   -6.476  0.50 14.00 ?  42   TYR   A HD1  1 
ATOM   989  H  HD1  B TYR   A 1 42  ? 34.039 5.376   -6.605  0.50 14.14 ?  42   TYR   A HD1  1 
ATOM   990  H  HD2  A TYR   A 1 42  ? 30.311 5.464   -7.115  0.50 14.25 ?  42   TYR   A HD2  1 
ATOM   991  H  HD2  B TYR   A 1 42  ? 30.074 5.606   -7.029  0.50 15.62 ?  42   TYR   A HD2  1 
ATOM   992  H  HE1  A TYR   A 1 42  ? 34.601 4.826   -8.693  0.50 14.26 ?  42   TYR   A HE1  1 
ATOM   993  H  HE1  B TYR   A 1 42  ? 34.259 4.924   -8.854  0.50 14.53 ?  42   TYR   A HE1  1 
ATOM   994  H  HE2  A TYR   A 1 42  ? 30.652 4.934   -9.337  0.50 15.08 ?  42   TYR   A HE2  1 
ATOM   995  H  HE2  B TYR   A 1 42  ? 30.284 5.156   -9.278  0.50 16.20 ?  42   TYR   A HE2  1 
ATOM   996  H  HH   A TYR   A 1 42  ? 33.679 4.331   -10.677 0.50 15.99 ?  42   TYR   A HH   1 
ATOM   997  H  HH   B TYR   A 1 42  ? 31.666 4.721   -10.994 0.50 16.78 ?  42   TYR   A HH   1 
ATOM   998  N  N    A LEU   A 1 43  ? 31.227 4.246   -2.046  0.50 9.57  ?  43   LEU   A N    1 
ATOM   999  N  N    B LEU   A 1 43  ? 31.129 4.238   -2.062  0.50 10.17 ?  43   LEU   A N    1 
ATOM   1000 C  CA   A LEU   A 1 43  ? 30.785 4.562   -0.692  0.50 9.40  ?  43   LEU   A CA   1 
ATOM   1001 C  CA   B LEU   A 1 43  ? 30.687 4.602   -0.715  0.50 9.89  ?  43   LEU   A CA   1 
ATOM   1002 C  C    A LEU   A 1 43  ? 30.291 6.004   -0.585  0.50 9.66  ?  43   LEU   A C    1 
ATOM   1003 C  C    B LEU   A 1 43  ? 30.225 6.057   -0.649  0.50 10.03 ?  43   LEU   A C    1 
ATOM   1004 O  O    A LEU   A 1 43  ? 30.534 6.695   0.407   0.50 10.56 ?  43   LEU   A O    1 
ATOM   1005 O  O    B LEU   A 1 43  ? 30.501 6.779   0.311   0.50 10.60 ?  43   LEU   A O    1 
ATOM   1006 C  CB   A LEU   A 1 43  ? 31.852 4.251   0.355   0.50 10.03 ?  43   LEU   A CB   1 
ATOM   1007 C  CB   B LEU   A 1 43  ? 31.733 4.298   0.357   0.50 9.45  ?  43   LEU   A CB   1 
ATOM   1008 C  CG   A LEU   A 1 43  ? 32.331 2.799   0.440   0.50 10.54 ?  43   LEU   A CG   1 
ATOM   1009 C  CG   B LEU   A 1 43  ? 32.234 2.855   0.468   0.50 9.59  ?  43   LEU   A CG   1 
ATOM   1010 C  CD1  A LEU   A 1 43  ? 33.428 2.677   1.486   0.50 11.00 ?  43   LEU   A CD1  1 
ATOM   1011 C  CD1  B LEU   A 1 43  ? 33.234 2.744   1.617   0.50 10.29 ?  43   LEU   A CD1  1 
ATOM   1012 C  CD2  A LEU   A 1 43  ? 31.195 1.849   0.759   0.50 10.91 ?  43   LEU   A CD2  1 
ATOM   1013 C  CD2  B LEU   A 1 43  ? 31.094 1.861   0.634   0.50 9.83  ?  43   LEU   A CD2  1 
ATOM   1014 H  H    A LEU   A 1 43  ? 30.880 3.518   -2.359  0.50 11.50 ?  43   LEU   A H    1 
ATOM   1015 H  H    B LEU   A 1 43  ? 30.773 3.509   -2.351  0.50 12.23 ?  43   LEU   A H    1 
ATOM   1016 H  HA   A LEU   A 1 43  ? 30.023 3.995   -0.492  0.50 11.30 ?  43   LEU   A HA   1 
ATOM   1017 H  HA   B LEU   A 1 43  ? 29.913 4.054   -0.506  0.50 11.89 ?  43   LEU   A HA   1 
ATOM   1018 H  HB2  A LEU   A 1 43  ? 32.629 4.798   0.172   0.50 12.05 ?  43   LEU   A HB2  1 
ATOM   1019 H  HB2  B LEU   A 1 43  ? 32.505 4.855   0.190   0.50 11.36 ?  43   LEU   A HB2  1 
ATOM   1020 H  HB3  A LEU   A 1 43  ? 31.492 4.479   1.225   0.50 12.05 ?  43   LEU   A HB3  1 
ATOM   1021 H  HB3  B LEU   A 1 43  ? 31.351 4.530   1.219   0.50 11.36 ?  43   LEU   A HB3  1 
ATOM   1022 H  HG   A LEU   A 1 43  ? 32.709 2.536   -0.414  0.50 12.67 ?  43   LEU   A HG   1 
ATOM   1023 H  HG   B LEU   A 1 43  ? 32.704 2.627   -0.347  0.50 11.53 ?  43   LEU   A HG   1 
ATOM   1024 H  HD11 A LEU   A 1 43  ? 33.724 1.753   1.529   0.50 13.23 ?  43   LEU   A HD11 1 
ATOM   1025 H  HD11 B LEU   A 1 43  ? 33.546 1.827   1.678   0.50 12.37 ?  43   LEU   A HD11 1 
ATOM   1026 H  HD12 A LEU   A 1 43  ? 34.168 3.250   1.234   0.50 13.23 ?  43   LEU   A HD12 1 
ATOM   1027 H  HD12 B LEU   A 1 43  ? 33.983 3.337   1.442   0.50 12.37 ?  43   LEU   A HD12 1 
ATOM   1028 H  HD13 A LEU   A 1 43  ? 33.074 2.950   2.346   0.50 13.23 ?  43   LEU   A HD13 1 
ATOM   1029 H  HD13 B LEU   A 1 43  ? 32.796 3.000   2.444   0.50 12.37 ?  43   LEU   A HD13 1 
ATOM   1030 H  HD21 A LEU   A 1 43  ? 31.558 0.960   0.906   0.50 13.11 ?  43   LEU   A HD21 1 
ATOM   1031 H  HD21 B LEU   A 1 43  ? 31.465 0.976   0.789   0.50 11.82 ?  43   LEU   A HD21 1 
ATOM   1032 H  HD22 A LEU   A 1 43  ? 30.743 2.157   1.559   0.50 13.11 ?  43   LEU   A HD22 1 
ATOM   1033 H  HD22 B LEU   A 1 43  ? 30.549 2.126   1.392   0.50 11.82 ?  43   LEU   A HD22 1 
ATOM   1034 H  HD23 A LEU   A 1 43  ? 30.579 1.835   0.012   0.50 13.11 ?  43   LEU   A HD23 1 
ATOM   1035 H  HD23 B LEU   A 1 43  ? 30.558 1.856   -0.174  0.50 11.82 ?  43   LEU   A HD23 1 
ATOM   1036 N  N    A LYS   A 1 44  ? 29.575 6.452   -1.616  0.50 9.84  ?  44   LYS   A N    1 
ATOM   1037 N  N    B LYS   A 1 44  ? 29.503 6.485   -1.682  0.50 9.97  ?  44   LYS   A N    1 
ATOM   1038 C  CA   A LYS   A 1 44  ? 28.939 7.766   -1.611  0.50 10.40 ?  44   LYS   A CA   1 
ATOM   1039 C  CA   B LYS   A 1 44  ? 28.856 7.796   -1.699  0.50 10.23 ?  44   LYS   A CA   1 
ATOM   1040 C  C    A LYS   A 1 44  ? 27.504 7.580   -1.138  0.50 9.90  ?  44   LYS   A C    1 
ATOM   1041 C  C    B LYS   A 1 44  ? 27.445 7.616   -1.160  0.50 9.59  ?  44   LYS   A C    1 
ATOM   1042 O  O    A LYS   A 1 44  ? 26.653 7.057   -1.870  0.50 10.77 ?  44   LYS   A O    1 
ATOM   1043 O  O    B LYS   A 1 44  ? 26.550 7.138   -1.864  0.50 10.29 ?  44   LYS   A O    1 
ATOM   1044 C  CB   A LYS   A 1 44  ? 29.008 8.418   -2.989  0.50 11.89 ?  44   LYS   A CB   1 
ATOM   1045 C  CB   B LYS   A 1 44  ? 28.853 8.377   -3.108  0.50 12.27 ?  44   LYS   A CB   1 
ATOM   1046 C  CG   A LYS   A 1 44  ? 30.413 8.812   -3.420  0.50 14.09 ?  44   LYS   A CG   1 
ATOM   1047 C  CG   B LYS   A 1 44  ? 30.186 8.970   -3.534  0.50 14.98 ?  44   LYS   A CG   1 
ATOM   1048 C  CD   A LYS   A 1 44  ? 31.105 9.704   -2.397  0.50 18.35 ?  44   LYS   A CD   1 
ATOM   1049 C  CD   B LYS   A 1 44  ? 30.666 10.022  -2.536  0.50 18.34 ?  44   LYS   A CD   1 
ATOM   1050 C  CE   A LYS   A 1 44  ? 32.418 10.241  -2.930  0.50 21.19 ?  44   LYS   A CE   1 
ATOM   1051 C  CE   B LYS   A 1 44  ? 31.978 10.647  -2.958  0.50 20.41 ?  44   LYS   A CE   1 
ATOM   1052 N  NZ   A LYS   A 1 44  ? 33.177 10.983  -1.888  0.50 22.84 ?  44   LYS   A NZ   1 
ATOM   1053 N  NZ   B LYS   A 1 44  ? 32.978 10.630  -1.849  0.50 21.43 ?  44   LYS   A NZ   1 
ATOM   1054 H  H    A LYS   A 1 44  ? 29.435 6.005   -2.339  0.50 11.83 ?  44   LYS   A H    1 
ATOM   1055 H  H    B LYS   A 1 44  ? 29.377 6.030   -2.399  0.50 11.99 ?  44   LYS   A H    1 
ATOM   1056 H  HA   A LYS   A 1 44  ? 29.388 8.337   -0.968  0.50 12.50 ?  44   LYS   A HA   1 
ATOM   1057 H  HA   B LYS   A 1 44  ? 29.319 8.392   -1.090  0.50 12.30 ?  44   LYS   A HA   1 
ATOM   1058 H  HB2  A LYS   A 1 44  ? 28.658 7.798   -3.644  0.50 14.30 ?  44   LYS   A HB2  1 
ATOM   1059 H  HB2  B LYS   A 1 44  ? 28.627 7.671   -3.735  0.50 14.75 ?  44   LYS   A HB2  1 
ATOM   1060 H  HB3  A LYS   A 1 44  ? 28.467 9.225   -2.976  0.50 14.30 ?  44   LYS   A HB3  1 
ATOM   1061 H  HB3  B LYS   A 1 44  ? 28.186 9.081   -3.154  0.50 14.75 ?  44   LYS   A HB3  1 
ATOM   1062 H  HG2  A LYS   A 1 44  ? 30.947 8.010   -3.530  0.50 16.93 ?  44   LYS   A HG2  1 
ATOM   1063 H  HG2  B LYS   A 1 44  ? 30.850 8.265   -3.584  0.50 17.99 ?  44   LYS   A HG2  1 
ATOM   1064 H  HG3  A LYS   A 1 44  ? 30.363 9.298   -4.258  0.50 16.93 ?  44   LYS   A HG3  1 
ATOM   1065 H  HG3  B LYS   A 1 44  ? 30.084 9.398   -4.401  0.50 17.99 ?  44   LYS   A HG3  1 
ATOM   1066 H  HD2  A LYS   A 1 44  ? 30.524 10.453  -2.184  0.50 22.05 ?  44   LYS   A HD2  1 
ATOM   1067 H  HD2  B LYS   A 1 44  ? 29.992 10.714  -2.457  0.50 22.03 ?  44   LYS   A HD2  1 
ATOM   1068 H  HD3  A LYS   A 1 44  ? 31.293 9.188   -1.597  0.50 22.05 ?  44   LYS   A HD3  1 
ATOM   1069 H  HD3  B LYS   A 1 44  ? 30.818 9.602   -1.673  0.50 22.03 ?  44   LYS   A HD3  1 
ATOM   1070 H  HE2  A LYS   A 1 44  ? 32.963 9.501   -3.235  0.50 25.45 ?  44   LYS   A HE2  1 
ATOM   1071 H  HE2  B LYS   A 1 44  ? 32.344 10.143  -3.701  0.50 24.52 ?  44   LYS   A HE2  1 
ATOM   1072 H  HE3  A LYS   A 1 44  ? 32.236 10.849  -3.664  0.50 25.45 ?  44   LYS   A HE3  1 
ATOM   1073 H  HE3  B LYS   A 1 44  ? 31.820 11.565  -3.215  0.50 24.52 ?  44   LYS   A HE3  1 
ATOM   1074 H  HZ1  A LYS   A 1 44  ? 33.946 11.273  -2.225  0.50 27.43 ?  44   LYS   A HZ1  1 
ATOM   1075 H  HZ1  B LYS   A 1 44  ? 33.736 11.007  -2.123  0.50 25.73 ?  44   LYS   A HZ1  1 
ATOM   1076 H  HZ2  A LYS   A 1 44  ? 32.701 11.681  -1.606  0.50 27.43 ?  44   LYS   A HZ2  1 
ATOM   1077 H  HZ2  B LYS   A 1 44  ? 32.663 11.090  -1.153  0.50 25.73 ?  44   LYS   A HZ2  1 
ATOM   1078 H  HZ3  A LYS   A 1 44  ? 33.344 10.449  -1.197  0.50 27.43 ?  44   LYS   A HZ3  1 
ATOM   1079 H  HZ3  B LYS   A 1 44  ? 33.140 9.796   -1.595  0.50 25.73 ?  44   LYS   A HZ3  1 
ATOM   1080 N  N    . HIS   A 1 45  ? 27.250 7.977   0.106   1.00 9.31  ?  45   HIS   A N    1 
ATOM   1081 C  CA   . HIS   A 1 45  ? 26.012 7.642   0.800   1.00 9.29  ?  45   HIS   A CA   1 
ATOM   1082 C  C    . HIS   A 1 45  ? 24.998 8.770   0.633   1.00 10.04 ?  45   HIS   A C    1 
ATOM   1083 O  O    . HIS   A 1 45  ? 24.713 9.535   1.550   1.00 11.29 ?  45   HIS   A O    1 
ATOM   1084 C  CB   . HIS   A 1 45  ? 26.302 7.389   2.267   1.00 9.34  ?  45   HIS   A CB   1 
ATOM   1085 C  CG   . HIS   A 1 45  ? 27.412 6.422   2.505   1.00 8.99  ?  45   HIS   A CG   1 
ATOM   1086 N  ND1  . HIS   A 1 45  ? 27.404 5.134   2.009   1.00 9.44  ?  45   HIS   A ND1  1 
ATOM   1087 C  CD2  . HIS   A 1 45  ? 28.578 6.575   3.178   1.00 9.54  ?  45   HIS   A CD2  1 
ATOM   1088 C  CE1  . HIS   A 1 45  ? 28.520 4.536   2.386   1.00 9.52  ?  45   HIS   A CE1  1 
ATOM   1089 N  NE2  . HIS   A 1 45  ? 29.248 5.384   3.095   1.00 9.68  ?  45   HIS   A NE2  1 
ATOM   1090 H  H    A HIS   A 1 45  ? 27.791 8.452   0.580   0.50 11.19 ?  45   HIS   A H    1 
ATOM   1091 H  H    B HIS   A 1 45  ? 27.816 8.414   0.587   0.50 11.19 ?  45   HIS   A H    1 
ATOM   1092 H  HA   . HIS   A 1 45  ? 25.634 6.834   0.417   1.00 11.17 ?  45   HIS   A HA   1 
ATOM   1093 H  HB2  . HIS   A 1 45  ? 26.531 8.228   2.691   1.00 11.23 ?  45   HIS   A HB2  1 
ATOM   1094 H  HB3  . HIS   A 1 45  ? 25.495 7.025   2.682   1.00 11.23 ?  45   HIS   A HB3  1 
ATOM   1095 H  HD2  . HIS   A 1 45  ? 28.866 7.345   3.618   1.00 11.48 ?  45   HIS   A HD2  1 
ATOM   1096 H  HE1  . HIS   A 1 45  ? 28.753 3.657   2.194   1.00 11.44 ?  45   HIS   A HE1  1 
ATOM   1097 H  HE2  . HIS   A 1 45  ? 30.018 5.219   3.442   1.00 11.64 ?  45   HIS   A HE2  1 
ATOM   1098 N  N    A GLY   A 1 46  ? 24.422 8.846   -0.562  0.50 10.70 ?  46   GLY   A N    1 
ATOM   1099 N  N    B GLY   A 1 46  ? 24.440 8.862   -0.568  0.50 10.53 ?  46   GLY   A N    1 
ATOM   1100 C  CA   A GLY   A 1 46  ? 23.599 9.985   -0.918  0.50 11.54 ?  46   GLY   A CA   1 
ATOM   1101 C  CA   B GLY   A 1 46  ? 23.645 10.028  -0.910  0.50 11.12 ?  46   GLY   A CA   1 
ATOM   1102 C  C    A GLY   A 1 46  ? 22.115 9.825   -0.648  0.50 11.64 ?  46   GLY   A C    1 
ATOM   1103 C  C    B GLY   A 1 46  ? 22.171 9.944   -0.561  0.50 10.91 ?  46   GLY   A C    1 
ATOM   1104 O  O    A GLY   A 1 46  ? 21.450 10.783  -0.240  0.50 12.75 ?  46   GLY   A O    1 
ATOM   1105 O  O    B GLY   A 1 46  ? 21.539 10.965  -0.271  0.50 12.35 ?  46   GLY   A O    1 
ATOM   1106 H  H    A GLY   A 1 46  ? 24.488 8.249   -1.176  0.50 12.86 ?  46   GLY   A H    1 
ATOM   1107 H  H    B GLY   A 1 46  ? 24.499 8.270   -1.188  0.50 12.66 ?  46   GLY   A H    1 
ATOM   1108 H  HA2  A GLY   A 1 46  ? 23.898 10.760  -0.420  0.50 13.87 ?  46   GLY   A HA2  1 
ATOM   1109 H  HA2  B GLY   A 1 46  ? 24.018 10.805  -0.457  0.50 13.37 ?  46   GLY   A HA2  1 
ATOM   1110 H  HA3  A GLY   A 1 46  ? 23.716 10.173  -1.862  0.50 13.87 ?  46   GLY   A HA3  1 
ATOM   1111 H  HA3  B GLY   A 1 46  ? 23.708 10.183  -1.863  0.50 13.37 ?  46   GLY   A HA3  1 
ATOM   1112 N  N    A GLY   A 1 47  ? 21.580 8.628   -0.877  0.50 11.12 ?  47   GLY   A N    1 
ATOM   1113 N  N    B GLY   A 1 47  ? 21.605 8.745   -0.616  0.50 10.32 ?  47   GLY   A N    1 
ATOM   1114 C  CA   A GLY   A 1 47  ? 20.150 8.415   -0.804  0.50 10.48 ?  47   GLY   A CA   1 
ATOM   1115 C  CA   B GLY   A 1 47  ? 20.185 8.562   -0.411  0.50 10.51 ?  47   GLY   A CA   1 
ATOM   1116 C  C    A GLY   A 1 47  ? 19.840 6.983   -0.428  0.50 10.36 ?  47   GLY   A C    1 
ATOM   1117 C  C    B GLY   A 1 47  ? 19.861 7.114   -0.104  0.50 10.44 ?  47   GLY   A C    1 
ATOM   1118 O  O    A GLY   A 1 47  ? 20.738 6.162   -0.234  0.50 10.08 ?  47   GLY   A O    1 
ATOM   1119 O  O    B GLY   A 1 47  ? 20.752 6.279   0.070   0.50 10.55 ?  47   GLY   A O    1 
ATOM   1120 H  H    A GLY   A 1 47  ? 22.031 7.917   -1.060  0.50 13.37 ?  47   GLY   A H    1 
ATOM   1121 H  H    B GLY   A 1 47  ? 22.033 8.026   -0.777  0.50 12.41 ?  47   GLY   A H    1 
ATOM   1122 H  HA2  A GLY   A 1 47  ? 19.757 9.006   -0.142  0.50 12.60 ?  47   GLY   A HA2  1 
ATOM   1123 H  HA2  B GLY   A 1 47  ? 19.884 9.111   0.332   0.50 12.64 ?  47   GLY   A HA2  1 
ATOM   1124 H  HA3  A GLY   A 1 47  ? 19.744 8.593   -1.665  0.50 12.60 ?  47   GLY   A HA3  1 
ATOM   1125 H  HA3  B GLY   A 1 47  ? 19.702 8.839   -1.211  0.50 12.64 ?  47   GLY   A HA3  1 
ATOM   1126 N  N    A GLY   A 1 48  ? 18.549 6.681   -0.338  0.50 10.47 ?  48   GLY   A N    1 
ATOM   1127 N  N    B GLY   A 1 48  ? 18.565 6.821   -0.038  0.50 10.98 ?  48   GLY   A N    1 
ATOM   1128 C  CA   A GLY   A 1 48  ? 18.170 5.348   0.076   0.50 11.05 ?  48   GLY   A CA   1 
ATOM   1129 C  CA   B GLY   A 1 48  ? 18.140 5.476   0.299   0.50 11.18 ?  48   GLY   A CA   1 
ATOM   1130 C  C    A GLY   A 1 48  ? 18.646 5.053   1.485   0.50 10.36 ?  48   GLY   A C    1 
ATOM   1131 C  C    B GLY   A 1 48  ? 18.640 5.069   1.673   0.50 10.68 ?  48   GLY   A C    1 
ATOM   1132 O  O    A GLY   A 1 48  ? 18.836 5.955   2.311   0.50 10.41 ?  48   GLY   A O    1 
ATOM   1133 O  O    B GLY   A 1 48  ? 18.796 5.894   2.583   0.50 11.15 ?  48   GLY   A O    1 
ATOM   1134 H  H    A GLY   A 1 48  ? 17.894 7.215   -0.502  0.50 12.59 ?  48   GLY   A H    1 
ATOM   1135 H  H    B GLY   A 1 48  ? 17.923 7.376   -0.180  0.50 13.20 ?  48   GLY   A H    1 
ATOM   1136 H  HA2  A GLY   A 1 48  ? 17.207 5.251   0.047   0.50 13.29 ?  48   GLY   A HA2  1 
ATOM   1137 H  HA2  B GLY   A 1 48  ? 17.172 5.423   0.291   0.50 13.44 ?  48   GLY   A HA2  1 
ATOM   1138 H  HA3  A GLY   A 1 48  ? 18.569 4.695   -0.518  0.50 13.29 ?  48   GLY   A HA3  1 
ATOM   1139 H  HA3  B GLY   A 1 48  ? 18.490 4.846   -0.354  0.50 13.44 ?  48   GLY   A HA3  1 
ATOM   1140 N  N    A VAL   A 1 49  ? 18.850 3.763   1.763   0.50 10.02 ?  49   VAL   A N    1 
ATOM   1141 N  N    B VAL   A 1 49  ? 18.895 3.768   1.824   0.50 9.99  ?  49   VAL   A N    1 
ATOM   1142 C  CA   A VAL   A 1 49  ? 19.342 3.351   3.075   0.50 10.17 ?  49   VAL   A CA   1 
ATOM   1143 C  CA   B VAL   A 1 49  ? 19.464 3.257   3.068   0.50 9.79  ?  49   VAL   A CA   1 
ATOM   1144 C  C    A VAL   A 1 49  ? 20.658 4.046   3.401   0.50 9.36  ?  49   VAL   A C    1 
ATOM   1145 C  C    B VAL   A 1 49  ? 20.728 4.024   3.429   0.50 9.10  ?  49   VAL   A C    1 
ATOM   1146 O  O    A VAL   A 1 49  ? 20.889 4.461   4.541   0.50 9.72  ?  49   VAL   A O    1 
ATOM   1147 O  O    B VAL   A 1 49  ? 20.916 4.446   4.575   0.50 9.43  ?  49   VAL   A O    1 
ATOM   1148 C  CB   A VAL   A 1 49  ? 19.483 1.817   3.128   0.50 10.80 ?  49   VAL   A CB   1 
ATOM   1149 C  CB   B VAL   A 1 49  ? 19.750 1.749   2.944   0.50 9.44  ?  49   VAL   A CB   1 
ATOM   1150 C  CG1  A VAL   A 1 49  ? 20.212 1.382   4.396   0.50 11.20 ?  49   VAL   A CG1  1 
ATOM   1151 C  CG1  B VAL   A 1 49  ? 20.589 1.275   4.123   0.50 8.59  ?  49   VAL   A CG1  1 
ATOM   1152 C  CG2  A VAL   A 1 49  ? 18.116 1.153   3.041   0.50 12.34 ?  49   VAL   A CG2  1 
ATOM   1153 C  CG2  B VAL   A 1 49  ? 18.456 0.952   2.841   0.50 10.28 ?  49   VAL   A CG2  1 
ATOM   1154 H  H    A VAL   A 1 49  ? 18.712 3.114   1.217   0.50 12.05 ?  49   VAL   A H    1 
ATOM   1155 H  H    B VAL   A 1 49  ? 18.749 3.167   1.228   0.50 12.01 ?  49   VAL   A H    1 
ATOM   1156 H  HA   A VAL   A 1 49  ? 18.696 3.604   3.751   0.50 12.22 ?  49   VAL   A HA   1 
ATOM   1157 H  HA   B VAL   A 1 49  ? 18.825 3.378   3.786   0.50 11.77 ?  49   VAL   A HA   1 
ATOM   1158 H  HB   A VAL   A 1 49  ? 20.012 1.518   2.371   0.50 12.99 ?  49   VAL   A HB   1 
ATOM   1159 H  HB   B VAL   A 1 49  ? 20.263 1.590   2.136   0.50 11.35 ?  49   VAL   A HB   1 
ATOM   1160 H  HG11 A VAL   A 1 49  ? 20.059 0.434   4.539   0.50 13.46 ?  49   VAL   A HG11 1 
ATOM   1161 H  HG11 B VAL   A 1 49  ? 20.509 0.311   4.201   0.50 10.33 ?  49   VAL   A HG11 1 
ATOM   1162 H  HG12 A VAL   A 1 49  ? 21.162 1.549   4.295   0.50 13.46 ?  49   VAL   A HG12 1 
ATOM   1163 H  HG12 B VAL   A 1 49  ? 21.520 1.513   3.972   0.50 10.33 ?  49   VAL   A HG12 1 
ATOM   1164 H  HG13 A VAL   A 1 49  ? 19.863 1.886   5.149   0.50 13.46 ?  49   VAL   A HG13 1 
ATOM   1165 H  HG13 B VAL   A 1 49  ? 20.267 1.698   4.934   0.50 10.33 ?  49   VAL   A HG13 1 
ATOM   1166 H  HG21 A VAL   A 1 49  ? 18.229 0.191   3.087   0.50 14.84 ?  49   VAL   A HG21 1 
ATOM   1167 H  HG21 B VAL   A 1 49  ? 18.667 0.011   2.740   0.50 12.36 ?  49   VAL   A HG21 1 
ATOM   1168 H  HG22 A VAL   A 1 49  ? 17.573 1.460   3.783   0.50 14.84 ?  49   VAL   A HG22 1 
ATOM   1169 H  HG22 B VAL   A 1 49  ? 17.937 1.088   3.652   0.50 12.36 ?  49   VAL   A HG22 1 
ATOM   1170 H  HG23 A VAL   A 1 49  ? 17.704 1.401   2.201   0.50 14.84 ?  49   VAL   A HG23 1 
ATOM   1171 H  HG23 B VAL   A 1 49  ? 17.953 1.264   2.073   0.50 12.36 ?  49   VAL   A HG23 1 
ATOM   1172 N  N    A ALA   A 1 50  ? 21.559 4.133   2.422   0.50 9.02  ?  50   ALA   A N    1 
ATOM   1173 N  N    B ALA   A 1 50  ? 21.636 4.165   2.464   0.50 8.87  ?  50   ALA   A N    1 
ATOM   1174 C  CA   A ALA   A 1 50  ? 22.882 4.690   2.681   0.50 9.04  ?  50   ALA   A CA   1 
ATOM   1175 C  CA   B ALA   A 1 50  ? 22.949 4.723   2.760   0.50 9.03  ?  50   ALA   A CA   1 
ATOM   1176 C  C    A ALA   A 1 50  ? 22.789 6.148   3.097   0.50 8.92  ?  50   ALA   A C    1 
ATOM   1177 C  C    B ALA   A 1 50  ? 22.839 6.172   3.202   0.50 8.72  ?  50   ALA   A C    1 
ATOM   1178 O  O    A ALA   A 1 50  ? 23.461 6.581   4.040   0.50 9.06  ?  50   ALA   A O    1 
ATOM   1179 O  O    B ALA   A 1 50  ? 23.415 6.570   4.221   0.50 8.66  ?  50   ALA   A O    1 
ATOM   1180 C  CB   A ALA   A 1 50  ? 23.754 4.553   1.437   0.50 8.95  ?  50   ALA   A CB   1 
ATOM   1181 C  CB   B ALA   A 1 50  ? 23.850 4.599   1.534   0.50 8.81  ?  50   ALA   A CB   1 
ATOM   1182 H  H    A ALA   A 1 50  ? 21.433 3.870   1.616   0.50 10.85 ?  50   ALA   A H    1 
ATOM   1183 H  H    B ALA   A 1 50  ? 21.517 3.943   1.641   0.50 10.66 ?  50   ALA   A H    1 
ATOM   1184 H  HA   A ALA   A 1 50  ? 23.299 4.203   3.408   0.50 10.87 ?  50   ALA   A HA   1 
ATOM   1185 H  HA   B ALA   A 1 50  ? 23.352 4.226   3.486   0.50 10.85 ?  50   ALA   A HA   1 
ATOM   1186 H  HB1  A ALA   A 1 50  ? 24.626 4.934   1.625   0.50 10.76 ?  50   ALA   A HB1  1 
ATOM   1187 H  HB1  B ALA   A 1 50  ? 24.719 4.975   1.741   0.50 10.60 ?  50   ALA   A HB1  1 
ATOM   1188 H  HB2  A ALA   A 1 50  ? 23.838 3.616   1.216   0.50 10.76 ?  50   ALA   A HB2  1 
ATOM   1189 H  HB2  B ALA   A 1 50  ? 23.942 3.660   1.304   0.50 10.60 ?  50   ALA   A HB2  1 
ATOM   1190 H  HB3  A ALA   A 1 50  ? 23.333 5.034   0.707   0.50 10.76 ?  50   ALA   A HB3  1 
ATOM   1191 H  HB3  B ALA   A 1 50  ? 23.447 5.082   0.795   0.50 10.60 ?  50   ALA   A HB3  1 
ATOM   1192 N  N    A GLY   A 1 51  ? 21.980 6.929   2.387   0.50 9.11  ?  51   GLY   A N    1 
ATOM   1193 N  N    B GLY   A 1 51  ? 22.104 6.982   2.442   0.50 8.85  ?  51   GLY   A N    1 
ATOM   1194 C  CA   A GLY   A 1 51  ? 21.807 8.320   2.764   0.50 9.48  ?  51   GLY   A CA   1 
ATOM   1195 C  CA   B GLY   A 1 51  ? 21.933 8.369   2.831   0.50 8.89  ?  51   GLY   A CA   1 
ATOM   1196 C  C    A GLY   A 1 51  ? 21.227 8.472   4.155   0.50 9.25  ?  51   GLY   A C    1 
ATOM   1197 C  C    B GLY   A 1 51  ? 21.278 8.505   4.190   0.50 9.37  ?  51   GLY   A C    1 
ATOM   1198 O  O    A GLY   A 1 51  ? 21.637 9.351   4.916   0.50 9.64  ?  51   GLY   A O    1 
ATOM   1199 O  O    B GLY   A 1 51  ? 21.609 9.409   4.962   0.50 10.02 ?  51   GLY   A O    1 
ATOM   1200 H  H    A GLY   A 1 51  ? 21.536 6.685   1.693   0.50 10.95 ?  51   GLY   A H    1 
ATOM   1201 H  H    B GLY   A 1 51  ? 21.705 6.756   1.712   0.50 10.65 ?  51   GLY   A H    1 
ATOM   1202 H  HA2  A GLY   A 1 51  ? 22.662 8.773   2.741   0.50 11.40 ?  51   GLY   A HA2  1 
ATOM   1203 H  HA2  B GLY   A 1 51  ? 22.795 8.807   2.859   0.50 10.69 ?  51   GLY   A HA2  1 
ATOM   1204 H  HA3  A GLY   A 1 51  ? 21.208 8.756   2.137   0.50 11.40 ?  51   GLY   A HA3  1 
ATOM   1205 H  HA3  B GLY   A 1 51  ? 21.376 8.822   2.177   0.50 10.69 ?  51   GLY   A HA3  1 
ATOM   1206 N  N    A ALA   A 1 52  ? 20.252 7.627   4.499   0.50 9.21  ?  52   ALA   A N    1 
ATOM   1207 N  N    B ALA   A 1 52  ? 20.334 7.613   4.497   0.50 9.58  ?  52   ALA   A N    1 
ATOM   1208 C  CA   A ALA   A 1 52  ? 19.610 7.719   5.806   0.50 9.85  ?  52   ALA   A CA   1 
ATOM   1209 C  CA   B ALA   A 1 52  ? 19.647 7.660   5.783   0.50 10.10 ?  52   ALA   A CA   1 
ATOM   1210 C  C    A ALA   A 1 52  ? 20.552 7.292   6.928   0.50 9.50  ?  52   ALA   A C    1 
ATOM   1211 C  C    B ALA   A 1 52  ? 20.573 7.249   6.924   0.50 9.80  ?  52   ALA   A C    1 
ATOM   1212 O  O    A ALA   A 1 52  ? 20.616 7.951   7.972   0.50 10.22 ?  52   ALA   A O    1 
ATOM   1213 O  O    B ALA   A 1 52  ? 20.633 7.923   7.958   0.50 10.39 ?  52   ALA   A O    1 
ATOM   1214 C  CB   A ALA   A 1 52  ? 18.326 6.889   5.815   0.50 11.37 ?  52   ALA   A CB   1 
ATOM   1215 C  CB   B ALA   A 1 52  ? 18.399 6.776   5.735   0.50 11.26 ?  52   ALA   A CB   1 
ATOM   1216 H  H    A ALA   A 1 52  ? 19.954 6.992   3.997   0.50 11.07 ?  52   ALA   A H    1 
ATOM   1217 H  H    B ALA   A 1 52  ? 20.083 6.969   3.982   0.50 11.51 ?  52   ALA   A H    1 
ATOM   1218 H  HA   A ALA   A 1 52  ? 19.366 8.638   5.964   0.50 11.85 ?  52   ALA   A HA   1 
ATOM   1219 H  HA   B ALA   A 1 52  ? 19.360 8.567   5.948   0.50 12.15 ?  52   ALA   A HA   1 
ATOM   1220 H  HB1  A ALA   A 1 52  ? 17.901 6.973   6.684   0.50 13.67 ?  52   ALA   A HB1  1 
ATOM   1221 H  HB1  B ALA   A 1 52  ? 17.931 6.844   6.583   0.50 13.53 ?  52   ALA   A HB1  1 
ATOM   1222 H  HB2  A ALA   A 1 52  ? 17.731 7.222   5.124   0.50 13.67 ?  52   ALA   A HB2  1 
ATOM   1223 H  HB2  B ALA   A 1 52  ? 17.823 7.084   5.016   0.50 13.53 ?  52   ALA   A HB2  1 
ATOM   1224 H  HB3  A ALA   A 1 52  ? 18.543 5.959   5.642   0.50 13.67 ?  52   ALA   A HB3  1 
ATOM   1225 H  HB3  B ALA   A 1 52  ? 18.663 5.857   5.575   0.50 13.53 ?  52   ALA   A HB3  1 
ATOM   1226 N  N    A LEU   A 1 53  ? 21.290 6.194   6.743   0.50 9.20  ?  53   LEU   A N    1 
ATOM   1227 N  N    B LEU   A 1 53  ? 21.303 6.141   6.763   0.50 9.49  ?  53   LEU   A N    1 
ATOM   1228 C  CA   A LEU   A 1 53  ? 22.243 5.783   7.771   0.50 9.66  ?  53   LEU   A CA   1 
ATOM   1229 C  CA   B LEU   A 1 53  ? 22.277 5.759   7.784   0.50 9.62  ?  53   LEU   A CA   1 
ATOM   1230 C  C    A LEU   A 1 53  ? 23.316 6.840   7.963   0.50 9.36  ?  53   LEU   A C    1 
ATOM   1231 C  C    B LEU   A 1 53  ? 23.293 6.870   7.989   0.50 9.42  ?  53   LEU   A C    1 
ATOM   1232 O  O    A LEU   A 1 53  ? 23.686 7.159   9.095   0.50 9.64  ?  53   LEU   A O    1 
ATOM   1233 O  O    B LEU   A 1 53  ? 23.569 7.274   9.122   0.50 10.18 ?  53   LEU   A O    1 
ATOM   1234 C  CB   A LEU   A 1 53  ? 22.886 4.442   7.411   0.50 9.90  ?  53   LEU   A CB   1 
ATOM   1235 C  CB   B LEU   A 1 53  ? 22.994 4.462   7.399   0.50 9.46  ?  53   LEU   A CB   1 
ATOM   1236 C  CG   A LEU   A 1 53  ? 21.978 3.211   7.450   0.50 10.25 ?  53   LEU   A CG   1 
ATOM   1237 C  CG   B LEU   A 1 53  ? 22.231 3.137   7.467   0.50 9.75  ?  53   LEU   A CG   1 
ATOM   1238 C  CD1  A LEU   A 1 53  ? 22.722 2.008   6.911   0.50 10.28 ?  53   LEU   A CD1  1 
ATOM   1239 C  CD1  B LEU   A 1 53  ? 23.061 2.043   6.813   0.50 10.55 ?  53   LEU   A CD1  1 
ATOM   1240 C  CD2  A LEU   A 1 53  ? 21.462 2.929   8.858   0.50 10.48 ?  53   LEU   A CD2  1 
ATOM   1241 C  CD2  B LEU   A 1 53  ? 21.881 2.748   8.901   0.50 10.08 ?  53   LEU   A CD2  1 
ATOM   1242 H  H    A LEU   A 1 53  ? 21.264 5.683   6.051   0.50 11.07 ?  53   LEU   A H    1 
ATOM   1243 H  H    B LEU   A 1 53  ? 21.260 5.606   6.090   0.50 11.41 ?  53   LEU   A H    1 
ATOM   1244 H  HA   A LEU   A 1 53  ? 21.775 5.672   8.614   0.50 11.61 ?  53   LEU   A HA   1 
ATOM   1245 H  HA   B LEU   A 1 53  ? 21.820 5.612   8.625   0.50 11.56 ?  53   LEU   A HA   1 
ATOM   1246 H  HB2  A LEU   A 1 53  ? 23.241 4.506   6.510   0.50 11.91 ?  53   LEU   A HB2  1 
ATOM   1247 H  HB2  B LEU   A 1 53  ? 23.303 4.555   6.486   0.50 11.38 ?  53   LEU   A HB2  1 
ATOM   1248 H  HB3  A LEU   A 1 53  ? 23.616 4.274   8.029   0.50 11.91 ?  53   LEU   A HB3  1 
ATOM   1249 H  HB3  B LEU   A 1 53  ? 23.764 4.365   7.982   0.50 11.38 ?  53   LEU   A HB3  1 
ATOM   1250 H  HG   A LEU   A 1 53  ? 21.211 3.365   6.874   0.50 12.32 ?  53   LEU   A HG   1 
ATOM   1251 H  HG   B LEU   A 1 53  ? 21.404 3.217   6.967   0.50 11.73 ?  53   LEU   A HG   1 
ATOM   1252 H  HD11 A LEU   A 1 53  ? 22.139 1.234   6.941   0.50 12.36 ?  53   LEU   A HD11 1 
ATOM   1253 H  HD11 B LEU   A 1 53  ? 22.578 1.202   6.866   0.50 12.68 ?  53   LEU   A HD11 1 
ATOM   1254 H  HD12 A LEU   A 1 53  ? 22.990 2.186   5.996   0.50 12.36 ?  53   LEU   A HD12 1 
ATOM   1255 H  HD12 B LEU   A 1 53  ? 23.217 2.276   5.885   0.50 12.68 ?  53   LEU   A HD12 1 
ATOM   1256 H  HD13 A LEU   A 1 53  ? 23.507 1.853   7.461   0.50 12.36 ?  53   LEU   A HD13 1 
ATOM   1257 H  HD13 B LEU   A 1 53  ? 23.908 1.966   7.281   0.50 12.68 ?  53   LEU   A HD13 1 
ATOM   1258 H  HD21 A LEU   A 1 53  ? 20.917 2.128   8.840   0.50 12.60 ?  53   LEU   A HD21 1 
ATOM   1259 H  HD21 B LEU   A 1 53  ? 21.363 1.928   8.891   0.50 12.12 ?  53   LEU   A HD21 1 
ATOM   1260 H  HD22 A LEU   A 1 53  ? 22.220 2.801   9.448   0.50 12.60 ?  53   LEU   A HD22 1 
ATOM   1261 H  HD22 B LEU   A 1 53  ? 22.700 2.616   9.403   0.50 12.12 ?  53   LEU   A HD22 1 
ATOM   1262 H  HD23 A LEU   A 1 53  ? 20.932 3.683   9.157   0.50 12.60 ?  53   LEU   A HD23 1 
ATOM   1263 H  HD23 B LEU   A 1 53  ? 21.360 3.462   9.302   0.50 12.12 ?  53   LEU   A HD23 1 
ATOM   1264 N  N    A ASN   A 1 54  ? 23.832 7.392   6.868   0.50 9.16  ?  54   ASN   A N    1 
ATOM   1265 N  N    B ASN   A 1 54  ? 23.856 7.384   6.896   0.50 9.11  ?  54   ASN   A N    1 
ATOM   1266 C  CA   A ASN   A 1 54  ? 24.885 8.388   6.997   0.50 9.43  ?  54   ASN   A CA   1 
ATOM   1267 C  CA   B ASN   A 1 54  ? 24.897 8.391   7.039   0.50 8.91  ?  54   ASN   A CA   1 
ATOM   1268 C  C    A ASN   A 1 54  ? 24.377 9.635   7.715   0.50 9.69  ?  54   ASN   A C    1 
ATOM   1269 C  C    B ASN   A 1 54  ? 24.367 9.633   7.746   0.50 9.41  ?  54   ASN   A C    1 
ATOM   1270 O  O    A ASN   A 1 54  ? 25.076 10.202  8.564   0.50 10.17 ?  54   ASN   A O    1 
ATOM   1271 O  O    B ASN   A 1 54  ? 25.039 10.194  8.620   0.50 9.64  ?  54   ASN   A O    1 
ATOM   1272 C  CB   A ASN   A 1 54  ? 25.445 8.742   5.627   0.50 9.78  ?  54   ASN   A CB   1 
ATOM   1273 C  CB   B ASN   A 1 54  ? 25.485 8.756   5.685   0.50 8.77  ?  54   ASN   A CB   1 
ATOM   1274 C  CG   A ASN   A 1 54  ? 26.492 9.814   5.712   0.50 10.50 ?  54   ASN   A CG   1 
ATOM   1275 C  CG   B ASN   A 1 54  ? 26.469 9.884   5.800   0.50 8.69  ?  54   ASN   A CG   1 
ATOM   1276 O  OD1  A ASN   A 1 54  ? 27.520 9.633   6.367   0.50 11.11 ?  54   ASN   A OD1  1 
ATOM   1277 O  OD1  B ASN   A 1 54  ? 27.469 9.767   6.518   0.50 8.32  ?  54   ASN   A OD1  1 
ATOM   1278 N  ND2  A ASN   A 1 54  ? 26.241 10.948  5.073   0.50 11.02 ?  54   ASN   A ND2  1 
ATOM   1279 N  ND2  B ASN   A 1 54  ? 26.187 10.998  5.136   0.50 9.74  ?  54   ASN   A ND2  1 
ATOM   1280 H  H    A ASN   A 1 54  ? 23.591 7.208   6.062   0.50 11.01 ?  54   ASN   A H    1 
ATOM   1281 H  H    B ASN   A 1 54  ? 23.652 7.174   6.087   0.50 10.96 ?  54   ASN   A H    1 
ATOM   1282 H  HA   A ASN   A 1 54  ? 25.600 8.012   7.529   0.50 11.33 ?  54   ASN   A HA   1 
ATOM   1283 H  HA   B ASN   A 1 54  ? 25.605 8.025   7.583   0.50 10.72 ?  54   ASN   A HA   1 
ATOM   1284 H  HB2  A ASN   A 1 54  ? 25.855 7.950   5.243   0.50 11.76 ?  54   ASN   A HB2  1 
ATOM   1285 H  HB2  B ASN   A 1 54  ? 25.954 7.983   5.326   0.50 10.55 ?  54   ASN   A HB2  1 
ATOM   1286 H  HB3  A ASN   A 1 54  ? 24.728 9.058   5.061   0.50 11.76 ?  54   ASN   A HB3  1 
ATOM   1287 H  HB3  B ASN   A 1 54  ? 24.775 9.025   5.086   0.50 10.55 ?  54   ASN   A HB3  1 
ATOM   1288 H  HD21 A ASN   A 1 54  ? 26.809 11.592  5.104   0.50 13.25 ?  54   ASN   A HD21 1 
ATOM   1289 H  HD21 B ASN   A 1 54  ? 26.717 11.675  5.184   0.50 11.71 ?  54   ASN   A HD21 1 
ATOM   1290 H  HD22 A ASN   A 1 54  ? 25.511 11.038  4.628   0.50 13.25 ?  54   ASN   A HD22 1 
ATOM   1291 H  HD22 B ASN   A 1 54  ? 25.477 11.043  4.651   0.50 11.71 ?  54   ASN   A HD22 1 
ATOM   1292 N  N    . LYS   A 1 55  ? 23.161 10.082  7.383   1.00 9.65  ?  55   LYS   A N    1 
ATOM   1293 C  CA   . LYS   A 1 55  ? 22.579 11.240  8.051   1.00 10.11 ?  55   LYS   A CA   1 
ATOM   1294 C  C    . LYS   A 1 55  ? 22.478 11.012  9.551   1.00 10.42 ?  55   LYS   A C    1 
ATOM   1295 O  O    . LYS   A 1 55  ? 22.758 11.916  10.348  1.00 10.95 ?  55   LYS   A O    1 
ATOM   1296 C  CB   . LYS   A 1 55  ? 21.206 11.539  7.435   1.00 10.82 ?  55   LYS   A CB   1 
ATOM   1297 C  CG   . LYS   A 1 55  ? 20.471 12.720  8.044   1.00 12.17 ?  55   LYS   A CG   1 
ATOM   1298 C  CD   . LYS   A 1 55  ? 19.141 12.956  7.323   1.00 13.47 ?  55   LYS   A CD   1 
ATOM   1299 C  CE   . LYS   A 1 55  ? 18.309 14.040  7.985   1.00 15.84 ?  55   LYS   A CE   1 
ATOM   1300 N  NZ   . LYS   A 1 55  ? 16.969 14.168  7.351   1.00 16.74 ?  55   LYS   A NZ   1 
ATOM   1301 H  H    A LYS   A 1 55  ? 22.654 9.730   6.778   0.50 11.60 ?  55   LYS   A H    1 
ATOM   1302 H  H    B LYS   A 1 55  ? 22.661 9.730   6.772   0.50 11.60 ?  55   LYS   A H    1 
ATOM   1303 H  HA   . LYS   A 1 55  ? 23.142 12.009  7.902   1.00 12.16 ?  55   LYS   A HA   1 
ATOM   1304 H  HB2  . LYS   A 1 55  ? 21.322 11.731  6.492   1.00 13.00 ?  55   LYS   A HB2  1 
ATOM   1305 H  HB3  . LYS   A 1 55  ? 20.636 10.763  7.542   1.00 13.00 ?  55   LYS   A HB3  1 
ATOM   1306 H  HG2  . LYS   A 1 55  ? 20.282 12.542  8.978   1.00 14.63 ?  55   LYS   A HG2  1 
ATOM   1307 H  HG3  . LYS   A 1 55  ? 21.012 13.521  7.954   1.00 14.63 ?  55   LYS   A HG3  1 
ATOM   1308 H  HD2  . LYS   A 1 55  ? 19.320 13.224  6.406   1.00 16.19 ?  55   LYS   A HD2  1 
ATOM   1309 H  HD3  . LYS   A 1 55  ? 18.627 12.129  7.329   1.00 16.19 ?  55   LYS   A HD3  1 
ATOM   1310 H  HE2  . LYS   A 1 55  ? 18.180 13.818  8.919   1.00 19.04 ?  55   LYS   A HE2  1 
ATOM   1311 H  HE3  . LYS   A 1 55  ? 18.766 14.890  7.899   1.00 19.04 ?  55   LYS   A HE3  1 
ATOM   1312 H  HZ1  . LYS   A 1 55  ? 16.386 14.506  7.934   1.00 20.11 ?  55   LYS   A HZ1  1 
ATOM   1313 H  HZ2  . LYS   A 1 55  ? 17.013 14.710  6.645   1.00 20.11 ?  55   LYS   A HZ2  1 
ATOM   1314 H  HZ3  . LYS   A 1 55  ? 16.676 13.369  7.085   1.00 20.11 ?  55   LYS   A HZ3  1 
ATOM   1315 N  N    . ALA   A 1 56  ? 22.089 9.801   9.958   1.00 10.64 ?  56   ALA   A N    1 
ATOM   1316 C  CA   . ALA   A 1 56  ? 21.960 9.490   11.373  1.00 11.17 ?  56   ALA   A CA   1 
ATOM   1317 C  C    . ALA   A 1 56  ? 23.299 9.506   12.098  1.00 11.44 ?  56   ALA   A C    1 
ATOM   1318 O  O    . ALA   A 1 56  ? 23.318 9.686   13.318  1.00 12.73 ?  56   ALA   A O    1 
ATOM   1319 C  CB   . ALA   A 1 56  ? 21.252 8.144   11.561  1.00 12.21 ?  56   ALA   A CB   1 
ATOM   1320 H  H    . ALA   A 1 56  ? 21.905 9.150   9.433   1.00 12.80 ?  56   ALA   A H    1 
ATOM   1321 H  HA   . ALA   A 1 56  ? 21.412 10.164  11.789  1.00 13.42 ?  56   ALA   A HA   1 
ATOM   1322 H  HB1  . ALA   A 1 56  ? 21.181 7.952   12.512  1.00 14.68 ?  56   ALA   A HB1  1 
ATOM   1323 H  HB2  . ALA   A 1 56  ? 20.364 8.201   11.172  1.00 14.68 ?  56   ALA   A HB2  1 
ATOM   1324 H  HB3  . ALA   A 1 56  ? 21.762 7.448   11.122  1.00 14.68 ?  56   ALA   A HB3  1 
ATOM   1325 N  N    . THR   A 1 57  ? 24.414 9.320   11.384  1.00 10.50 ?  57   THR   A N    1 
ATOM   1326 C  CA   . THR   A 1 57  ? 25.753 9.450   11.963  1.00 10.52 ?  57   THR   A CA   1 
ATOM   1327 C  C    . THR   A 1 57  ? 26.304 10.868  11.883  1.00 10.88 ?  57   THR   A C    1 
ATOM   1328 O  O    . THR   A 1 57  ? 27.490 11.077  12.176  1.00 11.55 ?  57   THR   A O    1 
ATOM   1329 C  CB   . THR   A 1 57  ? 26.766 8.503   11.295  1.00 10.47 ?  57   THR   A CB   1 
ATOM   1330 O  OG1  . THR   A 1 57  ? 27.158 9.000   10.003  1.00 10.22 ?  57   THR   A OG1  1 
ATOM   1331 C  CG2  . THR   A 1 57  ? 26.239 7.081   11.182  1.00 10.90 ?  57   THR   A CG2  1 
ATOM   1332 H  H    . THR   A 1 57  ? 24.424 9.102   10.550  1.00 12.62 ?  57   THR   A H    1 
ATOM   1333 H  HA   . THR   A 1 57  ? 25.706 9.195   12.905  1.00 12.65 ?  57   THR   A HA   1 
ATOM   1334 H  HB   . THR   A 1 57  ? 27.559 8.462   11.858  1.00 12.58 ?  57   THR   A HB   1 
ATOM   1335 H  HG1  . THR   A 1 57  ? 26.482 9.082   9.515   1.00 12.28 ?  57   THR   A HG1  1 
ATOM   1336 H  HG21 . THR   A 1 57  ? 26.909 6.504   10.776  1.00 13.11 ?  57   THR   A HG21 1 
ATOM   1337 H  HG22 . THR   A 1 57  ? 26.017 6.730   12.058  1.00 13.11 ?  57   THR   A HG22 1 
ATOM   1338 H  HG23 . THR   A 1 57  ? 25.442 7.060   10.629  1.00 13.11 ?  57   THR   A HG23 1 
ATOM   1339 N  N    . ASN   A 1 58  ? 25.495 11.840  11.472  1.00 11.47 ?  58   ASN   A N    1 
ATOM   1340 C  CA   . ASN   A 1 58  ? 25.961 13.221  11.369  1.00 12.40 ?  58   ASN   A CA   1 
ATOM   1341 C  C    . ASN   A 1 58  ? 27.114 13.348  10.367  1.00 11.41 ?  58   ASN   A C    1 
ATOM   1342 O  O    . ASN   A 1 58  ? 28.010 14.179  10.528  1.00 12.22 ?  58   ASN   A O    1 
ATOM   1343 C  CB   . ASN   A 1 58  ? 26.326 13.763  12.762  1.00 15.19 ?  58   ASN   A CB   1 
ATOM   1344 C  CG   . ASN   A 1 58  ? 26.737 15.217  12.751  1.00 19.27 ?  58   ASN   A CG   1 
ATOM   1345 O  OD1  . ASN   A 1 58  ? 26.128 16.037  12.073  1.00 20.85 ?  58   ASN   A OD1  1 
ATOM   1346 N  ND2  . ASN   A 1 58  ? 27.777 15.548  13.514  1.00 20.74 ?  58   ASN   A ND2  1 
ATOM   1347 H  H    . ASN   A 1 58  ? 24.673 11.715  11.237  1.00 13.78 ?  58   ASN   A H    1 
ATOM   1348 H  HA   . ASN   A 1 58  ? 25.225 13.750  11.034  1.00 14.91 ?  58   ASN   A HA   1 
ATOM   1349 H  HB2  . ASN   A 1 58  ? 25.549 13.668  13.348  1.00 18.25 ?  58   ASN   A HB2  1 
ATOM   1350 H  HB3  . ASN   A 1 58  ? 27.064 13.253  13.123  1.00 18.25 ?  58   ASN   A HB3  1 
ATOM   1351 H  HD21 . ASN   A 1 58  ? 28.039 16.367  13.546  1.00 24.91 ?  58   ASN   A HD21 1 
ATOM   1352 H  HD22 . ASN   A 1 58  ? 28.175 14.947  13.975  1.00 24.91 ?  58   ASN   A HD22 1 
ATOM   1353 N  N    . ASN   A 1 59  ? 27.099 12.524  9.314   1.00 10.22 ?  59   ASN   A N    1 
ATOM   1354 C  CA   . ASN   A 1 59  ? 28.084 12.490  8.225   1.00 10.06 ?  59   ASN   A CA   1 
ATOM   1355 C  C    . ASN   A 1 59  ? 29.397 11.812  8.621   1.00 9.92  ?  59   ASN   A C    1 
ATOM   1356 O  O    . ASN   A 1 59  ? 30.316 11.761  7.797   1.00 10.44 ?  59   ASN   A O    1 
ATOM   1357 C  CB   . ASN   A 1 59  ? 28.372 13.877  7.621   1.00 10.41 ?  59   ASN   A CB   1 
ATOM   1358 C  CG   . ASN   A 1 59  ? 28.738 13.812  6.157   1.00 10.60 ?  59   ASN   A CG   1 
ATOM   1359 O  OD1  . ASN   A 1 59  ? 28.040 13.185  5.358   1.00 10.73 ?  59   ASN   A OD1  1 
ATOM   1360 N  ND2  . ASN   A 1 59  ? 29.834 14.465  5.787   1.00 11.41 ?  59   ASN   A ND2  1 
ATOM   1361 H  H    . ASN   A 1 59  ? 26.479 11.936  9.198   1.00 12.29 ?  59   ASN   A H    1 
ATOM   1362 H  HA   . ASN   A 1 59  ? 27.707 11.956  7.513   1.00 12.10 ?  59   ASN   A HA   1 
ATOM   1363 H  HB2  . ASN   A 1 59  ? 27.580 14.432  7.702   1.00 12.52 ?  59   ASN   A HB2  1 
ATOM   1364 H  HB3  . ASN   A 1 59  ? 29.113 14.285  8.093   1.00 12.52 ?  59   ASN   A HB3  1 
ATOM   1365 H  HD21 . ASN   A 1 59  ? 30.090 14.461  4.965   1.00 13.71 ?  59   ASN   A HD21 1 
ATOM   1366 H  HD22 . ASN   A 1 59  ? 30.303 14.893  6.374   1.00 13.71 ?  59   ASN   A HD22 1 
ATOM   1367 N  N    . ALA   A 1 60  ? 29.517 11.272  9.834   1.00 10.15 ?  60   ALA   A N    1 
ATOM   1368 C  CA   . ALA   A 1 60  ? 30.750 10.582  10.195  1.00 10.23 ?  60   ALA   A CA   1 
ATOM   1369 C  C    . ALA   A 1 60  ? 30.974 9.343   9.334   1.00 10.29 ?  60   ALA   A C    1 
ATOM   1370 O  O    . ALA   A 1 60  ? 32.121 9.019   9.003   1.00 10.80 ?  60   ALA   A O    1 
ATOM   1371 C  CB   . ALA   A 1 60  ? 30.744 10.230  11.680  1.00 11.16 ?  60   ALA   A CB   1 
ATOM   1372 H  H    . ALA   A 1 60  ? 28.914 11.287  10.448  1.00 12.20 ?  60   ALA   A H    1 
ATOM   1373 H  HA   . ALA   A 1 60  ? 31.495 11.188  10.040  1.00 12.30 ?  60   ALA   A HA   1 
ATOM   1374 H  HB1  . ALA   A 1 60  ? 31.572 9.778   11.898  1.00 13.41 ?  60   ALA   A HB1  1 
ATOM   1375 H  HB2  . ALA   A 1 60  ? 30.669 11.051  12.197  1.00 13.41 ?  60   ALA   A HB2  1 
ATOM   1376 H  HB3  . ALA   A 1 60  ? 29.988 9.655   11.863  1.00 13.41 ?  60   ALA   A HB3  1 
ATOM   1377 N  N    . MET   A 1 61  ? 29.901 8.648   8.950   1.00 9.77  ?  61   MET   A N    1 
ATOM   1378 C  CA   . MET   A 1 61  ? 30.044 7.511   8.048   1.00 9.37  ?  61   MET   A CA   1 
ATOM   1379 C  C    . MET   A 1 61  ? 30.678 7.938   6.728   1.00 9.61  ?  61   MET   A C    1 
ATOM   1380 O  O    . MET   A 1 61  ? 31.571 7.257   6.209   1.00 9.82  ?  61   MET   A O    1 
ATOM   1381 C  CB   . MET   A 1 61  ? 28.682 6.852   7.823   1.00 9.51  ?  61   MET   A CB   1 
ATOM   1382 C  CG   . MET   A 1 61  ? 28.702 5.687   6.850   1.00 10.12 ?  61   MET   A CG   1 
ATOM   1383 S  SD   . MET   A 1 61  ? 27.074 4.939   6.650   1.00 10.88 ?  61   MET   A SD   1 
ATOM   1384 C  CE   . MET   A 1 61  ? 26.966 4.033   8.202   1.00 11.69 ?  61   MET   A CE   1 
ATOM   1385 H  H    . MET   A 1 61  ? 29.091 8.820   9.189   1.00 11.74 ?  61   MET   A H    1 
ATOM   1386 H  HA   . MET   A 1 61  ? 30.617 6.855   8.470   1.00 11.27 ?  61   MET   A HA   1 
ATOM   1387 H  HB2  . MET   A 1 61  ? 28.353 6.520   8.672   1.00 11.43 ?  61   MET   A HB2  1 
ATOM   1388 H  HB3  . MET   A 1 61  ? 28.067 7.514   7.472   1.00 11.43 ?  61   MET   A HB3  1 
ATOM   1389 H  HG2  . MET   A 1 61  ? 28.985 5.989   5.975   1.00 12.16 ?  61   MET   A HG2  1 
ATOM   1390 H  HG3  . MET   A 1 61  ? 29.300 4.997   7.178   1.00 12.16 ?  61   MET   A HG3  1 
ATOM   1391 H  HE1  . MET   A 1 61  ? 26.130 3.542   8.228   1.00 14.05 ?  61   MET   A HE1  1 
ATOM   1392 H  HE2  . MET   A 1 61  ? 27.714 3.416   8.259   1.00 14.05 ?  61   MET   A HE2  1 
ATOM   1393 H  HE3  . MET   A 1 61  ? 27.002 4.661   8.943   1.00 14.05 ?  61   MET   A HE3  1 
ATOM   1394 N  N    . GLN   A 1 62  ? 30.240 9.070   6.174   1.00 9.70  ?  62   GLN   A N    1 
ATOM   1395 C  CA   . GLN   A 1 62  ? 30.804 9.533   4.909   1.00 9.69  ?  62   GLN   A CA   1 
ATOM   1396 C  C    . GLN   A 1 62  ? 32.272 9.914   5.053   1.00 9.59  ?  62   GLN   A C    1 
ATOM   1397 O  O    . GLN   A 1 62  ? 33.086 9.597   4.178   1.00 10.18 ?  62   GLN   A O    1 
ATOM   1398 C  CB   . GLN   A 1 62  ? 30.002 10.715  4.370   1.00 10.03 ?  62   GLN   A CB   1 
ATOM   1399 C  CG   . GLN   A 1 62  ? 30.393 11.077  2.942   1.00 9.86  ?  62   GLN   A CG   1 
ATOM   1400 C  CD   . GLN   A 1 62  ? 30.060 9.946   1.991   1.00 10.07 ?  62   GLN   A CD   1 
ATOM   1401 O  OE1  . GLN   A 1 62  ? 28.883 9.639   1.786   1.00 10.37 ?  62   GLN   A OE1  1 
ATOM   1402 N  NE2  . GLN   A 1 62  ? 31.075 9.272   1.465   1.00 10.37 ?  62   GLN   A NE2  1 
ATOM   1403 H  H    . GLN   A 1 62  ? 29.625 9.570   6.502   1.00 11.66 ?  62   GLN   A H    1 
ATOM   1404 H  HA   . GLN   A 1 62  ? 30.750 8.809   4.265   1.00 11.65 ?  62   GLN   A HA   1 
ATOM   1405 H  HB2  . GLN   A 1 62  ? 29.060 10.492  4.380   1.00 12.06 ?  62   GLN   A HB2  1 
ATOM   1406 H  HB3  . GLN   A 1 62  ? 30.168 11.490  4.932   1.00 12.06 ?  62   GLN   A HB3  1 
ATOM   1407 H  HG2  . GLN   A 1 62  ? 29.889 11.860  2.665   1.00 11.86 ?  62   GLN   A HG2  1 
ATOM   1408 H  HG3  . GLN   A 1 62  ? 31.342 11.252  2.897   1.00 11.86 ?  62   GLN   A HG3  1 
ATOM   1409 H  HE21 . GLN   A 1 62  ? 31.886 9.497   1.651   1.00 12.46 ?  62   GLN   A HE21 1 
ATOM   1410 H  HE22 . GLN   A 1 62  ? 30.926 8.612   0.933   1.00 12.46 ?  62   GLN   A HE22 1 
ATOM   1411 N  N    . VAL   A 1 63  ? 32.629 10.603  6.139   1.00 10.20 ?  63   VAL   A N    1 
ATOM   1412 C  CA   . VAL   A 1 63  ? 34.020 10.991  6.355   1.00 11.07 ?  63   VAL   A CA   1 
ATOM   1413 C  C    . VAL   A 1 63  ? 34.913 9.757   6.424   1.00 10.55 ?  63   VAL   A C    1 
ATOM   1414 O  O    . VAL   A 1 63  ? 35.967 9.689   5.778   1.00 11.20 ?  63   VAL   A O    1 
ATOM   1415 C  CB   . VAL   A 1 63  ? 34.125 11.865  7.616   1.00 12.35 ?  63   VAL   A CB   1 
ATOM   1416 C  CG1  . VAL   A 1 63  ? 35.571 12.102  7.989   1.00 14.01 ?  63   VAL   A CG1  1 
ATOM   1417 C  CG2  . VAL   A 1 63  ? 33.409 13.201  7.383   1.00 13.10 ?  63   VAL   A CG2  1 
ATOM   1418 H  H    . VAL   A 1 63  ? 32.084 10.853  6.762   1.00 12.26 ?  63   VAL   A H    1 
ATOM   1419 H  HA   . VAL   A 1 63  ? 34.308 11.524  5.601   1.00 13.31 ?  63   VAL   A HA   1 
ATOM   1420 H  HB   . VAL   A 1 63  ? 33.691 11.421  8.357   1.00 14.85 ?  63   VAL   A HB   1 
ATOM   1421 H  HG11 . VAL   A 1 63  ? 35.616 12.839  8.618   1.00 16.84 ?  63   VAL   A HG11 1 
ATOM   1422 H  HG12 . VAL   A 1 63  ? 35.928 11.299  8.392   1.00 16.84 ?  63   VAL   A HG12 1 
ATOM   1423 H  HG13 . VAL   A 1 63  ? 36.069 12.325  7.186   1.00 16.84 ?  63   VAL   A HG13 1 
ATOM   1424 H  HG21 . VAL   A 1 63  ? 33.495 13.754  8.177   1.00 15.74 ?  63   VAL   A HG21 1 
ATOM   1425 H  HG22 . VAL   A 1 63  ? 33.814 13.655  6.624   1.00 15.74 ?  63   VAL   A HG22 1 
ATOM   1426 H  HG23 . VAL   A 1 63  ? 32.470 13.033  7.201   1.00 15.74 ?  63   VAL   A HG23 1 
ATOM   1427 N  N    . GLU   A 1 64  ? 34.489 8.753   7.192   1.00 10.37 ?  64   GLU   A N    1 
ATOM   1428 C  CA   . GLU   A 1 64  ? 35.250 7.515   7.294   1.00 10.54 ?  64   GLU   A CA   1 
ATOM   1429 C  C    . GLU   A 1 64  ? 35.342 6.826   5.940   1.00 10.17 ?  64   GLU   A C    1 
ATOM   1430 O  O    . GLU   A 1 64  ? 36.393 6.280   5.569   1.00 10.56 ?  64   GLU   A O    1 
ATOM   1431 C  CB   . GLU   A 1 64  ? 34.559 6.609   8.314   1.00 10.95 ?  64   GLU   A CB   1 
ATOM   1432 C  CG   . GLU   A 1 64  ? 35.210 5.258   8.474   1.00 11.71 ?  64   GLU   A CG   1 
ATOM   1433 C  CD   . GLU   A 1 64  ? 34.328 4.253   9.187   1.00 11.78 ?  64   GLU   A CD   1 
ATOM   1434 O  OE1  . GLU   A 1 64  ? 33.088 4.347   9.044   1.00 12.65 ?  64   GLU   A OE1  1 
ATOM   1435 O  OE2  . GLU   A 1 64  ? 34.878 3.363   9.876   1.00 12.19 -1 64   GLU   A OE2  1 
ATOM   1436 H  H    . GLU   A 1 64  ? 33.757 8.757   7.645   1.00 12.47 ?  64   GLU   A H    1 
ATOM   1437 H  HA   . GLU   A 1 64  ? 36.146 7.717   7.609   1.00 12.68 ?  64   GLU   A HA   1 
ATOM   1438 H  HB2  . GLU   A 1 64  ? 34.575 7.054   9.181   1.00 13.17 ?  64   GLU   A HB2  1 
ATOM   1439 H  HB3  . GLU   A 1 64  ? 33.641 6.477   8.034   1.00 13.17 ?  64   GLU   A HB3  1 
ATOM   1440 H  HG2  . GLU   A 1 64  ? 35.424 4.899   7.597   1.00 14.08 ?  64   GLU   A HG2  1 
ATOM   1441 H  HG3  . GLU   A 1 64  ? 36.021 5.366   8.990   1.00 14.08 ?  64   GLU   A HG3  1 
ATOM   1442 N  N    . SER   A 1 65  ? 34.229 6.815   5.204   1.00 9.73  ?  65   SER   A N    1 
ATOM   1443 C  CA   . SER   A 1 65  ? 34.177 6.154   3.906   1.00 9.94  ?  65   SER   A CA   1 
ATOM   1444 C  C    . SER   A 1 65  ? 35.100 6.819   2.898   1.00 10.15 ?  65   SER   A C    1 
ATOM   1445 O  O    . SER   A 1 65  ? 35.740 6.136   2.091   1.00 10.95 ?  65   SER   A O    1 
ATOM   1446 C  CB   . SER   A 1 65  ? 32.746 6.164   3.374   1.00 9.76  ?  65   SER   A CB   1 
ATOM   1447 O  OG   . SER   A 1 65  ? 31.896 5.351   4.171   1.00 10.25 ?  65   SER   A OG   1 
ATOM   1448 H  H    . SER   A 1 65  ? 33.492 7.190   5.437   1.00 11.70 ?  65   SER   A H    1 
ATOM   1449 H  HA   . SER   A 1 65  ? 34.459 5.234   4.006   1.00 11.95 ?  65   SER   A HA   1 
ATOM   1450 H  HB2  . SER   A 1 65  ? 32.409 7.072   3.385   1.00 11.73 ?  65   SER   A HB2  1 
ATOM   1451 H  HB3  . SER   A 1 65  ? 32.749 5.824   2.466   1.00 11.73 ?  65   SER   A HB3  1 
ATOM   1452 H  HG   . SER   A 1 65  ? 31.895 5.634   4.965   1.00 12.32 ?  65   SER   A HG   1 
ATOM   1453 N  N    . ASP   A 1 66  ? 35.174 8.152   2.914   1.00 10.39 ?  66   ASP   A N    1 
ATOM   1454 C  CA   . ASP   A 1 66  ? 36.040 8.847   1.966   1.00 11.01 ?  66   ASP   A CA   1 
ATOM   1455 C  C    . ASP   A 1 66  ? 37.503 8.499   2.208   1.00 10.84 ?  66   ASP   A C    1 
ATOM   1456 O  O    . ASP   A 1 66  ? 38.275 8.323   1.259   1.00 12.05 ?  66   ASP   A O    1 
ATOM   1457 C  CB   . ASP   A 1 66  ? 35.819 10.352  2.067   1.00 12.12 ?  66   ASP   A CB   1 
ATOM   1458 C  CG   . ASP   A 1 66  ? 34.488 10.807  1.460   1.00 13.50 ?  66   ASP   A CG   1 
ATOM   1459 O  OD1  . ASP   A 1 66  ? 33.775 10.002  0.824   1.00 13.81 ?  66   ASP   A OD1  1 
ATOM   1460 O  OD2  . ASP   A 1 66  ? 34.190 12.012  1.591   1.00 16.22 -1 66   ASP   A OD2  1 
ATOM   1461 H  H    . ASP   A 1 66  ? 34.732 8.668   3.445   1.00 12.50 ?  66   ASP   A H    1 
ATOM   1462 H  HA   . ASP   A 1 66  ? 35.808 8.572   1.064   1.00 13.23 ?  66   ASP   A HA   1 
ATOM   1463 H  HB2  . ASP   A 1 66  ? 35.818 10.610  3.002   1.00 14.56 ?  66   ASP   A HB2  1 
ATOM   1464 H  HB3  . ASP   A 1 66  ? 36.540 10.808  1.600   1.00 14.56 ?  66   ASP   A HB3  1 
ATOM   1465 N  N    . ASP   A 1 67  ? 37.898 8.372   3.472   1.00 11.13 ?  67   ASP   A N    1 
ATOM   1466 C  CA   . ASP   A 1 67  ? 39.251 7.923   3.774   1.00 12.25 ?  67   ASP   A CA   1 
ATOM   1467 C  C    . ASP   A 1 67  ? 39.469 6.489   3.306   1.00 12.07 ?  67   ASP   A C    1 
ATOM   1468 O  O    . ASP   A 1 67  ? 40.528 6.165   2.756   1.00 12.60 ?  67   ASP   A O    1 
ATOM   1469 C  CB   . ASP   A 1 67  ? 39.520 8.057   5.271   1.00 13.65 ?  67   ASP   A CB   1 
ATOM   1470 C  CG   . ASP   A 1 67  ? 40.817 7.393   5.690   1.00 14.92 ?  67   ASP   A CG   1 
ATOM   1471 O  OD1  . ASP   A 1 67  ? 41.892 8.018   5.541   1.00 17.63 ?  67   ASP   A OD1  1 
ATOM   1472 O  OD2  . ASP   A 1 67  ? 40.762 6.233   6.157   1.00 14.57 -1 67   ASP   A OD2  1 
ATOM   1473 H  H    . ASP   A 1 67  ? 37.409 8.530   4.157   1.00 13.38 ?  67   ASP   A H    1 
ATOM   1474 H  HA   . ASP   A 1 67  ? 39.883 8.486   3.301   1.00 14.73 ?  67   ASP   A HA   1 
ATOM   1475 H  HB2  . ASP   A 1 67  ? 39.575 8.998   5.493   1.00 16.40 ?  67   ASP   A HB2  1 
ATOM   1476 H  HB3  . ASP   A 1 67  ? 38.792 7.640   5.759   1.00 16.40 ?  67   ASP   A HB3  1 
ATOM   1477 N  N    . TYR   A 1 68  ? 38.474 5.616   3.504   1.00 11.76 ?  68   TYR   A N    1 
ATOM   1478 C  CA   . TYR   A 1 68  ? 38.591 4.236   3.032   1.00 11.80 ?  68   TYR   A CA   1 
ATOM   1479 C  C    . TYR   A 1 68  ? 38.837 4.188   1.525   1.00 11.53 ?  68   TYR   A C    1 
ATOM   1480 O  O    . TYR   A 1 68  ? 39.713 3.453   1.053   1.00 12.06 ?  68   TYR   A O    1 
ATOM   1481 C  CB   . TYR   A 1 68  ? 37.340 3.415   3.409   1.00 12.22 ?  68   TYR   A CB   1 
ATOM   1482 C  CG   . TYR   A 1 68  ? 37.367 2.031   2.781   1.00 13.36 ?  68   TYR   A CG   1 
ATOM   1483 C  CD1  . TYR   A 1 68  ? 36.908 1.837   1.481   1.00 14.69 ?  68   TYR   A CD1  1 
ATOM   1484 C  CD2  . TYR   A 1 68  ? 37.900 0.944   3.454   1.00 14.94 ?  68   TYR   A CD2  1 
ATOM   1485 C  CE1  . TYR   A 1 68  ? 36.980 0.622   0.866   1.00 15.64 ?  68   TYR   A CE1  1 
ATOM   1486 C  CE2  . TYR   A 1 68  ? 37.967 -0.313  2.839   1.00 15.52 ?  68   TYR   A CE2  1 
ATOM   1487 C  CZ   . TYR   A 1 68  ? 37.509 -0.448  1.546   1.00 16.06 ?  68   TYR   A CZ   1 
ATOM   1488 O  OH   . TYR   A 1 68  ? 37.590 -1.663  0.919   1.00 17.32 ?  68   TYR   A OH   1 
ATOM   1489 H  H    . TYR   A 1 68  ? 37.733 5.794   3.907   1.00 14.13 ?  68   TYR   A H    1 
ATOM   1490 H  HA   . TYR   A 1 68  ? 39.351 3.823   3.467   1.00 14.18 ?  68   TYR   A HA   1 
ATOM   1491 H  HB2  . TYR   A 1 68  ? 37.305 3.308   4.372   1.00 14.68 ?  68   TYR   A HB2  1 
ATOM   1492 H  HB3  . TYR   A 1 68  ? 36.546 3.877   3.094   1.00 14.68 ?  68   TYR   A HB3  1 
ATOM   1493 H  HD1  . TYR   A 1 68  ? 36.563 2.566   1.010   1.00 17.65 ?  68   TYR   A HD1  1 
ATOM   1494 H  HD2  . TYR   A 1 68  ? 38.233 1.055   4.312   1.00 17.95 ?  68   TYR   A HD2  1 
ATOM   1495 H  HE1  . TYR   A 1 68  ? 36.661 0.517   -0.002  1.00 18.79 ?  68   TYR   A HE1  1 
ATOM   1496 H  HE2  . TYR   A 1 68  ? 38.334 -1.040  3.282   1.00 18.64 ?  68   TYR   A HE2  1 
ATOM   1497 H  HH   . TYR   A 1 68  ? 37.919 -2.234  1.444   1.00 20.81 ?  68   TYR   A HH   1 
ATOM   1498 N  N    . ILE   A 1 69  ? 38.050 4.941   0.748   1.00 11.22 ?  69   ILE   A N    1 
ATOM   1499 C  CA   . ILE   A 1 69  ? 38.189 4.927   -0.708  1.00 11.26 ?  69   ILE   A CA   1 
ATOM   1500 C  C    . ILE   A 1 69  ? 39.520 5.533   -1.139  1.00 11.18 ?  69   ILE   A C    1 
ATOM   1501 O  O    . ILE   A 1 69  ? 40.167 5.042   -2.072  1.00 11.51 ?  69   ILE   A O    1 
ATOM   1502 C  CB   . ILE   A 1 69  ? 36.993 5.638   -1.372  1.00 11.99 ?  69   ILE   A CB   1 
ATOM   1503 C  CG1  . ILE   A 1 69  ? 35.680 4.904   -1.086  1.00 12.53 ?  69   ILE   A CG1  1 
ATOM   1504 C  CG2  . ILE   A 1 69  ? 37.225 5.818   -2.878  1.00 13.26 ?  69   ILE   A CG2  1 
ATOM   1505 C  CD1  . ILE   A 1 69  ? 35.522 3.606   -1.840  1.00 13.21 ?  69   ILE   A CD1  1 
ATOM   1506 H  H    . ILE   A 1 69  ? 37.434 5.470   1.040   1.00 13.48 ?  69   ILE   A H    1 
ATOM   1507 H  HA   . ILE   A 1 69  ? 38.182 4.006   -1.004  1.00 13.53 ?  69   ILE   A HA   1 
ATOM   1508 H  HB   . ILE   A 1 69  ? 36.922 6.519   -0.983  1.00 14.41 ?  69   ILE   A HB   1 
ATOM   1509 H  HG12 . ILE   A 1 69  ? 35.637 4.702   -0.135  1.00 15.06 ?  69   ILE   A HG12 1 
ATOM   1510 H  HG13 . ILE   A 1 69  ? 34.940 5.481   -1.329  1.00 15.06 ?  69   ILE   A HG13 1 
ATOM   1511 H  HG21 . ILE   A 1 69  ? 36.380 6.035   -3.306  1.00 15.94 ?  69   ILE   A HG21 1 
ATOM   1512 H  HG22 . ILE   A 1 69  ? 37.854 6.549   -3.017  1.00 15.94 ?  69   ILE   A HG22 1 
ATOM   1513 H  HG23 . ILE   A 1 69  ? 37.583 5.000   -3.250  1.00 15.94 ?  69   ILE   A HG23 1 
ATOM   1514 H  HD11 . ILE   A 1 69  ? 34.720 3.161   -1.527  1.00 15.87 ?  69   ILE   A HD11 1 
ATOM   1515 H  HD12 . ILE   A 1 69  ? 35.445 3.799   -2.786  1.00 15.87 ?  69   ILE   A HD12 1 
ATOM   1516 H  HD13 . ILE   A 1 69  ? 36.296 3.047   -1.674  1.00 15.87 ?  69   ILE   A HD13 1 
ATOM   1517 N  N    . ALA   A 1 70  ? 39.940 6.615   -0.490  1.00 11.60 ?  70   ALA   A N    1 
ATOM   1518 C  CA   . ALA   A 1 70  ? 41.216 7.221   -0.845  1.00 12.61 ?  70   ALA   A CA   1 
ATOM   1519 C  C    . ALA   A 1 70  ? 42.364 6.236   -0.668  1.00 12.87 ?  70   ALA   A C    1 
ATOM   1520 O  O    . ALA   A 1 70  ? 43.339 6.274   -1.425  1.00 14.62 ?  70   ALA   A O    1 
ATOM   1521 C  CB   . ALA   A 1 70  ? 41.456 8.477   -0.007  1.00 13.12 ?  70   ALA   A CB   1 
ATOM   1522 H  H    . ALA   A 1 70  ? 39.512 7.011   0.138   1.00 13.95 ?  70   ALA   A H    1 
ATOM   1523 H  HA   . ALA   A 1 70  ? 41.192 7.490   -1.778  1.00 15.15 ?  70   ALA   A HA   1 
ATOM   1524 H  HB1  . ALA   A 1 70  ? 42.313 8.865   -0.256  1.00 15.77 ?  70   ALA   A HB1  1 
ATOM   1525 H  HB2  . ALA   A 1 70  ? 40.746 9.114   -0.175  1.00 15.77 ?  70   ALA   A HB2  1 
ATOM   1526 H  HB3  . ALA   A 1 70  ? 41.469 8.234   0.932   1.00 15.77 ?  70   ALA   A HB3  1 
ATOM   1527 N  N    . THR   A 1 71  ? 42.256 5.336   0.308   1.00 12.41 ?  71   THR   A N    1 
ATOM   1528 C  CA   . THR   A 1 71  ? 43.307 4.359   0.563   1.00 13.99 ?  71   THR   A CA   1 
ATOM   1529 C  C    . THR   A 1 71  ? 43.186 3.134   -0.331  1.00 13.96 ?  71   THR   A C    1 
ATOM   1530 O  O    . THR   A 1 71  ? 44.197 2.626   -0.836  1.00 16.04 ?  71   THR   A O    1 
ATOM   1531 C  CB   . THR   A 1 71  ? 43.239 3.918   2.020   1.00 16.02 ?  71   THR   A CB   1 
ATOM   1532 O  OG1  . THR   A 1 71  ? 43.487 5.049   2.860   1.00 17.08 ?  71   THR   A OG1  1 
ATOM   1533 C  CG2  . THR   A 1 71  ? 44.251 2.814   2.311   1.00 17.75 ?  71   THR   A CG2  1 
ATOM   1534 H  H    . THR   A 1 71  ? 41.577 5.264   0.828   1.00 14.91 ?  71   THR   A H    1 
ATOM   1535 H  HA   . THR   A 1 71  ? 44.170 4.764   0.398   1.00 16.81 ?  71   THR   A HA   1 
ATOM   1536 H  HB   . THR   A 1 71  ? 42.351 3.567   2.205   1.00 19.25 ?  71   THR   A HB   1 
ATOM   1537 H  HG1  . THR   A 1 71  ? 43.455 4.811   3.666   1.00 20.52 ?  71   THR   A HG1  1 
ATOM   1538 H  HG21 . THR   A 1 71  ? 44.391 2.740   3.267   1.00 21.33 ?  71   THR   A HG21 1 
ATOM   1539 H  HG22 . THR   A 1 71  ? 43.932 1.963   1.973   1.00 21.33 ?  71   THR   A HG22 1 
ATOM   1540 H  HG23 . THR   A 1 71  ? 45.100 3.024   1.887   1.00 21.33 ?  71   THR   A HG23 1 
ATOM   1541 N  N    . ASN   A 1 72  ? 41.961 2.631   -0.519  1.00 12.87 ?  72   ASN   A N    1 
ATOM   1542 C  CA   . ASN   A 1 72  ? 41.741 1.306   -1.079  1.00 13.19 ?  72   ASN   A CA   1 
ATOM   1543 C  C    . ASN   A 1 72  ? 41.124 1.290   -2.465  1.00 13.23 ?  72   ASN   A C    1 
ATOM   1544 O  O    . ASN   A 1 72  ? 41.125 0.232   -3.106  1.00 14.71 ?  72   ASN   A O    1 
ATOM   1545 C  CB   . ASN   A 1 72  ? 40.849 0.490   -0.138  1.00 13.81 ?  72   ASN   A CB   1 
ATOM   1546 C  CG   . ASN   A 1 72  ? 41.463 0.329   1.224   1.00 15.07 ?  72   ASN   A CG   1 
ATOM   1547 O  OD1  . ASN   A 1 72  ? 41.015 0.929   2.198   1.00 16.88 ?  72   ASN   A OD1  1 
ATOM   1548 N  ND2  . ASN   A 1 72  ? 42.510 -0.465  1.299   1.00 15.83 ?  72   ASN   A ND2  1 
ATOM   1549 H  H    . ASN   A 1 72  ? 41.230 3.051   -0.327  1.00 15.47 ?  72   ASN   A H    1 
ATOM   1550 H  HA   . ASN   A 1 72  ? 42.592 0.855   -1.140  1.00 15.86 ?  72   ASN   A HA   1 
ATOM   1551 H  HB2  . ASN   A 1 72  ? 39.996 0.938   -0.037  1.00 16.59 ?  72   ASN   A HB2  1 
ATOM   1552 H  HB3  . ASN   A 1 72  ? 40.718 -0.395  -0.517  1.00 16.59 ?  72   ASN   A HB3  1 
ATOM   1553 H  HD21 . ASN   A 1 72  ? 42.904 -0.587  2.054   1.00 19.02 ?  72   ASN   A HD21 1 
ATOM   1554 H  HD22 . ASN   A 1 72  ? 42.803 -0.861  0.593   1.00 19.02 ?  72   ASN   A HD22 1 
ATOM   1555 N  N    . GLY   A 1 73  ? 40.580 2.404   -2.933  1.00 12.83 ?  73   GLY   A N    1 
ATOM   1556 C  CA   . GLY   A 1 73  ? 39.844 2.417   -4.171  1.00 12.69 ?  73   GLY   A CA   1 
ATOM   1557 C  C    . GLY   A 1 73  ? 38.451 1.846   -3.997  1.00 11.95 ?  73   GLY   A C    1 
ATOM   1558 O  O    . GLY   A 1 73  ? 38.062 1.397   -2.911  1.00 12.82 ?  73   GLY   A O    1 
ATOM   1559 H  H    . GLY   A 1 73  ? 40.630 3.180   -2.550  1.00 15.42 ?  73   GLY   A H    1 
ATOM   1560 H  HA2  . GLY   A 1 73  ? 39.771 3.334   -4.495  1.00 15.25 ?  73   GLY   A HA2  1 
ATOM   1561 H  HA3  . GLY   A 1 73  ? 40.321 1.897   -4.840  1.00 15.25 ?  73   GLY   A HA3  1 
ATOM   1562 N  N    . PRO   A 1 74  ? 37.677 1.858   -5.080  1.00 12.43 ?  74   PRO   A N    1 
ATOM   1563 C  CA   . PRO   A 1 74  ? 36.279 1.426   -5.005  1.00 12.59 ?  74   PRO   A CA   1 
ATOM   1564 C  C    . PRO   A 1 74  ? 36.134 -0.054  -4.685  1.00 11.90 ?  74   PRO   A C    1 
ATOM   1565 O  O    . PRO   A 1 74  ? 37.008 -0.878  -4.965  1.00 12.67 ?  74   PRO   A O    1 
ATOM   1566 C  CB   . PRO   A 1 74  ? 35.742 1.727   -6.411  1.00 14.19 ?  74   PRO   A CB   1 
ATOM   1567 C  CG   . PRO   A 1 74  ? 36.690 2.720   -7.001  1.00 16.96 ?  74   PRO   A CG   1 
ATOM   1568 C  CD   . PRO   A 1 74  ? 38.024 2.373   -6.415  1.00 14.36 ?  74   PRO   A CD   1 
ATOM   1569 H  HA   . PRO   A 1 74  ? 35.793 1.955   -4.352  1.00 15.14 ?  74   PRO   A HA   1 
ATOM   1570 H  HB2  . PRO   A 1 74  ? 35.728 0.911   -6.935  1.00 17.05 ?  74   PRO   A HB2  1 
ATOM   1571 H  HB3  . PRO   A 1 74  ? 34.850 2.106   -6.345  1.00 17.05 ?  74   PRO   A HB3  1 
ATOM   1572 H  HG2  . PRO   A 1 74  ? 36.709 2.628   -7.966  1.00 20.38 ?  74   PRO   A HG2  1 
ATOM   1573 H  HG3  . PRO   A 1 74  ? 36.432 3.617   -6.744  1.00 20.38 ?  74   PRO   A HG3  1 
ATOM   1574 H  HD2  . PRO   A 1 74  ? 38.461 1.682   -6.943  1.00 17.26 ?  74   PRO   A HD2  1 
ATOM   1575 H  HD3  . PRO   A 1 74  ? 38.581 3.170   -6.356  1.00 17.26 ?  74   PRO   A HD3  1 
ATOM   1576 N  N    . LEU   A 1 75  ? 34.989 -0.379  -4.099  1.00 11.21 ?  75   LEU   A N    1 
ATOM   1577 C  CA   . LEU   A 1 75  ? 34.592 -1.767  -3.942  1.00 10.86 ?  75   LEU   A CA   1 
ATOM   1578 C  C    . LEU   A 1 75  ? 34.204 -2.348  -5.299  1.00 11.08 ?  75   LEU   A C    1 
ATOM   1579 O  O    . LEU   A 1 75  ? 34.053 -1.636  -6.295  1.00 12.70 ?  75   LEU   A O    1 
ATOM   1580 C  CB   . LEU   A 1 75  ? 33.403 -1.885  -2.987  1.00 10.79 ?  75   LEU   A CB   1 
ATOM   1581 C  CG   . LEU   A 1 75  ? 33.614 -1.469  -1.533  1.00 12.37 ?  75   LEU   A CG   1 
ATOM   1582 C  CD1  . LEU   A 1 75  ? 32.324 -1.660  -0.739  1.00 14.32 ?  75   LEU   A CD1  1 
ATOM   1583 C  CD2  . LEU   A 1 75  ? 34.740 -2.208  -0.875  1.00 15.35 ?  75   LEU   A CD2  1 
ATOM   1584 H  H    . LEU   A 1 75  ? 34.422 0.189   -3.788  1.00 13.47 ?  75   LEU   A H    1 
ATOM   1585 H  HA   . LEU   A 1 75  ? 35.335 -2.277  -3.584  1.00 13.05 ?  75   LEU   A HA   1 
ATOM   1586 H  HB2  . LEU   A 1 75  ? 32.683 -1.342  -3.337  1.00 12.97 ?  75   LEU   A HB2  1 
ATOM   1587 H  HB3  . LEU   A 1 75  ? 33.122 -2.816  -2.979  1.00 12.97 ?  75   LEU   A HB3  1 
ATOM   1588 H  HG   . LEU   A 1 75  ? 33.837 -0.527  -1.513  1.00 14.87 ?  75   LEU   A HG   1 
ATOM   1589 H  HD11 . LEU   A 1 75  ? 32.480 -1.387  0.178   1.00 17.21 ?  75   LEU   A HD11 1 
ATOM   1590 H  HD12 . LEU   A 1 75  ? 31.633 -1.110  -1.137  1.00 17.21 ?  75   LEU   A HD12 1 
ATOM   1591 H  HD13 . LEU   A 1 75  ? 32.071 -2.593  -0.773  1.00 17.21 ?  75   LEU   A HD13 1 
ATOM   1592 H  HD21 . LEU   A 1 75  ? 34.793 -1.942  0.056   1.00 18.44 ?  75   LEU   A HD21 1 
ATOM   1593 H  HD22 . LEU   A 1 75  ? 34.579 -3.161  -0.939  1.00 18.44 ?  75   LEU   A HD22 1 
ATOM   1594 H  HD23 . LEU   A 1 75  ? 35.575 -1.985  -1.325  1.00 18.44 ?  75   LEU   A HD23 1 
ATOM   1595 N  N    . LYS   A 1 76  ? 34.047 -3.669  -5.321  1.00 11.33 ?  76   LYS   A N    1 
ATOM   1596 C  CA   . LYS   A 1 76  ? 33.450 -4.384  -6.442  1.00 11.80 ?  76   LYS   A CA   1 
ATOM   1597 C  C    . LYS   A 1 76  ? 31.939 -4.462  -6.253  1.00 10.74 ?  76   LYS   A C    1 
ATOM   1598 O  O    . LYS   A 1 76  ? 31.452 -4.571  -5.131  1.00 10.78 ?  76   LYS   A O    1 
ATOM   1599 C  CB   . LYS   A 1 76  ? 33.995 -5.820  -6.500  1.00 13.32 ?  76   LYS   A CB   1 
ATOM   1600 C  CG   . LYS   A 1 76  ? 35.502 -5.920  -6.704  1.00 14.79 ?  76   LYS   A CG   1 
ATOM   1601 C  CD   . LYS   A 1 76  ? 36.025 -7.319  -6.483  1.00 16.10 ?  76   LYS   A CD   1 
ATOM   1602 C  CE   . LYS   A 1 76  ? 37.518 -7.379  -6.689  1.00 18.52 ?  76   LYS   A CE   1 
ATOM   1603 N  NZ   . LYS   A 1 76  ? 38.045 -8.742  -6.465  1.00 19.26 ?  76   LYS   A NZ   1 
ATOM   1604 H  H    . LYS   A 1 76  ? 34.281 -4.192  -4.672  1.00 13.62 ?  76   LYS   A H    1 
ATOM   1605 H  HA   . LYS   A 1 76  ? 33.654 -3.931  -7.276  1.00 14.18 ?  76   LYS   A HA   1 
ATOM   1606 H  HB2  . LYS   A 1 76  ? 33.782 -6.267  -5.667  1.00 16.01 ?  76   LYS   A HB2  1 
ATOM   1607 H  HB3  . LYS   A 1 76  ? 33.569 -6.282  -7.239  1.00 16.01 ?  76   LYS   A HB3  1 
ATOM   1608 H  HG2  . LYS   A 1 76  ? 35.715 -5.657  -7.613  1.00 17.77 ?  76   LYS   A HG2  1 
ATOM   1609 H  HG3  . LYS   A 1 76  ? 35.945 -5.329  -6.075  1.00 17.77 ?  76   LYS   A HG3  1 
ATOM   1610 H  HD2  . LYS   A 1 76  ? 35.828 -7.595  -5.574  1.00 19.35 ?  76   LYS   A HD2  1 
ATOM   1611 H  HD3  . LYS   A 1 76  ? 35.602 -7.922  -7.116  1.00 19.35 ?  76   LYS   A HD3  1 
ATOM   1612 H  HE2  . LYS   A 1 76  ? 37.724 -7.117  -7.600  1.00 22.24 ?  76   LYS   A HE2  1 
ATOM   1613 H  HE3  . LYS   A 1 76  ? 37.950 -6.780  -6.061  1.00 22.24 ?  76   LYS   A HE3  1 
ATOM   1614 H  HZ1  . LYS   A 1 76  ? 38.924 -8.759  -6.593  1.00 23.14 ?  76   LYS   A HZ1  1 
ATOM   1615 H  HZ2  . LYS   A 1 76  ? 37.867 -9.010  -5.634  1.00 23.14 ?  76   LYS   A HZ2  1 
ATOM   1616 H  HZ3  . LYS   A 1 76  ? 37.662 -9.317  -7.035  1.00 23.14 ?  76   LYS   A HZ3  1 
ATOM   1617 N  N    . VAL   A 1 77  ? 31.196 -4.439  -7.362  1.00 11.08 ?  77   VAL   A N    1 
ATOM   1618 C  CA   . VAL   A 1 77  ? 29.789 -4.820  -7.285  1.00 10.86 ?  77   VAL   A CA   1 
ATOM   1619 C  C    . VAL   A 1 77  ? 29.725 -6.273  -6.839  1.00 10.65 ?  77   VAL   A C    1 
ATOM   1620 O  O    . VAL   A 1 77  ? 30.388 -7.144  -7.412  1.00 11.01 ?  77   VAL   A O    1 
ATOM   1621 C  CB   . VAL   A 1 77  ? 29.076 -4.610  -8.629  1.00 12.03 ?  77   VAL   A CB   1 
ATOM   1622 C  CG1  . VAL   A 1 77  ? 27.614 -5.032  -8.516  1.00 12.77 ?  77   VAL   A CG1  1 
ATOM   1623 C  CG2  . VAL   A 1 77  ? 29.187 -3.160  -9.068  1.00 13.48 ?  77   VAL   A CG2  1 
ATOM   1624 H  H    . VAL   A 1 77  ? 31.483 -4.211  -8.143  1.00 13.32 ?  77   VAL   A H    1 
ATOM   1625 H  HA   . VAL   A 1 77  ? 29.354 -4.276  -6.616  1.00 13.05 ?  77   VAL   A HA   1 
ATOM   1626 H  HB   . VAL   A 1 77  ? 29.503 -5.157  -9.305  1.00 14.46 ?  77   VAL   A HB   1 
ATOM   1627 H  HG11 . VAL   A 1 77  ? 27.148 -4.750  -9.314  1.00 15.35 ?  77   VAL   A HG11 1 
ATOM   1628 H  HG12 . VAL   A 1 77  ? 27.572 -5.994  -8.425  1.00 15.35 ?  77   VAL   A HG12 1 
ATOM   1629 H  HG13 . VAL   A 1 77  ? 27.227 -4.605  -7.735  1.00 15.35 ?  77   VAL   A HG13 1 
ATOM   1630 H  HG21 . VAL   A 1 77  ? 28.675 -3.038  -9.880  1.00 16.20 ?  77   VAL   A HG21 1 
ATOM   1631 H  HG22 . VAL   A 1 77  ? 28.838 -2.590  -8.365  1.00 16.20 ?  77   VAL   A HG22 1 
ATOM   1632 H  HG23 . VAL   A 1 77  ? 30.121 -2.947  -9.230  1.00 16.20 ?  77   VAL   A HG23 1 
ATOM   1633 N  N    . GLY   A 1 78  ? 28.936 -6.540  -5.797  1.00 10.48 ?  78   GLY   A N    1 
ATOM   1634 C  CA   . GLY   A 1 78  ? 28.912 -7.827  -5.136  1.00 10.67 ?  78   GLY   A CA   1 
ATOM   1635 C  C    . GLY   A 1 78  ? 29.821 -7.919  -3.929  1.00 10.08 ?  78   GLY   A C    1 
ATOM   1636 O  O    . GLY   A 1 78  ? 29.760 -8.921  -3.201  1.00 10.72 ?  78   GLY   A O    1 
ATOM   1637 H  H    . GLY   A 1 78  ? 28.390 -5.965  -5.454  1.00 12.60 ?  78   GLY   A H    1 
ATOM   1638 H  HA2  . GLY   A 1 78  ? 28.007 -8.016  -4.852  1.00 12.83 ?  78   GLY   A HA2  1 
ATOM   1639 H  HA3  . GLY   A 1 78  ? 29.180 -8.509  -5.773  1.00 12.83 ?  78   GLY   A HA3  1 
ATOM   1640 N  N    . GLY   A 1 79  ? 30.676 -6.916  -3.711  1.00 10.19 ?  79   GLY   A N    1 
ATOM   1641 C  CA   . GLY   A 1 79  ? 31.636 -6.922  -2.632  1.00 10.69 ?  79   GLY   A CA   1 
ATOM   1642 C  C    . GLY   A 1 79  ? 31.184 -6.120  -1.421  1.00 9.82  ?  79   GLY   A C    1 
ATOM   1643 O  O    . GLY   A 1 79  ? 30.067 -5.612  -1.348  1.00 10.30 ?  79   GLY   A O    1 
ATOM   1644 H  H    . GLY   A 1 79  ? 30.719 -6.204  -4.193  1.00 12.25 ?  79   GLY   A H    1 
ATOM   1645 H  HA2  . GLY   A 1 79  ? 31.795 -7.844  -2.351  1.00 12.85 ?  79   GLY   A HA2  1 
ATOM   1646 H  HA3  . GLY   A 1 79  ? 32.477 -6.557  -2.942  1.00 12.85 ?  79   GLY   A HA3  1 
ATOM   1647 N  N    . SER   A 1 80  ? 32.084 -6.038  -0.441  1.00 10.63 ?  80   SER   A N    1 
ATOM   1648 C  CA   . SER   A 1 80  ? 31.764 -5.403  0.827   1.00 10.20 ?  80   SER   A CA   1 
ATOM   1649 C  C    . SER   A 1 80  ? 33.033 -4.952  1.529   1.00 9.91  ?  80   SER   A C    1 
ATOM   1650 O  O    . SER   A 1 80  ? 34.145 -5.382  1.206   1.00 11.57 ?  80   SER   A O    1 
ATOM   1651 C  CB   . SER   A 1 80  ? 31.006 -6.361  1.748   1.00 10.92 ?  80   SER   A CB   1 
ATOM   1652 O  OG   . SER   A 1 80  ? 31.830 -7.412  2.218   1.00 12.56 ?  80   SER   A OG   1 
ATOM   1653 H  H    . SER   A 1 80  ? 32.887 -6.334  -0.490  1.00 12.78 ?  80   SER   A H    1 
ATOM   1654 H  HA   . SER   A 1 80  ? 31.209 -4.625  0.650   1.00 12.26 ?  80   SER   A HA   1 
ATOM   1655 H  HB2  . SER   A 1 80  ? 30.680 -5.862  2.508   1.00 13.12 ?  80   SER   A HB2  1 
ATOM   1656 H  HB3  . SER   A 1 80  ? 30.265 -6.739  1.254   1.00 13.12 ?  80   SER   A HB3  1 
ATOM   1657 H  HG   . SER   A 1 80  ? 32.122 -7.858  1.561   1.00 15.09 ?  80   SER   A HG   1 
ATOM   1658 N  N    . CYS   A 1 81  ? 32.842 -4.103  2.534   1.00 9.85  ?  81   CYS   A N    1 
ATOM   1659 C  CA   . CYS   A 1 81  ? 33.893 -3.813  3.496   1.00 10.15 ?  81   CYS   A CA   1 
ATOM   1660 C  C    . CYS   A 1 81  ? 33.244 -3.579  4.853   1.00 9.85  ?  81   CYS   A C    1 
ATOM   1661 O  O    . CYS   A 1 81  ? 32.077 -3.181  4.935   1.00 11.13 ?  81   CYS   A O    1 
ATOM   1662 C  CB   . CYS   A 1 81  ? 34.764 -2.625  3.074   1.00 10.90 ?  81   CYS   A CB   1 
ATOM   1663 S  SG   . CYS   A 1 81  ? 33.861 -1.051  3.085   1.00 10.67 ?  81   CYS   A SG   1 
ATOM   1664 H  H    . CYS   A 1 81  ? 32.105 -3.682  2.685   1.00 11.84 ?  81   CYS   A H    1 
ATOM   1665 H  HA   . CYS   A 1 81  ? 34.470 -4.588  3.573   1.00 12.20 ?  81   CYS   A HA   1 
ATOM   1666 H  HB2  . CYS   A 1 81  ? 35.515 -2.549  3.688   1.00 13.10 ?  81   CYS   A HB2  1 
ATOM   1667 H  HB3  . CYS   A 1 81  ? 35.095 -2.780  2.172   1.00 13.10 ?  81   CYS   A HB3  1 
ATOM   1668 H  HG   . CYS   A 1 81  ? 34.604 -0.169  2.746   1.00 12.82 ?  81   CYS   A HG   1 
ATOM   1669 N  N    . VAL   A 1 82  ? 34.007 -3.844  5.910   1.00 10.27 ?  82   VAL   A N    1 
ATOM   1670 C  CA   . VAL   A 1 82  ? 33.578 -3.601  7.281   1.00 10.47 ?  82   VAL   A CA   1 
ATOM   1671 C  C    . VAL   A 1 82  ? 34.173 -2.285  7.748   1.00 10.82 ?  82   VAL   A C    1 
ATOM   1672 O  O    . VAL   A 1 82  ? 35.395 -2.110  7.732   1.00 11.57 ?  82   VAL   A O    1 
ATOM   1673 C  CB   . VAL   A 1 82  ? 34.008 -4.737  8.219   1.00 12.04 ?  82   VAL   A CB   1 
ATOM   1674 C  CG1  . VAL   A 1 82  ? 33.558 -4.441  9.637   1.00 13.76 ?  82   VAL   A CG1  1 
ATOM   1675 C  CG2  . VAL   A 1 82  ? 33.458 -6.067  7.748   1.00 13.01 ?  82   VAL   A CG2  1 
ATOM   1676 H  H    . VAL   A 1 82  ? 34.801 -4.178  5.855   1.00 12.35 ?  82   VAL   A H    1 
ATOM   1677 H  HA   . VAL   A 1 82  ? 32.612 -3.524  7.307   1.00 12.59 ?  82   VAL   A HA   1 
ATOM   1678 H  HB   . VAL   A 1 82  ? 34.974 -4.792  8.219   1.00 14.47 ?  82   VAL   A HB   1 
ATOM   1679 H  HG11 . VAL   A 1 82  ? 33.644 -5.248  10.168  1.00 16.53 ?  82   VAL   A HG11 1 
ATOM   1680 H  HG12 . VAL   A 1 82  ? 34.115 -3.740  10.012  1.00 16.53 ?  82   VAL   A HG12 1 
ATOM   1681 H  HG13 . VAL   A 1 82  ? 32.630 -4.155  9.624   1.00 16.53 ?  82   VAL   A HG13 1 
ATOM   1682 H  HG21 . VAL   A 1 82  ? 33.710 -6.753  8.384   1.00 15.63 ?  82   VAL   A HG21 1 
ATOM   1683 H  HG22 . VAL   A 1 82  ? 32.491 -6.005  7.691   1.00 15.63 ?  82   VAL   A HG22 1 
ATOM   1684 H  HG23 . VAL   A 1 82  ? 33.828 -6.269  6.875   1.00 15.63 ?  82   VAL   A HG23 1 
ATOM   1685 N  N    . LEU   A 1 83  ? 33.316 -1.362  8.165   1.00 10.29 ?  83   LEU   A N    1 
ATOM   1686 C  CA   . LEU   A 1 83  ? 33.729 -0.093  8.742   1.00 10.31 ?  83   LEU   A CA   1 
ATOM   1687 C  C    . LEU   A 1 83  ? 33.004 0.086   10.071  1.00 10.60 ?  83   LEU   A C    1 
ATOM   1688 O  O    . LEU   A 1 83  ? 32.283 -0.805  10.538  1.00 11.11 ?  83   LEU   A O    1 
ATOM   1689 C  CB   . LEU   A 1 83  ? 33.487 1.063   7.761   1.00 10.89 ?  83   LEU   A CB   1 
ATOM   1690 C  CG   . LEU   A 1 83  ? 34.390 1.056   6.525   1.00 11.57 ?  83   LEU   A CG   1 
ATOM   1691 C  CD1  . LEU   A 1 83  ? 33.953 2.110   5.526   1.00 12.38 ?  83   LEU   A CD1  1 
ATOM   1692 C  CD2  . LEU   A 1 83  ? 35.859 1.264   6.918   1.00 12.35 ?  83   LEU   A CD2  1 
ATOM   1693 H  H    . LEU   A 1 83  ? 32.461 -1.449  8.114   1.00 12.37 ?  83   LEU   A H    1 
ATOM   1694 H  HA   . LEU   A 1 83  ? 34.678 -0.120  8.928   1.00 12.39 ?  83   LEU   A HA   1 
ATOM   1695 H  HB2  . LEU   A 1 83  ? 32.571 1.022   7.445   1.00 13.09 ?  83   LEU   A HB2  1 
ATOM   1696 H  HB3  . LEU   A 1 83  ? 33.632 1.905   8.221   1.00 13.09 ?  83   LEU   A HB3  1 
ATOM   1697 H  HG   . LEU   A 1 83  ? 34.324 0.193   6.094   1.00 13.90 ?  83   LEU   A HG   1 
ATOM   1698 H  HD11 . LEU   A 1 83  ? 34.546 2.078   4.757   1.00 14.88 ?  83   LEU   A HD11 1 
ATOM   1699 H  HD12 . LEU   A 1 83  ? 33.044 1.922   5.254   1.00 14.88 ?  83   LEU   A HD12 1 
ATOM   1700 H  HD13 . LEU   A 1 83  ? 34.004 2.982   5.946   1.00 14.88 ?  83   LEU   A HD13 1 
ATOM   1701 H  HD21 . LEU   A 1 83  ? 36.384 1.423   6.115   1.00 14.84 ?  83   LEU   A HD21 1 
ATOM   1702 H  HD22 . LEU   A 1 83  ? 35.926 2.033   7.509   1.00 14.84 ?  83   LEU   A HD22 1 
ATOM   1703 H  HD23 . LEU   A 1 83  ? 36.185 0.471   7.371   1.00 14.84 ?  83   LEU   A HD23 1 
ATOM   1704 N  N    . SER   A 1 84  ? 33.214 1.237   10.700  1.00 11.15 ?  84   SER   A N    1 
ATOM   1705 C  CA   . SER   A 1 84  ? 32.569 1.493   11.973  1.00 11.04 ?  84   SER   A CA   1 
ATOM   1706 C  C    . SER   A 1 84  ? 31.051 1.576   11.818  1.00 11.21 ?  84   SER   A C    1 
ATOM   1707 O  O    . SER   A 1 84  ? 30.529 2.045   10.806  1.00 11.23 ?  84   SER   A O    1 
ATOM   1708 C  CB   . SER   A 1 84  ? 33.063 2.816   12.543  1.00 11.98 ?  84   SER   A CB   1 
ATOM   1709 O  OG   . SER   A 1 84  ? 32.438 3.088   13.780  1.00 13.07 ?  84   SER   A OG   1 
ATOM   1710 H  H    . SER   A 1 84  ? 33.714 1.882   10.407  1.00 13.40 ?  84   SER   A H    1 
ATOM   1711 H  HA   . SER   A 1 84  ? 32.793 0.783   12.594  1.00 13.28 ?  84   SER   A HA   1 
ATOM   1712 H  HB2  . SER   A 1 84  ? 34.025 2.774   12.670  1.00 14.40 ?  84   SER   A HB2  1 
ATOM   1713 H  HB3  . SER   A 1 84  ? 32.844 3.532   11.923  1.00 14.40 ?  84   SER   A HB3  1 
ATOM   1714 H  HG   . SER   A 1 84  ? 32.721 3.815   14.094  1.00 15.71 ?  84   SER   A HG   1 
ATOM   1715 N  N    . GLY   A 1 85  ? 30.338 1.167   12.865  1.00 12.03 ?  85   GLY   A N    1 
ATOM   1716 C  CA   . GLY   A 1 85  ? 28.915 1.413   12.948  1.00 12.75 ?  85   GLY   A CA   1 
ATOM   1717 C  C    . GLY   A 1 85  ? 28.554 2.731   13.593  1.00 11.95 ?  85   GLY   A C    1 
ATOM   1718 O  O    . GLY   A 1 85  ? 27.365 3.052   13.710  1.00 12.53 ?  85   GLY   A O    1 
ATOM   1719 H  H    . GLY   A 1 85  ? 30.664 0.741   13.546  1.00 14.45 ?  85   GLY   A H    1 
ATOM   1720 H  HA2  . GLY   A 1 85  ? 28.545 1.402   12.052  1.00 15.32 ?  85   GLY   A HA2  1 
ATOM   1721 H  HA3  . GLY   A 1 85  ? 28.498 0.704   13.456  1.00 15.32 ?  85   GLY   A HA3  1 
ATOM   1722 N  N    . HIS   A 1 86  ? 29.548 3.505   14.024  1.00 11.72 ?  86   HIS   A N    1 
ATOM   1723 C  CA   . HIS   A 1 86  ? 29.334 4.840   14.595  1.00 12.32 ?  86   HIS   A CA   1 
ATOM   1724 C  C    . HIS   A 1 86  ? 28.348 4.722   15.751  1.00 12.82 ?  86   HIS   A C    1 
ATOM   1725 O  O    . HIS   A 1 86  ? 28.520 3.843   16.607  1.00 14.08 ?  86   HIS   A O    1 
ATOM   1726 C  CB   . HIS   A 1 86  ? 28.962 5.825   13.496  1.00 12.54 ?  86   HIS   A CB   1 
ATOM   1727 C  CG   . HIS   A 1 86  ? 30.018 5.926   12.459  1.00 12.13 ?  86   HIS   A CG   1 
ATOM   1728 N  ND1  . HIS   A 1 86  ? 31.117 6.745   12.604  1.00 13.16 ?  86   HIS   A ND1  1 
ATOM   1729 C  CD2  . HIS   A 1 86  ? 30.204 5.236   11.312  1.00 11.97 ?  86   HIS   A CD2  1 
ATOM   1730 C  CE1  . HIS   A 1 86  ? 31.915 6.580   11.565  1.00 13.03 ?  86   HIS   A CE1  1 
ATOM   1731 N  NE2  . HIS   A 1 86  ? 31.389 5.663   10.774  1.00 12.07 ?  86   HIS   A NE2  1 
ATOM   1732 H  H    . HIS   A 1 86  ? 30.375 3.282   14.001  1.00 14.09 ?  86   HIS   A H    1 
ATOM   1733 H  HA   . HIS   A 1 86  ? 30.174 5.148   14.968  1.00 14.80 ?  86   HIS   A HA   1 
ATOM   1734 H  HB2  . HIS   A 1 86  ? 28.142 5.538   13.066  1.00 15.07 ?  86   HIS   A HB2  1 
ATOM   1735 H  HB3  . HIS   A 1 86  ? 28.840 6.711   13.881  1.00 15.07 ?  86   HIS   A HB3  1 
ATOM   1736 H  HD2  . HIS   A 1 86  ? 29.638 4.587   10.953  1.00 14.39 ?  86   HIS   A HD2  1 
ATOM   1737 H  HE1  . HIS   A 1 86  ? 32.713 7.034   11.407  1.00 15.66 ?  86   HIS   A HE1  1 
ATOM   1738 H  HE2  . HIS   A 1 86  ? 31.728 5.392   10.022  1.00 14.50 ?  86   HIS   A HE2  1 
ATOM   1739 N  N    . ASN   A 1 87  ? 27.342 5.579   15.821  1.00 13.98 ?  87   ASN   A N    1 
ATOM   1740 C  CA   . ASN   A 1 87  ? 26.360 5.578   16.889  1.00 14.73 ?  87   ASN   A CA   1 
ATOM   1741 C  C    . ASN   A 1 87  ? 25.228 4.593   16.654  1.00 15.62 ?  87   ASN   A C    1 
ATOM   1742 O  O    . ASN   A 1 87  ? 24.315 4.526   17.479  1.00 18.14 ?  87   ASN   A O    1 
ATOM   1743 C  CB   . ASN   A 1 87  ? 25.779 6.991   17.048  1.00 15.58 ?  87   ASN   A CB   1 
ATOM   1744 C  CG   . ASN   A 1 87  ? 25.282 7.576   15.729  1.00 16.57 ?  87   ASN   A CG   1 
ATOM   1745 O  OD1  . ASN   A 1 87  ? 25.940 7.467   14.696  1.00 17.13 ?  87   ASN   A OD1  1 
ATOM   1746 N  ND2  . ASN   A 1 87  ? 24.116 8.196   15.764  1.00 17.63 ?  87   ASN   A ND2  1 
ATOM   1747 H  H    . ASN   A 1 87  ? 27.200 6.192   15.243  1.00 16.79 ?  87   ASN   A H    1 
ATOM   1748 H  HA   . ASN   A 1 87  ? 26.784 5.331   17.727  1.00 17.70 ?  87   ASN   A HA   1 
ATOM   1749 H  HB2  . ASN   A 1 87  ? 25.027 6.960   17.668  1.00 18.72 ?  87   ASN   A HB2  1 
ATOM   1750 H  HB3  . ASN   A 1 87  ? 26.466 7.578   17.400  1.00 18.72 ?  87   ASN   A HB3  1 
ATOM   1751 H  HD21 . ASN   A 1 87  ? 23.797 8.541   15.045  1.00 21.18 ?  87   ASN   A HD21 1 
ATOM   1752 H  HD22 . ASN   A 1 87  ? 23.683 8.261   16.504  1.00 21.18 ?  87   ASN   A HD22 1 
ATOM   1753 N  N    A LEU   A 1 88  ? 25.273 3.825   15.567  0.50 14.14 ?  88   LEU   A N    1 
ATOM   1754 N  N    B LEU   A 1 88  ? 25.273 3.813   15.573  0.50 14.44 ?  88   LEU   A N    1 
ATOM   1755 C  CA   A LEU   A 1 88  ? 24.164 2.962   15.171  0.50 13.81 ?  88   LEU   A CA   1 
ATOM   1756 C  CA   B LEU   A 1 88  ? 24.155 2.964   15.181  0.50 14.27 ?  88   LEU   A CA   1 
ATOM   1757 C  C    A LEU   A 1 88  ? 24.378 1.495   15.514  0.50 13.64 ?  88   LEU   A C    1 
ATOM   1758 C  C    B LEU   A 1 88  ? 24.375 1.480   15.431  0.50 13.97 ?  88   LEU   A C    1 
ATOM   1759 O  O    A LEU   A 1 88  ? 23.405 0.785   15.789  0.50 14.64 ?  88   LEU   A O    1 
ATOM   1760 O  O    B LEU   A 1 88  ? 23.393 0.737   15.530  0.50 14.60 ?  88   LEU   A O    1 
ATOM   1761 C  CB   A LEU   A 1 88  ? 23.931 3.081   13.661  0.50 13.89 ?  88   LEU   A CB   1 
ATOM   1762 C  CB   B LEU   A 1 88  ? 23.852 3.156   13.689  0.50 14.57 ?  88   LEU   A CB   1 
ATOM   1763 C  CG   A LEU   A 1 88  ? 23.663 4.485   13.119  0.50 15.36 ?  88   LEU   A CG   1 
ATOM   1764 C  CG   B LEU   A 1 88  ? 23.534 4.589   13.256  0.50 15.61 ?  88   LEU   A CG   1 
ATOM   1765 C  CD1  A LEU   A 1 88  ? 23.545 4.438   11.606  0.50 15.20 ?  88   LEU   A CD1  1 
ATOM   1766 C  CD1  B LEU   A 1 88  ? 23.329 4.670   11.747  0.50 15.43 ?  88   LEU   A CD1  1 
ATOM   1767 C  CD2  A LEU   A 1 88  ? 22.405 5.079   13.739  0.50 17.07 ?  88   LEU   A CD2  1 
ATOM   1768 C  CD2  B LEU   A 1 88  ? 22.310 5.115   13.990  0.50 16.70 ?  88   LEU   A CD2  1 
ATOM   1769 H  H    A LEU   A 1 88  ? 25.952 3.781   15.041  0.50 16.99 ?  88   LEU   A H    1 
ATOM   1770 H  H    B LEU   A 1 88  ? 25.953 3.755   15.054  0.50 17.35 ?  88   LEU   A H    1 
ATOM   1771 H  HA   A LEU   A 1 88  ? 23.357 3.257   15.616  0.50 16.59 ?  88   LEU   A HA   1 
ATOM   1772 H  HA   B LEU   A 1 88  ? 23.367 3.236   15.675  0.50 17.14 ?  88   LEU   A HA   1 
ATOM   1773 H  HB2  A LEU   A 1 88  ? 24.713 2.749   13.197  0.50 16.69 ?  88   LEU   A HB2  1 
ATOM   1774 H  HB2  B LEU   A 1 88  ? 24.622 2.862   13.181  0.50 17.50 ?  88   LEU   A HB2  1 
ATOM   1775 H  HB3  A LEU   A 1 88  ? 23.161 2.541   13.424  0.50 16.69 ?  88   LEU   A HB3  1 
ATOM   1776 H  HB3  B LEU   A 1 88  ? 23.085 2.607   13.462  0.50 17.50 ?  88   LEU   A HB3  1 
ATOM   1777 H  HG   A LEU   A 1 88  ? 24.409 5.064   13.341  0.50 18.46 ?  88   LEU   A HG   1 
ATOM   1778 H  HG   B LEU   A 1 88  ? 24.284 5.159   13.480  0.50 18.75 ?  88   LEU   A HG   1 
ATOM   1779 H  HD11 A LEU   A 1 88  ? 23.408 5.338   11.267  0.50 18.26 ?  88   LEU   A HD11 1 
ATOM   1780 H  HD11 B LEU   A 1 88  ? 23.143 5.591   11.500  0.50 18.54 ?  88   LEU   A HD11 1 
ATOM   1781 H  HD12 A LEU   A 1 88  ? 24.361 4.066   11.237  0.50 18.26 ?  88   LEU   A HD12 1 
ATOM   1782 H  HD12 B LEU   A 1 88  ? 24.136 4.367   11.300  0.50 18.54 ?  88   LEU   A HD12 1 
ATOM   1783 H  HD13 A LEU   A 1 88  ? 22.789 3.878   11.366  0.50 18.26 ?  88   LEU   A HD13 1 
ATOM   1784 H  HD13 B LEU   A 1 88  ? 22.581 4.105   11.496  0.50 18.54 ?  88   LEU   A HD13 1 
ATOM   1785 H  HD21 A LEU   A 1 88  ? 22.214 5.930   13.314  0.50 20.50 ?  88   LEU   A HD21 1 
ATOM   1786 H  HD21 B LEU   A 1 88  ? 22.056 5.968   13.604  0.50 20.07 ?  88   LEU   A HD21 1 
ATOM   1787 H  HD22 A LEU   A 1 88  ? 21.667 4.466   13.599  0.50 20.50 ?  88   LEU   A HD22 1 
ATOM   1788 H  HD22 B LEU   A 1 88  ? 21.587 4.478   13.892  0.50 20.07 ?  88   LEU   A HD22 1 
ATOM   1789 H  HD23 A LEU   A 1 88  ? 22.555 5.209   14.688  0.50 20.50 ?  88   LEU   A HD23 1 
ATOM   1790 H  HD23 B LEU   A 1 88  ? 22.532 5.227   14.926  0.50 20.07 ?  88   LEU   A HD23 1 
ATOM   1791 N  N    . ALA   A 1 89  ? 25.622 1.031   15.505  1.00 13.44 ?  89   ALA   A N    1 
ATOM   1792 C  CA   . ALA   A 1 89  ? 25.942 -0.384  15.627  1.00 13.09 ?  89   ALA   A CA   1 
ATOM   1793 C  C    . ALA   A 1 89  ? 27.425 -0.454  15.938  1.00 13.35 ?  89   ALA   A C    1 
ATOM   1794 O  O    . ALA   A 1 89  ? 28.141 0.539   15.814  1.00 13.98 ?  89   ALA   A O    1 
ATOM   1795 C  CB   . ALA   A 1 89  ? 25.669 -1.102  14.306  1.00 12.75 ?  89   ALA   A CB   1 
ATOM   1796 H  H    A ALA   A 1 89  ? 26.318 1.535   15.430  0.50 16.15 ?  89   ALA   A H    1 
ATOM   1797 H  H    B ALA   A 1 89  ? 26.317 1.540   15.460  0.50 16.15 ?  89   ALA   A H    1 
ATOM   1798 H  HA   . ALA   A 1 89  ? 25.429 -0.789  16.344  1.00 15.73 ?  89   ALA   A HA   1 
ATOM   1799 H  HB1  . ALA   A 1 89  ? 25.919 -2.035  14.397  1.00 15.32 ?  89   ALA   A HB1  1 
ATOM   1800 H  HB2  . ALA   A 1 89  ? 24.722 -1.034  14.096  1.00 15.32 ?  89   ALA   A HB2  1 
ATOM   1801 H  HB3  . ALA   A 1 89  ? 26.194 -0.687  13.606  1.00 15.32 ?  89   ALA   A HB3  1 
ATOM   1802 N  N    A LYS   A 1 90  ? 27.897 -1.638  16.321  0.50 13.82 ?  90   LYS   A N    1 
ATOM   1803 N  N    B LYS   A 1 90  ? 27.893 -1.634  16.336  0.50 13.77 ?  90   LYS   A N    1 
ATOM   1804 C  CA   A LYS   A 1 90  ? 29.339 -1.798  16.486  0.50 14.43 ?  90   LYS   A CA   1 
ATOM   1805 C  CA   B LYS   A 1 90  ? 29.335 -1.797  16.483  0.50 14.31 ?  90   LYS   A CA   1 
ATOM   1806 C  C    A LYS   A 1 90  ? 30.057 -1.636  15.150  0.50 13.69 ?  90   LYS   A C    1 
ATOM   1807 C  C    B LYS   A 1 90  ? 30.032 -1.607  15.140  0.50 13.49 ?  90   LYS   A C    1 
ATOM   1808 O  O    A LYS   A 1 90  ? 31.023 -0.866  15.034  0.50 14.88 ?  90   LYS   A O    1 
ATOM   1809 O  O    B LYS   A 1 90  ? 30.942 -0.776  15.003  0.50 14.40 ?  90   LYS   A O    1 
ATOM   1810 C  CB   A LYS   A 1 90  ? 29.666 -3.147  17.126  0.50 16.68 ?  90   LYS   A CB   1 
ATOM   1811 C  CB   B LYS   A 1 90  ? 29.664 -3.161  17.091  0.50 16.59 ?  90   LYS   A CB   1 
ATOM   1812 C  CG   A LYS   A 1 90  ? 31.147 -3.325  17.436  0.50 20.32 ?  90   LYS   A CG   1 
ATOM   1813 C  CG   B LYS   A 1 90  ? 31.132 -3.324  17.452  0.50 20.18 ?  90   LYS   A CG   1 
ATOM   1814 C  CD   A LYS   A 1 90  ? 31.383 -4.551  18.304  0.50 23.97 ?  90   LYS   A CD   1 
ATOM   1815 C  CD   B LYS   A 1 90  ? 31.371 -4.614  18.218  0.50 23.73 ?  90   LYS   A CD   1 
ATOM   1816 C  CE   A LYS   A 1 90  ? 32.799 -4.587  18.863  0.50 26.86 ?  90   LYS   A CE   1 
ATOM   1817 C  CE   B LYS   A 1 90  ? 32.745 -4.632  18.867  0.50 26.58 ?  90   LYS   A CE   1 
ATOM   1818 N  NZ   A LYS   A 1 90  ? 33.813 -4.955  17.838  0.50 28.76 ?  90   LYS   A NZ   1 
ATOM   1819 N  NZ   B LYS   A 1 90  ? 33.843 -4.626  17.865  0.50 28.39 ?  90   LYS   A NZ   1 
ATOM   1820 H  H    A LYS   A 1 90  ? 27.421 -2.331  16.495  0.50 16.60 ?  90   LYS   A H    1 
ATOM   1821 H  H    B LYS   A 1 90  ? 27.415 -2.321  16.527  0.50 16.54 ?  90   LYS   A H    1 
ATOM   1822 H  HA   A LYS   A 1 90  ? 29.664 -1.105  17.078  0.50 17.34 ?  90   LYS   A HA   1 
ATOM   1823 H  HA   B LYS   A 1 90  ? 29.666 -1.117  17.087  0.50 17.19 ?  90   LYS   A HA   1 
ATOM   1824 H  HB2  A LYS   A 1 90  ? 29.174 -3.226  17.960  0.50 20.04 ?  90   LYS   A HB2  1 
ATOM   1825 H  HB2  B LYS   A 1 90  ? 29.142 -3.278  17.904  0.50 19.94 ?  90   LYS   A HB2  1 
ATOM   1826 H  HB3  A LYS   A 1 90  ? 29.399 -3.857  16.521  0.50 20.04 ?  90   LYS   A HB3  1 
ATOM   1827 H  HB3  B LYS   A 1 90  ? 29.434 -3.857  16.455  0.50 19.94 ?  90   LYS   A HB3  1 
ATOM   1828 H  HG2  A LYS   A 1 90  ? 31.638 -3.438  16.607  0.50 24.40 ?  90   LYS   A HG2  1 
ATOM   1829 H  HG2  B LYS   A 1 90  ? 31.662 -3.350  16.639  0.50 24.24 ?  90   LYS   A HG2  1 
ATOM   1830 H  HG3  A LYS   A 1 90  ? 31.470 -2.546  17.915  0.50 24.40 ?  90   LYS   A HG3  1 
ATOM   1831 H  HG3  B LYS   A 1 90  ? 31.411 -2.582  18.011  0.50 24.24 ?  90   LYS   A HG3  1 
ATOM   1832 H  HD2  A LYS   A 1 90  ? 30.763 -4.539  19.050  0.50 28.79 ?  90   LYS   A HD2  1 
ATOM   1833 H  HD2  B LYS   A 1 90  ? 30.703 -4.700  18.917  0.50 28.50 ?  90   LYS   A HD2  1 
ATOM   1834 H  HD3  A LYS   A 1 90  ? 31.248 -5.351  17.771  0.50 28.79 ?  90   LYS   A HD3  1 
ATOM   1835 H  HD3  B LYS   A 1 90  ? 31.314 -5.365  17.606  0.50 28.50 ?  90   LYS   A HD3  1 
ATOM   1836 H  HE2  A LYS   A 1 90  ? 33.025 -3.709  19.207  0.50 32.26 ?  90   LYS   A HE2  1 
ATOM   1837 H  HE2  B LYS   A 1 90  ? 32.842 -3.844  19.426  0.50 31.92 ?  90   LYS   A HE2  1 
ATOM   1838 H  HE3  A LYS   A 1 90  ? 32.841 -5.243  19.576  0.50 32.26 ?  90   LYS   A HE3  1 
ATOM   1839 H  HE3  B LYS   A 1 90  ? 32.832 -5.434  19.406  0.50 31.92 ?  90   LYS   A HE3  1 
ATOM   1840 H  HZ1  A LYS   A 1 90  ? 34.618 -5.016  18.214  0.50 34.54 ?  90   LYS   A HZ1  1 
ATOM   1841 H  HZ1  B LYS   A 1 90  ? 34.632 -4.618  18.278  0.50 34.09 ?  90   LYS   A HZ1  1 
ATOM   1842 H  HZ2  A LYS   A 1 90  ? 33.606 -5.740  17.473  0.50 34.54 ?  90   LYS   A HZ2  1 
ATOM   1843 H  HZ2  B LYS   A 1 90  ? 33.793 -5.355  17.355  0.50 34.09 ?  90   LYS   A HZ2  1 
ATOM   1844 H  HZ3  A LYS   A 1 90  ? 33.839 -4.337  17.199  0.50 34.54 ?  90   LYS   A HZ3  1 
ATOM   1845 H  HZ3  B LYS   A 1 90  ? 33.780 -3.906  17.348  0.50 34.09 ?  90   LYS   A HZ3  1 
ATOM   1846 N  N    . HIS   A 1 91  ? 29.579 -2.341  14.125  1.00 12.35 ?  91   HIS   A N    1 
ATOM   1847 C  CA   . HIS   A 1 91  ? 30.166 -2.322  12.800  1.00 11.66 ?  91   HIS   A CA   1 
ATOM   1848 C  C    . HIS   A 1 91  ? 29.087 -2.055  11.768  1.00 10.75 ?  91   HIS   A C    1 
ATOM   1849 O  O    . HIS   A 1 91  ? 27.918 -2.406  11.958  1.00 11.37 ?  91   HIS   A O    1 
ATOM   1850 C  CB   . HIS   A 1 91  ? 30.773 -3.684  12.442  1.00 13.79 ?  91   HIS   A CB   1 
ATOM   1851 C  CG   . HIS   A 1 91  ? 31.722 -4.218  13.465  1.00 17.86 ?  91   HIS   A CG   1 
ATOM   1852 N  ND1  . HIS   A 1 91  ? 33.015 -3.761  13.587  1.00 19.81 ?  91   HIS   A ND1  1 
ATOM   1853 C  CD2  . HIS   A 1 91  ? 31.574 -5.183  14.403  1.00 19.72 ?  91   HIS   A CD2  1 
ATOM   1854 C  CE1  . HIS   A 1 91  ? 33.623 -4.417  14.560  1.00 20.39 ?  91   HIS   A CE1  1 
ATOM   1855 N  NE2  . HIS   A 1 91  ? 32.770 -5.287  15.072  1.00 20.93 ?  91   HIS   A NE2  1 
ATOM   1856 H  H    A HIS   A 1 91  ? 28.891 -2.863  14.183  0.50 14.85 ?  91   HIS   A H    1 
ATOM   1857 H  H    B HIS   A 1 91  ? 28.906 -2.881  14.189  0.50 14.85 ?  91   HIS   A H    1 
ATOM   1858 H  HA   . HIS   A 1 91  ? 30.852 -1.640  12.740  1.00 14.02 ?  91   HIS   A HA   1 
ATOM   1859 H  HB2  . HIS   A 1 91  ? 30.056 -4.329  12.343  1.00 16.57 ?  91   HIS   A HB2  1 
ATOM   1860 H  HB3  . HIS   A 1 91  ? 31.257 -3.600  11.606  1.00 16.57 ?  91   HIS   A HB3  1 
ATOM   1861 H  HD1  . HIS   A 1 91  ? 33.374 -3.143  13.104  1.00 23.80 ?  91   HIS   A HD1  1 
ATOM   1862 H  HD2  . HIS   A 1 91  ? 30.810 -5.682  14.566  1.00 23.69 ?  91   HIS   A HD2  1 
ATOM   1863 H  HE1  . HIS   A 1 91  ? 34.504 -4.285  14.837  1.00 24.49 ?  91   HIS   A HE1  1 
ATOM   1864 N  N    . CYS   A 1 92  ? 29.500 -1.460  10.655  1.00 10.36 ?  92   CYS   A N    1 
ATOM   1865 C  CA   . CYS   A 1 92  ? 28.673 -1.381  9.460   1.00 10.46 ?  92   CYS   A CA   1 
ATOM   1866 C  C    . CYS   A 1 92  ? 29.328 -2.205  8.360   1.00 9.80  ?  92   CYS   A C    1 
ATOM   1867 O  O    . CYS   A 1 92  ? 30.489 -1.959  7.998   1.00 10.50 ?  92   CYS   A O    1 
ATOM   1868 C  CB   . CYS   A 1 92  ? 28.466 0.063   9.001   1.00 10.31 ?  92   CYS   A CB   1 
ATOM   1869 S  SG   . CYS   A 1 92  ? 27.456 0.159   7.481   1.00 9.92  ?  92   CYS   A SG   1 
ATOM   1870 H  H    . CYS   A 1 92  ? 30.274 -1.090  10.563  1.00 12.46 ?  92   CYS   A H    1 
ATOM   1871 H  HA   . CYS   A 1 92  ? 27.805 -1.760  9.650   1.00 12.57 ?  92   CYS   A HA   1 
ATOM   1872 H  HB2  . CYS   A 1 92  ? 28.002 0.561   9.696   1.00 12.39 ?  92   CYS   A HB2  1 
ATOM   1873 H  HB3  . CYS   A 1 92  ? 29.323 0.473   8.814   1.00 12.39 ?  92   CYS   A HB3  1 
ATOM   1874 H  HG   . CYS   A 1 92  ? 27.313 1.311   7.180   1.00 11.93 ?  92   CYS   A HG   1 
ATOM   1875 N  N    . LEU   A 1 93  ? 28.593 -3.192  7.858   1.00 9.63  ?  93   LEU   A N    1 
ATOM   1876 C  CA   . LEU   A 1 93  ? 29.004 -3.953  6.686   1.00 9.51  ?  93   LEU   A CA   1 
ATOM   1877 C  C    . LEU   A 1 93  ? 28.412 -3.263  5.462   1.00 8.81  ?  93   LEU   A C    1 
ATOM   1878 O  O    . LEU   A 1 93  ? 27.199 -3.322  5.227   1.00 9.08  ?  93   LEU   A O    1 
ATOM   1879 C  CB   . LEU   A 1 93  ? 28.521 -5.397  6.792   1.00 9.73  ?  93   LEU   A CB   1 
ATOM   1880 C  CG   . LEU   A 1 93  ? 28.915 -6.298  5.622   1.00 9.95  ?  93   LEU   A CG   1 
ATOM   1881 C  CD1  . LEU   A 1 93  ? 30.414 -6.554  5.610   1.00 11.09 ?  93   LEU   A CD1  1 
ATOM   1882 C  CD2  . LEU   A 1 93  ? 28.142 -7.624  5.662   1.00 10.62 ?  93   LEU   A CD2  1 
ATOM   1883 H  H    . LEU   A 1 93  ? 27.838 -3.441  8.192   1.00 11.57 ?  93   LEU   A H    1 
ATOM   1884 H  HA   . LEU   A 1 93  ? 29.967 -3.942  6.617   1.00 11.44 ?  93   LEU   A HA   1 
ATOM   1885 H  HB2  . LEU   A 1 93  ? 28.895 -5.783  7.602   1.00 11.70 ?  93   LEU   A HB2  1 
ATOM   1886 H  HB3  . LEU   A 1 93  ? 27.556 -5.398  6.847   1.00 11.70 ?  93   LEU   A HB3  1 
ATOM   1887 H  HG   . LEU   A 1 93  ? 28.700 -5.852  4.795   1.00 11.96 ?  93   LEU   A HG   1 
ATOM   1888 H  HD11 . LEU   A 1 93  ? 30.625 -7.172  4.894   1.00 13.33 ?  93   LEU   A HD11 1 
ATOM   1889 H  HD12 . LEU   A 1 93  ? 30.882 -5.717  5.476   1.00 13.33 ?  93   LEU   A HD12 1 
ATOM   1890 H  HD13 . LEU   A 1 93  ? 30.676 -6.944  6.465   1.00 13.33 ?  93   LEU   A HD13 1 
ATOM   1891 H  HD21 . LEU   A 1 93  ? 28.419 -8.175  4.910   1.00 12.77 ?  93   LEU   A HD21 1 
ATOM   1892 H  HD22 . LEU   A 1 93  ? 28.337 -8.083  6.494   1.00 12.77 ?  93   LEU   A HD22 1 
ATOM   1893 H  HD23 . LEU   A 1 93  ? 27.194 -7.435  5.601   1.00 12.77 ?  93   LEU   A HD23 1 
ATOM   1894 N  N    . HIS   A 1 94  ? 29.266 -2.577  4.704   1.00 8.88  ?  94   HIS   A N    1 
ATOM   1895 C  CA   . HIS   A 1 94  ? 28.852 -1.900  3.477   1.00 8.96  ?  94   HIS   A CA   1 
ATOM   1896 C  C    . HIS   A 1 94  ? 28.867 -2.932  2.363   1.00 8.86  ?  94   HIS   A C    1 
ATOM   1897 O  O    . HIS   A 1 94  ? 29.932 -3.447  2.021   1.00 10.21 ?  94   HIS   A O    1 
ATOM   1898 C  CB   . HIS   A 1 94  ? 29.809 -0.755  3.150   1.00 9.08  ?  94   HIS   A CB   1 
ATOM   1899 C  CG   . HIS   A 1 94  ? 29.788 0.337   4.161   1.00 9.10  ?  94   HIS   A CG   1 
ATOM   1900 N  ND1  . HIS   A 1 94  ? 28.912 1.399   4.099   1.00 9.42  ?  94   HIS   A ND1  1 
ATOM   1901 C  CD2  . HIS   A 1 94  ? 30.523 0.508   5.283   1.00 9.84  ?  94   HIS   A CD2  1 
ATOM   1902 C  CE1  . HIS   A 1 94  ? 29.124 2.184   5.140   1.00 9.52  ?  94   HIS   A CE1  1 
ATOM   1903 N  NE2  . HIS   A 1 94  ? 30.095 1.665   5.873   1.00 9.87  ?  94   HIS   A NE2  1 
ATOM   1904 H  H    . HIS   A 1 94  ? 30.101 -2.481  4.885   1.00 10.68 ?  94   HIS   A H    1 
ATOM   1905 H  HA   . HIS   A 1 94  ? 27.949 -1.550  3.573   1.00 10.77 ?  94   HIS   A HA   1 
ATOM   1906 H  HB2  . HIS   A 1 94  ? 30.706 -1.105  3.104   1.00 10.92 ?  94   HIS   A HB2  1 
ATOM   1907 H  HB3  . HIS   A 1 94  ? 29.552 -0.374  2.294   1.00 10.92 ?  94   HIS   A HB3  1 
ATOM   1908 H  HD2  . HIS   A 1 94  ? 31.195 -0.045  5.595   1.00 11.83 ?  94   HIS   A HD2  1 
ATOM   1909 H  HE1  . HIS   A 1 94  ? 28.657 2.973   5.319   1.00 11.45 ?  94   HIS   A HE1  1 
ATOM   1910 H  HE2  . HIS   A 1 94  ? 30.403 2.014   6.595   1.00 11.87 ?  94   HIS   A HE2  1 
ATOM   1911 N  N    . VAL   A 1 95  ? 27.696 -3.255  1.811   1.00 8.47  ?  95   VAL   A N    1 
ATOM   1912 C  CA   . VAL   A 1 95  ? 27.558 -4.291  0.791   1.00 8.83  ?  95   VAL   A CA   1 
ATOM   1913 C  C    . VAL   A 1 95  ? 27.015 -3.659  -0.477  1.00 8.54  ?  95   VAL   A C    1 
ATOM   1914 O  O    . VAL   A 1 95  ? 26.003 -2.947  -0.431  1.00 9.24  ?  95   VAL   A O    1 
ATOM   1915 C  CB   . VAL   A 1 95  ? 26.633 -5.431  1.248   1.00 9.22  ?  95   VAL   A CB   1 
ATOM   1916 C  CG1  . VAL   A 1 95  ? 26.538 -6.479  0.152   1.00 9.95  ?  95   VAL   A CG1  1 
ATOM   1917 C  CG2  . VAL   A 1 95  ? 27.125 -6.044  2.538   1.00 9.39  ?  95   VAL   A CG2  1 
ATOM   1918 H  H    . VAL   A 1 95  ? 26.951 -2.876  2.016   1.00 10.19 ?  95   VAL   A H    1 
ATOM   1919 H  HA   . VAL   A 1 95  ? 28.426 -4.667  0.594   1.00 10.62 ?  95   VAL   A HA   1 
ATOM   1920 H  HB   . VAL   A 1 95  ? 25.746 -5.083  1.407   1.00 11.09 ?  95   VAL   A HB   1 
ATOM   1921 H  HG11 . VAL   A 1 95  ? 26.159 -7.294  0.525   1.00 11.97 ?  95   VAL   A HG11 1 
ATOM   1922 H  HG12 . VAL   A 1 95  ? 25.967 -6.149  -0.557  1.00 11.97 ?  95   VAL   A HG12 1 
ATOM   1923 H  HG13 . VAL   A 1 95  ? 27.427 -6.663  -0.193  1.00 11.97 ?  95   VAL   A HG13 1 
ATOM   1924 H  HG21 . VAL   A 1 95  ? 26.566 -6.803  2.764   1.00 11.29 ?  95   VAL   A HG21 1 
ATOM   1925 H  HG22 . VAL   A 1 95  ? 28.045 -6.334  2.421   1.00 11.29 ?  95   VAL   A HG22 1 
ATOM   1926 H  HG23 . VAL   A 1 95  ? 27.078 -5.377  3.241   1.00 11.29 ?  95   VAL   A HG23 1 
ATOM   1927 N  N    . VAL   A 1 96  ? 27.654 -3.948  -1.608  1.00 8.80  ?  96   VAL   A N    1 
ATOM   1928 C  CA   . VAL   A 1 96  ? 27.246 -3.398  -2.896  1.00 9.35  ?  96   VAL   A CA   1 
ATOM   1929 C  C    . VAL   A 1 96  ? 26.447 -4.455  -3.649  1.00 9.31  ?  96   VAL   A C    1 
ATOM   1930 O  O    . VAL   A 1 96  ? 27.008 -5.403  -4.204  1.00 10.23 ?  96   VAL   A O    1 
ATOM   1931 C  CB   . VAL   A 1 96  ? 28.436 -2.921  -3.724  1.00 9.72  ?  96   VAL   A CB   1 
ATOM   1932 C  CG1  . VAL   A 1 96  ? 27.930 -2.296  -5.004  1.00 9.85  ?  96   VAL   A CG1  1 
ATOM   1933 C  CG2  . VAL   A 1 96  ? 29.289 -1.937  -2.941  1.00 10.15 ?  96   VAL   A CG2  1 
ATOM   1934 H  H    . VAL   A 1 96  ? 28.352 -4.457  -1.654  1.00 10.58 ?  96   VAL   A H    1 
ATOM   1935 H  HA   . VAL   A 1 96  ? 26.666 -2.639  -2.744  1.00 11.24 ?  96   VAL   A HA   1 
ATOM   1936 H  HB   . VAL   A 1 96  ? 28.990 -3.675  -3.959  1.00 11.69 ?  96   VAL   A HB   1 
ATOM   1937 H  HG11 . VAL   A 1 96  ? 28.658 -1.810  -5.423  1.00 11.84 ?  96   VAL   A HG11 1 
ATOM   1938 H  HG12 . VAL   A 1 96  ? 27.617 -2.996  -5.594  1.00 11.84 ?  96   VAL   A HG12 1 
ATOM   1939 H  HG13 . VAL   A 1 96  ? 27.206 -1.686  -4.793  1.00 11.84 ?  96   VAL   A HG13 1 
ATOM   1940 H  HG21 . VAL   A 1 96  ? 29.993 -1.598  -3.515  1.00 12.21 ?  96   VAL   A HG21 1 
ATOM   1941 H  HG22 . VAL   A 1 96  ? 28.729 -1.199  -2.640  1.00 12.21 ?  96   VAL   A HG22 1 
ATOM   1942 H  HG23 . VAL   A 1 96  ? 29.673 -2.389  -2.176  1.00 12.21 ?  96   VAL   A HG23 1 
ATOM   1943 N  N    . GLY   A 1 97  ? 25.132 -4.291  -3.698  1.00 9.66  ?  97   GLY   A N    1 
ATOM   1944 C  CA   . GLY   A 1 97  ? 24.319 -5.055  -4.610  1.00 10.07 ?  97   GLY   A CA   1 
ATOM   1945 C  C    . GLY   A 1 97  ? 24.325 -4.410  -5.980  1.00 10.34 ?  97   GLY   A C    1 
ATOM   1946 O  O    . GLY   A 1 97  ? 24.613 -3.218  -6.121  1.00 11.26 ?  97   GLY   A O    1 
ATOM   1947 H  H    . GLY   A 1 97  ? 24.694 -3.735  -3.209  1.00 11.61 ?  97   GLY   A H    1 
ATOM   1948 H  HA2  . GLY   A 1 97  ? 24.670 -5.956  -4.663  1.00 12.10 ?  97   GLY   A HA2  1 
ATOM   1949 H  HA3  . GLY   A 1 97  ? 23.405 -5.093  -4.279  1.00 12.10 ?  97   GLY   A HA3  1 
ATOM   1950 N  N    A PRO   A 1 98  ? 23.959 -5.150  -7.022  0.50 10.25 ?  98   PRO   A N    1 
ATOM   1951 N  N    B PRO   A 1 98  ? 24.050 -5.213  -7.011  0.50 10.71 ?  98   PRO   A N    1 
ATOM   1952 C  CA   A PRO   A 1 98  ? 23.834 -4.515  -8.341  0.50 10.84 ?  98   PRO   A CA   1 
ATOM   1953 C  CA   B PRO   A 1 98  ? 24.019 -4.685  -8.377  0.50 11.96 ?  98   PRO   A CA   1 
ATOM   1954 C  C    A PRO   A 1 98  ? 22.729 -3.464  -8.356  0.50 10.65 ?  98   PRO   A C    1 
ATOM   1955 C  C    B PRO   A 1 98  ? 22.911 -3.663  -8.551  0.50 12.46 ?  98   PRO   A C    1 
ATOM   1956 O  O    A PRO   A 1 98  ? 21.652 -3.656  -7.786  0.50 10.73 ?  98   PRO   A O    1 
ATOM   1957 O  O    B PRO   A 1 98  ? 21.828 -3.770  -7.969  0.50 12.58 ?  98   PRO   A O    1 
ATOM   1958 C  CB   A PRO   A 1 98  ? 23.519 -5.691  -9.273  0.50 10.90 ?  98   PRO   A CB   1 
ATOM   1959 C  CB   B PRO   A 1 98  ? 23.765 -5.931  -9.233  0.50 11.82 ?  98   PRO   A CB   1 
ATOM   1960 C  CG   A PRO   A 1 98  ? 22.921 -6.737  -8.384  0.50 11.00 ?  98   PRO   A CG   1 
ATOM   1961 C  CG   B PRO   A 1 98  ? 23.095 -6.896  -8.309  0.50 11.91 ?  98   PRO   A CG   1 
ATOM   1962 C  CD   A PRO   A 1 98  ? 23.629 -6.586  -7.059  0.50 10.52 ?  98   PRO   A CD   1 
ATOM   1963 C  CD   B PRO   A 1 98  ? 23.758 -6.658  -6.977  0.50 10.79 ?  98   PRO   A CD   1 
ATOM   1964 H  HA   A PRO   A 1 98  ? 24.671 -4.111  -8.596  0.50 13.03 ?  98   PRO   A HA   1 
ATOM   1965 H  HA   B PRO   A 1 98  ? 24.874 -4.295  -8.613  0.50 14.37 ?  98   PRO   A HA   1 
ATOM   1966 H  HB2  A PRO   A 1 98  ? 22.883 -5.414  -9.948  0.50 13.10 ?  98   PRO   A HB2  1 
ATOM   1967 H  HB2  B PRO   A 1 98  ? 23.179 -5.705  -9.973  0.50 14.20 ?  98   PRO   A HB2  1 
ATOM   1968 H  HB3  A PRO   A 1 98  ? 24.339 -6.014  -9.677  0.50 13.10 ?  98   PRO   A HB3  1 
ATOM   1969 H  HB3  B PRO   A 1 98  ? 24.604 -6.293  -9.555  0.50 14.20 ?  98   PRO   A HB3  1 
ATOM   1970 H  HG2  A PRO   A 1 98  ? 21.971 -6.580  -8.283  0.50 13.22 ?  98   PRO   A HG2  1 
ATOM   1971 H  HG2  B PRO   A 1 98  ? 22.145 -6.700  -8.262  0.50 14.31 ?  98   PRO   A HG2  1 
ATOM   1972 H  HG3  A PRO   A 1 98  ? 23.086 -7.618  -8.757  0.50 13.22 ?  98   PRO   A HG3  1 
ATOM   1973 H  HG3  B PRO   A 1 98  ? 23.245 -7.804  -8.616  0.50 14.31 ?  98   PRO   A HG3  1 
ATOM   1974 H  HD2  A PRO   A 1 98  ? 23.032 -6.825  -6.327  0.50 12.65 ?  98   PRO   A HD2  1 
ATOM   1975 H  HD2  B PRO   A 1 98  ? 23.147 -6.869  -6.253  0.50 12.98 ?  98   PRO   A HD2  1 
ATOM   1976 H  HD3  A PRO   A 1 98  ? 24.439 -7.119  -7.040  0.50 12.65 ?  98   PRO   A HD3  1 
ATOM   1977 H  HD3  B PRO   A 1 98  ? 24.578 -7.177  -6.910  0.50 12.98 ?  98   PRO   A HD3  1 
ATOM   1978 N  N    A ASN   A 1 99  ? 23.019 -2.333  -9.005  0.50 11.13 ?  99   ASN   A N    1 
ATOM   1979 N  N    B ASN   A 1 99  ? 23.199 -2.667  -9.370  0.50 12.78 ?  99   ASN   A N    1 
ATOM   1980 C  CA   A ASN   A 1 99  ? 22.047 -1.264  -9.230  0.50 12.27 ?  99   ASN   A CA   1 
ATOM   1981 C  CA   B ASN   A 1 99  ? 22.259 -1.609  -9.697  0.50 13.50 ?  99   ASN   A CA   1 
ATOM   1982 C  C    A ASN   A 1 99  ? 21.511 -1.407  -10.651 0.50 13.69 ?  99   ASN   A C    1 
ATOM   1983 C  C    B ASN   A 1 99  ? 21.616 -1.956  -11.033 0.50 14.31 ?  99   ASN   A C    1 
ATOM   1984 O  O    A ASN   A 1 99  ? 22.202 -1.074  -11.622 0.50 14.45 ?  99   ASN   A O    1 
ATOM   1985 O  O    B ASN   A 1 99  ? 22.256 -1.856  -12.087 0.50 13.96 ?  99   ASN   A O    1 
ATOM   1986 C  CB   A ASN   A 1 99  ? 22.691 0.109   -9.036  0.50 12.44 ?  99   ASN   A CB   1 
ATOM   1987 C  CB   B ASN   A 1 99  ? 22.988 -0.273  -9.762  0.50 14.27 ?  99   ASN   A CB   1 
ATOM   1988 C  CG   A ASN   A 1 99  ? 21.671 1.249   -9.022  0.50 12.91 ?  99   ASN   A CG   1 
ATOM   1989 C  CG   B ASN   A 1 99  ? 22.057 0.878   -10.019 0.50 14.99 ?  99   ASN   A CG   1 
ATOM   1990 O  OD1  A ASN   A 1 99  ? 20.668 1.210   -9.736  0.50 13.28 ?  99   ASN   A OD1  1 
ATOM   1991 O  OD1  B ASN   A 1 99  ? 21.026 0.718   -10.664 0.50 14.95 ?  99   ASN   A OD1  1 
ATOM   1992 N  ND2  A ASN   A 1 99  ? 21.929 2.266   -8.203  0.50 13.32 ?  99   ASN   A ND2  1 
ATOM   1993 N  ND2  B ASN   A 1 99  ? 22.412 2.052   -9.512  0.50 16.56 ?  99   ASN   A ND2  1 
ATOM   1994 H  H    A ASN   A 1 99  ? 23.797 -2.154  -9.316  0.50 13.38 ?  99   ASN   A H    1 
ATOM   1995 H  H    B ASN   A 1 99  ? 23.962 -2.584  -9.751  0.50 15.36 ?  99   ASN   A H    1 
ATOM   1996 H  HA   A ASN   A 1 99  ? 21.307 -1.354  -8.603  0.50 14.74 ?  99   ASN   A HA   1 
ATOM   1997 H  HA   B ASN   A 1 99  ? 21.567 -1.564  -9.014  0.50 16.23 ?  99   ASN   A HA   1 
ATOM   1998 H  HB2  A ASN   A 1 99  ? 23.168 0.118   -8.194  0.50 14.95 ?  99   ASN   A HB2  1 
ATOM   1999 H  HB2  B ASN   A 1 99  ? 23.438 -0.118  -8.917  0.50 17.15 ?  99   ASN   A HB2  1 
ATOM   2000 H  HB3  A ASN   A 1 99  ? 23.309 0.267   -9.770  0.50 14.95 ?  99   ASN   A HB3  1 
ATOM   2001 H  HB3  B ASN   A 1 99  ? 23.636 -0.308  -10.482 0.50 17.15 ?  99   ASN   A HB3  1 
ATOM   2002 H  HD21 A ASN   A 1 99  ? 21.391 2.934   -8.158  0.50 16.01 ?  99   ASN   A HD21 1 
ATOM   2003 H  HD21 B ASN   A 1 99  ? 21.917 2.743   -9.634  0.50 19.89 ?  99   ASN   A HD21 1 
ATOM   2004 H  HD22 A ASN   A 1 99  ? 22.641 2.255   -7.717  0.50 16.01 ?  99   ASN   A HD22 1 
ATOM   2005 H  HD22 B ASN   A 1 99  ? 23.145 2.122   -9.065  0.50 19.89 ?  99   ASN   A HD22 1 
ATOM   2006 N  N    A VAL   A 1 100 ? 20.276 -1.907  -10.762 0.50 15.13 ?  100  VAL   A N    1 
ATOM   2007 N  N    B VAL   A 1 100 ? 20.350 -2.375  -10.969 0.50 15.92 ?  100  VAL   A N    1 
ATOM   2008 C  CA   A VAL   A 1 100 ? 19.670 -2.153  -12.068 0.50 16.74 ?  100  VAL   A CA   1 
ATOM   2009 C  CA   B VAL   A 1 100 ? 19.588 -2.747  -12.158 0.50 17.70 ?  100  VAL   A CA   1 
ATOM   2010 C  C    A VAL   A 1 100 ? 19.513 -0.852  -12.842 0.50 16.96 ?  100  VAL   A C    1 
ATOM   2011 C  C    B VAL   A 1 100 ? 19.574 -1.607  -13.165 0.50 17.42 ?  100  VAL   A C    1 
ATOM   2012 O  O    A VAL   A 1 100 ? 19.580 -0.843  -14.077 0.50 17.35 ?  100  VAL   A O    1 
ATOM   2013 O  O    B VAL   A 1 100 ? 19.623 -1.828  -14.382 0.50 17.99 ?  100  VAL   A O    1 
ATOM   2014 C  CB   A VAL   A 1 100 ? 18.335 -2.917  -11.905 0.50 18.48 ?  100  VAL   A CB   1 
ATOM   2015 C  CB   B VAL   A 1 100 ? 18.161 -3.155  -11.738 0.50 20.17 ?  100  VAL   A CB   1 
ATOM   2016 C  CG1  A VAL   A 1 100 ? 17.669 -3.164  -13.256 0.50 19.20 ?  100  VAL   A CG1  1 
ATOM   2017 C  CG1  B VAL   A 1 100 ? 17.118 -2.610  -12.711 0.50 21.23 ?  100  VAL   A CG1  1 
ATOM   2018 C  CG2  A VAL   A 1 100 ? 18.571 -4.242  -11.188 0.50 18.62 ?  100  VAL   A CG2  1 
ATOM   2019 C  CG2  B VAL   A 1 100 ? 18.058 -4.662  -11.618 0.50 21.07 ?  100  VAL   A CG2  1 
ATOM   2020 H  H    A VAL   A 1 100 ? 19.762 -2.112  -10.092 0.50 18.18 ?  100  VAL   A H    1 
ATOM   2021 H  H    B VAL   A 1 100 ? 19.909 -2.452  -10.235 0.50 19.12 ?  100  VAL   A H    1 
ATOM   2022 H  HA   A VAL   A 1 100 ? 20.259 -2.729  -12.577 0.50 20.11 ?  100  VAL   A HA   1 
ATOM   2023 H  HA   B VAL   A 1 100 ? 20.007 -3.512  -12.578 0.50 21.27 ?  100  VAL   A HA   1 
ATOM   2024 H  HB   A VAL   A 1 100 ? 17.726 -2.393  -11.364 0.50 22.20 ?  100  VAL   A HB   1 
ATOM   2025 H  HB   B VAL   A 1 100 ? 17.972 -2.776  -10.864 0.50 24.23 ?  100  VAL   A HB   1 
ATOM   2026 H  HG11 A VAL   A 1 100 ? 16.922 -3.775  -13.137 0.50 23.07 ?  100  VAL   A HG11 1 
ATOM   2027 H  HG11 B VAL   A 1 100 ? 16.260 -3.000  -12.487 0.50 25.50 ?  100  VAL   A HG11 1 
ATOM   2028 H  HG12 A VAL   A 1 100 ? 17.348 -2.320  -13.610 0.50 23.07 ?  100  VAL   A HG12 1 
ATOM   2029 H  HG12 B VAL   A 1 100 ? 17.064 -1.643  -12.621 0.50 25.50 ?  100  VAL   A HG12 1 
ATOM   2030 H  HG13 A VAL   A 1 100 ? 18.317 -3.554  -13.862 0.50 23.07 ?  100  VAL   A HG13 1 
ATOM   2031 H  HG13 B VAL   A 1 100 ? 17.360 -2.855  -13.616 0.50 25.50 ?  100  VAL   A HG13 1 
ATOM   2032 H  HG21 A VAL   A 1 100 ? 17.741 -4.747  -11.169 0.50 22.37 ?  100  VAL   A HG21 1 
ATOM   2033 H  HG21 B VAL   A 1 100 ? 17.153 -4.893  -11.358 0.50 25.31 ?  100  VAL   A HG21 1 
ATOM   2034 H  HG22 A VAL   A 1 100 ? 19.249 -4.744  -11.667 0.50 22.37 ?  100  VAL   A HG22 1 
ATOM   2035 H  HG22 B VAL   A 1 100 ? 18.270 -5.059  -12.476 0.50 25.31 ?  100  VAL   A HG22 1 
ATOM   2036 H  HG23 A VAL   A 1 100 ? 18.869 -4.064  -10.283 0.50 22.37 ?  100  VAL   A HG23 1 
ATOM   2037 H  HG23 B VAL   A 1 100 ? 18.686 -4.967  -10.946 0.50 25.31 ?  100  VAL   A HG23 1 
ATOM   2038 N  N    A ASN   A 1 101 ? 19.312 0.263   -12.144 0.50 17.58 ?  101  ASN   A N    1 
ATOM   2039 N  N    B ASN   A 1 101 ? 19.471 -0.372  -12.676 0.50 17.11 ?  101  ASN   A N    1 
ATOM   2040 C  CA   A ASN   A 1 101 ? 19.240 1.548   -12.827 0.50 18.56 ?  101  ASN   A CA   1 
ATOM   2041 C  CA   B ASN   A 1 101 ? 19.373 0.784   -13.559 0.50 17.73 ?  101  ASN   A CA   1 
ATOM   2042 C  C    A ASN   A 1 101 ? 20.590 1.998   -13.385 0.50 20.58 ?  101  ASN   A C    1 
ATOM   2043 C  C    B ASN   A 1 101 ? 20.670 1.052   -14.310 0.50 18.16 ?  101  ASN   A C    1 
ATOM   2044 O  O    A ASN   A 1 101 ? 20.648 3.044   -14.043 0.50 21.77 ?  101  ASN   A O    1 
ATOM   2045 O  O    B ASN   A 1 101 ? 20.646 1.754   -15.328 0.50 18.53 ?  101  ASN   A O    1 
ATOM   2046 C  CB   A ASN   A 1 101 ? 18.635 2.598   -11.894 0.50 17.53 ?  101  ASN   A CB   1 
ATOM   2047 C  CB   B ASN   A 1 101 ? 18.975 2.018   -12.749 0.50 17.61 ?  101  ASN   A CB   1 
ATOM   2048 C  CG   A ASN   A 1 101 ? 17.251 2.204   -11.404 0.50 16.73 ?  101  ASN   A CG   1 
ATOM   2049 C  CG   B ASN   A 1 101 ? 17.707 1.800   -11.937 0.50 18.43 ?  101  ASN   A CG   1 
ATOM   2050 O  OD1  A ASN   A 1 101 ? 16.425 1.716   -12.175 0.50 16.45 ?  101  ASN   A OD1  1 
ATOM   2051 O  OD1  B ASN   A 1 101 ? 16.730 1.228   -12.421 0.50 19.51 ?  101  ASN   A OD1  1 
ATOM   2052 N  ND2  A ASN   A 1 101 ? 16.998 2.397   -10.115 0.50 17.02 ?  101  ASN   A ND2  1 
ATOM   2053 N  ND2  B ASN   A 1 101 ? 17.723 2.247   -10.690 0.50 18.59 ?  101  ASN   A ND2  1 
ATOM   2054 H  H    A ASN   A 1 101 ? 19.206 0.299   -11.294 0.50 21.12 ?  101  ASN   A H    1 
ATOM   2055 H  H    B ASN   A 1 101 ? 19.450 -0.176  -11.837 0.50 20.55 ?  101  ASN   A H    1 
ATOM   2056 H  HA   A ASN   A 1 101 ? 18.639 1.451   -13.582 0.50 22.29 ?  101  ASN   A HA   1 
ATOM   2057 H  HA   B ASN   A 1 101 ? 18.681 0.622   -14.215 0.50 21.30 ?  101  ASN   A HA   1 
ATOM   2058 H  HB2  A ASN   A 1 101 ? 19.213 2.706   -11.125 0.50 21.06 ?  101  ASN   A HB2  1 
ATOM   2059 H  HB2  B ASN   A 1 101 ? 19.692 2.241   -12.134 0.50 21.16 ?  101  ASN   A HB2  1 
ATOM   2060 H  HB3  A ASN   A 1 101 ? 18.556 3.435   -12.377 0.50 21.06 ?  101  ASN   A HB3  1 
ATOM   2061 H  HB3  B ASN   A 1 101 ? 18.820 2.760   -13.358 0.50 21.16 ?  101  ASN   A HB3  1 
ATOM   2062 H  HD21 A ASN   A 1 101 ? 16.231 2.182   -9.791  0.50 20.44 ?  101  ASN   A HD21 1 
ATOM   2063 H  HD21 B ASN   A 1 101 ? 17.030 2.145   -10.193 0.50 22.33 ?  101  ASN   A HD21 1 
ATOM   2064 H  HD22 A ASN   A 1 101 ? 17.601 2.737   -9.606  0.50 20.44 ?  101  ASN   A HD22 1 
ATOM   2065 H  HD22 B ASN   A 1 101 ? 18.422 2.641   -10.384 0.50 22.33 ?  101  ASN   A HD22 1 
ATOM   2066 N  N    A LYS   A 1 102 ? 21.660 1.232   -13.146 0.50 21.43 ?  102  LYS   A N    1 
ATOM   2067 N  N    B LYS   A 1 102 ? 21.793 0.521   -13.828 0.50 19.67 ?  102  LYS   A N    1 
ATOM   2068 C  CA   A LYS   A 1 102 ? 22.947 1.423   -13.805 0.50 22.25 ?  102  LYS   A CA   1 
ATOM   2069 C  CA   B LYS   A 1 102 ? 23.087 0.648   -14.486 0.50 20.58 ?  102  LYS   A CA   1 
ATOM   2070 C  C    A LYS   A 1 102 ? 23.256 0.334   -14.821 0.50 22.81 ?  102  LYS   A C    1 
ATOM   2071 C  C    B LYS   A 1 102 ? 23.413 -0.541  -15.385 0.50 19.69 ?  102  LYS   A C    1 
ATOM   2072 O  O    A LYS   A 1 102 ? 24.324 0.374   -15.440 0.50 23.16 ?  102  LYS   A O    1 
ATOM   2073 O  O    B LYS   A 1 102 ? 24.539 -0.636  -15.882 0.50 19.84 ?  102  LYS   A O    1 
ATOM   2074 C  CB   A LYS   A 1 102 ? 24.078 1.469   -12.770 0.50 23.55 ?  102  LYS   A CB   1 
ATOM   2075 C  CB   B LYS   A 1 102 ? 24.205 0.784   -13.443 0.50 23.50 ?  102  LYS   A CB   1 
ATOM   2076 C  CG   A LYS   A 1 102 ? 23.978 2.611   -11.782 0.50 24.46 ?  102  LYS   A CG   1 
ATOM   2077 C  CG   B LYS   A 1 102 ? 24.431 2.183   -12.899 0.50 25.99 ?  102  LYS   A CG   1 
ATOM   2078 C  CD   A LYS   A 1 102 ? 25.118 2.559   -10.779 0.50 25.61 ?  102  LYS   A CD   1 
ATOM   2079 C  CD   B LYS   A 1 102 ? 25.925 2.460   -12.762 0.50 28.49 ?  102  LYS   A CD   1 
ATOM   2080 C  CE   A LYS   A 1 102 ? 25.080 3.740   -9.828  0.50 26.70 ?  102  LYS   A CE   1 
ATOM   2081 C  CE   B LYS   A 1 102 ? 26.201 3.733   -11.981 0.50 30.02 ?  102  LYS   A CE   1 
ATOM   2082 N  NZ   A LYS   A 1 102 ? 26.126 3.633   -8.773  0.50 27.17 ?  102  LYS   A NZ   1 
ATOM   2083 N  NZ   B LYS   A 1 102 ? 27.597 4.217   -12.184 0.50 30.90 ?  102  LYS   A NZ   1 
ATOM   2084 H  H    A LYS   A 1 102 ? 21.664 0.573   -12.589 0.50 25.74 ?  102  LYS   A H    1 
ATOM   2085 H  H    B LYS   A 1 102 ? 21.829 0.071   -13.092 0.50 23.62 ?  102  LYS   A H    1 
ATOM   2086 H  HA   A LYS   A 1 102 ? 22.939 2.262   -14.278 0.50 26.73 ?  102  LYS   A HA   1 
ATOM   2087 H  HA   B LYS   A 1 102 ? 23.087 1.452   -15.025 0.50 24.72 ?  102  LYS   A HA   1 
ATOM   2088 H  HB2  A LYS   A 1 102 ? 24.072 0.640   -12.265 0.50 28.28 ?  102  LYS   A HB2  1 
ATOM   2089 H  HB2  B LYS   A 1 102 ? 23.996 0.212   -12.689 0.50 28.22 ?  102  LYS   A HB2  1 
ATOM   2090 H  HB3  A LYS   A 1 102 ? 24.923 1.557   -13.239 0.50 28.28 ?  102  LYS   A HB3  1 
ATOM   2091 H  HB3  B LYS   A 1 102 ? 25.040 0.496   -13.844 0.50 28.22 ?  102  LYS   A HB3  1 
ATOM   2092 H  HG2  A LYS   A 1 102 ? 24.027 3.453   -12.261 0.50 29.37 ?  102  LYS   A HG2  1 
ATOM   2093 H  HG2  B LYS   A 1 102 ? 24.052 2.836   -13.507 0.50 31.22 ?  102  LYS   A HG2  1 
ATOM   2094 H  HG3  A LYS   A 1 102 ? 23.139 2.544   -11.299 0.50 29.37 ?  102  LYS   A HG3  1 
ATOM   2095 H  HG3  B LYS   A 1 102 ? 24.024 2.260   -12.021 0.50 31.22 ?  102  LYS   A HG3  1 
ATOM   2096 H  HD2  A LYS   A 1 102 ? 25.046 1.745   -10.256 0.50 30.76 ?  102  LYS   A HD2  1 
ATOM   2097 H  HD2  B LYS   A 1 102 ? 26.346 1.721   -12.295 0.50 34.21 ?  102  LYS   A HD2  1 
ATOM   2098 H  HD3  A LYS   A 1 102 ? 25.963 2.577   -11.255 0.50 30.76 ?  102  LYS   A HD3  1 
ATOM   2099 H  HD3  B LYS   A 1 102 ? 26.313 2.559   -13.647 0.50 34.21 ?  102  LYS   A HD3  1 
ATOM   2100 H  HE2  A LYS   A 1 102 ? 25.237 4.557   -10.330 0.50 32.06 ?  102  LYS   A HE2  1 
ATOM   2101 H  HE2  B LYS   A 1 102 ? 25.593 4.428   -12.277 0.50 36.05 ?  102  LYS   A HE2  1 
ATOM   2102 H  HE3  A LYS   A 1 102 ? 24.213 3.775   -9.397  0.50 32.06 ?  102  LYS   A HE3  1 
ATOM   2103 H  HE3  B LYS   A 1 102 ? 26.075 3.559   -11.034 0.50 36.05 ?  102  LYS   A HE3  1 
ATOM   2104 H  HZ1  A LYS   A 1 102 ? 26.083 4.336   -8.231  0.50 32.62 ?  102  LYS   A HZ1  1 
ATOM   2105 H  HZ1  B LYS   A 1 102 ? 27.733 4.962   -11.716 0.50 37.10 ?  102  LYS   A HZ1  1 
ATOM   2106 H  HZ2  A LYS   A 1 102 ? 26.000 2.891   -8.298  0.50 32.62 ?  102  LYS   A HZ2  1 
ATOM   2107 H  HZ2  B LYS   A 1 102 ? 28.177 3.597   -11.915 0.50 37.10 ?  102  LYS   A HZ2  1 
ATOM   2108 H  HZ3  A LYS   A 1 102 ? 26.932 3.603   -9.147  0.50 32.62 ?  102  LYS   A HZ3  1 
ATOM   2109 H  HZ3  B LYS   A 1 102 ? 27.738 4.388   -13.046 0.50 37.10 ?  102  LYS   A HZ3  1 
ATOM   2110 N  N    A GLY   A 1 103 ? 22.364 -0.639  -15.004 0.50 23.84 ?  103  GLY   A N    1 
ATOM   2111 N  N    B GLY   A 1 103 ? 22.471 -1.458  -15.587 0.50 18.89 ?  103  GLY   A N    1 
ATOM   2112 C  CA   A GLY   A 1 103 ? 22.610 -1.726  -15.930 0.50 24.26 ?  103  GLY   A CA   1 
ATOM   2113 C  CA   B GLY   A 1 103 ? 22.759 -2.652  -16.357 0.50 18.86 ?  103  GLY   A CA   1 
ATOM   2114 C  C    A GLY   A 1 103 ? 23.496 -2.823  -15.393 0.50 24.67 ?  103  GLY   A C    1 
ATOM   2115 C  C    B GLY   A 1 103 ? 23.594 -3.692  -15.643 0.50 17.75 ?  103  GLY   A C    1 
ATOM   2116 O  O    A GLY   A 1 103 ? 24.138 -3.524  -16.181 0.50 25.19 ?  103  GLY   A O    1 
ATOM   2117 O  O    B GLY   A 1 103 ? 24.044 -4.649  -16.281 0.50 18.01 ?  103  GLY   A O    1 
ATOM   2118 H  H    A GLY   A 1 103 ? 21.611 -0.698  -14.598 0.50 28.63 ?  103  GLY   A H    1 
ATOM   2119 H  H    B GLY   A 1 103 ? 21.663 -1.400  -15.296 0.50 22.69 ?  103  GLY   A H    1 
ATOM   2120 H  HA2  A GLY   A 1 103 ? 21.758 -2.109  -16.212 0.50 29.13 ?  103  GLY   A HA2  1 
ATOM   2121 H  HA2  B GLY   A 1 103 ? 21.923 -3.068  -16.605 0.50 22.65 ?  103  GLY   A HA2  1 
ATOM   2122 H  HA3  A GLY   A 1 103 ? 23.053 -1.381  -16.717 0.50 29.13 ?  103  GLY   A HA3  1 
ATOM   2123 H  HA3  B GLY   A 1 103 ? 23.218 -2.388  -17.173 0.50 22.65 ?  103  GLY   A HA3  1 
ATOM   2124 N  N    A GLU   A 1 104 ? 23.567 -2.987  -14.075 0.50 24.00 ?  104  GLU   A N    1 
ATOM   2125 N  N    B GLU   A 1 104 ? 23.811 -3.542  -14.338 0.50 16.38 ?  104  GLU   A N    1 
ATOM   2126 C  CA   A GLU   A 1 104 ? 24.437 -3.985  -13.472 0.50 23.22 ?  104  GLU   A CA   1 
ATOM   2127 C  CA   B GLU   A 1 104 ? 24.657 -4.479  -13.612 0.50 14.59 ?  104  GLU   A CA   1 
ATOM   2128 C  C    A GLU   A 1 104 ? 23.743 -5.341  -13.379 0.50 23.51 ?  104  GLU   A C    1 
ATOM   2129 C  C    B GLU   A 1 104 ? 23.940 -5.814  -13.425 0.50 14.11 ?  104  GLU   A C    1 
ATOM   2130 O  O    A GLU   A 1 104 ? 22.516 -5.433  -13.280 0.50 23.68 ?  104  GLU   A O    1 
ATOM   2131 O  O    B GLU   A 1 104 ? 22.723 -5.867  -13.216 0.50 15.42 ?  104  GLU   A O    1 
ATOM   2132 C  CB   A GLU   A 1 104 ? 24.921 -3.504  -12.101 0.50 22.31 ?  104  GLU   A CB   1 
ATOM   2133 C  CB   B GLU   A 1 104 ? 25.087 -3.868  -12.274 0.50 13.91 ?  104  GLU   A CB   1 
ATOM   2134 C  CG   A GLU   A 1 104 ? 25.932 -2.361  -12.231 0.50 21.76 ?  104  GLU   A CG   1 
ATOM   2135 C  CG   B GLU   A 1 104 ? 25.870 -2.563  -12.470 0.50 14.19 ?  104  GLU   A CG   1 
ATOM   2136 C  CD   A GLU   A 1 104 ? 26.152 -1.563  -10.953 0.50 21.29 ?  104  GLU   A CD   1 
ATOM   2137 C  CD   B GLU   A 1 104 ? 26.309 -1.857  -11.197 0.50 14.25 ?  104  GLU   A CD   1 
ATOM   2138 O  OE1  A GLU   A 1 104 ? 25.562 -1.906  -9.909  0.50 20.28 ?  104  GLU   A OE1  1 
ATOM   2139 O  OE1  B GLU   A 1 104 ? 25.794 -2.158  -10.103 0.50 14.08 ?  104  GLU   A OE1  1 
ATOM   2140 O  OE2  A GLU   A 1 104 ? 26.914 -0.572  -11.001 0.50 21.82 -1 104  GLU   A OE2  1 
ATOM   2141 O  OE2  B GLU   A 1 104 ? 27.182 -0.965  -11.311 0.50 15.17 -1 104  GLU   A OE2  1 
ATOM   2142 H  H    A GLU   A 1 104 ? 23.126 -2.519  -13.504 0.50 28.82 ?  104  GLU   A H    1 
ATOM   2143 H  H    B GLU   A 1 104 ? 23.480 -2.908  -13.856 0.50 19.67 ?  104  GLU   A H    1 
ATOM   2144 H  HA   A GLU   A 1 104 ? 25.210 -4.099  -14.037 0.50 27.89 ?  104  GLU   A HA   1 
ATOM   2145 H  HA   B GLU   A 1 104 ? 25.459 -4.641  -14.135 0.50 17.53 ?  104  GLU   A HA   1 
ATOM   2146 H  HB2  A GLU   A 1 104 ? 24.161 -3.186  -11.590 0.50 26.79 ?  104  GLU   A HB2  1 
ATOM   2147 H  HB2  B GLU   A 1 104 ? 24.300 -3.677  -11.746 0.50 16.72 ?  104  GLU   A HB2  1 
ATOM   2148 H  HB3  A GLU   A 1 104 ? 25.349 -4.243  -11.639 0.50 26.79 ?  104  GLU   A HB3  1 
ATOM   2149 H  HB3  B GLU   A 1 104 ? 25.661 -4.497  -11.812 0.50 16.72 ?  104  GLU   A HB3  1 
ATOM   2150 H  HG2  A GLU   A 1 104 ? 26.780 -2.735  -12.516 0.50 26.13 ?  104  GLU   A HG2  1 
ATOM   2151 H  HG2  B GLU   A 1 104 ? 26.669 -2.755  -12.974 0.50 17.05 ?  104  GLU   A HG2  1 
ATOM   2152 H  HG3  A GLU   A 1 104 ? 25.608 -1.740  -12.902 0.50 26.13 ?  104  GLU   A HG3  1 
ATOM   2153 H  HG3  B GLU   A 1 104 ? 25.309 -1.940  -12.959 0.50 17.05 ?  104  GLU   A HG3  1 
ATOM   2154 N  N    A ASP   A 1 105 ? 24.555 -6.397  -13.419 0.50 23.97 ?  105  ASP   A N    1 
ATOM   2155 N  N    B ASP   A 1 105 ? 24.711 -6.897  -13.519 0.50 14.68 ?  105  ASP   A N    1 
ATOM   2156 C  CA   A ASP   A 1 105 ? 24.058 -7.761  -13.552 0.50 24.55 ?  105  ASP   A CA   1 
ATOM   2157 C  CA   B ASP   A 1 105 ? 24.177 -8.256  -13.585 0.50 15.83 ?  105  ASP   A CA   1 
ATOM   2158 C  C    A ASP   A 1 105 ? 23.364 -8.194  -12.264 0.50 22.78 ?  105  ASP   A C    1 
ATOM   2159 C  C    B ASP   A 1 105 ? 23.476 -8.637  -12.283 0.50 14.54 ?  105  ASP   A C    1 
ATOM   2160 O  O    A ASP   A 1 105 ? 23.990 -8.246  -11.201 0.50 21.64 ?  105  ASP   A O    1 
ATOM   2161 O  O    B ASP   A 1 105 ? 24.097 -8.669  -11.217 0.50 12.97 ?  105  ASP   A O    1 
ATOM   2162 C  CB   A ASP   A 1 105 ? 25.236 -8.685  -13.865 0.50 26.77 ?  105  ASP   A CB   1 
ATOM   2163 C  CB   B ASP   A 1 105 ? 25.343 -9.205  -13.867 0.50 18.72 ?  105  ASP   A CB   1 
ATOM   2164 C  CG   A ASP   A 1 105 ? 24.799 -10.088 -14.213 0.50 28.63 ?  105  ASP   A CG   1 
ATOM   2165 C  CG   B ASP   A 1 105 ? 24.951 -10.667 -13.814 0.50 21.10 ?  105  ASP   A CG   1 
ATOM   2166 O  OD1  A ASP   A 1 105 ? 23.577 -10.323 -14.295 0.50 29.10 ?  105  ASP   A OD1  1 
ATOM   2167 O  OD1  B ASP   A 1 105 ? 23.745 -10.975 -13.897 0.50 20.98 ?  105  ASP   A OD1  1 
ATOM   2168 O  OD2  A ASP   A 1 105 ? 25.680 -10.952 -14.414 0.50 29.61 -1 105  ASP   A OD2  1 
ATOM   2169 O  OD2  B ASP   A 1 105 ? 25.868 -11.511 -13.685 0.50 23.10 -1 105  ASP   A OD2  1 
ATOM   2170 H  H    A ASP   A 1 105 ? 25.413 -6.355  -13.364 0.50 28.79 ?  105  ASP   A H    1 
ATOM   2171 H  H    B ASP   A 1 105 ? 25.570 -6.861  -13.564 0.50 17.64 ?  105  ASP   A H    1 
ATOM   2172 H  HA   A ASP   A 1 105 ? 23.424 -7.823  -14.283 0.50 29.48 ?  105  ASP   A HA   1 
ATOM   2173 H  HA   B ASP   A 1 105 ? 23.537 -8.316  -14.313 0.50 19.02 ?  105  ASP   A HA   1 
ATOM   2174 H  HB2  A ASP   A 1 105 ? 25.721 -8.341  -14.635 0.50 32.14 ?  105  ASP   A HB2  1 
ATOM   2175 H  HB2  B ASP   A 1 105 ? 25.700 -9.006  -14.750 0.50 22.49 ?  105  ASP   A HB2  1 
ATOM   2176 H  HB3  A ASP   A 1 105 ? 25.830 -8.726  -13.097 0.50 32.14 ?  105  ASP   A HB3  1 
ATOM   2177 H  HB3  B ASP   A 1 105 ? 26.026 -9.068  -13.197 0.50 22.49 ?  105  ASP   A HB3  1 
ATOM   2178 N  N    A ILE   A 1 106 ? 22.068 -8.508  -12.360 0.50 22.22 ?  106  ILE   A N    1 
ATOM   2179 N  N    B ILE   A 1 106 ? 22.182 -8.951  -12.371 0.50 15.27 ?  106  ILE   A N    1 
ATOM   2180 C  CA   A ILE   A 1 106 ? 21.313 -8.946  -11.191 0.50 21.25 ?  106  ILE   A CA   1 
ATOM   2181 C  CA   B ILE   A 1 106 ? 21.425 -9.275  -11.168 0.50 15.82 ?  106  ILE   A CA   1 
ATOM   2182 C  C    A ILE   A 1 106 ? 21.869 -10.238 -10.617 0.50 19.87 ?  106  ILE   A C    1 
ATOM   2183 C  C    B ILE   A 1 106 ? 21.936 -10.544 -10.498 0.50 15.09 ?  106  ILE   A C    1 
ATOM   2184 O  O    A ILE   A 1 106 ? 21.679 -10.513 -9.429  0.50 19.07 ?  106  ILE   A O    1 
ATOM   2185 O  O    B ILE   A 1 106 ? 21.708 -10.742 -9.300  0.50 15.26 ?  106  ILE   A O    1 
ATOM   2186 C  CB   A ILE   A 1 106 ? 19.806 -9.064  -11.517 0.50 22.20 ?  106  ILE   A CB   1 
ATOM   2187 C  CB   B ILE   A 1 106 ? 19.910 -9.316  -11.475 0.50 18.56 ?  106  ILE   A CB   1 
ATOM   2188 C  CG1  A ILE   A 1 106 ? 18.976 -9.197  -10.237 0.50 22.23 ?  106  ILE   A CG1  1 
ATOM   2189 C  CG1  B ILE   A 1 106 ? 19.096 -9.207  -10.183 0.50 19.97 ?  106  ILE   A CG1  1 
ATOM   2190 C  CG2  A ILE   A 1 106 ? 19.542 -10.261 -12.405 0.50 22.76 ?  106  ILE   A CG2  1 
ATOM   2191 C  CG2  B ILE   A 1 106 ? 19.545 -10.579 -12.234 0.50 19.24 ?  106  ILE   A CG2  1 
ATOM   2192 C  CD1  A ILE   A 1 106 ? 19.083 -8.013  -9.306  0.50 22.13 ?  106  ILE   A CD1  1 
ATOM   2193 C  CD1  B ILE   A 1 106 ? 19.329 -7.919  -9.414  0.50 20.68 ?  106  ILE   A CD1  1 
ATOM   2194 H  H    A ILE   A 1 106 ? 21.611 -8.471  -13.082 0.50 26.69 ?  106  ILE   A H    1 
ATOM   2195 H  H    B ILE   A 1 106 ? 21.735 -8.969  -13.103 0.50 18.35 ?  106  ILE   A H    1 
ATOM   2196 H  HA   A ILE   A 1 106 ? 21.414 -8.278  -10.504 0.50 25.52 ?  106  ILE   A HA   1 
ATOM   2197 H  HA   B ILE   A 1 106 ? 21.577 -8.560  -10.538 0.50 19.01 ?  106  ILE   A HA   1 
ATOM   2198 H  HB   A ILE   A 1 106 ? 19.529 -8.262  -11.985 0.50 26.66 ?  106  ILE   A HB   1 
ATOM   2199 H  HB   B ILE   A 1 106 ? 19.695 -8.551  -12.034 0.50 22.29 ?  106  ILE   A HB   1 
ATOM   2200 H  HG12 A ILE   A 1 106 ? 18.041 -9.292  -10.482 0.50 26.70 ?  106  ILE   A HG12 1 
ATOM   2201 H  HG12 B ILE   A 1 106 ? 18.153 -9.247  -10.405 0.50 23.98 ?  106  ILE   A HG12 1 
ATOM   2202 H  HG13 A ILE   A 1 106 ? 19.268 -9.983  -9.751  0.50 26.70 ?  106  ILE   A HG13 1 
ATOM   2203 H  HG13 B ILE   A 1 106 ? 19.331 -9.944  -9.602  0.50 23.98 ?  106  ILE   A HG13 1 
ATOM   2204 H  HG21 A ILE   A 1 106 ? 18.652 -10.181 -12.780 0.50 27.33 ?  106  ILE   A HG21 1 
ATOM   2205 H  HG21 B ILE   A 1 106 ? 18.647 -10.482 -12.585 0.50 23.11 ?  106  ILE   A HG21 1 
ATOM   2206 H  HG22 A ILE   A 1 106 ? 20.203 -10.276 -13.112 0.50 27.33 ?  106  ILE   A HG22 1 
ATOM   2207 H  HG22 B ILE   A 1 106 ? 20.175 -10.698 -12.961 0.50 23.11 ?  106  ILE   A HG22 1 
ATOM   2208 H  HG23 A ILE   A 1 106 ? 19.606 -11.069 -11.872 0.50 27.33 ?  106  ILE   A HG23 1 
ATOM   2209 H  HG23 B ILE   A 1 106 ? 19.588 -11.332 -11.628 0.50 23.11 ?  106  ILE   A HG23 1 
ATOM   2210 H  HD11 A ILE   A 1 106 ? 18.360 -8.052  -8.663  0.50 26.58 ?  106  ILE   A HD11 1 
ATOM   2211 H  HD11 B ILE   A 1 106 ? 18.594 -7.781  -8.799  0.50 24.83 ?  106  ILE   A HD11 1 
ATOM   2212 H  HD12 A ILE   A 1 106 ? 19.937 -8.049  -8.846  0.50 26.58 ?  106  ILE   A HD12 1 
ATOM   2213 H  HD12 B ILE   A 1 106 ? 20.163 -7.991  -8.920  0.50 24.83 ?  106  ILE   A HD12 1 
ATOM   2214 H  HD13 A ILE   A 1 106 ? 19.021 -7.196  -9.826  0.50 26.58 ?  106  ILE   A HD13 1 
ATOM   2215 H  HD13 B ILE   A 1 106 ? 19.380 -7.180  -10.041 0.50 24.83 ?  106  ILE   A HD13 1 
ATOM   2216 N  N    A GLN   A 1 107 ? 22.568 -11.038 -11.430 0.50 20.45 ?  107  GLN   A N    1 
ATOM   2217 N  N    B GLN   A 1 107 ? 22.646 -11.404 -11.239 0.50 15.73 ?  107  GLN   A N    1 
ATOM   2218 C  CA   A GLN   A 1 107 ? 23.179 -12.266 -10.932 0.50 22.00 ?  107  GLN   A CA   1 
ATOM   2219 C  CA   B GLN   A 1 107 ? 23.258 -12.572 -10.613 0.50 17.86 ?  107  GLN   A CA   1 
ATOM   2220 C  C    A GLN   A 1 107 ? 24.161 -11.994 -9.801  0.50 19.47 ?  107  GLN   A C    1 
ATOM   2221 C  C    B GLN   A 1 107 ? 24.253 -12.164 -9.531  0.50 15.75 ?  107  GLN   A C    1 
ATOM   2222 O  O    A GLN   A 1 107 ? 24.420 -12.889 -8.991  0.50 21.38 ?  107  GLN   A O    1 
ATOM   2223 O  O    B GLN   A 1 107 ? 24.486 -12.918 -8.575  0.50 15.82 ?  107  GLN   A O    1 
ATOM   2224 C  CB   A GLN   A 1 107 ? 23.887 -13.009 -12.073 0.50 26.06 ?  107  GLN   A CB   1 
ATOM   2225 C  CB   B GLN   A 1 107 ? 23.906 -13.454 -11.684 0.50 22.40 ?  107  GLN   A CB   1 
ATOM   2226 C  CG   A GLN   A 1 107 ? 23.009 -13.271 -13.291 0.50 30.05 ?  107  GLN   A CG   1 
ATOM   2227 C  CG   B GLN   A 1 107 ? 22.933 -13.887 -12.779 0.50 26.65 ?  107  GLN   A CG   1 
ATOM   2228 C  CD   A GLN   A 1 107 ? 21.753 -14.047 -12.952 0.50 33.24 ?  107  GLN   A CD   1 
ATOM   2229 C  CD   B GLN   A 1 107 ? 21.702 -14.587 -12.225 0.50 30.40 ?  107  GLN   A CD   1 
ATOM   2230 O  OE1  A GLN   A 1 107 ? 21.814 -15.118 -12.348 0.50 34.50 ?  107  GLN   A OE1  1 
ATOM   2231 O  OE1  B GLN   A 1 107 ? 21.796 -15.385 -11.290 0.50 31.55 ?  107  GLN   A OE1  1 
ATOM   2232 N  NE2  A GLN   A 1 107 ? 20.603 -13.507 -13.336 0.50 34.26 ?  107  GLN   A NE2  1 
ATOM   2233 N  NE2  B GLN   A 1 107 ? 20.540 -14.284 -12.795 0.50 31.50 ?  107  GLN   A NE2  1 
ATOM   2234 H  H    A GLN   A 1 107 ? 22.706 -10.891 -12.263 0.50 24.56 ?  107  GLN   A H    1 
ATOM   2235 H  H    B GLN   A 1 107 ? 22.779 -11.336 -12.091 0.50 18.90 ?  107  GLN   A H    1 
ATOM   2236 H  HA   A GLN   A 1 107 ? 22.491 -12.852 -10.587 0.50 26.42 ?  107  GLN   A HA   1 
ATOM   2237 H  HA   B GLN   A 1 107 ? 22.565 -13.092 -10.193 0.50 21.46 ?  107  GLN   A HA   1 
ATOM   2238 H  HB2  A GLN   A 1 107 ? 24.646 -12.483 -12.371 0.50 31.30 ?  107  GLN   A HB2  1 
ATOM   2239 H  HB2  B GLN   A 1 107 ? 24.628 -12.966 -12.110 0.50 26.90 ?  107  GLN   A HB2  1 
ATOM   2240 H  HB3  A GLN   A 1 107 ? 24.197 -13.871 -11.749 0.50 31.30 ?  107  GLN   A HB3  1 
ATOM   2241 H  HB3  B GLN   A 1 107 ? 24.252 -14.258 -11.266 0.50 26.90 ?  107  GLN   A HB3  1 
ATOM   2242 H  HG2  A GLN   A 1 107 ? 22.739 -12.426 -13.678 0.50 36.09 ?  107  GLN   A HG2  1 
ATOM   2243 H  HG2  B GLN   A 1 107 ? 22.637 -13.103 -13.270 0.50 32.00 ?  107  GLN   A HG2  1 
ATOM   2244 H  HG3  A GLN   A 1 107 ? 23.514 -13.787 -13.940 0.50 36.09 ?  107  GLN   A HG3  1 
ATOM   2245 H  HG3  B GLN   A 1 107 ? 23.380 -14.503 -13.379 0.50 32.00 ?  107  GLN   A HG3  1 
ATOM   2246 H  HE21 A GLN   A 1 107 ? 20.599 -12.757 -13.756 0.50 41.13 ?  107  GLN   A HE21 1 
ATOM   2247 H  HE21 B GLN   A 1 107 ? 20.511 -13.720 -13.445 0.50 37.82 ?  107  GLN   A HE21 1 
ATOM   2248 H  HE22 A GLN   A 1 107 ? 19.862 -13.909 -13.165 0.50 41.13 ?  107  GLN   A HE22 1 
ATOM   2249 H  HE22 B GLN   A 1 107 ? 19.813 -14.651 -12.515 0.50 37.82 ?  107  GLN   A HE22 1 
ATOM   2250 N  N    A LEU   A 1 108 ? 24.701 -10.776 -9.714  0.50 15.52 ?  108  LEU   A N    1 
ATOM   2251 N  N    B LEU   A 1 108 ? 24.817 -10.958 -9.640  0.50 14.49 ?  108  LEU   A N    1 
ATOM   2252 C  CA   A LEU   A 1 108 ? 25.647 -10.437 -8.659  0.50 13.86 ?  108  LEU   A CA   1 
ATOM   2253 C  CA   B LEU   A 1 108 ? 25.697 -10.436 -8.604  0.50 13.63 ?  108  LEU   A CA   1 
ATOM   2254 C  C    A LEU   A 1 108 ? 24.971 -10.243 -7.310  0.50 12.15 ?  108  LEU   A C    1 
ATOM   2255 C  C    B LEU   A 1 108 ? 24.975 -10.235 -7.281  0.50 12.01 ?  108  LEU   A C    1 
ATOM   2256 O  O    A LEU   A 1 108 ? 25.665 -10.077 -6.304  0.50 12.33 ?  108  LEU   A O    1 
ATOM   2257 O  O    B LEU   A 1 108 ? 25.640 -10.053 -6.256  0.50 12.20 ?  108  LEU   A O    1 
ATOM   2258 C  CB   A LEU   A 1 108 ? 26.452 -9.189  -9.041  0.50 13.51 ?  108  LEU   A CB   1 
ATOM   2259 C  CB   B LEU   A 1 108 ? 26.353 -9.128  -9.065  0.50 13.82 ?  108  LEU   A CB   1 
ATOM   2260 C  CG   A LEU   A 1 108 ? 27.421 -9.408  -10.207 0.50 14.70 ?  108  LEU   A CG   1 
ATOM   2261 C  CG   B LEU   A 1 108 ? 27.391 -9.287  -10.177 0.50 15.29 ?  108  LEU   A CG   1 
ATOM   2262 C  CD1  A LEU   A 1 108 ? 27.984 -8.087  -10.709 0.50 15.15 ?  108  LEU   A CD1  1 
ATOM   2263 C  CD1  B LEU   A 1 108 ? 27.720 -7.943  -10.814 0.50 15.78 ?  108  LEU   A CD1  1 
ATOM   2264 C  CD2  A LEU   A 1 108 ? 28.552 -10.351 -9.808  0.50 15.74 ?  108  LEU   A CD2  1 
ATOM   2265 C  CD2  B LEU   A 1 108 ? 28.654 -9.945  -9.637  0.50 16.44 ?  108  LEU   A CD2  1 
ATOM   2266 H  H    A LEU   A 1 108 ? 24.533 -10.139 -10.257 0.50 18.65 ?  108  LEU   A H    1 
ATOM   2267 H  H    B LEU   A 1 108 ? 24.707 -10.430 -10.306 0.50 17.41 ?  108  LEU   A H    1 
ATOM   2268 H  HA   A LEU   A 1 108 ? 26.273 -11.170 -8.561  0.50 16.66 ?  108  LEU   A HA   1 
ATOM   2269 H  HA   B LEU   A 1 108 ? 26.405 -11.079 -8.448  0.50 16.37 ?  108  LEU   A HA   1 
ATOM   2270 H  HB2  A LEU   A 1 108 ? 25.835 -8.487  -9.298  0.50 16.24 ?  108  LEU   A HB2  1 
ATOM   2271 H  HB2  B LEU   A 1 108 ? 25.662 -8.532  -9.393  0.50 16.60 ?  108  LEU   A HB2  1 
ATOM   2272 H  HB3  A LEU   A 1 108 ? 26.972 -8.908  -8.273  0.50 16.24 ?  108  LEU   A HB3  1 
ATOM   2273 H  HB3  B LEU   A 1 108 ? 26.798 -8.724  -8.307  0.50 16.60 ?  108  LEU   A HB3  1 
ATOM   2274 H  HG   A LEU   A 1 108 ? 26.940 -9.821  -10.940 0.50 17.67 ?  108  LEU   A HG   1 
ATOM   2275 H  HG   B LEU   A 1 108 ? 27.029 -9.863  -10.869 0.50 18.37 ?  108  LEU   A HG   1 
ATOM   2276 H  HD11 A LEU   A 1 108 ? 28.588 -8.262  -11.449 0.50 18.20 ?  108  LEU   A HD11 1 
ATOM   2277 H  HD11 B LEU   A 1 108 ? 28.328 -8.087  -11.558 0.50 18.95 ?  108  LEU   A HD11 1 
ATOM   2278 H  HD12 A LEU   A 1 108 ? 27.251 -7.525  -11.007 0.50 18.20 ?  108  LEU   A HD12 1 
ATOM   2279 H  HD12 B LEU   A 1 108 ? 26.901 -7.534  -11.131 0.50 18.95 ?  108  LEU   A HD12 1 
ATOM   2280 H  HD13 A LEU   A 1 108 ? 28.462 -7.652  -9.987  0.50 18.20 ?  108  LEU   A HD13 1 
ATOM   2281 H  HD13 B LEU   A 1 108 ? 28.141 -7.374  -10.151 0.50 18.95 ?  108  LEU   A HD13 1 
ATOM   2282 H  HD21 A LEU   A 1 108 ? 29.231 -10.337 -10.499 0.50 18.91 ?  108  LEU   A HD21 1 
ATOM   2283 H  HD21 B LEU   A 1 108 ? 29.332 -9.944  -10.331 0.50 19.76 ?  108  LEU   A HD21 1 
ATOM   2284 H  HD22 A LEU   A 1 108 ? 28.929 -10.048 -8.966  0.50 18.91 ?  108  LEU   A HD22 1 
ATOM   2285 H  HD22 B LEU   A 1 108 ? 28.966 -9.443  -8.868  0.50 19.76 ?  108  LEU   A HD22 1 
ATOM   2286 H  HD23 A LEU   A 1 108 ? 28.196 -11.246 -9.708  0.50 18.91 ?  108  LEU   A HD23 1 
ATOM   2287 H  HD23 B LEU   A 1 108 ? 28.449 -10.856 -9.376  0.50 19.76 ?  108  LEU   A HD23 1 
ATOM   2288 N  N    . LEU   A 1 109 ? 23.640 -10.278 -7.262  1.00 11.69 ?  109  LEU   A N    1 
ATOM   2289 C  CA   . LEU   A 1 109 ? 22.942 -10.148 -5.992  1.00 10.98 ?  109  LEU   A CA   1 
ATOM   2290 C  C    . LEU   A 1 109 ? 23.278 -11.306 -5.060  1.00 10.57 ?  109  LEU   A C    1 
ATOM   2291 O  O    . LEU   A 1 109 ? 23.398 -11.120 -3.845  1.00 10.94 ?  109  LEU   A O    1 
ATOM   2292 C  CB   . LEU   A 1 109 ? 21.440 -10.059 -6.242  1.00 12.09 ?  109  LEU   A CB   1 
ATOM   2293 C  CG   . LEU   A 1 109 ? 20.554 -9.773  -5.033  1.00 12.23 ?  109  LEU   A CG   1 
ATOM   2294 C  CD1  . LEU   A 1 109 ? 21.005 -8.512  -4.320  1.00 12.61 ?  109  LEU   A CD1  1 
ATOM   2295 C  CD2  . LEU   A 1 109 ? 19.101 -9.645  -5.465  1.00 13.27 ?  109  LEU   A CD2  1 
ATOM   2296 H  H    A LEU   A 1 109 ? 23.124 -10.370 -7.944  0.50 14.05 ?  109  LEU   A H    1 
ATOM   2297 H  H    B LEU   A 1 109 ? 23.133 -10.378 -7.949  0.50 14.05 ?  109  LEU   A H    1 
ATOM   2298 H  HA   . LEU   A 1 109 ? 23.229 -9.325  -5.561  1.00 13.19 ?  109  LEU   A HA   1 
ATOM   2299 H  HB2  . LEU   A 1 109 ? 21.284 -9.346  -6.884  1.00 14.53 ?  109  LEU   A HB2  1 
ATOM   2300 H  HB3  . LEU   A 1 109 ? 21.145 -10.899 -6.617  1.00 14.53 ?  109  LEU   A HB3  1 
ATOM   2301 H  HG   . LEU   A 1 109 ? 20.620 -10.506 -4.407  1.00 14.70 ?  109  LEU   A HG   1 
ATOM   2302 H  HD11 . LEU   A 1 109 ? 20.313 -8.224  -3.707  1.00 15.15 ?  109  LEU   A HD11 1 
ATOM   2303 H  HD12 . LEU   A 1 109 ? 21.825 -8.694  -3.833  1.00 15.15 ?  109  LEU   A HD12 1 
ATOM   2304 H  HD13 . LEU   A 1 109 ? 21.166 -7.813  -4.980  1.00 15.15 ?  109  LEU   A HD13 1 
ATOM   2305 H  HD21 . LEU   A 1 109 ? 18.570 -9.335  -4.712  1.00 15.95 ?  109  LEU   A HD21 1 
ATOM   2306 H  HD22 . LEU   A 1 109 ? 19.038 -9.011  -6.194  1.00 15.95 ?  109  LEU   A HD22 1 
ATOM   2307 H  HD23 . LEU   A 1 109 ? 18.780 -10.515 -5.755  1.00 15.95 ?  109  LEU   A HD23 1 
ATOM   2308 N  N    . LYS   A 1 110 ? 23.426 -12.516 -5.601  1.00 10.58 ?  110  LYS   A N    1 
ATOM   2309 C  CA   . LYS   A 1 110 ? 23.794 -13.635 -4.743  1.00 10.77 ?  110  LYS   A CA   1 
ATOM   2310 C  C    . LYS   A 1 110 ? 25.175 -13.415 -4.132  1.00 10.17 ?  110  LYS   A C    1 
ATOM   2311 O  O    . LYS   A 1 110 ? 25.371 -13.619 -2.932  1.00 10.37 ?  110  LYS   A O    1 
ATOM   2312 C  CB   . LYS   A 1 110 ? 23.715 -14.957 -5.508  1.00 11.53 ?  110  LYS   A CB   1 
ATOM   2313 C  CG   . LYS   A 1 110 ? 23.910 -16.168 -4.599  1.00 11.55 ?  110  LYS   A CG   1 
ATOM   2314 C  CD   . LYS   A 1 110 ? 23.683 -17.490 -5.312  1.00 12.37 ?  110  LYS   A CD   1 
ATOM   2315 C  CE   . LYS   A 1 110 ? 23.793 -18.676 -4.359  1.00 12.82 ?  110  LYS   A CE   1 
ATOM   2316 N  NZ   . LYS   A 1 110 ? 22.609 -18.802 -3.467  1.00 13.35 ?  110  LYS   A NZ   1 
ATOM   2317 H  H    . LYS   A 1 110 ? 23.328 -12.709 -6.432  1.00 12.71 ?  110  LYS   A H    1 
ATOM   2318 H  HA   . LYS   A 1 110 ? 23.152 -13.682 -4.012  1.00 12.95 ?  110  LYS   A HA   1 
ATOM   2319 H  HB2  . LYS   A 1 110 ? 22.840 -15.030 -5.923  1.00 13.86 ?  110  LYS   A HB2  1 
ATOM   2320 H  HB3  . LYS   A 1 110 ? 24.408 -14.974 -6.181  1.00 13.86 ?  110  LYS   A HB3  1 
ATOM   2321 H  HG2  . LYS   A 1 110 ? 24.812 -16.164 -4.252  1.00 13.88 ?  110  LYS   A HG2  1 
ATOM   2322 H  HG3  . LYS   A 1 110 ? 23.273 -16.116 -3.865  1.00 13.88 ?  110  LYS   A HG3  1 
ATOM   2323 H  HD2  . LYS   A 1 110 ? 22.799 -17.497 -5.701  1.00 14.87 ?  110  LYS   A HD2  1 
ATOM   2324 H  HD3  . LYS   A 1 110 ? 24.359 -17.595 -5.999  1.00 14.87 ?  110  LYS   A HD3  1 
ATOM   2325 H  HE2  . LYS   A 1 110 ? 23.867 -19.495 -4.873  1.00 15.41 ?  110  LYS   A HE2  1 
ATOM   2326 H  HE3  . LYS   A 1 110 ? 24.577 -18.566 -3.795  1.00 15.41 ?  110  LYS   A HE3  1 
ATOM   2327 H  HZ1  . LYS   A 1 110 ? 22.700 -19.500 -2.926  1.00 16.04 ?  110  LYS   A HZ1  1 
ATOM   2328 H  HZ2  . LYS   A 1 110 ? 22.517 -18.064 -2.974  1.00 16.04 ?  110  LYS   A HZ2  1 
ATOM   2329 H  HZ3  . LYS   A 1 110 ? 21.870 -18.910 -3.956  1.00 16.04 ?  110  LYS   A HZ3  1 
ATOM   2330 N  N    . SER   A 1 111 ? 26.140 -12.979 -4.946  1.00 10.24 ?  111  SER   A N    1 
ATOM   2331 C  CA   . SER   A 1 111 ? 27.469 -12.675 -4.427  1.00 10.32 ?  111  SER   A CA   1 
ATOM   2332 C  C    . SER   A 1 111 ? 27.397 -11.630 -3.321  1.00 10.10 ?  111  SER   A C    1 
ATOM   2333 O  O    . SER   A 1 111 ? 28.097 -11.732 -2.307  1.00 10.63 ?  111  SER   A O    1 
ATOM   2334 C  CB   . SER   A 1 111 ? 28.358 -12.182 -5.569  1.00 11.66 ?  111  SER   A CB   1 
ATOM   2335 O  OG   . SER   A 1 111 ? 28.431 -13.162 -6.594  1.00 13.48 ?  111  SER   A OG   1 
ATOM   2336 H  H    . SER   A 1 111 ? 26.039 -12.850 -5.789  1.00 12.32 ?  111  SER   A H    1 
ATOM   2337 H  HA   . SER   A 1 111 ? 27.860 -13.487 -4.066  1.00 12.41 ?  111  SER   A HA   1 
ATOM   2338 H  HB2  . SER   A 1 111 ? 27.973 -11.375 -5.944  1.00 14.02 ?  111  SER   A HB2  1 
ATOM   2339 H  HB3  . SER   A 1 111 ? 29.245 -12.002 -5.224  1.00 14.02 ?  111  SER   A HB3  1 
ATOM   2340 H  HG   . SER   A 1 111 ? 28.939 -12.890 -7.213  1.00 16.19 ?  111  SER   A HG   1 
ATOM   2341 N  N    . ALA   A 1 112 ? 26.558 -10.612 -3.506  1.00 10.22 ?  112  ALA   A N    1 
ATOM   2342 C  CA   . ALA   A 1 112 ? 26.403 -9.572  -2.491  1.00 10.20 ?  112  ALA   A CA   1 
ATOM   2343 C  C    . ALA   A 1 112 ? 25.923 -10.168 -1.171  1.00 9.93  ?  112  ALA   A C    1 
ATOM   2344 O  O    . ALA   A 1 112 ? 26.474 -9.884  -0.102  1.00 10.23 ?  112  ALA   A O    1 
ATOM   2345 C  CB   . ALA   A 1 112 ? 25.441 -8.491  -2.995  1.00 10.42 ?  112  ALA   A CB   1 
ATOM   2346 H  H    . ALA   A 1 112 ? 26.076 -10.498 -4.207  1.00 12.29 ?  112  ALA   A H    1 
ATOM   2347 H  HA   . ALA   A 1 112 ? 27.260 -9.151  -2.332  1.00 12.27 ?  112  ALA   A HA   1 
ATOM   2348 H  HB1  . ALA   A 1 112 ? 25.366 -7.791  -2.320  1.00 12.52 ?  112  ALA   A HB1  1 
ATOM   2349 H  HB2  . ALA   A 1 112 ? 25.788 -8.111  -3.818  1.00 12.52 ?  112  ALA   A HB2  1 
ATOM   2350 H  HB3  . ALA   A 1 112 ? 24.569 -8.884  -3.155  1.00 12.52 ?  112  ALA   A HB3  1 
ATOM   2351 N  N    . TYR   A 1 113 ? 24.888 -11.008 -1.222  1.00 9.76  ?  113  TYR   A N    1 
ATOM   2352 C  CA   . TYR   A 1 113 ? 24.376 -11.614 0.006   1.00 9.72  ?  113  TYR   A CA   1 
ATOM   2353 C  C    . TYR   A 1 113 ? 25.380 -12.567 0.653   1.00 9.43  ?  113  TYR   A C    1 
ATOM   2354 O  O    . TYR   A 1 113 ? 25.341 -12.755 1.872   1.00 9.91  ?  113  TYR   A O    1 
ATOM   2355 C  CB   . TYR   A 1 113 ? 23.049 -12.328 -0.259  1.00 10.10 ?  113  TYR   A CB   1 
ATOM   2356 C  CG   . TYR   A 1 113 ? 21.842 -11.421 -0.191  1.00 10.02 ?  113  TYR   A CG   1 
ATOM   2357 C  CD1  . TYR   A 1 113 ? 21.482 -10.810 1.002   1.00 10.24 ?  113  TYR   A CD1  1 
ATOM   2358 C  CD2  . TYR   A 1 113 ? 21.048 -11.200 -1.307  1.00 10.43 ?  113  TYR   A CD2  1 
ATOM   2359 C  CE1  . TYR   A 1 113 ? 20.359 -9.999  1.085   1.00 10.63 ?  113  TYR   A CE1  1 
ATOM   2360 C  CE2  . TYR   A 1 113 ? 19.907 -10.384 -1.235  1.00 10.72 ?  113  TYR   A CE2  1 
ATOM   2361 C  CZ   . TYR   A 1 113 ? 19.577 -9.789  -0.032  1.00 10.64 ?  113  TYR   A CZ   1 
ATOM   2362 O  OH   . TYR   A 1 113 ? 18.463 -8.980  0.092   1.00 11.51 ?  113  TYR   A OH   1 
ATOM   2363 H  H    . TYR   A 1 113 ? 24.472 -11.238 -1.940  1.00 11.74 ?  113  TYR   A H    1 
ATOM   2364 H  HA   . TYR   A 1 113 ? 24.206 -10.909 0.645   1.00 11.69 ?  113  TYR   A HA   1 
ATOM   2365 H  HB2  . TYR   A 1 113 ? 23.069 -12.718 -1.144  1.00 12.15 ?  113  TYR   A HB2  1 
ATOM   2366 H  HB3  . TYR   A 1 113 ? 22.929 -13.024 0.406   1.00 12.15 ?  113  TYR   A HB3  1 
ATOM   2367 H  HD1  . TYR   A 1 113 ? 22.001 -10.959 1.762   1.00 12.31 ?  113  TYR   A HD1  1 
ATOM   2368 H  HD2  . TYR   A 1 113 ? 21.268 -11.608 -2.113  1.00 12.54 ?  113  TYR   A HD2  1 
ATOM   2369 H  HE1  . TYR   A 1 113 ? 20.137 -9.602  1.896   1.00 12.78 ?  113  TYR   A HE1  1 
ATOM   2370 H  HE2  . TYR   A 1 113 ? 19.379 -10.238 -1.989  1.00 12.88 ?  113  TYR   A HE2  1 
ATOM   2371 H  HH   . TYR   A 1 113 ? 18.074 -8.923  -0.659  1.00 13.83 ?  113  TYR   A HH   1 
ATOM   2372 N  N    . GLU   A 1 114 ? 26.278 -13.181 -0.131  1.00 9.79  ?  114  GLU   A N    1 
ATOM   2373 C  CA   . GLU   A 1 114 ? 27.271 -14.078 0.459   1.00 10.07 ?  114  GLU   A CA   1 
ATOM   2374 C  C    . GLU   A 1 114 ? 28.118 -13.371 1.509   1.00 9.92  ?  114  GLU   A C    1 
ATOM   2375 O  O    . GLU   A 1 114 ? 28.594 -14.009 2.458   1.00 10.16 ?  114  GLU   A O    1 
ATOM   2376 C  CB   . GLU   A 1 114 ? 28.140 -14.719 -0.629  1.00 10.12 ?  114  GLU   A CB   1 
ATOM   2377 C  CG   . GLU   A 1 114 ? 27.374 -15.764 -1.417  1.00 10.47 ?  114  GLU   A CG   1 
ATOM   2378 C  CD   . GLU   A 1 114 ? 28.090 -16.297 -2.651  1.00 10.94 ?  114  GLU   A CD   1 
ATOM   2379 O  OE1  . GLU   A 1 114 ? 29.042 -15.666 -3.156  1.00 11.17 ?  114  GLU   A OE1  1 
ATOM   2380 O  OE2  . GLU   A 1 114 ? 27.650 -17.361 -3.135  1.00 12.11 -1 114  GLU   A OE2  1 
ATOM   2381 H  H    . GLU   A 1 114 ? 26.337 -13.086 -0.991  1.00 11.77 ?  114  GLU   A H    1 
ATOM   2382 H  HA   . GLU   A 1 114 ? 26.797 -14.792 0.904   1.00 12.11 ?  114  GLU   A HA   1 
ATOM   2383 H  HB2  . GLU   A 1 114 ? 28.434 -14.036 -1.253  1.00 12.16 ?  114  GLU   A HB2  1 
ATOM   2384 H  HB3  . GLU   A 1 114 ? 28.899 -15.153 -0.220  1.00 12.16 ?  114  GLU   A HB3  1 
ATOM   2385 H  HG2  . GLU   A 1 114 ? 27.197 -16.522 -0.836  1.00 12.58 ?  114  GLU   A HG2  1 
ATOM   2386 H  HG3  . GLU   A 1 114 ? 26.529 -15.379 -1.708  1.00 12.58 ?  114  GLU   A HG3  1 
ATOM   2387 N  N    . ASN   A 1 115 ? 28.298 -12.054 1.380   1.00 10.00 ?  115  ASN   A N    1 
ATOM   2388 C  CA   . ASN   A 1 115 ? 29.068 -11.330 2.383   1.00 10.12 ?  115  ASN   A CA   1 
ATOM   2389 C  C    . ASN   A 1 115 ? 28.453 -11.462 3.768   1.00 10.07 ?  115  ASN   A C    1 
ATOM   2390 O  O    . ASN   A 1 115 ? 29.166 -11.388 4.775   1.00 10.46 ?  115  ASN   A O    1 
ATOM   2391 C  CB   . ASN   A 1 115 ? 29.183 -9.856  2.007   1.00 10.37 ?  115  ASN   A CB   1 
ATOM   2392 C  CG   . ASN   A 1 115 ? 29.981 -9.647  0.746   1.00 11.08 ?  115  ASN   A CG   1 
ATOM   2393 O  OD1  . ASN   A 1 115 ? 31.198 -9.760  0.759   1.00 14.27 ?  115  ASN   A OD1  1 
ATOM   2394 N  ND2  . ASN   A 1 115 ? 29.305 -9.342  -0.346  1.00 10.68 ?  115  ASN   A ND2  1 
ATOM   2395 H  H    . ASN   A 1 115 ? 27.989 -11.568 0.737   1.00 12.02 ?  115  ASN   A H    1 
ATOM   2396 H  HA   . ASN   A 1 115 ? 29.959 -11.702 2.422   1.00 12.17 ?  115  ASN   A HA   1 
ATOM   2397 H  HB2  . ASN   A 1 115 ? 28.297 -9.491  1.874   1.00 12.47 ?  115  ASN   A HB2  1 
ATOM   2398 H  HB3  . ASN   A 1 115 ? 29.633 -9.384  2.729   1.00 12.47 ?  115  ASN   A HB3  1 
ATOM   2399 H  HD21 . ASN   A 1 115 ? 29.714 -9.212  -1.092  1.00 12.83 ?  115  ASN   A HD21 1 
ATOM   2400 H  HD22 . ASN   A 1 115 ? 28.443 -9.290  -0.320  1.00 12.83 ?  115  ASN   A HD22 1 
ATOM   2401 N  N    . PHE   A 1 116 ? 27.126 -11.631 3.846   1.00 9.93  ?  116  PHE   A N    1 
ATOM   2402 C  CA   . PHE   A 1 116 ? 26.477 -11.724 5.150   1.00 9.76  ?  116  PHE   A CA   1 
ATOM   2403 C  C    . PHE   A 1 116 ? 26.952 -12.950 5.925   1.00 10.14 ?  116  PHE   A C    1 
ATOM   2404 O  O    . PHE   A 1 116 ? 26.874 -12.969 7.154   1.00 10.66 ?  116  PHE   A O    1 
ATOM   2405 C  CB   . PHE   A 1 116 ? 24.950 -11.852 5.017   1.00 9.85  ?  116  PHE   A CB   1 
ATOM   2406 C  CG   . PHE   A 1 116 ? 24.199 -10.607 4.542   1.00 9.96  ?  116  PHE   A CG   1 
ATOM   2407 C  CD1  . PHE   A 1 116 ? 24.772 -9.590  3.783   1.00 9.90  ?  116  PHE   A CD1  1 
ATOM   2408 C  CD2  . PHE   A 1 116 ? 22.850 -10.497 4.864   1.00 10.55 ?  116  PHE   A CD2  1 
ATOM   2409 C  CE1  . PHE   A 1 116 ? 24.007 -8.515  3.353   1.00 10.43 ?  116  PHE   A CE1  1 
ATOM   2410 C  CE2  . PHE   A 1 116 ? 22.088 -9.424  4.443   1.00 10.63 ?  116  PHE   A CE2  1 
ATOM   2411 C  CZ   . PHE   A 1 116 ? 22.657 -8.432  3.686   1.00 9.97  ?  116  PHE   A CZ   1 
ATOM   2412 H  H    . PHE   A 1 116 ? 26.590 -11.685 3.170   1.00 11.94 ?  116  PHE   A H    1 
ATOM   2413 H  HA   . PHE   A 1 116 ? 26.676 -10.931 5.669   1.00 11.73 ?  116  PHE   A HA   1 
ATOM   2414 H  HB2  . PHE   A 1 116 ? 24.760 -12.566 4.386   1.00 11.84 ?  116  PHE   A HB2  1 
ATOM   2415 H  HB3  . PHE   A 1 116 ? 24.593 -12.095 5.887   1.00 11.84 ?  116  PHE   A HB3  1 
ATOM   2416 H  HD1  . PHE   A 1 116 ? 25.661 -9.650  3.546   1.00 11.91 ?  116  PHE   A HD1  1 
ATOM   2417 H  HD2  . PHE   A 1 116 ? 22.443 -11.178 5.365   1.00 12.69 ?  116  PHE   A HD2  1 
ATOM   2418 H  HE1  . PHE   A 1 116 ? 24.402 -7.844  2.850   1.00 12.54 ?  116  PHE   A HE1  1 
ATOM   2419 H  HE2  . PHE   A 1 116 ? 21.186 -9.380  4.674   1.00 12.77 ?  116  PHE   A HE2  1 
ATOM   2420 H  HZ   . PHE   A 1 116 ? 22.152 -7.703  3.414   1.00 11.98 ?  116  PHE   A HZ   1 
ATOM   2421 N  N    . ASN   A 1 117 ? 27.397 -14.000 5.224   1.00 10.38 ?  117  ASN   A N    1 
ATOM   2422 C  CA   . ASN   A 1 117 ? 27.765 -15.243 5.896   1.00 10.58 ?  117  ASN   A CA   1 
ATOM   2423 C  C    . ASN   A 1 117 ? 29.025 -15.120 6.732   1.00 11.17 ?  117  ASN   A C    1 
ATOM   2424 O  O    . ASN   A 1 117 ? 29.325 -16.038 7.504   1.00 11.90 ?  117  ASN   A O    1 
ATOM   2425 C  CB   . ASN   A 1 117 ? 27.884 -16.370 4.874   1.00 10.62 ?  117  ASN   A CB   1 
ATOM   2426 C  CG   . ASN   A 1 117 ? 26.534 -16.750 4.326   1.00 10.73 ?  117  ASN   A CG   1 
ATOM   2427 O  OD1  . ASN   A 1 117 ? 25.555 -16.778 5.069   1.00 11.59 ?  117  ASN   A OD1  1 
ATOM   2428 N  ND2  . ASN   A 1 117 ? 26.454 -17.007 3.038   1.00 10.93 ?  117  ASN   A ND2  1 
ATOM   2429 H  H    . ASN   A 1 117 ? 27.482 -14.020 4.366   1.00 12.48 ?  117  ASN   A H    1 
ATOM   2430 H  HA   . ASN   A 1 117 ? 27.039 -15.478 6.498   1.00 12.71 ?  117  ASN   A HA   1 
ATOM   2431 H  HB2  . ASN   A 1 117 ? 28.442 -16.078 4.136   1.00 12.77 ?  117  ASN   A HB2  1 
ATOM   2432 H  HB3  . ASN   A 1 117 ? 28.271 -17.149 5.302   1.00 12.77 ?  117  ASN   A HB3  1 
ATOM   2433 H  HD21 . ASN   A 1 117 ? 25.697 -17.218 2.695   1.00 13.14 ?  117  ASN   A HD21 1 
ATOM   2434 H  HD22 . ASN   A 1 117 ? 27.159 -16.966 2.553   1.00 13.14 ?  117  ASN   A HD22 1 
ATOM   2435 N  N    . GLN   A 1 118 ? 29.747 -14.008 6.616   1.00 11.04 ?  118  GLN   A N    1 
ATOM   2436 C  CA   . GLN   A 1 118 ? 30.925 -13.775 7.438   1.00 11.76 ?  118  GLN   A CA   1 
ATOM   2437 C  C    . GLN   A 1 118 ? 30.581 -13.195 8.803   1.00 11.63 ?  118  GLN   A C    1 
ATOM   2438 O  O    . GLN   A 1 118 ? 31.493 -12.896 9.583   1.00 12.79 ?  118  GLN   A O    1 
ATOM   2439 C  CB   . GLN   A 1 118 ? 31.914 -12.868 6.698   1.00 12.03 ?  118  GLN   A CB   1 
ATOM   2440 C  CG   . GLN   A 1 118 ? 32.384 -13.452 5.382   1.00 12.04 ?  118  GLN   A CG   1 
ATOM   2441 C  CD   . GLN   A 1 118 ? 33.219 -14.708 5.562   1.00 12.40 ?  118  GLN   A CD   1 
ATOM   2442 O  OE1  . GLN   A 1 118 ? 34.083 -14.777 6.448   1.00 13.17 ?  118  GLN   A OE1  1 
ATOM   2443 N  NE2  . GLN   A 1 118 ? 32.971 -15.707 4.718   1.00 12.56 ?  118  GLN   A NE2  1 
ATOM   2444 H  H    . GLN   A 1 118 ? 29.563 -13.361 6.069   1.00 13.28 ?  118  GLN   A H    1 
ATOM   2445 H  HA   . GLN   A 1 118 ? 31.355 -14.628 7.586   1.00 14.14 ?  118  GLN   A HA   1 
ATOM   2446 H  HB2  . GLN   A 1 118 ? 31.484 -12.018 6.517   1.00 14.46 ?  118  GLN   A HB2  1 
ATOM   2447 H  HB3  . GLN   A 1 118 ? 32.689 -12.733 7.265   1.00 14.46 ?  118  GLN   A HB3  1 
ATOM   2448 H  HG2  . GLN   A 1 118 ? 31.614 -13.676 4.834   1.00 14.47 ?  118  GLN   A HG2  1 
ATOM   2449 H  HG3  . GLN   A 1 118 ? 32.934 -12.795 4.922   1.00 14.47 ?  118  GLN   A HG3  1 
ATOM   2450 H  HE21 . GLN   A 1 118 ? 32.356 -15.619 4.113   1.00 15.09 ?  118  GLN   A HE21 1 
ATOM   2451 H  HE22 . GLN   A 1 118 ? 33.409 -16.440 4.773   1.00 15.09 ?  118  GLN   A HE22 1 
ATOM   2452 N  N    . HIS   A 1 119 ? 29.292 -13.039 9.108   1.00 11.43 ?  119  HIS   A N    1 
ATOM   2453 C  CA   . HIS   A 1 119 ? 28.830 -12.430 10.350  1.00 11.81 ?  119  HIS   A CA   1 
ATOM   2454 C  C    . HIS   A 1 119 ? 27.692 -13.256 10.919  1.00 11.92 ?  119  HIS   A C    1 
ATOM   2455 O  O    . HIS   A 1 119 ? 26.748 -13.590 10.200  1.00 12.13 ?  119  HIS   A O    1 
ATOM   2456 C  CB   . HIS   A 1 119 ? 28.372 -10.998 10.076  1.00 12.25 ?  119  HIS   A CB   1 
ATOM   2457 C  CG   . HIS   A 1 119 ? 29.454 -10.184 9.470   1.00 13.40 ?  119  HIS   A CG   1 
ATOM   2458 N  ND1  . HIS   A 1 119 ? 30.426 -9.577  10.232  1.00 15.96 ?  119  HIS   A ND1  1 
ATOM   2459 C  CD2  . HIS   A 1 119 ? 29.798 -9.986  8.178   1.00 14.58 ?  119  HIS   A CD2  1 
ATOM   2460 C  CE1  . HIS   A 1 119 ? 31.296 -8.990  9.431   1.00 16.25 ?  119  HIS   A CE1  1 
ATOM   2461 N  NE2  . HIS   A 1 119 ? 30.947 -9.235  8.181   1.00 16.14 ?  119  HIS   A NE2  1 
ATOM   2462 H  H    . HIS   A 1 119 ? 28.642 -13.297 8.602   1.00 13.74 ?  119  HIS   A H    1 
ATOM   2463 H  HA   . HIS   A 1 119 ? 29.556 -12.413 10.995  1.00 14.19 ?  119  HIS   A HA   1 
ATOM   2464 H  HB2  . HIS   A 1 119 ? 27.622 -11.020 9.460   1.00 14.72 ?  119  HIS   A HB2  1 
ATOM   2465 H  HB3  . HIS   A 1 119 ? 28.109 -10.586 10.912  1.00 14.72 ?  119  HIS   A HB3  1 
ATOM   2466 H  HD1  . HIS   A 1 119 ? 30.453 -9.570  11.089  1.00 19.17 ?  119  HIS   A HD1  1 
ATOM   2467 H  HD2  . HIS   A 1 119 ? 29.340 -10.292 7.427   1.00 17.51 ?  119  HIS   A HD2  1 
ATOM   2468 H  HE1  . HIS   A 1 119 ? 32.031 -8.489  9.701   1.00 19.53 ?  119  HIS   A HE1  1 
ATOM   2469 N  N    . GLU   A 1 120 ? 27.775 -13.567 12.213  1.00 12.46 ?  120  GLU   A N    1 
ATOM   2470 C  CA   . GLU   A 1 120 ? 26.813 -14.489 12.812  1.00 14.83 ?  120  GLU   A CA   1 
ATOM   2471 C  C    . GLU   A 1 120 ? 25.399 -13.920 12.867  1.00 13.37 ?  120  GLU   A C    1 
ATOM   2472 O  O    . GLU   A 1 120 ? 24.428 -14.683 12.753  1.00 13.21 ?  120  GLU   A O    1 
ATOM   2473 C  CB   . GLU   A 1 120 ? 27.275 -14.889 14.213  1.00 19.58 ?  120  GLU   A CB   1 
ATOM   2474 C  CG   . GLU   A 1 120 ? 28.492 -15.791 14.217  1.00 26.88 ?  120  GLU   A CG   1 
ATOM   2475 C  CD   . GLU   A 1 120 ? 28.677 -16.518 15.530  1.00 34.98 ?  120  GLU   A CD   1 
ATOM   2476 O  OE1  . GLU   A 1 120 ? 28.182 -16.023 16.565  1.00 36.30 ?  120  GLU   A OE1  1 
ATOM   2477 O  OE2  . GLU   A 1 120 ? 29.319 -17.590 15.525  1.00 38.92 -1 120  GLU   A OE2  1 
ATOM   2478 H  H    . GLU   A 1 120 ? 28.377 -13.271 12.756  1.00 14.98 ?  120  GLU   A H    1 
ATOM   2479 H  HA   . GLU   A 1 120 ? 26.787 -15.297 12.280  1.00 17.82 ?  120  GLU   A HA   1 
ATOM   2480 H  HB2  . GLU   A 1 120 ? 27.502 -14.095 14.719  1.00 23.51 ?  120  GLU   A HB2  1 
ATOM   2481 H  HB3  . GLU   A 1 120 ? 26.557 -15.369 14.661  1.00 23.51 ?  120  GLU   A HB3  1 
ATOM   2482 H  HG2  . GLU   A 1 120 ? 28.404 -16.453 13.514  1.00 32.28 ?  120  GLU   A HG2  1 
ATOM   2483 H  HG3  . GLU   A 1 120 ? 29.288 -15.259 14.081  1.00 32.28 ?  120  GLU   A HG3  1 
ATOM   2484 N  N    . VAL   A 1 121 ? 25.265 -12.609 13.076  1.00 12.70 ?  121  VAL   A N    1 
ATOM   2485 C  CA   . VAL   A 1 121 ? 23.968 -11.947 13.195  1.00 12.72 ?  121  VAL   A CA   1 
ATOM   2486 C  C    . VAL   A 1 121 ? 24.074 -10.566 12.560  1.00 11.73 ?  121  VAL   A C    1 
ATOM   2487 O  O    . VAL   A 1 121 ? 25.035 -9.833  12.813  1.00 12.23 ?  121  VAL   A O    1 
ATOM   2488 C  CB   . VAL   A 1 121 ? 23.530 -11.803 14.672  1.00 15.98 ?  121  VAL   A CB   1 
ATOM   2489 C  CG1  . VAL   A 1 121 ? 22.132 -11.202 14.756  1.00 16.39 ?  121  VAL   A CG1  1 
ATOM   2490 C  CG2  . VAL   A 1 121 ? 23.584 -13.124 15.417  1.00 18.01 ?  121  VAL   A CG2  1 
ATOM   2491 H  H    . VAL   A 1 121 ? 25.930 -12.066 13.157  1.00 15.26 ?  121  VAL   A H    1 
ATOM   2492 H  HA   . VAL   A 1 121 ? 23.297 -12.462 12.722  1.00 15.28 ?  121  VAL   A HA   1 
ATOM   2493 H  HB   . VAL   A 1 121 ? 24.134 -11.193 15.117  1.00 19.20 ?  121  VAL   A HB   1 
ATOM   2494 H  HG11 . VAL   A 1 121 ? 21.818 -11.256 15.674  1.00 19.69 ?  121  VAL   A HG11 1 
ATOM   2495 H  HG12 . VAL   A 1 121 ? 22.164 -10.275 14.475  1.00 19.69 ?  121  VAL   A HG12 1 
ATOM   2496 H  HG13 . VAL   A 1 121 ? 21.535 -11.703 14.177  1.00 19.69 ?  121  VAL   A HG13 1 
ATOM   2497 H  HG21 . VAL   A 1 121 ? 23.229 -12.995 16.316  1.00 21.64 ?  121  VAL   A HG21 1 
ATOM   2498 H  HG22 . VAL   A 1 121 ? 23.043 -13.778 14.946  1.00 21.64 ?  121  VAL   A HG22 1 
ATOM   2499 H  HG23 . VAL   A 1 121 ? 24.501 -13.425 15.467  1.00 21.64 ?  121  VAL   A HG23 1 
ATOM   2500 N  N    . LEU   A 1 122 ? 23.064 -10.190 11.770  1.00 10.89 ?  122  LEU   A N    1 
ATOM   2501 C  CA   . LEU   A 1 122 ? 23.062 -8.898  11.090  1.00 10.67 ?  122  LEU   A CA   1 
ATOM   2502 C  C    . LEU   A 1 122 ? 21.663 -8.314  11.057  1.00 10.13 ?  122  LEU   A C    1 
ATOM   2503 O  O    . LEU   A 1 122 ? 20.679 -9.041  10.907  1.00 11.35 ?  122  LEU   A O    1 
ATOM   2504 C  CB   . LEU   A 1 122 ? 23.469 -9.005  9.617   1.00 12.01 ?  122  LEU   A CB   1 
ATOM   2505 C  CG   . LEU   A 1 122 ? 24.694 -9.842  9.275   1.00 12.04 ?  122  LEU   A CG   1 
ATOM   2506 C  CD1  . LEU   A 1 122 ? 24.313 -11.294 9.047   1.00 12.76 ?  122  LEU   A CD1  1 
ATOM   2507 C  CD2  . LEU   A 1 122 ? 25.395 -9.275  8.054   1.00 11.71 ?  122  LEU   A CD2  1 
ATOM   2508 H  H    . LEU   A 1 122 ? 22.365 -10.669 11.614  1.00 13.10 ?  122  LEU   A H    1 
ATOM   2509 H  HA   . LEU   A 1 122 ? 23.662 -8.282  11.543  1.00 12.82 ?  122  LEU   A HA   1 
ATOM   2510 H  HB2  . LEU   A 1 122 ? 22.729 -9.389  9.130   1.00 14.44 ?  122  LEU   A HB2  1 
ATOM   2511 H  HB3  . LEU   A 1 122 ? 23.646 -8.113  9.290   1.00 14.44 ?  122  LEU   A HB3  1 
ATOM   2512 H  HG   . LEU   A 1 122 ? 25.326 -9.816  10.013  1.00 14.47 ?  122  LEU   A HG   1 
ATOM   2513 H  HD11 . LEU   A 1 122 ? 25.099 -11.803 8.798   1.00 15.33 ?  122  LEU   A HD11 1 
ATOM   2514 H  HD12 . LEU   A 1 122 ? 23.934 -11.655 9.866   1.00 15.33 ?  122  LEU   A HD12 1 
ATOM   2515 H  HD13 . LEU   A 1 122 ? 23.652 -11.341 8.335   1.00 15.33 ?  122  LEU   A HD13 1 
ATOM   2516 H  HD21 . LEU   A 1 122 ? 26.154 -9.837  7.825   1.00 14.07 ?  122  LEU   A HD21 1 
ATOM   2517 H  HD22 . LEU   A 1 122 ? 24.771 -9.246  7.313   1.00 14.07 ?  122  LEU   A HD22 1 
ATOM   2518 H  HD23 . LEU   A 1 122 ? 25.707 -8.375  8.257   1.00 14.07 ?  122  LEU   A HD23 1 
ATOM   2519 N  N    . LEU   A 1 123 ? 21.600 -6.986  11.151  1.00 10.16 ?  123  LEU   A N    1 
ATOM   2520 C  CA   . LEU   A 1 123 ? 20.431 -6.196  10.777  1.00 10.03 ?  123  LEU   A CA   1 
ATOM   2521 C  C    . LEU   A 1 123 ? 20.672 -5.680  9.366   1.00 9.62  ?  123  LEU   A C    1 
ATOM   2522 O  O    . LEU   A 1 123 ? 21.720 -5.086  9.108   1.00 10.33 ?  123  LEU   A O    1 
ATOM   2523 C  CB   . LEU   A 1 123 ? 20.295 -5.008  11.730  1.00 10.39 ?  123  LEU   A CB   1 
ATOM   2524 C  CG   . LEU   A 1 123 ? 19.248 -3.959  11.374  1.00 11.30 ?  123  LEU   A CG   1 
ATOM   2525 C  CD1  . LEU   A 1 123 ? 17.841 -4.552  11.373  1.00 11.78 ?  123  LEU   A CD1  1 
ATOM   2526 C  CD2  . LEU   A 1 123 ? 19.342 -2.780  12.339  1.00 12.04 ?  123  LEU   A CD2  1 
ATOM   2527 H  H    . LEU   A 1 123 ? 22.254 -6.502  11.436  1.00 12.21 ?  123  LEU   A H    1 
ATOM   2528 H  HA   . LEU   A 1 123 ? 19.627 -6.741  10.808  1.00 12.06 ?  123  LEU   A HA   1 
ATOM   2529 H  HB2  . LEU   A 1 123 ? 20.063 -5.348  12.613  1.00 12.50 ?  123  LEU   A HB2  1 
ATOM   2530 H  HB3  . LEU   A 1 123 ? 21.146 -4.553  11.779  1.00 12.50 ?  123  LEU   A HB3  1 
ATOM   2531 H  HG   . LEU   A 1 123 ? 19.420 -3.619  10.481  1.00 13.59 ?  123  LEU   A HG   1 
ATOM   2532 H  HD11 . LEU   A 1 123 ? 17.198 -3.855  11.177  1.00 14.16 ?  123  LEU   A HD11 1 
ATOM   2533 H  HD12 . LEU   A 1 123 ? 17.790 -5.250  10.700  1.00 14.16 ?  123  LEU   A HD12 1 
ATOM   2534 H  HD13 . LEU   A 1 123 ? 17.658 -4.931  12.251  1.00 14.16 ?  123  LEU   A HD13 1 
ATOM   2535 H  HD21 . LEU   A 1 123 ? 18.674 -2.119  12.107  1.00 14.47 ?  123  LEU   A HD21 1 
ATOM   2536 H  HD22 . LEU   A 1 123 ? 19.189 -3.102  13.244  1.00 14.47 ?  123  LEU   A HD22 1 
ATOM   2537 H  HD23 . LEU   A 1 123 ? 20.230 -2.393  12.275  1.00 14.47 ?  123  LEU   A HD23 1 
ATOM   2538 N  N    . ALA   A 1 124 ? 19.713 -5.879  8.460   1.00 9.27  ?  124  ALA   A N    1 
ATOM   2539 C  CA   . ALA   A 1 124 ? 19.988 -5.600  7.060   1.00 9.36  ?  124  ALA   A CA   1 
ATOM   2540 C  C    . ALA   A 1 124 ? 18.758 -5.136  6.296   1.00 9.20  ?  124  ALA   A C    1 
ATOM   2541 O  O    . ALA   A 1 124 ? 17.621 -5.464  6.666   1.00 9.99  ?  124  ALA   A O    1 
ATOM   2542 C  CB   . ALA   A 1 124 ? 20.554 -6.835  6.350   1.00 10.06 ?  124  ALA   A CB   1 
ATOM   2543 H  H    . ALA   A 1 124 ? 18.912 -6.172  8.626   1.00 11.15 ?  124  ALA   A H    1 
ATOM   2544 H  HA   . ALA   A 1 124 ? 20.660 -4.906  7.031   1.00 11.26 ?  124  ALA   A HA   1 
ATOM   2545 H  HB1  . ALA   A 1 124 ? 20.738 -6.620  5.421   1.00 12.09 ?  124  ALA   A HB1  1 
ATOM   2546 H  HB2  . ALA   A 1 124 ? 21.389 -7.098  6.790   1.00 12.09 ?  124  ALA   A HB2  1 
ATOM   2547 H  HB3  . ALA   A 1 124 ? 19.919 -7.561  6.404   1.00 12.09 ?  124  ALA   A HB3  1 
ATOM   2548 N  N    A PRO   A 1 125 ? 18.957 -4.399  5.206   0.50 9.49  ?  125  PRO   A N    1 
ATOM   2549 N  N    B PRO   A 1 125 ? 18.961 -4.374  5.218   0.50 8.89  ?  125  PRO   A N    1 
ATOM   2550 C  CA   A PRO   A 1 125 ? 17.905 -4.169  4.216   0.50 9.55  ?  125  PRO   A CA   1 
ATOM   2551 C  CA   B PRO   A 1 125 ? 17.871 -4.026  4.309   0.50 9.31  ?  125  PRO   A CA   1 
ATOM   2552 C  C    A PRO   A 1 125 ? 17.951 -5.237  3.127   0.50 8.94  ?  125  PRO   A C    1 
ATOM   2553 C  C    B PRO   A 1 125 ? 17.833 -5.035  3.175   0.50 9.46  ?  125  PRO   A C    1 
ATOM   2554 O  O    A PRO   A 1 125 ? 18.915 -5.992  3.000   0.50 9.12  ?  125  PRO   A O    1 
ATOM   2555 O  O    B PRO   A 1 125 ? 18.718 -5.892  3.086   0.50 10.04 ?  125  PRO   A O    1 
ATOM   2556 C  CB   A PRO   A 1 125 ? 18.336 -2.825  3.616   0.50 9.71  ?  125  PRO   A CB   1 
ATOM   2557 C  CB   B PRO   A 1 125 ? 18.329 -2.667  3.776   0.50 9.08  ?  125  PRO   A CB   1 
ATOM   2558 C  CG   A PRO   A 1 125 ? 19.841 -2.937  3.587   0.50 10.10 ?  125  PRO   A CG   1 
ATOM   2559 C  CG   B PRO   A 1 125 ? 19.837 -2.889  3.595   0.50 9.15  ?  125  PRO   A CG   1 
ATOM   2560 C  CD   A PRO   A 1 125 ? 20.186 -3.648  4.883   0.50 10.01 ?  125  PRO   A CD   1 
ATOM   2561 C  CD   B PRO   A 1 125 ? 20.250 -3.850  4.721   0.50 8.43  ?  125  PRO   A CD   1 
ATOM   2562 H  HA   A PRO   A 1 125 ? 17.027 -4.115  4.616   0.50 11.48 ?  125  PRO   A HA   1 
ATOM   2563 H  HA   B PRO   A 1 125 ? 17.012 -3.959  4.764   0.50 11.20 ?  125  PRO   A HA   1 
ATOM   2564 H  HB2  A PRO   A 1 125 ? 17.970 -2.726  2.720   0.50 11.68 ?  125  PRO   A HB2  1 
ATOM   2565 H  HB2  B PRO   A 1 125 ? 17.890 -2.473  2.928   0.50 10.92 ?  125  PRO   A HB2  1 
ATOM   2566 H  HB3  A PRO   A 1 125 ? 18.046 -2.098  4.191   0.50 11.68 ?  125  PRO   A HB3  1 
ATOM   2567 H  HB3  B PRO   A 1 125 ? 18.143 -1.964  4.427   0.50 10.92 ?  125  PRO   A HB3  1 
ATOM   2568 H  HG2  A PRO   A 1 125 ? 20.116 -3.462  2.817   0.50 12.15 ?  125  PRO   A HG2  1 
ATOM   2569 H  HG2  B PRO   A 1 125 ? 20.001 -3.286  2.723   0.50 11.00 ?  125  PRO   A HG2  1 
ATOM   2570 H  HG3  A PRO   A 1 125 ? 20.234 -2.050  3.555   0.50 12.15 ?  125  PRO   A HG3  1 
ATOM   2571 H  HG3  B PRO   A 1 125 ? 20.302 -2.040  3.673   0.50 11.00 ?  125  PRO   A HG3  1 
ATOM   2572 H  HD2  A PRO   A 1 125 ? 20.933 -4.246  4.749   0.50 12.03 ?  125  PRO   A HD2  1 
ATOM   2573 H  HD2  B PRO   A 1 125 ? 20.795 -4.565  4.362   0.50 10.14 ?  125  PRO   A HD2  1 
ATOM   2574 H  HD3  A PRO   A 1 125 ? 20.370 -2.995  5.580   0.50 12.03 ?  125  PRO   A HD3  1 
ATOM   2575 H  HD3  B PRO   A 1 125 ? 20.715 -3.358  5.416   0.50 10.14 ?  125  PRO   A HD3  1 
ATOM   2576 N  N    A LEU   A 1 126 ? 16.894 -5.265  2.319   0.50 8.92  ?  126  LEU   A N    1 
ATOM   2577 N  N    B LEU   A 1 126 ? 16.852 -4.926  2.286   0.50 9.62  ?  126  LEU   A N    1 
ATOM   2578 C  CA   A LEU   A 1 126 ? 16.903 -6.085  1.115   0.50 9.86  ?  126  LEU   A CA   1 
ATOM   2579 C  CA   B LEU   A 1 126 ? 16.838 -5.745  1.077   0.50 9.67  ?  126  LEU   A CA   1 
ATOM   2580 C  C    A LEU   A 1 126 ? 17.833 -5.463  0.083   0.50 9.92  ?  126  LEU   A C    1 
ATOM   2581 C  C    B LEU   A 1 126 ? 17.792 -5.145  0.048   0.50 9.52  ?  126  LEU   A C    1 
ATOM   2582 O  O    A LEU   A 1 126 ? 17.627 -4.326  -0.353  0.50 11.02 ?  126  LEU   A O    1 
ATOM   2583 O  O    B LEU   A 1 126 ? 17.550 -4.055  -0.480  0.50 10.80 ?  126  LEU   A O    1 
ATOM   2584 C  CB   A LEU   A 1 126 ? 15.492 -6.221  0.556   0.50 10.09 ?  126  LEU   A CB   1 
ATOM   2585 C  CB   B LEU   A 1 126 ? 15.427 -5.842  0.515   0.50 10.38 ?  126  LEU   A CB   1 
ATOM   2586 C  CG   A LEU   A 1 126 ? 14.624 -7.223  1.315   0.50 10.81 ?  126  LEU   A CG   1 
ATOM   2587 C  CG   B LEU   A 1 126 ? 14.462 -6.734  1.291   0.50 10.42 ?  126  LEU   A CG   1 
ATOM   2588 C  CD1  A LEU   A 1 126 ? 13.187 -7.105  0.868   0.50 11.66 ?  126  LEU   A CD1  1 
ATOM   2589 C  CD1  B LEU   A 1 126 ? 13.088 -6.644  0.666   0.50 11.59 ?  126  LEU   A CD1  1 
ATOM   2590 C  CD2  A LEU   A 1 126 ? 15.142 -8.640  1.100   0.50 10.84 ?  126  LEU   A CD2  1 
ATOM   2591 C  CD2  B LEU   A 1 126 ? 14.928 -8.185  1.324   0.50 10.70 ?  126  LEU   A CD2  1 
ATOM   2592 H  H    A LEU   A 1 126 ? 16.172 -4.819  2.436   0.50 10.72 ?  126  LEU   A H    1 
ATOM   2593 H  H    B LEU   A 1 126 ? 16.184 -4.386  2.367   0.50 11.56 ?  126  LEU   A H    1 
ATOM   2594 H  HA   A LEU   A 1 126 ? 17.239 -6.967  1.321   0.50 11.86 ?  126  LEU   A HA   1 
ATOM   2595 H  HA   B LEU   A 1 126 ? 17.145 -6.637  1.301   0.50 11.63 ?  126  LEU   A HA   1 
ATOM   2596 H  HB2  A LEU   A 1 126 ? 15.050 -5.359  0.603   0.50 12.13 ?  126  LEU   A HB2  1 
ATOM   2597 H  HB2  B LEU   A 1 126 ? 15.047 -4.948  0.492   0.50 12.48 ?  126  LEU   A HB2  1 
ATOM   2598 H  HB3  A LEU   A 1 126 ? 15.541 -6.515  -0.369  0.50 12.13 ?  126  LEU   A HB3  1 
ATOM   2599 H  HB3  B LEU   A 1 126 ? 15.486 -6.192  -0.385  0.50 12.48 ?  126  LEU   A HB3  1 
ATOM   2600 H  HG   A LEU   A 1 126 ? 14.666 -7.032  2.264   0.50 12.99 ?  126  LEU   A HG   1 
ATOM   2601 H  HG   B LEU   A 1 126 ? 14.395 -6.410  2.204   0.50 12.53 ?  126  LEU   A HG   1 
ATOM   2602 H  HD11 A LEU   A 1 126 ? 12.649 -7.747  1.357   0.50 14.01 ?  126  LEU   A HD11 1 
ATOM   2603 H  HD11 B LEU   A 1 126 ? 12.476 -7.208  1.166   0.50 13.93 ?  126  LEU   A HD11 1 
ATOM   2604 H  HD12 A LEU   A 1 126 ? 12.876 -6.205  1.051   0.50 14.01 ?  126  LEU   A HD12 1 
ATOM   2605 H  HD12 B LEU   A 1 126 ? 12.783 -5.724  0.689   0.50 13.93 ?  126  LEU   A HD12 1 
ATOM   2606 H  HD13 A LEU   A 1 126 ? 13.136 -7.286  -0.084  0.50 14.01 ?  126  LEU   A HD13 1 
ATOM   2607 H  HD13 B LEU   A 1 126 ? 13.139 -6.951  -0.255  0.50 13.93 ?  126  LEU   A HD13 1 
ATOM   2608 H  HD21 A LEU   A 1 126 ? 14.472 -9.271  1.397   0.50 13.03 ?  126  LEU   A HD21 1 
ATOM   2609 H  HD21 B LEU   A 1 126 ? 14.209 -8.736  1.666   0.50 12.86 ?  126  LEU   A HD21 1 
ATOM   2610 H  HD22 A LEU   A 1 126 ? 15.322 -8.768  0.153   0.50 13.03 ?  126  LEU   A HD22 1 
ATOM   2611 H  HD22 B LEU   A 1 126 ? 15.157 -8.458  0.421   0.50 12.86 ?  126  LEU   A HD22 1 
ATOM   2612 H  HD23 A LEU   A 1 126 ? 15.960 -8.760  1.608   0.50 13.03 ?  126  LEU   A HD23 1 
ATOM   2613 H  HD23 B LEU   A 1 126 ? 15.704 -8.251  1.898   0.50 12.86 ?  126  LEU   A HD23 1 
ATOM   2614 N  N    A LEU   A 1 127 ? 18.854 -6.215  -0.313  0.50 10.24 ?  127  LEU   A N    1 
ATOM   2615 N  N    B LEU   A 1 127 ? 18.872 -5.858  -0.252  0.50 8.91  ?  127  LEU   A N    1 
ATOM   2616 C  CA   A LEU   A 1 127 ? 19.849 -5.700  -1.237  0.50 9.82  ?  127  LEU   A CA   1 
ATOM   2617 C  CA   B LEU   A 1 127 ? 19.853 -5.349  -1.198  0.50 9.14  ?  127  LEU   A CA   1 
ATOM   2618 C  C    A LEU   A 1 127 ? 19.239 -5.479  -2.610  0.50 9.34  ?  127  LEU   A C    1 
ATOM   2619 C  C    B LEU   A 1 127 ? 19.284 -5.309  -2.614  0.50 9.43  ?  127  LEU   A C    1 
ATOM   2620 O  O    A LEU   A 1 127 ? 18.407 -6.260  -3.079  0.50 9.46  ?  127  LEU   A O    1 
ATOM   2621 O  O    B LEU   A 1 127 ? 18.446 -6.128  -3.003  0.50 9.95  ?  127  LEU   A O    1 
ATOM   2622 C  CB   A LEU   A 1 127 ? 21.019 -6.674  -1.343  0.50 9.42  ?  127  LEU   A CB   1 
ATOM   2623 C  CB   B LEU   A 1 127 ? 21.115 -6.210  -1.163  0.50 9.89  ?  127  LEU   A CB   1 
ATOM   2624 C  CG   A LEU   A 1 127 ? 21.828 -6.877  -0.064  0.50 9.55  ?  127  LEU   A CG   1 
ATOM   2625 C  CG   B LEU   A 1 127 ? 21.884 -6.193  0.160   0.50 11.15 ?  127  LEU   A CG   1 
ATOM   2626 C  CD1  A LEU   A 1 127 ? 22.939 -7.865  -0.333  0.50 9.95  ?  127  LEU   A CD1  1 
ATOM   2627 C  CD1  B LEU   A 1 127 ? 23.030 -7.183  0.107   0.50 12.50 ?  127  LEU   A CD1  1 
ATOM   2628 C  CD2  A LEU   A 1 127 ? 22.398 -5.568  0.458   0.50 10.66 ?  127  LEU   A CD2  1 
ATOM   2629 C  CD2  B LEU   A 1 127 ? 22.401 -4.788  0.477   0.50 11.68 ?  127  LEU   A CD2  1 
ATOM   2630 H  H    A LEU   A 1 127 ? 18.989 -7.027  -0.060  0.50 12.31 ?  127  LEU   A H    1 
ATOM   2631 H  H    B LEU   A 1 127 ? 19.063 -6.633  0.087   0.50 10.72 ?  127  LEU   A H    1 
ATOM   2632 H  HA   A LEU   A 1 127 ? 20.181 -4.856  -0.914  0.50 11.81 ?  127  LEU   A HA   1 
ATOM   2633 H  HA   B LEU   A 1 127 ? 20.096 -4.445  -0.935  0.50 10.99 ?  127  LEU   A HA   1 
ATOM   2634 H  HB2  A LEU   A 1 127 ? 20.673 -7.543  -1.604  0.50 11.33 ?  127  LEU   A HB2  1 
ATOM   2635 H  HB2  B LEU   A 1 127 ? 20.863 -7.129  -1.345  0.50 11.89 ?  127  LEU   A HB2  1 
ATOM   2636 H  HB3  A LEU   A 1 127 ? 21.627 -6.350  -2.025  0.50 11.33 ?  127  LEU   A HB3  1 
ATOM   2637 H  HB3  B LEU   A 1 127 ? 21.716 -5.894  -1.855  0.50 11.89 ?  127  LEU   A HB3  1 
ATOM   2638 H  HG   A LEU   A 1 127 ? 21.252 -7.249  0.623   0.50 11.49 ?  127  LEU   A HG   1 
ATOM   2639 H  HG   B LEU   A 1 127 ? 21.287 -6.462  0.877   0.50 13.41 ?  127  LEU   A HG   1 
ATOM   2640 H  HD11 A LEU   A 1 127 ? 23.429 -8.019  0.490   0.50 11.96 ?  127  LEU   A HD11 1 
ATOM   2641 H  HD11 B LEU   A 1 127 ? 23.533 -7.127  0.934   0.50 15.02 ?  127  LEU   A HD11 1 
ATOM   2642 H  HD12 A LEU   A 1 127 ? 22.553 -8.695  -0.650  0.50 11.96 ?  127  LEU   A HD12 1 
ATOM   2643 H  HD12 B LEU   A 1 127 ? 22.669 -8.078  0.000   0.50 15.02 ?  127  LEU   A HD12 1 
ATOM   2644 H  HD13 A LEU   A 1 127 ? 23.531 -7.495  -1.006  0.50 11.96 ?  127  LEU   A HD13 1 
ATOM   2645 H  HD13 B LEU   A 1 127 ? 23.601 -6.964  -0.644  0.50 15.02 ?  127  LEU   A HD13 1 
ATOM   2646 H  HD21 A LEU   A 1 127 ? 23.023 -5.759  1.173   0.50 12.82 ?  127  LEU   A HD21 1 
ATOM   2647 H  HD21 B LEU   A 1 127 ? 23.004 -4.837  1.235   0.50 14.04 ?  127  LEU   A HD21 1 
ATOM   2648 H  HD22 A LEU   A 1 127 ? 22.857 -5.115  -0.269  0.50 12.82 ?  127  LEU   A HD22 1 
ATOM   2649 H  HD22 B LEU   A 1 127 ? 22.874 -4.445  -0.299  0.50 14.04 ?  127  LEU   A HD22 1 
ATOM   2650 H  HD23 A LEU   A 1 127 ? 21.674 -5.015  0.787   0.50 12.82 ?  127  LEU   A HD23 1 
ATOM   2651 H  HD23 B LEU   A 1 127 ? 21.650 -4.213  0.687   0.50 14.04 ?  127  LEU   A HD23 1 
ATOM   2652 N  N    A SER   A 1 128 ? 19.678 -4.406  -3.256  0.50 9.18  ?  128  SER   A N    1 
ATOM   2653 N  N    B SER   A 1 128 ? 19.763 -4.328  -3.380  0.50 9.85  ?  128  SER   A N    1 
ATOM   2654 C  CA   A SER   A 1 128 ? 19.267 -4.002  -4.593  0.50 9.46  ?  128  SER   A CA   1 
ATOM   2655 C  CA   B SER   A 1 128 ? 19.435 -4.103  -4.787  0.50 9.90  ?  128  SER   A CA   1 
ATOM   2656 C  C    A SER   A 1 128 ? 17.806 -3.579  -4.677  0.50 9.83  ?  128  SER   A C    1 
ATOM   2657 C  C    B SER   A 1 128 ? 18.015 -3.609  -5.051  0.50 10.12 ?  128  SER   A C    1 
ATOM   2658 O  O    A SER   A 1 128 ? 17.323 -3.298  -5.777  0.50 10.57 ?  128  SER   A O    1 
ATOM   2659 O  O    B SER   A 1 128 ? 17.716 -3.191  -6.173  0.50 10.32 ?  128  SER   A O    1 
ATOM   2660 C  CB   A SER   A 1 128 ? 19.619 -5.042  -5.663  0.50 9.44  ?  128  SER   A CB   1 
ATOM   2661 C  CB   B SER   A 1 128 ? 19.775 -5.315  -5.658  0.50 10.14 ?  128  SER   A CB   1 
ATOM   2662 O  OG   A SER   A 1 128 ? 21.026 -5.234  -5.712  0.50 9.93  ?  128  SER   A OG   1 
ATOM   2663 O  OG   B SER   A 1 128 ? 21.181 -5.465  -5.775  0.50 10.58 ?  128  SER   A OG   1 
ATOM   2664 H  H    A SER   A 1 128 ? 20.258 -3.869  -2.918  0.50 11.04 ?  128  SER   A H    1 
ATOM   2665 H  H    B SER   A 1 128 ? 20.334 -3.756  -3.083  0.50 11.84 ?  128  SER   A H    1 
ATOM   2666 H  HA   A SER   A 1 128 ? 19.782 -3.218  -4.812  0.50 11.38 ?  128  SER   A HA   1 
ATOM   2667 H  HA   B SER   A 1 128 ? 20.012 -3.393  -5.087  0.50 11.90 ?  128  SER   A HA   1 
ATOM   2668 H  HB2  A SER   A 1 128 ? 19.184 -5.882  -5.445  0.50 11.35 ?  128  SER   A HB2  1 
ATOM   2669 H  HB2  B SER   A 1 128 ? 19.397 -6.112  -5.262  0.50 12.19 ?  128  SER   A HB2  1 
ATOM   2670 H  HB3  A SER   A 1 128 ? 19.306 -4.722  -6.526  0.50 11.35 ?  128  SER   A HB3  1 
ATOM   2671 H  HB3  B SER   A 1 128 ? 19.401 -5.172  -6.545  0.50 12.19 ?  128  SER   A HB3  1 
ATOM   2672 H  HG   A SER   A 1 128 ? 21.405 -4.506  -5.895  0.50 11.93 ?  128  SER   A HG   1 
ATOM   2673 H  HG   B SER   A 1 128 ? 21.510 -4.761  -6.101  0.50 12.72 ?  128  SER   A HG   1 
ATOM   2674 N  N    A ALA   A 1 129 ? 17.097 -3.504  -3.550  0.50 9.88  ?  129  ALA   A N    1 
ATOM   2675 N  N    B ALA   A 1 129 ? 17.142 -3.637  -4.049  0.50 10.40 ?  129  ALA   A N    1 
ATOM   2676 C  CA   A ALA   A 1 129 ? 15.726 -3.021  -3.532  0.50 9.65  ?  129  ALA   A CA   1 
ATOM   2677 C  CA   B ALA   A 1 129 ? 15.803 -3.083  -4.200  0.50 10.62 ?  129  ALA   A CA   1 
ATOM   2678 C  C    A ALA   A 1 129 ? 15.714 -1.493  -3.482  0.50 8.99  ?  129  ALA   A C    1 
ATOM   2679 C  C    B ALA   A 1 129 ? 15.857 -1.568  -3.977  0.50 10.61 ?  129  ALA   A C    1 
ATOM   2680 O  O    A ALA   A 1 129 ? 16.758 -0.833  -3.520  0.50 9.56  ?  129  ALA   A O    1 
ATOM   2681 O  O    B ALA   A 1 129 ? 16.930 -0.960  -3.926  0.50 10.76 ?  129  ALA   A O    1 
ATOM   2682 C  CB   A ALA   A 1 129 ? 14.965 -3.631  -2.356  0.50 10.34 ?  129  ALA   A CB   1 
ATOM   2683 C  CB   B ALA   A 1 129 ? 14.821 -3.828  -3.298  0.50 11.40 ?  129  ALA   A CB   1 
ATOM   2684 H  H    A ALA   A 1 129 ? 17.393 -3.728  -2.773  0.50 11.88 ?  129  ALA   A H    1 
ATOM   2685 H  H    B ALA   A 1 129 ? 17.292 -3.986  -3.273  0.50 12.50 ?  129  ALA   A H    1 
ATOM   2686 H  HA   A ALA   A 1 129 ? 15.283 -3.295  -4.342  0.50 11.60 ?  129  ALA   A HA   1 
ATOM   2687 H  HA   B ALA   A 1 129 ? 15.516 -3.223  -5.113  0.50 12.77 ?  129  ALA   A HA   1 
ATOM   2688 H  HB1  A ALA   A 1 129 ? 14.049 -3.305  -2.362  0.50 12.43 ?  129  ALA   A HB1  1 
ATOM   2689 H  HB1  B ALA   A 1 129 ? 13.934 -3.452  -3.422  0.50 13.70 ?  129  ALA   A HB1  1 
ATOM   2690 H  HB2  A ALA   A 1 129 ? 14.971 -4.597  -2.441  0.50 12.43 ?  129  ALA   A HB2  1 
ATOM   2691 H  HB2  B ALA   A 1 129 ? 14.813 -4.769  -3.551  0.50 13.70 ?  129  ALA   A HB2  1 
ATOM   2692 H  HB3  A ALA   A 1 129 ? 15.398 -3.372  -1.523  0.50 12.43 ?  129  ALA   A HB3  1 
ATOM   2693 H  HB3  B ALA   A 1 129 ? 15.098 -3.736  -2.378  0.50 13.70 ?  129  ALA   A HB3  1 
ATOM   2694 N  N    A GLY   A 1 130 ? 14.515 -0.927  -3.390  0.50 9.59  ?  130  GLY   A N    1 
ATOM   2695 N  N    B GLY   A 1 130 ? 14.694 -0.938  -3.855  0.50 10.94 ?  130  GLY   A N    1 
ATOM   2696 C  CA   A GLY   A 1 130 ? 14.400 0.520   -3.347  0.50 10.48 ?  130  GLY   A CA   1 
ATOM   2697 C  CA   B GLY   A 1 130 ? 14.676 0.506   -3.716  0.50 11.84 ?  130  GLY   A CA   1 
ATOM   2698 C  C    A GLY   A 1 130 ? 15.009 1.142   -4.587  0.50 10.35 ?  130  GLY   A C    1 
ATOM   2699 C  C    B GLY   A 1 130 ? 15.325 1.185   -4.901  0.50 11.83 ?  130  GLY   A C    1 
ATOM   2700 O  O    A GLY   A 1 130 ? 14.779 0.690   -5.714  0.50 10.16 ?  130  GLY   A O    1 
ATOM   2701 O  O    B GLY   A 1 130 ? 15.126 0.799   -6.058  0.50 12.21 ?  130  GLY   A O    1 
ATOM   2702 H  H    A GLY   A 1 130 ? 13.761 -1.348  -3.354  0.50 11.53 ?  130  GLY   A H    1 
ATOM   2703 H  H    B GLY   A 1 130 ? 13.923 -1.316  -3.846  0.50 13.15 ?  130  GLY   A H    1 
ATOM   2704 H  HA2  A GLY   A 1 130 ? 13.461 0.775   -3.288  0.50 12.60 ?  130  GLY   A HA2  1 
ATOM   2705 H  HA2  B GLY   A 1 130 ? 13.758 0.819   -3.636  0.50 14.24 ?  130  GLY   A HA2  1 
ATOM   2706 H  HA3  A GLY   A 1 130 ? 14.862 0.864   -2.572  0.50 12.60 ?  130  GLY   A HA3  1 
ATOM   2707 H  HA3  B GLY   A 1 130 ? 15.166 0.768   -2.930  0.50 14.24 ?  130  GLY   A HA3  1 
ATOM   2708 N  N    A ILE   A 1 131 ? 15.798 2.201   -4.380  0.50 10.85 ?  131  ILE   A N    1 
ATOM   2709 N  N    B ILE   A 1 131 ? 16.123 2.215   -4.608  0.50 11.99 ?  131  ILE   A N    1 
ATOM   2710 C  CA   A ILE   A 1 131 ? 16.335 2.976   -5.496  0.50 10.99 ?  131  ILE   A CA   1 
ATOM   2711 C  CA   B ILE   A 1 131 ? 16.731 3.026   -5.655  0.50 11.56 ?  131  ILE   A CA   1 
ATOM   2712 C  C    A ILE   A 1 131 ? 17.379 2.227   -6.310  0.50 11.00 ?  131  ILE   A C    1 
ATOM   2713 C  C    B ILE   A 1 131 ? 17.714 2.247   -6.511  0.50 11.42 ?  131  ILE   A C    1 
ATOM   2714 O  O    A ILE   A 1 131 ? 17.804 2.739   -7.351  0.50 11.45 ?  131  ILE   A O    1 
ATOM   2715 O  O    B ILE   A 1 131 ? 18.118 2.742   -7.570  0.50 12.15 ?  131  ILE   A O    1 
ATOM   2716 C  CB   A ILE   A 1 131 ? 16.864 4.356   -5.047  0.50 11.93 ?  131  ILE   A CB   1 
ATOM   2717 C  CB   B ILE   A 1 131 ? 17.369 4.316   -5.088  0.50 12.28 ?  131  ILE   A CB   1 
ATOM   2718 C  CG1  A ILE   A 1 131 ? 18.110 4.219   -4.162  0.50 12.89 ?  131  ILE   A CG1  1 
ATOM   2719 C  CG1  B ILE   A 1 131 ? 18.589 3.999   -4.211  0.50 13.22 ?  131  ILE   A CG1  1 
ATOM   2720 C  CG2  A ILE   A 1 131 ? 15.762 5.136   -4.341  0.50 12.07 ?  131  ILE   A CG2  1 
ATOM   2721 C  CG2  B ILE   A 1 131 ? 16.330 5.126   -4.323  0.50 12.30 ?  131  ILE   A CG2  1 
ATOM   2722 C  CD1  A ILE   A 1 131 ? 18.779 5.553   -3.835  0.50 13.95 ?  131  ILE   A CD1  1 
ATOM   2723 C  CD1  B ILE   A 1 131 ? 19.257 5.235   -3.597  0.50 14.24 ?  131  ILE   A CD1  1 
ATOM   2724 H  H    A ILE   A 1 131 ? 16.019 2.497   -3.607  0.50 13.04 ?  131  ILE   A H    1 
ATOM   2725 H  H    B ILE   A 1 131 ? 16.316 2.468   -3.809  0.50 14.41 ?  131  ILE   A H    1 
ATOM   2726 H  HA   A ILE   A 1 131 ? 15.602 3.155   -6.105  0.50 13.21 ?  131  ILE   A HA   1 
ATOM   2727 H  HA   B ILE   A 1 131 ? 16.030 3.306   -6.252  0.50 13.90 ?  131  ILE   A HA   1 
ATOM   2728 H  HB   A ILE   A 1 131 ? 17.114 4.851   -5.840  0.50 14.34 ?  131  ILE   A HB   1 
ATOM   2729 H  HB   B ILE   A 1 131 ? 17.670 4.852   -5.837  0.50 14.76 ?  131  ILE   A HB   1 
ATOM   2730 H  HG12 A ILE   A 1 131 ? 17.857 3.799   -3.326  0.50 15.49 ?  131  ILE   A HG12 1 
ATOM   2731 H  HG12 B ILE   A 1 131 ? 18.312 3.423   -3.487  0.50 15.89 ?  131  ILE   A HG12 1 
ATOM   2732 H  HG13 A ILE   A 1 131 ? 18.765 3.669   -4.621  0.50 15.49 ?  131  ILE   A HG13 1 
ATOM   2733 H  HG13 B ILE   A 1 131 ? 19.256 3.552   -4.755  0.50 15.89 ?  131  ILE   A HG13 1 
ATOM   2734 H  HG21 A ILE   A 1 131 ? 16.068 6.039   -4.175  0.50 14.50 ?  131  ILE   A HG21 1 
ATOM   2735 H  HG21 B ILE   A 1 131 ? 16.690 6.005   -4.133  0.50 14.78 ?  131  ILE   A HG21 1 
ATOM   2736 H  HG22 A ILE   A 1 131 ? 14.975 5.152   -4.910  0.50 14.50 ?  131  ILE   A HG22 1 
ATOM   2737 H  HG22 B ILE   A 1 131 ? 15.532 5.206   -4.870  0.50 14.78 ?  131  ILE   A HG22 1 
ATOM   2738 H  HG23 A ILE   A 1 131 ? 15.550 4.696   -3.502  0.50 14.50 ?  131  ILE   A HG23 1 
ATOM   2739 H  HG23 B ILE   A 1 131 ? 16.118 4.666   -3.496  0.50 14.78 ?  131  ILE   A HG23 1 
ATOM   2740 H  HD11 A ILE   A 1 131 ? 19.606 5.382   -3.355  0.50 16.76 ?  131  ILE   A HD11 1 
ATOM   2741 H  HD11 B ILE   A 1 131 ? 20.084 4.966   -3.165  0.50 17.11 ?  131  ILE   A HD11 1 
ATOM   2742 H  HD12 A ILE   A 1 131 ? 18.971 6.023   -4.662  0.50 16.76 ?  131  ILE   A HD12 1 
ATOM   2743 H  HD12 B ILE   A 1 131 ? 19.448 5.879   -4.299  0.50 17.11 ?  131  ILE   A HD12 1 
ATOM   2744 H  HD13 A ILE   A 1 131 ? 18.182 6.082   -3.285  0.50 16.76 ?  131  ILE   A HD13 1 
ATOM   2745 H  HD13 B ILE   A 1 131 ? 18.658 5.631   -2.944  0.50 17.11 ?  131  ILE   A HD13 1 
ATOM   2746 N  N    A PHE   A 1 132 ? 17.798 1.032   -5.876  0.50 10.97 ?  132  PHE   A N    1 
ATOM   2747 N  N    B PHE   A 1 132 ? 18.104 1.039   -6.089  0.50 11.26 ?  132  PHE   A N    1 
ATOM   2748 C  CA   A PHE   A 1 132 ? 18.678 0.202   -6.691  0.50 11.14 ?  132  PHE   A CA   1 
ATOM   2749 C  CA   B PHE   A 1 132 ? 18.983 0.204   -6.900  0.50 11.33 ?  132  PHE   A CA   1 
ATOM   2750 C  C    A PHE   A 1 132 ? 17.931 -0.547  -7.796  0.50 11.32 ?  132  PHE   A C    1 
ATOM   2751 C  C    B PHE   A 1 132 ? 18.248 -0.548  -8.010  0.50 12.17 ?  132  PHE   A C    1 
ATOM   2752 O  O    A PHE   A 1 132 ? 18.573 -1.148  -8.663  0.50 12.21 ?  132  PHE   A O    1 
ATOM   2753 O  O    B PHE   A 1 132 ? 18.907 -1.165  -8.857  0.50 13.48 ?  132  PHE   A O    1 
ATOM   2754 C  CB   A PHE   A 1 132 ? 19.457 -0.778  -5.805  0.50 11.32 ?  132  PHE   A CB   1 
ATOM   2755 C  CB   B PHE   A 1 132 ? 19.765 -0.778  -6.017  0.50 10.75 ?  132  PHE   A CB   1 
ATOM   2756 C  CG   A PHE   A 1 132 ? 20.708 -0.198  -5.172  0.50 11.32 ?  132  PHE   A CG   1 
ATOM   2757 C  CG   B PHE   A 1 132 ? 20.928 -0.156  -5.269  0.50 10.30 ?  132  PHE   A CG   1 
ATOM   2758 C  CD1  A PHE   A 1 132 ? 20.638 0.850   -4.267  0.50 12.35 ?  132  PHE   A CD1  1 
ATOM   2759 C  CD1  B PHE   A 1 132 ? 20.722 0.769   -4.256  0.50 11.43 ?  132  PHE   A CD1  1 
ATOM   2760 C  CD2  A PHE   A 1 132 ? 21.953 -0.748  -5.450  0.50 11.98 ?  132  PHE   A CD2  1 
ATOM   2761 C  CD2  B PHE   A 1 132 ? 22.231 -0.535  -5.559  0.50 11.01 ?  132  PHE   A CD2  1 
ATOM   2762 C  CE1  A PHE   A 1 132 ? 21.791 1.359   -3.678  0.50 12.68 ?  132  PHE   A CE1  1 
ATOM   2763 C  CE1  B PHE   A 1 132 ? 21.796 1.322   -3.566  0.50 11.66 ?  132  PHE   A CE1  1 
ATOM   2764 C  CE2  A PHE   A 1 132 ? 23.107 -0.248  -4.862  0.50 12.64 ?  132  PHE   A CE2  1 
ATOM   2765 C  CE2  B PHE   A 1 132 ? 23.308 0.011   -4.871  0.50 11.56 ?  132  PHE   A CE2  1 
ATOM   2766 C  CZ   A PHE   A 1 132 ? 23.023 0.807   -3.974  0.50 12.95 ?  132  PHE   A CZ   1 
ATOM   2767 C  CZ   B PHE   A 1 132 ? 23.088 0.940   -3.872  0.50 11.78 ?  132  PHE   A CZ   1 
ATOM   2768 H  H    A PHE   A 1 132 ? 17.588 0.685   -5.113  0.50 13.18 ?  132  PHE   A H    1 
ATOM   2769 H  H    B PHE   A 1 132 ? 17.884 0.686   -5.327  0.50 13.54 ?  132  PHE   A H    1 
ATOM   2770 H  HA   A PHE   A 1 132 ? 19.329 0.778   -7.117  0.50 13.39 ?  132  PHE   A HA   1 
ATOM   2771 H  HA   B PHE   A 1 132 ? 19.638 0.780   -7.320  0.50 13.62 ?  132  PHE   A HA   1 
ATOM   2772 H  HB2  A PHE   A 1 132 ? 18.880 -1.076  -5.084  0.50 13.60 ?  132  PHE   A HB2  1 
ATOM   2773 H  HB2  B PHE   A 1 132 ? 19.169 -1.157  -5.355  0.50 12.92 ?  132  PHE   A HB2  1 
ATOM   2774 H  HB3  A PHE   A 1 132 ? 19.729 -1.537  -6.343  0.50 13.60 ?  132  PHE   A HB3  1 
ATOM   2775 H  HB3  B PHE   A 1 132 ? 20.126 -1.486  -6.577  0.50 12.92 ?  132  PHE   A HB3  1 
ATOM   2776 H  HD1  A PHE   A 1 132 ? 19.815 1.226   -4.058  0.50 14.84 ?  132  PHE   A HD1  1 
ATOM   2777 H  HD1  B PHE   A 1 132 ? 19.859 1.030   -4.040  0.50 13.74 ?  132  PHE   A HD1  1 
ATOM   2778 H  HD2  A PHE   A 1 132 ? 22.018 -1.459  -6.047  0.50 14.40 ?  132  PHE   A HD2  1 
ATOM   2779 H  HD2  B PHE   A 1 132 ? 22.391 -1.161  -6.229  0.50 13.23 ?  132  PHE   A HD2  1 
ATOM   2780 H  HE1  A PHE   A 1 132 ? 21.735 2.067   -3.077  0.50 15.24 ?  132  PHE   A HE1  1 
ATOM   2781 H  HE1  B PHE   A 1 132 ? 21.644 1.946   -2.893  0.50 14.02 ?  132  PHE   A HE1  1 
ATOM   2782 H  HE2  A PHE   A 1 132 ? 23.936 -0.620  -5.067  0.50 15.19 ?  132  PHE   A HE2  1 
ATOM   2783 H  HE2  B PHE   A 1 132 ? 24.178 -0.247  -5.084  0.50 13.89 ?  132  PHE   A HE2  1 
ATOM   2784 H  HZ   A PHE   A 1 132 ? 23.794 1.150   -3.578  0.50 15.56 ?  132  PHE   A HZ   1 
ATOM   2785 H  HZ   B PHE   A 1 132 ? 23.808 1.312   -3.412  0.50 14.16 ?  132  PHE   A HZ   1 
ATOM   2786 N  N    A GLY   A 1 133 ? 16.600 -0.538  -7.784  0.50 11.55 ?  133  GLY   A N    1 
ATOM   2787 N  N    B GLY   A 1 133 ? 16.912 -0.529  -8.029  0.50 11.91 ?  133  GLY   A N    1 
ATOM   2788 C  CA   A GLY   A 1 133 ? 15.824 -0.912  -8.951  0.50 12.27 ?  133  GLY   A CA   1 
ATOM   2789 C  CA   B GLY   A 1 133 ? 16.155 -0.893  -9.208  0.50 12.01 ?  133  GLY   A CA   1 
ATOM   2790 C  C    A GLY   A 1 133 ? 15.563 -2.387  -9.179  0.50 12.78 ?  133  GLY   A C    1 
ATOM   2791 C  C    B GLY   A 1 133 ? 15.556 -2.289  -9.231  0.50 12.38 ?  133  GLY   A C    1 
ATOM   2792 O  O    A GLY   A 1 133 ? 15.027 -2.733  -10.239 0.50 13.60 ?  133  GLY   A O    1 
ATOM   2793 O  O    B GLY   A 1 133 ? 14.661 -2.536  -10.050 0.50 12.66 ?  133  GLY   A O    1 
ATOM   2794 H  H    A GLY   A 1 133 ? 16.126 -0.307  -7.109  0.50 13.88 ?  133  GLY   A H    1 
ATOM   2795 H  H    B GLY   A 1 133 ? 16.424 -0.289  -7.357  0.50 14.31 ?  133  GLY   A H    1 
ATOM   2796 H  HA2  A GLY   A 1 133 ? 14.965 -0.470  -8.897  0.50 14.75 ?  133  GLY   A HA2  1 
ATOM   2797 H  HA2  B GLY   A 1 133 ? 15.420 -0.275  -9.305  0.50 14.44 ?  133  GLY   A HA2  1 
ATOM   2798 H  HA3  A GLY   A 1 133 ? 16.277 -0.581  -9.742  0.50 14.75 ?  133  GLY   A HA3  1 
ATOM   2799 H  HA3  B GLY   A 1 133 ? 16.732 -0.791  -9.984  0.50 14.44 ?  133  GLY   A HA3  1 
ATOM   2800 N  N    A ALA   A 1 134 ? 15.915 -3.270  -8.245  0.50 12.38 ?  134  ALA   A N    1 
ATOM   2801 N  N    B ALA   A 1 134 ? 16.006 -3.205  -8.376  0.50 12.14 ?  134  ALA   A N    1 
ATOM   2802 C  CA   A ALA   A 1 134 ? 15.615 -4.684  -8.424  0.50 12.81 ?  134  ALA   A CA   1 
ATOM   2803 C  CA   B ALA   A 1 134 ? 15.565 -4.590  -8.484  0.50 12.44 ?  134  ALA   A CA   1 
ATOM   2804 C  C    A ALA   A 1 134 ? 14.251 -5.033  -7.828  0.50 12.97 ?  134  ALA   A C    1 
ATOM   2805 C  C    B ALA   A 1 134 ? 14.263 -4.828  -7.716  0.50 12.23 ?  134  ALA   A C    1 
ATOM   2806 O  O    A ALA   A 1 134 ? 13.653 -4.264  -7.072  0.50 13.97 ?  134  ALA   A O    1 
ATOM   2807 O  O    B ALA   A 1 134 ? 13.818 -4.008  -6.908  0.50 12.87 ?  134  ALA   A O    1 
ATOM   2808 C  CB   A ALA   A 1 134 ? 16.701 -5.564  -7.802  0.50 13.60 ?  134  ALA   A CB   1 
ATOM   2809 C  CB   B ALA   A 1 134 ? 16.654 -5.550  -8.005  0.50 13.66 ?  134  ALA   A CB   1 
ATOM   2810 H  H    A ALA   A 1 134 ? 16.334 -3.076  -7.514  0.50 14.88 ?  134  ALA   A H    1 
ATOM   2811 H  H    B ALA   A 1 134 ? 16.556 -3.049  -7.730  0.50 14.59 ?  134  ALA   A H    1 
ATOM   2812 H  HA   A ALA   A 1 134 ? 15.586 -4.879  -9.373  0.50 15.40 ?  134  ALA   A HA   1 
ATOM   2813 H  HA   B ALA   A 1 134 ? 15.398 -4.783  -9.419  0.50 14.96 ?  134  ALA   A HA   1 
ATOM   2814 H  HB1  A ALA   A 1 134 ? 16.483 -6.495  -7.968  0.50 16.35 ?  134  ALA   A HB1  1 
ATOM   2815 H  HB1  B ALA   A 1 134 ? 16.331 -6.459  -8.097  0.50 16.41 ?  134  ALA   A HB1  1 
ATOM   2816 H  HB2  A ALA   A 1 134 ? 17.555 -5.347  -8.212  0.50 16.35 ?  134  ALA   A HB2  1 
ATOM   2817 H  HB2  B ALA   A 1 134 ? 17.447 -5.423  -8.551  0.50 16.41 ?  134  ALA   A HB2  1 
ATOM   2818 H  HB3  A ALA   A 1 134 ? 16.739 -5.396  -6.850  0.50 16.35 ?  134  ALA   A HB3  1 
ATOM   2819 H  HB3  B ALA   A 1 134 ? 16.857 -5.360  -7.078  0.50 16.41 ?  134  ALA   A HB3  1 
ATOM   2820 N  N    A ASP   A 1 135 ? 13.763 -6.217  -8.184  0.50 13.37 ?  135  ASP   A N    1 
ATOM   2821 N  N    B ASP   A 1 135 ? 13.656 -5.986  -7.984  0.50 12.91 ?  135  ASP   A N    1 
ATOM   2822 C  CA   A ASP   A 1 135 ? 12.510 -6.727  -7.636  0.50 13.69 ?  135  ASP   A CA   1 
ATOM   2823 C  CA   B ASP   A 1 135 ? 12.389 -6.364  -7.367  0.50 13.69 ?  135  ASP   A CA   1 
ATOM   2824 C  C    A ASP   A 1 135 ? 12.737 -7.164  -6.195  0.50 13.12 ?  135  ASP   A C    1 
ATOM   2825 C  C    B ASP   A 1 135 ? 12.635 -6.844  -5.940  0.50 12.91 ?  135  ASP   A C    1 
ATOM   2826 O  O    A ASP   A 1 135 ? 13.544 -8.071  -5.955  0.50 13.24 ?  135  ASP   A O    1 
ATOM   2827 O  O    B ASP   A 1 135 ? 13.379 -7.812  -5.744  0.50 12.66 ?  135  ASP   A O    1 
ATOM   2828 C  CB   A ASP   A 1 135 ? 12.050 -7.920  -8.467  0.50 15.43 ?  135  ASP   A CB   1 
ATOM   2829 C  CB   B ASP   A 1 135 ? 11.751 -7.487  -8.176  0.50 15.24 ?  135  ASP   A CB   1 
ATOM   2830 C  CG   A ASP   A 1 135 ? 10.779 -8.568  -7.939  0.50 17.19 ?  135  ASP   A CG   1 
ATOM   2831 C  CG   B ASP   A 1 135 ? 10.339 -7.827  -7.712  0.50 17.16 ?  135  ASP   A CG   1 
ATOM   2832 O  OD1  A ASP   A 1 135 ? 10.192 -8.081  -6.952  0.50 17.23 ?  135  ASP   A OD1  1 
ATOM   2833 O  OD1  B ASP   A 1 135 ? 9.964  -7.448  -6.580  0.50 17.58 ?  135  ASP   A OD1  1 
ATOM   2834 O  OD2  A ASP   A 1 135 ? 10.366 -9.586  -8.527  0.50 19.06 -1 135  ASP   A OD2  1 
ATOM   2835 O  OD2  B ASP   A 1 135 ? 9.607  -8.487  -8.482  0.50 18.86 -1 135  ASP   A OD2  1 
ATOM   2836 H  H    A ASP   A 1 135 ? 14.140 -6.745  -8.747  0.50 16.07 ?  135  ASP   A H    1 
ATOM   2837 H  H    B ASP   A 1 135 ? 13.961 -6.574  -8.529  0.50 15.52 ?  135  ASP   A H    1 
ATOM   2838 H  HA   A ASP   A 1 135 ? 11.834 -6.034  -7.673  0.50 16.46 ?  135  ASP   A HA   1 
ATOM   2839 H  HA   B ASP   A 1 135 ? 11.784 -5.602  -7.370  0.50 16.46 ?  135  ASP   A HA   1 
ATOM   2840 H  HB2  A ASP   A 1 135 ? 11.876 -7.627  -9.370  0.50 18.54 ?  135  ASP   A HB2  1 
ATOM   2841 H  HB2  B ASP   A 1 135 ? 11.725 -7.223  -9.111  0.50 18.31 ?  135  ASP   A HB2  1 
ATOM   2842 H  HB3  A ASP   A 1 135 ? 12.738 -8.598  -8.455  0.50 18.54 ?  135  ASP   A HB3  1 
ATOM   2843 H  HB3  B ASP   A 1 135 ? 12.286 -8.287  -8.075  0.50 18.31 ?  135  ASP   A HB3  1 
ATOM   2844 N  N    A PRO   A 1 136 ? 12.060 -6.563  -5.215  0.50 12.65 ?  136  PRO   A N    1 
ATOM   2845 N  N    B PRO   A 1 136 ? 12.037 -6.212  -4.927  0.50 12.40 ?  136  PRO   A N    1 
ATOM   2846 C  CA   A PRO   A 1 136 ? 12.298 -6.965  -3.820  0.50 12.38 ?  136  PRO   A CA   1 
ATOM   2847 C  CA   B PRO   A 1 136 ? 12.275 -6.659  -3.544  0.50 12.51 ?  136  PRO   A CA   1 
ATOM   2848 C  C    A PRO   A 1 136 ? 11.882 -8.392  -3.516  0.50 11.70 ?  136  PRO   A C    1 
ATOM   2849 C  C    B PRO   A 1 136 ? 11.834 -8.087  -3.263  0.50 12.04 ?  136  PRO   A C    1 
ATOM   2850 O  O    A PRO   A 1 136 ? 12.486 -9.021  -2.640  0.50 11.67 ?  136  PRO   A O    1 
ATOM   2851 O  O    B PRO   A 1 136 ? 12.426 -8.742  -2.397  0.50 10.99 ?  136  PRO   A O    1 
ATOM   2852 C  CB   A PRO   A 1 136 ? 11.489 -5.942  -3.011  0.50 13.16 ?  136  PRO   A CB   1 
ATOM   2853 C  CB   B PRO   A 1 136 ? 11.504 -5.628  -2.704  0.50 13.23 ?  136  PRO   A CB   1 
ATOM   2854 C  CG   A PRO   A 1 136 ? 10.436 -5.456  -3.959  0.50 13.76 ?  136  PRO   A CG   1 
ATOM   2855 C  CG   B PRO   A 1 136 ? 10.509 -5.036  -3.647  0.50 13.57 ?  136  PRO   A CG   1 
ATOM   2856 C  CD   A PRO   A 1 136 ? 11.056 -5.490  -5.324  0.50 13.27 ?  136  PRO   A CD   1 
ATOM   2857 C  CD   B PRO   A 1 136 ? 11.177 -5.020  -4.978  0.50 12.89 ?  136  PRO   A CD   1 
ATOM   2858 H  HA   A PRO   A 1 136 ? 13.238 -6.865  -3.598  0.50 14.88 ?  136  PRO   A HA   1 
ATOM   2859 H  HA   B PRO   A 1 136 ? 13.217 -6.577  -3.333  0.50 15.04 ?  136  PRO   A HA   1 
ATOM   2860 H  HB2  A PRO   A 1 136 ? 11.088 -6.375  -2.241  0.50 15.82 ?  136  PRO   A HB2  1 
ATOM   2861 H  HB2  B PRO   A 1 136 ? 11.056 -6.069  -1.966  0.50 15.90 ?  136  PRO   A HB2  1 
ATOM   2862 H  HB3  A PRO   A 1 136 ? 12.068 -5.214  -2.733  0.50 15.82 ?  136  PRO   A HB3  1 
ATOM   2863 H  HB3  B PRO   A 1 136 ? 12.113 -4.943  -2.377  0.50 15.90 ?  136  PRO   A HB3  1 
ATOM   2864 H  HG2  A PRO   A 1 136 ? 9.669  -6.045  -3.920  0.50 16.53 ?  136  PRO   A HG2  1 
ATOM   2865 H  HG2  B PRO   A 1 136 ? 9.718  -5.597  -3.679  0.50 16.31 ?  136  PRO   A HG2  1 
ATOM   2866 H  HG3  A PRO   A 1 136 ? 10.185 -4.549  -3.725  0.50 16.53 ?  136  PRO   A HG3  1 
ATOM   2867 H  HG3  B PRO   A 1 136 ? 10.282 -4.137  -3.368  0.50 16.31 ?  136  PRO   A HG3  1 
ATOM   2868 H  HD2  A PRO   A 1 136 ? 10.391 -5.724  -5.993  0.50 15.95 ?  136  PRO   A HD2  1 
ATOM   2869 H  HD2  B PRO   A 1 136 ? 10.514 -5.104  -5.685  0.50 15.49 ?  136  PRO   A HD2  1 
ATOM   2870 H  HD3  A PRO   A 1 136 ? 11.484 -4.644  -5.530  0.50 15.95 ?  136  PRO   A HD3  1 
ATOM   2871 H  HD3  B PRO   A 1 136 ? 11.711 -4.217  -5.084  0.50 15.49 ?  136  PRO   A HD3  1 
ATOM   2872 N  N    A ILE   A 1 137 ? 10.865 -8.924  -4.197  0.50 11.57 ?  137  ILE   A N    1 
ATOM   2873 N  N    B ILE   A 1 137 ? 10.801 -8.586  -3.947  0.50 12.49 ?  137  ILE   A N    1 
ATOM   2874 C  CA   A ILE   A 1 137 ? 10.493 -10.320 -3.982  0.50 11.85 ?  137  ILE   A CA   1 
ATOM   2875 C  CA   B ILE   A 1 137 ? 10.425 -9.990  -3.786  0.50 12.67 ?  137  ILE   A CA   1 
ATOM   2876 C  C    A ILE   A 1 137 ? 11.643 -11.238 -4.373  0.50 11.20 ?  137  ILE   A C    1 
ATOM   2877 C  C    B ILE   A 1 137 ? 11.597 -10.886 -4.159  0.50 11.91 ?  137  ILE   A C    1 
ATOM   2878 O  O    A ILE   A 1 137 ? 11.971 -12.194 -3.657  0.50 11.21 ?  137  ILE   A O    1 
ATOM   2879 O  O    B ILE   A 1 137 ? 11.912 -11.860 -3.462  0.50 12.14 ?  137  ILE   A O    1 
ATOM   2880 C  CB   A ILE   A 1 137 ? 9.189  -10.656 -4.730  0.50 13.67 ?  137  ILE   A CB   1 
ATOM   2881 C  CB   B ILE   A 1 137 ? 9.181  -10.312 -4.636  0.50 14.15 ?  137  ILE   A CB   1 
ATOM   2882 C  CG1  A ILE   A 1 137 ? 8.019  -9.870  -4.125  0.50 15.76 ?  137  ILE   A CG1  1 
ATOM   2883 C  CG1  B ILE   A 1 137 ? 7.995  -9.418  -4.262  0.50 16.14 ?  137  ILE   A CG1  1 
ATOM   2884 C  CG2  A ILE   A 1 137 ? 8.916  -12.157 -4.679  0.50 14.23 ?  137  ILE   A CG2  1 
ATOM   2885 C  CG2  B ILE   A 1 137 ? 8.800  -11.785 -4.498  0.50 14.48 ?  137  ILE   A CG2  1 
ATOM   2886 C  CD1  A ILE   A 1 137 ? 6.723  -9.973  -4.901  0.50 17.60 ?  137  ILE   A CD1  1 
ATOM   2887 C  CD1  B ILE   A 1 137 ? 6.751  -9.734  -5.067  0.50 17.99 ?  137  ILE   A CD1  1 
ATOM   2888 H  H    A ILE   A 1 137 ? 10.382 -8.506  -4.770  0.50 13.91 ?  137  ILE   A H    1 
ATOM   2889 H  H    B ILE   A 1 137 ? 10.315 -8.136  -4.499  0.50 15.02 ?  137  ILE   A H    1 
ATOM   2890 H  HA   A ILE   A 1 137 ? 10.329 -10.459 -3.040  0.50 14.24 ?  137  ILE   A HA   1 
ATOM   2891 H  HA   B ILE   A 1 137 ? 10.199 -10.147 -2.856  0.50 15.23 ?  137  ILE   A HA   1 
ATOM   2892 H  HB   A ILE   A 1 137 ? 9.286  -10.398 -5.658  0.50 16.43 ?  137  ILE   A HB   1 
ATOM   2893 H  HB   B ILE   A 1 137 ? 9.393  -10.139 -5.563  0.50 17.00 ?  137  ILE   A HB   1 
ATOM   2894 H  HG12 A ILE   A 1 137 ? 7.856  -10.200 -3.228  0.50 18.93 ?  137  ILE   A HG12 1 
ATOM   2895 H  HG12 B ILE   A 1 137 ? 7.784  -9.535  -3.323  0.50 19.39 ?  137  ILE   A HG12 1 
ATOM   2896 H  HG13 A ILE   A 1 137 ? 8.268  -8.932  -4.088  0.50 18.93 ?  137  ILE   A HG13 1 
ATOM   2897 H  HG13 B ILE   A 1 137 ? 8.227  -8.487  -4.434  0.50 19.39 ?  137  ILE   A HG13 1 
ATOM   2898 H  HG21 A ILE   A 1 137 ? 7.994  -12.330 -4.936  0.50 17.10 ?  137  ILE   A HG21 1 
ATOM   2899 H  HG21 B ILE   A 1 137 ? 8.667  -12.149 -5.387  0.50 17.40 ?  137  ILE   A HG21 1 
ATOM   2900 H  HG22 A ILE   A 1 137 ? 9.512  -12.609 -5.296  0.50 17.10 ?  137  ILE   A HG22 1 
ATOM   2901 H  HG22 B ILE   A 1 137 ? 9.502  -12.265 -4.043  0.50 17.40 ?  137  ILE   A HG22 1 
ATOM   2902 H  HG23 A ILE   A 1 137 ? 9.066  -12.475 -3.777  0.50 17.10 ?  137  ILE   A HG23 1 
ATOM   2903 H  HG23 B ILE   A 1 137 ? 7.980  -11.850 -3.987  0.50 17.40 ?  137  ILE   A HG23 1 
ATOM   2904 H  HD11 A ILE   A 1 137 ? 6.010  -10.214 -4.290  0.50 21.15 ?  137  ILE   A HD11 1 
ATOM   2905 H  HD11 B ILE   A 1 137 ? 5.984  -9.708  -4.476  0.50 21.62 ?  137  ILE   A HD11 1 
ATOM   2906 H  HD12 A ILE   A 1 137 ? 6.537  -9.113  -5.306  0.50 21.15 ?  137  ILE   A HD12 1 
ATOM   2907 H  HD12 B ILE   A 1 137 ? 6.661  -9.077  -5.769  0.50 21.62 ?  137  ILE   A HD12 1 
ATOM   2908 H  HD13 A ILE   A 1 137 ? 6.812  -10.647 -5.591  0.50 21.15 ?  137  ILE   A HD13 1 
ATOM   2909 H  HD13 B ILE   A 1 137 ? 6.823  -10.617 -5.462  0.50 21.62 ?  137  ILE   A HD13 1 
ATOM   2910 N  N    A HIS   A 1 138 ? 12.287 -10.950 -5.505  0.50 11.00 ?  138  HIS   A N    1 
ATOM   2911 N  N    B HIS   A 1 138 ? 12.254 -10.571 -5.276  0.50 11.75 ?  138  HIS   A N    1 
ATOM   2912 C  CA   A HIS   A 1 138 ? 13.451 -11.729 -5.907  0.50 11.86 ?  138  HIS   A CA   1 
ATOM   2913 C  CA   B HIS   A 1 138 ? 13.424 -11.332 -5.699  0.50 11.19 ?  138  HIS   A CA   1 
ATOM   2914 C  C    A HIS   A 1 138 ? 14.591 -11.575 -4.908  0.50 11.20 ?  138  HIS   A C    1 
ATOM   2915 C  C    B HIS   A 1 138 ? 14.567 -11.194 -4.697  0.50 10.63 ?  138  HIS   A C    1 
ATOM   2916 O  O    A HIS   A 1 138 ? 15.255 -12.558 -4.559  0.50 11.86 ?  138  HIS   A O    1 
ATOM   2917 O  O    B HIS   A 1 138 ? 15.240 -12.179 -4.369  0.50 10.74 ?  138  HIS   A O    1 
ATOM   2918 C  CB   A HIS   A 1 138 ? 13.897 -11.317 -7.307  0.50 12.52 ?  138  HIS   A CB   1 
ATOM   2919 C  CB   B HIS   A 1 138 ? 13.845 -10.868 -7.094  0.50 11.46 ?  138  HIS   A CB   1 
ATOM   2920 C  CG   A HIS   A 1 138 ? 15.179 -11.955 -7.736  0.50 13.23 ?  138  HIS   A CG   1 
ATOM   2921 C  CG   B HIS   A 1 138 ? 15.096 -11.516 -7.592  0.50 12.65 ?  138  HIS   A CG   1 
ATOM   2922 N  ND1  A HIS   A 1 138 ? 15.298 -13.311 -7.956  0.50 14.03 ?  138  HIS   A ND1  1 
ATOM   2923 N  ND1  B HIS   A 1 138 ? 15.164 -12.851 -7.927  0.50 13.86 ?  138  HIS   A ND1  1 
ATOM   2924 C  CD2  A HIS   A 1 138 ? 16.404 -11.427 -7.964  0.50 13.62 ?  138  HIS   A CD2  1 
ATOM   2925 C  CD2  B HIS   A 1 138 ? 16.334 -11.011 -7.802  0.50 12.92 ?  138  HIS   A CD2  1 
ATOM   2926 C  CE1  A HIS   A 1 138 ? 16.539 -13.588 -8.315  0.50 14.72 ?  138  HIS   A CE1  1 
ATOM   2927 C  CE1  B HIS   A 1 138 ? 16.390 -13.139 -8.327  0.50 13.87 ?  138  HIS   A CE1  1 
ATOM   2928 N  NE2  A HIS   A 1 138 ? 17.231 -12.463 -8.326  0.50 14.19 ?  138  HIS   A NE2  1 
ATOM   2929 N  NE2  B HIS   A 1 138 ? 17.120 -12.040 -8.260  0.50 13.48 ?  138  HIS   A NE2  1 
ATOM   2930 H  H    A HIS   A 1 138 ? 12.080 -10.312 -6.046  0.50 13.22 ?  138  HIS   A H    1 
ATOM   2931 H  H    B HIS   A 1 138 ? 12.037 -9.921  -5.802  0.50 14.12 ?  138  HIS   A H    1 
ATOM   2932 H  HA   A HIS   A 1 138 ? 13.207 -12.665 -5.940  0.50 14.25 ?  138  HIS   A HA   1 
ATOM   2933 H  HA   B HIS   A 1 138 ? 13.181 -12.265 -5.757  0.50 13.45 ?  138  HIS   A HA   1 
ATOM   2934 H  HB2  A HIS   A 1 138 ? 13.209 -11.576 -7.944  0.50 15.04 ?  138  HIS   A HB2  1 
ATOM   2935 H  HB2  B HIS   A 1 138 ? 13.131 -11.078 -7.723  0.50 13.78 ?  138  HIS   A HB2  1 
ATOM   2936 H  HB3  A HIS   A 1 138 ? 14.020 -10.356 -7.330  0.50 15.04 ?  138  HIS   A HB3  1 
ATOM   2937 H  HB3  B HIS   A 1 138 ? 13.990 -9.909  -7.079  0.50 13.78 ?  138  HIS   A HB3  1 
ATOM   2938 H  HD1  A HIS   A 1 138 ? 14.660 -13.884 -7.881  0.50 16.86 ?  138  HIS   A HD1  1 
ATOM   2939 H  HD1  B HIS   A 1 138 ? 14.507 -13.406 -7.884  0.50 16.65 ?  138  HIS   A HD1  1 
ATOM   2940 H  HD2  A HIS   A 1 138 ? 16.638 -10.529 -7.892  0.50 16.37 ?  138  HIS   A HD2  1 
ATOM   2941 H  HD2  B HIS   A 1 138 ? 16.601 -10.132 -7.663  0.50 15.52 ?  138  HIS   A HD2  1 
ATOM   2942 H  HE1  A HIS   A 1 138 ? 16.867 -14.430 -8.521  0.50 17.69 ?  138  HIS   A HE1  1 
ATOM   2943 H  HE1  B HIS   A 1 138 ? 16.685 -13.977 -8.605  0.50 16.67 ?  138  HIS   A HE1  1 
ATOM   2944 N  N    A SER   A 1 139 ? 14.839 -10.349 -4.441  0.50 10.24 ?  139  SER   A N    1 
ATOM   2945 N  N    B SER   A 1 139 ? 14.796 -9.978  -4.196  0.50 10.44 ?  139  SER   A N    1 
ATOM   2946 C  CA   A SER   A 1 139 ? 15.918 -10.140 -3.482  0.50 10.08 ?  139  SER   A CA   1 
ATOM   2947 C  CA   B SER   A 1 139 ? 15.861 -9.767  -3.222  0.50 9.98  ?  139  SER   A CA   1 
ATOM   2948 C  C    A SER   A 1 139 ? 15.701 -10.956 -2.214  0.50 9.89  ?  139  SER   A C    1 
ATOM   2949 C  C    B SER   A 1 139 ? 15.645 -10.612 -1.970  0.50 9.84  ?  139  SER   A C    1 
ATOM   2950 O  O    A SER   A 1 139 ? 16.650 -11.535 -1.671  0.50 9.57  ?  139  SER   A O    1 
ATOM   2951 O  O    B SER   A 1 139 ? 16.594 -11.201 -1.435  0.50 10.31 ?  139  SER   A O    1 
ATOM   2952 C  CB   A SER   A 1 139 ? 16.061 -8.655  -3.151  0.50 9.44  ?  139  SER   A CB   1 
ATOM   2953 C  CB   B SER   A 1 139 ? 15.956 -8.280  -2.873  0.50 10.50 ?  139  SER   A CB   1 
ATOM   2954 O  OG   A SER   A 1 139 ? 17.155 -8.452  -2.269  0.50 8.79  ?  139  SER   A OG   1 
ATOM   2955 O  OG   B SER   A 1 139 ? 16.984 -8.047  -1.925  0.50 10.47 ?  139  SER   A OG   1 
ATOM   2956 H  H    A SER   A 1 139 ? 14.410 -9.641  -4.661  0.50 12.31 ?  139  SER   A H    1 
ATOM   2957 H  H    B SER   A 1 139 ? 14.355 -9.267  -4.400  0.50 12.56 ?  139  SER   A H    1 
ATOM   2958 H  HA   A SER   A 1 139 ? 16.754 -10.431 -3.881  0.50 12.12 ?  139  SER   A HA   1 
ATOM   2959 H  HA   B SER   A 1 139 ? 16.705 -10.034 -3.617  0.50 12.00 ?  139  SER   A HA   1 
ATOM   2960 H  HB2  A SER   A 1 139 ? 16.220 -8.158  -3.970  0.50 11.35 ?  139  SER   A HB2  1 
ATOM   2961 H  HB2  B SER   A 1 139 ? 16.149 -7.777  -3.685  0.50 12.62 ?  139  SER   A HB2  1 
ATOM   2962 H  HB3  A SER   A 1 139 ? 15.249 -8.343  -2.725  0.50 11.35 ?  139  SER   A HB3  1 
ATOM   2963 H  HB3  B SER   A 1 139 ? 15.114 -7.986  -2.498  0.50 12.62 ?  139  SER   A HB3  1 
ATOM   2964 H  HG   A SER   A 1 139 ? 17.234 -7.633  -2.087  0.50 10.57 ?  139  SER   A HG   1 
ATOM   2965 H  HG   B SER   A 1 139 ? 17.032 -7.216  -1.754  0.50 12.59 ?  139  SER   A HG   1 
ATOM   2966 N  N    A LEU   A 1 140 ? 14.459 -11.026 -1.730  0.50 9.95  ?  140  LEU   A N    1 
ATOM   2967 N  N    B LEU   A 1 140 ? 14.404 -10.678 -1.484  0.50 9.45  ?  140  LEU   A N    1 
ATOM   2968 C  CA   A LEU   A 1 140 ? 14.186 -11.848 -0.555  0.50 10.00 ?  140  LEU   A CA   1 
ATOM   2969 C  CA   B LEU   A 1 140 ? 14.119 -11.494 -0.307  0.50 9.25  ?  140  LEU   A CA   1 
ATOM   2970 C  C    A LEU   A 1 140 ? 14.458 -13.317 -0.848  0.50 10.10 ?  140  LEU   A C    1 
ATOM   2971 C  C    B LEU   A 1 140 ? 14.394 -12.972 -0.574  0.50 9.69  ?  140  LEU   A C    1 
ATOM   2972 O  O    A LEU   A 1 140 ? 15.036 -14.030 -0.019  0.50 10.31 ?  140  LEU   A O    1 
ATOM   2973 O  O    B LEU   A 1 140 ? 14.936 -13.677 0.288   0.50 10.19 ?  140  LEU   A O    1 
ATOM   2974 C  CB   A LEU   A 1 140 ? 12.744 -11.647 -0.090  0.50 10.38 ?  140  LEU   A CB   1 
ATOM   2975 C  CB   B LEU   A 1 140 ? 12.671 -11.272 0.133   0.50 9.68  ?  140  LEU   A CB   1 
ATOM   2976 C  CG   A LEU   A 1 140 ? 12.308 -12.533 1.082   0.50 10.26 ?  140  LEU   A CG   1 
ATOM   2977 C  CG   B LEU   A 1 140 ? 12.183 -12.107 1.317   0.50 10.05 ?  140  LEU   A CG   1 
ATOM   2978 C  CD1  A LEU   A 1 140 ? 13.201 -12.334 2.294   0.50 10.78 ?  140  LEU   A CD1  1 
ATOM   2979 C  CD1  B LEU   A 1 140 ? 13.061 -11.903 2.540   0.50 10.02 ?  140  LEU   A CD1  1 
ATOM   2980 C  CD2  A LEU   A 1 140 ? 10.853 -12.260 1.445   0.50 10.73 ?  140  LEU   A CD2  1 
ATOM   2981 C  CD2  B LEU   A 1 140 ? 10.731 -11.769 1.631   0.50 10.80 ?  140  LEU   A CD2  1 
ATOM   2982 H  H    A LEU   A 1 140 ? 13.774 -10.623 -2.058  0.50 11.96 ?  140  LEU   A H    1 
ATOM   2983 H  H    B LEU   A 1 140 ? 13.723 -10.259 -1.810  0.50 11.36 ?  140  LEU   A H    1 
ATOM   2984 H  HA   A LEU   A 1 140 ? 14.771 -11.574 0.163   0.50 12.02 ?  140  LEU   A HA   1 
ATOM   2985 H  HA   B LEU   A 1 140 ? 14.693 -11.203 0.418   0.50 11.13 ?  140  LEU   A HA   1 
ATOM   2986 H  HB2  A LEU   A 1 140 ? 12.634 -10.726 0.189   0.50 12.48 ?  140  LEU   A HB2  1 
ATOM   2987 H  HB2  B LEU   A 1 140 ? 12.562 -10.338 0.379   0.50 11.63 ?  140  LEU   A HB2  1 
ATOM   2988 H  HB3  A LEU   A 1 140 ? 12.147 -11.835 -0.832  0.50 12.48 ?  140  LEU   A HB3  1 
ATOM   2989 H  HB3  B LEU   A 1 140 ? 12.089 -11.472 -0.617  0.50 11.63 ?  140  LEU   A HB3  1 
ATOM   2990 H  HG   A LEU   A 1 140 ? 12.367 -13.465 0.817   0.50 12.34 ?  140  LEU   A HG   1 
ATOM   2991 H  HG   B LEU   A 1 140 ? 12.217 -13.044 1.076   0.50 12.08 ?  140  LEU   A HG   1 
ATOM   2992 H  HD11 A LEU   A 1 140 ? 12.828 -12.823 3.044   0.50 12.96 ?  140  LEU   A HD11 1 
ATOM   2993 H  HD11 B LEU   A 1 140 ? 12.667 -12.373 3.291   0.50 12.05 ?  140  LEU   A HD11 1 
ATOM   2994 H  HD12 A LEU   A 1 140 ? 14.087 -12.668 2.088   0.50 12.96 ?  140  LEU   A HD12 1 
ATOM   2995 H  HD12 B LEU   A 1 140 ? 13.943 -12.259 2.353   0.50 12.05 ?  140  LEU   A HD12 1 
ATOM   2996 H  HD13 A LEU   A 1 140 ? 13.241 -11.388 2.502   0.50 12.96 ?  140  LEU   A HD13 1 
ATOM   2997 H  HD13 B LEU   A 1 140 ? 13.117 -10.956 2.733   0.50 12.05 ?  140  LEU   A HD13 1 
ATOM   2998 H  HD21 A LEU   A 1 140 ? 10.596 -12.833 2.188   0.50 12.90 ?  140  LEU   A HD21 1 
ATOM   2999 H  HD21 B LEU   A 1 140 ? 10.429 -12.325 2.367   0.50 12.99 ?  140  LEU   A HD21 1 
ATOM   3000 H  HD22 A LEU   A 1 140 ? 10.758 -11.329 1.702   0.50 12.90 ?  140  LEU   A HD22 1 
ATOM   3001 H  HD22 B LEU   A 1 140 ? 10.668 -10.833 1.875   0.50 12.99 ?  140  LEU   A HD22 1 
ATOM   3002 H  HD23 A LEU   A 1 140 ? 10.290 -12.449 0.677   0.50 12.90 ?  140  LEU   A HD23 1 
ATOM   3003 H  HD23 B LEU   A 1 140 ? 10.188 -11.943 0.844   0.50 12.99 ?  140  LEU   A HD23 1 
ATOM   3004 N  N    A ARG   A 1 141 ? 14.043 -13.787 -2.024  0.50 10.76 ?  141  ARG   A N    1 
ATOM   3005 N  N    B ARG   A 1 141 ? 14.027 -13.463 -1.763  0.50 10.29 ?  141  ARG   A N    1 
ATOM   3006 C  CA   A ARG   A 1 141 ? 14.320 -15.160 -2.427  0.50 12.04 ?  141  ARG   A CA   1 
ATOM   3007 C  CA   B ARG   A 1 141 ? 14.249 -14.874 -2.067  0.50 10.68 ?  141  ARG   A CA   1 
ATOM   3008 C  C    A ARG   A 1 141 ? 15.816 -15.439 -2.387  0.50 11.58 ?  141  ARG   A C    1 
ATOM   3009 C  C    B ARG   A 1 141 ? 15.739 -15.191 -2.150  0.50 10.59 ?  141  ARG   A C    1 
ATOM   3010 O  O    A ARG   A 1 141 ? 16.258 -16.462 -1.852  0.50 11.31 ?  141  ARG   A O    1 
ATOM   3011 O  O    B ARG   A 1 141 ? 16.204 -16.188 -1.584  0.50 10.99 ?  141  ARG   A O    1 
ATOM   3012 C  CB   A ARG   A 1 141 ? 13.765 -15.380 -3.837  0.50 13.74 ?  141  ARG   A CB   1 
ATOM   3013 C  CB   B ARG   A 1 141 ? 13.530 -15.274 -3.358  0.50 11.53 ?  141  ARG   A CB   1 
ATOM   3014 C  CG   A ARG   A 1 141 ? 13.617 -16.827 -4.259  0.50 15.72 ?  141  ARG   A CG   1 
ATOM   3015 C  CG   B ARG   A 1 141 ? 13.721 -16.760 -3.739  0.50 13.26 ?  141  ARG   A CG   1 
ATOM   3016 C  CD   A ARG   A 1 141 ? 12.592 -17.518 -3.402  0.50 16.44 ?  141  ARG   A CD   1 
ATOM   3017 C  CD   B ARG   A 1 141 ? 13.146 -17.734 -2.701  0.50 14.48 ?  141  ARG   A CD   1 
ATOM   3018 N  NE   A ARG   A 1 141 ? 13.219 -18.292 -2.342  0.50 17.01 ?  141  ARG   A NE   1 
ATOM   3019 N  NE   B ARG   A 1 141 ? 11.712 -17.537 -2.529  0.50 15.35 ?  141  ARG   A NE   1 
ATOM   3020 C  CZ   A ARG   A 1 141 ? 12.559 -18.845 -1.334  0.50 17.46 ?  141  ARG   A CZ   1 
ATOM   3021 C  CZ   B ARG   A 1 141 ? 10.970 -18.122 -1.599  0.50 15.50 ?  141  ARG   A CZ   1 
ATOM   3022 N  NH1  A ARG   A 1 141 ? 11.263 -18.641 -1.161  0.50 17.87 ?  141  ARG   A NH1  1 
ATOM   3023 N  NH1  B ARG   A 1 141 ? 11.485 -18.988 -0.740  0.50 15.80 ?  141  ARG   A NH1  1 
ATOM   3024 N  NH2  A ARG   A 1 141 ? 13.215 -19.623 -0.479  0.50 17.95 ?  141  ARG   A NH2  1 
ATOM   3025 N  NH2  B ARG   A 1 141 ? 9.675  -17.826 -1.527  0.50 16.15 ?  141  ARG   A NH2  1 
ATOM   3026 H  H    A ARG   A 1 141 ? 13.605 -13.338 -2.604  0.50 12.94 ?  141  ARG   A H    1 
ATOM   3027 H  H    B ARG   A 1 141 ? 13.646 -13.001 -2.391  0.50 12.37 ?  141  ARG   A H    1 
ATOM   3028 H  HA   A ARG   A 1 141 ? 13.886 -15.779 -1.820  0.50 14.47 ?  141  ARG   A HA   1 
ATOM   3029 H  HA   B ARG   A 1 141 ? 13.876 -15.395 -1.349  0.50 12.84 ?  141  ARG   A HA   1 
ATOM   3030 H  HB2  A ARG   A 1 141 ? 12.887 -14.975 -3.887  0.50 16.51 ?  141  ARG   A HB2  1 
ATOM   3031 H  HB2  B ARG   A 1 141 ? 12.574 -15.114 -3.246  0.50 13.86 ?  141  ARG   A HB2  1 
ATOM   3032 H  HB3  A ARG   A 1 141 ? 14.357 -14.957 -4.474  0.50 16.51 ?  141  ARG   A HB3  1 
ATOM   3033 H  HB3  B ARG   A 1 141 ? 13.863 -14.729 -4.089  0.50 13.86 ?  141  ARG   A HB3  1 
ATOM   3034 H  HG2  A ARG   A 1 141 ? 13.323 -16.869 -5.184  0.50 18.89 ?  141  ARG   A HG2  1 
ATOM   3035 H  HG2  B ARG   A 1 141 ? 13.273 -16.928 -4.582  0.50 15.94 ?  141  ARG   A HG2  1 
ATOM   3036 H  HG3  A ARG   A 1 141 ? 14.466 -17.287 -4.155  0.50 18.89 ?  141  ARG   A HG3  1 
ATOM   3037 H  HG3  B ARG   A 1 141 ? 14.669 -16.946 -3.830  0.50 15.94 ?  141  ARG   A HG3  1 
ATOM   3038 H  HD2  A ARG   A 1 141 ? 12.020 -16.853 -2.989  0.50 19.75 ?  141  ARG   A HD2  1 
ATOM   3039 H  HD2  B ARG   A 1 141 ? 13.292 -18.643 -3.000  0.50 17.40 ?  141  ARG   A HD2  1 
ATOM   3040 H  HD3  A ARG   A 1 141 ? 12.063 -18.117 -3.954  0.50 19.75 ?  141  ARG   A HD3  1 
ATOM   3041 H  HD3  B ARG   A 1 141 ? 13.579 -17.586 -1.846  0.50 17.40 ?  141  ARG   A HD3  1 
ATOM   3042 H  HE   A ARG   A 1 141 ? 14.063 -18.447 -2.405  0.50 20.43 ?  141  ARG   A HE   1 
ATOM   3043 H  HE   B ARG   A 1 141 ? 11.317 -16.997 -3.071  0.50 18.44 ?  141  ARG   A HE   1 
ATOM   3044 H  HH11 A ARG   A 1 141 ? 10.825 -18.152 -1.714  0.50 21.47 ?  141  ARG   A HH11 1 
ATOM   3045 H  HH11 B ARG   A 1 141 ? 12.319 -19.189 -0.778  0.50 18.98 ?  141  ARG   A HH11 1 
ATOM   3046 H  HH12 A ARG   A 1 141 ? 10.857 -19.012 -0.500  0.50 21.47 ?  141  ARG   A HH12 1 
ATOM   3047 H  HH12 B ARG   A 1 141 ? 10.980 -19.359 -0.150  0.50 18.98 ?  141  ARG   A HH12 1 
ATOM   3048 H  HH21 A ARG   A 1 141 ? 14.060 -19.759 -0.581  0.50 21.56 ?  141  ARG   A HH21 1 
ATOM   3049 H  HH21 B ARG   A 1 141 ? 9.329  -17.265 -2.080  0.50 19.41 ?  141  ARG   A HH21 1 
ATOM   3050 H  HH22 A ARG   A 1 141 ? 12.801 -19.980 0.184   0.50 21.56 ?  141  ARG   A HH22 1 
ATOM   3051 H  HH22 B ARG   A 1 141 ? 9.179  -18.203 -0.932  0.50 19.41 ?  141  ARG   A HH22 1 
ATOM   3052 N  N    A VAL   A 1 142 ? 16.615 -14.530 -2.945  0.50 11.21 ?  142  VAL   A N    1 
ATOM   3053 N  N    B VAL   A 1 142 ? 16.507 -14.355 -2.859  0.50 10.99 ?  142  VAL   A N    1 
ATOM   3054 C  CA   A VAL   A 1 142 ? 18.062 -14.714 -2.926  0.50 11.22 ?  142  VAL   A CA   1 
ATOM   3055 C  CA   B VAL   A 1 142 ? 17.949 -14.581 -2.946  0.50 11.20 ?  142  VAL   A CA   1 
ATOM   3056 C  C    A VAL   A 1 142 ? 18.598 -14.646 -1.501  0.50 11.01 ?  142  VAL   A C    1 
ATOM   3057 C  C    B VAL   A 1 142 ? 18.560 -14.608 -1.552  0.50 11.00 ?  142  VAL   A C    1 
ATOM   3058 O  O    A VAL   A 1 142 ? 19.455 -15.451 -1.115  0.50 11.42 ?  142  VAL   A O    1 
ATOM   3059 O  O    B VAL   A 1 142 ? 19.428 -15.437 -1.247  0.50 11.45 ?  142  VAL   A O    1 
ATOM   3060 C  CB   A VAL   A 1 142 ? 18.765 -13.724 -3.875  0.50 11.20 ?  142  VAL   A CB   1 
ATOM   3061 C  CB   B VAL   A 1 142 ? 18.617 -13.523 -3.848  0.50 11.68 ?  142  VAL   A CB   1 
ATOM   3062 C  CG1  A VAL   A 1 142 ? 20.270 -13.959 -3.864  0.50 10.58 ?  142  VAL   A CG1  1 
ATOM   3063 C  CG1  B VAL   A 1 142 ? 20.132 -13.672 -3.810  0.50 11.79 ?  142  VAL   A CG1  1 
ATOM   3064 C  CG2  A VAL   A 1 142 ? 18.228 -13.868 -5.292  0.50 12.13 ?  142  VAL   A CG2  1 
ATOM   3065 C  CG2  B VAL   A 1 142 ? 18.124 -13.648 -5.278  0.50 12.33 ?  142  VAL   A CG2  1 
ATOM   3066 H  H    A VAL   A 1 142 ? 16.352 -13.812 -3.334  0.50 13.48 ?  142  VAL   A H    1 
ATOM   3067 H  H    B VAL   A 1 142 ? 16.227 -13.650 -3.282  0.50 13.21 ?  142  VAL   A H    1 
ATOM   3068 H  HA   A VAL   A 1 142 ? 18.263 -15.600 -3.256  0.50 13.48 ?  142  VAL   A HA   1 
ATOM   3069 H  HA   B VAL   A 1 142 ? 18.101 -15.440 -3.353  0.50 13.46 ?  142  VAL   A HA   1 
ATOM   3070 H  HB   A VAL   A 1 142 ? 18.605 -12.814 -3.578  0.50 13.47 ?  142  VAL   A HB   1 
ATOM   3071 H  HB   B VAL   A 1 142 ? 18.395 -12.630 -3.529  0.50 14.04 ?  142  VAL   A HB   1 
ATOM   3072 H  HG11 A VAL   A 1 142 ? 20.675 -13.458 -4.589  0.50 12.71 ?  142  VAL   A HG11 1 
ATOM   3073 H  HG11 B VAL   A 1 142 ? 20.519 -13.132 -4.518  0.50 14.17 ?  142  VAL   A HG11 1 
ATOM   3074 H  HG12 A VAL   A 1 142 ? 20.633 -13.662 -3.015  0.50 12.71 ?  142  VAL   A HG12 1 
ATOM   3075 H  HG12 B VAL   A 1 142 ? 20.461 -13.367 -2.949  0.50 14.17 ?  142  VAL   A HG12 1 
ATOM   3076 H  HG13 A VAL   A 1 142 ? 20.441 -14.907 -3.984  0.50 12.71 ?  142  VAL   A HG13 1 
ATOM   3077 H  HG13 B VAL   A 1 142 ? 20.357 -14.603 -3.942  0.50 14.17 ?  142  VAL   A HG13 1 
ATOM   3078 H  HG21 A VAL   A 1 142 ? 18.712 -13.264 -5.878  0.50 14.57 ?  142  VAL   A HG21 1 
ATOM   3079 H  HG21 B VAL   A 1 142 ? 18.565 -12.978 -5.825  0.50 14.82 ?  142  VAL   A HG21 1 
ATOM   3080 H  HG22 A VAL   A 1 142 ? 18.354 -14.783 -5.585  0.50 14.57 ?  142  VAL   A HG22 1 
ATOM   3081 H  HG22 B VAL   A 1 142 ? 18.341 -14.536 -5.604  0.50 14.82 ?  142  VAL   A HG22 1 
ATOM   3082 H  HG23 A VAL   A 1 142 ? 17.286 -13.645 -5.295  0.50 14.57 ?  142  VAL   A HG23 1 
ATOM   3083 H  HG23 B VAL   A 1 142 ? 17.167 -13.512 -5.293  0.50 14.82 ?  142  VAL   A HG23 1 
ATOM   3084 N  N    . CYS   A 1 143 ? 18.113 -13.700 -0.689  1.00 11.00 ?  143  CYS   A N    1 
ATOM   3085 C  CA   . CYS   A 1 143 ? 18.572 -13.654 0.693   1.00 11.31 ?  143  CYS   A CA   1 
ATOM   3086 C  C    . CYS   A 1 143 ? 18.342 -14.993 1.383   1.00 11.24 ?  143  CYS   A C    1 
ATOM   3087 O  O    . CYS   A 1 143 ? 19.258 -15.580 1.966   1.00 11.07 ?  143  CYS   A O    1 
ATOM   3088 C  CB   . CYS   A 1 143 ? 17.835 -12.544 1.435   1.00 11.62 ?  143  CYS   A CB   1 
ATOM   3089 S  SG   . CYS   A 1 143 ? 18.348 -12.363 3.150   1.00 11.82 ?  143  CYS   A SG   1 
ATOM   3090 H  H    A CYS   A 1 143 ? 17.538 -13.098 -0.906  0.50 13.22 ?  143  CYS   A H    1 
ATOM   3091 H  H    B CYS   A 1 143 ? 17.535 -13.093 -0.882  0.50 13.22 ?  143  CYS   A H    1 
ATOM   3092 H  HA   . CYS   A 1 143 ? 19.519 -13.464 0.715   1.00 13.60 ?  143  CYS   A HA   1 
ATOM   3093 H  HB2  . CYS   A 1 143 ? 17.994 -11.704 0.981   1.00 13.96 ?  143  CYS   A HB2  1 
ATOM   3094 H  HB3  . CYS   A 1 143 ? 16.886 -12.742 1.435   1.00 13.96 ?  143  CYS   A HB3  1 
ATOM   3095 H  HG   . CYS   A 1 143 ? 17.738 -11.448 3.631   1.00 14.21 ?  143  CYS   A HG   1 
ATOM   3096 N  N    . VAL   A 1 144 ? 17.115 -15.498 1.313   1.00 11.81 ?  144  VAL   A N    1 
ATOM   3097 C  CA   . VAL   A 1 144 ? 16.770 -16.731 2.008   1.00 12.61 ?  144  VAL   A CA   1 
ATOM   3098 C  C    . VAL   A 1 144 ? 17.592 -17.902 1.489   1.00 12.26 ?  144  VAL   A C    1 
ATOM   3099 O  O    . VAL   A 1 144 ? 17.958 -18.809 2.249   1.00 13.10 ?  144  VAL   A O    1 
ATOM   3100 C  CB   . VAL   A 1 144 ? 15.257 -16.967 1.862   1.00 15.05 ?  144  VAL   A CB   1 
ATOM   3101 C  CG1  . VAL   A 1 144 ? 14.890 -18.397 2.188   1.00 16.70 ?  144  VAL   A CG1  1 
ATOM   3102 C  CG2  . VAL   A 1 144 ? 14.495 -15.973 2.744   1.00 15.35 ?  144  VAL   A CG2  1 
ATOM   3103 H  H    . VAL   A 1 144 ? 16.464 -15.150 0.864   1.00 14.19 ?  144  VAL   A H    1 
ATOM   3104 H  HA   . VAL   A 1 144 ? 16.955 -16.624 2.949   1.00 15.15 ?  144  VAL   A HA   1 
ATOM   3105 H  HB   . VAL   A 1 144 ? 14.993 -16.795 0.938   1.00 18.09 ?  144  VAL   A HB   1 
ATOM   3106 H  HG11 . VAL   A 1 144 ? 13.932 -18.448 2.362   1.00 20.06 ?  144  VAL   A HG11 1 
ATOM   3107 H  HG12 . VAL   A 1 144 ? 15.113 -18.966 1.436   1.00 20.06 ?  144  VAL   A HG12 1 
ATOM   3108 H  HG13 . VAL   A 1 144 ? 15.377 -18.675 2.978   1.00 20.06 ?  144  VAL   A HG13 1 
ATOM   3109 H  HG21 . VAL   A 1 144 ? 13.538 -16.128 2.656   1.00 18.45 ?  144  VAL   A HG21 1 
ATOM   3110 H  HG22 . VAL   A 1 144 ? 14.763 -16.093 3.666   1.00 18.45 ?  144  VAL   A HG22 1 
ATOM   3111 H  HG23 . VAL   A 1 144 ? 14.701 -15.065 2.457   1.00 18.45 ?  144  VAL   A HG23 1 
ATOM   3112 N  N    . ASP   A 1 145 ? 17.861 -17.921 0.186   1.00 12.35 ?  145  ASP   A N    1 
ATOM   3113 C  CA   . ASP   A 1 145 ? 18.571 -19.027 -0.443  1.00 13.26 ?  145  ASP   A CA   1 
ATOM   3114 C  C    . ASP   A 1 145 ? 20.088 -18.880 -0.400  1.00 12.99 ?  145  ASP   A C    1 
ATOM   3115 O  O    . ASP   A 1 145 ? 20.791 -19.770 -0.892  1.00 15.08 ?  145  ASP   A O    1 
ATOM   3116 C  CB   . ASP   A 1 145 ? 18.123 -19.168 -1.900  1.00 14.54 ?  145  ASP   A CB   1 
ATOM   3117 C  CG   . ASP   A 1 145 ? 16.680 -19.627 -2.033  1.00 16.83 ?  145  ASP   A CG   1 
ATOM   3118 O  OD1  . ASP   A 1 145 ? 16.116 -20.177 -1.060  1.00 17.36 ?  145  ASP   A OD1  1 
ATOM   3119 O  OD2  . ASP   A 1 145 ? 16.115 -19.430 -3.126  1.00 18.29 -1 145  ASP   A OD2  1 
ATOM   3120 H  H    . ASP   A 1 145 ? 17.624 -17.301 -0.366  1.00 14.85 ?  145  ASP   A H    1 
ATOM   3121 H  HA   . ASP   A 1 145 ? 18.336 -19.846 0.016   1.00 15.94 ?  145  ASP   A HA   1 
ATOM   3122 H  HB2  . ASP   A 1 145 ? 18.217 -18.308 -2.343  1.00 17.47 ?  145  ASP   A HB2  1 
ATOM   3123 H  HB3  . ASP   A 1 145 ? 18.684 -19.827 -2.337  1.00 17.47 ?  145  ASP   A HB3  1 
ATOM   3124 N  N    . THR   A 1 146 ? 20.610 -17.791 0.161   1.00 11.59 ?  146  THR   A N    1 
ATOM   3125 C  CA   . THR   A 1 146 ? 22.051 -17.541 0.180   1.00 11.10 ?  146  THR   A CA   1 
ATOM   3126 C  C    . THR   A 1 146 ? 22.610 -17.352 1.578   1.00 11.09 ?  146  THR   A C    1 
ATOM   3127 O  O    . THR   A 1 146 ? 23.689 -17.879 1.890   1.00 12.06 ?  146  THR   A O    1 
ATOM   3128 C  CB   . THR   A 1 146 ? 22.367 -16.289 -0.658  1.00 11.23 ?  146  THR   A CB   1 
ATOM   3129 O  OG1  . THR   A 1 146 ? 21.842 -16.457 -1.974  1.00 11.69 ?  146  THR   A OG1  1 
ATOM   3130 C  CG2  . THR   A 1 146 ? 23.868 -16.054 -0.755  1.00 11.79 ?  146  THR   A CG2  1 
ATOM   3131 H  H    . THR   A 1 146 ? 20.145 -17.170 0.537   1.00 13.93 ?  146  THR   A H    1 
ATOM   3132 H  HA   . THR   A 1 146 ? 22.510 -18.289 -0.223  1.00 13.35 ?  146  THR   A HA   1 
ATOM   3133 H  HB   . THR   A 1 146 ? 21.968 -15.509 -0.243  1.00 13.50 ?  146  THR   A HB   1 
ATOM   3134 H  HG1  . THR   A 1 146 ? 21.005 -16.533 -1.937  1.00 14.05 ?  146  THR   A HG1  1 
ATOM   3135 H  HG21 . THR   A 1 146 ? 24.052 -15.388 -1.432  1.00 14.18 ?  146  THR   A HG21 1 
ATOM   3136 H  HG22 . THR   A 1 146 ? 24.212 -15.744 0.097   1.00 14.18 ?  146  THR   A HG22 1 
ATOM   3137 H  HG23 . THR   A 1 146 ? 24.314 -16.882 -0.995  1.00 14.18 ?  146  THR   A HG23 1 
ATOM   3138 N  N    . VAL   A 1 147 ? 21.929 -16.575 2.412   1.00 10.82 ?  147  VAL   A N    1 
ATOM   3139 C  CA   . VAL   A 1 147 ? 22.416 -16.280 3.750   1.00 11.15 ?  147  VAL   A CA   1 
ATOM   3140 C  C    . VAL   A 1 147 ? 22.091 -17.453 4.662   1.00 11.59 ?  147  VAL   A C    1 
ATOM   3141 O  O    . VAL   A 1 147 ? 20.949 -17.929 4.700   1.00 12.20 ?  147  VAL   A O    1 
ATOM   3142 C  CB   . VAL   A 1 147 ? 21.793 -14.974 4.270   1.00 11.07 ?  147  VAL   A CB   1 
ATOM   3143 C  CG1  . VAL   A 1 147 ? 22.319 -14.663 5.648   1.00 12.20 ?  147  VAL   A CG1  1 
ATOM   3144 C  CG2  . VAL   A 1 147 ? 22.056 -13.824 3.306   1.00 11.39 ?  147  VAL   A CG2  1 
ATOM   3145 H  H    . VAL   A 1 147 ? 21.172 -16.208 2.228   1.00 13.01 ?  147  VAL   A H    1 
ATOM   3146 H  HA   . VAL   A 1 147 ? 23.377 -16.169 3.725   1.00 13.40 ?  147  VAL   A HA   1 
ATOM   3147 H  HB   . VAL   A 1 147 ? 20.834 -15.089 4.342   1.00 13.30 ?  147  VAL   A HB   1 
ATOM   3148 H  HG11 . VAL   A 1 147 ? 22.071 -13.758 5.885   1.00 14.66 ?  147  VAL   A HG11 1 
ATOM   3149 H  HG12 . VAL   A 1 147 ? 21.934 -15.289 6.284   1.00 14.66 ?  147  VAL   A HG12 1 
ATOM   3150 H  HG13 . VAL   A 1 147 ? 23.286 -14.751 5.644   1.00 14.66 ?  147  VAL   A HG13 1 
ATOM   3151 H  HG21 . VAL   A 1 147 ? 21.720 -13.001 3.700   1.00 13.69 ?  147  VAL   A HG21 1 
ATOM   3152 H  HG22 . VAL   A 1 147 ? 23.006 -13.754 3.149   1.00 13.69 ?  147  VAL   A HG22 1 
ATOM   3153 H  HG23 . VAL   A 1 147 ? 21.591 -14.002 2.472   1.00 13.69 ?  147  VAL   A HG23 1 
ATOM   3154 N  N    . ARG   A 1 148 ? 23.108 -17.920 5.389   1.00 11.74 ?  148  ARG   A N    1 
ATOM   3155 C  CA   . ARG   A 1 148 ? 22.975 -18.998 6.352   1.00 12.03 ?  148  ARG   A CA   1 
ATOM   3156 C  C    . ARG   A 1 148 ? 23.099 -18.526 7.788   1.00 12.06 ?  148  ARG   A C    1 
ATOM   3157 O  O    . ARG   A 1 148 ? 22.687 -19.252 8.702   1.00 13.49 ?  148  ARG   A O    1 
ATOM   3158 C  CB   . ARG   A 1 148 ? 24.017 -20.091 6.077   1.00 12.61 ?  148  ARG   A CB   1 
ATOM   3159 C  CG   . ARG   A 1 148 ? 23.859 -20.738 4.719   1.00 13.73 ?  148  ARG   A CG   1 
ATOM   3160 C  CD   . ARG   A 1 148 ? 24.946 -21.762 4.434   1.00 14.72 ?  148  ARG   A CD   1 
ATOM   3161 N  NE   . ARG   A 1 148 ? 26.282 -21.178 4.463   1.00 14.63 ?  148  ARG   A NE   1 
ATOM   3162 C  CZ   . ARG   A 1 148 ? 26.799 -20.450 3.483   1.00 14.00 ?  148  ARG   A CZ   1 
ATOM   3163 N  NH1  . ARG   A 1 148 ? 26.123 -20.207 2.373   1.00 14.36 ?  148  ARG   A NH1  1 
ATOM   3164 N  NH2  . ARG   A 1 148 ? 28.018 -19.930 3.630   1.00 14.23 ?  148  ARG   A NH2  1 
ATOM   3165 H  H    . ARG   A 1 148 ? 23.912 -17.609 5.325   1.00 14.11 ?  148  ARG   A H    1 
ATOM   3166 H  HA   . ARG   A 1 148 ? 22.103 -19.394 6.247   1.00 14.46 ?  148  ARG   A HA   1 
ATOM   3167 H  HB2  . ARG   A 1 148 ? 24.904 -19.707 6.120   1.00 15.16 ?  148  ARG   A HB2  1 
ATOM   3168 H  HB3  . ARG   A 1 148 ? 23.923 -20.788 6.744   1.00 15.16 ?  148  ARG   A HB3  1 
ATOM   3169 H  HG2  . ARG   A 1 148 ? 23.000 -21.182 4.682   1.00 16.50 ?  148  ARG   A HG2  1 
ATOM   3170 H  HG3  . ARG   A 1 148 ? 23.908 -20.046 4.039   1.00 16.50 ?  148  ARG   A HG3  1 
ATOM   3171 H  HD2  . ARG   A 1 148 ? 24.910 -22.462 5.108   1.00 17.69 ?  148  ARG   A HD2  1 
ATOM   3172 H  HD3  . ARG   A 1 148 ? 24.799 -22.147 3.554   1.00 17.69 ?  148  ARG   A HD3  1 
ATOM   3173 H  HE   . ARG   A 1 148 ? 26.773 -21.331 5.150   1.00 17.58 ?  148  ARG   A HE   1 
ATOM   3174 H  HH11 . ARG   A 1 148 ? 25.337 -20.530 2.265   1.00 17.25 ?  148  ARG   A HH11 1 
ATOM   3175 H  HH12 . ARG   A 1 148 ? 26.476 -19.721 1.754   1.00 17.25 ?  148  ARG   A HH12 1 
ATOM   3176 H  HH21 . ARG   A 1 148 ? 28.463 -20.072 4.350   1.00 17.10 ?  148  ARG   A HH21 1 
ATOM   3177 H  HH22 . ARG   A 1 148 ? 28.359 -19.443 3.004   1.00 17.10 ?  148  ARG   A HH22 1 
ATOM   3178 N  N    . THR   A 1 149 ? 23.651 -17.336 8.004   1.00 11.97 ?  149  THR   A N    1 
ATOM   3179 C  CA   . THR   A 1 149 ? 23.722 -16.737 9.322   1.00 12.15 ?  149  THR   A CA   1 
ATOM   3180 C  C    . THR   A 1 149 ? 22.398 -16.036 9.616   1.00 11.32 ?  149  THR   A C    1 
ATOM   3181 O  O    . THR   A 1 149 ? 21.470 -16.032 8.798   1.00 12.27 ?  149  THR   A O    1 
ATOM   3182 C  CB   . THR   A 1 149 ? 24.920 -15.798 9.385   1.00 12.52 ?  149  THR   A CB   1 
ATOM   3183 O  OG1  . THR   A 1 149 ? 24.791 -14.864 8.310   1.00 12.63 ?  149  THR   A OG1  1 
ATOM   3184 C  CG2  . THR   A 1 149 ? 26.232 -16.588 9.271   1.00 13.16 ?  149  THR   A CG2  1 
ATOM   3185 H  H    . THR   A 1 149 ? 24.009 -16.850 7.388   1.00 14.39 ?  149  THR   A H    1 
ATOM   3186 H  HA   . THR   A 1 149 ? 23.849 -17.438 9.983   1.00 14.60 ?  149  THR   A HA   1 
ATOM   3187 H  HB   . THR   A 1 149 ? 24.908 -15.321 10.228  1.00 15.05 ?  149  THR   A HB   1 
ATOM   3188 H  HG1  . THR   A 1 149 ? 25.441 -14.336 8.308   1.00 15.18 ?  149  THR   A HG1  1 
ATOM   3189 H  HG21 . THR   A 1 149 ? 26.989 -15.985 9.329   1.00 15.81 ?  149  THR   A HG21 1 
ATOM   3190 H  HG22 . THR   A 1 149 ? 26.294 -17.239 9.990   1.00 15.81 ?  149  THR   A HG22 1 
ATOM   3191 H  HG23 . THR   A 1 149 ? 26.269 -17.058 8.422   1.00 15.81 ?  149  THR   A HG23 1 
ATOM   3192 N  N    . ASN   A 1 150 ? 22.270 -15.495 10.820  1.00 11.61 ?  150  ASN   A N    1 
ATOM   3193 C  CA   . ASN   A 1 150 ? 20.985 -14.988 11.290  1.00 12.18 ?  150  ASN   A CA   1 
ATOM   3194 C  C    . ASN   A 1 150 ? 20.801 -13.549 10.835  1.00 11.57 ?  150  ASN   A C    1 
ATOM   3195 O  O    . ASN   A 1 150 ? 21.554 -12.657 11.245  1.00 13.04 ?  150  ASN   A O    1 
ATOM   3196 C  CB   . ASN   A 1 150 ? 20.905 -15.102 12.807  1.00 14.79 ?  150  ASN   A CB   1 
ATOM   3197 C  CG   . ASN   A 1 150 ? 20.794 -16.534 13.264  1.00 18.78 ?  150  ASN   A CG   1 
ATOM   3198 O  OD1  . ASN   A 1 150 ? 20.200 -17.366 12.579  1.00 20.16 ?  150  ASN   A OD1  1 
ATOM   3199 N  ND2  . ASN   A 1 150 ? 21.378 -16.839 14.418  1.00 20.87 ?  150  ASN   A ND2  1 
ATOM   3200 H  H    . ASN   A 1 150 ? 22.907 -15.409 11.385  1.00 13.95 ?  150  ASN   A H    1 
ATOM   3201 H  HA   . ASN   A 1 150 ? 20.264 -15.524 10.913  1.00 14.64 ?  150  ASN   A HA   1 
ATOM   3202 H  HB2  . ASN   A 1 150 ? 21.706 -14.726 13.198  1.00 17.77 ?  150  ASN   A HB2  1 
ATOM   3203 H  HB3  . ASN   A 1 150 ? 20.120 -14.631 13.126  1.00 17.77 ?  150  ASN   A HB3  1 
ATOM   3204 H  HD21 . ASN   A 1 150 ? 21.347 -17.647 14.724  1.00 25.07 ?  150  ASN   A HD21 1 
ATOM   3205 H  HD22 . ASN   A 1 150 ? 21.785 -16.231 14.871  1.00 25.07 ?  150  ASN   A HD22 1 
ATOM   3206 N  N    . VAL   A 1 151 ? 19.806 -13.324 9.983   1.00 11.40 ?  151  VAL   A N    1 
ATOM   3207 C  CA   . VAL   A 1 151 ? 19.597 -12.025 9.369   1.00 11.09 ?  151  VAL   A CA   1 
ATOM   3208 C  C    . VAL   A 1 151 ? 18.210 -11.515 9.723   1.00 10.98 ?  151  VAL   A C    1 
ATOM   3209 O  O    . VAL   A 1 151 ? 17.204 -12.228 9.572   1.00 12.30 ?  151  VAL   A O    1 
ATOM   3210 C  CB   . VAL   A 1 151 ? 19.898 -12.030 7.854   1.00 12.50 ?  151  VAL   A CB   1 
ATOM   3211 C  CG1  . VAL   A 1 151 ? 19.083 -13.060 7.104   1.00 13.43 ?  151  VAL   A CG1  1 
ATOM   3212 C  CG2  . VAL   A 1 151 ? 19.725 -10.633 7.262   1.00 12.86 ?  151  VAL   A CG2  1 
ATOM   3213 H  H    . VAL   A 1 151 ? 19.236 -13.921 9.735   1.00 13.70 ?  151  VAL   A H    1 
ATOM   3214 H  HA   . VAL   A 1 151 ? 20.234 -11.406 9.761   1.00 13.33 ?  151  VAL   A HA   1 
ATOM   3215 H  HB   . VAL   A 1 151 ? 20.834 -12.270 7.729   1.00 15.03 ?  151  VAL   A HB   1 
ATOM   3216 H  HG11 . VAL   A 1 151 ? 19.293 -13.019 6.157   1.00 16.14 ?  151  VAL   A HG11 1 
ATOM   3217 H  HG12 . VAL   A 1 151 ? 19.298 -13.949 7.445   1.00 16.14 ?  151  VAL   A HG12 1 
ATOM   3218 H  HG13 . VAL   A 1 151 ? 18.138 -12.883 7.239   1.00 16.14 ?  151  VAL   A HG13 1 
ATOM   3219 H  HG21 . VAL   A 1 151 ? 20.042 -10.638 6.340   1.00 15.45 ?  151  VAL   A HG21 1 
ATOM   3220 H  HG22 . VAL   A 1 151 ? 18.788 -10.393 7.282   1.00 15.45 ?  151  VAL   A HG22 1 
ATOM   3221 H  HG23 . VAL   A 1 151 ? 20.245 -10.002 7.780   1.00 15.45 ?  151  VAL   A HG23 1 
ATOM   3222 N  N    . TYR   A 1 152 ? 18.188 -10.272 10.204  1.00 10.98 ?  152  TYR   A N    1 
ATOM   3223 C  CA   . TYR   A 1 152 ? 16.992 -9.542  10.587  1.00 10.84 ?  152  TYR   A CA   1 
ATOM   3224 C  C    . TYR   A 1 152 ? 16.790 -8.446  9.551   1.00 10.42 ?  152  TYR   A C    1 
ATOM   3225 O  O    . TYR   A 1 152 ? 17.564 -7.484  9.499   1.00 10.96 ?  152  TYR   A O    1 
ATOM   3226 C  CB   . TYR   A 1 152 ? 17.178 -8.994  11.998  1.00 11.57 ?  152  TYR   A CB   1 
ATOM   3227 C  CG   . TYR   A 1 152 ? 17.134 -10.118 12.995  1.00 12.13 ?  152  TYR   A CG   1 
ATOM   3228 C  CD1  . TYR   A 1 152 ? 18.252 -10.897 13.258  1.00 13.69 ?  152  TYR   A CD1  1 
ATOM   3229 C  CD2  . TYR   A 1 152 ? 15.950 -10.456 13.628  1.00 12.86 ?  152  TYR   A CD2  1 
ATOM   3230 C  CE1  . TYR   A 1 152 ? 18.202 -11.962 14.139  1.00 15.17 ?  152  TYR   A CE1  1 
ATOM   3231 C  CE2  . TYR   A 1 152 ? 15.885 -11.527 14.517  1.00 13.96 ?  152  TYR   A CE2  1 
ATOM   3232 C  CZ   . TYR   A 1 152 ? 17.018 -12.271 14.767  1.00 15.19 ?  152  TYR   A CZ   1 
ATOM   3233 O  OH   . TYR   A 1 152 ? 16.969 -13.340 15.640  1.00 17.14 ?  152  TYR   A OH   1 
ATOM   3234 H  H    . TYR   A 1 152 ? 18.909 -9.799  10.308  1.00 13.19 ?  152  TYR   A H    1 
ATOM   3235 H  HA   . TYR   A 1 152 ? 16.229 -10.135 10.572  1.00 13.03 ?  152  TYR   A HA   1 
ATOM   3236 H  HB2  . TYR   A 1 152 ? 18.044 -8.561  12.066  1.00 13.91 ?  152  TYR   A HB2  1 
ATOM   3237 H  HB3  . TYR   A 1 152 ? 16.467 -8.372  12.201  1.00 13.91 ?  152  TYR   A HB3  1 
ATOM   3238 H  HD1  . TYR   A 1 152 ? 19.053 -10.696 12.830  1.00 16.45 ?  152  TYR   A HD1  1 
ATOM   3239 H  HD2  . TYR   A 1 152 ? 15.179 -9.958  13.457  1.00 15.46 ?  152  TYR   A HD2  1 
ATOM   3240 H  HE1  . TYR   A 1 152 ? 18.966 -12.462 14.307  1.00 18.23 ?  152  TYR   A HE1  1 
ATOM   3241 H  HE2  . TYR   A 1 152 ? 15.084 -11.730 14.941  1.00 16.78 ?  152  TYR   A HE2  1 
ATOM   3242 H  HH   . TYR   A 1 152 ? 16.197 -13.407 15.962  1.00 20.59 ?  152  TYR   A HH   1 
ATOM   3243 N  N    A LEU   A 1 153 ? 15.788 -8.639  8.688   0.50 10.28 ?  153  LEU   A N    1 
ATOM   3244 N  N    B LEU   A 1 153 ? 15.737 -8.562  8.755   0.50 10.51 ?  153  LEU   A N    1 
ATOM   3245 C  CA   A LEU   A 1 153 ? 15.526 -7.778  7.539   0.50 10.31 ?  153  LEU   A CA   1 
ATOM   3246 C  CA   B LEU   A 1 153 ? 15.475 -7.624  7.676   0.50 10.33 ?  153  LEU   A CA   1 
ATOM   3247 C  C    A LEU   A 1 153 ? 14.507 -6.710  7.910   0.50 10.01 ?  153  LEU   A C    1 
ATOM   3248 C  C    B LEU   A 1 153 ? 14.501 -6.549  8.134   0.50 10.84 ?  153  LEU   A C    1 
ATOM   3249 O  O    A LEU   A 1 153 ? 13.382 -7.026  8.312   0.50 10.65 ?  153  LEU   A O    1 
ATOM   3250 O  O    B LEU   A 1 153 ? 13.438 -6.856  8.685   0.50 11.24 ?  153  LEU   A O    1 
ATOM   3251 C  CB   A LEU   A 1 153 ? 14.983 -8.605  6.370   0.50 10.51 ?  153  LEU   A CB   1 
ATOM   3252 C  CB   B LEU   A 1 153 ? 14.904 -8.357  6.466   0.50 10.45 ?  153  LEU   A CB   1 
ATOM   3253 C  CG   A LEU   A 1 153 ? 15.936 -9.610  5.717   0.50 10.74 ?  153  LEU   A CG   1 
ATOM   3254 C  CG   B LEU   A 1 153 ? 15.840 -9.371  5.809   0.50 10.54 ?  153  LEU   A CG   1 
ATOM   3255 C  CD1  A LEU   A 1 153 ? 15.190 -10.494 4.719   0.50 10.68 ?  153  LEU   A CD1  1 
ATOM   3256 C  CD1  B LEU   A 1 153 ? 15.048 -10.253 4.872   0.50 10.79 ?  153  LEU   A CD1  1 
ATOM   3257 C  CD2  A LEU   A 1 153 ? 17.088 -8.895  5.029   0.50 11.32 ?  153  LEU   A CD2  1 
ATOM   3258 C  CD2  B LEU   A 1 153 ? 16.964 -8.675  5.058   0.50 11.36 ?  153  LEU   A CD2  1 
ATOM   3259 H  H    A LEU   A 1 153 ? 15.224 -9.294  8.756   0.50 12.35 ?  153  LEU   A H    1 
ATOM   3260 H  H    B LEU   A 1 153 ? 15.136 -9.183  8.833   0.50 12.64 ?  153  LEU   A H    1 
ATOM   3261 H  HA   A LEU   A 1 153 ? 16.342 -7.350  7.264   0.50 12.39 ?  153  LEU   A HA   1 
ATOM   3262 H  HA   B LEU   A 1 153 ? 16.302 -7.197  7.427   0.50 12.42 ?  153  LEU   A HA   1 
ATOM   3263 H  HB2  A LEU   A 1 153 ? 14.212 -9.108  6.680   0.50 12.64 ?  153  LEU   A HB2  1 
ATOM   3264 H  HB2  B LEU   A 1 153 ? 14.107 -8.829  6.747   0.50 12.57 ?  153  LEU   A HB2  1 
ATOM   3265 H  HB3  A LEU   A 1 153 ? 14.700 -7.993  5.672   0.50 12.64 ?  153  LEU   A HB3  1 
ATOM   3266 H  HB3  B LEU   A 1 153 ? 14.673 -7.695  5.799   0.50 12.57 ?  153  LEU   A HB3  1 
ATOM   3267 H  HG   A LEU   A 1 153 ? 16.307 -10.188 6.402   0.50 12.91 ?  153  LEU   A HG   1 
ATOM   3268 H  HG   B LEU   A 1 153 ? 16.234 -9.931  6.498   0.50 12.67 ?  153  LEU   A HG   1 
ATOM   3269 H  HD11 A LEU   A 1 153 ? 15.728 -11.277 4.520   0.50 12.84 ?  153  LEU   A HD11 1 
ATOM   3270 H  HD11 B LEU   A 1 153 ? 15.651 -10.890 4.462   0.50 12.97 ?  153  LEU   A HD11 1 
ATOM   3271 H  HD12 A LEU   A 1 153 ? 14.345 -10.767 5.108   0.50 12.84 ?  153  LEU   A HD12 1 
ATOM   3272 H  HD12 B LEU   A 1 153 ? 14.364 -10.715 5.377   0.50 12.97 ?  153  LEU   A HD12 1 
ATOM   3273 H  HD13 A LEU   A 1 153 ? 15.030 -9.988  3.906   0.50 12.84 ?  153  LEU   A HD13 1 
ATOM   3274 H  HD13 B LEU   A 1 153 ? 14.640 -9.694  4.191   0.50 12.97 ?  153  LEU   A HD13 1 
ATOM   3275 H  HD21 A LEU   A 1 153 ? 17.706 -9.555  4.685   0.50 13.60 ?  153  LEU   A HD21 1 
ATOM   3276 H  HD21 B LEU   A 1 153 ? 17.518 -9.351  4.638   0.50 13.66 ?  153  LEU   A HD21 1 
ATOM   3277 H  HD22 A LEU   A 1 153 ? 16.732 -8.360  4.304   0.50 13.60 ?  153  LEU   A HD22 1 
ATOM   3278 H  HD22 B LEU   A 1 153 ? 16.575 -8.098  4.384   0.50 13.66 ?  153  LEU   A HD22 1 
ATOM   3279 H  HD23 A LEU   A 1 153 ? 17.532 -8.331  5.676   0.50 13.60 ?  153  LEU   A HD23 1 
ATOM   3280 H  HD23 B LEU   A 1 153 ? 17.486 -8.155  5.684   0.50 13.66 ?  153  LEU   A HD23 1 
ATOM   3281 N  N    A ALA   A 1 154 ? 14.892 -5.452  7.747   0.50 10.19 ?  154  ALA   A N    1 
ATOM   3282 N  N    B ALA   A 1 154 ? 14.868 -5.293  7.899   0.50 10.76 ?  154  ALA   A N    1 
ATOM   3283 C  CA   A ALA   A 1 154 ? 14.007 -4.318  7.962   0.50 10.09 ?  154  ALA   A CA   1 
ATOM   3284 C  CA   B ALA   A 1 154 ? 14.026 -4.139  8.181   0.50 11.54 ?  154  ALA   A CA   1 
ATOM   3285 C  C    A ALA   A 1 154 ? 13.532 -3.813  6.609   0.50 9.68  ?  154  ALA   A C    1 
ATOM   3286 C  C    B ALA   A 1 154 ? 13.485 -3.605  6.861   0.50 11.68 ?  154  ALA   A C    1 
ATOM   3287 O  O    A ALA   A 1 154 ? 14.349 -3.428  5.767   0.50 10.90 ?  154  ALA   A O    1 
ATOM   3288 O  O    B ALA   A 1 154 ? 14.260 -3.186  5.996   0.50 11.72 ?  154  ALA   A O    1 
ATOM   3289 C  CB   A ALA   A 1 154 ? 14.742 -3.204  8.700   0.50 11.22 ?  154  ALA   A CB   1 
ATOM   3290 C  CB   B ALA   A 1 154 ? 14.825 -3.057  8.907   0.50 12.56 ?  154  ALA   A CB   1 
ATOM   3291 H  H    A ALA   A 1 154 ? 15.680 -5.234  7.497   0.50 12.25 ?  154  ALA   A H    1 
ATOM   3292 H  H    B ALA   A 1 154 ? 15.628 -5.076  7.558   0.50 12.93 ?  154  ALA   A H    1 
ATOM   3293 H  HA   A ALA   A 1 154 ? 13.234 -4.594  8.482   0.50 12.13 ?  154  ALA   A HA   1 
ATOM   3294 H  HA   B ALA   A 1 154 ? 13.277 -4.399  8.737   0.50 13.87 ?  154  ALA   A HA   1 
ATOM   3295 H  HB1  A ALA   A 1 154 ? 14.133 -2.462  8.826   0.50 13.49 ?  154  ALA   A HB1  1 
ATOM   3296 H  HB1  B ALA   A 1 154 ? 14.246 -2.300  9.083   0.50 15.10 ?  154  ALA   A HB1  1 
ATOM   3297 H  HB2  A ALA   A 1 154 ? 15.042 -3.542  9.555   0.50 13.49 ?  154  ALA   A HB2  1 
ATOM   3298 H  HB2  B ALA   A 1 154 ? 15.158 -3.422  9.741   0.50 15.10 ?  154  ALA   A HB2  1 
ATOM   3299 H  HB3  A ALA   A 1 154 ? 15.501 -2.925  8.164   0.50 13.49 ?  154  ALA   A HB3  1 
ATOM   3300 H  HB3  B ALA   A 1 154 ? 15.567 -2.784  8.345   0.50 15.10 ?  154  ALA   A HB3  1 
ATOM   3301 N  N    A VAL   A 1 155 ? 12.218 -3.828  6.402   0.30 8.10  ?  155  VAL   A N    1 
ATOM   3302 N  N    B VAL   A 1 155 ? 12.162 -3.630  6.717   0.50 11.91 ?  155  VAL   A N    1 
ATOM   3303 C  CA   A VAL   A 1 155 ? 11.580 -3.337  5.186   0.30 9.66  ?  155  VAL   A CA   1 
ATOM   3304 C  CA   B VAL   A 1 155 ? 11.437 -3.155  5.539   0.50 13.96 ?  155  VAL   A CA   1 
ATOM   3305 C  CA   T VAL   A 1 155 ? 11.556 -3.353  5.259   0.20 10.75 ?  155  VAL   A CA   1 
ATOM   3306 C  C    A VAL   A 1 155 ? 10.888 -2.026  5.534   0.30 10.06 ?  155  VAL   A C    1 
ATOM   3307 C  C    B VAL   A 1 155 ? 10.498 -2.056  6.027   0.50 16.60 ?  155  VAL   A C    1 
ATOM   3308 C  C    T VAL   A 1 155 ? 10.928 -1.990  5.569   0.20 10.48 ?  155  VAL   A C    1 
ATOM   3309 O  O    A VAL   A 1 155 ? 9.945  -2.010  6.335   0.30 10.39 ?  155  VAL   A O    1 
ATOM   3310 O  O    B VAL   A 1 155 ? 9.484  -2.349  6.669   0.50 17.26 ?  155  VAL   A O    1 
ATOM   3311 O  O    T VAL   A 1 155 ? 10.059 -1.873  6.432   0.20 10.39 ?  155  VAL   A O    1 
ATOM   3312 C  CB   A VAL   A 1 155 ? 10.582 -4.366  4.631   0.30 10.47 ?  155  VAL   A CB   1 
ATOM   3313 C  CB   B VAL   A 1 155 ? 10.632 -4.294  4.891   0.50 13.72 ?  155  VAL   A CB   1 
ATOM   3314 C  CB   T VAL   A 1 155 ? 10.535 -4.375  4.708   0.20 11.07 ?  155  VAL   A CB   1 
ATOM   3315 C  CG1  A VAL   A 1 155 ? 9.942  -3.861  3.348   0.30 11.51 ?  155  VAL   A CG1  1 
ATOM   3316 C  CG1  B VAL   A 1 155 ? 9.777  -3.778  3.739   0.50 14.29 ?  155  VAL   A CG1  1 
ATOM   3317 C  CG1  T VAL   A 1 155 ? 9.850  -3.835  3.464   0.20 11.69 ?  155  VAL   A CG1  1 
ATOM   3318 C  CG2  A VAL   A 1 155 ? 11.278 -5.701  4.391   0.30 11.05 ?  155  VAL   A CG2  1 
ATOM   3319 C  CG2  B VAL   A 1 155 ? 11.553 -5.421  4.424   0.50 14.27 ?  155  VAL   A CG2  1 
ATOM   3320 C  CG2  T VAL   A 1 155 ? 11.223 -5.703  4.402   0.20 11.36 ?  155  VAL   A CG2  1 
ATOM   3321 H  H    A VAL   A 1 155 ? 11.655 -4.149  6.969   0.30 9.74  ?  155  VAL   A H    1 
ATOM   3322 H  H    B VAL   A 1 155 ? 11.635 -3.930  7.319   0.50 14.32 ?  155  VAL   A H    1 
ATOM   3323 H  HA   A VAL   A 1 155 ? 12.251 -3.164  4.510   0.30 11.61 ?  155  VAL   A HA   1 
ATOM   3324 H  HA   B VAL   A 1 155 ? 12.050 -2.785  4.879   0.50 16.78 ?  155  VAL   A HA   1 
ATOM   3325 H  HB   A VAL   A 1 155 ? 9.875  -4.508  5.281   0.30 12.58 ?  155  VAL   A HB   1 
ATOM   3326 H  HB   B VAL   A 1 155 ? 10.029 -4.663  5.555   0.50 16.49 ?  155  VAL   A HB   1 
ATOM   3327 H  HB   T VAL   A 1 155 ? 9.856  -4.538  5.379   0.20 13.31 ?  155  VAL   A HB   1 
ATOM   3328 H  HG11 A VAL   A 1 155 ? 9.407  -4.571  2.962   0.30 13.83 ?  155  VAL   A HG11 1 
ATOM   3329 H  HG11 B VAL   A 1 155 ? 9.454  -4.534  3.222   0.50 17.18 ?  155  VAL   A HG11 1 
ATOM   3330 H  HG11 T VAL   A 1 155 ? 9.328  -4.544  3.058   0.20 14.06 ?  155  VAL   A HG11 1 
ATOM   3331 H  HG12 A VAL   A 1 155 ? 9.378  -3.098  3.554   0.30 13.83 ?  155  VAL   A HG12 1 
ATOM   3332 H  HG12 B VAL   A 1 155 ? 9.026  -3.279  4.097   0.50 17.18 ?  155  VAL   A HG12 1 
ATOM   3333 H  HG12 T VAL   A 1 155 ? 9.270  -3.100  3.716   0.20 14.06 ?  155  VAL   A HG12 1 
ATOM   3334 H  HG13 A VAL   A 1 155 ? 10.642 -3.599  2.730   0.30 13.83 ?  155  VAL   A HG13 1 
ATOM   3335 H  HG13 B VAL   A 1 155 ? 10.320 -3.204  3.176   0.50 17.18 ?  155  VAL   A HG13 1 
ATOM   3336 H  HG13 T VAL   A 1 155 ? 10.527 -3.526  2.841   0.20 14.06 ?  155  VAL   A HG13 1 
ATOM   3337 H  HG21 A VAL   A 1 155 ? 10.660 -6.307  3.955   0.30 13.28 ?  155  VAL   A HG21 1 
ATOM   3338 H  HG21 B VAL   A 1 155 ? 11.021 -6.097  3.970   0.50 17.15 ?  155  VAL   A HG21 1 
ATOM   3339 H  HG21 T VAL   A 1 155 ? 10.566 -6.330  4.060   0.20 13.66 ?  155  VAL   A HG21 1 
ATOM   3340 H  HG22 A VAL   A 1 155 ? 12.052 -5.554  3.823   0.30 13.28 ?  155  VAL   A HG22 1 
ATOM   3341 H  HG22 B VAL   A 1 155 ? 12.214 -5.059  3.816   0.50 17.15 ?  155  VAL   A HG22 1 
ATOM   3342 H  HG22 T VAL   A 1 155 ? 11.914 -5.555  3.735   0.20 13.66 ?  155  VAL   A HG22 1 
ATOM   3343 H  HG23 A VAL   A 1 155 ? 11.559 -6.070  5.242   0.30 13.28 ?  155  VAL   A HG23 1 
ATOM   3344 H  HG23 B VAL   A 1 155 ? 11.989 -5.811  5.197   0.50 17.15 ?  155  VAL   A HG23 1 
ATOM   3345 H  HG23 T VAL   A 1 155 ? 11.620 -6.049  5.216   0.20 13.66 ?  155  VAL   A HG23 1 
ATOM   3346 N  N    A PHE   A 1 156 ? 11.354 -0.922  4.941   0.30 10.84 ?  156  PHE   A N    1 
ATOM   3347 N  N    B PHE   A 1 156 ? 10.817 -0.793  5.733   0.50 18.43 ?  156  PHE   A N    1 
ATOM   3348 N  N    T PHE   A 1 156 ? 11.389 -0.959  4.859   0.20 10.59 ?  156  PHE   A N    1 
ATOM   3349 C  CA   A PHE   A 1 156 ? 10.838 0.391   5.330   0.30 12.18 ?  156  PHE   A CA   1 
ATOM   3350 C  CA   B PHE   A 1 156 ? 10.001 0.289   6.285   0.50 19.98 ?  156  PHE   A CA   1 
ATOM   3351 C  CA   T PHE   A 1 156 ? 10.951 0.408   5.141   0.20 10.98 ?  156  PHE   A CA   1 
ATOM   3352 C  C    A PHE   A 1 156 ? 9.371  0.559   4.946   0.30 12.21 ?  156  PHE   A C    1 
ATOM   3353 C  C    B PHE   A 1 156 ? 8.682  0.476   5.539   0.50 20.33 ?  156  PHE   A C    1 
ATOM   3354 C  C    T PHE   A 1 156 ? 9.496  0.627   4.747   0.20 11.89 ?  156  PHE   A C    1 
ATOM   3355 O  O    A PHE   A 1 156 ? 8.576  1.093   5.729   0.30 12.77 ?  156  PHE   A O    1 
ATOM   3356 O  O    B PHE   A 1 156 ? 7.690  0.900   6.145   0.50 21.20 ?  156  PHE   A O    1 
ATOM   3357 O  O    T PHE   A 1 156 ? 8.746  1.297   5.467   0.20 12.25 ?  156  PHE   A O    1 
ATOM   3358 C  CB   A PHE   A 1 156 ? 11.692 1.507   4.720   0.30 13.67 ?  156  PHE   A CB   1 
ATOM   3359 C  CB   B PHE   A 1 156 ? 10.788 1.602   6.323   0.50 21.53 ?  156  PHE   A CB   1 
ATOM   3360 C  CB   T PHE   A 1 156 ? 11.849 1.391   4.389   0.20 10.72 ?  156  PHE   A CB   1 
ATOM   3361 C  CG   A PHE   A 1 156 ? 11.193 2.897   5.040   0.30 15.27 ?  156  PHE   A CG   1 
ATOM   3362 C  CG   B PHE   A 1 156 ? 10.778 2.360   5.026   0.50 22.68 ?  156  PHE   A CG   1 
ATOM   3363 C  CG   T PHE   A 1 156 ? 11.481 2.842   4.590   0.20 10.05 ?  156  PHE   A CG   1 
ATOM   3364 C  CD1  A PHE   A 1 156 ? 11.132 3.335   6.355   0.30 16.00 ?  156  PHE   A CD1  1 
ATOM   3365 C  CD1  B PHE   A 1 156 ? 11.722 2.095   4.049   0.50 22.99 ?  156  PHE   A CD1  1 
ATOM   3366 C  CD1  T PHE   A 1 156 ? 11.865 3.512   5.743   0.20 10.24 ?  156  PHE   A CD1  1 
ATOM   3367 C  CD2  A PHE   A 1 156 ? 10.790 3.761   4.033   0.30 15.96 ?  156  PHE   A CD2  1 
ATOM   3368 C  CD2  B PHE   A 1 156 ? 9.835  3.345   4.791   0.50 23.50 ?  156  PHE   A CD2  1 
ATOM   3369 C  CD2  T PHE   A 1 156 ? 10.767 3.534   3.624   0.20 10.57 ?  156  PHE   A CD2  1 
ATOM   3370 C  CE1  A PHE   A 1 156 ? 10.677 4.607   6.659   0.30 16.44 ?  156  PHE   A CE1  1 
ATOM   3371 C  CE1  B PHE   A 1 156 ? 11.720 2.794   2.859   0.50 23.57 ?  156  PHE   A CE1  1 
ATOM   3372 C  CE1  T PHE   A 1 156 ? 11.534 4.840   5.935   0.20 11.17 ?  156  PHE   A CE1  1 
ATOM   3373 C  CE2  A PHE   A 1 156 ? 10.334 5.035   4.332   0.30 16.56 ?  156  PHE   A CE2  1 
ATOM   3374 C  CE2  B PHE   A 1 156 ? 9.828  4.046   3.604   0.50 23.85 ?  156  PHE   A CE2  1 
ATOM   3375 C  CE2  T PHE   A 1 156 ? 10.437 4.864   3.809   0.20 11.25 ?  156  PHE   A CE2  1 
ATOM   3376 C  CZ   A PHE   A 1 156 ? 10.280 5.456   5.646   0.30 16.89 ?  156  PHE   A CZ   1 
ATOM   3377 C  CZ   B PHE   A 1 156 ? 10.770 3.770   2.637   0.50 23.75 ?  156  PHE   A CZ   1 
ATOM   3378 C  CZ   T PHE   A 1 156 ? 10.821 5.517   4.966   0.20 11.21 ?  156  PHE   A CZ   1 
ATOM   3379 H  H    A PHE   A 1 156 ? 11.951 -0.909  4.321   0.30 13.03 ?  156  PHE   A H    1 
ATOM   3380 H  H    B PHE   A 1 156 ? 11.479 -0.543  5.245   0.50 22.14 ?  156  PHE   A H    1 
ATOM   3381 H  H    T PHE   A 1 156 ? 11.958 -1.027  4.221   0.20 12.73 ?  156  PHE   A H    1 
ATOM   3382 H  HA   A PHE   A 1 156 ? 10.905 0.479   6.293   0.30 14.63 ?  156  PHE   A HA   1 
ATOM   3383 H  HA   B PHE   A 1 156 ? 9.781  0.061   7.200   0.50 24.00 ?  156  PHE   A HA   1 
ATOM   3384 H  HA   T PHE   A 1 156 ? 11.042 0.577   6.093   0.20 13.19 ?  156  PHE   A HA   1 
ATOM   3385 H  HB2  A PHE   A 1 156 ? 12.604 1.433   5.060   0.30 16.43 ?  156  PHE   A HB2  1 
ATOM   3386 H  HB2  B PHE   A 1 156 ? 10.408 2.175   7.008   0.50 25.86 ?  156  PHE   A HB2  1 
ATOM   3387 H  HB2  T PHE   A 1 156 ? 12.762 1.270   4.693   0.20 12.89 ?  156  PHE   A HB2  1 
ATOM   3388 H  HB3  A PHE   A 1 156 ? 11.701 1.411   3.755   0.30 16.43 ?  156  PHE   A HB3  1 
ATOM   3389 H  HB3  B PHE   A 1 156 ? 11.710 1.398   6.537   0.50 25.86 ?  156  PHE   A HB3  1 
ATOM   3390 H  HB3  T PHE   A 1 156 ? 11.789 1.200   3.441   0.20 12.89 ?  156  PHE   A HB3  1 
ATOM   3391 H  HD1  A PHE   A 1 156 ? 11.405 2.766   7.042   0.30 19.23 ?  156  PHE   A HD1  1 
ATOM   3392 H  HD1  B PHE   A 1 156 ? 12.365 1.437   4.197   0.50 27.61 ?  156  PHE   A HD1  1 
ATOM   3393 H  HD1  T PHE   A 1 156 ? 12.339 3.051   6.406   0.20 12.31 ?  156  PHE   A HD1  1 
ATOM   3394 H  HD2  A PHE   A 1 156 ? 10.833 3.480   3.148   0.30 19.18 ?  156  PHE   A HD2  1 
ATOM   3395 H  HD2  B PHE   A 1 156 ? 9.199  3.534   5.441   0.50 28.22 ?  156  PHE   A HD2  1 
ATOM   3396 H  HD2  T PHE   A 1 156 ? 10.510 3.097   2.848   0.20 12.71 ?  156  PHE   A HD2  1 
ATOM   3397 H  HE1  A PHE   A 1 156 ? 10.643 4.888   7.547   0.30 19.75 ?  156  PHE   A HE1  1 
ATOM   3398 H  HE1  B PHE   A 1 156 ? 12.359 2.606   2.209   0.50 28.31 ?  156  PHE   A HE1  1 
ATOM   3399 H  HE1  T PHE   A 1 156 ? 11.788 5.271   6.720   0.20 13.43 ?  156  PHE   A HE1  1 
ATOM   3400 H  HE2  A PHE   A 1 156 ? 10.070 5.604   3.648   0.30 19.90 ?  156  PHE   A HE2  1 
ATOM   3401 H  HE2  B PHE   A 1 156 ? 9.189  4.704   3.457   0.50 28.64 ?  156  PHE   A HE2  1 
ATOM   3402 H  HE2  T PHE   A 1 156 ? 9.958  5.318   3.159   0.20 13.52 ?  156  PHE   A HE2  1 
ATOM   3403 H  HZ   A PHE   A 1 156 ? 9.975  6.310   5.850   0.30 20.29 ?  156  PHE   A HZ   1 
ATOM   3404 H  HZ   B PHE   A 1 156 ? 10.768 4.243   1.837   0.50 28.52 ?  156  PHE   A HZ   1 
ATOM   3405 H  HZ   T PHE   A 1 156 ? 10.596 6.408   5.096   0.20 13.47 ?  156  PHE   A HZ   1 
ATOM   3406 N  N    A ASP   A 1 157 ? 8.989  0.098   3.759   0.30 13.39 ?  157  ASP   A N    1 
ATOM   3407 N  N    B ASP   A 1 157 ? 8.651  0.180   4.243   0.50 19.51 ?  157  ASP   A N    1 
ATOM   3408 N  N    T ASP   A 1 157 ? 9.085  0.089   3.604   0.20 13.10 ?  157  ASP   A N    1 
ATOM   3409 C  CA   A ASP   A 1 157 ? 7.663  0.371   3.213   0.30 14.94 ?  157  ASP   A CA   1 
ATOM   3410 C  CA   B ASP   A 1 157 ? 7.440  0.355   3.447   0.50 19.09 ?  157  ASP   A CA   1 
ATOM   3411 C  CA   T ASP   A 1 157 ? 7.770  0.360   3.038   0.20 14.56 ?  157  ASP   A CA   1 
ATOM   3412 C  C    A ASP   A 1 157 ? 6.667  -0.668  3.721   0.30 15.58 ?  157  ASP   A C    1 
ATOM   3413 C  C    B ASP   A 1 157 ? 6.427  -0.735  3.791   0.50 19.21 ?  157  ASP   A C    1 
ATOM   3414 C  C    T ASP   A 1 157 ? 6.754  -0.628  3.603   0.20 15.44 ?  157  ASP   A C    1 
ATOM   3415 O  O    A ASP   A 1 157 ? 6.815  -1.864  3.446   0.30 15.11 ?  157  ASP   A O    1 
ATOM   3416 O  O    B ASP   A 1 157 ? 6.678  -1.923  3.561   0.50 19.10 ?  157  ASP   A O    1 
ATOM   3417 O  O    T ASP   A 1 157 ? 6.879  -1.840  3.397   0.20 15.20 ?  157  ASP   A O    1 
ATOM   3418 C  CB   A ASP   A 1 157 ? 7.717  0.355   1.687   0.30 15.74 ?  157  ASP   A CB   1 
ATOM   3419 C  CB   B ASP   A 1 157 ? 7.810  0.300   1.968   0.50 18.62 ?  157  ASP   A CB   1 
ATOM   3420 C  CB   T ASP   A 1 157 ? 7.843  0.239   1.519   0.20 15.11 ?  157  ASP   A CB   1 
ATOM   3421 C  CG   A ASP   A 1 157 ? 6.404  0.792   1.048   0.30 16.63 ?  157  ASP   A CG   1 
ATOM   3422 C  CG   B ASP   A 1 157 ? 6.665  0.664   1.062   0.50 18.35 ?  157  ASP   A CG   1 
ATOM   3423 C  CG   T ASP   A 1 157 ? 6.654  0.864   0.823   0.20 15.43 ?  157  ASP   A CG   1 
ATOM   3424 O  OD1  A ASP   A 1 157 ? 6.023  1.974   1.190   0.30 17.19 ?  157  ASP   A OD1  1 
ATOM   3425 O  OD1  B ASP   A 1 157 ? 5.520  0.263   1.360   0.50 18.10 ?  157  ASP   A OD1  1 
ATOM   3426 O  OD1  T ASP   A 1 157 ? 5.577  0.231   0.791   0.20 15.66 ?  157  ASP   A OD1  1 
ATOM   3427 O  OD2  A ASP   A 1 157 ? 5.744  -0.054  0.404   0.30 16.91 -1 157  ASP   A OD2  1 
ATOM   3428 O  OD2  B ASP   A 1 157 ? 6.918  1.343   0.045   0.50 18.13 -1 157  ASP   A OD2  1 
ATOM   3429 O  OD2  T ASP   A 1 157 ? 6.796  1.998   0.318   0.20 15.25 -1 157  ASP   A OD2  1 
ATOM   3430 H  H    A ASP   A 1 157 ? 9.489  -0.388  3.255   0.30 16.09 ?  157  ASP   A H    1 
ATOM   3431 H  H    B ASP   A 1 157 ? 9.327  -0.112  3.799   0.50 23.43 ?  157  ASP   A H    1 
ATOM   3432 H  H    T ASP   A 1 157 ? 9.566  -0.440  3.127   0.20 15.74 ?  157  ASP   A H    1 
ATOM   3433 H  HA   A ASP   A 1 157 ? 7.375  1.248   3.507   0.30 17.95 ?  157  ASP   A HA   1 
ATOM   3434 H  HA   B ASP   A 1 157 ? 7.045  1.221   3.638   0.50 22.93 ?  157  ASP   A HA   1 
ATOM   3435 H  HA   T ASP   A 1 157 ? 7.496  1.262   3.270   0.20 17.49 ?  157  ASP   A HA   1 
ATOM   3436 H  HB2  A ASP   A 1 157 ? 8.447  0.933   1.400   0.30 18.91 ?  157  ASP   A HB2  1 
ATOM   3437 H  HB2  B ASP   A 1 157 ? 8.536  0.919   1.799   0.50 22.36 ?  157  ASP   A HB2  1 
ATOM   3438 H  HB2  T ASP   A 1 157 ? 8.648  0.677   1.210   0.20 18.15 ?  157  ASP   A HB2  1 
ATOM   3439 H  HB3  A ASP   A 1 157 ? 7.893  -0.554  1.394   0.30 18.91 ?  157  ASP   A HB3  1 
ATOM   3440 H  HB3  B ASP   A 1 157 ? 8.080  -0.600  1.741   0.50 22.36 ?  157  ASP   A HB3  1 
ATOM   3441 H  HB3  T ASP   A 1 157 ? 7.876  -0.702  1.286   0.20 18.15 ?  157  ASP   A HB3  1 
ATOM   3442 N  N    A LYS   A 1 158 ? 5.646  -0.207  4.451   0.30 16.93 ?  158  LYS   A N    1 
ATOM   3443 N  N    B LYS   A 1 158 ? 5.273  -0.324  4.322   0.50 19.85 ?  158  LYS   A N    1 
ATOM   3444 N  N    T LYS   A 1 158 ? 5.742  -0.106  4.302   0.20 16.70 ?  158  LYS   A N    1 
ATOM   3445 C  CA   A LYS   A 1 158 ? 4.672  -1.128  5.033   0.30 17.99 ?  158  LYS   A CA   1 
ATOM   3446 C  CA   B LYS   A 1 158 ? 4.281  -1.276  4.819   0.50 20.56 ?  158  LYS   A CA   1 
ATOM   3447 C  CA   T LYS   A 1 158 ? 4.748  -0.977  4.923   0.20 17.86 ?  158  LYS   A CA   1 
ATOM   3448 C  C    A LYS   A 1 158 ? 3.904  -1.877  3.952   0.30 17.65 ?  158  LYS   A C    1 
ATOM   3449 C  C    B LYS   A 1 158 ? 3.680  -2.102  3.684   0.50 19.35 ?  158  LYS   A C    1 
ATOM   3450 C  C    T LYS   A 1 158 ? 3.978  -1.772  3.875   0.20 17.88 ?  158  LYS   A C    1 
ATOM   3451 O  O    A LYS   A 1 158 ? 3.650  -3.080  4.082   0.30 18.19 ?  158  LYS   A O    1 
ATOM   3452 O  O    B LYS   A 1 158 ? 3.600  -3.334  3.773   0.50 18.90 ?  158  LYS   A O    1 
ATOM   3453 O  O    T LYS   A 1 158 ? 3.747  -2.975  4.045   0.20 18.21 ?  158  LYS   A O    1 
ATOM   3454 C  CB   A LYS   A 1 158 ? 3.716  -0.372  5.959   0.30 19.22 ?  158  LYS   A CB   1 
ATOM   3455 C  CB   B LYS   A 1 158 ? 3.193  -0.516  5.583   0.50 22.31 ?  158  LYS   A CB   1 
ATOM   3456 C  CB   T LYS   A 1 158 ? 3.793  -0.156  5.793   0.20 19.07 ?  158  LYS   A CB   1 
ATOM   3457 C  CG   A LYS   A 1 158 ? 2.489  -1.169  6.413   0.30 20.68 ?  158  LYS   A CG   1 
ATOM   3458 C  CG   B LYS   A 1 158 ? 1.952  -1.330  5.949   0.50 23.98 ?  158  LYS   A CG   1 
ATOM   3459 C  CG   T LYS   A 1 158 ? 2.568  -0.924  6.283   0.20 20.39 ?  158  LYS   A CG   1 
ATOM   3460 C  CD   A LYS   A 1 158 ? 2.860  -2.410  7.220   0.30 22.06 ?  158  LYS   A CD   1 
ATOM   3461 C  CD   B LYS   A 1 158 ? 2.257  -2.422  6.963   0.50 25.23 ?  158  LYS   A CD   1 
ATOM   3462 C  CD   T LYS   A 1 158 ? 2.953  -2.119  7.144   0.20 21.64 ?  158  LYS   A CD   1 
ATOM   3463 C  CE   A LYS   A 1 158 ? 1.614  -3.093  7.775   0.30 22.93 ?  158  LYS   A CE   1 
ATOM   3464 C  CE   B LYS   A 1 158 ? 0.996  -3.183  7.358   0.50 25.68 ?  158  LYS   A CE   1 
ATOM   3465 C  CE   T LYS   A 1 158 ? 1.725  -2.919  7.557   0.20 22.48 ?  158  LYS   A CE   1 
ATOM   3466 N  NZ   A LYS   A 1 158 ? 1.905  -4.422  8.385   0.30 23.51 ?  158  LYS   A NZ   1 
ATOM   3467 N  NZ   B LYS   A 1 158 ? 1.298  -4.460  8.072   0.50 25.77 ?  158  LYS   A NZ   1 
ATOM   3468 N  NZ   T LYS   A 1 158 ? 2.081  -4.119  8.363   0.20 22.97 ?  158  LYS   A NZ   1 
ATOM   3469 H  H    A LYS   A 1 158 ? 5.497  0.623   4.613   0.30 20.33 ?  158  LYS   A H    1 
ATOM   3470 H  H    B LYS   A 1 158 ? 5.046  0.499   4.405   0.50 23.85 ?  158  LYS   A H    1 
ATOM   3471 H  H    T LYS   A 1 158 ? 5.608  0.734   4.424   0.20 20.07 ?  158  LYS   A H    1 
ATOM   3472 H  HA   A LYS   A 1 158 ? 5.144  -1.784  5.569   0.30 21.61 ?  158  LYS   A HA   1 
ATOM   3473 H  HA   B LYS   A 1 158 ? 4.710  -1.884  5.441   0.50 24.69 ?  158  LYS   A HA   1 
ATOM   3474 H  HA   T LYS   A 1 158 ? 5.201  -1.609  5.501   0.20 21.45 ?  158  LYS   A HA   1 
ATOM   3475 H  HB2  A LYS   A 1 158 ? 4.202  -0.109  6.758   0.30 23.09 ?  158  LYS   A HB2  1 
ATOM   3476 H  HB2  B LYS   A 1 158 ? 3.575  -0.183  6.413   0.50 26.80 ?  158  LYS   A HB2  1 
ATOM   3477 H  HB2  T LYS   A 1 158 ? 4.275  0.154   6.578   0.20 22.91 ?  158  LYS   A HB2  1 
ATOM   3478 H  HB3  A LYS   A 1 158 ? 3.398  0.419   5.498   0.30 23.09 ?  158  LYS   A HB3  1 
ATOM   3479 H  HB3  B LYS   A 1 158 ? 2.901  0.233   5.040   0.50 26.80 ?  158  LYS   A HB3  1 
ATOM   3480 H  HB3  T LYS   A 1 158 ? 3.478  0.604   5.282   0.20 22.91 ?  158  LYS   A HB3  1 
ATOM   3481 H  HG2  A LYS   A 1 158 ? 1.942  -0.602  6.977   0.30 24.84 ?  158  LYS   A HG2  1 
ATOM   3482 H  HG2  B LYS   A 1 158 ? 1.296  -0.733  6.341   0.50 28.80 ?  158  LYS   A HG2  1 
ATOM   3483 H  HG2  T LYS   A 1 158 ? 2.023  -0.333  6.823   0.20 24.48 ?  158  LYS   A HG2  1 
ATOM   3484 H  HG3  A LYS   A 1 158 ? 1.976  -1.451  5.638   0.30 24.84 ?  158  LYS   A HG3  1 
ATOM   3485 H  HG3  B LYS   A 1 158 ? 1.585  -1.744  5.153   0.50 28.80 ?  158  LYS   A HG3  1 
ATOM   3486 H  HG3  T LYS   A 1 158 ? 2.052  -1.244  5.526   0.20 24.48 ?  158  LYS   A HG3  1 
ATOM   3487 H  HD2  A LYS   A 1 158 ? 3.323  -3.040  6.648   0.30 26.49 ?  158  LYS   A HD2  1 
ATOM   3488 H  HD2  B LYS   A 1 158 ? 2.886  -3.050  6.579   0.50 30.29 ?  158  LYS   A HD2  1 
ATOM   3489 H  HD2  T LYS   A 1 158 ? 3.540  -2.706  6.643   0.20 26.00 ?  158  LYS   A HD2  1 
ATOM   3490 H  HD3  A LYS   A 1 158 ? 3.425  -2.150  7.964   0.30 26.49 ?  158  LYS   A HD3  1 
ATOM   3491 H  HD3  B LYS   A 1 158 ? 2.630  -2.016  7.762   0.50 30.29 ?  158  LYS   A HD3  1 
ATOM   3492 H  HD3  T LYS   A 1 158 ? 3.397  -1.806  7.948   0.20 26.00 ?  158  LYS   A HD3  1 
ATOM   3493 H  HE2  A LYS   A 1 158 ? 1.212  -2.527  8.454   0.30 27.53 ?  158  LYS   A HE2  1 
ATOM   3494 H  HE2  B LYS   A 1 158 ? 0.464  -2.625  7.949   0.50 30.84 ?  158  LYS   A HE2  1 
ATOM   3495 H  HE2  T LYS   A 1 158 ? 1.142  -2.357  8.091   0.20 27.00 ?  158  LYS   A HE2  1 
ATOM   3496 H  HE3  A LYS   A 1 158 ? 0.984  -3.229  7.053   0.30 27.53 ?  158  LYS   A HE3  1 
ATOM   3497 H  HE3  B LYS   A 1 158 ? 0.492  -3.394  6.558   0.50 30.84 ?  158  LYS   A HE3  1 
ATOM   3498 H  HE3  T LYS   A 1 158 ? 1.260  -3.219  6.761   0.20 27.00 ?  158  LYS   A HE3  1 
ATOM   3499 H  HZ1  A LYS   A 1 158 ? 1.155  -4.785  8.697   0.30 28.24 ?  158  LYS   A HZ1  1 
ATOM   3500 H  HZ1  B LYS   A 1 158 ? 0.541  -4.875  8.286   0.50 30.95 ?  158  LYS   A HZ1  1 
ATOM   3501 H  HZ1  T LYS   A 1 158 ? 1.344  -4.564  8.588   0.20 27.58 ?  158  LYS   A HZ1  1 
ATOM   3502 H  HZ2  A LYS   A 1 158 ? 2.256  -4.965  7.773   0.30 28.24 ?  158  LYS   A HZ2  1 
ATOM   3503 H  HZ2  B LYS   A 1 158 ? 1.783  -4.993  7.549   0.50 30.95 ?  158  LYS   A HZ2  1 
ATOM   3504 H  HZ2  T LYS   A 1 158 ? 2.610  -4.657  7.890   0.20 27.58 ?  158  LYS   A HZ2  1 
ATOM   3505 H  HZ3  A LYS   A 1 158 ? 2.483  -4.330  9.056   0.30 28.24 ?  158  LYS   A HZ3  1 
ATOM   3506 H  HZ3  B LYS   A 1 158 ? 1.757  -4.292  8.816   0.50 30.95 ?  158  LYS   A HZ3  1 
ATOM   3507 H  HZ3  T LYS   A 1 158 ? 2.508  -3.874  9.104   0.20 27.58 ?  158  LYS   A HZ3  1 
ATOM   3508 N  N    A ASN   A 1 159 ? 3.517  -1.185  2.879   0.30 17.35 ?  159  ASN   A N    1 
ATOM   3509 N  N    B ASN   A 1 159 ? 3.227  -1.440  2.618   0.50 20.06 ?  159  ASN   A N    1 
ATOM   3510 N  N    T ASN   A 1 159 ? 3.567  -1.121  2.793   0.20 17.89 ?  159  ASN   A N    1 
ATOM   3511 C  CA   A ASN   A 1 159 ? 2.820  -1.865  1.793   0.30 17.13 ?  159  ASN   A CA   1 
ATOM   3512 C  CA   B ASN   A 1 159 ? 2.653  -2.170  1.493   0.50 20.87 ?  159  ASN   A CA   1 
ATOM   3513 C  CA   T ASN   A 1 159 ? 2.829  -1.805  1.737   0.20 17.89 ?  159  ASN   A CA   1 
ATOM   3514 C  C    A ASN   A 1 159 ? 3.697  -2.946  1.172   0.30 16.63 ?  159  ASN   A C    1 
ATOM   3515 C  C    B ASN   A 1 159 ? 3.638  -3.202  0.961   0.50 19.23 ?  159  ASN   A C    1 
ATOM   3516 C  C    T ASN   A 1 159 ? 3.670  -2.905  1.095   0.20 17.89 ?  159  ASN   A C    1 
ATOM   3517 O  O    A ASN   A 1 159 ? 3.227  -4.054  0.895   0.30 16.62 ?  159  ASN   A O    1 
ATOM   3518 O  O    B ASN   A 1 159 ? 3.265  -4.345  0.671   0.50 19.22 ?  159  ASN   A O    1 
ATOM   3519 O  O    T ASN   A 1 159 ? 3.149  -3.960  0.739   0.20 17.94 ?  159  ASN   A O    1 
ATOM   3520 C  CB   A ASN   A 1 159 ? 2.350  -0.851  0.748   0.30 17.77 ?  159  ASN   A CB   1 
ATOM   3521 C  CB   B ASN   A 1 159 ? 2.237  -1.182  0.401   0.50 23.64 ?  159  ASN   A CB   1 
ATOM   3522 C  CB   T ASN   A 1 159 ? 2.349  -0.811  0.676   0.20 18.19 ?  159  ASN   A CB   1 
ATOM   3523 C  CG   A ASN   A 1 159 ? 1.136  -0.064  1.206   0.30 18.83 ?  159  ASN   A CG   1 
ATOM   3524 C  CG   B ASN   A 1 159 ? 1.085  -0.290  0.830   0.50 26.24 ?  159  ASN   A CG   1 
ATOM   3525 C  CG   T ASN   A 1 159 ? 1.145  -0.009  1.134   0.20 18.73 ?  159  ASN   A CG   1 
ATOM   3526 O  OD1  A ASN   A 1 159 ? 0.285  -0.587  1.923   0.30 19.12 ?  159  ASN   A OD1  1 
ATOM   3527 O  OD1  B ASN   A 1 159 ? 1.286  0.726   1.495   0.50 27.32 ?  159  ASN   A OD1  1 
ATOM   3528 O  OD1  T ASN   A 1 159 ? 0.318  -0.497  1.902   0.20 18.95 ?  159  ASN   A OD1  1 
ATOM   3529 N  ND2  A ASN   A 1 159 ? 1.048  1.196   0.792   0.30 18.87 ?  159  ASN   A ND2  1 
ATOM   3530 N  ND2  B ASN   A 1 159 ? -0.130 -0.667  0.450   0.50 27.12 ?  159  ASN   A ND2  1 
ATOM   3531 N  ND2  T ASN   A 1 159 ? 1.039  1.226   0.660   0.20 18.62 ?  159  ASN   A ND2  1 
ATOM   3532 H  H    A ASN   A 1 159 ? 3.646  -0.345  2.760   0.30 20.84 ?  159  ASN   A H    1 
ATOM   3533 H  H    B ASN   A 1 159 ? 3.244  -0.588  2.525   0.50 24.10 ?  159  ASN   A H    1 
ATOM   3534 H  H    T ASN   A 1 159 ? 3.697  -0.285  2.650   0.20 21.49 ?  159  ASN   A H    1 
ATOM   3535 H  HA   A ASN   A 1 159 ? 2.030  -2.300  2.155   0.30 20.58 ?  159  ASN   A HA   1 
ATOM   3536 H  HA   B ASN   A 1 159 ? 1.856  -2.637  1.786   0.50 25.07 ?  159  ASN   A HA   1 
ATOM   3537 H  HA   T ASN   A 1 159 ? 2.048  -2.227  2.125   0.20 21.49 ?  159  ASN   A HA   1 
ATOM   3538 H  HB2  A ASN   A 1 159 ? 3.062  -0.221  0.573   0.30 21.34 ?  159  ASN   A HB2  1 
ATOM   3539 H  HB2  B ASN   A 1 159 ? 2.990  -0.606  0.185   0.50 28.39 ?  159  ASN   A HB2  1 
ATOM   3540 H  HB2  T ASN   A 1 159 ? 3.065  -0.191  0.476   0.20 21.85 ?  159  ASN   A HB2  1 
ATOM   3541 H  HB3  A ASN   A 1 159 ? 2.110  -1.323  -0.065  0.30 21.34 ?  159  ASN   A HB3  1 
ATOM   3542 H  HB3  B ASN   A 1 159 ? 1.955  -1.669  -0.387  0.50 28.39 ?  159  ASN   A HB3  1 
ATOM   3543 H  HB3  T ASN   A 1 159 ? 2.099  -1.302  -0.124  0.20 21.85 ?  159  ASN   A HB3  1 
ATOM   3544 H  HD21 A ASN   A 1 159 ? 0.379  1.680   1.025   0.30 22.66 ?  159  ASN   A HD21 1 
ATOM   3545 H  HD21 B ASN   A 1 159 ? -0.818 -0.194  0.664   0.50 32.56 ?  159  ASN   A HD21 1 
ATOM   3546 H  HD21 T ASN   A 1 159 ? 0.374  1.718   0.891   0.20 22.36 ?  159  ASN   A HD21 1 
ATOM   3547 H  HD22 A ASN   A 1 159 ? 1.665  1.526   0.295   0.30 22.66 ?  159  ASN   A HD22 1 
ATOM   3548 H  HD22 B ASN   A 1 159 ? -0.231 -1.384  -0.013  0.50 32.56 ?  159  ASN   A HD22 1 
ATOM   3549 H  HD22 T ASN   A 1 159 ? 1.638  1.532   0.127   0.20 22.36 ?  159  ASN   A HD22 1 
ATOM   3550 N  N    A LEU   A 1 160 ? 4.983  -2.655  0.971   0.30 16.15 ?  160  LEU   A N    1 
ATOM   3551 N  N    B LEU   A 1 160 ? 4.910  -2.828  0.865   0.50 17.92 ?  160  LEU   A N    1 
ATOM   3552 N  N    T LEU   A 1 160 ? 4.968  -2.663  0.952   0.20 17.79 ?  160  LEU   A N    1 
ATOM   3553 C  CA   A LEU   A 1 160 ? 5.878  -3.672  0.429   0.30 15.83 ?  160  LEU   A CA   1 
ATOM   3554 C  CA   B LEU   A 1 160 ? 5.920  -3.764  0.397   0.50 16.92 ?  160  LEU   A CA   1 
ATOM   3555 C  CA   T LEU   A 1 160 ? 5.857  -3.668  0.381   0.20 17.67 ?  160  LEU   A CA   1 
ATOM   3556 C  C    A LEU   A 1 160 ? 6.068  -4.817  1.415   0.30 15.15 ?  160  LEU   A C    1 
ATOM   3557 C  C    B LEU   A 1 160 ? 6.081  -4.924  1.373   0.50 15.47 ?  160  LEU   A C    1 
ATOM   3558 O  O    A LEU   A 1 160 ? 6.095  -5.988  1.019   0.30 15.18 ?  160  LEU   A O    1 
ATOM   3559 O  O    B LEU   A 1 160 ? 6.097  -6.094  0.973   0.50 15.69 ?  160  LEU   A O    1 
ATOM   3560 C  CB   A LEU   A 1 160 ? 7.224  -3.049  0.065   0.30 15.76 ?  160  LEU   A CB   1 
ATOM   3561 C  CB   B LEU   A 1 160 ? 7.242  -3.024  0.218   0.50 16.82 ?  160  LEU   A CB   1 
ATOM   3562 C  CB   T LEU   A 1 160 ? 7.235  -3.076  0.093   0.20 17.43 ?  160  LEU   A CB   1 
ATOM   3563 C  CG   A LEU   A 1 160 ? 8.301  -4.058  -0.340  0.30 16.12 ?  160  LEU   A CG   1 
ATOM   3564 C  CG   B LEU   A 1 160 ? 8.370  -3.958  -0.185  0.50 17.47 ?  160  LEU   A CG   1 
ATOM   3565 C  CG   T LEU   A 1 160 ? 8.299  -4.090  -0.328  0.20 17.43 ?  160  LEU   A CG   1 
ATOM   3566 C  CD1  A LEU   A 1 160 ? 7.860  -4.856  -1.555  0.30 16.66 ?  160  LEU   A CD1  1 
ATOM   3567 C  CD1  B LEU   A 1 160 ? 7.954  -4.721  -1.422  0.50 18.11 ?  160  LEU   A CD1  1 
ATOM   3568 C  CD1  T LEU   A 1 160 ? 7.859  -4.855  -1.563  0.20 17.65 ?  160  LEU   A CD1  1 
ATOM   3569 C  CD2  A LEU   A 1 160 ? 9.624  -3.361  -0.600  0.30 16.09 ?  160  LEU   A CD2  1 
ATOM   3570 C  CD2  B LEU   A 1 160 ? 9.641  -3.177  -0.427  0.50 17.52 ?  160  LEU   A CD2  1 
ATOM   3571 C  CD2  T LEU   A 1 160 ? 9.629  -3.398  -0.569  0.20 17.27 ?  160  LEU   A CD2  1 
ATOM   3572 H  H    A LEU   A 1 160 ? 5.351  -1.899  1.146   0.30 19.40 ?  160  LEU   A H    1 
ATOM   3573 H  H    B LEU   A 1 160 ? 5.209  -2.049  1.072   0.50 21.52 ?  160  LEU   A H    1 
ATOM   3574 H  H    T LEU   A 1 160 ? 5.357  -1.929  1.178   0.20 21.37 ?  160  LEU   A H    1 
ATOM   3575 H  HA   A LEU   A 1 160 ? 5.486  -4.032  -0.380  0.30 19.02 ?  160  LEU   A HA   1 
ATOM   3576 H  HA   B LEU   A 1 160 ? 5.640  -4.113  -0.462  0.50 20.32 ?  160  LEU   A HA   1 
ATOM   3577 H  HB2  A LEU   A 1 160 ? 7.097  -2.434  -0.677  0.30 18.93 ?  160  LEU   A HB2  1 
ATOM   3578 H  HB2  B LEU   A 1 160 ? 7.145  -2.347  -0.475  0.50 20.20 ?  160  LEU   A HB2  1 
ATOM   3579 H  HB2  T LEU   A 1 160 ? 7.149  -2.412  -0.613  0.20 20.93 ?  160  LEU   A HB2  1 
ATOM   3580 H  HB3  A LEU   A 1 160 ? 7.556  -2.567  0.836   0.30 18.93 ?  160  LEU   A HB3  1 
ATOM   3581 H  HB3  B LEU   A 1 160 ? 7.486  -2.601  1.058   0.50 20.20 ?  160  LEU   A HB3  1 
ATOM   3582 H  HB3  T LEU   A 1 160 ? 7.560  -2.657  0.903   0.20 20.93 ?  160  LEU   A HB3  1 
ATOM   3583 H  HG   A LEU   A 1 160 ? 8.445  -4.679  0.389   0.30 19.37 ?  160  LEU   A HG   1 
ATOM   3584 H  HG   B LEU   A 1 160 ? 8.540  -4.592  0.529   0.50 20.99 ?  160  LEU   A HG   1 
ATOM   3585 H  HG   T LEU   A 1 160 ? 8.424  -4.727  0.393   0.20 20.94 ?  160  LEU   A HG   1 
ATOM   3586 H  HD11 A LEU   A 1 160 ? 8.596  -5.414  -1.848  0.30 20.02 ?  160  LEU   A HD11 1 
ATOM   3587 H  HD11 B LEU   A 1 160 ? 8.723  -5.180  -1.770  0.50 21.76 ?  160  LEU   A HD11 1 
ATOM   3588 H  HD11 T LEU   A 1 160 ? 8.592  -5.416  -1.862  0.20 21.20 ?  160  LEU   A HD11 1 
ATOM   3589 H  HD12 A LEU   A 1 160 ? 7.102  -5.411  -1.310  0.30 20.02 ?  160  LEU   A HD12 1 
ATOM   3590 H  HD12 B LEU   A 1 160 ? 7.269  -5.368  -1.186  0.50 21.76 ?  160  LEU   A HD12 1 
ATOM   3591 H  HD12 T LEU   A 1 160 ? 7.093  -5.405  -1.337  0.20 21.20 ?  160  LEU   A HD12 1 
ATOM   3592 H  HD13 A LEU   A 1 160 ? 7.607  -4.242  -2.261  0.30 20.02 ?  160  LEU   A HD13 1 
ATOM   3593 H  HD13 B LEU   A 1 160 ? 7.607  -4.094  -2.079  0.50 21.76 ?  160  LEU   A HD13 1 
ATOM   3594 H  HD13 T LEU   A 1 160 ? 7.621  -4.222  -2.257  0.20 21.20 ?  160  LEU   A HD13 1 
ATOM   3595 H  HD21 A LEU   A 1 160 ? 10.286 -4.025  -0.852  0.30 19.33 ?  160  LEU   A HD21 1 
ATOM   3596 H  HD21 B LEU   A 1 160 ? 10.347 -3.792  -0.680  0.50 21.04 ?  160  LEU   A HD21 1 
ATOM   3597 H  HD21 T LEU   A 1 160 ? 10.286 -4.062  -0.832  0.20 20.75 ?  160  LEU   A HD21 1 
ATOM   3598 H  HD22 A LEU   A 1 160 ? 9.509  -2.720  -1.319  0.30 19.33 ?  160  LEU   A HD22 1 
ATOM   3599 H  HD22 B LEU   A 1 160 ? 9.488  -2.537  -1.141  0.50 21.04 ?  160  LEU   A HD22 1 
ATOM   3600 H  HD22 T LEU   A 1 160 ? 9.519  -2.743  -1.276  0.20 20.75 ?  160  LEU   A HD22 1 
ATOM   3601 H  HD23 A LEU   A 1 160 ? 9.906  -2.904  0.208   0.30 19.33 ?  160  LEU   A HD23 1 
ATOM   3602 H  HD23 B LEU   A 1 160 ? 9.887  -2.709  0.388   0.50 21.04 ?  160  LEU   A HD23 1 
ATOM   3603 H  HD23 T LEU   A 1 160 ? 9.911  -2.959  0.249   0.20 20.75 ?  160  LEU   A HD23 1 
ATOM   3604 N  N    A TYR   A 1 161 ? 6.207  -4.498  2.702   0.50 15.38 ?  161  TYR   A N    1 
ATOM   3605 N  N    B TYR   A 1 161 ? 6.211  -4.610  2.660   0.50 15.49 ?  161  TYR   A N    1 
ATOM   3606 C  CA   A TYR   A 1 161 ? 6.336  -5.541  3.713   0.50 14.96 ?  161  TYR   A CA   1 
ATOM   3607 C  CA   B TYR   A 1 161 ? 6.314  -5.649  3.677   0.50 14.99 ?  161  TYR   A CA   1 
ATOM   3608 C  C    A TYR   A 1 161 ? 5.174  -6.520  3.635   0.50 15.55 ?  161  TYR   A C    1 
ATOM   3609 C  C    B TYR   A 1 161 ? 5.161  -6.644  3.579   0.50 15.13 ?  161  TYR   A C    1 
ATOM   3610 O  O    A TYR   A 1 161 ? 5.374  -7.737  3.547   0.50 15.21 ?  161  TYR   A O    1 
ATOM   3611 O  O    B TYR   A 1 161 ? 5.367  -7.858  3.688   0.50 14.69 ?  161  TYR   A O    1 
ATOM   3612 C  CB   A TYR   A 1 161 ? 6.414  -4.916  5.106   0.50 14.78 ?  161  TYR   A CB   1 
ATOM   3613 C  CB   B TYR   A 1 161 ? 6.368  -4.996  5.059   0.50 15.15 ?  161  TYR   A CB   1 
ATOM   3614 C  CG   A TYR   A 1 161 ? 6.311  -5.939  6.211   0.50 14.08 ?  161  TYR   A CG   1 
ATOM   3615 C  CG   B TYR   A 1 161 ? 6.183  -5.960  6.205   0.50 15.01 ?  161  TYR   A CG   1 
ATOM   3616 C  CD1  A TYR   A 1 161 ? 7.421  -6.665  6.609   0.50 14.29 ?  161  TYR   A CD1  1 
ATOM   3617 C  CD1  B TYR   A 1 161 ? 7.262  -6.642  6.751   0.50 15.21 ?  161  TYR   A CD1  1 
ATOM   3618 C  CD2  A TYR   A 1 161 ? 5.103  -6.184  6.854   0.50 14.03 ?  161  TYR   A CD2  1 
ATOM   3619 C  CD2  B TYR   A 1 161 ? 4.926  -6.186  6.745   0.50 15.50 ?  161  TYR   A CD2  1 
ATOM   3620 C  CE1  A TYR   A 1 161 ? 7.337  -7.607  7.610   0.50 14.41 ?  161  TYR   A CE1  1 
ATOM   3621 C  CE1  B TYR   A 1 161 ? 7.088  -7.530  7.799   0.50 15.53 ?  161  TYR   A CE1  1 
ATOM   3622 C  CE2  A TYR   A 1 161 ? 5.009  -7.129  7.862   0.50 14.23 ?  161  TYR   A CE2  1 
ATOM   3623 C  CE2  B TYR   A 1 161 ? 4.743  -7.067  7.788   0.50 15.88 ?  161  TYR   A CE2  1 
ATOM   3624 C  CZ   A TYR   A 1 161 ? 6.131  -7.837  8.235   0.50 14.82 ?  161  TYR   A CZ   1 
ATOM   3625 C  CZ   B TYR   A 1 161 ? 5.822  -7.736  8.313   0.50 16.19 ?  161  TYR   A CZ   1 
ATOM   3626 O  OH   A TYR   A 1 161 ? 6.059  -8.781  9.237   0.50 15.38 ?  161  TYR   A OH   1 
ATOM   3627 O  OH   B TYR   A 1 161 ? 5.629  -8.615  9.356   0.50 17.44 ?  161  TYR   A OH   1 
ATOM   3628 H  H    A TYR   A 1 161 ? 6.220  -3.700  3.011   0.50 18.48 ?  161  TYR   A H    1 
ATOM   3629 H  H    B TYR   A 1 161 ? 6.245  -3.812  2.965   0.50 18.61 ?  161  TYR   A H    1 
ATOM   3630 H  HA   A TYR   A 1 161 ? 7.151  -6.038  3.560   0.50 17.98 ?  161  TYR   A HA   1 
ATOM   3631 H  HA   B TYR   A 1 161 ? 7.133  -6.143  3.543   0.50 18.01 ?  161  TYR   A HA   1 
ATOM   3632 H  HB2  A TYR   A 1 161 ? 7.266  -4.462  5.200   0.50 17.76 ?  161  TYR   A HB2  1 
ATOM   3633 H  HB2  B TYR   A 1 161 ? 7.234  -4.574  5.165   0.50 18.20 ?  161  TYR   A HB2  1 
ATOM   3634 H  HB3  A TYR   A 1 161 ? 5.687  -4.286  5.215   0.50 17.76 ?  161  TYR   A HB3  1 
ATOM   3635 H  HB3  B TYR   A 1 161 ? 5.667  -4.330  5.119   0.50 18.20 ?  161  TYR   A HB3  1 
ATOM   3636 H  HD1  A TYR   A 1 161 ? 8.238  -6.518  6.192   0.50 17.17 ?  161  TYR   A HD1  1 
ATOM   3637 H  HD1  B TYR   A 1 161 ? 8.115  -6.506  6.406   0.50 18.27 ?  161  TYR   A HD1  1 
ATOM   3638 H  HD2  A TYR   A 1 161 ? 4.343  -5.711  6.604   0.50 16.86 ?  161  TYR   A HD2  1 
ATOM   3639 H  HD2  B TYR   A 1 161 ? 4.191  -5.740  6.396   0.50 18.63 ?  161  TYR   A HD2  1 
ATOM   3640 H  HE1  A TYR   A 1 161 ? 8.092  -8.089  7.869   0.50 17.31 ?  161  TYR   A HE1  1 
ATOM   3641 H  HE1  B TYR   A 1 161 ? 7.821  -7.984  8.157   0.50 18.66 ?  161  TYR   A HE1  1 
ATOM   3642 H  HE2  A TYR   A 1 161 ? 4.192  -7.286  8.286   0.50 17.10 ?  161  TYR   A HE2  1 
ATOM   3643 H  HE2  B TYR   A 1 161 ? 3.892  -7.212  8.141   0.50 19.08 ?  161  TYR   A HE2  1 
ATOM   3644 H  HH   A TYR   A 1 161 ? 5.268  -8.824  9.536   0.50 18.47 ?  161  TYR   A HH   1 
ATOM   3645 H  HH   B TYR   A 1 161 ? 4.817  -8.646  9.567   0.50 20.95 ?  161  TYR   A HH   1 
ATOM   3646 N  N    A ASP   A 1 162 ? 3.943  -6.004  3.671   0.50 16.31 ?  162  ASP   A N    1 
ATOM   3647 N  N    B ASP   A 1 162 ? 3.935  -6.150  3.369   0.50 15.61 ?  162  ASP   A N    1 
ATOM   3648 C  CA   A ASP   A 1 162 ? 2.778  -6.879  3.582   0.50 16.98 ?  162  ASP   A CA   1 
ATOM   3649 C  CA   B ASP   A 1 162 ? 2.778  -7.042  3.288   0.50 16.25 ?  162  ASP   A CA   1 
ATOM   3650 C  C    A ASP   A 1 162 ? 2.810  -7.706  2.304   0.50 17.38 ?  162  ASP   A C    1 
ATOM   3651 C  C    B ASP   A 1 162 ? 2.885  -7.980  2.090   0.50 16.26 ?  162  ASP   A C    1 
ATOM   3652 O  O    A ASP   A 1 162 ? 2.440  -8.886  2.310   0.50 17.71 ?  162  ASP   A O    1 
ATOM   3653 O  O    B ASP   A 1 162 ? 2.573  -9.173  2.193   0.50 16.66 ?  162  ASP   A O    1 
ATOM   3654 C  CB   A ASP   A 1 162 ? 1.487  -6.062  3.642   0.50 17.45 ?  162  ASP   A CB   1 
ATOM   3655 C  CB   B ASP   A 1 162 ? 1.481  -6.225  3.211   0.50 17.54 ?  162  ASP   A CB   1 
ATOM   3656 C  CG   A ASP   A 1 162 ? 1.191  -5.519  5.024   0.50 18.15 ?  162  ASP   A CG   1 
ATOM   3657 C  CG   B ASP   A 1 162 ? 1.187  -5.453  4.486   0.50 18.56 ?  162  ASP   A CG   1 
ATOM   3658 O  OD1  A ASP   A 1 162 ? 1.908  -5.862  5.986   0.50 18.83 ?  162  ASP   A OD1  1 
ATOM   3659 O  OD1  B ASP   A 1 162 ? 1.647  -5.870  5.567   0.50 18.68 ?  162  ASP   A OD1  1 
ATOM   3660 O  OD2  A ASP   A 1 162 ? 0.218  -4.745  5.140   0.50 18.58 -1 162  ASP   A OD2  1 
ATOM   3661 O  OD2  B ASP   A 1 162 ? 0.464  -4.434  4.407   0.50 19.26 -1 162  ASP   A OD2  1 
ATOM   3662 H  H    A ASP   A 1 162 ? 3.756  -5.165  3.742   0.50 19.59 ?  162  ASP   A H    1 
ATOM   3663 H  H    B ASP   A 1 162 ? 3.745  -5.319  3.275   0.50 18.75 ?  162  ASP   A H    1 
ATOM   3664 H  HA   A ASP   A 1 162 ? 2.780  -7.490  4.334   0.50 20.39 ?  162  ASP   A HA   1 
ATOM   3665 H  HA   B ASP   A 1 162 ? 2.730  -7.586  4.087   0.50 19.52 ?  162  ASP   A HA   1 
ATOM   3666 H  HB2  A ASP   A 1 162 ? 1.558  -5.310  3.038   0.50 20.96 ?  162  ASP   A HB2  1 
ATOM   3667 H  HB2  B ASP   A 1 162 ? 1.540  -5.588  2.482   0.50 21.07 ?  162  ASP   A HB2  1 
ATOM   3668 H  HB3  A ASP   A 1 162 ? 0.741  -6.628  3.387   0.50 20.96 ?  162  ASP   A HB3  1 
ATOM   3669 H  HB3  B ASP   A 1 162 ? 0.727  -6.820  3.067   0.50 21.07 ?  162  ASP   A HB3  1 
ATOM   3670 N  N    A LYS   A 1 163 ? 3.233  -7.101  1.192   0.50 18.13 ?  163  LYS   A N    1 
ATOM   3671 N  N    B LYS   A 1 163 ? 3.324  -7.455  0.945   0.50 16.80 ?  163  LYS   A N    1 
ATOM   3672 C  CA   A LYS   A 1 163 ? 3.340  -7.863  -0.047  0.50 19.16 ?  163  LYS   A CA   1 
ATOM   3673 C  CA   B LYS   A 1 163 ? 3.466  -8.269  -0.258  0.50 18.12 ?  163  LYS   A CA   1 
ATOM   3674 C  C    A LYS   A 1 163 ? 4.424  -8.927  0.051   0.50 18.08 ?  163  LYS   A C    1 
ATOM   3675 C  C    B LYS   A 1 163 ? 4.552  -9.329  -0.088  0.50 17.25 ?  163  LYS   A C    1 
ATOM   3676 O  O    A LYS   A 1 163 ? 4.260  -10.032 -0.475  0.50 18.24 ?  163  LYS   A O    1 
ATOM   3677 O  O    B LYS   A 1 163 ? 4.391  -10.471 -0.535  0.50 18.19 ?  163  LYS   A O    1 
ATOM   3678 C  CB   A LYS   A 1 163 ? 3.613  -6.939  -1.233  0.50 21.67 ?  163  LYS   A CB   1 
ATOM   3679 C  CB   B LYS   A 1 163 ? 3.771  -7.343  -1.438  0.50 20.98 ?  163  LYS   A CB   1 
ATOM   3680 C  CG   A LYS   A 1 163 ? 3.673  -7.678  -2.566  0.50 24.61 ?  163  LYS   A CG   1 
ATOM   3681 C  CG   B LYS   A 1 163 ? 3.876  -8.023  -2.784  0.50 24.44 ?  163  LYS   A CG   1 
ATOM   3682 C  CD   A LYS   A 1 163 ? 4.093  -6.766  -3.701  0.50 27.30 ?  163  LYS   A CD   1 
ATOM   3683 C  CD   B LYS   A 1 163 ? 3.615  -7.039  -3.922  0.50 27.73 ?  163  LYS   A CD   1 
ATOM   3684 C  CE   A LYS   A 1 163 ? 4.042  -7.487  -5.039  0.50 29.58 ?  163  LYS   A CE   1 
ATOM   3685 C  CE   B LYS   A 1 163 ? 4.842  -6.849  -4.796  0.50 30.18 ?  163  LYS   A CE   1 
ATOM   3686 N  NZ   A LYS   A 1 163 ? 4.675  -6.687  -6.124  0.50 30.78 ?  163  LYS   A NZ   1 
ATOM   3687 N  NZ   B LYS   A 1 163 ? 4.515  -6.320  -6.147  0.50 31.67 ?  163  LYS   A NZ   1 
ATOM   3688 H  H    A LYS   A 1 163 ? 3.450  -6.271  1.130   0.50 21.78 ?  163  LYS   A H    1 
ATOM   3689 H  H    B LYS   A 1 163 ? 3.548  -6.631  0.841   0.50 20.19 ?  163  LYS   A H    1 
ATOM   3690 H  HA   A LYS   A 1 163 ? 2.499  -8.317  -0.208  0.50 23.01 ?  163  LYS   A HA   1 
ATOM   3691 H  HA   B LYS   A 1 163 ? 2.624  -8.718  -0.441  0.50 21.77 ?  163  LYS   A HA   1 
ATOM   3692 H  HB2  A LYS   A 1 163 ? 2.900  -6.283  -1.289  0.50 26.02 ?  163  LYS   A HB2  1 
ATOM   3693 H  HB2  B LYS   A 1 163 ? 3.061  -6.683  -1.497  0.50 25.20 ?  163  LYS   A HB2  1 
ATOM   3694 H  HB3  A LYS   A 1 163 ? 4.463  -6.496  -1.099  0.50 26.02 ?  163  LYS   A HB3  1 
ATOM   3695 H  HB3  B LYS   A 1 163 ? 4.615  -6.896  -1.272  0.50 25.20 ?  163  LYS   A HB3  1 
ATOM   3696 H  HG2  A LYS   A 1 163 ? 4.319  -8.400  -2.509  0.50 29.55 ?  163  LYS   A HG2  1 
ATOM   3697 H  HG2  B LYS   A 1 163 ? 4.770  -8.384  -2.889  0.50 29.35 ?  163  LYS   A HG2  1 
ATOM   3698 H  HG3  A LYS   A 1 163 ? 2.794  -8.036  -2.771  0.50 29.55 ?  163  LYS   A HG3  1 
ATOM   3699 H  HG3  B LYS   A 1 163 ? 3.218  -8.730  -2.839  0.50 29.35 ?  163  LYS   A HG3  1 
ATOM   3700 H  HD2  A LYS   A 1 163 ? 3.490  -6.008  -3.740  0.50 32.78 ?  163  LYS   A HD2  1 
ATOM   3701 H  HD2  B LYS   A 1 163 ? 2.897  -7.377  -4.476  0.50 33.30 ?  163  LYS   A HD2  1 
ATOM   3702 H  HD3  A LYS   A 1 163 ? 5.002  -6.467  -3.550  0.50 32.78 ?  163  LYS   A HD3  1 
ATOM   3703 H  HD3  B LYS   A 1 163 ? 3.374  -6.172  -3.555  0.50 33.30 ?  163  LYS   A HD3  1 
ATOM   3704 H  HE2  A LYS   A 1 163 ? 4.513  -8.332  -4.966  0.50 35.51 ?  163  LYS   A HE2  1 
ATOM   3705 H  HE2  B LYS   A 1 163 ? 5.450  -6.228  -4.365  0.50 36.24 ?  163  LYS   A HE2  1 
ATOM   3706 H  HE3  A LYS   A 1 163 ? 3.116  -7.643  -5.281  0.50 35.51 ?  163  LYS   A HE3  1 
ATOM   3707 H  HE3  B LYS   A 1 163 ? 5.271  -7.704  -4.914  0.50 36.24 ?  163  LYS   A HE3  1 
ATOM   3708 H  HZ1  A LYS   A 1 163 ? 4.632  -7.130  -6.894  0.50 36.96 ?  163  LYS   A HZ1  1 
ATOM   3709 H  HZ1  B LYS   A 1 163 ? 5.261  -6.228  -6.626  0.50 38.02 ?  163  LYS   A HZ1  1 
ATOM   3710 H  HZ2  A LYS   A 1 163 ? 4.251  -5.909  -6.214  0.50 36.96 ?  163  LYS   A HZ2  1 
ATOM   3711 H  HZ2  B LYS   A 1 163 ? 3.970  -6.884  -6.570  0.50 38.02 ?  163  LYS   A HZ2  1 
ATOM   3712 H  HZ3  A LYS   A 1 163 ? 5.529  -6.529  -5.927  0.50 36.96 ?  163  LYS   A HZ3  1 
ATOM   3713 H  HZ3  B LYS   A 1 163 ? 4.117  -5.530  -6.076  0.50 38.02 ?  163  LYS   A HZ3  1 
ATOM   3714 N  N    A LEU   A 1 164 ? 5.545  -8.609  0.704   0.50 16.48 ?  164  LEU   A N    1 
ATOM   3715 N  N    B LEU   A 1 164 ? 5.663  -8.965  0.559   0.50 15.48 ?  164  LEU   A N    1 
ATOM   3716 C  CA   A LEU   A 1 164 ? 6.625  -9.586  0.822   0.50 15.83 ?  164  LEU   A CA   1 
ATOM   3717 C  CA   B LEU   A 1 164 ? 6.759  -9.908  0.782   0.50 14.83 ?  164  LEU   A CA   1 
ATOM   3718 C  C    A LEU   A 1 164 ? 6.194  -10.776 1.667   0.50 15.92 ?  164  LEU   A C    1 
ATOM   3719 C  C    B LEU   A 1 164 ? 6.315  -11.078 1.651   0.50 14.89 ?  164  LEU   A C    1 
ATOM   3720 O  O    A LEU   A 1 164 ? 6.436  -11.932 1.301   0.50 16.32 ?  164  LEU   A O    1 
ATOM   3721 O  O    B LEU   A 1 164 ? 6.686  -12.230 1.396   0.50 14.83 ?  164  LEU   A O    1 
ATOM   3722 C  CB   A LEU   A 1 164 ? 7.866  -8.928  1.416   0.50 15.22 ?  164  LEU   A CB   1 
ATOM   3723 C  CB   B LEU   A 1 164 ? 7.924  -9.186  1.459   0.50 14.49 ?  164  LEU   A CB   1 
ATOM   3724 C  CG   A LEU   A 1 164 ? 8.660  -8.057  0.447   0.50 15.14 ?  164  LEU   A CG   1 
ATOM   3725 C  CG   B LEU   A 1 164 ? 8.643  -8.099  0.661   0.50 14.96 ?  164  LEU   A CG   1 
ATOM   3726 C  CD1  A LEU   A 1 164 ? 9.592  -7.164  1.235   0.50 14.25 ?  164  LEU   A CD1  1 
ATOM   3727 C  CD1  B LEU   A 1 164 ? 9.558  -7.272  1.560   0.50 14.72 ?  164  LEU   A CD1  1 
ATOM   3728 C  CD2  A LEU   A 1 164 ? 9.439  -8.908  -0.548  0.50 15.76 ?  164  LEU   A CD2  1 
ATOM   3729 C  CD2  B LEU   A 1 164 ? 9.438  -8.724  -0.465  0.50 15.79 ?  164  LEU   A CD2  1 
ATOM   3730 H  H    A LEU   A 1 164 ? 5.703  -7.848  1.083   0.50 19.80 ?  164  LEU   A H    1 
ATOM   3731 H  H    B LEU   A 1 164 ? 5.803  -8.185  0.878   0.50 18.60 ?  164  LEU   A H    1 
ATOM   3732 H  HA   A LEU   A 1 164 ? 6.851  -9.911  -0.061  0.50 19.02 ?  164  LEU   A HA   1 
ATOM   3733 H  HA   B LEU   A 1 164 ? 7.062  -10.261 -0.070  0.50 17.82 ?  164  LEU   A HA   1 
ATOM   3734 H  HB2  A LEU   A 1 164 ? 7.593  -8.366  2.157   0.50 18.28 ?  164  LEU   A HB2  1 
ATOM   3735 H  HB2  B LEU   A 1 164 ? 7.587  -8.772  2.268   0.50 17.41 ?  164  LEU   A HB2  1 
ATOM   3736 H  HB3  A LEU   A 1 164 ? 8.460  -9.624  1.736   0.50 18.28 ?  164  LEU   A HB3  1 
ATOM   3737 H  HB3  B LEU   A 1 164 ? 8.589  -9.850  1.696   0.50 17.41 ?  164  LEU   A HB3  1 
ATOM   3738 H  HG   A LEU   A 1 164 ? 8.047  -7.492  -0.049  0.50 18.19 ?  164  LEU   A HG   1 
ATOM   3739 H  HG   B LEU   A 1 164 ? 7.988  -7.499  0.274   0.50 17.98 ?  164  LEU   A HG   1 
ATOM   3740 H  HD11 A LEU   A 1 164 ? 10.109 -6.627  0.618   0.50 17.13 ?  164  LEU   A HD11 1 
ATOM   3741 H  HD11 B LEU   A 1 164 ? 9.999  -6.591  1.026   0.50 17.69 ?  164  LEU   A HD11 1 
ATOM   3742 H  HD12 A LEU   A 1 164 ? 9.063  -6.592  1.814   0.50 17.13 ?  164  LEU   A HD12 1 
ATOM   3743 H  HD12 B LEU   A 1 164 ? 9.027  -6.851  2.256   0.50 17.69 ?  164  LEU   A HD12 1 
ATOM   3744 H  HD13 A LEU   A 1 164 ? 10.181 -7.720  1.769   0.50 17.13 ?  164  LEU   A HD13 1 
ATOM   3745 H  HD13 B LEU   A 1 164 ? 10.222 -7.856  1.962   0.50 17.69 ?  164  LEU   A HD13 1 
ATOM   3746 H  HD21 A LEU   A 1 164 ? 9.976  -8.324  -1.109  0.50 18.94 ?  164  LEU   A HD21 1 
ATOM   3747 H  HD21 B LEU   A 1 164 ? 9.922  -8.025  -0.933  0.50 18.97 ?  164  LEU   A HD21 1 
ATOM   3748 H  HD22 A LEU   A 1 164 ? 10.013 -9.518  -0.062  0.50 18.94 ?  164  LEU   A HD22 1 
ATOM   3749 H  HD22 B LEU   A 1 164 ? 10.062 -9.364  -0.091  0.50 18.97 ?  164  LEU   A HD22 1 
ATOM   3750 H  HD23 A LEU   A 1 164 ? 8.813  -9.406  -1.098  0.50 18.94 ?  164  LEU   A HD23 1 
ATOM   3751 H  HD23 B LEU   A 1 164 ? 8.826  -9.168  -1.070  0.50 18.97 ?  164  LEU   A HD23 1 
ATOM   3752 N  N    A VAL   A 1 165 ? 5.555  -10.513 2.806   0.50 14.82 ?  165  VAL   A N    1 
ATOM   3753 N  N    B VAL   A 1 165 ? 5.540  -10.797 2.696   0.50 14.71 ?  165  VAL   A N    1 
ATOM   3754 C  CA   A VAL   A 1 165 ? 5.073  -11.603 3.648   0.50 14.98 ?  165  VAL   A CA   1 
ATOM   3755 C  CA   B VAL   A 1 165 ? 5.080  -11.851 3.593   0.50 14.61 ?  165  VAL   A CA   1 
ATOM   3756 C  C    A VAL   A 1 165 ? 4.023  -12.416 2.905   0.50 14.85 ?  165  VAL   A C    1 
ATOM   3757 C  C    B VAL   A 1 165 ? 4.098  -12.772 2.877   0.50 14.58 ?  165  VAL   A C    1 
ATOM   3758 O  O    A VAL   A 1 165 ? 4.113  -13.645 2.811   0.50 15.22 ?  165  VAL   A O    1 
ATOM   3759 O  O    B VAL   A 1 165 ? 4.231  -14.001 2.917   0.50 14.84 ?  165  VAL   A O    1 
ATOM   3760 C  CB   A VAL   A 1 165 ? 4.541  -11.053 4.984   0.50 15.48 ?  165  VAL   A CB   1 
ATOM   3761 C  CB   B VAL   A 1 165 ? 4.466  -11.233 4.863   0.50 15.13 ?  165  VAL   A CB   1 
ATOM   3762 C  CG1  A VAL   A 1 165 ? 3.734  -12.116 5.721   0.50 15.91 ?  165  VAL   A CG1  1 
ATOM   3763 C  CG1  B VAL   A 1 165 ? 3.865  -12.314 5.745   0.50 15.63 ?  165  VAL   A CG1  1 
ATOM   3764 C  CG2  A VAL   A 1 165 ? 5.694  -10.552 5.838   0.50 15.53 ?  165  VAL   A CG2  1 
ATOM   3765 C  CG2  B VAL   A 1 165 ? 5.507  -10.423 5.631   0.50 15.08 ?  165  VAL   A CG2  1 
ATOM   3766 H  H    A VAL   A 1 165 ? 5.381  -9.727  3.105   0.50 17.80 ?  165  VAL   A H    1 
ATOM   3767 H  H    B VAL   A 1 165 ? 5.267  -10.016 2.907   0.50 17.67 ?  165  VAL   A H    1 
ATOM   3768 H  HA   A VAL   A 1 165 ? 5.810  -12.197 3.849   0.50 17.99 ?  165  VAL   A HA   1 
ATOM   3769 H  HA   B VAL   A 1 165 ? 5.839  -12.390 3.866   0.50 17.56 ?  165  VAL   A HA   1 
ATOM   3770 H  HB   A VAL   A 1 165 ? 3.954  -10.303 4.809   0.50 18.60 ?  165  VAL   A HB   1 
ATOM   3771 H  HB   B VAL   A 1 165 ? 3.751  -10.631 4.605   0.50 18.17 ?  165  VAL   A HB   1 
ATOM   3772 H  HG11 A VAL   A 1 165 ? 3.655  -11.859 6.654   0.50 19.11 ?  165  VAL   A HG11 1 
ATOM   3773 H  HG11 B VAL   A 1 165 ? 3.711  -11.945 6.629   0.50 18.78 ?  165  VAL   A HG11 1 
ATOM   3774 H  HG12 A VAL   A 1 165 ? 2.851  -12.177 5.324   0.50 19.11 ?  165  VAL   A HG12 1 
ATOM   3775 H  HG12 B VAL   A 1 165 ? 3.025  -12.607 5.360   0.50 18.78 ?  165  VAL   A HG12 1 
ATOM   3776 H  HG13 A VAL   A 1 165 ? 4.192  -12.967 5.652   0.50 19.11 ?  165  VAL   A HG13 1 
ATOM   3777 H  HG13 B VAL   A 1 165 ? 4.486  -13.055 5.801   0.50 18.78 ?  165  VAL   A HG13 1 
ATOM   3778 H  HG21 A VAL   A 1 165 ? 5.344  -10.204 6.672   0.50 18.66 ?  165  VAL   A HG21 1 
ATOM   3779 H  HG21 B VAL   A 1 165 ? 5.074  -9.972  6.374   0.50 18.12 ?  165  VAL   A HG21 1 
ATOM   3780 H  HG22 A VAL   A 1 165 ? 6.302  -11.287 6.013   0.50 18.66 ?  165  VAL   A HG22 1 
ATOM   3781 H  HG22 B VAL   A 1 165 ? 6.194  -11.020 5.964   0.50 18.12 ?  165  VAL   A HG22 1 
ATOM   3782 H  HG23 A VAL   A 1 165 ? 6.158  -9.848  5.355   0.50 18.66 ?  165  VAL   A HG23 1 
ATOM   3783 H  HG23 B VAL   A 1 165 ? 5.902  -9.765  5.036   0.50 18.12 ?  165  VAL   A HG23 1 
ATOM   3784 N  N    A SER   A 1 166 ? 3.014  -11.740 2.356   0.50 14.94 ?  166  SER   A N    1 
ATOM   3785 N  N    B SER   A 1 166 ? 3.100  -12.189 2.203   0.50 14.86 ?  166  SER   A N    1 
ATOM   3786 C  CA   A SER   A 1 166 ? 1.907  -12.458 1.737   0.50 15.60 ?  166  SER   A CA   1 
ATOM   3787 C  CA   B SER   A 1 166 ? 2.013  -12.983 1.632   0.50 15.39 ?  166  SER   A CA   1 
ATOM   3788 C  C    A SER   A 1 166 ? 2.324  -13.241 0.498   0.50 15.57 ?  166  SER   A C    1 
ATOM   3789 C  C    B SER   A 1 166 ? 2.524  -13.942 0.573   0.50 15.95 ?  166  SER   A C    1 
ATOM   3790 O  O    A SER   A 1 166 ? 1.611  -14.175 0.107   0.50 16.61 ?  166  SER   A O    1 
ATOM   3791 O  O    B SER   A 1 166 ? 2.015  -15.064 0.440   0.50 16.23 ?  166  SER   A O    1 
ATOM   3792 C  CB   A SER   A 1 166 ? 0.772  -11.494 1.385   0.50 16.97 ?  166  SER   A CB   1 
ATOM   3793 C  CB   B SER   A 1 166 ? 0.956  -12.064 1.017   0.50 15.90 ?  166  SER   A CB   1 
ATOM   3794 O  OG   A SER   A 1 166 ? 0.149  -10.967 2.549   0.50 18.56 ?  166  SER   A OG   1 
ATOM   3795 O  OG   B SER   A 1 166 ? 0.297  -11.300 2.009   0.50 17.16 ?  166  SER   A OG   1 
ATOM   3796 H  H    A SER   A 1 166 ? 2.932  -10.882 2.352   0.50 17.96 ?  166  SER   A H    1 
ATOM   3797 H  H    B SER   A 1 166 ? 3.029  -11.354 2.066   0.50 17.86 ?  166  SER   A H    1 
ATOM   3798 H  HA   A SER   A 1 166 ? 1.549  -13.096 2.376   0.50 18.74 ?  166  SER   A HA   1 
ATOM   3799 H  HA   B SER   A 1 166 ? 1.587  -13.511 2.327   0.50 18.48 ?  166  SER   A HA   1 
ATOM   3800 H  HB2  A SER   A 1 166 ? 1.127  -10.768 0.854   0.50 20.38 ?  166  SER   A HB2  1 
ATOM   3801 H  HB2  B SER   A 1 166 ? 1.386  -11.466 0.387   0.50 19.10 ?  166  SER   A HB2  1 
ATOM   3802 H  HB3  A SER   A 1 166 ? 0.095  -11.974 0.879   0.50 20.38 ?  166  SER   A HB3  1 
ATOM   3803 H  HB3  B SER   A 1 166 ? 0.293  -12.605 0.552   0.50 19.10 ?  166  SER   A HB3  1 
ATOM   3804 H  HG   A SER   A 1 166 ? -0.456 -10.427 2.335   0.50 22.29 ?  166  SER   A HG   1 
ATOM   3805 H  HG   B SER   A 1 166 ? 0.854  -10.816 2.415   0.50 20.61 ?  166  SER   A HG   1 
ATOM   3806 N  N    A SER   A 1 167 ? 3.443  -12.889 -0.137  0.50 15.21 ?  167  SER   A N    1 
ATOM   3807 N  N    B SER   A 1 167 ? 3.509  -13.506 -0.204  0.50 16.77 ?  167  SER   A N    1 
ATOM   3808 C  CA   A SER   A 1 167 ? 3.905  -13.608 -1.318  0.50 15.43 ?  167  SER   A CA   1 
ATOM   3809 C  CA   B SER   A 1 167 ? 4.116  -14.325 -1.246  0.50 18.45 ?  167  SER   A CA   1 
ATOM   3810 C  C    A SER   A 1 167 ? 5.036  -14.592 -1.023  0.50 15.58 ?  167  SER   A C    1 
ATOM   3811 C  C    B SER   A 1 167 ? 5.447  -14.880 -0.762  0.50 20.00 ?  167  SER   A C    1 
ATOM   3812 O  O    A SER   A 1 167 ? 5.543  -15.234 -1.950  0.50 15.63 ?  167  SER   A O    1 
ATOM   3813 O  O    B SER   A 1 167 ? 6.509  -14.552 -1.290  0.50 22.38 ?  167  SER   A O    1 
ATOM   3814 C  CB   A SER   A 1 167 ? 4.348  -12.626 -2.414  0.50 15.44 ?  167  SER   A CB   1 
ATOM   3815 C  CB   B SER   A 1 167 ? 4.319  -13.496 -2.505  0.50 18.65 ?  167  SER   A CB   1 
ATOM   3816 O  OG   A SER   A 1 167 ? 5.410  -11.795 -1.963  0.50 15.66 ?  167  SER   A OG   1 
ATOM   3817 O  OG   B SER   A 1 167 ? 5.423  -12.619 -2.345  0.50 18.70 ?  167  SER   A OG   1 
ATOM   3818 H  H    A SER   A 1 167 ? 3.947  -12.224 0.097   0.50 18.28 ?  167  SER   A H    1 
ATOM   3819 H  H    B SER   A 1 167 ? 3.846  -12.714 -0.152  0.50 20.15 ?  167  SER   A H    1 
ATOM   3820 H  HA   A SER   A 1 167 ? 3.156  -14.109 -1.672  0.50 18.54 ?  167  SER   A HA   1 
ATOM   3821 H  HA   B SER   A 1 167 ? 3.555  -15.079 -1.448  0.50 22.17 ?  167  SER   A HA   1 
ATOM   3822 H  HB2  A SER   A 1 167 ? 4.650  -13.138 -3.183  0.50 18.56 ?  167  SER   A HB2  1 
ATOM   3823 H  HB2  B SER   A 1 167 ? 4.491  -14.092 -3.249  0.50 22.40 ?  167  SER   A HB2  1 
ATOM   3824 H  HB3  A SER   A 1 167 ? 3.585  -12.076 -2.672  0.50 18.56 ?  167  SER   A HB3  1 
ATOM   3825 H  HB3  B SER   A 1 167 ? 3.522  -12.974 -2.669  0.50 22.40 ?  167  SER   A HB3  1 
ATOM   3826 H  HG   A SER   A 1 167 ? 5.142  -11.335 -1.312  0.50 18.81 ?  167  SER   A HG   1 
ATOM   3827 H  HG   B SER   A 1 167 ? 6.145  -13.049 -2.388  0.50 22.47 ?  167  SER   A HG   1 
ATOM   3828 N  N    A PHE   A 1 168 ? 5.445  -14.736 0.234   0.50 15.08 ?  168  PHE   A N    1 
ATOM   3829 N  N    B PHE   A 1 168 ? 5.390  -15.725 0.262   0.50 18.01 ?  168  PHE   A N    1 
ATOM   3830 C  CA   A PHE   A 1 168 ? 6.630  -15.530 0.519   0.50 15.52 ?  168  PHE   A CA   1 
ATOM   3831 C  CA   B PHE   A 1 168 ? 6.621  -16.362 0.708   0.50 16.67 ?  168  PHE   A CA   1 
ATOM   3832 C  C    A PHE   A 1 168 ? 6.332  -17.016 0.391   0.50 16.99 ?  168  PHE   A C    1 
ATOM   3833 C  C    B PHE   A 1 168 ? 6.594  -17.877 0.636   0.50 17.13 ?  168  PHE   A C    1 
ATOM   3834 O  O    A PHE   A 1 168 ? 5.326  -17.507 0.911   0.50 18.56 ?  168  PHE   A O    1 
ATOM   3835 O  O    B PHE   A 1 168 ? 7.532  -18.471 0.089   0.50 16.50 ?  168  PHE   A O    1 
ATOM   3836 C  CB   A PHE   A 1 168 ? 7.161  -15.241 1.916   0.50 14.63 ?  168  PHE   A CB   1 
ATOM   3837 C  CB   B PHE   A 1 168 ? 7.065  -15.913 2.103   0.50 16.47 ?  168  PHE   A CB   1 
ATOM   3838 C  CG   A PHE   A 1 168 ? 8.426  -15.977 2.219   0.50 14.04 ?  168  PHE   A CG   1 
ATOM   3839 C  CG   B PHE   A 1 168 ? 8.396  -16.477 2.490   0.50 16.13 ?  168  PHE   A CG   1 
ATOM   3840 C  CD1  A PHE   A 1 168 ? 9.606  -15.603 1.604   0.50 14.29 ?  168  PHE   A CD1  1 
ATOM   3841 C  CD1  B PHE   A 1 168 ? 9.551  -16.023 1.877   0.50 16.30 ?  168  PHE   A CD1  1 
ATOM   3842 C  CD2  A PHE   A 1 168 ? 8.438  -17.060 3.081   0.50 13.84 ?  168  PHE   A CD2  1 
ATOM   3843 C  CD2  B PHE   A 1 168 ? 8.494  -17.492 3.425   0.50 15.99 ?  168  PHE   A CD2  1 
ATOM   3844 C  CE1  A PHE   A 1 168 ? 10.777 -16.282 1.854   0.50 14.01 ?  168  PHE   A CE1  1 
ATOM   3845 C  CE1  B PHE   A 1 168 ? 10.778 -16.551 2.208   0.50 16.43 ?  168  PHE   A CE1  1 
ATOM   3846 C  CE2  A PHE   A 1 168 ? 9.612  -17.742 3.336   0.50 14.08 ?  168  PHE   A CE2  1 
ATOM   3847 C  CE2  B PHE   A 1 168 ? 9.723  -18.023 3.762   0.50 16.10 ?  168  PHE   A CE2  1 
ATOM   3848 C  CZ   A PHE   A 1 168 ? 10.781 -17.351 2.721   0.50 13.96 ?  168  PHE   A CZ   1 
ATOM   3849 C  CZ   B PHE   A 1 168 ? 10.866 -17.552 3.152   0.50 16.50 ?  168  PHE   A CZ   1 
ATOM   3850 H  H    A PHE   A 1 168 ? 5.058  -14.396 0.921   0.50 18.12 ?  168  PHE   A H    1 
ATOM   3851 H  H    B PHE   A 1 168 ? 4.672  -15.943 0.693   0.50 21.64 ?  168  PHE   A H    1 
ATOM   3852 H  HA   A PHE   A 1 168 ? 7.316  -15.306 -0.126  0.50 18.65 ?  168  PHE   A HA   1 
ATOM   3853 H  HA   B PHE   A 1 168 ? 7.322  -16.087 0.109   0.50 20.02 ?  168  PHE   A HA   1 
ATOM   3854 H  HB2  A PHE   A 1 168 ? 7.333  -14.290 1.990   0.50 17.58 ?  168  PHE   A HB2  1 
ATOM   3855 H  HB2  B PHE   A 1 168 ? 7.136  -14.947 2.110   0.50 19.79 ?  168  PHE   A HB2  1 
ATOM   3856 H  HB3  A PHE   A 1 168 ? 6.490  -15.507 2.566   0.50 17.58 ?  168  PHE   A HB3  1 
ATOM   3857 H  HB3  B PHE   A 1 168 ? 6.413  -16.208 2.753   0.50 19.79 ?  168  PHE   A HB3  1 
ATOM   3858 H  HD1  A PHE   A 1 168 ? 9.608  -14.879 1.015   0.50 17.18 ?  168  PHE   A HD1  1 
ATOM   3859 H  HD1  B PHE   A 1 168 ? 9.499  -15.348 1.237   0.50 19.58 ?  168  PHE   A HD1  1 
ATOM   3860 H  HD2  A PHE   A 1 168 ? 7.649  -17.329 3.496   0.50 16.63 ?  168  PHE   A HD2  1 
ATOM   3861 H  HD2  B PHE   A 1 168 ? 7.723  -17.814 3.835   0.50 19.22 ?  168  PHE   A HD2  1 
ATOM   3862 H  HE1  A PHE   A 1 168 ? 11.568 -16.015 1.440   0.50 16.83 ?  168  PHE   A HE1  1 
ATOM   3863 H  HE1  B PHE   A 1 168 ? 11.549 -16.230 1.796   0.50 19.73 ?  168  PHE   A HE1  1 
ATOM   3864 H  HE2  A PHE   A 1 168 ? 9.611  -18.465 3.921   0.50 16.91 ?  168  PHE   A HE2  1 
ATOM   3865 H  HE2  B PHE   A 1 168 ? 9.780  -18.699 4.397   0.50 19.35 ?  168  PHE   A HE2  1 
ATOM   3866 H  HZ   A PHE   A 1 168 ? 11.573 -17.808 2.893   0.50 16.77 ?  168  PHE   A HZ   1 
ATOM   3867 H  HZ   B PHE   A 1 168 ? 11.696 -17.906 3.378   0.50 19.82 ?  168  PHE   A HZ   1 
ATOM   3868 N  N    A LEU   A 1 169 ? 7.229  -17.736 -0.279  0.50 17.78 ?  169  LEU   A N    1 
ATOM   3869 N  N    B LEU   A 1 169 ? 5.576  -18.526 1.187   0.50 18.19 ?  169  LEU   A N    1 
ATOM   3870 C  CA   A LEU   A 1 169 ? 7.066  -19.175 -0.443  0.50 19.81 ?  169  LEU   A CA   1 
ATOM   3871 C  CA   B LEU   A 1 169 ? 5.588  -19.985 1.276   0.50 19.77 ?  169  LEU   A CA   1 
ATOM   3872 C  C    A LEU   A 1 169 ? 7.920  -19.928 0.574   0.50 19.64 ?  169  LEU   A C    1 
ATOM   3873 C  C    B LEU   A 1 169 ? 5.006  -20.652 0.032   0.50 20.67 ?  169  LEU   A C    1 
ATOM   3874 O  O    A LEU   A 1 169 ? 7.370  -20.449 1.548   0.50 20.22 ?  169  LEU   A O    1 
ATOM   3875 O  O    B LEU   A 1 169 ? 4.044  -20.170 -0.567  0.50 20.53 ?  169  LEU   A O    1 
ATOM   3876 C  CB   A LEU   A 1 169 ? 7.393  -19.604 -1.881  0.50 20.97 ?  169  LEU   A CB   1 
ATOM   3877 C  CB   B LEU   A 1 169 ? 4.849  -20.467 2.528   0.50 20.50 ?  169  LEU   A CB   1 
ATOM   3878 C  CG   A LEU   A 1 169 ? 7.050  -21.052 -2.254  0.50 22.02 ?  169  LEU   A CG   1 
ATOM   3879 C  CG   B LEU   A 1 169 ? 4.772  -21.987 2.714   0.50 21.45 ?  169  LEU   A CG   1 
ATOM   3880 C  CD1  A LEU   A 1 169 ? 5.606  -21.378 -1.906  0.50 22.32 ?  169  LEU   A CD1  1 
ATOM   3881 C  CD1  B LEU   A 1 169 ? 6.145  -22.634 2.650   0.50 22.93 ?  169  LEU   A CD1  1 
ATOM   3882 C  CD2  A LEU   A 1 169 ? 7.304  -21.311 -3.735  0.50 22.18 ?  169  LEU   A CD2  1 
ATOM   3883 C  CD2  B LEU   A 1 169 ? 4.080  -22.332 4.030   0.50 21.29 ?  169  LEU   A CD2  1 
ATOM   3884 O  OXT  A LEU   A 1 169 ? 9.148  -20.027 0.475   0.50 19.01 -1 169  LEU   A OXT  1 
ATOM   3885 O  OXT  B LEU   A 1 169 ? 5.496  -21.701 -0.392  0.50 21.94 -1 169  LEU   A OXT  1 
ATOM   3886 H  H    A LEU   A 1 169 ? 7.944  -17.419 -0.645  0.50 21.36 ?  169  LEU   A H    1 
ATOM   3887 H  H    B LEU   A 1 169 ? 4.874  -18.150 1.512   0.50 21.86 ?  169  LEU   A H    1 
ATOM   3888 H  HA   A LEU   A 1 169 ? 6.148  -19.409 -0.267  0.50 23.80 ?  169  LEU   A HA   1 
ATOM   3889 H  HA   B LEU   A 1 169 ? 6.508  -20.269 1.358   0.50 23.75 ?  169  LEU   A HA   1 
ATOM   3890 H  HB2  A LEU   A 1 169 ? 6.899  -19.032 -2.490  0.50 25.18 ?  169  LEU   A HB2  1 
ATOM   3891 H  HB2  B LEU   A 1 169 ? 5.296  -20.102 3.306   0.50 24.63 ?  169  LEU   A HB2  1 
ATOM   3892 H  HB3  A LEU   A 1 169 ? 8.342  -19.491 -2.032  0.50 25.18 ?  169  LEU   A HB3  1 
ATOM   3893 H  HB3  B LEU   A 1 169 ? 3.938  -20.140 2.494   0.50 24.63 ?  169  LEU   A HB3  1 
ATOM   3894 H  HG   A LEU   A 1 169 ? 7.619  -21.654 -1.750  0.50 26.45 ?  169  LEU   A HG   1 
ATOM   3895 H  HG   B LEU   A 1 169 ? 4.233  -22.363 2.002   0.50 25.76 ?  169  LEU   A HG   1 
ATOM   3896 H  HD11 A LEU   A 1 169 ? 5.354  -22.210 -2.338  0.50 26.80 ?  169  LEU   A HD11 1 
ATOM   3897 H  HD11 B LEU   A 1 169 ? 6.042  -23.594 2.738   0.50 27.54 ?  169  LEU   A HD11 1 
ATOM   3898 H  HD12 A LEU   A 1 169 ? 5.526  -21.469 -0.944  0.50 26.80 ?  169  LEU   A HD12 1 
ATOM   3899 H  HD12 B LEU   A 1 169 ? 6.558  -22.425 1.798   0.50 27.54 ?  169  LEU   A HD12 1 
ATOM   3900 H  HD13 A LEU   A 1 169 ? 5.036  -20.658 -2.220  0.50 26.80 ?  169  LEU   A HD13 1 
ATOM   3901 H  HD13 B LEU   A 1 169 ? 6.683  -22.293 3.377   0.50 27.54 ?  169  LEU   A HD13 1 
ATOM   3902 H  HD21 A LEU   A 1 169 ? 7.087  -22.236 -3.939  0.50 26.63 ?  169  LEU   A HD21 1 
ATOM   3903 H  HD21 B LEU   A 1 169 ? 4.044  -23.297 4.125   0.50 25.58 ?  169  LEU   A HD21 1 
ATOM   3904 H  HD22 A LEU   A 1 169 ? 6.744  -20.718 -4.261  0.50 26.63 ?  169  LEU   A HD22 1 
ATOM   3905 H  HD22 B LEU   A 1 169 ? 4.586  -21.946 4.763   0.50 25.58 ?  169  LEU   A HD22 1 
ATOM   3906 H  HD23 A LEU   A 1 169 ? 8.239  -21.141 -3.930  0.50 26.63 ?  169  LEU   A HD23 1 
ATOM   3907 H  HD23 B LEU   A 1 169 ? 3.182  -21.966 4.021   0.50 25.58 ?  169  LEU   A HD23 1 
ATOM   3908 N  N    A SER   B 1 1   ? 50.794 -9.203  -23.682 0.50 26.30 ?  1    SER   B N    1 
ATOM   3909 N  N    B SER   B 1 1   ? 50.809 -9.281  -23.691 0.50 24.69 ?  1    SER   B N    1 
ATOM   3910 C  CA   A SER   B 1 1   ? 51.296 -10.272 -22.796 0.50 26.44 ?  1    SER   B CA   1 
ATOM   3911 C  CA   B SER   B 1 1   ? 51.253 -10.279 -22.696 0.50 24.90 ?  1    SER   B CA   1 
ATOM   3912 C  C    A SER   B 1 1   ? 50.227 -11.329 -22.566 0.50 25.39 ?  1    SER   B C    1 
ATOM   3913 C  C    B SER   B 1 1   ? 50.178 -11.332 -22.466 0.50 23.74 ?  1    SER   B C    1 
ATOM   3914 O  O    A SER   B 1 1   ? 49.039 -11.125 -22.847 0.50 24.99 ?  1    SER   B O    1 
ATOM   3915 O  O    B SER   B 1 1   ? 48.990 -11.130 -22.758 0.50 23.21 ?  1    SER   B O    1 
ATOM   3916 C  CB   A SER   B 1 1   ? 51.758 -9.695  -21.459 0.50 27.02 ?  1    SER   B CB   1 
ATOM   3917 C  CB   B SER   B 1 1   ? 51.607 -9.607  -21.372 0.50 25.61 ?  1    SER   B CB   1 
ATOM   3918 O  OG   A SER   B 1 1   ? 50.652 -9.360  -20.643 0.50 28.76 ?  1    SER   B OG   1 
ATOM   3919 O  OG   B SER   B 1 1   ? 50.446 -9.387  -20.593 0.50 27.42 ?  1    SER   B OG   1 
ATOM   3920 H  H1   A SER   B 1 1   ? 50.697 -9.531  -24.501 0.50 31.58 ?  1    SER   B H1   1 
ATOM   3921 H  H1   B SER   B 1 1   ? 51.466 -8.699  -23.827 0.50 29.66 ?  1    SER   B H1   1 
ATOM   3922 H  H2   A SER   B 1 1   ? 50.014 -8.916  -23.375 0.50 31.58 ?  1    SER   B H2   1 
ATOM   3923 H  H2   B SER   B 1 1   ? 50.614 -9.698  -24.450 0.50 29.66 ?  1    SER   B H2   1 
ATOM   3924 H  H3   A SER   B 1 1   ? 51.382 -8.539  -23.690 0.50 31.58 ?  1    SER   B H3   1 
ATOM   3925 H  H3   B SER   B 1 1   ? 50.093 -8.862  -23.381 0.50 29.66 ?  1    SER   B H3   1 
ATOM   3926 H  HA   A SER   B 1 1   ? 52.052 -10.693 -23.225 0.50 31.75 ?  1    SER   B HA   1 
ATOM   3927 H  HA   B SER   B 1 1   ? 52.044 -10.718 -23.037 0.50 29.91 ?  1    SER   B HA   1 
ATOM   3928 H  HB2  A SER   B 1 1   ? 52.297 -10.360 -21.005 0.50 32.45 ?  1    SER   B HB2  1 
ATOM   3929 H  HB2  B SER   B 1 1   ? 52.216 -10.184 -20.886 0.50 30.76 ?  1    SER   B HB2  1 
ATOM   3930 H  HB3  A SER   B 1 1   ? 52.285 -8.897  -21.624 0.50 32.45 ?  1    SER   B HB3  1 
ATOM   3931 H  HB3  B SER   B 1 1   ? 52.033 -8.754  -21.553 0.50 30.76 ?  1    SER   B HB3  1 
ATOM   3932 H  HG   A SER   B 1 1   ? 50.919 -8.949  -19.960 0.50 34.54 ?  1    SER   B HG   1 
ATOM   3933 H  HG   B SER   B 1 1   ? 50.627 -8.866  -19.958 0.50 32.92 ?  1    SER   B HG   1 
ATOM   3934 N  N    A MET   B 1 2   ? 50.672 -12.465 -22.044 0.50 24.82 ?  2    MET   B N    1 
ATOM   3935 N  N    B MET   B 1 2   ? 50.617 -12.463 -21.931 0.50 23.11 ?  2    MET   B N    1 
ATOM   3936 C  CA   A MET   B 1 2   ? 49.839 -13.643 -21.871 0.50 24.99 ?  2    MET   B CA   1 
ATOM   3937 C  CA   B MET   B 1 2   ? 49.780 -13.637 -21.742 0.50 23.04 ?  2    MET   B CA   1 
ATOM   3938 C  C    A MET   B 1 2   ? 49.594 -13.848 -20.385 0.50 22.74 ?  2    MET   B C    1 
ATOM   3939 C  C    B MET   B 1 2   ? 49.514 -13.801 -20.254 0.50 21.36 ?  2    MET   B C    1 
ATOM   3940 O  O    A MET   B 1 2   ? 50.537 -14.084 -19.624 0.50 22.90 ?  2    MET   B O    1 
ATOM   3941 O  O    B MET   B 1 2   ? 50.428 -14.119 -19.486 0.50 21.84 ?  2    MET   B O    1 
ATOM   3942 C  CB   A MET   B 1 2   ? 50.543 -14.854 -22.475 0.50 28.39 ?  2    MET   B CB   1 
ATOM   3943 C  CB   B MET   B 1 2   ? 50.510 -14.849 -22.297 0.50 25.60 ?  2    MET   B CB   1 
ATOM   3944 C  CG   A MET   B 1 2   ? 49.689 -16.105 -22.570 0.50 31.52 ?  2    MET   B CG   1 
ATOM   3945 C  CG   B MET   B 1 2   ? 49.618 -16.004 -22.732 0.50 27.60 ?  2    MET   B CG   1 
ATOM   3946 S  SD   A MET   B 1 2   ? 50.509 -17.384 -23.538 0.50 34.61 ?  2    MET   B SD   1 
ATOM   3947 S  SD   B MET   B 1 2   ? 50.493 -17.132 -23.827 0.50 29.54 ?  2    MET   B SD   1 
ATOM   3948 C  CE   A MET   B 1 2   ? 51.061 -16.398 -24.926 0.50 35.02 ?  2    MET   B CE   1 
ATOM   3949 C  CE   B MET   B 1 2   ? 51.561 -15.985 -24.668 0.50 29.98 ?  2    MET   B CE   1 
ATOM   3950 H  H    A MET   B 1 2   ? 51.481 -12.583 -21.773 0.50 29.81 ?  2    MET   B H    1 
ATOM   3951 H  H    B MET   B 1 2   ? 51.432 -12.588 -21.672 0.50 27.75 ?  2    MET   B H    1 
ATOM   3952 H  HA   A MET   B 1 2   ? 48.995 -13.527 -22.331 0.50 30.01 ?  2    MET   B HA   1 
ATOM   3953 H  HA   B MET   B 1 2   ? 48.949 -13.540 -22.232 0.50 27.67 ?  2    MET   B HA   1 
ATOM   3954 H  HB2  A MET   B 1 2   ? 50.821 -14.589 -23.363 0.50 34.10 ?  2    MET   B HB2  1 
ATOM   3955 H  HB2  B MET   B 1 2   ? 50.999 -14.495 -23.045 0.50 30.74 ?  2    MET   B HB2  1 
ATOM   3956 H  HB3  A MET   B 1 2   ? 51.320 -15.078 -21.944 0.50 34.10 ?  2    MET   B HB3  1 
ATOM   3957 H  HB3  B MET   B 1 2   ? 51.127 -15.209 -21.646 0.50 30.74 ?  2    MET   B HB3  1 
ATOM   3958 H  HG2  A MET   B 1 2   ? 49.528 -16.452 -21.677 0.50 37.85 ?  2    MET   B HG2  1 
ATOM   3959 H  HG2  B MET   B 1 2   ? 49.323 -16.500 -21.945 0.50 33.14 ?  2    MET   B HG2  1 
ATOM   3960 H  HG3  A MET   B 1 2   ? 48.848 -15.892 -23.004 0.50 37.85 ?  2    MET   B HG3  1 
ATOM   3961 H  HG3  B MET   B 1 2   ? 48.853 -15.670 -23.218 0.50 33.14 ?  2    MET   B HG3  1 
ATOM   3962 H  HE1  A MET   B 1 2   ? 51.229 -16.979 -25.671 0.50 42.05 ?  2    MET   B HE1  1 
ATOM   3963 H  HE1  B MET   B 1 2   ? 51.904 -16.429 -25.427 0.50 36.00 ?  2    MET   B HE1  1 
ATOM   3964 H  HE2  A MET   B 1 2   ? 50.364 -15.756 -25.150 0.50 42.05 ?  2    MET   B HE2  1 
ATOM   3965 H  HE2  B MET   B 1 2   ? 51.035 -15.212 -24.941 0.50 36.00 ?  2    MET   B HE2  1 
ATOM   3966 H  HE3  A MET   B 1 2   ? 51.876 -15.924 -24.680 0.50 42.05 ?  2    MET   B HE3  1 
ATOM   3967 H  HE3  B MET   B 1 2   ? 52.292 -15.712 -24.078 0.50 36.00 ?  2    MET   B HE3  1 
ATOM   3968 N  N    A VAL   B 1 3   ? 48.332 -13.738 -19.976 0.50 20.53 ?  3    VAL   B N    1 
ATOM   3969 N  N    B VAL   B 1 3   ? 48.271 -13.572 -19.849 0.50 19.70 ?  3    VAL   B N    1 
ATOM   3970 C  CA   A VAL   B 1 3   ? 47.927 -13.969 -18.598 0.50 19.36 ?  3    VAL   B CA   1 
ATOM   3971 C  CA   B VAL   B 1 3   ? 47.839 -13.817 -18.480 0.50 19.24 ?  3    VAL   B CA   1 
ATOM   3972 C  C    A VAL   B 1 3   ? 46.695 -14.863 -18.607 0.50 17.67 ?  3    VAL   B C    1 
ATOM   3973 C  C    B VAL   B 1 3   ? 46.588 -14.679 -18.505 0.50 17.96 ?  3    VAL   B C    1 
ATOM   3974 O  O    A VAL   B 1 3   ? 46.010 -15.009 -19.623 0.50 17.35 ?  3    VAL   B O    1 
ATOM   3975 O  O    B VAL   B 1 3   ? 45.784 -14.622 -19.441 0.50 18.40 ?  3    VAL   B O    1 
ATOM   3976 C  CB   A VAL   B 1 3   ? 47.651 -12.653 -17.836 0.50 20.69 ?  3    VAL   B CB   1 
ATOM   3977 C  CB   B VAL   B 1 3   ? 47.583 -12.513 -17.694 0.50 20.71 ?  3    VAL   B CB   1 
ATOM   3978 C  CG1  A VAL   B 1 3   ? 48.922 -11.810 -17.747 0.50 21.26 ?  3    VAL   B CG1  1 
ATOM   3979 C  CG1  B VAL   B 1 3   ? 48.860 -11.688 -17.592 0.50 21.32 ?  3    VAL   B CG1  1 
ATOM   3980 C  CG2  A VAL   B 1 3   ? 46.531 -11.873 -18.507 0.50 21.17 ?  3    VAL   B CG2  1 
ATOM   3981 C  CG2  B VAL   B 1 3   ? 46.462 -11.716 -18.337 0.50 21.12 ?  3    VAL   B CG2  1 
ATOM   3982 H  H    A VAL   B 1 3   ? 47.679 -13.525 -20.494 0.50 24.66 ?  3    VAL   B H    1 
ATOM   3983 H  H    B VAL   B 1 3   ? 47.653 -13.272 -20.365 0.50 23.66 ?  3    VAL   B H    1 
ATOM   3984 H  HA   A VAL   B 1 3   ? 48.633 -14.443 -18.132 0.50 23.25 ?  3    VAL   B HA   1 
ATOM   3985 H  HA   B VAL   B 1 3   ? 48.530 -14.314 -18.018 0.50 23.11 ?  3    VAL   B HA   1 
ATOM   3986 H  HB   A VAL   B 1 3   ? 47.370 -12.865 -16.932 0.50 24.86 ?  3    VAL   B HB   1 
ATOM   3987 H  HB   B VAL   B 1 3   ? 47.305 -12.746 -16.795 0.50 24.88 ?  3    VAL   B HB   1 
ATOM   3988 H  HG11 A VAL   B 1 3   ? 48.727 -10.997 -17.255 0.50 25.53 ?  3    VAL   B HG11 1 
ATOM   3989 H  HG11 B VAL   B 1 3   ? 48.673 -10.885 -17.082 0.50 25.61 ?  3    VAL   B HG11 1 
ATOM   3990 H  HG12 A VAL   B 1 3   ? 49.607 -12.320 -17.286 0.50 25.53 ?  3    VAL   B HG12 1 
ATOM   3991 H  HG12 B VAL   B 1 3   ? 49.540 -12.215 -17.145 0.50 25.61 ?  3    VAL   B HG12 1 
ATOM   3992 H  HG13 A VAL   B 1 3   ? 49.219 -11.591 -18.644 0.50 25.53 ?  3    VAL   B HG13 1 
ATOM   3993 H  HG13 B VAL   B 1 3   ? 49.155 -11.453 -18.485 0.50 25.61 ?  3    VAL   B HG13 1 
ATOM   3994 H  HG21 A VAL   B 1 3   ? 46.465 -11.000 -18.091 0.50 25.43 ?  3    VAL   B HG21 1 
ATOM   3995 H  HG21 B VAL   B 1 3   ? 46.428 -10.840 -17.928 0.50 25.36 ?  3    VAL   B HG21 1 
ATOM   3996 H  HG22 A VAL   B 1 3   ? 46.733 -11.776 -19.450 0.50 25.43 ?  3    VAL   B HG22 1 
ATOM   3997 H  HG22 B VAL   B 1 3   ? 46.638 -11.634 -19.287 0.50 25.36 ?  3    VAL   B HG22 1 
ATOM   3998 H  HG23 A VAL   B 1 3   ? 45.697 -12.356 -18.394 0.50 25.43 ?  3    VAL   B HG23 1 
ATOM   3999 H  HG23 B VAL   B 1 3   ? 45.621 -12.181 -18.196 0.50 25.36 ?  3    VAL   B HG23 1 
ATOM   4000 N  N    . ASN   B 1 4   ? 46.426 -15.479 -17.455 1.00 16.58 ?  4    ASN   B N    1 
ATOM   4001 C  CA   . ASN   B 1 4   ? 45.288 -16.389 -17.326 1.00 14.95 ?  4    ASN   B CA   1 
ATOM   4002 C  C    . ASN   B 1 4   ? 45.227 -17.357 -18.505 1.00 15.15 ?  4    ASN   B C    1 
ATOM   4003 O  O    . ASN   B 1 4   ? 44.167 -17.600 -19.075 1.00 15.82 ?  4    ASN   B O    1 
ATOM   4004 C  CB   . ASN   B 1 4   ? 43.968 -15.629 -17.158 1.00 14.24 ?  4    ASN   B CB   1 
ATOM   4005 C  CG   . ASN   B 1 4   ? 43.925 -14.816 -15.878 1.00 13.75 ?  4    ASN   B CG   1 
ATOM   4006 O  OD1  . ASN   B 1 4   ? 44.215 -15.328 -14.800 1.00 13.69 ?  4    ASN   B OD1  1 
ATOM   4007 N  ND2  . ASN   B 1 4   ? 43.577 -13.538 -15.994 1.00 14.72 ?  4    ASN   B ND2  1 
ATOM   4008 H  H    A ASN   B 1 4   ? 46.891 -15.396 -16.740 0.50 19.91 ?  4    ASN   B H    1 
ATOM   4009 H  H    B ASN   B 1 4   ? 46.973 -15.519 -16.795 0.50 19.91 ?  4    ASN   B H    1 
ATOM   4010 H  HA   . ASN   B 1 4   ? 45.419 -16.919 -16.522 1.00 17.97 ?  4    ASN   B HA   1 
ATOM   4011 H  HB2  . ASN   B 1 4   ? 43.854 -15.023 -17.902 1.00 17.11 ?  4    ASN   B HB2  1 
ATOM   4012 H  HB3  . ASN   B 1 4   ? 43.237 -16.269 -17.132 1.00 17.11 ?  4    ASN   B HB3  1 
ATOM   4013 H  HD21 . ASN   B 1 4   ? 43.541 -13.035 -15.294 1.00 17.69 ?  4    ASN   B HD21 1 
ATOM   4014 H  HD22 . ASN   B 1 4   ? 43.385 -13.210 -16.765 1.00 17.69 ?  4    ASN   B HD22 1 
ATOM   4015 N  N    . SER   B 1 5   ? 46.382 -17.908 -18.882 1.00 16.27 ?  5    SER   B N    1 
ATOM   4016 C  CA   . SER   B 1 5   ? 46.477 -18.828 -20.016 1.00 18.52 ?  5    SER   B CA   1 
ATOM   4017 C  C    . SER   B 1 5   ? 46.463 -20.246 -19.460 1.00 20.34 ?  5    SER   B C    1 
ATOM   4018 O  O    . SER   B 1 5   ? 47.491 -20.908 -19.334 1.00 22.35 ?  5    SER   B O    1 
ATOM   4019 C  CB   . SER   B 1 5   ? 47.735 -18.546 -20.833 1.00 19.82 ?  5    SER   B CB   1 
ATOM   4020 O  OG   . SER   B 1 5   ? 48.902 -18.691 -20.042 1.00 22.37 ?  5    SER   B OG   1 
ATOM   4021 H  H    . SER   B 1 5   ? 47.134 -17.763 -18.493 1.00 19.54 ?  5    SER   B H    1 
ATOM   4022 H  HA   . SER   B 1 5   ? 45.705 -18.718 -20.589 1.00 22.25 ?  5    SER   B HA   1 
ATOM   4023 H  HB2  . SER   B 1 5   ? 47.770 -19.168 -21.580 1.00 23.80 ?  5    SER   B HB2  1 
ATOM   4024 H  HB3  . SER   B 1 5   ? 47.681 -17.638 -21.166 1.00 23.80 ?  5    SER   B HB3  1 
ATOM   4025 H  HG   . SER   B 1 5   ? 48.963 -19.484 -19.771 1.00 26.87 ?  5    SER   B HG   1 
ATOM   4026 N  N    . PHE   B 1 6   ? 45.267 -20.696 -19.096 1.00 20.90 ?  6    PHE   B N    1 
ATOM   4027 C  CA   . PHE   B 1 6   ? 45.083 -22.036 -18.559 1.00 20.60 ?  6    PHE   B CA   1 
ATOM   4028 C  C    . PHE   B 1 6   ? 45.007 -23.028 -19.709 1.00 24.50 ?  6    PHE   B C    1 
ATOM   4029 O  O    . PHE   B 1 6   ? 44.321 -22.782 -20.705 1.00 26.80 ?  6    PHE   B O    1 
ATOM   4030 C  CB   . PHE   B 1 6   ? 43.801 -22.093 -17.728 1.00 18.55 ?  6    PHE   B CB   1 
ATOM   4031 C  CG   . PHE   B 1 6   ? 43.825 -21.215 -16.507 1.00 16.82 ?  6    PHE   B CG   1 
ATOM   4032 C  CD1  . PHE   B 1 6   ? 44.328 -21.686 -15.313 1.00 15.76 ?  6    PHE   B CD1  1 
ATOM   4033 C  CD2  . PHE   B 1 6   ? 43.343 -19.916 -16.559 1.00 16.22 ?  6    PHE   B CD2  1 
ATOM   4034 C  CE1  . PHE   B 1 6   ? 44.339 -20.884 -14.184 1.00 15.00 ?  6    PHE   B CE1  1 
ATOM   4035 C  CE2  . PHE   B 1 6   ? 43.355 -19.105 -15.441 1.00 16.74 ?  6    PHE   B CE2  1 
ATOM   4036 C  CZ   . PHE   B 1 6   ? 43.864 -19.581 -14.254 1.00 15.71 ?  6    PHE   B CZ   1 
ATOM   4037 H  H    . PHE   B 1 6   ? 44.538 -20.245 -19.156 1.00 25.10 ?  6    PHE   B H    1 
ATOM   4038 H  HA   . PHE   B 1 6   ? 45.830 -22.275 -17.994 1.00 24.74 ?  6    PHE   B HA   1 
ATOM   4039 H  HB2  . PHE   B 1 6   ? 43.055 -21.810 -18.281 1.00 22.28 ?  6    PHE   B HB2  1 
ATOM   4040 H  HB3  . PHE   B 1 6   ? 43.657 -23.007 -17.432 1.00 22.28 ?  6    PHE   B HB3  1 
ATOM   4041 H  HD1  . PHE   B 1 6   ? 44.657 -22.556 -15.263 1.00 18.94 ?  6    PHE   B HD1  1 
ATOM   4042 H  HD2  . PHE   B 1 6   ? 43.000 -19.591 -17.359 1.00 19.48 ?  6    PHE   B HD2  1 
ATOM   4043 H  HE1  . PHE   B 1 6   ? 44.691 -21.207 -13.384 1.00 18.03 ?  6    PHE   B HE1  1 
ATOM   4044 H  HE2  . PHE   B 1 6   ? 43.029 -18.236 -15.494 1.00 20.11 ?  6    PHE   B HE2  1 
ATOM   4045 H  HZ   . PHE   B 1 6   ? 43.876 -19.041 -13.497 1.00 18.88 ?  6    PHE   B HZ   1 
ATOM   4046 N  N    . SER   B 1 7   ? 45.731 -24.139 -19.580 1.00 25.87 ?  7    SER   B N    1 
ATOM   4047 C  CA   . SER   B 1 7   ? 45.827 -25.129 -20.641 1.00 28.59 ?  7    SER   B CA   1 
ATOM   4048 C  C    . SER   B 1 7   ? 45.732 -26.529 -20.054 1.00 27.57 ?  7    SER   B C    1 
ATOM   4049 O  O    . SER   B 1 7   ? 46.312 -26.815 -19.003 1.00 28.28 ?  7    SER   B O    1 
ATOM   4050 C  CB   . SER   B 1 7   ? 47.149 -24.982 -21.408 1.00 32.06 ?  7    SER   B CB   1 
ATOM   4051 O  OG   . SER   B 1 7   ? 47.238 -25.929 -22.459 1.00 34.37 ?  7    SER   B OG   1 
ATOM   4052 H  H    . SER   B 1 7   ? 46.187 -24.337 -18.876 1.00 31.06 ?  7    SER   B H    1 
ATOM   4053 H  HA   . SER   B 1 7   ? 45.097 -25.012 -21.264 1.00 34.33 ?  7    SER   B HA   1 
ATOM   4054 H  HB2  . SER   B 1 7   ? 47.196 -24.089 -21.786 1.00 38.49 ?  7    SER   B HB2  1 
ATOM   4055 H  HB3  . SER   B 1 7   ? 47.889 -25.119 -20.795 1.00 38.49 ?  7    SER   B HB3  1 
ATOM   4056 H  HG   . SER   B 1 7   ? 47.966 -25.837 -22.868 1.00 41.27 ?  7    SER   B HG   1 
ATOM   4057 N  N    . GLY   B 1 8   ? 44.997 -27.397 -20.745 1.00 27.38 ?  8    GLY   B N    1 
ATOM   4058 C  CA   . GLY   B 1 8   ? 44.937 -28.791 -20.372 1.00 26.05 ?  8    GLY   B CA   1 
ATOM   4059 C  C    . GLY   B 1 8   ? 43.996 -29.110 -19.240 1.00 24.24 ?  8    GLY   B C    1 
ATOM   4060 O  O    . GLY   B 1 8   ? 44.129 -30.175 -18.627 1.00 25.60 ?  8    GLY   B O    1 
ATOM   4061 H  H    . GLY   B 1 8   ? 44.529 -27.193 -21.434 1.00 32.88 ?  8    GLY   B H    1 
ATOM   4062 H  HA2  . GLY   B 1 8   ? 44.660 -29.310 -21.141 1.00 31.29 ?  8    GLY   B HA2  1 
ATOM   4063 H  HA3  . GLY   B 1 8   ? 45.821 -29.088 -20.109 1.00 31.29 ?  8    GLY   B HA3  1 
ATOM   4064 N  N    . TYR   B 1 9   ? 43.033 -28.238 -18.951 1.00 22.42 ?  9    TYR   B N    1 
ATOM   4065 C  CA   . TYR   B 1 9   ? 42.077 -28.508 -17.891 1.00 20.29 ?  9    TYR   B CA   1 
ATOM   4066 C  C    . TYR   B 1 9   ? 40.896 -29.304 -18.411 1.00 19.88 ?  9    TYR   B C    1 
ATOM   4067 O  O    . TYR   B 1 9   ? 40.473 -29.161 -19.562 1.00 21.94 ?  9    TYR   B O    1 
ATOM   4068 C  CB   . TYR   B 1 9   ? 41.567 -27.220 -17.249 1.00 19.79 ?  9    TYR   B CB   1 
ATOM   4069 C  CG   . TYR   B 1 9   ? 42.592 -26.595 -16.340 1.00 18.97 ?  9    TYR   B CG   1 
ATOM   4070 C  CD1  . TYR   B 1 9   ? 43.678 -25.913 -16.864 1.00 19.43 ?  9    TYR   B CD1  1 
ATOM   4071 C  CD2  . TYR   B 1 9   ? 42.492 -26.707 -14.962 1.00 18.18 ?  9    TYR   B CD2  1 
ATOM   4072 C  CE1  . TYR   B 1 9   ? 44.633 -25.354 -16.045 1.00 19.43 ?  9    TYR   B CE1  1 
ATOM   4073 C  CE2  . TYR   B 1 9   ? 43.443 -26.145 -14.130 1.00 18.36 ?  9    TYR   B CE2  1 
ATOM   4074 C  CZ   . TYR   B 1 9   ? 44.513 -25.466 -14.680 1.00 19.15 ?  9    TYR   B CZ   1 
ATOM   4075 O  OH   . TYR   B 1 9   ? 45.472 -24.911 -13.870 1.00 19.77 ?  9    TYR   B OH   1 
ATOM   4076 H  H    . TYR   B 1 9   ? 42.895 -27.498 -19.368 1.00 26.93 ?  9    TYR   B H    1 
ATOM   4077 H  HA   . TYR   B 1 9   ? 42.500 -29.035 -17.204 1.00 24.37 ?  9    TYR   B HA   1 
ATOM   4078 H  HB2  . TYR   B 1 9   ? 41.332 -26.578 -17.939 1.00 23.77 ?  9    TYR   B HB2  1 
ATOM   4079 H  HB3  . TYR   B 1 9   ? 40.788 -27.438 -16.716 1.00 23.77 ?  9    TYR   B HB3  1 
ATOM   4080 H  HD1  . TYR   B 1 9   ? 43.759 -25.837 -17.788 1.00 23.34 ?  9    TYR   B HD1  1 
ATOM   4081 H  HD2  . TYR   B 1 9   ? 41.766 -27.169 -14.590 1.00 21.84 ?  9    TYR   B HD2  1 
ATOM   4082 H  HE1  . TYR   B 1 9   ? 45.346 -24.900 -16.415 1.00 23.34 ?  9    TYR   B HE1  1 
ATOM   4083 H  HE2  . TYR   B 1 9   ? 43.354 -26.230 -13.208 1.00 22.05 ?  9    TYR   B HE2  1 
ATOM   4084 H  HH   . TYR   B 1 9   ? 46.045 -24.530 -14.341 1.00 23.74 ?  9    TYR   B HH   1 
ATOM   4085 N  N    . LEU   B 1 10  ? 40.379 -30.161 -17.540 1.00 18.19 ?  10   LEU   B N    1 
ATOM   4086 C  CA   . LEU   B 1 10  ? 39.175 -30.925 -17.805 1.00 17.77 ?  10   LEU   B CA   1 
ATOM   4087 C  C    . LEU   B 1 10  ? 37.992 -30.154 -17.238 1.00 17.12 ?  10   LEU   B C    1 
ATOM   4088 O  O    . LEU   B 1 10  ? 38.016 -29.733 -16.078 1.00 16.67 ?  10   LEU   B O    1 
ATOM   4089 C  CB   . LEU   B 1 10  ? 39.281 -32.290 -17.125 1.00 18.85 ?  10   LEU   B CB   1 
ATOM   4090 C  CG   . LEU   B 1 10  ? 38.157 -33.267 -17.459 1.00 20.46 ?  10   LEU   B CG   1 
ATOM   4091 C  CD1  . LEU   B 1 10  ? 38.307 -33.786 -18.883 1.00 21.65 ?  10   LEU   B CD1  1 
ATOM   4092 C  CD2  . LEU   B 1 10  ? 38.116 -34.413 -16.463 1.00 21.55 ?  10   LEU   B CD2  1 
ATOM   4093 H  H    . LEU   B 1 10  ? 40.713 -30.325 -16.763 1.00 21.85 ?  10   LEU   B H    1 
ATOM   4094 H  HA   . LEU   B 1 10  ? 39.049 -31.055 -18.758 1.00 21.35 ?  10   LEU   B HA   1 
ATOM   4095 H  HB2  . LEU   B 1 10  ? 40.117 -32.706 -17.391 1.00 22.65 ?  10   LEU   B HB2  1 
ATOM   4096 H  HB3  . LEU   B 1 10  ? 39.277 -32.161 -16.162 1.00 22.65 ?  10   LEU   B HB3  1 
ATOM   4097 H  HG   . LEU   B 1 10  ? 37.309 -32.800 -17.404 1.00 24.57 ?  10   LEU   B HG   1 
ATOM   4098 H  HD11 . LEU   B 1 10  ? 37.619 -34.446 -19.051 1.00 26.00 ?  10   LEU   B HD11 1 
ATOM   4099 H  HD12 . LEU   B 1 10  ? 38.211 -33.042 -19.500 1.00 26.00 ?  10   LEU   B HD12 1 
ATOM   4100 H  HD13 . LEU   B 1 10  ? 39.184 -34.186 -18.981 1.00 26.00 ?  10   LEU   B HD13 1 
ATOM   4101 H  HD21 . LEU   B 1 10  ? 37.395 -35.012 -16.708 1.00 25.89 ?  10   LEU   B HD21 1 
ATOM   4102 H  HD22 . LEU   B 1 10  ? 38.963 -34.879 -16.489 1.00 25.89 ?  10   LEU   B HD22 1 
ATOM   4103 H  HD23 . LEU   B 1 10  ? 37.960 -34.049 -15.578 1.00 25.89 ?  10   LEU   B HD23 1 
ATOM   4104 N  N    . LYS   B 1 11  ? 36.966 -29.970 -18.059 1.00 18.40 ?  11   LYS   B N    1 
ATOM   4105 C  CA   . LYS   B 1 11  ? 35.773 -29.252 -17.644 1.00 20.87 ?  11   LYS   B CA   1 
ATOM   4106 C  C    . LYS   B 1 11  ? 34.904 -30.178 -16.798 1.00 19.91 ?  11   LYS   B C    1 
ATOM   4107 O  O    . LYS   B 1 11  ? 34.540 -31.274 -17.242 1.00 21.75 ?  11   LYS   B O    1 
ATOM   4108 C  CB   . LYS   B 1 11  ? 35.023 -28.785 -18.891 1.00 25.07 ?  11   LYS   B CB   1 
ATOM   4109 C  CG   . LYS   B 1 11  ? 33.906 -27.788 -18.647 1.00 28.59 ?  11   LYS   B CG   1 
ATOM   4110 C  CD   . LYS   B 1 11  ? 33.165 -27.495 -19.947 1.00 31.52 ?  11   LYS   B CD   1 
ATOM   4111 C  CE   . LYS   B 1 11  ? 32.139 -26.391 -19.778 1.00 33.61 ?  11   LYS   B CE   1 
ATOM   4112 N  NZ   . LYS   B 1 11  ? 32.781 -25.062 -19.591 1.00 34.76 ?  11   LYS   B NZ   1 
ATOM   4113 H  H    . LYS   B 1 11  ? 36.930 -30.264 -18.869 1.00 22.11 ?  11   LYS   B H    1 
ATOM   4114 H  HA   . LYS   B 1 11  ? 36.019 -28.477 -17.116 1.00 25.07 ?  11   LYS   B HA   1 
ATOM   4115 H  HB2  . LYS   B 1 11  ? 35.659 -28.363 -19.493 1.00 30.10 ?  11   LYS   B HB2  1 
ATOM   4116 H  HB3  . LYS   B 1 11  ? 34.631 -29.557 -19.326 1.00 30.10 ?  11   LYS   B HB3  1 
ATOM   4117 H  HG2  . LYS   B 1 11  ? 33.275 -28.159 -18.011 1.00 34.33 ?  11   LYS   B HG2  1 
ATOM   4118 H  HG3  . LYS   B 1 11  ? 34.279 -26.958 -18.313 1.00 34.33 ?  11   LYS   B HG3  1 
ATOM   4119 H  HD2  . LYS   B 1 11  ? 33.804 -27.215 -20.622 1.00 37.84 ?  11   LYS   B HD2  1 
ATOM   4120 H  HD3  . LYS   B 1 11  ? 32.703 -28.297 -20.239 1.00 37.84 ?  11   LYS   B HD3  1 
ATOM   4121 H  HE2  . LYS   B 1 11  ? 31.581 -26.348 -20.571 1.00 40.35 ?  11   LYS   B HE2  1 
ATOM   4122 H  HE3  . LYS   B 1 11  ? 31.596 -26.585 -18.999 1.00 40.35 ?  11   LYS   B HE3  1 
ATOM   4123 H  HZ1  . LYS   B 1 11  ? 32.158 -24.432 -19.504 1.00 41.74 ?  11   LYS   B HZ1  1 
ATOM   4124 H  HZ2  . LYS   B 1 11  ? 33.290 -25.069 -18.862 1.00 41.74 ?  11   LYS   B HZ2  1 
ATOM   4125 H  HZ3  . LYS   B 1 11  ? 33.289 -24.868 -20.297 1.00 41.74 ?  11   LYS   B HZ3  1 
ATOM   4126 N  N    . LEU   B 1 12  ? 34.580 -29.748 -15.578 1.00 18.12 ?  12   LEU   B N    1 
ATOM   4127 C  CA   . LEU   B 1 12  ? 33.623 -30.457 -14.735 1.00 17.27 ?  12   LEU   B CA   1 
ATOM   4128 C  C    . LEU   B 1 12  ? 32.230 -29.854 -14.826 1.00 16.98 ?  12   LEU   B C    1 
ATOM   4129 O  O    . LEU   B 1 12  ? 31.246 -30.572 -14.997 1.00 17.52 ?  12   LEU   B O    1 
ATOM   4130 C  CB   . LEU   B 1 12  ? 34.085 -30.462 -13.275 1.00 16.71 ?  12   LEU   B CB   1 
ATOM   4131 C  CG   . LEU   B 1 12  ? 35.426 -31.140 -13.007 1.00 16.32 ?  12   LEU   B CG   1 
ATOM   4132 C  CD1  . LEU   B 1 12  ? 35.776 -31.097 -11.529 1.00 16.65 ?  12   LEU   B CD1  1 
ATOM   4133 C  CD2  . LEU   B 1 12  ? 35.419 -32.572 -13.521 1.00 17.09 ?  12   LEU   B CD2  1 
ATOM   4134 H  H    . LEU   B 1 12  ? 34.898 -29.035 -15.217 1.00 21.77 ?  12   LEU   B H    1 
ATOM   4135 H  HA   . LEU   B 1 12  ? 33.555 -31.374 -15.037 1.00 20.74 ?  12   LEU   B HA   1 
ATOM   4136 H  HB2  . LEU   B 1 12  ? 34.154 -29.544 -12.974 1.00 20.08 ?  12   LEU   B HB2  1 
ATOM   4137 H  HB3  . LEU   B 1 12  ? 33.414 -30.925 -12.747 1.00 20.08 ?  12   LEU   B HB3  1 
ATOM   4138 H  HG   . LEU   B 1 12  ? 36.116 -30.655 -13.485 1.00 19.61 ?  12   LEU   B HG   1 
ATOM   4139 H  HD11 . LEU   B 1 12  ? 36.637 -31.530 -11.396 1.00 20.00 ?  12   LEU   B HD11 1 
ATOM   4140 H  HD12 . LEU   B 1 12  ? 35.827 -30.172 -11.239 1.00 20.00 ?  12   LEU   B HD12 1 
ATOM   4141 H  HD13 . LEU   B 1 12  ? 35.093 -31.565 -11.026 1.00 20.00 ?  12   LEU   B HD13 1 
ATOM   4142 H  HD21 . LEU   B 1 12  ? 36.209 -33.026 -13.193 1.00 20.53 ?  12   LEU   B HD21 1 
ATOM   4143 H  HD22 . LEU   B 1 12  ? 34.621 -33.017 -13.199 1.00 20.53 ?  12   LEU   B HD22 1 
ATOM   4144 H  HD23 . LEU   B 1 12  ? 35.423 -32.558 -14.491 1.00 20.53 ?  12   LEU   B HD23 1 
ATOM   4145 N  N    . THR   B 1 13  ? 32.141 -28.536 -14.711 1.00 16.78 ?  13   THR   B N    1 
ATOM   4146 C  CA   . THR   B 1 13  ? 30.921 -27.781 -14.918 1.00 16.55 ?  13   THR   B CA   1 
ATOM   4147 C  C    . THR   B 1 13  ? 31.263 -26.593 -15.805 1.00 18.57 ?  13   THR   B C    1 
ATOM   4148 O  O    . THR   B 1 13  ? 32.411 -26.410 -16.224 1.00 19.44 ?  13   THR   B O    1 
ATOM   4149 C  CB   . THR   B 1 13  ? 30.325 -27.301 -13.591 1.00 16.16 ?  13   THR   B CB   1 
ATOM   4150 O  OG1  . THR   B 1 13  ? 31.172 -26.282 -13.044 1.00 16.03 ?  13   THR   B OG1  1 
ATOM   4151 C  CG2  . THR   B 1 13  ? 30.193 -28.455 -12.599 1.00 16.69 ?  13   THR   B CG2  1 
ATOM   4152 H  H    . THR   B 1 13  ? 32.808 -28.034 -14.508 1.00 20.16 ?  13   THR   B H    1 
ATOM   4153 H  HA   . THR   B 1 13  ? 30.263 -28.334 -15.370 1.00 19.89 ?  13   THR   B HA   1 
ATOM   4154 H  HB   . THR   B 1 13  ? 29.433 -26.936 -13.750 1.00 19.42 ?  13   THR   B HB   1 
ATOM   4155 H  HG1  . THR   B 1 13  ? 30.862 -25.520 -13.241 1.00 19.25 ?  13   THR   B HG1  1 
ATOM   4156 H  HG21 . THR   B 1 13  ? 29.700 -28.169 -11.813 1.00 20.05 ?  13   THR   B HG21 1 
ATOM   4157 H  HG22 . THR   B 1 13  ? 29.717 -29.197 -13.011 1.00 20.05 ?  13   THR   B HG22 1 
ATOM   4158 H  HG23 . THR   B 1 13  ? 31.071 -28.761 -12.326 1.00 20.05 ?  13   THR   B HG23 1 
ATOM   4159 N  N    A ASP   B 1 14  ? 30.255 -25.768 -16.085 0.50 19.36 ?  14   ASP   B N    1 
ATOM   4160 N  N    B ASP   B 1 14  ? 30.260 -25.759 -16.083 0.50 19.35 ?  14   ASP   B N    1 
ATOM   4161 C  CA   A ASP   B 1 14  ? 30.482 -24.614 -16.944 0.50 20.72 ?  14   ASP   B CA   1 
ATOM   4162 C  CA   B ASP   B 1 14  ? 30.481 -24.612 -16.956 0.50 20.63 ?  14   ASP   B CA   1 
ATOM   4163 C  C    A ASP   B 1 14  ? 31.589 -23.718 -16.404 0.50 18.97 ?  14   ASP   B C    1 
ATOM   4164 C  C    B ASP   B 1 14  ? 31.466 -23.605 -16.379 0.50 19.01 ?  14   ASP   B C    1 
ATOM   4165 O  O    A ASP   B 1 14  ? 32.297 -23.074 -17.187 0.50 19.56 ?  14   ASP   B O    1 
ATOM   4166 O  O    B ASP   B 1 14  ? 31.919 -22.722 -17.114 0.50 19.63 ?  14   ASP   B O    1 
ATOM   4167 C  CB   A ASP   B 1 14  ? 29.181 -23.829 -17.130 0.50 23.92 ?  14   ASP   B CB   1 
ATOM   4168 C  CB   B ASP   B 1 14  ? 29.165 -23.896 -17.253 0.50 23.69 ?  14   ASP   B CB   1 
ATOM   4169 C  CG   A ASP   B 1 14  ? 28.202 -24.526 -18.049 0.50 27.06 ?  14   ASP   B CG   1 
ATOM   4170 C  CG   B ASP   B 1 14  ? 28.294 -24.666 -18.227 0.50 26.69 ?  14   ASP   B CG   1 
ATOM   4171 O  OD1  A ASP   B 1 14  ? 28.542 -25.592 -18.609 0.50 28.03 ?  14   ASP   B OD1  1 
ATOM   4172 O  OD1  B ASP   B 1 14  ? 28.856 -25.371 -19.093 0.50 27.61 ?  14   ASP   B OD1  1 
ATOM   4173 O  OD2  A ASP   B 1 14  ? 27.079 -24.002 -18.205 0.50 28.17 -1 14   ASP   B OD2  1 
ATOM   4174 O  OD2  B ASP   B 1 14  ? 27.053 -24.572 -18.128 0.50 27.61 -1 14   ASP   B OD2  1 
ATOM   4175 H  H    A ASP   B 1 14  ? 29.454 -25.843 -15.786 0.50 23.25 ?  14   ASP   B H    1 
ATOM   4176 H  H    B ASP   B 1 14  ? 29.458 -25.834 -15.785 0.50 23.24 ?  14   ASP   B H    1 
ATOM   4177 H  HA   A ASP   B 1 14  ? 30.770 -24.914 -17.813 0.50 24.88 ?  14   ASP   B HA   1 
ATOM   4178 H  HA   B ASP   B 1 14  ? 30.840 -24.926 -17.799 0.50 24.78 ?  14   ASP   B HA   1 
ATOM   4179 H  HB2  A ASP   B 1 14  ? 28.735 -23.729 -16.279 0.50 28.73 ?  14   ASP   B HB2  1 
ATOM   4180 H  HB2  B ASP   B 1 14  ? 28.673 -23.784 -16.424 0.50 28.46 ?  14   ASP   B HB2  1 
ATOM   4181 H  HB3  A ASP   B 1 14  ? 29.374 -22.962 -17.515 0.50 28.73 ?  14   ASP   B HB3  1 
ATOM   4182 H  HB3  B ASP   B 1 14  ? 29.362 -23.022 -17.637 0.50 28.46 ?  14   ASP   B HB3  1 
ATOM   4183 N  N    . ASN   B 1 15  ? 31.781 -23.687 -15.082 1.00 16.96 ?  15   ASN   B N    1 
ATOM   4184 C  CA   . ASN   B 1 15  ? 32.737 -22.767 -14.469 1.00 14.77 ?  15   ASN   B CA   1 
ATOM   4185 C  C    . ASN   B 1 15  ? 33.829 -23.419 -13.631 1.00 13.69 ?  15   ASN   B C    1 
ATOM   4186 O  O    . ASN   B 1 15  ? 34.681 -22.693 -13.106 1.00 13.64 ?  15   ASN   B O    1 
ATOM   4187 C  CB   . ASN   B 1 15  ? 32.017 -21.717 -13.607 1.00 14.85 ?  15   ASN   B CB   1 
ATOM   4188 C  CG   . ASN   B 1 15  ? 31.403 -22.318 -12.366 1.00 14.51 ?  15   ASN   B CG   1 
ATOM   4189 O  OD1  . ASN   B 1 15  ? 30.464 -23.112 -12.452 1.00 16.17 ?  15   ASN   B OD1  1 
ATOM   4190 N  ND2  . ASN   B 1 15  ? 31.931 -21.966 -11.205 1.00 13.54 ?  15   ASN   B ND2  1 
ATOM   4191 H  H    A ASN   B 1 15  ? 31.377 -24.198 -14.520 0.50 20.37 ?  15   ASN   B H    1 
ATOM   4192 H  H    B ASN   B 1 15  ? 31.423 -24.240 -14.530 0.50 20.37 ?  15   ASN   B H    1 
ATOM   4193 H  HA   . ASN   B 1 15  ? 33.182 -22.276 -15.169 1.00 17.75 ?  15   ASN   B HA   1 
ATOM   4194 H  HB2  . ASN   B 1 15  ? 32.656 -21.036 -13.328 1.00 17.84 ?  15   ASN   B HB2  1 
ATOM   4195 H  HB3  . ASN   B 1 15  ? 31.304 -21.303 -14.122 1.00 17.84 ?  15   ASN   B HB3  1 
ATOM   4196 H  HD21 . ASN   B 1 15  ? 31.613 -22.280 -10.466 1.00 16.27 ?  15   ASN   B HD21 1 
ATOM   4197 H  HD22 . ASN   B 1 15  ? 32.592 -21.409 -11.175 1.00 16.27 ?  15   ASN   B HD22 1 
ATOM   4198 N  N    . VAL   B 1 16  ? 33.838 -24.741 -13.476 1.00 13.61 ?  16   VAL   B N    1 
ATOM   4199 C  CA   . VAL   B 1 16  ? 34.839 -25.431 -12.669 1.00 13.28 ?  16   VAL   B CA   1 
ATOM   4200 C  C    . VAL   B 1 16  ? 35.630 -26.368 -13.567 1.00 13.68 ?  16   VAL   B C    1 
ATOM   4201 O  O    . VAL   B 1 16  ? 35.052 -27.244 -14.229 1.00 14.57 ?  16   VAL   B O    1 
ATOM   4202 C  CB   . VAL   B 1 16  ? 34.212 -26.205 -11.497 1.00 13.56 ?  16   VAL   B CB   1 
ATOM   4203 C  CG1  . VAL   B 1 16  ? 35.299 -26.934 -10.710 1.00 13.37 ?  16   VAL   B CG1  1 
ATOM   4204 C  CG2  . VAL   B 1 16  ? 33.413 -25.262 -10.597 1.00 14.54 ?  16   VAL   B CG2  1 
ATOM   4205 H  H    . VAL   B 1 16  ? 33.257 -25.270 -13.836 1.00 16.35 ?  16   VAL   B H    1 
ATOM   4206 H  HA   . VAL   B 1 16  ? 35.449 -24.775 -12.297 1.00 15.95 ?  16   VAL   B HA   1 
ATOM   4207 H  HB   . VAL   B 1 16  ? 33.600 -26.872 -11.852 1.00 16.30 ?  16   VAL   B HB   1 
ATOM   4208 H  HG11 . VAL   B 1 16  ? 34.927 -27.231 -9.865  1.00 16.06 ?  16   VAL   B HG11 1 
ATOM   4209 H  HG12 . VAL   B 1 16  ? 35.606 -27.697 -11.222 1.00 16.06 ?  16   VAL   B HG12 1 
ATOM   4210 H  HG13 . VAL   B 1 16  ? 36.034 -26.321 -10.550 1.00 16.06 ?  16   VAL   B HG13 1 
ATOM   4211 H  HG21 . VAL   B 1 16  ? 33.070 -25.767 -9.841  1.00 17.47 ?  16   VAL   B HG21 1 
ATOM   4212 H  HG22 . VAL   B 1 16  ? 33.994 -24.555 -10.287 1.00 17.47 ?  16   VAL   B HG22 1 
ATOM   4213 H  HG23 . VAL   B 1 16  ? 32.675 -24.890 -11.105 1.00 17.47 ?  16   VAL   B HG23 1 
ATOM   4214 N  N    . TYR   B 1 17  ? 36.953 -26.201 -13.546 1.00 13.79 ?  17   TYR   B N    1 
ATOM   4215 C  CA   . TYR   B 1 17  ? 37.900 -26.949 -14.356 1.00 14.23 ?  17   TYR   B CA   1 
ATOM   4216 C  C    . TYR   B 1 17  ? 38.952 -27.559 -13.439 1.00 13.49 ?  17   TYR   B C    1 
ATOM   4217 O  O    . TYR   B 1 17  ? 39.227 -27.032 -12.357 1.00 13.73 ?  17   TYR   B O    1 
ATOM   4218 C  CB   . TYR   B 1 17  ? 38.607 -26.024 -15.352 1.00 16.49 ?  17   TYR   B CB   1 
ATOM   4219 C  CG   . TYR   B 1 17  ? 37.682 -25.256 -16.263 1.00 19.65 ?  17   TYR   B CG   1 
ATOM   4220 C  CD1  . TYR   B 1 17  ? 37.105 -24.058 -15.857 1.00 21.37 ?  17   TYR   B CD1  1 
ATOM   4221 C  CD2  . TYR   B 1 17  ? 37.391 -25.724 -17.535 1.00 21.73 ?  17   TYR   B CD2  1 
ATOM   4222 C  CE1  . TYR   B 1 17  ? 36.258 -23.350 -16.694 1.00 23.05 ?  17   TYR   B CE1  1 
ATOM   4223 C  CE2  . TYR   B 1 17  ? 36.550 -25.023 -18.381 1.00 23.20 ?  17   TYR   B CE2  1 
ATOM   4224 C  CZ   . TYR   B 1 17  ? 35.986 -23.838 -17.954 1.00 24.15 ?  17   TYR   B CZ   1 
ATOM   4225 O  OH   . TYR   B 1 17  ? 35.147 -23.141 -18.793 1.00 25.42 ?  17   TYR   B OH   1 
ATOM   4226 H  H    . TYR   B 1 17  ? 37.347 -25.620 -13.042 1.00 16.57 ?  17   TYR   B H    1 
ATOM   4227 H  HA   . TYR   B 1 17  ? 37.438 -27.655 -14.842 1.00 17.09 ?  17   TYR   B HA   1 
ATOM   4228 H  HB2  . TYR   B 1 17  ? 39.145 -25.385 -14.862 1.00 19.81 ?  17   TYR   B HB2  1 
ATOM   4229 H  HB3  . TYR   B 1 17  ? 39.173 -26.566 -15.917 1.00 19.81 ?  17   TYR   B HB3  1 
ATOM   4230 H  HD1  . TYR   B 1 17  ? 37.289 -23.726 -15.009 1.00 25.67 ?  17   TYR   B HD1  1 
ATOM   4231 H  HD2  . TYR   B 1 17  ? 37.767 -26.523 -17.827 1.00 26.10 ?  17   TYR   B HD2  1 
ATOM   4232 H  HE1  . TYR   B 1 17  ? 35.879 -22.549 -16.410 1.00 27.69 ?  17   TYR   B HE1  1 
ATOM   4233 H  HE2  . TYR   B 1 17  ? 36.360 -25.351 -19.232 1.00 27.86 ?  17   TYR   B HE2  1 
ATOM   4234 H  HH   . TYR   B 1 17  ? 35.067 -23.546 -19.525 1.00 30.53 ?  17   TYR   B HH   1 
ATOM   4235 N  N    . ILE   B 1 18  ? 39.561 -28.664 -13.871 1.00 13.53 ?  18   ILE   B N    1 
ATOM   4236 C  CA   . ILE   B 1 18  ? 40.486 -29.387 -13.008 1.00 13.41 ?  18   ILE   B CA   1 
ATOM   4237 C  C    . ILE   B 1 18  ? 41.643 -29.943 -13.826 1.00 13.92 ?  18   ILE   B C    1 
ATOM   4238 O  O    . ILE   B 1 18  ? 41.482 -30.339 -14.984 1.00 15.33 ?  18   ILE   B O    1 
ATOM   4239 C  CB   . ILE   B 1 18  ? 39.741 -30.488 -12.210 1.00 13.75 ?  18   ILE   B CB   1 
ATOM   4240 C  CG1  . ILE   B 1 18  ? 40.602 -31.026 -11.065 1.00 14.25 ?  18   ILE   B CG1  1 
ATOM   4241 C  CG2  . ILE   B 1 18  ? 39.245 -31.604 -13.141 1.00 14.06 ?  18   ILE   B CG2  1 
ATOM   4242 C  CD1  . ILE   B 1 18  ? 39.806 -31.851 -10.062 1.00 15.71 ?  18   ILE   B CD1  1 
ATOM   4243 H  H    . ILE   B 1 18  ? 39.455 -29.011 -14.650 1.00 16.26 ?  18   ILE   B H    1 
ATOM   4244 H  HA   . ILE   B 1 18  ? 40.849 -28.772 -12.358 1.00 16.11 ?  18   ILE   B HA   1 
ATOM   4245 H  HB   . ILE   B 1 18  ? 38.954 -30.088 -11.810 1.00 16.52 ?  18   ILE   B HB   1 
ATOM   4246 H  HG12 . ILE   B 1 18  ? 41.300 -31.589 -11.427 1.00 17.12 ?  18   ILE   B HG12 1 
ATOM   4247 H  HG13 . ILE   B 1 18  ? 40.990 -30.275 -10.588 1.00 17.12 ?  18   ILE   B HG13 1 
ATOM   4248 H  HG21 . ILE   B 1 18  ? 38.650 -32.191 -12.645 1.00 16.89 ?  18   ILE   B HG21 1 
ATOM   4249 H  HG22 . ILE   B 1 18  ? 38.764 -31.201 -13.881 1.00 16.89 ?  18   ILE   B HG22 1 
ATOM   4250 H  HG23 . ILE   B 1 18  ? 40.004 -32.105 -13.471 1.00 16.89 ?  18   ILE   B HG23 1 
ATOM   4251 H  HD11 . ILE   B 1 18  ? 40.395 -32.123 -9.341  1.00 18.88 ?  18   ILE   B HD11 1 
ATOM   4252 H  HD12 . ILE   B 1 18  ? 39.081 -31.310 -9.712  1.00 18.88 ?  18   ILE   B HD12 1 
ATOM   4253 H  HD13 . ILE   B 1 18  ? 39.449 -32.633 -10.510 1.00 18.88 ?  18   ILE   B HD13 1 
ATOM   4254 N  N    . LYS   B 1 19  ? 42.821 -29.977 -13.204 1.00 14.41 ?  19   LYS   B N    1 
ATOM   4255 C  CA   . LYS   B 1 19  ? 44.032 -30.446 -13.861 1.00 15.50 ?  19   LYS   B CA   1 
ATOM   4256 C  C    . LYS   B 1 19  ? 44.931 -31.126 -12.841 1.00 15.21 ?  19   LYS   B C    1 
ATOM   4257 O  O    . LYS   B 1 19  ? 45.016 -30.694 -11.690 1.00 14.54 ?  19   LYS   B O    1 
ATOM   4258 C  CB   . LYS   B 1 19  ? 44.799 -29.280 -14.497 1.00 16.77 ?  19   LYS   B CB   1 
ATOM   4259 C  CG   . LYS   B 1 19  ? 45.997 -29.693 -15.329 1.00 18.66 ?  19   LYS   B CG   1 
ATOM   4260 C  CD   . LYS   B 1 19  ? 46.715 -28.469 -15.882 1.00 20.34 ?  19   LYS   B CD   1 
ATOM   4261 C  CE   . LYS   B 1 19  ? 47.919 -28.854 -16.719 1.00 22.14 ?  19   LYS   B CE   1 
ATOM   4262 N  NZ   . LYS   B 1 19  ? 48.621 -27.657 -17.248 1.00 22.92 ?  19   LYS   B NZ   1 
ATOM   4263 H  H    . LYS   B 1 19  ? 42.935 -29.724 -12.386 1.00 17.31 ?  19   LYS   B H    1 
ATOM   4264 H  HA   . LYS   B 1 19  ? 43.795 -31.084 -14.550 1.00 18.63 ?  19   LYS   B HA   1 
ATOM   4265 H  HB2  . LYS   B 1 19  ? 44.192 -28.793 -15.072 1.00 20.15 ?  19   LYS   B HB2  1 
ATOM   4266 H  HB3  . LYS   B 1 19  ? 45.114 -28.696 -13.784 1.00 20.15 ?  19   LYS   B HB3  1 
ATOM   4267 H  HG2  . LYS   B 1 19  ? 46.614 -30.193 -14.775 1.00 22.41 ?  19   LYS   B HG2  1 
ATOM   4268 H  HG3  . LYS   B 1 19  ? 45.690 -30.237 -16.072 1.00 22.41 ?  19   LYS   B HG3  1 
ATOM   4269 H  HD2  . LYS   B 1 19  ? 46.102 -27.964 -16.441 1.00 24.43 ?  19   LYS   B HD2  1 
ATOM   4270 H  HD3  . LYS   B 1 19  ? 47.020 -27.919 -15.142 1.00 24.43 ?  19   LYS   B HD3  1 
ATOM   4271 H  HE2  . LYS   B 1 19  ? 48.540 -29.359 -16.171 1.00 26.59 ?  19   LYS   B HE2  1 
ATOM   4272 H  HE3  . LYS   B 1 19  ? 47.623 -29.394 -17.471 1.00 26.59 ?  19   LYS   B HE3  1 
ATOM   4273 H  HZ1  . LYS   B 1 19  ? 49.275 -27.907 -17.799 1.00 27.53 ?  19   LYS   B HZ1  1 
ATOM   4274 H  HZ2  . LYS   B 1 19  ? 48.050 -27.141 -17.694 1.00 27.53 ?  19   LYS   B HZ2  1 
ATOM   4275 H  HZ3  . LYS   B 1 19  ? 48.972 -27.189 -16.579 1.00 27.53 ?  19   LYS   B HZ3  1 
ATOM   4276 N  N    . ASN   B 1 20  ? 45.613 -32.181 -13.274 1.00 16.45 ?  20   ASN   B N    1 
ATOM   4277 C  CA   . ASN   B 1 20  ? 46.642 -32.809 -12.455 1.00 17.18 ?  20   ASN   B CA   1 
ATOM   4278 C  C    . ASN   B 1 20  ? 47.922 -31.998 -12.636 1.00 17.56 ?  20   ASN   B C    1 
ATOM   4279 O  O    . ASN   B 1 20  ? 48.569 -32.076 -13.686 1.00 19.51 ?  20   ASN   B O    1 
ATOM   4280 C  CB   . ASN   B 1 20  ? 46.809 -34.267 -12.883 1.00 18.95 ?  20   ASN   B CB   1 
ATOM   4281 C  CG   . ASN   B 1 20  ? 47.976 -34.963 -12.206 1.00 20.50 ?  20   ASN   B CG   1 
ATOM   4282 O  OD1  . ASN   B 1 20  ? 48.640 -35.809 -12.816 1.00 22.44 ?  20   ASN   B OD1  1 
ATOM   4283 N  ND2  . ASN   B 1 20  ? 48.224 -34.637 -10.946 1.00 20.16 ?  20   ASN   B ND2  1 
ATOM   4284 H  H    . ASN   B 1 20  ? 45.502 -32.544 -14.042 1.00 19.76 ?  20   ASN   B H    1 
ATOM   4285 H  HA   . ASN   B 1 20  ? 46.369 -32.792 -11.521 1.00 20.64 ?  20   ASN   B HA   1 
ATOM   4286 H  HB2  . ASN   B 1 20  ? 45.996 -34.759 -12.658 1.00 22.76 ?  20   ASN   B HB2  1 
ATOM   4287 H  HB3  . ASN   B 1 20  ? 46.954 -34.300 -13.838 1.00 22.76 ?  20   ASN   B HB3  1 
ATOM   4288 H  HD21 . ASN   B 1 20  ? 48.879 -35.004 -10.528 1.00 24.22 ?  20   ASN   B HD21 1 
ATOM   4289 H  HD22 . ASN   B 1 20  ? 47.743 -34.042 -10.546 1.00 24.22 ?  20   ASN   B HD22 1 
ATOM   4290 N  N    . ALA   B 1 21  ? 48.277 -31.197 -11.631 1.00 17.17 ?  21   ALA   B N    1 
ATOM   4291 C  CA   . ALA   B 1 21  ? 49.393 -30.281 -11.792 1.00 17.65 ?  21   ALA   B CA   1 
ATOM   4292 C  C    . ALA   B 1 21  ? 49.851 -29.769 -10.437 1.00 16.62 ?  21   ALA   B C    1 
ATOM   4293 O  O    . ALA   B 1 21  ? 49.107 -29.786 -9.452  1.00 16.17 ?  21   ALA   B O    1 
ATOM   4294 C  CB   . ALA   B 1 21  ? 49.008 -29.117 -12.702 1.00 18.75 ?  21   ALA   B CB   1 
ATOM   4295 H  H    . ALA   B 1 21  ? 47.890 -31.176 -10.856 1.00 20.62 ?  21   ALA   B H    1 
ATOM   4296 H  HA   . ALA   B 1 21  ? 50.131 -30.763 -12.195 1.00 21.20 ?  21   ALA   B HA   1 
ATOM   4297 H  HB1  . ALA   B 1 21  ? 49.799 -28.596 -12.871 1.00 22.52 ?  21   ALA   B HB1  1 
ATOM   4298 H  HB2  . ALA   B 1 21  ? 48.663 -29.485 -13.532 1.00 22.52 ?  21   ALA   B HB2  1 
ATOM   4299 H  HB3  . ALA   B 1 21  ? 48.328 -28.591 -12.263 1.00 22.52 ?  21   ALA   B HB3  1 
ATOM   4300 N  N    . ASP   B 1 22  ? 51.107 -29.322 -10.420 1.00 15.89 ?  22   ASP   B N    1 
ATOM   4301 C  CA   . ASP   B 1 22  ? 51.723 -28.625 -9.297  1.00 15.25 ?  22   ASP   B CA   1 
ATOM   4302 C  C    . ASP   B 1 22  ? 51.313 -27.154 -9.377  1.00 13.59 ?  22   ASP   B C    1 
ATOM   4303 O  O    . ASP   B 1 22  ? 51.617 -26.480 -10.366 1.00 13.92 ?  22   ASP   B O    1 
ATOM   4304 C  CB   . ASP   B 1 22  ? 53.240 -28.801 -9.456  1.00 16.51 ?  22   ASP   B CB   1 
ATOM   4305 C  CG   . ASP   B 1 22  ? 54.067 -28.050 -8.422  1.00 18.21 ?  22   ASP   B CG   1 
ATOM   4306 O  OD1  . ASP   B 1 22  ? 53.694 -26.937 -8.015  1.00 18.25 ?  22   ASP   B OD1  1 
ATOM   4307 O  OD2  . ASP   B 1 22  ? 55.139 -28.572 -8.042  1.00 20.85 -1 22   ASP   B OD2  1 
ATOM   4308 H  H    . ASP   B 1 22  ? 51.646 -29.422 -11.085 1.00 19.09 ?  22   ASP   B H    1 
ATOM   4309 H  HA   . ASP   B 1 22  ? 51.437 -29.009 -8.452  1.00 18.32 ?  22   ASP   B HA   1 
ATOM   4310 H  HB2  . ASP   B 1 22  ? 53.462 -29.739 -9.381  1.00 19.84 ?  22   ASP   B HB2  1 
ATOM   4311 H  HB3  . ASP   B 1 22  ? 53.504 -28.467 -10.329 1.00 19.84 ?  22   ASP   B HB3  1 
ATOM   4312 N  N    . ILE   B 1 23  ? 50.596 -26.666 -8.357  1.00 12.90 ?  23   ILE   B N    1 
ATOM   4313 C  CA   . ILE   B 1 23  ? 50.009 -25.324 -8.421  1.00 12.34 ?  23   ILE   B CA   1 
ATOM   4314 C  C    . ILE   B 1 23  ? 51.066 -24.235 -8.555  1.00 11.92 ?  23   ILE   B C    1 
ATOM   4315 O  O    . ILE   B 1 23  ? 50.803 -23.192 -9.162  1.00 11.58 ?  23   ILE   B O    1 
ATOM   4316 C  CB   . ILE   B 1 23  ? 49.070 -25.083 -7.224  1.00 12.54 ?  23   ILE   B CB   1 
ATOM   4317 C  CG1  . ILE   B 1 23  ? 48.247 -23.813 -7.428  1.00 13.13 ?  23   ILE   B CG1  1 
ATOM   4318 C  CG2  . ILE   B 1 23  ? 49.841 -25.052 -5.913  1.00 13.23 ?  23   ILE   B CG2  1 
ATOM   4319 C  CD1  . ILE   B 1 23  ? 47.115 -23.658 -6.429  1.00 13.80 ?  23   ILE   B CD1  1 
ATOM   4320 H  H    . ILE   B 1 23  ? 50.431 -27.094 -7.630  1.00 15.50 ?  23   ILE   B H    1 
ATOM   4321 H  HA   . ILE   B 1 23  ? 49.459 -25.279 -9.217  1.00 14.84 ?  23   ILE   B HA   1 
ATOM   4322 H  HB   . ILE   B 1 23  ? 48.447 -25.826 -7.183  1.00 15.07 ?  23   ILE   B HB   1 
ATOM   4323 H  HG12 . ILE   B 1 23  ? 48.834 -23.041 -7.335  1.00 15.78 ?  23   ILE   B HG12 1 
ATOM   4324 H  HG13 . ILE   B 1 23  ? 47.864 -23.823 -8.320  1.00 15.78 ?  23   ILE   B HG13 1 
ATOM   4325 H  HG21 . ILE   B 1 23  ? 49.210 -25.046 -5.177  1.00 15.90 ?  23   ILE   B HG21 1 
ATOM   4326 H  HG22 . ILE   B 1 23  ? 50.401 -25.842 -5.862  1.00 15.90 ?  23   ILE   B HG22 1 
ATOM   4327 H  HG23 . ILE   B 1 23  ? 50.390 -24.254 -5.889  1.00 15.90 ?  23   ILE   B HG23 1 
ATOM   4328 H  HD11 . ILE   B 1 23  ? 46.596 -22.874 -6.662  1.00 16.58 ?  23   ILE   B HD11 1 
ATOM   4329 H  HD12 . ILE   B 1 23  ? 46.557 -24.450 -6.470  1.00 16.58 ?  23   ILE   B HD12 1 
ATOM   4330 H  HD13 . ILE   B 1 23  ? 47.490 -23.559 -5.542  1.00 16.58 ?  23   ILE   B HD13 1 
ATOM   4331 N  N    . VAL   B 1 24  ? 52.259 -24.442 -7.995  1.00 12.21 ?  24   VAL   B N    1 
ATOM   4332 C  CA   . VAL   B 1 24  ? 53.334 -23.466 -8.163  1.00 12.67 ?  24   VAL   B CA   1 
ATOM   4333 C  C    . VAL   B 1 24  ? 53.785 -23.422 -9.615  1.00 12.70 ?  24   VAL   B C    1 
ATOM   4334 O  O    . VAL   B 1 24  ? 53.927 -22.347 -10.210 1.00 13.37 ?  24   VAL   B O    1 
ATOM   4335 C  CB   . VAL   B 1 24  ? 54.509 -23.782 -7.218  1.00 13.60 ?  24   VAL   B CB   1 
ATOM   4336 C  CG1  . VAL   B 1 24  ? 55.717 -22.910 -7.550  1.00 14.64 ?  24   VAL   B CG1  1 
ATOM   4337 C  CG2  . VAL   B 1 24  ? 54.095 -23.590 -5.775  1.00 14.89 ?  24   VAL   B CG2  1 
ATOM   4338 H  H    . VAL   B 1 24  ? 52.466 -25.129 -7.519  1.00 14.68 ?  24   VAL   B H    1 
ATOM   4339 H  HA   . VAL   B 1 24  ? 52.999 -22.591 -7.927  1.00 15.22 ?  24   VAL   B HA   1 
ATOM   4340 H  HB   . VAL   B 1 24  ? 54.770 -24.712 -7.328  1.00 16.34 ?  24   VAL   B HB   1 
ATOM   4341 H  HG11 . VAL   B 1 24  ? 56.321 -22.908 -6.790  1.00 17.59 ?  24   VAL   B HG11 1 
ATOM   4342 H  HG12 . VAL   B 1 24  ? 56.166 -23.275 -8.326  1.00 17.59 ?  24   VAL   B HG12 1 
ATOM   4343 H  HG13 . VAL   B 1 24  ? 55.411 -22.008 -7.730  1.00 17.59 ?  24   VAL   B HG13 1 
ATOM   4344 H  HG21 . VAL   B 1 24  ? 54.825 -23.857 -5.196  1.00 17.89 ?  24   VAL   B HG21 1 
ATOM   4345 H  HG22 . VAL   B 1 24  ? 53.882 -22.655 -5.631  1.00 17.89 ?  24   VAL   B HG22 1 
ATOM   4346 H  HG23 . VAL   B 1 24  ? 53.313 -24.139 -5.594  1.00 17.89 ?  24   VAL   B HG23 1 
ATOM   4347 N  N    . GLU   B 1 25  ? 54.049 -24.592 -10.201 1.00 13.79 ?  25   GLU   B N    1 
ATOM   4348 C  CA   . GLU   B 1 25  ? 54.442 -24.631 -11.603 1.00 15.45 ?  25   GLU   B CA   1 
ATOM   4349 C  C    . GLU   B 1 25  ? 53.335 -24.084 -12.490 1.00 14.23 ?  25   GLU   B C    1 
ATOM   4350 O  O    . GLU   B 1 25  ? 53.605 -23.369 -13.465 1.00 15.03 ?  25   GLU   B O    1 
ATOM   4351 C  CB   . GLU   B 1 25  ? 54.832 -26.054 -12.001 1.00 19.47 ?  25   GLU   B CB   1 
ATOM   4352 C  CG   . GLU   B 1 25  ? 56.139 -26.506 -11.363 1.00 25.26 ?  25   GLU   B CG   1 
ATOM   4353 C  CD   . GLU   B 1 25  ? 57.250 -25.471 -11.464 1.00 30.47 ?  25   GLU   B CD   1 
ATOM   4354 O  OE1  . GLU   B 1 25  ? 57.608 -25.085 -12.598 1.00 32.48 ?  25   GLU   B OE1  1 
ATOM   4355 O  OE2  . GLU   B 1 25  ? 57.755 -25.027 -10.407 1.00 32.35 -1 25   GLU   B OE2  1 
ATOM   4356 H  H    . GLU   B 1 25  ? 54.009 -25.360 -9.814  1.00 16.57 ?  25   GLU   B H    1 
ATOM   4357 H  HA   . GLU   B 1 25  ? 55.202 -24.049 -11.729 1.00 18.56 ?  25   GLU   B HA   1 
ATOM   4358 H  HB2  . GLU   B 1 25  ? 54.134 -26.667 -11.713 1.00 23.39 ?  25   GLU   B HB2  1 
ATOM   4359 H  HB3  . GLU   B 1 25  ? 54.932 -26.099 -12.965 1.00 23.39 ?  25   GLU   B HB3  1 
ATOM   4360 H  HG2  . GLU   B 1 25  ? 55.992 -26.672 -10.425 1.00 30.33 ?  25   GLU   B HG2  1 
ATOM   4361 H  HG3  . GLU   B 1 25  ? 56.447 -27.306 -11.810 1.00 30.33 ?  25   GLU   B HG3  1 
ATOM   4362 N  N    A GLU   B 1 26  ? 52.080 -24.402 -12.165 0.50 13.60 ?  26   GLU   B N    1 
ATOM   4363 N  N    B GLU   B 1 26  ? 52.080 -24.407 -12.164 0.50 13.83 ?  26   GLU   B N    1 
ATOM   4364 C  CA   A GLU   B 1 26  ? 50.957 -23.872 -12.930 0.50 13.82 ?  26   GLU   B CA   1 
ATOM   4365 C  CA   B GLU   B 1 26  ? 50.948 -23.879 -12.921 0.50 14.31 ?  26   GLU   B CA   1 
ATOM   4366 C  C    A GLU   B 1 26  ? 50.909 -22.355 -12.850 0.50 13.26 ?  26   GLU   B C    1 
ATOM   4367 C  C    B GLU   B 1 26  ? 50.903 -22.361 -12.847 0.50 13.41 ?  26   GLU   B C    1 
ATOM   4368 O  O    A GLU   B 1 26  ? 50.717 -21.674 -13.863 0.50 14.46 ?  26   GLU   B O    1 
ATOM   4369 O  O    B GLU   B 1 26  ? 50.705 -21.685 -13.863 0.50 14.48 ?  26   GLU   B O    1 
ATOM   4370 C  CB   A GLU   B 1 26  ? 49.645 -24.454 -12.406 0.50 14.95 ?  26   GLU   B CB   1 
ATOM   4371 C  CB   B GLU   B 1 26  ? 49.639 -24.459 -12.381 0.50 15.95 ?  26   GLU   B CB   1 
ATOM   4372 C  CG   A GLU   B 1 26  ? 49.322 -25.821 -12.944 0.50 17.09 ?  26   GLU   B CG   1 
ATOM   4373 C  CG   B GLU   B 1 26  ? 49.133 -25.684 -13.114 0.50 18.51 ?  26   GLU   B CG   1 
ATOM   4374 C  CD   A GLU   B 1 26  ? 49.168 -25.847 -14.452 0.50 17.44 ?  26   GLU   B CD   1 
ATOM   4375 C  CD   B GLU   B 1 26  ? 48.811 -25.397 -14.580 0.50 19.03 ?  26   GLU   B CD   1 
ATOM   4376 O  OE1  A GLU   B 1 26  ? 48.356 -25.066 -14.992 0.50 17.00 ?  26   GLU   B OE1  1 
ATOM   4377 O  OE1  B GLU   B 1 26  ? 47.747 -24.808 -14.883 0.50 19.81 ?  26   GLU   B OE1  1 
ATOM   4378 O  OE2  A GLU   B 1 26  ? 49.870 -26.651 -15.094 0.50 18.35 -1 26   GLU   B OE2  1 
ATOM   4379 O  OE2  B GLU   B 1 26  ? 49.637 -25.754 -15.435 0.50 18.64 -1 26   GLU   B OE2  1 
ATOM   4380 H  H    A GLU   B 1 26  ? 51.855 -24.923 -11.515 0.50 16.34 ?  26   GLU   B H    1 
ATOM   4381 H  H    B GLU   B 1 26  ? 51.860 -24.932 -11.517 0.50 16.61 ?  26   GLU   B H    1 
ATOM   4382 H  HA   A GLU   B 1 26  ? 51.056 -24.120 -13.860 0.50 16.61 ?  26   GLU   B HA   1 
ATOM   4383 H  HA   B GLU   B 1 26  ? 51.040 -24.134 -13.851 0.50 17.20 ?  26   GLU   B HA   1 
ATOM   4384 H  HB2  A GLU   B 1 26  ? 49.698 -24.522 -11.438 0.50 17.96 ?  26   GLU   B HB2  1 
ATOM   4385 H  HB2  B GLU   B 1 26  ? 49.766 -24.699 -11.451 0.50 19.16 ?  26   GLU   B HB2  1 
ATOM   4386 H  HB3  A GLU   B 1 26  ? 48.919 -23.855 -12.649 0.50 17.96 ?  26   GLU   B HB3  1 
ATOM   4387 H  HB3  B GLU   B 1 26  ? 48.951 -23.777 -12.448 0.50 19.16 ?  26   GLU   B HB3  1 
ATOM   4388 H  HG2  A GLU   B 1 26  ? 50.046 -26.414 -12.724 0.50 20.54 ?  26   GLU   B HG2  1 
ATOM   4389 H  HG2  B GLU   B 1 26  ? 49.811 -26.381 -13.045 0.50 22.23 ?  26   GLU   B HG2  1 
ATOM   4390 H  HG3  A GLU   B 1 26  ? 48.493 -26.122 -12.545 0.50 20.54 ?  26   GLU   B HG3  1 
ATOM   4391 H  HG3  B GLU   B 1 26  ? 48.312 -25.982 -12.698 0.50 22.23 ?  26   GLU   B HG3  1 
ATOM   4392 N  N    . ALA   B 1 27  ? 51.056 -21.806 -11.643 1.00 12.36 ?  27   ALA   B N    1 
ATOM   4393 C  CA   . ALA   B 1 27  ? 51.016 -20.357 -11.495 1.00 12.81 ?  27   ALA   B CA   1 
ATOM   4394 C  C    . ALA   B 1 27  ? 52.089 -19.696 -12.349 1.00 13.81 ?  27   ALA   B C    1 
ATOM   4395 O  O    . ALA   B 1 27  ? 51.830 -18.696 -13.033 1.00 14.49 ?  27   ALA   B O    1 
ATOM   4396 C  CB   . ALA   B 1 27  ? 51.161 -19.976 -10.021 1.00 12.68 ?  27   ALA   B CB   1 
ATOM   4397 H  H    A ALA   B 1 27  ? 51.178 -22.243 -10.910 0.50 14.86 ?  27   ALA   B H    1 
ATOM   4398 H  H    B ALA   B 1 27  ? 51.180 -22.241 -10.910 0.50 14.86 ?  27   ALA   B H    1 
ATOM   4399 H  HA   . ALA   B 1 27  ? 50.157 -20.033 -11.798 1.00 15.39 ?  27   ALA   B HA   1 
ATOM   4400 H  HB1  . ALA   B 1 27  ? 51.121 -19.010 -9.936  1.00 15.24 ?  27   ALA   B HB1  1 
ATOM   4401 H  HB2  . ALA   B 1 27  ? 50.429 -20.377 -9.518  1.00 15.24 ?  27   ALA   B HB2  1 
ATOM   4402 H  HB3  . ALA   B 1 27  ? 52.007 -20.304 -9.685  1.00 15.24 ?  27   ALA   B HB3  1 
ATOM   4403 N  N    . LYS   B 1 28  ? 53.302 -20.245 -12.335 1.00 15.14 ?  28   LYS   B N    1 
ATOM   4404 C  CA   . LYS   B 1 28  ? 54.379 -19.632 -13.102 1.00 17.14 ?  28   LYS   B CA   1 
ATOM   4405 C  C    . LYS   B 1 28  ? 54.125 -19.712 -14.603 1.00 17.93 ?  28   LYS   B C    1 
ATOM   4406 O  O    . LYS   B 1 28  ? 54.542 -18.814 -15.347 1.00 19.20 ?  28   LYS   B O    1 
ATOM   4407 C  CB   . LYS   B 1 28  ? 55.728 -20.239 -12.706 1.00 20.28 ?  28   LYS   B CB   1 
ATOM   4408 C  CG   . LYS   B 1 28  ? 56.135 -19.872 -11.281 1.00 23.54 ?  28   LYS   B CG   1 
ATOM   4409 C  CD   . LYS   B 1 28  ? 57.557 -20.291 -10.942 1.00 28.06 ?  28   LYS   B CD   1 
ATOM   4410 C  CE   . LYS   B 1 28  ? 57.662 -21.778 -10.715 1.00 32.32 ?  28   LYS   B CE   1 
ATOM   4411 N  NZ   . LYS   B 1 28  ? 59.006 -22.145 -10.187 1.00 34.48 ?  28   LYS   B NZ   1 
ATOM   4412 H  H    . LYS   B 1 28  ? 53.527 -20.952 -11.896 1.00 18.19 ?  28   LYS   B H    1 
ATOM   4413 H  HA   . LYS   B 1 28  ? 54.418 -18.692 -12.876 1.00 20.59 ?  28   LYS   B HA   1 
ATOM   4414 H  HB2  . LYS   B 1 28  ? 55.677 -21.205 -12.761 1.00 24.36 ?  28   LYS   B HB2  1 
ATOM   4415 H  HB3  . LYS   B 1 28  ? 56.419 -19.908 -13.306 1.00 24.36 ?  28   LYS   B HB3  1 
ATOM   4416 H  HG2  . LYS   B 1 28  ? 56.071 -18.908 -11.175 1.00 28.27 ?  28   LYS   B HG2  1 
ATOM   4417 H  HG3  . LYS   B 1 28  ? 55.535 -20.312 -10.660 1.00 28.27 ?  28   LYS   B HG3  1 
ATOM   4418 H  HD2  . LYS   B 1 28  ? 58.143 -20.052 -11.678 1.00 33.69 ?  28   LYS   B HD2  1 
ATOM   4419 H  HD3  . LYS   B 1 28  ? 57.837 -19.836 -10.132 1.00 33.69 ?  28   LYS   B HD3  1 
ATOM   4420 H  HE2  . LYS   B 1 28  ? 56.993 -22.052 -10.068 1.00 38.80 ?  28   LYS   B HE2  1 
ATOM   4421 H  HE3  . LYS   B 1 28  ? 57.526 -22.242 -11.556 1.00 38.80 ?  28   LYS   B HE3  1 
ATOM   4422 H  HZ1  . LYS   B 1 28  ? 59.051 -23.024 -10.058 1.00 41.40 ?  28   LYS   B HZ1  1 
ATOM   4423 H  HZ2  . LYS   B 1 28  ? 59.636 -21.904 -10.767 1.00 41.40 ?  28   LYS   B HZ2  1 
ATOM   4424 H  HZ3  . LYS   B 1 28  ? 59.151 -21.731 -9.413  1.00 41.40 ?  28   LYS   B HZ3  1 
ATOM   4425 N  N    . LYS   B 1 29  ? 53.426 -20.752 -15.063 1.00 18.91 ?  29   LYS   B N    1 
ATOM   4426 C  CA   . LYS   B 1 29  ? 53.139 -20.902 -16.487 1.00 21.99 ?  29   LYS   B CA   1 
ATOM   4427 C  C    . LYS   B 1 29  ? 51.896 -20.132 -16.925 1.00 20.94 ?  29   LYS   B C    1 
ATOM   4428 O  O    . LYS   B 1 29  ? 51.913 -19.477 -17.973 1.00 22.28 ?  29   LYS   B O    1 
ATOM   4429 C  CB   . LYS   B 1 29  ? 52.972 -22.385 -16.834 1.00 26.68 ?  29   LYS   B CB   1 
ATOM   4430 C  CG   . LYS   B 1 29  ? 52.837 -22.663 -18.325 1.00 31.36 ?  29   LYS   B CG   1 
ATOM   4431 C  CD   . LYS   B 1 29  ? 53.074 -24.134 -18.650 1.00 34.79 ?  29   LYS   B CD   1 
ATOM   4432 C  CE   . LYS   B 1 29  ? 51.947 -25.017 -18.144 1.00 37.26 ?  29   LYS   B CE   1 
ATOM   4433 N  NZ   . LYS   B 1 29  ? 52.189 -26.456 -18.452 1.00 38.88 ?  29   LYS   B NZ   1 
ATOM   4434 H  H    . LYS   B 1 29  ? 53.108 -21.388 -14.568 1.00 22.72 ?  29   LYS   B H    1 
ATOM   4435 H  HA   . LYS   B 1 29  ? 53.890 -20.560 -16.993 1.00 26.41 ?  29   LYS   B HA   1 
ATOM   4436 H  HB2  . LYS   B 1 29  ? 53.751 -22.868 -16.514 1.00 32.03 ?  29   LYS   B HB2  1 
ATOM   4437 H  HB3  . LYS   B 1 29  ? 52.175 -22.721 -16.398 1.00 32.03 ?  29   LYS   B HB3  1 
ATOM   4438 H  HG2  . LYS   B 1 29  ? 51.940 -22.430 -18.613 1.00 37.65 ?  29   LYS   B HG2  1 
ATOM   4439 H  HG3  . LYS   B 1 29  ? 53.492 -22.136 -18.809 1.00 37.65 ?  29   LYS   B HG3  1 
ATOM   4440 H  HD2  . LYS   B 1 29  ? 53.135 -24.243 -19.612 1.00 41.77 ?  29   LYS   B HD2  1 
ATOM   4441 H  HD3  . LYS   B 1 29  ? 53.899 -24.426 -18.229 1.00 41.77 ?  29   LYS   B HD3  1 
ATOM   4442 H  HE2  . LYS   B 1 29  ? 51.872 -24.923 -17.182 1.00 44.73 ?  29   LYS   B HE2  1 
ATOM   4443 H  HE3  . LYS   B 1 29  ? 51.117 -24.752 -18.571 1.00 44.73 ?  29   LYS   B HE3  1 
ATOM   4444 H  HZ1  . LYS   B 1 29  ? 51.515 -26.951 -18.146 1.00 46.68 ?  29   LYS   B HZ1  1 
ATOM   4445 H  HZ2  . LYS   B 1 29  ? 52.256 -26.572 -19.332 1.00 46.68 ?  29   LYS   B HZ2  1 
ATOM   4446 H  HZ3  . LYS   B 1 29  ? 52.944 -26.727 -18.066 1.00 46.68 ?  29   LYS   B HZ3  1 
ATOM   4447 N  N    . VAL   B 1 30  ? 50.817 -20.211 -16.141 1.00 19.07 ?  30   VAL   B N    1 
ATOM   4448 C  CA   . VAL   B 1 30  ? 49.530 -19.621 -16.516 1.00 18.99 ?  30   VAL   B CA   1 
ATOM   4449 C  C    . VAL   B 1 30  ? 49.535 -18.107 -16.366 1.00 17.80 ?  30   VAL   B C    1 
ATOM   4450 O  O    . VAL   B 1 30  ? 48.789 -17.401 -17.061 1.00 18.66 ?  30   VAL   B O    1 
ATOM   4451 C  CB   . VAL   B 1 30  ? 48.423 -20.234 -15.634 1.00 20.51 ?  30   VAL   B CB   1 
ATOM   4452 C  CG1  . VAL   B 1 30  ? 47.141 -19.410 -15.706 1.00 21.09 ?  30   VAL   B CG1  1 
ATOM   4453 C  CG2  . VAL   B 1 30  ? 48.169 -21.686 -16.021 1.00 21.26 ?  30   VAL   B CG2  1 
ATOM   4454 H  H    . VAL   B 1 30  ? 50.796 -20.629 -15.379 1.00 22.91 ?  30   VAL   B H    1 
ATOM   4455 H  HA   . VAL   B 1 30  ? 49.331 -19.861 -17.440 1.00 22.81 ?  30   VAL   B HA   1 
ATOM   4456 H  HB   . VAL   B 1 30  ? 48.717 -20.237 -14.710 1.00 24.64 ?  30   VAL   B HB   1 
ATOM   4457 H  HG11 . VAL   B 1 30  ? 46.392 -19.978 -15.463 1.00 25.33 ?  30   VAL   B HG11 1 
ATOM   4458 H  HG12 . VAL   B 1 30  ? 47.202 -18.670 -15.085 1.00 25.33 ?  30   VAL   B HG12 1 
ATOM   4459 H  HG13 . VAL   B 1 30  ? 47.018 -19.090 -16.609 1.00 25.33 ?  30   VAL   B HG13 1 
ATOM   4460 H  HG21 . VAL   B 1 30  ? 47.470 -22.055 -15.450 1.00 25.53 ?  30   VAL   B HG21 1 
ATOM   4461 H  HG22 . VAL   B 1 30  ? 47.881 -21.722 -16.948 1.00 25.53 ?  30   VAL   B HG22 1 
ATOM   4462 H  HG23 . VAL   B 1 30  ? 48.985 -22.194 -15.908 1.00 25.53 ?  30   VAL   B HG23 1 
ATOM   4463 N  N    . LYS   B 1 31  ? 50.323 -17.600 -15.431 1.00 17.43 ?  31   LYS   B N    1 
ATOM   4464 C  CA   . LYS   B 1 31  ? 50.341 -16.188 -15.068 1.00 17.89 ?  31   LYS   B CA   1 
ATOM   4465 C  C    . LYS   B 1 31  ? 48.947 -15.703 -14.669 1.00 15.73 ?  31   LYS   B C    1 
ATOM   4466 O  O    . LYS   B 1 31  ? 48.405 -14.781 -15.291 1.00 16.51 ?  31   LYS   B O    1 
ATOM   4467 C  CB   . LYS   B 1 31  ? 50.970 -15.359 -16.190 1.00 21.20 ?  31   LYS   B CB   1 
ATOM   4468 C  CG   . LYS   B 1 31  ? 52.395 -15.813 -16.514 1.00 24.49 ?  31   LYS   B CG   1 
ATOM   4469 C  CD   . LYS   B 1 31  ? 52.984 -15.053 -17.677 1.00 28.22 ?  31   LYS   B CD   1 
ATOM   4470 C  CE   . LYS   B 1 31  ? 54.464 -15.329 -17.803 1.00 31.26 ?  31   LYS   B CE   1 
ATOM   4471 N  NZ   . LYS   B 1 31  ? 55.188 -14.927 -16.566 1.00 33.02 ?  31   LYS   B NZ   1 
ATOM   4472 H  H    . LYS   B 1 31  ? 50.890 -18.088 -14.991 1.00 20.94 ?  31   LYS   B H    1 
ATOM   4473 H  HA   . LYS   B 1 31  ? 50.904 -16.108 -14.301 1.00 21.49 ?  31   LYS   B HA   1 
ATOM   4474 H  HB2  . LYS   B 1 31  ? 50.430 -15.444 -16.991 1.00 25.46 ?  31   LYS   B HB2  1 
ATOM   4475 H  HB3  . LYS   B 1 31  ? 50.998 -14.437 -15.897 1.00 25.46 ?  31   LYS   B HB3  1 
ATOM   4476 H  HG2  . LYS   B 1 31  ? 52.952 -15.671 -15.732 1.00 29.41 ?  31   LYS   B HG2  1 
ATOM   4477 H  HG3  . LYS   B 1 31  ? 52.385 -16.760 -16.742 1.00 29.41 ?  31   LYS   B HG3  1 
ATOM   4478 H  HD2  . LYS   B 1 31  ? 52.542 -15.337 -18.493 1.00 33.88 ?  31   LYS   B HD2  1 
ATOM   4479 H  HD3  . LYS   B 1 31  ? 52.853 -14.106 -17.531 1.00 33.88 ?  31   LYS   B HD3  1 
ATOM   4480 H  HE2  . LYS   B 1 31  ? 54.603 -16.280 -17.944 1.00 37.54 ?  31   LYS   B HE2  1 
ATOM   4481 H  HE3  . LYS   B 1 31  ? 54.820 -14.822 -18.547 1.00 37.54 ?  31   LYS   B HE3  1 
ATOM   4482 H  HZ1  . LYS   B 1 31  ? 56.065 -14.928 -16.714 1.00 39.65 ?  31   LYS   B HZ1  1 
ATOM   4483 H  HZ2  . LYS   B 1 31  ? 54.936 -14.109 -16.320 1.00 39.65 ?  31   LYS   B HZ2  1 
ATOM   4484 H  HZ3  . LYS   B 1 31  ? 55.005 -15.495 -15.906 1.00 39.65 ?  31   LYS   B HZ3  1 
ATOM   4485 N  N    . PRO   B 1 32  ? 48.344 -16.289 -13.632 1.00 13.50 ?  32   PRO   B N    1 
ATOM   4486 C  CA   . PRO   B 1 32  ? 46.971 -15.923 -13.269 1.00 12.88 ?  32   PRO   B CA   1 
ATOM   4487 C  C    . PRO   B 1 32  ? 46.899 -14.578 -12.563 1.00 12.91 ?  32   PRO   B C    1 
ATOM   4488 O  O    . PRO   B 1 32  ? 47.826 -14.158 -11.861 1.00 14.00 ?  32   PRO   B O    1 
ATOM   4489 C  CB   . PRO   B 1 32  ? 46.569 -17.040 -12.298 1.00 13.04 ?  32   PRO   B CB   1 
ATOM   4490 C  CG   . PRO   B 1 32  ? 47.869 -17.388 -11.618 1.00 13.36 ?  32   PRO   B CG   1 
ATOM   4491 C  CD   . PRO   B 1 32  ? 48.924 -17.264 -12.686 1.00 13.75 ?  32   PRO   B CD   1 
ATOM   4492 H  HA   . PRO   B 1 32  ? 46.387 -15.937 -14.051 1.00 15.48 ?  32   PRO   B HA   1 
ATOM   4493 H  HB2  . PRO   B 1 32  ? 45.915 -16.707 -11.663 1.00 15.67 ?  32   PRO   B HB2  1 
ATOM   4494 H  HB3  . PRO   B 1 32  ? 46.216 -17.803 -12.790 1.00 15.67 ?  32   PRO   B HB3  1 
ATOM   4495 H  HG2  . PRO   B 1 32  ? 48.035 -16.761 -10.895 1.00 16.05 ?  32   PRO   B HG2  1 
ATOM   4496 H  HG3  . PRO   B 1 32  ? 47.828 -18.296 -11.278 1.00 16.05 ?  32   PRO   B HG3  1 
ATOM   4497 H  HD2  . PRO   B 1 32  ? 49.745 -16.915 -12.309 1.00 16.52 ?  32   PRO   B HD2  1 
ATOM   4498 H  HD3  . PRO   B 1 32  ? 49.064 -18.118 -13.121 1.00 16.52 ?  32   PRO   B HD3  1 
ATOM   4499 N  N    . THR   B 1 33  ? 45.745 -13.923 -12.723 1.00 12.43 ?  33   THR   B N    1 
ATOM   4500 C  CA   . THR   B 1 33  ? 45.457 -12.746 -11.913 1.00 12.45 ?  33   THR   B CA   1 
ATOM   4501 C  C    . THR   B 1 33  ? 45.408 -13.099 -10.432 1.00 12.42 ?  33   THR   B C    1 
ATOM   4502 O  O    . THR   B 1 33  ? 45.885 -12.325 -9.590  1.00 13.29 ?  33   THR   B O    1 
ATOM   4503 C  CB   . THR   B 1 33  ? 44.139 -12.109 -12.358 1.00 13.23 ?  33   THR   B CB   1 
ATOM   4504 O  OG1  . THR   B 1 33  ? 44.179 -11.855 -13.763 1.00 13.32 ?  33   THR   B OG1  1 
ATOM   4505 C  CG2  . THR   B 1 33  ? 43.882 -10.816 -11.607 1.00 14.51 ?  33   THR   B CG2  1 
ATOM   4506 H  H    . THR   B 1 33  ? 45.123 -14.139 -13.286 1.00 14.94 ?  33   THR   B H    1 
ATOM   4507 H  HA   . THR   B 1 33  ? 46.161 -12.096 -12.047 1.00 14.97 ?  33   THR   B HA   1 
ATOM   4508 H  HB   . THR   B 1 33  ? 43.406 -12.718 -12.173 1.00 15.90 ?  33   THR   B HB   1 
ATOM   4509 H  HG1  . THR   B 1 33  ? 43.462 -11.479 -14.011 1.00 16.00 ?  33   THR   B HG1  1 
ATOM   4510 H  HG21 . THR   B 1 33  ? 43.131 -10.348 -11.999 1.00 17.44 ?  33   THR   B HG21 1 
ATOM   4511 H  HG22 . THR   B 1 33  ? 43.685 -11.007 -10.676 1.00 17.44 ?  33   THR   B HG22 1 
ATOM   4512 H  HG23 . THR   B 1 33  ? 44.668 -10.247 -11.652 1.00 17.44 ?  33   THR   B HG23 1 
ATOM   4513 N  N    . VAL   B 1 34  ? 44.855 -14.268 -10.094 1.00 11.46 ?  34   VAL   B N    1 
ATOM   4514 C  CA   . VAL   B 1 34  ? 44.653 -14.662 -8.704  1.00 10.83 ?  34   VAL   B CA   1 
ATOM   4515 C  C    . VAL   B 1 34  ? 45.079 -16.110 -8.538  1.00 10.11 ?  34   VAL   B C    1 
ATOM   4516 O  O    . VAL   B 1 34  ? 44.549 -16.996 -9.218  1.00 10.92 ?  34   VAL   B O    1 
ATOM   4517 C  CB   . VAL   B 1 34  ? 43.185 -14.524 -8.262  1.00 11.93 ?  34   VAL   B CB   1 
ATOM   4518 C  CG1  . VAL   B 1 34  ? 43.031 -14.973 -6.810  1.00 12.52 ?  34   VAL   B CG1  1 
ATOM   4519 C  CG2  . VAL   B 1 34  ? 42.694 -13.105 -8.460  1.00 12.90 ?  34   VAL   B CG2  1 
ATOM   4520 H  H    . VAL   B 1 34  ? 44.597 -14.861 -10.662 1.00 13.77 ?  34   VAL   B H    1 
ATOM   4521 H  HA   . VAL   B 1 34  ? 45.209 -14.113 -8.125  1.00 13.02 ?  34   VAL   B HA   1 
ATOM   4522 H  HB   . VAL   B 1 34  ? 42.643 -15.107 -8.810  1.00 14.34 ?  34   VAL   B HB   1 
ATOM   4523 H  HG11 . VAL   B 1 34  ? 42.182 -14.654 -6.469  1.00 15.05 ?  34   VAL   B HG11 1 
ATOM   4524 H  HG12 . VAL   B 1 34  ? 43.058 -15.944 -6.769  1.00 15.05 ?  34   VAL   B HG12 1 
ATOM   4525 H  HG13 . VAL   B 1 34  ? 43.758 -14.602 -6.281  1.00 15.05 ?  34   VAL   B HG13 1 
ATOM   4526 H  HG21 . VAL   B 1 34  ? 41.780 -13.039 -8.142  1.00 15.50 ?  34   VAL   B HG21 1 
ATOM   4527 H  HG22 . VAL   B 1 34  ? 43.262 -12.495 -7.964  1.00 15.50 ?  34   VAL   B HG22 1 
ATOM   4528 H  HG23 . VAL   B 1 34  ? 42.728 -12.886 -9.408  1.00 15.50 ?  34   VAL   B HG23 1 
ATOM   4529 N  N    . VAL   B 1 35  ? 45.987 -16.361 -7.602  1.00 9.69  ?  35   VAL   B N    1 
ATOM   4530 C  CA   . VAL   B 1 35  ? 46.214 -17.702 -7.082  1.00 9.63  ?  35   VAL   B CA   1 
ATOM   4531 C  C    . VAL   B 1 35  ? 45.676 -17.758 -5.662  1.00 9.32  ?  35   VAL   B C    1 
ATOM   4532 O  O    . VAL   B 1 35  ? 45.905 -16.839 -4.870  1.00 9.79  ?  35   VAL   B O    1 
ATOM   4533 C  CB   . VAL   B 1 35  ? 47.696 -18.133 -7.163  1.00 10.30 ?  35   VAL   B CB   1 
ATOM   4534 C  CG1  . VAL   B 1 35  ? 48.596 -17.308 -6.239  1.00 11.09 ?  35   VAL   B CG1  1 
ATOM   4535 C  CG2  . VAL   B 1 35  ? 47.836 -19.629 -6.850  1.00 10.71 ?  35   VAL   B CG2  1 
ATOM   4536 H  H    . VAL   B 1 35  ? 46.488 -15.761 -7.240  1.00 11.65 ?  35   VAL   B H    1 
ATOM   4537 H  HA   . VAL   B 1 35  ? 45.700 -18.332 -7.605  1.00 11.58 ?  35   VAL   B HA   1 
ATOM   4538 H  HB   . VAL   B 1 35  ? 48.008 -17.999 -8.071  1.00 12.39 ?  35   VAL   B HB   1 
ATOM   4539 H  HG11 . VAL   B 1 35  ? 49.520 -17.531 -6.422  1.00 13.33 ?  35   VAL   B HG11 1 
ATOM   4540 H  HG12 . VAL   B 1 35  ? 48.435 -16.371 -6.403  1.00 13.33 ?  35   VAL   B HG12 1 
ATOM   4541 H  HG13 . VAL   B 1 35  ? 48.380 -17.528 -5.316  1.00 13.33 ?  35   VAL   B HG13 1 
ATOM   4542 H  HG21 . VAL   B 1 35  ? 48.763 -19.898 -6.950  1.00 12.88 ?  35   VAL   B HG21 1 
ATOM   4543 H  HG22 . VAL   B 1 35  ? 47.544 -19.798 -5.936  1.00 12.88 ?  35   VAL   B HG22 1 
ATOM   4544 H  HG23 . VAL   B 1 35  ? 47.280 -20.141 -7.465  1.00 12.88 ?  35   VAL   B HG23 1 
ATOM   4545 N  N    . VAL   B 1 36  ? 44.954 -18.829 -5.346  1.00 9.33  ?  36   VAL   B N    1 
ATOM   4546 C  CA   . VAL   B 1 36  ? 44.410 -19.035 -4.014  1.00 9.08  ?  36   VAL   B CA   1 
ATOM   4547 C  C    . VAL   B 1 36  ? 45.419 -19.795 -3.167  1.00 8.77  ?  36   VAL   B C    1 
ATOM   4548 O  O    . VAL   B 1 36  ? 45.960 -20.826 -3.589  1.00 10.02 ?  36   VAL   B O    1 
ATOM   4549 C  CB   . VAL   B 1 36  ? 43.074 -19.790 -4.089  1.00 9.30  ?  36   VAL   B CB   1 
ATOM   4550 C  CG1  . VAL   B 1 36  ? 42.568 -20.162 -2.702  1.00 9.73  ?  36   VAL   B CG1  1 
ATOM   4551 C  CG2  . VAL   B 1 36  ? 42.049 -18.956 -4.840  1.00 10.20 ?  36   VAL   B CG2  1 
ATOM   4552 H  H    . VAL   B 1 36  ? 44.765 -19.463 -5.892  1.00 11.22 ?  36   VAL   B H    1 
ATOM   4553 H  HA   . VAL   B 1 36  ? 44.246 -18.178 -3.591  1.00 10.92 ?  36   VAL   B HA   1 
ATOM   4554 H  HB   . VAL   B 1 36  ? 43.206 -20.615 -4.582  1.00 11.18 ?  36   VAL   B HB   1 
ATOM   4555 H  HG11 . VAL   B 1 36  ? 41.631 -20.401 -2.762  1.00 11.70 ?  36   VAL   B HG11 1 
ATOM   4556 H  HG12 . VAL   B 1 36  ? 43.081 -20.908 -2.363  1.00 11.70 ?  36   VAL   B HG12 1 
ATOM   4557 H  HG13 . VAL   B 1 36  ? 42.672 -19.392 -2.115  1.00 11.70 ?  36   VAL   B HG13 1 
ATOM   4558 H  HG21 . VAL   B 1 36  ? 41.202 -19.430 -4.855  1.00 12.27 ?  36   VAL   B HG21 1 
ATOM   4559 H  HG22 . VAL   B 1 36  ? 41.943 -18.103 -4.393  1.00 12.27 ?  36   VAL   B HG22 1 
ATOM   4560 H  HG23 . VAL   B 1 36  ? 42.362 -18.815 -5.750  1.00 12.27 ?  36   VAL   B HG23 1 
ATOM   4561 N  N    . ASN   B 1 37  ? 45.639 -19.303 -1.953  1.00 9.16  ?  37   ASN   B N    1 
ATOM   4562 C  CA   . ASN   B 1 37  ? 46.390 -20.027 -0.944  1.00 9.22  ?  37   ASN   B CA   1 
ATOM   4563 C  C    . ASN   B 1 37  ? 45.439 -20.698 0.035   1.00 9.08  ?  37   ASN   B C    1 
ATOM   4564 O  O    . ASN   B 1 37  ? 44.428 -20.119 0.445   1.00 9.87  ?  37   ASN   B O    1 
ATOM   4565 C  CB   . ASN   B 1 37  ? 47.315 -19.087 -0.176  1.00 9.40  ?  37   ASN   B CB   1 
ATOM   4566 C  CG   . ASN   B 1 37  ? 48.163 -19.806 0.835   1.00 9.48  ?  37   ASN   B CG   1 
ATOM   4567 O  OD1  . ASN   B 1 37  ? 48.503 -20.978 0.656   1.00 10.33 ?  37   ASN   B OD1  1 
ATOM   4568 N  ND2  . ASN   B 1 37  ? 48.521 -19.105 1.909   1.00 9.83  ?  37   ASN   B ND2  1 
ATOM   4569 H  H    . ASN   B 1 37  ? 45.360 -18.532 -1.681  1.00 11.01 ?  37   ASN   B H    1 
ATOM   4570 H  HA   . ASN   B 1 37  ? 46.926 -20.716 -1.363  1.00 11.08 ?  37   ASN   B HA   1 
ATOM   4571 H  HB2  . ASN   B 1 37  ? 47.913 -18.656 -0.803  1.00 11.30 ?  37   ASN   B HB2  1 
ATOM   4572 H  HB3  . ASN   B 1 37  ? 46.786 -18.430 0.295   1.00 11.30 ?  37   ASN   B HB3  1 
ATOM   4573 H  HD21 . ASN   B 1 37  ? 49.013 -19.468 2.515   1.00 11.82 ?  37   ASN   B HD21 1 
ATOM   4574 H  HD22 . ASN   B 1 37  ? 48.269 -18.294 1.997   1.00 11.82 ?  37   ASN   B HD22 1 
ATOM   4575 N  N    . ALA   B 1 38  ? 45.791 -21.929 0.414   1.00 9.45  ?  38   ALA   B N    1 
ATOM   4576 C  CA   . ALA   B 1 38  ? 45.135 -22.675 1.489   1.00 9.96  ?  38   ALA   B CA   1 
ATOM   4577 C  C    . ALA   B 1 38  ? 45.716 -22.189 2.815   1.00 9.73  ?  38   ALA   B C    1 
ATOM   4578 O  O    . ALA   B 1 38  ? 46.620 -22.791 3.398   1.00 10.62 ?  38   ALA   B O    1 
ATOM   4579 C  CB   . ALA   B 1 38  ? 45.351 -24.172 1.298   1.00 11.15 ?  38   ALA   B CB   1 
ATOM   4580 H  H    . ALA   B 1 38  ? 46.441 -22.366 0.056   1.00 11.36 ?  38   ALA   B H    1 
ATOM   4581 H  HA   . ALA   B 1 38  ? 44.182 -22.495 1.480   1.00 11.97 ?  38   ALA   B HA   1 
ATOM   4582 H  HB1  . ALA   B 1 38  ? 44.903 -24.652 2.022   1.00 13.40 ?  38   ALA   B HB1  1 
ATOM   4583 H  HB2  . ALA   B 1 38  ? 44.969 -24.444 0.448   1.00 13.40 ?  38   ALA   B HB2  1 
ATOM   4584 H  HB3  . ALA   B 1 38  ? 46.297 -24.365 1.316   1.00 13.40 ?  38   ALA   B HB3  1 
ATOM   4585 N  N    . ALA   B 1 39  ? 45.198 -21.053 3.275   1.00 9.80  ?  39   ALA   B N    1 
ATOM   4586 C  CA   . ALA   B 1 39  ? 45.750 -20.313 4.399   1.00 10.06 ?  39   ALA   B CA   1 
ATOM   4587 C  C    . ALA   B 1 39  ? 45.140 -20.757 5.724   1.00 10.23 ?  39   ALA   B C    1 
ATOM   4588 O  O    . ALA   B 1 39  ? 44.115 -21.435 5.778   1.00 11.03 ?  39   ALA   B O    1 
ATOM   4589 C  CB   . ALA   B 1 39  ? 45.511 -18.812 4.197   1.00 10.68 ?  39   ALA   B CB   1 
ATOM   4590 H  H    . ALA   B 1 39  ? 44.500 -20.689 2.934   1.00 11.78 ?  39   ALA   B H    1 
ATOM   4591 H  HA   . ALA   B 1 39  ? 46.702 -20.461 4.440   1.00 12.10 ?  39   ALA   B HA   1 
ATOM   4592 H  HB1  . ALA   B 1 39  ? 45.881 -18.327 4.950   1.00 12.84 ?  39   ALA   B HB1  1 
ATOM   4593 H  HB2  . ALA   B 1 39  ? 45.948 -18.529 3.375   1.00 12.84 ?  39   ALA   B HB2  1 
ATOM   4594 H  HB3  . ALA   B 1 39  ? 44.556 -18.645 4.132   1.00 12.84 ?  39   ALA   B HB3  1 
ATOM   4595 N  N    . ASN   B 1 40  ? 45.785 -20.339 6.807   1.00 10.98 ?  40   ASN   B N    1 
ATOM   4596 C  CA   . ASN   B 1 40  ? 45.218 -20.385 8.145   1.00 11.33 ?  40   ASN   B CA   1 
ATOM   4597 C  C    . ASN   B 1 40  ? 45.035 -18.959 8.666   1.00 11.21 ?  40   ASN   B C    1 
ATOM   4598 O  O    . ASN   B 1 40  ? 45.445 -17.982 8.035   1.00 10.93 ?  40   ASN   B O    1 
ATOM   4599 C  CB   . ASN   B 1 40  ? 46.064 -21.260 9.084   1.00 12.02 ?  40   ASN   B CB   1 
ATOM   4600 C  CG   . ASN   B 1 40  ? 47.518 -20.858 9.107   1.00 13.30 ?  40   ASN   B CG   1 
ATOM   4601 O  OD1  . ASN   B 1 40  ? 47.840 -19.674 9.158   1.00 15.46 ?  40   ASN   B OD1  1 
ATOM   4602 N  ND2  . ASN   B 1 40  ? 48.407 -21.838 9.067   1.00 13.25 ?  40   ASN   B ND2  1 
ATOM   4603 H  H    . ASN   B 1 40  ? 46.578 -20.012 6.788   1.00 13.19 ?  40   ASN   B H    1 
ATOM   4604 H  HA   . ASN   B 1 40  ? 44.336 -20.781 8.097   1.00 13.61 ?  40   ASN   B HA   1 
ATOM   4605 H  HB2  . ASN   B 1 40  ? 45.714 -21.183 9.986   1.00 14.45 ?  40   ASN   B HB2  1 
ATOM   4606 H  HB3  . ASN   B 1 40  ? 46.006 -22.181 8.784   1.00 14.45 ?  40   ASN   B HB3  1 
ATOM   4607 H  HD21 . ASN   B 1 40  ? 49.247 -21.662 9.079   1.00 15.92 ?  40   ASN   B HD21 1 
ATOM   4608 H  HD22 . ASN   B 1 40  ? 48.141 -22.658 9.029   1.00 15.92 ?  40   ASN   B HD22 1 
ATOM   4609 N  N    . VAL   B 1 41  ? 44.379 -18.833 9.823   1.00 11.63 ?  41   VAL   B N    1 
ATOM   4610 C  CA   . VAL   B 1 41  ? 43.918 -17.514 10.265  1.00 12.48 ?  41   VAL   B CA   1 
ATOM   4611 C  C    . VAL   B 1 41  ? 45.070 -16.559 10.560  1.00 11.99 ?  41   VAL   B C    1 
ATOM   4612 O  O    . VAL   B 1 41  ? 44.889 -15.338 10.476  1.00 12.15 ?  41   VAL   B O    1 
ATOM   4613 C  CB   . VAL   B 1 41  ? 42.940 -17.595 11.454  1.00 13.78 ?  41   VAL   B CB   1 
ATOM   4614 C  CG1  . VAL   B 1 41  ? 41.648 -18.279 11.042  1.00 14.02 ?  41   VAL   B CG1  1 
ATOM   4615 C  CG2  . VAL   B 1 41  ? 43.587 -18.288 12.643  1.00 14.72 ?  41   VAL   B CG2  1 
ATOM   4616 H  H    . VAL   B 1 41  ? 44.194 -19.476 10.357  1.00 13.97 ?  41   VAL   B H    1 
ATOM   4617 H  HA   . VAL   B 1 41  ? 43.420 -17.119 9.532   1.00 14.99 ?  41   VAL   B HA   1 
ATOM   4618 H  HB   . VAL   B 1 41  ? 42.713 -16.695 11.734  1.00 16.56 ?  41   VAL   B HB   1 
ATOM   4619 H  HG11 . VAL   B 1 41  ? 41.036 -18.282 11.796  1.00 16.85 ?  41   VAL   B HG11 1 
ATOM   4620 H  HG12 . VAL   B 1 41  ? 41.256 -17.793 10.301  1.00 16.85 ?  41   VAL   B HG12 1 
ATOM   4621 H  HG13 . VAL   B 1 41  ? 41.845 -19.191 10.775  1.00 16.85 ?  41   VAL   B HG13 1 
ATOM   4622 H  HG21 . VAL   B 1 41  ? 42.956 -18.307 13.379  1.00 17.69 ?  41   VAL   B HG21 1 
ATOM   4623 H  HG22 . VAL   B 1 41  ? 43.821 -19.197 12.389  1.00 17.69 ?  41   VAL   B HG22 1 
ATOM   4624 H  HG23 . VAL   B 1 41  ? 44.383 -17.801 12.898  1.00 17.69 ?  41   VAL   B HG23 1 
ATOM   4625 N  N    . TYR   B 1 42  ? 46.240 -17.071 10.943  1.00 12.22 ?  42   TYR   B N    1 
ATOM   4626 C  CA   . TYR   B 1 42  ? 47.395 -16.227 11.215  1.00 12.57 ?  42   TYR   B CA   1 
ATOM   4627 C  C    . TYR   B 1 42  ? 48.363 -16.154 10.038  1.00 12.10 ?  42   TYR   B C    1 
ATOM   4628 O  O    . TYR   B 1 42  ? 49.457 -15.587 10.172  1.00 12.97 ?  42   TYR   B O    1 
ATOM   4629 C  CB   . TYR   B 1 42  ? 48.084 -16.647 12.519  1.00 14.25 ?  42   TYR   B CB   1 
ATOM   4630 C  CG   . TYR   B 1 42  ? 47.490 -15.951 13.742  1.00 14.09 ?  42   TYR   B CG   1 
ATOM   4631 C  CD1  . TYR   B 1 42  ? 47.711 -14.597 13.958  1.00 12.96 ?  42   TYR   B CD1  1 
ATOM   4632 C  CD2  . TYR   B 1 42  ? 46.716 -16.638 14.667  1.00 15.79 ?  42   TYR   B CD2  1 
ATOM   4633 C  CE1  . TYR   B 1 42  ? 47.183 -13.944 15.049  1.00 14.17 ?  42   TYR   B CE1  1 
ATOM   4634 C  CE2  . TYR   B 1 42  ? 46.181 -15.987 15.774  1.00 15.93 ?  42   TYR   B CE2  1 
ATOM   4635 C  CZ   . TYR   B 1 42  ? 46.419 -14.637 15.960  1.00 15.94 ?  42   TYR   B CZ   1 
ATOM   4636 O  OH   . TYR   B 1 42  ? 45.909 -13.965 17.054  1.00 18.60 ?  42   TYR   B OH   1 
ATOM   4637 H  H    . TYR   B 1 42  ? 46.383 -17.918 11.047  1.00 14.68 ?  42   TYR   B H    1 
ATOM   4638 H  HA   . TYR   B 1 42  ? 47.066 -15.329 11.353  1.00 15.11 ?  42   TYR   B HA   1 
ATOM   4639 H  HB2  . TYR   B 1 42  ? 47.983 -17.604 12.636  1.00 17.13 ?  42   TYR   B HB2  1 
ATOM   4640 H  HB3  . TYR   B 1 42  ? 49.023 -16.415 12.462  1.00 17.13 ?  42   TYR   B HB3  1 
ATOM   4641 H  HD1  . TYR   B 1 42  ? 48.230 -14.121 13.338  1.00 15.57 ?  42   TYR   B HD1  1 
ATOM   4642 H  HD2  . TYR   B 1 42  ? 46.554 -17.550 14.538  1.00 18.98 ?  42   TYR   B HD2  1 
ATOM   4643 H  HE1  . TYR   B 1 42  ? 47.352 -13.038 15.167  1.00 17.02 ?  42   TYR   B HE1  1 
ATOM   4644 H  HE2  . TYR   B 1 42  ? 45.666 -16.463 16.382  1.00 19.14 ?  42   TYR   B HE2  1 
ATOM   4645 H  HH   . TYR   B 1 42  ? 46.143 -13.162 17.016  1.00 22.34 ?  42   TYR   B HH   1 
ATOM   4646 N  N    . LEU   B 1 43  ? 47.967 -16.676 8.879   1.00 10.95 ?  43   LEU   B N    1 
ATOM   4647 C  CA   . LEU   B 1 43  ? 48.781 -16.600 7.672   1.00 10.85 ?  43   LEU   B CA   1 
ATOM   4648 C  C    . LEU   B 1 43  ? 50.193 -17.109 7.932   1.00 10.98 ?  43   LEU   B C    1 
ATOM   4649 O  O    . LEU   B 1 43  ? 51.176 -16.513 7.489   1.00 11.72 ?  43   LEU   B O    1 
ATOM   4650 C  CB   . LEU   B 1 43  ? 48.800 -15.190 7.081   1.00 10.95 ?  43   LEU   B CB   1 
ATOM   4651 C  CG   . LEU   B 1 43  ? 47.445 -14.582 6.706   1.00 11.27 ?  43   LEU   B CG   1 
ATOM   4652 C  CD1  . LEU   B 1 43  ? 47.663 -13.194 6.118   1.00 12.56 ?  43   LEU   B CD1  1 
ATOM   4653 C  CD2  . LEU   B 1 43  ? 46.674 -15.464 5.735   1.00 11.65 ?  43   LEU   B CD2  1 
ATOM   4654 H  H    . LEU   B 1 43  ? 47.225 -17.098 8.765   1.00 13.17 ?  43   LEU   B H    1 
ATOM   4655 H  HA   . LEU   B 1 43  ? 48.382 -17.185 7.003   1.00 13.04 ?  43   LEU   B HA   1 
ATOM   4656 H  HB2  . LEU   B 1 43  ? 49.216 -14.598 7.726   1.00 13.16 ?  43   LEU   B HB2  1 
ATOM   4657 H  HB3  . LEU   B 1 43  ? 49.337 -15.212 6.272   1.00 13.16 ?  43   LEU   B HB3  1 
ATOM   4658 H  HG   . LEU   B 1 43  ? 46.912 -14.482 7.508   1.00 13.55 ?  43   LEU   B HG   1 
ATOM   4659 H  HD11 . LEU   B 1 43  ? 46.806 -12.806 5.883   1.00 15.10 ?  43   LEU   B HD11 1 
ATOM   4660 H  HD12 . LEU   B 1 43  ? 48.105 -12.634 6.782   1.00 15.10 ?  43   LEU   B HD12 1 
ATOM   4661 H  HD13 . LEU   B 1 43  ? 48.223 -13.264 5.328   1.00 15.10 ?  43   LEU   B HD13 1 
ATOM   4662 H  HD21 . LEU   B 1 43  ? 45.875 -14.992 5.449   1.00 14.00 ?  43   LEU   B HD21 1 
ATOM   4663 H  HD22 . LEU   B 1 43  ? 47.235 -15.657 4.970   1.00 14.00 ?  43   LEU   B HD22 1 
ATOM   4664 H  HD23 . LEU   B 1 43  ? 46.428 -16.286 6.186   1.00 14.00 ?  43   LEU   B HD23 1 
ATOM   4665 N  N    . LYS   B 1 44  ? 50.286 -18.241 8.632   1.00 11.26 ?  44   LYS   B N    1 
ATOM   4666 C  CA   . LYS   B 1 44  ? 51.553 -18.919 8.884   1.00 11.89 ?  44   LYS   B CA   1 
ATOM   4667 C  C    . LYS   B 1 44  ? 51.667 -20.038 7.860   1.00 11.46 ?  44   LYS   B C    1 
ATOM   4668 O  O    . LYS   B 1 44  ? 50.972 -21.051 7.944   1.00 12.51 ?  44   LYS   B O    1 
ATOM   4669 C  CB   . LYS   B 1 44  ? 51.597 -19.423 10.324  1.00 13.87 ?  44   LYS   B CB   1 
ATOM   4670 C  CG   . LYS   B 1 44  ? 51.802 -18.303 11.335  1.00 16.47 ?  44   LYS   B CG   1 
ATOM   4671 C  CD   . LYS   B 1 44  ? 53.025 -17.468 10.934  1.00 19.76 ?  44   LYS   B CD   1 
ATOM   4672 C  CE   . LYS   B 1 44  ? 53.464 -16.487 11.988  1.00 22.68 ?  44   LYS   B CE   1 
ATOM   4673 N  NZ   . LYS   B 1 44  ? 54.739 -15.811 11.633  1.00 24.01 ?  44   LYS   B NZ   1 
ATOM   4674 H  H    . LYS   B 1 44  ? 49.609 -18.635 8.991   1.00 13.53 ?  44   LYS   B H    1 
ATOM   4675 H  HA   . LYS   B 1 44  ? 52.284 -18.310 8.717   1.00 14.29 ?  44   LYS   B HA   1 
ATOM   4676 H  HB2  . LYS   B 1 44  ? 50.752 -19.858 10.533  1.00 16.67 ?  44   LYS   B HB2  1 
ATOM   4677 H  HB3  . LYS   B 1 44  ? 52.325 -20.051 10.419  1.00 16.67 ?  44   LYS   B HB3  1 
ATOM   4678 H  HG2  . LYS   B 1 44  ? 51.023 -17.731 11.355  1.00 19.79 ?  44   LYS   B HG2  1 
ATOM   4679 H  HG3  . LYS   B 1 44  ? 51.966 -18.690 12.215  1.00 19.79 ?  44   LYS   B HG3  1 
ATOM   4680 H  HD2  . LYS   B 1 44  ? 53.763 -18.074 10.734  1.00 23.73 ?  44   LYS   B HD2  1 
ATOM   4681 H  HD3  . LYS   B 1 44  ? 52.801 -16.952 10.144  1.00 23.73 ?  44   LYS   B HD3  1 
ATOM   4682 H  HE2  . LYS   B 1 44  ? 52.779 -15.809 12.085  1.00 27.24 ?  44   LYS   B HE2  1 
ATOM   4683 H  HE3  . LYS   B 1 44  ? 53.601 -16.963 12.816  1.00 27.24 ?  44   LYS   B HE3  1 
ATOM   4684 H  HZ1  . LYS   B 1 44  ? 54.964 -15.238 12.275  1.00 28.83 ?  44   LYS   B HZ1  1 
ATOM   4685 H  HZ2  . LYS   B 1 44  ? 55.388 -16.413 11.541  1.00 28.83 ?  44   LYS   B HZ2  1 
ATOM   4686 H  HZ3  . LYS   B 1 44  ? 54.647 -15.366 10.867  1.00 28.83 ?  44   LYS   B HZ3  1 
ATOM   4687 N  N    . HIS   B 1 45  ? 52.516 -19.821 6.858   1.00 11.23 ?  45   HIS   B N    1 
ATOM   4688 C  CA   . HIS   B 1 45  ? 52.537 -20.650 5.653   1.00 11.47 ?  45   HIS   B CA   1 
ATOM   4689 C  C    . HIS   B 1 45  ? 53.549 -21.778 5.816   1.00 13.44 ?  45   HIS   B C    1 
ATOM   4690 O  O    . HIS   B 1 45  ? 54.607 -21.801 5.198   1.00 15.69 ?  45   HIS   B O    1 
ATOM   4691 C  CB   . HIS   B 1 45  ? 52.860 -19.790 4.443   1.00 11.63 ?  45   HIS   B CB   1 
ATOM   4692 C  CG   . HIS   B 1 45  ? 51.990 -18.588 4.332   1.00 11.10 ?  45   HIS   B CG   1 
ATOM   4693 N  ND1  . HIS   B 1 45  ? 50.613 -18.664 4.300   1.00 11.04 ?  45   HIS   B ND1  1 
ATOM   4694 C  CD2  . HIS   B 1 45  ? 52.309 -17.275 4.267   1.00 11.73 ?  45   HIS   B CD2  1 
ATOM   4695 C  CE1  . HIS   B 1 45  ? 50.127 -17.439 4.200   1.00 10.85 ?  45   HIS   B CE1  1 
ATOM   4696 N  NE2  . HIS   B 1 45  ? 51.132 -16.580 4.173   1.00 11.47 ?  45   HIS   B NE2  1 
ATOM   4697 H  H    . HIS   B 1 45  ? 53.082 -19.177 6.845   1.00 13.50 ?  45   HIS   B H    1 
ATOM   4698 H  HA   . HIS   B 1 45  ? 51.657 -21.041 5.515   1.00 13.79 ?  45   HIS   B HA   1 
ATOM   4699 H  HB2  . HIS   B 1 45  ? 53.779 -19.492 4.504   1.00 13.98 ?  45   HIS   B HB2  1 
ATOM   4700 H  HB3  . HIS   B 1 45  ? 52.739 -20.322 3.637   1.00 13.98 ?  45   HIS   B HB3  1 
ATOM   4701 H  HD2  . HIS   B 1 45  ? 53.167 -16.910 4.275   1.00 14.09 ?  45   HIS   B HD2  1 
ATOM   4702 H  HE1  . HIS   B 1 45  ? 49.227 -17.215 4.150   1.00 13.04 ?  45   HIS   B HE1  1 
ATOM   4703 H  HE2  . HIS   B 1 45  ? 51.059 -15.721 4.127   1.00 13.79 ?  45   HIS   B HE2  1 
ATOM   4704 N  N    A GLY   B 1 46  ? 53.177 -22.748 6.647   0.50 14.55 ?  46   GLY   B N    1 
ATOM   4705 N  N    B GLY   B 1 46  ? 53.191 -22.730 6.667   0.50 14.53 ?  46   GLY   B N    1 
ATOM   4706 C  CA   A GLY   B 1 46  ? 54.100 -23.795 7.044   0.50 16.15 ?  46   GLY   B CA   1 
ATOM   4707 C  CA   B GLY   B 1 46  ? 54.111 -23.795 7.005   0.50 16.05 ?  46   GLY   B CA   1 
ATOM   4708 C  C    A GLY   B 1 46  ? 54.156 -25.035 6.172   0.50 17.47 ?  46   GLY   B C    1 
ATOM   4709 C  C    B GLY   B 1 46  ? 54.142 -24.936 6.009   0.50 17.50 ?  46   GLY   B C    1 
ATOM   4710 O  O    A GLY   B 1 46  ? 55.247 -25.512 5.843   0.50 19.41 ?  46   GLY   B O    1 
ATOM   4711 O  O    B GLY   B 1 46  ? 55.177 -25.213 5.393   0.50 19.15 ?  46   GLY   B O    1 
ATOM   4712 H  H    A GLY   B 1 46  ? 52.395 -22.805 7.011   0.50 17.48 ?  46   GLY   B H    1 
ATOM   4713 H  H    B GLY   B 1 46  ? 52.425 -22.770 7.067   0.50 17.46 ?  46   GLY   B H    1 
ATOM   4714 H  HA2  A GLY   B 1 46  ? 54.991 -23.418 7.082   0.50 19.41 ?  46   GLY   B HA2  1 
ATOM   4715 H  HA2  B GLY   B 1 46  ? 55.005 -23.426 7.066   0.50 19.28 ?  46   GLY   B HA2  1 
ATOM   4716 H  HA3  A GLY   B 1 46  ? 53.863 -24.093 7.934   0.50 19.41 ?  46   GLY   B HA3  1 
ATOM   4717 H  HA3  B GLY   B 1 46  ? 53.872 -24.149 7.876   0.50 19.28 ?  46   GLY   B HA3  1 
ATOM   4718 N  N    . GLY   B 1 47  ? 53.001 -25.597 5.820   1.00 17.27 ?  47   GLY   B N    1 
ATOM   4719 C  CA   . GLY   B 1 47  ? 52.948 -26.868 5.129   1.00 14.85 ?  47   GLY   B CA   1 
ATOM   4720 C  C    . GLY   B 1 47  ? 52.040 -26.849 3.915   1.00 12.77 ?  47   GLY   B C    1 
ATOM   4721 O  O    . GLY   B 1 47  ? 51.389 -25.848 3.614   1.00 13.02 ?  47   GLY   B O    1 
ATOM   4722 H  H    A GLY   B 1 47  ? 52.225 -25.269 6.001   0.50 20.74 ?  47   GLY   B H    1 
ATOM   4723 H  H    B GLY   B 1 47  ? 52.230 -25.317 6.087   0.50 20.74 ?  47   GLY   B H    1 
ATOM   4724 H  HA2  . GLY   B 1 47  ? 53.836 -27.121 4.834   1.00 17.85 ?  47   GLY   B HA2  1 
ATOM   4725 H  HA3  . GLY   B 1 47  ? 52.628 -27.553 5.742   1.00 17.85 ?  47   GLY   B HA3  1 
ATOM   4726 N  N    . GLY   B 1 48  ? 52.000 -27.988 3.228   1.00 12.16 ?  48   GLY   B N    1 
ATOM   4727 C  CA   . GLY   B 1 48  ? 51.079 -28.134 2.117   1.00 12.02 ?  48   GLY   B CA   1 
ATOM   4728 C  C    . GLY   B 1 48  ? 51.212 -27.013 1.113   1.00 11.58 ?  48   GLY   B C    1 
ATOM   4729 O  O    . GLY   B 1 48  ? 52.311 -26.546 0.799   1.00 12.13 ?  48   GLY   B O    1 
ATOM   4730 H  H    . GLY   B 1 48  ? 52.492 -28.667 3.379   1.00 14.61 ?  48   GLY   B H    1 
ATOM   4731 H  HA2  . GLY   B 1 48  ? 51.249 -28.979 1.667   1.00 14.45 ?  48   GLY   B HA2  1 
ATOM   4732 H  HA3  . GLY   B 1 48  ? 50.166 -28.143 2.446   1.00 14.45 ?  48   GLY   B HA3  1 
ATOM   4733 N  N    . VAL   B 1 49  ? 50.067 -26.578 0.590   1.00 11.32 ?  49   VAL   B N    1 
ATOM   4734 C  CA   . VAL   B 1 49  ? 50.052 -25.556 -0.454  1.00 11.30 ?  49   VAL   B CA   1 
ATOM   4735 C  C    . VAL   B 1 49  ? 50.708 -24.268 0.034   1.00 10.47 ?  49   VAL   B C    1 
ATOM   4736 O  O    . VAL   B 1 49  ? 51.498 -23.650 -0.687  1.00 11.15 ?  49   VAL   B O    1 
ATOM   4737 C  CB   . VAL   B 1 49  ? 48.610 -25.308 -0.935  1.00 12.60 ?  49   VAL   B CB   1 
ATOM   4738 C  CG1  . VAL   B 1 49  ? 48.530 -24.065 -1.814  1.00 12.58 ?  49   VAL   B CG1  1 
ATOM   4739 C  CG2  . VAL   B 1 49  ? 48.076 -26.529 -1.679  1.00 14.05 ?  49   VAL   B CG2  1 
ATOM   4740 H  H    . VAL   B 1 49  ? 49.282 -26.853 0.822   1.00 13.61 ?  49   VAL   B H    1 
ATOM   4741 H  HA   . VAL   B 1 49  ? 50.559 -25.878 -1.213  1.00 13.58 ?  49   VAL   B HA   1 
ATOM   4742 H  HB   . VAL   B 1 49  ? 48.039 -25.163 -0.168  1.00 15.14 ?  49   VAL   B HB   1 
ATOM   4743 H  HG11 . VAL   B 1 49  ? 47.697 -24.083 -2.314  1.00 15.11 ?  49   VAL   B HG11 1 
ATOM   4744 H  HG12 . VAL   B 1 49  ? 48.554 -23.275 -1.250  1.00 15.11 ?  49   VAL   B HG12 1 
ATOM   4745 H  HG13 . VAL   B 1 49  ? 49.280 -24.059 -2.428  1.00 15.11 ?  49   VAL   B HG13 1 
ATOM   4746 H  HG21 . VAL   B 1 49  ? 47.169 -26.352 -1.976  1.00 16.89 ?  49   VAL   B HG21 1 
ATOM   4747 H  HG22 . VAL   B 1 49  ? 48.644 -26.706 -2.449  1.00 16.89 ?  49   VAL   B HG22 1 
ATOM   4748 H  HG23 . VAL   B 1 49  ? 48.086 -27.293 -1.082  1.00 16.89 ?  49   VAL   B HG23 1 
ATOM   4749 N  N    . ALA   B 1 50  ? 50.367 -23.827 1.246   1.00 10.33 ?  50   ALA   B N    1 
ATOM   4750 C  CA   . ALA   B 1 50  ? 50.883 -22.551 1.727   1.00 10.32 ?  50   ALA   B CA   1 
ATOM   4751 C  C    . ALA   B 1 50  ? 52.400 -22.582 1.837   1.00 10.42 ?  50   ALA   B C    1 
ATOM   4752 O  O    . ALA   B 1 50  ? 53.080 -21.616 1.468   1.00 10.56 ?  50   ALA   B O    1 
ATOM   4753 C  CB   . ALA   B 1 50  ? 50.249 -22.196 3.069   1.00 10.56 ?  50   ALA   B CB   1 
ATOM   4754 H  H    . ALA   B 1 50  ? 49.855 -24.239 1.798   1.00 12.42 ?  50   ALA   B H    1 
ATOM   4755 H  HA   . ALA   B 1 50  ? 50.657 -21.858 1.096   1.00 12.41 ?  50   ALA   B HA   1 
ATOM   4756 H  HB1  . ALA   B 1 50  ? 50.604 -21.345 3.373   1.00 12.70 ?  50   ALA   B HB1  1 
ATOM   4757 H  HB2  . ALA   B 1 50  ? 49.287 -22.128 2.952   1.00 12.70 ?  50   ALA   B HB2  1 
ATOM   4758 H  HB3  . ALA   B 1 50  ? 50.455 -22.890 3.714   1.00 12.70 ?  50   ALA   B HB3  1 
ATOM   4759 N  N    . GLY   B 1 51  ? 52.951 -23.677 2.351   1.00 10.81 ?  51   GLY   B N    1 
ATOM   4760 C  CA   . GLY   B 1 51  ? 54.394 -23.782 2.426   1.00 11.83 ?  51   GLY   B CA   1 
ATOM   4761 C  C    . GLY   B 1 51  ? 55.042 -23.729 1.058   1.00 11.41 ?  51   GLY   B C    1 
ATOM   4762 O  O    . GLY   B 1 51  ? 56.082 -23.094 0.877   1.00 12.27 ?  51   GLY   B O    1 
ATOM   4763 H  H    . GLY   B 1 51  ? 52.525 -24.363 2.650   1.00 13.00 ?  51   GLY   B H    1 
ATOM   4764 H  HA2  . GLY   B 1 51  ? 54.749 -23.052 2.958   1.00 14.21 ?  51   GLY   B HA2  1 
ATOM   4765 H  HA3  . GLY   B 1 51  ? 54.644 -24.620 2.852   1.00 14.21 ?  51   GLY   B HA3  1 
ATOM   4766 N  N    . ALA   B 1 52  ? 54.434 -24.392 0.075   1.00 11.33 ?  52   ALA   B N    1 
ATOM   4767 C  CA   . ALA   B 1 52  ? 54.996 -24.398 -1.269  1.00 11.58 ?  52   ALA   B CA   1 
ATOM   4768 C  C    . ALA   B 1 52  ? 54.918 -23.018 -1.915  1.00 11.09 ?  52   ALA   B C    1 
ATOM   4769 O  O    . ALA   B 1 52  ? 55.883 -22.570 -2.549  1.00 11.60 ?  52   ALA   B O    1 
ATOM   4770 C  CB   . ALA   B 1 52  ? 54.284 -25.441 -2.125  1.00 12.32 ?  52   ALA   B CB   1 
ATOM   4771 H  H    . ALA   B 1 52  ? 53.694 -24.828 0.159   1.00 13.62 ?  52   ALA   B H    1 
ATOM   4772 H  HA   . ALA   B 1 52  ? 55.928 -24.646 -1.212  1.00 13.92 ?  52   ALA   B HA   1 
ATOM   4773 H  HB1  . ALA   B 1 52  ? 54.673 -25.434 -3.014  1.00 14.81 ?  52   ALA   B HB1  1 
ATOM   4774 H  HB2  . ALA   B 1 52  ? 54.405 -26.314 -1.718  1.00 14.81 ?  52   ALA   B HB2  1 
ATOM   4775 H  HB3  . ALA   B 1 52  ? 53.342 -25.224 -2.172  1.00 14.81 ?  52   ALA   B HB3  1 
ATOM   4776 N  N    . LEU   B 1 53  ? 53.775 -22.337 -1.793  1.00 10.81 ?  53   LEU   B N    1 
ATOM   4777 C  CA   . LEU   B 1 53  ? 53.666 -20.997 -2.364  1.00 11.06 ?  53   LEU   B CA   1 
ATOM   4778 C  C    . LEU   B 1 53  ? 54.676 -20.059 -1.716  1.00 10.82 ?  53   LEU   B C    1 
ATOM   4779 O  O    . LEU   B 1 53  ? 55.382 -19.310 -2.401  1.00 11.53 ?  53   LEU   B O    1 
ATOM   4780 C  CB   . LEU   B 1 53  ? 52.244 -20.452 -2.192  1.00 11.28 ?  53   LEU   B CB   1 
ATOM   4781 C  CG   . LEU   B 1 53  ? 51.113 -21.174 -2.936  1.00 11.47 ?  53   LEU   B CG   1 
ATOM   4782 C  CD1  . LEU   B 1 53  ? 49.771 -20.574 -2.578  1.00 12.87 ?  53   LEU   B CD1  1 
ATOM   4783 C  CD2  . LEU   B 1 53  ? 51.316 -21.151 -4.447  1.00 13.48 ?  53   LEU   B CD2  1 
ATOM   4784 H  H    . LEU   B 1 53  ? 53.071 -22.614 -1.390  1.00 12.99 ?  53   LEU   B H    1 
ATOM   4785 H  HA   . LEU   B 1 53  ? 53.869 -21.040 -3.315  1.00 13.29 ?  53   LEU   B HA   1 
ATOM   4786 H  HB2  . LEU   B 1 53  ? 52.029 -20.485 -1.249  1.00 13.55 ?  53   LEU   B HB2  1 
ATOM   4787 H  HB3  . LEU   B 1 53  ? 52.240 -19.533 -2.492  1.00 13.55 ?  53   LEU   B HB3  1 
ATOM   4788 H  HG   . LEU   B 1 53  ? 51.099 -22.101 -2.658  1.00 13.78 ?  53   LEU   B HG   1 
ATOM   4789 H  HD11 . LEU   B 1 53  ? 49.072 -21.053 -3.060  1.00 15.47 ?  53   LEU   B HD11 1 
ATOM   4790 H  HD12 . LEU   B 1 53  ? 49.626 -20.669 -1.622  1.00 15.47 ?  53   LEU   B HD12 1 
ATOM   4791 H  HD13 . LEU   B 1 53  ? 49.760 -19.640 -2.824  1.00 15.47 ?  53   LEU   B HD13 1 
ATOM   4792 H  HD21 . LEU   B 1 53  ? 50.630 -21.696 -4.866  1.00 16.20 ?  53   LEU   B HD21 1 
ATOM   4793 H  HD22 . LEU   B 1 53  ? 51.245 -20.237 -4.763  1.00 16.20 ?  53   LEU   B HD22 1 
ATOM   4794 H  HD23 . LEU   B 1 53  ? 52.192 -21.509 -4.658  1.00 16.20 ?  53   LEU   B HD23 1 
ATOM   4795 N  N    . ASN   B 1 54  ? 54.766 -20.090 -0.391  1.00 10.52 ?  54   ASN   B N    1 
ATOM   4796 C  CA   . ASN   B 1 54  ? 55.684 -19.184 0.276   1.00 11.11 ?  54   ASN   B CA   1 
ATOM   4797 C  C    . ASN   B 1 54  ? 57.124 -19.471 -0.126  1.00 11.48 ?  54   ASN   B C    1 
ATOM   4798 O  O    . ASN   B 1 54  ? 57.907 -18.541 -0.361  1.00 11.93 ?  54   ASN   B O    1 
ATOM   4799 C  CB   . ASN   B 1 54  ? 55.521 -19.258 1.785   1.00 11.96 ?  54   ASN   B CB   1 
ATOM   4800 C  CG   . ASN   B 1 54  ? 56.497 -18.351 2.494   1.00 11.98 ?  54   ASN   B CG   1 
ATOM   4801 O  OD1  . ASN   B 1 54  ? 56.520 -17.140 2.252   1.00 12.34 ?  54   ASN   B OD1  1 
ATOM   4802 N  ND2  . ASN   B 1 54  ? 57.334 -18.927 3.349   1.00 13.75 ?  54   ASN   B ND2  1 
ATOM   4803 H  H    . ASN   B 1 54  ? 54.320 -20.610 0.128   1.00 12.65 ?  54   ASN   B H    1 
ATOM   4804 H  HA   . ASN   B 1 54  ? 55.479 -18.277 0.002   1.00 13.36 ?  54   ASN   B HA   1 
ATOM   4805 H  HB2  . ASN   B 1 54  ? 54.623 -18.978 2.024   1.00 14.37 ?  54   ASN   B HB2  1 
ATOM   4806 H  HB3  . ASN   B 1 54  ? 55.683 -20.164 2.082   1.00 14.37 ?  54   ASN   B HB3  1 
ATOM   4807 H  HD21 . ASN   B 1 54  ? 57.916 -18.451 3.772   1.00 16.53 ?  54   ASN   B HD21 1 
ATOM   4808 H  HD22 . ASN   B 1 54  ? 57.299 -19.775 3.484   1.00 16.53 ?  54   ASN   B HD22 1 
ATOM   4809 N  N    . LYS   B 1 55  ? 57.503 -20.751 -0.191  1.00 12.20 ?  55   LYS   B N    1 
ATOM   4810 C  CA   . LYS   B 1 55  ? 58.859 -21.091 -0.603  1.00 12.87 ?  55   LYS   B CA   1 
ATOM   4811 C  C    . LYS   B 1 55  ? 59.158 -20.549 -1.994  1.00 12.97 ?  55   LYS   B C    1 
ATOM   4812 O  O    . LYS   B 1 55  ? 60.259 -20.045 -2.251  1.00 13.73 ?  55   LYS   B O    1 
ATOM   4813 C  CB   . LYS   B 1 55  ? 59.048 -22.607 -0.559  1.00 14.67 ?  55   LYS   B CB   1 
ATOM   4814 C  CG   . LYS   B 1 55  ? 60.418 -23.076 -1.014  1.00 18.80 ?  55   LYS   B CG   1 
ATOM   4815 C  CD   . LYS   B 1 55  ? 60.590 -24.576 -0.831  1.00 22.27 ?  55   LYS   B CD   1 
ATOM   4816 C  CE   . LYS   B 1 55  ? 60.647 -24.963 0.644   1.00 25.47 ?  55   LYS   B CE   1 
ATOM   4817 N  NZ   . LYS   B 1 55  ? 61.009 -26.388 0.830   1.00 26.98 ?  55   LYS   B NZ   1 
ATOM   4818 H  H    . LYS   B 1 55  ? 56.995 -21.423 -0.010  1.00 14.66 ?  55   LYS   B H    1 
ATOM   4819 H  HA   . LYS   B 1 55  ? 59.485 -20.691 0.018   1.00 15.47 ?  55   LYS   B HA   1 
ATOM   4820 H  HB2  . LYS   B 1 55  ? 58.915 -22.905 0.355   1.00 17.62 ?  55   LYS   B HB2  1 
ATOM   4821 H  HB3  . LYS   B 1 55  ? 58.386 -23.021 -1.136  1.00 17.62 ?  55   LYS   B HB3  1 
ATOM   4822 H  HG2  . LYS   B 1 55  ? 60.531 -22.873 -1.957  1.00 22.58 ?  55   LYS   B HG2  1 
ATOM   4823 H  HG3  . LYS   B 1 55  ? 61.101 -22.625 -0.492  1.00 22.58 ?  55   LYS   B HG3  1 
ATOM   4824 H  HD2  . LYS   B 1 55  ? 59.839 -25.039 -1.235  1.00 26.74 ?  55   LYS   B HD2  1 
ATOM   4825 H  HD3  . LYS   B 1 55  ? 61.420 -24.860 -1.248  1.00 26.74 ?  55   LYS   B HD3  1 
ATOM   4826 H  HE2  . LYS   B 1 55  ? 61.315 -24.412 1.087   1.00 30.58 ?  55   LYS   B HE2  1 
ATOM   4827 H  HE3  . LYS   B 1 55  ? 59.775 -24.813 1.044   1.00 30.58 ?  55   LYS   B HE3  1 
ATOM   4828 H  HZ1  . LYS   B 1 55  ? 61.010 -26.587 1.697   1.00 32.40 ?  55   LYS   B HZ1  1 
ATOM   4829 H  HZ2  . LYS   B 1 55  ? 60.418 -26.905 0.413   1.00 32.40 ?  55   LYS   B HZ2  1 
ATOM   4830 H  HZ3  . LYS   B 1 55  ? 61.818 -26.540 0.495   1.00 32.40 ?  55   LYS   B HZ3  1 
ATOM   4831 N  N    . ALA   B 1 56  ? 58.186 -20.631 -2.906  1.00 12.52 ?  56   ALA   B N    1 
ATOM   4832 C  CA   . ALA   B 1 56  ? 58.407 -20.131 -4.258  1.00 13.13 ?  56   ALA   B CA   1 
ATOM   4833 C  C    . ALA   B 1 56  ? 58.689 -18.635 -4.255  1.00 13.03 ?  56   ALA   B C    1 
ATOM   4834 O  O    . ALA   B 1 56  ? 59.423 -18.140 -5.122  1.00 14.06 ?  56   ALA   B O    1 
ATOM   4835 C  CB   . ALA   B 1 56  ? 57.204 -20.462 -5.144  1.00 14.20 ?  56   ALA   B CB   1 
ATOM   4836 H  H    . ALA   B 1 56  ? 57.400 -20.954 -2.765  1.00 15.04 ?  56   ALA   B H    1 
ATOM   4837 H  HA   . ALA   B 1 56  ? 59.181 -20.574 -4.631  1.00 15.77 ?  56   ALA   B HA   1 
ATOM   4838 H  HB1  . ALA   B 1 56  ? 57.374 -20.128 -6.041  1.00 17.07 ?  56   ALA   B HB1  1 
ATOM   4839 H  HB2  . ALA   B 1 56  ? 57.088 -21.425 -5.168  1.00 17.07 ?  56   ALA   B HB2  1 
ATOM   4840 H  HB3  . ALA   B 1 56  ? 56.414 -20.040 -4.778  1.00 17.07 ?  56   ALA   B HB3  1 
ATOM   4841 N  N    . THR   B 1 57  ? 58.126 -17.903 -3.292  1.00 12.60 ?  57   THR   B N    1 
ATOM   4842 C  CA   . THR   B 1 57  ? 58.363 -16.469 -3.165  1.00 12.66 ?  57   THR   B CA   1 
ATOM   4843 C  C    . THR   B 1 57  ? 59.614 -16.147 -2.355  1.00 13.28 ?  57   THR   B C    1 
ATOM   4844 O  O    . THR   B 1 57  ? 59.853 -14.973 -2.050  1.00 13.86 ?  57   THR   B O    1 
ATOM   4845 C  CB   . THR   B 1 57  ? 57.164 -15.741 -2.527  1.00 11.91 ?  57   THR   B CB   1 
ATOM   4846 O  OG1  . THR   B 1 57  ? 57.150 -15.952 -1.106  1.00 12.16 ?  57   THR   B OG1  1 
ATOM   4847 C  CG2  . THR   B 1 57  ? 55.845 -16.159 -3.159  1.00 12.22 ?  57   THR   B CG2  1 
ATOM   4848 H  H    . THR   B 1 57  ? 57.588 -18.217 -2.697  1.00 15.14 ?  57   THR   B H    1 
ATOM   4849 H  HA   . THR   B 1 57  ? 58.488 -16.100 -4.053  1.00 15.21 ?  57   THR   B HA   1 
ATOM   4850 H  HB   . THR   B 1 57  ? 57.269 -14.791 -2.693  1.00 14.31 ?  57   THR   B HB   1 
ATOM   4851 H  HG1  . THR   B 1 57  ? 57.081 -16.771 -0.941  1.00 14.61 ?  57   THR   B HG1  1 
ATOM   4852 H  HG21 . THR   B 1 57  ? 55.123 -15.624 -2.802  1.00 14.69 ?  57   THR   B HG21 1 
ATOM   4853 H  HG22 . THR   B 1 57  ? 55.885 -16.039 -4.120  1.00 14.69 ?  57   THR   B HG22 1 
ATOM   4854 H  HG23 . THR   B 1 57  ? 55.670 -17.094 -2.968  1.00 14.69 ?  57   THR   B HG23 1 
ATOM   4855 N  N    . ASN   B 1 58  ? 60.408 -17.153 -1.998  1.00 14.17 ?  58   ASN   B N    1 
ATOM   4856 C  CA   . ASN   B 1 58  ? 61.607 -16.939 -1.193  1.00 16.96 ?  58   ASN   B CA   1 
ATOM   4857 C  C    . ASN   B 1 58  ? 61.266 -16.229 0.117   1.00 14.68 ?  58   ASN   B C    1 
ATOM   4858 O  O    . ASN   B 1 58  ? 61.994 -15.349 0.580   1.00 15.49 ?  58   ASN   B O    1 
ATOM   4859 C  CB   . ASN   B 1 58  ? 62.688 -16.183 -1.972  1.00 24.91 ?  58   ASN   B CB   1 
ATOM   4860 C  CG   . ASN   B 1 58  ? 64.062 -16.322 -1.345  1.00 34.32 ?  58   ASN   B CG   1 
ATOM   4861 O  OD1  . ASN   B 1 58  ? 64.374 -17.339 -0.725  1.00 36.54 ?  58   ASN   B OD1  1 
ATOM   4862 N  ND2  . ASN   B 1 58  ? 64.891 -15.296 -1.499  1.00 38.82 ?  58   ASN   B ND2  1 
ATOM   4863 H  H    . ASN   B 1 58  ? 60.271 -17.979 -2.205  1.00 17.03 ?  58   ASN   B H    1 
ATOM   4864 H  HA   . ASN   B 1 58  ? 61.977 -17.808 -0.970  1.00 20.37 ?  58   ASN   B HA   1 
ATOM   4865 H  HB2  . ASN   B 1 58  ? 62.733 -16.533 -2.878  1.00 29.92 ?  58   ASN   B HB2  1 
ATOM   4866 H  HB3  . ASN   B 1 58  ? 62.465 -15.240 -1.993  1.00 29.92 ?  58   ASN   B HB3  1 
ATOM   4867 H  HD21 . ASN   B 1 58  ? 65.682 -15.327 -1.164  1.00 46.61 ?  58   ASN   B HD21 1 
ATOM   4868 H  HD22 . ASN   B 1 58  ? 64.637 -14.600 -1.936  1.00 46.61 ?  58   ASN   B HD22 1 
ATOM   4869 N  N    . ASN   B 1 59  ? 60.138 -16.611 0.717   1.00 13.55 ?  59   ASN   B N    1 
ATOM   4870 C  CA   . ASN   B 1 59  ? 59.662 -16.137 2.015   1.00 13.68 ?  59   ASN   B CA   1 
ATOM   4871 C  C    . ASN   B 1 59  ? 59.068 -14.731 1.958   1.00 13.18 ?  59   ASN   B C    1 
ATOM   4872 O  O    . ASN   B 1 59  ? 58.638 -14.224 2.998   1.00 13.34 ?  59   ASN   B O    1 
ATOM   4873 C  CB   . ASN   B 1 59  ? 60.737 -16.186 3.118   1.00 14.81 ?  59   ASN   B CB   1 
ATOM   4874 C  CG   . ASN   B 1 59  ? 60.150 -16.367 4.498   1.00 15.53 ?  59   ASN   B CG   1 
ATOM   4875 O  OD1  . ASN   B 1 59  ? 59.319 -17.249 4.719   1.00 15.83 ?  59   ASN   B OD1  1 
ATOM   4876 N  ND2  . ASN   B 1 59  ? 60.572 -15.530 5.438   1.00 16.15 ?  59   ASN   B ND2  1 
ATOM   4877 H  H    . ASN   B 1 59  ? 59.601 -17.189 0.369   1.00 16.28 ?  59   ASN   B H    1 
ATOM   4878 H  HA   . ASN   B 1 59  ? 58.955 -16.733 2.302   1.00 16.44 ?  59   ASN   B HA   1 
ATOM   4879 H  HB2  . ASN   B 1 59  ? 61.337 -16.931 2.955   1.00 17.80 ?  59   ASN   B HB2  1 
ATOM   4880 H  HB3  . ASN   B 1 59  ? 61.234 -15.354 3.121   1.00 17.80 ?  59   ASN   B HB3  1 
ATOM   4881 H  HD21 . ASN   B 1 59  ? 60.268 -15.595 6.241   1.00 19.41 ?  59   ASN   B HD21 1 
ATOM   4882 H  HD22 . ASN   B 1 59  ? 61.151 -14.925 5.247   1.00 19.41 ?  59   ASN   B HD22 1 
ATOM   4883 N  N    . ALA   B 1 60  ? 59.014 -14.087 0.790   1.00 12.78 ?  60   ALA   B N    1 
ATOM   4884 C  CA   . ALA   B 1 60  ? 58.418 -12.756 0.719   1.00 12.72 ?  60   ALA   B CA   1 
ATOM   4885 C  C    . ALA   B 1 60  ? 56.949 -12.782 1.119   1.00 11.88 ?  60   ALA   B C    1 
ATOM   4886 O  O    . ALA   B 1 60  ? 56.445 -11.831 1.732   1.00 12.57 ?  60   ALA   B O    1 
ATOM   4887 C  CB   . ALA   B 1 60  ? 58.584 -12.177 -0.686  1.00 13.60 ?  60   ALA   B CB   1 
ATOM   4888 H  H    . ALA   B 1 60  ? 59.310 -14.398 0.044   1.00 15.36 ?  60   ALA   B H    1 
ATOM   4889 H  HA   . ALA   B 1 60  ? 58.886 -12.175 1.338   1.00 15.29 ?  60   ALA   B HA   1 
ATOM   4890 H  HB1  . ALA   B 1 60  ? 58.185 -11.295 -0.709  1.00 16.34 ?  60   ALA   B HB1  1 
ATOM   4891 H  HB2  . ALA   B 1 60  ? 59.532 -12.119 -0.893  1.00 16.34 ?  60   ALA   B HB2  1 
ATOM   4892 H  HB3  . ALA   B 1 60  ? 58.143 -12.761 -1.321  1.00 16.34 ?  60   ALA   B HB3  1 
ATOM   4893 N  N    . MET   B 1 61  ? 56.242 -13.856 0.772   1.00 11.39 ?  61   MET   B N    1 
ATOM   4894 C  CA   . MET   B 1 61  ? 54.848 -13.975 1.169   1.00 11.06 ?  61   MET   B CA   1 
ATOM   4895 C  C    . MET   B 1 61  ? 54.710 -13.984 2.688   1.00 11.19 ?  61   MET   B C    1 
ATOM   4896 O  O    . MET   B 1 61  ? 53.808 -13.340 3.239   1.00 11.13 ?  61   MET   B O    1 
ATOM   4897 C  CB   . MET   B 1 61  ? 54.266 -15.244 0.545   1.00 11.05 ?  61   MET   B CB   1 
ATOM   4898 C  CG   . MET   B 1 61  ? 52.822 -15.531 0.943   1.00 10.80 ?  61   MET   B CG   1 
ATOM   4899 S  SD   . MET   B 1 61  ? 52.179 -17.030 0.181   1.00 11.33 ?  61   MET   B SD   1 
ATOM   4900 C  CE   . MET   B 1 61  ? 51.926 -16.435 -1.487  1.00 12.20 ?  61   MET   B CE   1 
ATOM   4901 H  H    . MET   B 1 61  ? 56.545 -14.522 0.311   1.00 13.70 ?  61   MET   B H    1 
ATOM   4902 H  HA   . MET   B 1 61  ? 54.355 -13.223 0.811   1.00 13.30 ?  61   MET   B HA   1 
ATOM   4903 H  HB2  . MET   B 1 61  ? 54.288 -15.158 -0.425  1.00 13.29 ?  61   MET   B HB2  1 
ATOM   4904 H  HB3  . MET   B 1 61  ? 54.801 -16.005 0.815   1.00 13.29 ?  61   MET   B HB3  1 
ATOM   4905 H  HG2  . MET   B 1 61  ? 52.772 -15.643 1.908   1.00 12.98 ?  61   MET   B HG2  1 
ATOM   4906 H  HG3  . MET   B 1 61  ? 52.261 -14.786 0.670   1.00 12.98 ?  61   MET   B HG3  1 
ATOM   4907 H  HE1  . MET   B 1 61  ? 51.539 -17.146 -2.019  1.00 14.67 ?  61   MET   B HE1  1 
ATOM   4908 H  HE2  . MET   B 1 61  ? 51.322 -15.673 -1.464  1.00 14.67 ?  61   MET   B HE2  1 
ATOM   4909 H  HE3  . MET   B 1 61  ? 52.780 -16.167 -1.860  1.00 14.67 ?  61   MET   B HE3  1 
ATOM   4910 N  N    . GLN   B 1 62  ? 55.593 -14.699 3.388   1.00 11.16 ?  62   GLN   B N    1 
ATOM   4911 C  CA   . GLN   B 1 62  ? 55.476 -14.761 4.841   1.00 11.40 ?  62   GLN   B CA   1 
ATOM   4912 C  C    . GLN   B 1 62  ? 55.759 -13.407 5.476   1.00 11.72 ?  62   GLN   B C    1 
ATOM   4913 O  O    . GLN   B 1 62  ? 55.073 -13.006 6.422   1.00 12.16 ?  62   GLN   B O    1 
ATOM   4914 C  CB   . GLN   B 1 62  ? 56.423 -15.818 5.407   1.00 11.96 ?  62   GLN   B CB   1 
ATOM   4915 C  CG   . GLN   B 1 62  ? 56.202 -16.088 6.883   1.00 12.06 ?  62   GLN   B CG   1 
ATOM   4916 C  CD   . GLN   B 1 62  ? 54.825 -16.674 7.119   1.00 11.56 ?  62   GLN   B CD   1 
ATOM   4917 O  OE1  . GLN   B 1 62  ? 54.565 -17.821 6.757   1.00 12.07 ?  62   GLN   B OE1  1 
ATOM   4918 N  NE2  . GLN   B 1 62  ? 53.918 -15.876 7.673   1.00 12.10 ?  62   GLN   B NE2  1 
ATOM   4919 H  H    . GLN   B 1 62  ? 56.246 -15.151 3.053   1.00 13.41 ?  62   GLN   B H    1 
ATOM   4920 H  HA   . GLN   B 1 62  ? 54.567 -15.018 5.068   1.00 13.70 ?  62   GLN   B HA   1 
ATOM   4921 H  HB2  . GLN   B 1 62  ? 56.290 -16.654 4.931   1.00 14.37 ?  62   GLN   B HB2  1 
ATOM   4922 H  HB3  . GLN   B 1 62  ? 57.337 -15.517 5.294   1.00 14.37 ?  62   GLN   B HB3  1 
ATOM   4923 H  HG2  . GLN   B 1 62  ? 56.866 -16.729 7.191   1.00 14.49 ?  62   GLN   B HG2  1 
ATOM   4924 H  HG3  . GLN   B 1 62  ? 56.277 -15.261 7.378   1.00 14.49 ?  62   GLN   B HG3  1 
ATOM   4925 H  HE21 . GLN   B 1 62  ? 54.132 -15.073 7.897   1.00 14.54 ?  62   GLN   B HE21 1 
ATOM   4926 H  HE22 . GLN   B 1 62  ? 53.122 -16.165 7.818   1.00 14.54 ?  62   GLN   B HE22 1 
ATOM   4927 N  N    . VAL   B 1 63  ? 56.778 -12.696 4.989   1.00 12.26 ?  63   VAL   B N    1 
ATOM   4928 C  CA   . VAL   B 1 63  ? 57.086 -11.379 5.541   1.00 13.08 ?  63   VAL   B CA   1 
ATOM   4929 C  C    . VAL   B 1 63  ? 55.896 -10.444 5.360   1.00 12.54 ?  63   VAL   B C    1 
ATOM   4930 O  O    . VAL   B 1 63  ? 55.482 -9.735  6.288   1.00 12.97 ?  63   VAL   B O    1 
ATOM   4931 C  CB   . VAL   B 1 63  ? 58.371 -10.828 4.901   1.00 14.13 ?  63   VAL   B CB   1 
ATOM   4932 C  CG1  . VAL   B 1 63  ? 58.610 -9.395  5.338   1.00 14.71 ?  63   VAL   B CG1  1 
ATOM   4933 C  CG2  . VAL   B 1 63  ? 59.555 -11.704 5.285   1.00 14.91 ?  63   VAL   B CG2  1 
ATOM   4934 H  H    . VAL   B 1 63  ? 57.290 -12.951 4.345   1.00 14.73 ?  63   VAL   B H    1 
ATOM   4935 H  HA   . VAL   B 1 63  ? 57.248 -11.474 6.489   1.00 15.71 ?  63   VAL   B HA   1 
ATOM   4936 H  HB   . VAL   B 1 63  ? 58.289 -10.850 3.934   1.00 16.98 ?  63   VAL   B HB   1 
ATOM   4937 H  HG11 . VAL   B 1 63  ? 59.528 -9.157  5.141   1.00 17.68 ?  63   VAL   B HG11 1 
ATOM   4938 H  HG12 . VAL   B 1 63  ? 58.004 -8.815  4.855   1.00 17.68 ?  63   VAL   B HG12 1 
ATOM   4939 H  HG13 . VAL   B 1 63  ? 58.449 -9.330  6.292   1.00 17.68 ?  63   VAL   B HG13 1 
ATOM   4940 H  HG21 . VAL   B 1 63  ? 60.364 -11.335 4.896   1.00 17.91 ?  63   VAL   B HG21 1 
ATOM   4941 H  HG22 . VAL   B 1 63  ? 59.634 -11.721 6.254   1.00 17.91 ?  63   VAL   B HG22 1 
ATOM   4942 H  HG23 . VAL   B 1 63  ? 59.410 -12.605 4.953   1.00 17.91 ?  63   VAL   B HG23 1 
ATOM   4943 N  N    . GLU   B 1 64  ? 55.326 -10.434 4.156   1.00 11.92 ?  64   GLU   B N    1 
ATOM   4944 C  CA   . GLU   B 1 64  ? 54.163 -9.595  3.882   1.00 11.70 ?  64   GLU   B CA   1 
ATOM   4945 C  C    . GLU   B 1 64  ? 52.978 -9.996  4.752   1.00 11.14 ?  64   GLU   B C    1 
ATOM   4946 O  O    . GLU   B 1 64  ? 52.230 -9.138  5.247   1.00 11.69 ?  64   GLU   B O    1 
ATOM   4947 C  CB   . GLU   B 1 64  ? 53.803 -9.742  2.403   1.00 11.74 ?  64   GLU   B CB   1 
ATOM   4948 C  CG   . GLU   B 1 64  ? 52.532 -9.020  1.975   1.00 12.03 ?  64   GLU   B CG   1 
ATOM   4949 C  CD   . GLU   B 1 64  ? 51.997 -9.521  0.645   1.00 12.38 ?  64   GLU   B CD   1 
ATOM   4950 O  OE1  . GLU   B 1 64  ? 52.178 -10.728 0.331   1.00 13.34 ?  64   GLU   B OE1  1 
ATOM   4951 O  OE2  . GLU   B 1 64  ? 51.385 -8.703  -0.083  1.00 13.31 -1 64   GLU   B OE2  1 
ATOM   4952 H  H    . GLU   B 1 64  ? 55.595 -10.901 3.480   1.00 14.32 ?  64   GLU   B H    1 
ATOM   4953 H  HA   . GLU   B 1 64  ? 54.379 -8.667  4.055   1.00 14.07 ?  64   GLU   B HA   1 
ATOM   4954 H  HB2  . GLU   B 1 64  ? 54.529 -9.378  1.866   1.00 14.11 ?  64   GLU   B HB2  1 
ATOM   4955 H  HB3  . GLU   B 1 64  ? 53.689 -10.680 2.200   1.00 14.11 ?  64   GLU   B HB3  1 
ATOM   4956 H  HG2  . GLU   B 1 64  ? 51.831 -9.162  2.635   1.00 14.45 ?  64   GLU   B HG2  1 
ATOM   4957 H  HG3  . GLU   B 1 64  ? 52.714 -8.071  1.894   1.00 14.45 ?  64   GLU   B HG3  1 
ATOM   4958 N  N    . SER   B 1 65  ? 52.792 -11.301 4.937   1.00 10.94 ?  65   SER   B N    1 
ATOM   4959 C  CA   . SER   B 1 65  ? 51.680 -11.803 5.730   1.00 11.09 ?  65   SER   B CA   1 
ATOM   4960 C  C    . SER   B 1 65  ? 51.811 -11.405 7.191   1.00 11.22 ?  65   SER   B C    1 
ATOM   4961 O  O    . SER   B 1 65  ? 50.812 -11.040 7.825   1.00 11.50 ?  65   SER   B O    1 
ATOM   4962 C  CB   . SER   B 1 65  ? 51.600 -13.323 5.601   1.00 11.28 ?  65   SER   B CB   1 
ATOM   4963 O  OG   . SER   B 1 65  ? 51.261 -13.717 4.281   1.00 11.37 ?  65   SER   B OG   1 
ATOM   4964 H  H    . SER   B 1 65  ? 53.299 -11.920 4.615   1.00 13.15 ?  65   SER   B H    1 
ATOM   4965 H  HA   . SER   B 1 65  ? 50.852 -11.430 5.390   1.00 13.33 ?  65   SER   B HA   1 
ATOM   4966 H  HB2  . SER   B 1 65  ? 52.455 -13.707 5.831   1.00 13.56 ?  65   SER   B HB2  1 
ATOM   4967 H  HB3  . SER   B 1 65  ? 50.915 -13.652 6.209   1.00 13.56 ?  65   SER   B HB3  1 
ATOM   4968 H  HG   . SER   B 1 65  ? 51.838 -13.435 3.734   1.00 13.66 ?  65   SER   B HG   1 
ATOM   4969 N  N    . ASP   B 1 66  ? 53.018 -11.504 7.758   1.00 11.79 ?  66   ASP   B N    1 
ATOM   4970 C  CA   . ASP   B 1 66  ? 53.200 -11.112 9.152   1.00 11.80 ?  66   ASP   B CA   1 
ATOM   4971 C  C    . ASP   B 1 66  ? 52.889 -9.633  9.348   1.00 11.94 ?  66   ASP   B C    1 
ATOM   4972 O  O    . ASP   B 1 66  ? 52.310 -9.238  10.367  1.00 12.43 ?  66   ASP   B O    1 
ATOM   4973 C  CB   . ASP   B 1 66  ? 54.628 -11.422 9.607   1.00 12.94 ?  66   ASP   B CB   1 
ATOM   4974 C  CG   . ASP   B 1 66  ? 54.900 -12.918 9.753   1.00 14.74 ?  66   ASP   B CG   1 
ATOM   4975 O  OD1  . ASP   B 1 66  ? 53.948 -13.726 9.667   1.00 15.39 ?  66   ASP   B OD1  1 
ATOM   4976 O  OD2  . ASP   B 1 66  ? 56.081 -13.286 9.967   1.00 17.27 -1 66   ASP   B OD2  1 
ATOM   4977 H  H    . ASP   B 1 66  ? 53.724 -11.795 7.368   1.00 14.17 ?  66   ASP   B H    1 
ATOM   4978 H  HA   . ASP   B 1 66  ? 52.593 -11.618 9.714   1.00 14.19 ?  66   ASP   B HA   1 
ATOM   4979 H  HB2  . ASP   B 1 66  ? 55.252 -11.070 8.955   1.00 15.55 ?  66   ASP   B HB2  1 
ATOM   4980 H  HB3  . ASP   B 1 66  ? 54.783 -11.000 10.472  1.00 15.55 ?  66   ASP   B HB3  1 
ATOM   4981 N  N    . ASP   B 1 67  ? 53.270 -8.796  8.383   1.00 11.66 ?  67   ASP   B N    1 
ATOM   4982 C  CA   . ASP   B 1 67  ? 52.926 -7.384  8.465   1.00 12.23 ?  67   ASP   B CA   1 
ATOM   4983 C  C    . ASP   B 1 67  ? 51.415 -7.175  8.383   1.00 12.32 ?  67   ASP   B C    1 
ATOM   4984 O  O    . ASP   B 1 67  ? 50.854 -6.363  9.128   1.00 13.11 ?  67   ASP   B O    1 
ATOM   4985 C  CB   . ASP   B 1 67  ? 53.651 -6.618  7.365   1.00 13.45 ?  67   ASP   B CB   1 
ATOM   4986 C  CG   . ASP   B 1 67  ? 53.221 -5.181  7.304   1.00 14.69 ?  67   ASP   B CG   1 
ATOM   4987 O  OD1  . ASP   B 1 67  ? 53.721 -4.358  8.105   1.00 16.13 ?  67   ASP   B OD1  1 
ATOM   4988 O  OD2  . ASP   B 1 67  ? 52.344 -4.894  6.476   1.00 15.86 -1 67   ASP   B OD2  1 
ATOM   4989 H  H    . ASP   B 1 67  ? 53.729 -9.019  7.689   1.00 14.02 ?  67   ASP   B H    1 
ATOM   4990 H  HA   . ASP   B 1 67  ? 53.231 -7.034  9.316   1.00 14.70 ?  67   ASP   B HA   1 
ATOM   4991 H  HB2  . ASP   B 1 67  ? 54.606 -6.638  7.535   1.00 16.17 ?  67   ASP   B HB2  1 
ATOM   4992 H  HB3  . ASP   B 1 67  ? 53.461 -7.038  6.507   1.00 16.17 ?  67   ASP   B HB3  1 
ATOM   4993 N  N    . TYR   B 1 68  ? 50.736 -7.905  7.490   1.00 11.91 ?  68   TYR   B N    1 
ATOM   4994 C  CA   . TYR   B 1 68  ? 49.280 -7.834  7.417   1.00 12.80 ?  68   TYR   B CA   1 
ATOM   4995 C  C    . TYR   B 1 68  ? 48.648 -8.173  8.762   1.00 12.64 ?  68   TYR   B C    1 
ATOM   4996 O  O    . TYR   B 1 68  ? 47.716 -7.498  9.212   1.00 12.93 ?  68   TYR   B O    1 
ATOM   4997 C  CB   . TYR   B 1 68  ? 48.749 -8.769  6.321   1.00 13.42 ?  68   TYR   B CB   1 
ATOM   4998 C  CG   . TYR   B 1 68  ? 47.248 -8.920  6.381   1.00 14.30 ?  68   TYR   B CG   1 
ATOM   4999 C  CD1  . TYR   B 1 68  ? 46.663 -9.864  7.215   1.00 14.88 ?  68   TYR   B CD1  1 
ATOM   5000 C  CD2  . TYR   B 1 68  ? 46.417 -8.093  5.644   1.00 15.14 ?  68   TYR   B CD2  1 
ATOM   5001 C  CE1  . TYR   B 1 68  ? 45.298 -9.988  7.309   1.00 16.15 ?  68   TYR   B CE1  1 
ATOM   5002 C  CE2  . TYR   B 1 68  ? 45.033 -8.218  5.723   1.00 15.18 ?  68   TYR   B CE2  1 
ATOM   5003 C  CZ   . TYR   B 1 68  ? 44.494 -9.163  6.565   1.00 15.80 ?  68   TYR   B CZ   1 
ATOM   5004 O  OH   . TYR   B 1 68  ? 43.128 -9.286  6.666   1.00 16.89 ?  68   TYR   B OH   1 
ATOM   5005 H  H    . TYR   B 1 68  ? 51.097 -8.448  6.919   1.00 14.32 ?  68   TYR   B H    1 
ATOM   5006 H  HA   . TYR   B 1 68  ? 49.026 -6.929  7.189   1.00 15.39 ?  68   TYR   B HA   1 
ATOM   5007 H  HB2  . TYR   B 1 68  ? 48.975 -8.403  5.454   1.00 16.12 ?  68   TYR   B HB2  1 
ATOM   5008 H  HB3  . TYR   B 1 68  ? 49.141 -9.647  6.431   1.00 16.12 ?  68   TYR   B HB3  1 
ATOM   5009 H  HD1  . TYR   B 1 68  ? 47.204 -10.425 7.724   1.00 17.88 ?  68   TYR   B HD1  1 
ATOM   5010 H  HD2  . TYR   B 1 68  ? 46.789 -7.445  5.094   1.00 18.19 ?  68   TYR   B HD2  1 
ATOM   5011 H  HE1  . TYR   B 1 68  ? 44.917 -10.635 7.862   1.00 19.40 ?  68   TYR   B HE1  1 
ATOM   5012 H  HE2  . TYR   B 1 68  ? 44.478 -7.655  5.230   1.00 18.24 ?  68   TYR   B HE2  1 
ATOM   5013 H  HH   . TYR   B 1 68  ? 42.736 -8.738  6.152   1.00 20.29 ?  68   TYR   B HH   1 
ATOM   5014 N  N    . ILE   B 1 69  ? 49.131 -9.236  9.411   1.00 12.04 ?  69   ILE   B N    1 
ATOM   5015 C  CA   . ILE   B 1 69  ? 48.569 -9.658  10.692  1.00 12.49 ?  69   ILE   B CA   1 
ATOM   5016 C  C    . ILE   B 1 69  ? 48.822 -8.611  11.767  1.00 12.55 ?  69   ILE   B C    1 
ATOM   5017 O  O    . ILE   B 1 69  ? 47.952 -8.330  12.596  1.00 12.64 ?  69   ILE   B O    1 
ATOM   5018 C  CB   . ILE   B 1 69  ? 49.144 -11.032 11.088  1.00 13.25 ?  69   ILE   B CB   1 
ATOM   5019 C  CG1  . ILE   B 1 69  ? 48.623 -12.139 10.162  1.00 13.80 ?  69   ILE   B CG1  1 
ATOM   5020 C  CG2  . ILE   B 1 69  ? 48.845 -11.351 12.543  1.00 14.00 ?  69   ILE   B CG2  1 
ATOM   5021 C  CD1  . ILE   B 1 69  ? 47.145 -12.442 10.312  1.00 14.28 ?  69   ILE   B CD1  1 
ATOM   5022 H  H    . ILE   B 1 69  ? 49.781 -9.724  9.136   1.00 14.47 ?  69   ILE   B H    1 
ATOM   5023 H  HA   . ILE   B 1 69  ? 47.611 -9.755  10.595  1.00 15.01 ?  69   ILE   B HA   1 
ATOM   5024 H  HB   . ILE   B 1 69  ? 50.109 -10.991 10.990  1.00 15.93 ?  69   ILE   B HB   1 
ATOM   5025 H  HG12 . ILE   B 1 69  ? 48.781 -11.870 9.243   1.00 16.58 ?  69   ILE   B HG12 1 
ATOM   5026 H  HG13 . ILE   B 1 69  ? 49.115 -12.956 10.350  1.00 16.58 ?  69   ILE   B HG13 1 
ATOM   5027 H  HG21 . ILE   B 1 69  ? 48.986 -12.302 12.690  1.00 16.82 ?  69   ILE   B HG21 1 
ATOM   5028 H  HG22 . ILE   B 1 69  ? 49.441 -10.842 13.113  1.00 16.82 ?  69   ILE   B HG22 1 
ATOM   5029 H  HG23 . ILE   B 1 69  ? 47.922 -11.124 12.734  1.00 16.82 ?  69   ILE   B HG23 1 
ATOM   5030 H  HD11 . ILE   B 1 69  ? 46.911 -13.154 9.699   1.00 17.16 ?  69   ILE   B HD11 1 
ATOM   5031 H  HD12 . ILE   B 1 69  ? 46.970 -12.721 11.224  1.00 17.16 ?  69   ILE   B HD12 1 
ATOM   5032 H  HD13 . ILE   B 1 69  ? 46.636 -11.645 10.104  1.00 17.16 ?  69   ILE   B HD13 1 
ATOM   5033 N  N    . ALA   B 1 70  ? 50.015 -8.025  11.787  1.00 12.33 ?  70   ALA   B N    1 
ATOM   5034 C  CA   . ALA   B 1 70  ? 50.293 -6.989  12.773  1.00 12.14 ?  70   ALA   B CA   1 
ATOM   5035 C  C    . ALA   B 1 70  ? 49.296 -5.846  12.661  1.00 12.78 ?  70   ALA   B C    1 
ATOM   5036 O  O    . ALA   B 1 70  ? 48.859 -5.294  13.674  1.00 12.95 ?  70   ALA   B O    1 
ATOM   5037 C  CB   . ALA   B 1 70  ? 51.720 -6.476  12.601  1.00 12.96 ?  70   ALA   B CB   1 
ATOM   5038 H  H    . ALA   B 1 70  ? 50.659 -8.203  11.252  1.00 14.82 ?  70   ALA   B H    1 
ATOM   5039 H  HA   . ALA   B 1 70  ? 50.218 -7.370  13.664  1.00 14.59 ?  70   ALA   B HA   1 
ATOM   5040 H  HB1  . ALA   B 1 70  ? 51.906 -5.817  13.290  1.00 15.57 ?  70   ALA   B HB1  1 
ATOM   5041 H  HB2  . ALA   B 1 70  ? 52.339 -7.220  12.685  1.00 15.57 ?  70   ALA   B HB2  1 
ATOM   5042 H  HB3  . ALA   B 1 70  ? 51.809 -6.071  11.724  1.00 15.57 ?  70   ALA   B HB3  1 
ATOM   5043 N  N    . THR   B 1 71  ? 48.924 -5.482  11.437  1.00 13.13 ?  71   THR   B N    1 
ATOM   5044 C  CA   . THR   B 1 71  ? 48.029 -4.351  11.223  1.00 14.05 ?  71   THR   B CA   1 
ATOM   5045 C  C    . THR   B 1 71  ? 46.563 -4.721  11.428  1.00 14.58 ?  71   THR   B C    1 
ATOM   5046 O  O    . THR   B 1 71  ? 45.786 -3.906  11.945  1.00 16.07 ?  71   THR   B O    1 
ATOM   5047 C  CB   . THR   B 1 71  ? 48.254 -3.794  9.817   1.00 15.98 ?  71   THR   B CB   1 
ATOM   5048 O  OG1  . THR   B 1 71  ? 49.575 -3.247  9.729   1.00 17.64 ?  71   THR   B OG1  1 
ATOM   5049 C  CG2  . THR   B 1 71  ? 47.225 -2.725  9.476   1.00 17.18 ?  71   THR   B CG2  1 
ATOM   5050 H  H    . THR   B 1 71  ? 49.178 -5.877  10.717  1.00 15.78 ?  71   THR   B H    1 
ATOM   5051 H  HA   . THR   B 1 71  ? 48.248 -3.656  11.858  1.00 16.88 ?  71   THR   B HA   1 
ATOM   5052 H  HB   . THR   B 1 71  ? 48.175 -4.507  9.167   1.00 19.19 ?  71   THR   B HB   1 
ATOM   5053 H  HG1  . THR   B 1 71  ? 49.700 -2.911  8.965   1.00 21.19 ?  71   THR   B HG1  1 
ATOM   5054 H  HG21 . THR   B 1 71  ? 47.528 -2.204  8.715   1.00 20.64 ?  71   THR   B HG21 1 
ATOM   5055 H  HG22 . THR   B 1 71  ? 46.376 -3.137  9.255   1.00 20.64 ?  71   THR   B HG22 1 
ATOM   5056 H  HG23 . THR   B 1 71  ? 47.101 -2.130  10.232  1.00 20.64 ?  71   THR   B HG23 1 
ATOM   5057 N  N    . ASN   B 1 72  ? 46.171 -5.938  11.039  1.00 14.21 ?  72   ASN   B N    1 
ATOM   5058 C  CA   . ASN   B 1 72  ? 44.767 -6.299  10.916  1.00 15.07 ?  72   ASN   B CA   1 
ATOM   5059 C  C    . ASN   B 1 72  ? 44.297 -7.398  11.861  1.00 15.34 ?  72   ASN   B C    1 
ATOM   5060 O  O    . ASN   B 1 72  ? 43.081 -7.553  12.033  1.00 16.56 ?  72   ASN   B O    1 
ATOM   5061 C  CB   . ASN   B 1 72  ? 44.458 -6.724  9.471   1.00 15.76 ?  72   ASN   B CB   1 
ATOM   5062 C  CG   . ASN   B 1 72  ? 44.743 -5.626  8.473   1.00 16.93 ?  72   ASN   B CG   1 
ATOM   5063 O  OD1  . ASN   B 1 72  ? 45.773 -5.636  7.790   1.00 17.98 ?  72   ASN   B OD1  1 
ATOM   5064 N  ND2  . ASN   B 1 72  ? 43.852 -4.652  8.405   1.00 18.74 ?  72   ASN   B ND2  1 
ATOM   5065 H  H    . ASN   B 1 72  ? 46.713 -6.583  10.835  1.00 17.08 ?  72   ASN   B H    1 
ATOM   5066 H  HA   . ASN   B 1 72  ? 44.236 -5.516  11.103  1.00 18.10 ?  72   ASN   B HA   1 
ATOM   5067 H  HB2  . ASN   B 1 72  ? 45.011 -7.488  9.237   1.00 18.94 ?  72   ASN   B HB2  1 
ATOM   5068 H  HB3  . ASN   B 1 72  ? 43.522 -6.955  9.400   1.00 18.94 ?  72   ASN   B HB3  1 
ATOM   5069 H  HD21 . ASN   B 1 72  ? 43.962 -4.000  7.854   1.00 22.51 ?  72   ASN   B HD21 1 
ATOM   5070 H  HD22 . ASN   B 1 72  ? 43.145 -4.681  8.896   1.00 22.51 ?  72   ASN   B HD22 1 
ATOM   5071 N  N    . GLY   B 1 73  ? 45.199 -8.153  12.478  1.00 14.73 ?  73   GLY   B N    1 
ATOM   5072 C  CA   . GLY   B 1 73  ? 44.802 -9.289  13.271  1.00 14.49 ?  73   GLY   B CA   1 
ATOM   5073 C  C    . GLY   B 1 73  ? 44.445 -10.473 12.399  1.00 13.16 ?  73   GLY   B C    1 
ATOM   5074 O  O    . GLY   B 1 73  ? 44.441 -10.392 11.167  1.00 13.02 ?  73   GLY   B O    1 
ATOM   5075 H  H    . GLY   B 1 73  ? 46.052 -8.027  12.447  1.00 17.70 ?  73   GLY   B H    1 
ATOM   5076 H  HA2  . GLY   B 1 73  ? 45.526 -9.545  13.866  1.00 17.41 ?  73   GLY   B HA2  1 
ATOM   5077 H  HA3  . GLY   B 1 73  ? 44.028 -9.057  13.812  1.00 17.41 ?  73   GLY   B HA3  1 
ATOM   5078 N  N    . PRO   B 1 74  ? 44.144 -11.600 13.036  1.00 13.22 ?  74   PRO   B N    1 
ATOM   5079 C  CA   . PRO   B 1 74  ? 43.885 -12.829 12.288  1.00 12.89 ?  74   PRO   B CA   1 
ATOM   5080 C  C    . PRO   B 1 74  ? 42.583 -12.764 11.504  1.00 12.16 ?  74   PRO   B C    1 
ATOM   5081 O  O    . PRO   B 1 74  ? 41.644 -12.025 11.828  1.00 13.51 ?  74   PRO   B O    1 
ATOM   5082 C  CB   . PRO   B 1 74  ? 43.808 -13.893 13.388  1.00 13.96 ?  74   PRO   B CB   1 
ATOM   5083 C  CG   . PRO   B 1 74  ? 43.346 -13.140 14.591  1.00 15.31 ?  74   PRO   B CG   1 
ATOM   5084 C  CD   . PRO   B 1 74  ? 44.027 -11.806 14.488  1.00 14.72 ?  74   PRO   B CD   1 
ATOM   5085 H  HA   . PRO   B 1 74  ? 44.625 -13.027 11.685  1.00 15.49 ?  74   PRO   B HA   1 
ATOM   5086 H  HB2  . PRO   B 1 74  ? 43.168 -14.577 13.137  1.00 16.77 ?  74   PRO   B HB2  1 
ATOM   5087 H  HB3  . PRO   B 1 74  ? 44.687 -14.277 13.535  1.00 16.77 ?  74   PRO   B HB3  1 
ATOM   5088 H  HG2  . PRO   B 1 74  ? 42.380 -13.036 14.561  1.00 18.40 ?  74   PRO   B HG2  1 
ATOM   5089 H  HG3  . PRO   B 1 74  ? 43.618 -13.606 15.395  1.00 18.40 ?  74   PRO   B HG3  1 
ATOM   5090 H  HD2  . PRO   B 1 74  ? 43.476 -11.112 14.890  1.00 17.69 ?  74   PRO   B HD2  1 
ATOM   5091 H  HD3  . PRO   B 1 74  ? 44.906 -11.841 14.897  1.00 17.69 ?  74   PRO   B HD3  1 
ATOM   5092 N  N    . LEU   B 1 75  ? 42.548 -13.574 10.450  1.00 11.66 ?  75   LEU   B N    1 
ATOM   5093 C  CA   . LEU   B 1 75  ? 41.338 -13.787 9.679   1.00 11.81 ?  75   LEU   B CA   1 
ATOM   5094 C  C    . LEU   B 1 75  ? 40.362 -14.647 10.476  1.00 12.34 ?  75   LEU   B C    1 
ATOM   5095 O  O    . LEU   B 1 75  ? 40.702 -15.218 11.512  1.00 13.24 ?  75   LEU   B O    1 
ATOM   5096 C  CB   . LEU   B 1 75  ? 41.666 -14.498 8.366   1.00 12.13 ?  75   LEU   B CB   1 
ATOM   5097 C  CG   . LEU   B 1 75  ? 42.510 -13.748 7.331   1.00 13.75 ?  75   LEU   B CG   1 
ATOM   5098 C  CD1  . LEU   B 1 75  ? 42.712 -14.593 6.070   1.00 15.03 ?  75   LEU   B CD1  1 
ATOM   5099 C  CD2  . LEU   B 1 75  ? 41.904 -12.417 6.978   1.00 17.26 ?  75   LEU   B CD2  1 
ATOM   5100 H  H    . LEU   B 1 75  ? 43.222 -14.018 10.157  1.00 14.01 ?  75   LEU   B H    1 
ATOM   5101 H  HA   . LEU   B 1 75  ? 40.917 -12.938 9.480   1.00 14.20 ?  75   LEU   B HA   1 
ATOM   5102 H  HB2  . LEU   B 1 75  ? 42.140 -15.318 8.577   1.00 14.57 ?  75   LEU   B HB2  1 
ATOM   5103 H  HB3  . LEU   B 1 75  ? 40.827 -14.726 7.929   1.00 14.57 ?  75   LEU   B HB3  1 
ATOM   5104 H  HG   . LEU   B 1 75  ? 43.386 -13.584 7.709   1.00 16.52 ?  75   LEU   B HG   1 
ATOM   5105 H  HD11 . LEU   B 1 75  ? 43.255 -14.093 5.435   1.00 18.06 ?  75   LEU   B HD11 1 
ATOM   5106 H  HD12 . LEU   B 1 75  ? 43.166 -15.419 6.305   1.00 18.06 ?  75   LEU   B HD12 1 
ATOM   5107 H  HD13 . LEU   B 1 75  ? 41.849 -14.793 5.675   1.00 18.06 ?  75   LEU   B HD13 1 
ATOM   5108 H  HD21 . LEU   B 1 75  ? 42.418 -12.017 6.261   1.00 20.74 ?  75   LEU   B HD21 1 
ATOM   5109 H  HD22 . LEU   B 1 75  ? 40.987 -12.554 6.694   1.00 20.74 ?  75   LEU   B HD22 1 
ATOM   5110 H  HD23 . LEU   B 1 75  ? 41.927 -11.846 7.762   1.00 20.74 ?  75   LEU   B HD23 1 
ATOM   5111 N  N    . LYS   B 1 76  ? 39.131 -14.728 9.979   1.00 13.28 ?  76   LYS   B N    1 
ATOM   5112 C  CA   . LYS   B 1 76  ? 38.149 -15.686 10.464  1.00 14.60 ?  76   LYS   B CA   1 
ATOM   5113 C  C    . LYS   B 1 76  ? 38.241 -16.958 9.627   1.00 13.38 ?  76   LYS   B C    1 
ATOM   5114 O  O    . LYS   B 1 76  ? 38.514 -16.902 8.429   1.00 13.00 ?  76   LYS   B O    1 
ATOM   5115 C  CB   . LYS   B 1 76  ? 36.733 -15.117 10.289  1.00 16.95 ?  76   LYS   B CB   1 
ATOM   5116 C  CG   . LYS   B 1 76  ? 36.455 -13.736 10.910  1.00 18.74 ?  76   LYS   B CG   1 
ATOM   5117 C  CD   . LYS   B 1 76  ? 35.059 -13.211 10.534  1.00 19.88 ?  76   LYS   B CD   1 
ATOM   5118 C  CE   . LYS   B 1 76  ? 34.776 -11.854 11.160  1.00 21.87 ?  76   LYS   B CE   1 
ATOM   5119 N  NZ   . LYS   B 1 76  ? 33.483 -11.272 10.701  1.00 22.31 ?  76   LYS   B NZ   1 
ATOM   5120 H  H    . LYS   B 1 76  ? 38.836 -14.231 9.343   1.00 15.96 ?  76   LYS   B H    1 
ATOM   5121 H  HA   . LYS   B 1 76  ? 38.302 -15.900 11.399  1.00 17.54 ?  76   LYS   B HA   1 
ATOM   5122 H  HB2  . LYS   B 1 76  ? 36.552 -15.044 9.340   1.00 20.36 ?  76   LYS   B HB2  1 
ATOM   5123 H  HB3  . LYS   B 1 76  ? 36.103 -15.738 10.688  1.00 20.36 ?  76   LYS   B HB3  1 
ATOM   5124 H  HG2  . LYS   B 1 76  ? 36.506 -13.803 11.876  1.00 22.51 ?  76   LYS   B HG2  1 
ATOM   5125 H  HG3  . LYS   B 1 76  ? 37.117 -13.102 10.585  1.00 22.51 ?  76   LYS   B HG3  1 
ATOM   5126 H  HD2  . LYS   B 1 76  ? 35.003 -13.119 9.569   1.00 23.88 ?  76   LYS   B HD2  1 
ATOM   5127 H  HD3  . LYS   B 1 76  ? 34.389 -13.837 10.849  1.00 23.88 ?  76   LYS   B HD3  1 
ATOM   5128 H  HE2  . LYS   B 1 76  ? 34.739 -11.953 12.123  1.00 26.26 ?  76   LYS   B HE2  1 
ATOM   5129 H  HE3  . LYS   B 1 76  ? 35.488 -11.240 10.916  1.00 26.26 ?  76   LYS   B HE3  1 
ATOM   5130 H  HZ1  . LYS   B 1 76  ? 33.353 -10.480 11.086  1.00 26.80 ?  76   LYS   B HZ1  1 
ATOM   5131 H  HZ2  . LYS   B 1 76  ? 33.494 -11.163 9.817   1.00 26.80 ?  76   LYS   B HZ2  1 
ATOM   5132 H  HZ3  . LYS   B 1 76  ? 32.811 -11.813 10.917  1.00 26.80 ?  76   LYS   B HZ3  1 
ATOM   5133 N  N    . VAL   B 1 77  ? 38.000 -18.113 10.255  1.00 13.96 ?  77   VAL   B N    1 
ATOM   5134 C  CA   . VAL   B 1 77  ? 37.797 -19.326 9.469   1.00 14.00 ?  77   VAL   B CA   1 
ATOM   5135 C  C    . VAL   B 1 77  ? 36.605 -19.094 8.551   1.00 13.04 ?  77   VAL   B C    1 
ATOM   5136 O  O    . VAL   B 1 77  ? 35.541 -18.647 8.997   1.00 13.03 ?  77   VAL   B O    1 
ATOM   5137 C  CB   . VAL   B 1 77  ? 37.601 -20.549 10.376  1.00 15.65 ?  77   VAL   B CB   1 
ATOM   5138 C  CG1  . VAL   B 1 77  ? 37.324 -21.783 9.528   1.00 16.21 ?  77   VAL   B CG1  1 
ATOM   5139 C  CG2  . VAL   B 1 77  ? 38.830 -20.766 11.264  1.00 17.00 ?  77   VAL   B CG2  1 
ATOM   5140 H  H    . VAL   B 1 77  ? 37.949 -18.217 11.103  1.00 16.78 ?  77   VAL   B H    1 
ATOM   5141 H  HA   . VAL   B 1 77  ? 38.573 -19.480 8.910   1.00 16.83 ?  77   VAL   B HA   1 
ATOM   5142 H  HB   . VAL   B 1 77  ? 36.828 -20.399 10.946  1.00 18.81 ?  77   VAL   B HB   1 
ATOM   5143 H  HG11 . VAL   B 1 77  ? 37.383 -22.568 10.092  1.00 19.48 ?  77   VAL   B HG11 1 
ATOM   5144 H  HG12 . VAL   B 1 77  ? 36.432 -21.718 9.147   1.00 19.48 ?  77   VAL   B HG12 1 
ATOM   5145 H  HG13 . VAL   B 1 77  ? 37.983 -21.832 8.819   1.00 19.48 ?  77   VAL   B HG13 1 
ATOM   5146 H  HG21 . VAL   B 1 77  ? 38.694 -21.566 11.790  1.00 20.43 ?  77   VAL   B HG21 1 
ATOM   5147 H  HG22 . VAL   B 1 77  ? 39.608 -20.864 10.696  1.00 20.43 ?  77   VAL   B HG22 1 
ATOM   5148 H  HG23 . VAL   B 1 77  ? 38.933 -19.996 11.843  1.00 20.43 ?  77   VAL   B HG23 1 
ATOM   5149 N  N    . GLY   B 1 78  ? 36.782 -19.370 7.259   1.00 12.34 ?  78   GLY   B N    1 
ATOM   5150 C  CA   . GLY   B 1 78  ? 35.801 -19.052 6.247   1.00 11.90 ?  78   GLY   B CA   1 
ATOM   5151 C  C    . GLY   B 1 78  ? 36.040 -17.732 5.549   1.00 11.41 ?  78   GLY   B C    1 
ATOM   5152 O  O    . GLY   B 1 78  ? 35.357 -17.447 4.561   1.00 11.86 ?  78   GLY   B O    1 
ATOM   5153 H  H    . GLY   B 1 78  ? 37.484 -19.755 6.940   1.00 14.83 ?  78   GLY   B H    1 
ATOM   5154 H  HA2  . GLY   B 1 78  ? 35.796 -19.746 5.574   1.00 14.31 ?  78   GLY   B HA2  1 
ATOM   5155 H  HA3  . GLY   B 1 78  ? 34.922 -19.016 6.655   1.00 14.31 ?  78   GLY   B HA3  1 
ATOM   5156 N  N    . GLY   B 1 79  ? 36.991 -16.927 6.031   1.00 11.35 ?  79   GLY   B N    1 
ATOM   5157 C  CA   . GLY   B 1 79  ? 37.286 -15.632 5.454   1.00 11.23 ?  79   GLY   B CA   1 
ATOM   5158 C  C    . GLY   B 1 79  ? 38.526 -15.655 4.570   1.00 10.66 ?  79   GLY   B C    1 
ATOM   5159 O  O    . GLY   B 1 79  ? 39.141 -16.690 4.328   1.00 11.18 ?  79   GLY   B O    1 
ATOM   5160 H  H    . GLY   B 1 79  ? 37.488 -17.118 6.700   1.00 13.64 ?  79   GLY   B H    1 
ATOM   5161 H  HA2  . GLY   B 1 79  ? 36.535 -15.332 4.914   1.00 13.50 ?  79   GLY   B HA2  1 
ATOM   5162 H  HA3  . GLY   B 1 79  ? 37.433 -14.986 6.159   1.00 13.50 ?  79   GLY   B HA3  1 
ATOM   5163 N  N    . SER   B 1 80  ? 38.895 -14.464 4.091   1.00 10.94 ?  80   SER   B N    1 
ATOM   5164 C  CA   . SER   B 1 80  ? 40.010 -14.335 3.165   1.00 10.47 ?  80   SER   B CA   1 
ATOM   5165 C  C    . SER   B 1 80  ? 40.586 -12.928 3.223   1.00 10.26 ?  80   SER   B C    1 
ATOM   5166 O  O    . SER   B 1 80  ? 39.968 -11.992 3.733   1.00 11.47 ?  80   SER   B O    1 
ATOM   5167 C  CB   . SER   B 1 80  ? 39.579 -14.622 1.723   1.00 10.80 ?  80   SER   B CB   1 
ATOM   5168 O  OG   . SER   B 1 80  ? 38.730 -13.607 1.219   1.00 11.90 ?  80   SER   B OG   1 
ATOM   5169 H  H    . SER   B 1 80  ? 38.512 -13.718 4.281   1.00 13.15 ?  80   SER   B H    1 
ATOM   5170 H  HA   . SER   B 1 80  ? 40.698 -14.967 3.414   1.00 12.59 ?  80   SER   B HA   1 
ATOM   5171 H  HB2  . SER   B 1 80  ? 40.368 -14.667 1.158   1.00 12.98 ?  80   SER   B HB2  1 
ATOM   5172 H  HB3  . SER   B 1 80  ? 39.108 -15.469 1.695   1.00 12.98 ?  80   SER   B HB3  1 
ATOM   5173 H  HG   . SER   B 1 80  ? 38.030 -13.557 1.696   1.00 14.30 ?  80   SER   B HG   1 
ATOM   5174 N  N    . CYS   B 1 81  ? 41.775 -12.788 2.645   1.00 10.13 ?  81   CYS   B N    1 
ATOM   5175 C  CA   . CYS   B 1 81  ? 42.320 -11.477 2.333   1.00 10.50 ?  81   CYS   B CA   1 
ATOM   5176 C  C    . CYS   B 1 81  ? 43.093 -11.564 1.025   1.00 9.96  ?  81   CYS   B C    1 
ATOM   5177 O  O    . CYS   B 1 81  ? 43.607 -12.627 0.657   1.00 10.63 ?  81   CYS   B O    1 
ATOM   5178 C  CB   . CYS   B 1 81  ? 43.207 -10.927 3.456   1.00 11.28 ?  81   CYS   B CB   1 
ATOM   5179 S  SG   . CYS   B 1 81  ? 44.730 -11.864 3.698   1.00 11.41 ?  81   CYS   B SG   1 
ATOM   5180 H  H    . CYS   B 1 81  ? 42.294 -13.441 2.420   1.00 12.17 ?  81   CYS   B H    1 
ATOM   5181 H  HA   . CYS   B 1 81  ? 41.588 -10.853 2.206   1.00 12.62 ?  81   CYS   B HA   1 
ATOM   5182 H  HB2  . CYS   B 1 81  ? 43.458 -10.012 3.246   1.00 13.56 ?  81   CYS   B HB2  1 
ATOM   5183 H  HB3  . CYS   B 1 81  ? 42.707 -10.941 4.291   1.00 13.56 ?  81   CYS   B HB3  1 
ATOM   5184 H  HG   . CYS   B 1 81  ? 45.356 -11.373 4.601   1.00 13.71 ?  81   CYS   B HG   1 
ATOM   5185 N  N    . VAL   B 1 82  ? 43.202 -10.422 0.351   1.00 10.26 ?  82   VAL   B N    1 
ATOM   5186 C  CA   . VAL   B 1 82  ? 43.965 -10.298 -0.887  1.00 10.18 ?  82   VAL   B CA   1 
ATOM   5187 C  C    . VAL   B 1 82  ? 45.305 -9.658  -0.565  1.00 10.66 ?  82   VAL   B C    1 
ATOM   5188 O  O    . VAL   B 1 82  ? 45.358 -8.541  -0.034  1.00 11.51 ?  82   VAL   B O    1 
ATOM   5189 C  CB   . VAL   B 1 82  ? 43.217 -9.456  -1.932  1.00 11.58 ?  82   VAL   B CB   1 
ATOM   5190 C  CG1  . VAL   B 1 82  ? 44.062 -9.313  -3.190  1.00 12.68 ?  82   VAL   B CG1  1 
ATOM   5191 C  CG2  . VAL   B 1 82  ? 41.863 -10.063 -2.241  1.00 12.51 ?  82   VAL   B CG2  1 
ATOM   5192 H  H    . VAL   B 1 82  ? 42.826 -9.682  0.596   1.00 12.33 ?  82   VAL   B H    1 
ATOM   5193 H  HA   . VAL   B 1 82  ? 44.124 -11.175 -1.256  1.00 12.24 ?  82   VAL   B HA   1 
ATOM   5194 H  HB   . VAL   B 1 82  ? 43.067 -8.569  -1.578  1.00 13.92 ?  82   VAL   B HB   1 
ATOM   5195 H  HG11 . VAL   B 1 82  ? 43.501 -8.998  -3.917  1.00 15.24 ?  82   VAL   B HG11 1 
ATOM   5196 H  HG12 . VAL   B 1 82  ? 44.775 -8.672  -3.026  1.00 15.24 ?  82   VAL   B HG12 1 
ATOM   5197 H  HG13 . VAL   B 1 82  ? 44.442 -10.176 -3.420  1.00 15.24 ?  82   VAL   B HG13 1 
ATOM   5198 H  HG21 . VAL   B 1 82  ? 41.430 -9.546  -2.938  1.00 15.04 ?  82   VAL   B HG21 1 
ATOM   5199 H  HG22 . VAL   B 1 82  ? 41.984 -10.980 -2.540  1.00 15.04 ?  82   VAL   B HG22 1 
ATOM   5200 H  HG23 . VAL   B 1 82  ? 41.319 -10.051 -1.436  1.00 15.04 ?  82   VAL   B HG23 1 
ATOM   5201 N  N    . LEU   B 1 83  ? 46.381 -10.348 -0.925  1.00 10.29 ?  83   LEU   B N    1 
ATOM   5202 C  CA   . LEU   B 1 83  ? 47.737 -9.832  -0.807  1.00 10.35 ?  83   LEU   B CA   1 
ATOM   5203 C  C    . LEU   B 1 83  ? 48.438 -9.979  -2.156  1.00 10.37 ?  83   LEU   B C    1 
ATOM   5204 O  O    . LEU   B 1 83  ? 47.833 -10.393 -3.149  1.00 10.23 ?  83   LEU   B O    1 
ATOM   5205 C  CB   . LEU   B 1 83  ? 48.487 -10.514 0.343   1.00 10.72 ?  83   LEU   B CB   1 
ATOM   5206 C  CG   . LEU   B 1 83  ? 47.981 -10.147 1.747   1.00 12.12 ?  83   LEU   B CG   1 
ATOM   5207 C  CD1  . LEU   B 1 83  ? 48.607 -11.017 2.814   1.00 12.47 ?  83   LEU   B CD1  1 
ATOM   5208 C  CD2  . LEU   B 1 83  ? 48.182 -8.667  2.074   1.00 13.15 ?  83   LEU   B CD2  1 
ATOM   5209 H  H    . LEU   B 1 83  ? 46.344 -11.151 -1.239  1.00 12.37 ?  83   LEU   B H    1 
ATOM   5210 H  HA   . LEU   B 1 83  ? 47.686 -8.886  -0.609  1.00 12.44 ?  83   LEU   B HA   1 
ATOM   5211 H  HB2  . LEU   B 1 83  ? 48.403 -11.471 0.244   1.00 12.89 ?  83   LEU   B HB2  1 
ATOM   5212 H  HB3  . LEU   B 1 83  ? 49.422 -10.258 0.292   1.00 12.89 ?  83   LEU   B HB3  1 
ATOM   5213 H  HG   . LEU   B 1 83  ? 47.030 -10.311 1.771   1.00 14.57 ?  83   LEU   B HG   1 
ATOM   5214 H  HD11 . LEU   B 1 83  ? 48.253 -10.759 3.681   1.00 14.99 ?  83   LEU   B HD11 1 
ATOM   5215 H  HD12 . LEU   B 1 83  ? 48.385 -11.945 2.633   1.00 14.99 ?  83   LEU   B HD12 1 
ATOM   5216 H  HD13 . LEU   B 1 83  ? 49.568 -10.899 2.802   1.00 14.99 ?  83   LEU   B HD13 1 
ATOM   5217 H  HD21 . LEU   B 1 83  ? 47.969 -8.521  3.010   1.00 15.80 ?  83   LEU   B HD21 1 
ATOM   5218 H  HD22 . LEU   B 1 83  ? 49.102 -8.425  1.900   1.00 15.80 ?  83   LEU   B HD22 1 
ATOM   5219 H  HD23 . LEU   B 1 83  ? 47.587 -8.139  1.516   1.00 15.80 ?  83   LEU   B HD23 1 
ATOM   5220 N  N    . SER   B 1 84  ? 49.715 -9.613  -2.209  1.00 11.27 ?  84   SER   B N    1 
ATOM   5221 C  CA   . SER   B 1 84  ? 50.444 -9.728  -3.461  1.00 11.33 ?  84   SER   B CA   1 
ATOM   5222 C  C    . SER   B 1 84  ? 50.602 -11.185 -3.876  1.00 10.74 ?  84   SER   B C    1 
ATOM   5223 O  O    . SER   B 1 84  ? 50.711 -12.084 -3.042  1.00 10.68 ?  84   SER   B O    1 
ATOM   5224 C  CB   . SER   B 1 84  ? 51.836 -9.118  -3.318  1.00 13.06 ?  84   SER   B CB   1 
ATOM   5225 O  OG   . SER   B 1 84  ? 52.583 -9.336  -4.502  1.00 14.42 ?  84   SER   B OG   1 
ATOM   5226 H  H    . SER   B 1 84  ? 50.169 -9.287  -1.551  1.00 13.55 ?  84   SER   B H    1 
ATOM   5227 H  HA   . SER   B 1 84  ? 49.970 -9.252  -4.163  1.00 13.61 ?  84   SER   B HA   1 
ATOM   5228 H  HB2  . SER   B 1 84  ? 51.752 -8.157  -3.161  1.00 15.69 ?  84   SER   B HB2  1 
ATOM   5229 H  HB3  . SER   B 1 84  ? 52.296 -9.531  -2.573  1.00 15.69 ?  84   SER   B HB3  1 
ATOM   5230 H  HG   . SER   B 1 84  ? 53.352 -8.986  -4.425  1.00 17.32 ?  84   SER   B HG   1 
ATOM   5231 N  N    . GLY   B 1 85  ? 50.667 -11.405 -5.182  1.00 11.75 ?  85   GLY   B N    1 
ATOM   5232 C  CA   . GLY   B 1 85  ? 51.019 -12.698 -5.716  1.00 12.45 ?  85   GLY   B CA   1 
ATOM   5233 C  C    . GLY   B 1 85  ? 52.486 -12.891 -6.016  1.00 11.57 ?  85   GLY   B C    1 
ATOM   5234 O  O    . GLY   B 1 85  ? 52.863 -13.970 -6.476  1.00 12.19 ?  85   GLY   B O    1 
ATOM   5235 H  H    . GLY   B 1 85  ? 50.508 -10.817 -5.784  1.00 14.12 ?  85   GLY   B H    1 
ATOM   5236 H  HA2  . GLY   B 1 85  ? 50.759 -13.385 -5.080  1.00 14.97 ?  85   GLY   B HA2  1 
ATOM   5237 H  HA3  . GLY   B 1 85  ? 50.528 -12.849 -6.534  1.00 14.97 ?  85   GLY   B HA3  1 
ATOM   5238 N  N    . HIS   B 1 86  ? 53.334 -11.893 -5.786  1.00 11.66 ?  86   HIS   B N    1 
ATOM   5239 C  CA   . HIS   B 1 86  ? 54.795 -12.063 -5.867  1.00 11.75 ?  86   HIS   B CA   1 
ATOM   5240 C  C    . HIS   B 1 86  ? 55.172 -12.567 -7.257  1.00 12.01 ?  86   HIS   B C    1 
ATOM   5241 O  O    . HIS   B 1 86  ? 54.788 -11.943 -8.260  1.00 12.61 ?  86   HIS   B O    1 
ATOM   5242 C  CB   . HIS   B 1 86  ? 55.291 -12.906 -4.695  1.00 12.46 ?  86   HIS   B CB   1 
ATOM   5243 C  CG   . HIS   B 1 86  ? 54.981 -12.298 -3.372  1.00 12.20 ?  86   HIS   B CG   1 
ATOM   5244 N  ND1  . HIS   B 1 86  ? 55.810 -11.382 -2.760  1.00 13.36 ?  86   HIS   B ND1  1 
ATOM   5245 C  CD2  . HIS   B 1 86  ? 53.904 -12.439 -2.565  1.00 12.41 ?  86   HIS   B CD2  1 
ATOM   5246 C  CE1  . HIS   B 1 86  ? 55.255 -10.995 -1.625  1.00 13.18 ?  86   HIS   B CE1  1 
ATOM   5247 N  NE2  . HIS   B 1 86  ? 54.096 -11.615 -1.486  1.00 12.45 ?  86   HIS   B NE2  1 
ATOM   5248 H  H    . HIS   B 1 86  ? 53.099 -11.096 -5.579  1.00 14.02 ?  86   HIS   B H    1 
ATOM   5249 H  HA   . HIS   B 1 86  ? 55.209 -11.194 -5.768  1.00 14.12 ?  86   HIS   B HA   1 
ATOM   5250 H  HB2  . HIS   B 1 86  ? 54.873 -13.781 -4.732  1.00 14.97 ?  86   HIS   B HB2  1 
ATOM   5251 H  HB3  . HIS   B 1 86  ? 56.258 -13.004 -4.758  1.00 14.97 ?  86   HIS   B HB3  1 
ATOM   5252 H  HD2  . HIS   B 1 86  ? 53.164 -12.985 -2.721  1.00 14.92 ?  86   HIS   B HD2  1 
ATOM   5253 H  HE1  . HIS   B 1 86  ? 55.623 -10.395 -1.020  1.00 15.84 ?  86   HIS   B HE1  1 
ATOM   5254 H  HE2  . HIS   B 1 86  ? 53.558 -11.534 -0.820  1.00 14.96 ?  86   HIS   B HE2  1 
ATOM   5255 N  N    . ASN   B 1 87  ? 55.941 -13.648 -7.367  1.00 12.32 ?  87   ASN   B N    1 
ATOM   5256 C  CA   . ASN   B 1 87  ? 56.341 -14.219 -8.642  1.00 13.13 ?  87   ASN   B CA   1 
ATOM   5257 C  C    . ASN   B 1 87  ? 55.365 -15.265 -9.146  1.00 12.74 ?  87   ASN   B C    1 
ATOM   5258 O  O    . ASN   B 1 87  ? 55.684 -15.977 -10.103 1.00 14.38 ?  87   ASN   B O    1 
ATOM   5259 C  CB   . ASN   B 1 87  ? 57.737 -14.841 -8.526  1.00 15.04 ?  87   ASN   B CB   1 
ATOM   5260 C  CG   . ASN   B 1 87  ? 57.800 -15.951 -7.486  1.00 15.90 ?  87   ASN   B CG   1 
ATOM   5261 O  OD1  . ASN   B 1 87  ? 57.149 -15.877 -6.438  1.00 14.93 ?  87   ASN   B OD1  1 
ATOM   5262 N  ND2  . ASN   B 1 87  ? 58.560 -17.005 -7.786  1.00 18.30 ?  87   ASN   B ND2  1 
ATOM   5263 H  H    . ASN   B 1 87  ? 56.248 -14.090 -6.694  1.00 14.80 ?  87   ASN   B H    1 
ATOM   5264 H  HA   . ASN   B 1 87  ? 56.382 -13.514 -9.303  1.00 15.78 ?  87   ASN   B HA   1 
ATOM   5265 H  HB2  . ASN   B 1 87  ? 57.988 -15.219 -9.385  1.00 18.07 ?  87   ASN   B HB2  1 
ATOM   5266 H  HB3  . ASN   B 1 87  ? 58.367 -14.149 -8.271  1.00 18.07 ?  87   ASN   B HB3  1 
ATOM   5267 H  HD21 . ASN   B 1 87  ? 58.631 -17.653 -7.230  1.00 21.98 ?  87   ASN   B HD21 1 
ATOM   5268 H  HD22 . ASN   B 1 87  ? 58.991 -17.025 -8.532  1.00 21.98 ?  87   ASN   B HD22 1 
ATOM   5269 N  N    . LEU   B 1 88  ? 54.183 -15.368 -8.535  1.00 11.82 ?  88   LEU   B N    1 
ATOM   5270 C  CA   . LEU   B 1 88  ? 53.205 -16.397 -8.864  1.00 12.12 ?  88   LEU   B CA   1 
ATOM   5271 C  C    . LEU   B 1 88  ? 51.973 -15.880 -9.587  1.00 12.01 ?  88   LEU   B C    1 
ATOM   5272 O  O    . LEU   B 1 88  ? 51.375 -16.627 -10.375 1.00 13.50 ?  88   LEU   B O    1 
ATOM   5273 C  CB   . LEU   B 1 88  ? 52.732 -17.080 -7.577  1.00 13.07 ?  88   LEU   B CB   1 
ATOM   5274 C  CG   . LEU   B 1 88  ? 53.859 -17.731 -6.784  1.00 15.38 ?  88   LEU   B CG   1 
ATOM   5275 C  CD1  . LEU   B 1 88  ? 53.369 -18.130 -5.403  1.00 16.85 ?  88   LEU   B CD1  1 
ATOM   5276 C  CD2  . LEU   B 1 88  ? 54.399 -18.928 -7.541  1.00 18.66 ?  88   LEU   B CD2  1 
ATOM   5277 H  H    . LEU   B 1 88  ? 53.919 -14.839 -7.904  1.00 14.21 ?  88   LEU   B H    1 
ATOM   5278 H  HA   . LEU   B 1 88  ? 53.621 -17.064 -9.423  1.00 14.56 ?  88   LEU   B HA   1 
ATOM   5279 H  HB2  . LEU   B 1 88  ? 52.308 -16.422 -7.004  1.00 15.71 ?  88   LEU   B HB2  1 
ATOM   5280 H  HB3  . LEU   B 1 88  ? 52.092 -17.774 -7.806  1.00 15.71 ?  88   LEU   B HB3  1 
ATOM   5281 H  HG   . LEU   B 1 88  ? 54.579 -17.093 -6.671  1.00 18.48 ?  88   LEU   B HG   1 
ATOM   5282 H  HD11 . LEU   B 1 88  ? 54.055 -18.656 -4.964  1.00 20.25 ?  88   LEU   B HD11 1 
ATOM   5283 H  HD12 . LEU   B 1 88  ? 53.184 -17.329 -4.889  1.00 20.25 ?  88   LEU   B HD12 1 
ATOM   5284 H  HD13 . LEU   B 1 88  ? 52.560 -18.656 -5.499  1.00 20.25 ?  88   LEU   B HD13 1 
ATOM   5285 H  HD21 . LEU   B 1 88  ? 55.023 -19.403 -6.972  1.00 22.41 ?  88   LEU   B HD21 1 
ATOM   5286 H  HD22 . LEU   B 1 88  ? 53.661 -19.507 -7.783  1.00 22.41 ?  88   LEU   B HD22 1 
ATOM   5287 H  HD23 . LEU   B 1 88  ? 54.852 -18.616 -8.340  1.00 22.41 ?  88   LEU   B HD23 1 
ATOM   5288 N  N    . ALA   B 1 89  ? 51.561 -14.647 -9.313  1.00 11.31 ?  89   ALA   B N    1 
ATOM   5289 C  CA   . ALA   B 1 89  ? 50.266 -14.152 -9.757  1.00 10.78 ?  89   ALA   B CA   1 
ATOM   5290 C  C    . ALA   B 1 89  ? 50.244 -12.663 -9.474  1.00 11.24 ?  89   ALA   B C    1 
ATOM   5291 O  O    . ALA   B 1 89  ? 51.078 -12.150 -8.727  1.00 11.94 ?  89   ALA   B O    1 
ATOM   5292 C  CB   . ALA   B 1 89  ? 49.141 -14.820 -8.980  1.00 11.06 ?  89   ALA   B CB   1 
ATOM   5293 H  H    . ALA   B 1 89  ? 52.014 -14.069 -8.865  1.00 13.60 ?  89   ALA   B H    1 
ATOM   5294 H  HA   . ALA   B 1 89  ? 50.142 -14.303 -10.708 1.00 12.96 ?  89   ALA   B HA   1 
ATOM   5295 H  HB1  . ALA   B 1 89  ? 48.290 -14.481 -9.298  1.00 13.29 ?  89   ALA   B HB1  1 
ATOM   5296 H  HB2  . ALA   B 1 89  ? 49.188 -15.779 -9.123  1.00 13.29 ?  89   ALA   B HB2  1 
ATOM   5297 H  HB3  . ALA   B 1 89  ? 49.247 -14.620 -8.038  1.00 13.29 ?  89   ALA   B HB3  1 
ATOM   5298 N  N    . LYS   B 1 90  ? 49.259 -11.968 -10.038 1.00 12.13 ?  90   LYS   B N    1 
ATOM   5299 C  CA   . LYS   B 1 90  ? 49.076 -10.581 -9.635  1.00 12.17 ?  90   LYS   B CA   1 
ATOM   5300 C  C    . LYS   B 1 90  ? 48.749 -10.508 -8.148  1.00 11.97 ?  90   LYS   B C    1 
ATOM   5301 O  O    . LYS   B 1 90  ? 49.387 -9.758  -7.393  1.00 12.83 ?  90   LYS   B O    1 
ATOM   5302 C  CB   . LYS   B 1 90  ? 48.001 -9.919  -10.491 1.00 13.38 ?  90   LYS   B CB   1 
ATOM   5303 C  CG   . LYS   B 1 90  ? 47.691 -8.483  -10.098 1.00 14.00 ?  90   LYS   B CG   1 
ATOM   5304 C  CD   . LYS   B 1 90  ? 48.899 -7.583  -10.173 1.00 16.48 ?  90   LYS   B CD   1 
ATOM   5305 C  CE   . LYS   B 1 90  ? 48.452 -6.167  -9.907  1.00 18.59 ?  90   LYS   B CE   1 
ATOM   5306 N  NZ   . LYS   B 1 90  ? 49.592 -5.232  -9.785  1.00 18.37 ?  90   LYS   B NZ   1 
ATOM   5307 H  H    . LYS   B 1 90  ? 48.711 -12.265 -10.630 1.00 14.58 ?  90   LYS   B H    1 
ATOM   5308 H  HA   . LYS   B 1 90  ? 49.906 -10.106 -9.776  1.00 14.63 ?  90   LYS   B HA   1 
ATOM   5309 H  HB2  . LYS   B 1 90  ? 48.304 -9.909  -11.416 1.00 16.08 ?  90   LYS   B HB2  1 
ATOM   5310 H  HB3  . LYS   B 1 90  ? 47.182 -10.429 -10.423 1.00 16.08 ?  90   LYS   B HB3  1 
ATOM   5311 H  HG2  . LYS   B 1 90  ? 47.018 -8.128  -10.701 1.00 16.83 ?  90   LYS   B HG2  1 
ATOM   5312 H  HG3  . LYS   B 1 90  ? 47.356 -8.464  -9.186  1.00 16.83 ?  90   LYS   B HG3  1 
ATOM   5313 H  HD2  . LYS   B 1 90  ? 49.545 -7.838  -9.494  1.00 19.80 ?  90   LYS   B HD2  1 
ATOM   5314 H  HD3  . LYS   B 1 90  ? 49.292 -7.629  -11.058 1.00 19.80 ?  90   LYS   B HD3  1 
ATOM   5315 H  HE2  . LYS   B 1 90  ? 47.896 -5.861  -10.643 1.00 22.33 ?  90   LYS   B HE2  1 
ATOM   5316 H  HE3  . LYS   B 1 90  ? 47.952 -6.135  -9.078  1.00 22.33 ?  90   LYS   B HE3  1 
ATOM   5317 H  HZ1  . LYS   B 1 90  ? 49.299 -4.404  -9.631  1.00 22.07 ?  90   LYS   B HZ1  1 
ATOM   5318 H  HZ2  . LYS   B 1 90  ? 50.120 -5.479  -9.112  1.00 22.07 ?  90   LYS   B HZ2  1 
ATOM   5319 H  HZ3  . LYS   B 1 90  ? 50.070 -5.230  -10.539 1.00 22.07 ?  90   LYS   B HZ3  1 
ATOM   5320 N  N    . HIS   B 1 91  ? 47.783 -11.315 -7.707  1.00 10.56 ?  91   HIS   B N    1 
ATOM   5321 C  CA   . HIS   B 1 91  ? 47.318 -11.342 -6.334  1.00 10.29 ?  91   HIS   B CA   1 
ATOM   5322 C  C    . HIS   B 1 91  ? 47.315 -12.769 -5.816  1.00 9.99  ?  91   HIS   B C    1 
ATOM   5323 O  O    . HIS   B 1 91  ? 47.089 -13.721 -6.569  1.00 10.39 ?  91   HIS   B O    1 
ATOM   5324 C  CB   . HIS   B 1 91  ? 45.868 -10.861 -6.215  1.00 11.82 ?  91   HIS   B CB   1 
ATOM   5325 C  CG   . HIS   B 1 91  ? 45.657 -9.455  -6.654  1.00 15.53 ?  91   HIS   B CG   1 
ATOM   5326 N  ND1  . HIS   B 1 91  ? 46.261 -8.380  -6.036  1.00 18.34 ?  91   HIS   B ND1  1 
ATOM   5327 C  CD2  . HIS   B 1 91  ? 44.882 -8.940  -7.634  1.00 17.76 ?  91   HIS   B CD2  1 
ATOM   5328 C  CE1  . HIS   B 1 91  ? 45.881 -7.262  -6.630  1.00 19.13 ?  91   HIS   B CE1  1 
ATOM   5329 N  NE2  . HIS   B 1 91  ? 45.040 -7.575  -7.600  1.00 19.02 ?  91   HIS   B NE2  1 
ATOM   5330 H  H    . HIS   B 1 91  ? 47.363 -11.874 -8.211  1.00 12.70 ?  91   HIS   B H    1 
ATOM   5331 H  HA   . HIS   B 1 91  ? 47.891 -10.787 -5.771  1.00 12.38 ?  91   HIS   B HA   1 
ATOM   5332 H  HB2  . HIS   B 1 91  ? 45.304 -11.425 -6.765  1.00 14.21 ?  91   HIS   B HB2  1 
ATOM   5333 H  HB3  . HIS   B 1 91  ? 45.589 -10.924 -5.287  1.00 14.21 ?  91   HIS   B HB3  1 
ATOM   5334 H  HD1  . HIS   B 1 91  ? 46.805 -8.426  -5.371  1.00 22.03 ?  91   HIS   B HD1  1 
ATOM   5335 H  HD2  . HIS   B 1 91  ? 44.349 -9.411  -8.227  1.00 21.33 ?  91   HIS   B HD2  1 
ATOM   5336 H  HE1  . HIS   B 1 91  ? 46.155 -6.399  -6.398  1.00 22.98 ?  91   HIS   B HE1  1 
ATOM   5337 N  N    . CYS   B 1 92  ? 47.504 -12.901 -4.511  1.00 9.73  ?  92   CYS   B N    1 
ATOM   5338 C  CA   . CYS   B 1 92  ? 47.204 -14.135 -3.799  1.00 9.52  ?  92   CYS   B CA   1 
ATOM   5339 C  C    . CYS   B 1 92  ? 45.983 -13.899 -2.918  1.00 9.19  ?  92   CYS   B C    1 
ATOM   5340 O  O    . CYS   B 1 92  ? 45.984 -12.996 -2.070  1.00 10.03 ?  92   CYS   B O    1 
ATOM   5341 C  CB   . CYS   B 1 92  ? 48.383 -14.594 -2.947  1.00 9.82  ?  92   CYS   B CB   1 
ATOM   5342 S  SG   . CYS   B 1 92  ? 48.024 -16.132 -2.049  1.00 10.01 ?  92   CYS   B SG   1 
ATOM   5343 H  H    . CYS   B 1 92  ? 47.820 -12.276 -4.003  1.00 11.69 ?  92   CYS   B H    1 
ATOM   5344 H  HA   . CYS   B 1 92  ? 47.004 -14.831 -4.446  1.00 11.44 ?  92   CYS   B HA   1 
ATOM   5345 H  HB2  . CYS   B 1 92  ? 49.148 -14.744 -3.520  1.00 11.81 ?  92   CYS   B HB2  1 
ATOM   5346 H  HB3  . CYS   B 1 92  ? 48.583 -13.899 -2.298  1.00 11.81 ?  92   CYS   B HB3  1 
ATOM   5347 H  HG   . CYS   B 1 92  ? 48.996 -16.443 -1.416  1.00 12.03 ?  92   CYS   B HG   1 
ATOM   5348 N  N    . LEU   B 1 93  ? 44.944 -14.701 -3.132  1.00 9.13  ?  93   LEU   B N    1 
ATOM   5349 C  CA   . LEU   B 1 93  ? 43.768 -14.711 -2.270  1.00 9.21  ?  93   LEU   B CA   1 
ATOM   5350 C  C    . LEU   B 1 93  ? 43.991 -15.778 -1.205  1.00 8.90  ?  93   LEU   B C    1 
ATOM   5351 O  O    . LEU   B 1 93  ? 43.951 -16.980 -1.497  1.00 9.49  ?  93   LEU   B O    1 
ATOM   5352 C  CB   . LEU   B 1 93  ? 42.509 -15.008 -3.075  1.00 9.75  ?  93   LEU   B CB   1 
ATOM   5353 C  CG   . LEU   B 1 93  ? 41.213 -15.025 -2.264  1.00 10.31 ?  93   LEU   B CG   1 
ATOM   5354 C  CD1  . LEU   B 1 93  ? 40.854 -13.633 -1.782  1.00 10.66 ?  93   LEU   B CD1  1 
ATOM   5355 C  CD2  . LEU   B 1 93  ? 40.085 -15.615 -3.094  1.00 10.52 ?  93   LEU   B CD2  1 
ATOM   5356 H  H    . LEU   B 1 93  ? 44.902 -15.273 -3.784  1.00 10.98 ?  93   LEU   B H    1 
ATOM   5357 H  HA   . LEU   B 1 93  ? 43.676 -13.849 -1.841  1.00 11.07 ?  93   LEU   B HA   1 
ATOM   5358 H  HB2  . LEU   B 1 93  ? 42.414 -14.320 -3.757  1.00 11.72 ?  93   LEU   B HB2  1 
ATOM   5359 H  HB3  . LEU   B 1 93  ? 42.604 -15.871 -3.495  1.00 11.72 ?  93   LEU   B HB3  1 
ATOM   5360 H  HG   . LEU   B 1 93  ? 41.331 -15.586 -1.486  1.00 12.39 ?  93   LEU   B HG   1 
ATOM   5361 H  HD11 . LEU   B 1 93  ? 39.999 -13.668 -1.326  1.00 12.82 ?  93   LEU   B HD11 1 
ATOM   5362 H  HD12 . LEU   B 1 93  ? 41.541 -13.319 -1.180  1.00 12.82 ?  93   LEU   B HD12 1 
ATOM   5363 H  HD13 . LEU   B 1 93  ? 40.790 -13.040 -2.552  1.00 12.82 ?  93   LEU   B HD13 1 
ATOM   5364 H  HD21 . LEU   B 1 93  ? 39.271 -15.611 -2.567  1.00 12.65 ?  93   LEU   B HD21 1 
ATOM   5365 H  HD22 . LEU   B 1 93  ? 39.965 -15.078 -3.893  1.00 12.65 ?  93   LEU   B HD22 1 
ATOM   5366 H  HD23 . LEU   B 1 93  ? 40.317 -16.525 -3.338  1.00 12.65 ?  93   LEU   B HD23 1 
ATOM   5367 N  N    . HIS   B 1 94  ? 44.270 -15.340 0.017   1.00 9.06  ?  94   HIS   B N    1 
ATOM   5368 C  CA   . HIS   B 1 94  ? 44.489 -16.244 1.137   1.00 9.11  ?  94   HIS   B CA   1 
ATOM   5369 C  C    . HIS   B 1 94  ? 43.131 -16.599 1.715   1.00 9.31  ?  94   HIS   B C    1 
ATOM   5370 O  O    . HIS   B 1 94  ? 42.461 -15.728 2.268   1.00 10.58 ?  94   HIS   B O    1 
ATOM   5371 C  CB   . HIS   B 1 94  ? 45.359 -15.569 2.191   1.00 9.40  ?  94   HIS   B CB   1 
ATOM   5372 C  CG   . HIS   B 1 94  ? 46.739 -15.272 1.721   1.00 9.61  ?  94   HIS   B CG   1 
ATOM   5373 N  ND1  . HIS   B 1 94  ? 47.765 -16.188 1.813   1.00 9.65  ?  94   HIS   B ND1  1 
ATOM   5374 C  CD2  . HIS   B 1 94  ? 47.249 -14.169 1.121   1.00 9.70  ?  94   HIS   B CD2  1 
ATOM   5375 C  CE1  . HIS   B 1 94  ? 48.856 -15.642 1.304   1.00 9.87  ?  94   HIS   B CE1  1 
ATOM   5376 N  NE2  . HIS   B 1 94  ? 48.571 -14.423 0.875   1.00 9.83  ?  94   HIS   B NE2  1 
ATOM   5377 H  H    . HIS   B 1 94  ? 44.350 -14.503 0.221   1.00 10.89 ?  94   HIS   B H    1 
ATOM   5378 H  HA   . HIS   B 1 94  ? 44.926 -17.052 0.828   1.00 10.96 ?  94   HIS   B HA   1 
ATOM   5379 H  HB2  . HIS   B 1 94  ? 44.948 -14.732 2.449   1.00 11.30 ?  94   HIS   B HB2  1 
ATOM   5380 H  HB3  . HIS   B 1 94  ? 45.429 -16.157 2.959   1.00 11.30 ?  94   HIS   B HB3  1 
ATOM   5381 H  HD2  . HIS   B 1 94  ? 46.795 -13.389 0.918   1.00 11.66 ?  94   HIS   B HD2  1 
ATOM   5382 H  HE1  . HIS   B 1 94  ? 49.686 -16.062 1.256   1.00 11.87 ?  94   HIS   B HE1  1 
ATOM   5383 H  HE2  . HIS   B 1 94  ? 49.131 -13.887 0.510   1.00 11.82 ?  94   HIS   B HE2  1 
ATOM   5384 N  N    . VAL   B 1 95  ? 42.698 -17.851 1.560   1.00 9.20  ?  95   VAL   B N    1 
ATOM   5385 C  CA   . VAL   B 1 95  ? 41.368 -18.282 1.991   1.00 9.39  ?  95   VAL   B CA   1 
ATOM   5386 C  C    . VAL   B 1 95  ? 41.534 -19.321 3.085   1.00 9.89  ?  95   VAL   B C    1 
ATOM   5387 O  O    . VAL   B 1 95  ? 42.308 -20.270 2.926   1.00 10.49 ?  95   VAL   B O    1 
ATOM   5388 C  CB   . VAL   B 1 95  ? 40.546 -18.885 0.835   1.00 9.72  ?  95   VAL   B CB   1 
ATOM   5389 C  CG1  . VAL   B 1 95  ? 39.167 -19.319 1.323   1.00 10.77 ?  95   VAL   B CG1  1 
ATOM   5390 C  CG2  . VAL   B 1 95  ? 40.431 -17.910 -0.307  1.00 9.79  ?  95   VAL   B CG2  1 
ATOM   5391 H  H    . VAL   B 1 95  ? 43.159 -18.482 1.198   1.00 11.06 ?  95   VAL   B H    1 
ATOM   5392 H  HA   . VAL   B 1 95  ? 40.879 -17.527 2.356   1.00 11.29 ?  95   VAL   B HA   1 
ATOM   5393 H  HB   . VAL   B 1 95  ? 40.996 -19.670 0.505   1.00 11.69 ?  95   VAL   B HB   1 
ATOM   5394 H  HG11 . VAL   B 1 95  ? 38.602 -19.511 0.550   1.00 12.95 ?  95   VAL   B HG11 1 
ATOM   5395 H  HG12 . VAL   B 1 95  ? 39.252 -20.115 1.867   1.00 12.95 ?  95   VAL   B HG12 1 
ATOM   5396 H  HG13 . VAL   B 1 95  ? 38.766 -18.602 1.841   1.00 12.95 ?  95   VAL   B HG13 1 
ATOM   5397 H  HG21 . VAL   B 1 95  ? 39.852 -18.297 -0.986  1.00 11.76 ?  95   VAL   B HG21 1 
ATOM   5398 H  HG22 . VAL   B 1 95  ? 40.045 -17.085 0.023   1.00 11.76 ?  95   VAL   B HG22 1 
ATOM   5399 H  HG23 . VAL   B 1 95  ? 41.310 -17.753 -0.668  1.00 11.76 ?  95   VAL   B HG23 1 
ATOM   5400 N  N    . VAL   B 1 96  ? 40.801 -19.152 4.181   1.00 10.32 ?  96   VAL   B N    1 
ATOM   5401 C  CA   . VAL   B 1 96  ? 40.885 -20.064 5.321   1.00 10.61 ?  96   VAL   B CA   1 
ATOM   5402 C  C    . VAL   B 1 96  ? 39.698 -21.022 5.272   1.00 10.96 ?  96   VAL   B C    1 
ATOM   5403 O  O    . VAL   B 1 96  ? 38.578 -20.666 5.645   1.00 11.48 ?  96   VAL   B O    1 
ATOM   5404 C  CB   . VAL   B 1 96  ? 40.939 -19.317 6.658   1.00 11.43 ?  96   VAL   B CB   1 
ATOM   5405 C  CG1  . VAL   B 1 96  ? 41.107 -20.320 7.793   1.00 12.10 ?  96   VAL   B CG1  1 
ATOM   5406 C  CG2  . VAL   B 1 96  ? 42.054 -18.285 6.672   1.00 11.84 ?  96   VAL   B CG2  1 
ATOM   5407 H  H    . VAL   B 1 96  ? 40.241 -18.510 4.297   1.00 12.41 ?  96   VAL   B H    1 
ATOM   5408 H  HA   . VAL   B 1 96  ? 41.697 -20.592 5.246   1.00 12.76 ?  96   VAL   B HA   1 
ATOM   5409 H  HB   . VAL   B 1 96  ? 40.098 -18.857 6.796   1.00 13.74 ?  96   VAL   B HB   1 
ATOM   5410 H  HG11 . VAL   B 1 96  ? 41.310 -19.838 8.613   1.00 14.54 ?  96   VAL   B HG11 1 
ATOM   5411 H  HG12 . VAL   B 1 96  ? 40.285 -20.822 7.906   1.00 14.54 ?  96   VAL   B HG12 1 
ATOM   5412 H  HG13 . VAL   B 1 96  ? 41.838 -20.923 7.581   1.00 14.54 ?  96   VAL   B HG13 1 
ATOM   5413 H  HG21 . VAL   B 1 96  ? 42.096 -17.875 7.553   1.00 14.24 ?  96   VAL   B HG21 1 
ATOM   5414 H  HG22 . VAL   B 1 96  ? 42.894 -18.718 6.468   1.00 14.24 ?  96   VAL   B HG22 1 
ATOM   5415 H  HG23 . VAL   B 1 96  ? 41.861 -17.604 6.005   1.00 14.24 ?  96   VAL   B HG23 1 
ATOM   5416 N  N    . GLY   B 1 97  ? 39.941 -22.252 4.833   1.00 11.02 ?  97   GLY   B N    1 
ATOM   5417 C  CA   . GLY   B 1 97  ? 38.965 -23.307 4.984   1.00 11.68 ?  97   GLY   B CA   1 
ATOM   5418 C  C    . GLY   B 1 97  ? 39.090 -23.925 6.359   1.00 12.65 ?  97   GLY   B C    1 
ATOM   5419 O  O    . GLY   B 1 97  ? 40.132 -23.806 7.017   1.00 13.23 ?  97   GLY   B O    1 
ATOM   5420 H  H    . GLY   B 1 97  ? 40.670 -22.497 4.442   1.00 13.25 ?  97   GLY   B H    1 
ATOM   5421 H  HA2  . GLY   B 1 97  ? 38.071 -22.941 4.867   1.00 14.04 ?  97   GLY   B HA2  1 
ATOM   5422 H  HA3  . GLY   B 1 97  ? 39.109 -23.990 4.306   1.00 14.04 ?  97   GLY   B HA3  1 
ATOM   5423 N  N    . PRO   B 1 98  ? 38.037 -24.602 6.822   1.00 13.87 ?  98   PRO   B N    1 
ATOM   5424 C  CA   . PRO   B 1 98  ? 38.124 -25.301 8.107   1.00 14.87 ?  98   PRO   B CA   1 
ATOM   5425 C  C    . PRO   B 1 98  ? 39.147 -26.426 8.062   1.00 14.48 ?  98   PRO   B C    1 
ATOM   5426 O  O    . PRO   B 1 98  ? 39.258 -27.155 7.079   1.00 14.90 ?  98   PRO   B O    1 
ATOM   5427 C  CB   . PRO   B 1 98  ? 36.702 -25.836 8.312   1.00 15.65 ?  98   PRO   B CB   1 
ATOM   5428 C  CG   . PRO   B 1 98  ? 36.134 -25.962 6.947   1.00 15.15 ?  98   PRO   B CG   1 
ATOM   5429 C  CD   . PRO   B 1 98  ? 36.724 -24.803 6.177   1.00 14.23 ?  98   PRO   B CD   1 
ATOM   5430 H  HA   . PRO   B 1 98  ? 38.346 -24.680 8.810   1.00 17.86 ?  98   PRO   B HA   1 
ATOM   5431 H  HB2  . PRO   B 1 98  ? 36.737 -26.703 8.747   1.00 18.81 ?  98   PRO   B HB2  1 
ATOM   5432 H  HB3  . PRO   B 1 98  ? 36.187 -25.206 8.837   1.00 18.81 ?  98   PRO   B HB3  1 
ATOM   5433 H  HG2  . PRO   B 1 98  ? 36.403 -26.811 6.556   1.00 18.20 ?  98   PRO   B HG2  1 
ATOM   5434 H  HG3  . PRO   B 1 98  ? 35.166 -25.897 6.986   1.00 18.20 ?  98   PRO   B HG3  1 
ATOM   5435 H  HD2  . PRO   B 1 98  ? 36.826 -25.045 5.237   1.00 17.09 ?  98   PRO   B HD2  1 
ATOM   5436 H  HD3  . PRO   B 1 98  ? 36.171 -24.015 6.279   1.00 17.09 ?  98   PRO   B HD3  1 
ATOM   5437 N  N    . ASN   B 1 99  ? 39.903 -26.552 9.143   1.00 15.58 ?  99   ASN   B N    1 
ATOM   5438 C  CA   . ASN   B 1 99  ? 40.888 -27.619 9.299   1.00 16.73 ?  99   ASN   B CA   1 
ATOM   5439 C  C    . ASN   B 1 99  ? 40.271 -28.701 10.181  1.00 19.19 ?  99   ASN   B C    1 
ATOM   5440 O  O    . ASN   B 1 99  ? 40.212 -28.559 11.404  1.00 19.66 ?  99   ASN   B O    1 
ATOM   5441 C  CB   . ASN   B 1 99  ? 42.165 -27.055 9.908   1.00 16.59 ?  99   ASN   B CB   1 
ATOM   5442 C  CG   . ASN   B 1 99  ? 43.298 -28.060 9.921   1.00 17.45 ?  99   ASN   B CG   1 
ATOM   5443 O  OD1  . ASN   B 1 99  ? 43.075 -29.253 10.086  1.00 18.21 ?  99   ASN   B OD1  1 
ATOM   5444 N  ND2  . ASN   B 1 99  ? 44.519 -27.585 9.737   1.00 17.80 ?  99   ASN   B ND2  1 
ATOM   5445 H  H    . ASN   B 1 99  ? 39.863 -26.015 9.809   1.00 18.72 ?  99   ASN   B H    1 
ATOM   5446 H  HA   . ASN   B 1 99  ? 41.090 -28.008 8.434   1.00 20.09 ?  99   ASN   B HA   1 
ATOM   5447 H  HB2  . ASN   B 1 99  ? 42.441 -26.288 9.396   1.00 19.93 ?  99   ASN   B HB2  1 
ATOM   5448 H  HB3  . ASN   B 1 99  ? 41.979 -26.801 10.828  1.00 19.93 ?  99   ASN   B HB3  1 
ATOM   5449 H  HD21 . ASN   B 1 99  ? 45.190 -28.118 9.730   1.00 21.38 ?  99   ASN   B HD21 1 
ATOM   5450 H  HD22 . ASN   B 1 99  ? 44.631 -26.741 9.628   1.00 21.38 ?  99   ASN   B HD22 1 
ATOM   5451 N  N    A VAL   B 1 100 ? 39.792 -29.778 9.551   0.50 21.33 ?  100  VAL   B N    1 
ATOM   5452 N  N    B VAL   B 1 100 ? 39.809 -29.783 9.545   0.50 21.30 ?  100  VAL   B N    1 
ATOM   5453 C  CA   A VAL   B 1 100 ? 39.185 -30.871 10.308  0.50 23.64 ?  100  VAL   B CA   1 
ATOM   5454 C  CA   B VAL   B 1 100 ? 39.191 -30.889 10.272  0.50 23.56 ?  100  VAL   B CA   1 
ATOM   5455 C  C    A VAL   B 1 100 ? 40.202 -31.528 11.233  0.50 24.10 ?  100  VAL   B C    1 
ATOM   5456 C  C    B VAL   B 1 100 ? 40.194 -31.562 11.202  0.50 23.97 ?  100  VAL   B C    1 
ATOM   5457 O  O    A VAL   B 1 100 ? 39.845 -32.023 12.309  0.50 24.62 ?  100  VAL   B O    1 
ATOM   5458 O  O    B VAL   B 1 100 ? 39.816 -32.104 12.248  0.50 24.29 ?  100  VAL   B O    1 
ATOM   5459 C  CB   A VAL   B 1 100 ? 38.523 -31.884 9.352   0.50 25.72 ?  100  VAL   B CB   1 
ATOM   5460 C  CB   B VAL   B 1 100 ? 38.562 -31.883 9.274   0.50 25.58 ?  100  VAL   B CB   1 
ATOM   5461 C  CG1  A VAL   B 1 100 ? 38.039 -33.108 10.116  0.50 26.57 ?  100  VAL   B CG1  1 
ATOM   5462 C  CG1  B VAL   B 1 100 ? 38.034 -33.113 9.994   0.50 26.41 ?  100  VAL   B CG1  1 
ATOM   5463 C  CG2  A VAL   B 1 100 ? 37.366 -31.231 8.612   0.50 26.34 ?  100  VAL   B CG2  1 
ATOM   5464 C  CG2  B VAL   B 1 100 ? 37.449 -31.208 8.486   0.50 26.23 ?  100  VAL   B CG2  1 
ATOM   5465 H  H    A VAL   B 1 100 ? 39.797 -29.892 8.696   0.50 25.61 ?  100  VAL   B H    1 
ATOM   5466 H  H    B VAL   B 1 100 ? 39.838 -29.894 8.690   0.50 25.58 ?  100  VAL   B H    1 
ATOM   5467 H  HA   A VAL   B 1 100 ? 38.479 -30.502 10.862  0.50 28.39 ?  100  VAL   B HA   1 
ATOM   5468 H  HA   B VAL   B 1 100 ? 38.470 -30.535 10.816  0.50 28.29 ?  100  VAL   B HA   1 
ATOM   5469 H  HB   A VAL   B 1 100 ? 39.174 -32.179 8.698   0.50 30.89 ?  100  VAL   B HB   1 
ATOM   5470 H  HB   B VAL   B 1 100 ? 39.239 -32.175 8.644   0.50 30.72 ?  100  VAL   B HB   1 
ATOM   5471 H  HG11 A VAL   B 1 100 ? 37.441 -33.618 9.546   0.50 31.91 ?  100  VAL   B HG11 1 
ATOM   5472 H  HG11 B VAL   B 1 100 ? 37.469 -33.617 9.386   0.50 31.71 ?  100  VAL   B HG11 1 
ATOM   5473 H  HG12 A VAL   B 1 100 ? 38.802 -33.654 10.363  0.50 31.91 ?  100  VAL   B HG12 1 
ATOM   5474 H  HG12 B VAL   B 1 100 ? 38.781 -33.662 10.278  0.50 31.71 ?  100  VAL   B HG12 1 
ATOM   5475 H  HG13 A VAL   B 1 100 ? 37.565 -32.818 10.911  0.50 31.91 ?  100  VAL   B HG13 1 
ATOM   5476 H  HG13 B VAL   B 1 100 ? 37.516 -32.830 10.764  0.50 31.71 ?  100  VAL   B HG13 1 
ATOM   5477 H  HG21 A VAL   B 1 100 ? 36.955 -31.887 8.027   0.50 31.63 ?  100  VAL   B HG21 1 
ATOM   5478 H  HG21 B VAL   B 1 100 ? 37.040 -31.859 7.894   0.50 31.50 ?  100  VAL   B HG21 1 
ATOM   5479 H  HG22 A VAL   B 1 100 ? 36.716 -30.913 9.259   0.50 31.63 ?  100  VAL   B HG22 1 
ATOM   5480 H  HG22 B VAL   B 1 100 ? 36.787 -30.865 9.107   0.50 31.50 ?  100  VAL   B HG22 1 
ATOM   5481 H  HG23 A VAL   B 1 100 ? 37.705 -30.489 8.090   0.50 31.63 ?  100  VAL   B HG23 1 
ATOM   5482 H  HG23 B VAL   B 1 100 ? 37.825 -30.480 7.968   0.50 31.50 ?  100  VAL   B HG23 1 
ATOM   5483 N  N    . ASN   B 1 101 ? 41.478 -31.557 10.835  1.00 24.59 ?  101  ASN   B N    1 
ATOM   5484 C  CA   . ASN   B 1 101 ? 42.514 -32.105 11.709  1.00 26.06 ?  101  ASN   B CA   1 
ATOM   5485 C  C    . ASN   B 1 101 ? 42.715 -31.270 12.968  1.00 28.17 ?  101  ASN   B C    1 
ATOM   5486 O  O    . ASN   B 1 101 ? 43.347 -31.745 13.921  1.00 29.48 ?  101  ASN   B O    1 
ATOM   5487 C  CB   . ASN   B 1 101 ? 43.834 -32.245 10.948  1.00 26.12 ?  101  ASN   B CB   1 
ATOM   5488 C  CG   . ASN   B 1 101 ? 43.817 -33.397 9.960   1.00 25.74 ?  101  ASN   B CG   1 
ATOM   5489 O  OD1  . ASN   B 1 101 ? 43.125 -34.389 10.166  1.00 26.30 ?  101  ASN   B OD1  1 
ATOM   5490 N  ND2  . ASN   B 1 101 ? 44.574 -33.267 8.879   1.00 25.29 ?  101  ASN   B ND2  1 
ATOM   5491 H  H    A ASN   B 1 101 ? 41.758 -31.283 10.068  0.50 29.53 ?  101  ASN   B H    1 
ATOM   5492 H  H    B ASN   B 1 101 ? 41.767 -31.255 10.082  0.50 29.53 ?  101  ASN   B H    1 
ATOM   5493 H  HA   . ASN   B 1 101 ? 42.239 -32.987 11.990  1.00 31.29 ?  101  ASN   B HA   1 
ATOM   5494 H  HB2  . ASN   B 1 101 ? 44.009 -31.431 10.452  1.00 31.36 ?  101  ASN   B HB2  1 
ATOM   5495 H  HB3  . ASN   B 1 101 ? 44.549 -32.404 11.586  1.00 31.36 ?  101  ASN   B HB3  1 
ATOM   5496 H  HD21 . ASN   B 1 101 ? 44.599 -33.896 8.293   1.00 30.37 ?  101  ASN   B HD21 1 
ATOM   5497 H  HD22 . ASN   B 1 101 ? 45.041 -32.555 8.765   1.00 30.37 ?  101  ASN   B HD22 1 
ATOM   5498 N  N    . LYS   B 1 102 ? 42.203 -30.037 12.987  1.00 30.55 ?  102  LYS   B N    1 
ATOM   5499 C  CA   . LYS   B 1 102 ? 42.179 -29.199 14.178  1.00 33.27 ?  102  LYS   B CA   1 
ATOM   5500 C  C    . LYS   B 1 102 ? 40.800 -29.153 14.825  1.00 32.73 ?  102  LYS   B C    1 
ATOM   5501 O  O    . LYS   B 1 102 ? 40.580 -28.350 15.736  1.00 33.64 ?  102  LYS   B O    1 
ATOM   5502 C  CB   . LYS   B 1 102 ? 42.616 -27.773 13.836  1.00 36.86 ?  102  LYS   B CB   1 
ATOM   5503 C  CG   . LYS   B 1 102 ? 44.080 -27.610 13.470  1.00 40.04 ?  102  LYS   B CG   1 
ATOM   5504 C  CD   . LYS   B 1 102 ? 44.334 -26.197 12.965  1.00 43.08 ?  102  LYS   B CD   1 
ATOM   5505 C  CE   . LYS   B 1 102 ? 45.814 -25.892 12.822  1.00 45.37 ?  102  LYS   B CE   1 
ATOM   5506 N  NZ   . LYS   B 1 102 ? 46.029 -24.497 12.338  1.00 46.66 ?  102  LYS   B NZ   1 
ATOM   5507 H  H    . LYS   B 1 102 ? 41.847 -29.655 12.300  1.00 36.68 ?  102  LYS   B H    1 
ATOM   5508 H  HA   . LYS   B 1 102 ? 42.809 -29.554 14.823  1.00 39.94 ?  102  LYS   B HA   1 
ATOM   5509 H  HB2  . LYS   B 1 102 ? 42.092 -27.461 13.083  1.00 44.25 ?  102  LYS   B HB2  1 
ATOM   5510 H  HB3  . LYS   B 1 102 ? 42.446 -27.206 14.606  1.00 44.25 ?  102  LYS   B HB3  1 
ATOM   5511 H  HG2  . LYS   B 1 102 ? 44.632 -27.761 14.254  1.00 48.07 ?  102  LYS   B HG2  1 
ATOM   5512 H  HG3  . LYS   B 1 102 ? 44.311 -28.236 12.766  1.00 48.07 ?  102  LYS   B HG3  1 
ATOM   5513 H  HD2  . LYS   B 1 102 ? 43.919 -26.092 12.094  1.00 51.72 ?  102  LYS   B HD2  1 
ATOM   5514 H  HD3  . LYS   B 1 102 ? 43.955 -25.563 13.593  1.00 51.72 ?  102  LYS   B HD3  1 
ATOM   5515 H  HE2  . LYS   B 1 102 ? 46.247 -25.986 13.685  1.00 54.47 ?  102  LYS   B HE2  1 
ATOM   5516 H  HE3  . LYS   B 1 102 ? 46.208 -26.502 12.179  1.00 54.47 ?  102  LYS   B HE3  1 
ATOM   5517 H  HZ1  . LYS   B 1 102 ? 46.899 -24.333 12.259  1.00 56.02 ?  102  LYS   B HZ1  1 
ATOM   5518 H  HZ2  . LYS   B 1 102 ? 45.640 -24.388 11.545  1.00 56.02 ?  102  LYS   B HZ2  1 
ATOM   5519 H  HZ3  . LYS   B 1 102 ? 45.676 -23.918 12.915  1.00 56.02 ?  102  LYS   B HZ3  1 
ATOM   5520 N  N    . GLY   B 1 103 ? 39.861 -29.972 14.357  1.00 31.95 ?  103  GLY   B N    1 
ATOM   5521 C  CA   . GLY   B 1 103 ? 38.534 -30.027 14.936  1.00 31.61 ?  103  GLY   B CA   1 
ATOM   5522 C  C    . GLY   B 1 103 ? 37.577 -28.956 14.469  1.00 30.73 ?  103  GLY   B C    1 
ATOM   5523 O  O    . GLY   B 1 103 ? 36.475 -28.853 15.020  1.00 31.12 ?  103  GLY   B O    1 
ATOM   5524 H  H    . GLY   B 1 103 ? 39.971 -30.504 13.693  1.00 38.37 ?  103  GLY   B H    1 
ATOM   5525 H  HA2  . GLY   B 1 103 ? 38.138 -30.887 14.729  1.00 37.95 ?  103  GLY   B HA2  1 
ATOM   5526 H  HA3  . GLY   B 1 103 ? 38.609 -29.957 15.901  1.00 37.95 ?  103  GLY   B HA3  1 
ATOM   5527 N  N    A GLU   B 1 104 ? 37.963 -28.148 13.484  0.50 29.92 ?  104  GLU   B N    1 
ATOM   5528 N  N    B GLU   B 1 104 ? 37.943 -28.169 13.462  0.50 29.71 ?  104  GLU   B N    1 
ATOM   5529 C  CA   A GLU   B 1 104 ? 37.121 -27.051 13.035  0.50 28.88 ?  104  GLU   B CA   1 
ATOM   5530 C  CA   B GLU   B 1 104 ? 37.080 -27.096 12.995  0.50 28.47 ?  104  GLU   B CA   1 
ATOM   5531 C  C    A GLU   B 1 104 ? 35.933 -27.576 12.228  0.50 29.44 ?  104  GLU   B C    1 
ATOM   5532 C  C    B GLU   B 1 104 ? 35.919 -27.647 12.171  0.50 28.90 ?  104  GLU   B C    1 
ATOM   5533 O  O    A GLU   B 1 104 ? 35.970 -28.662 11.642  0.50 30.05 ?  104  GLU   B O    1 
ATOM   5534 O  O    B GLU   B 1 104 ? 36.001 -28.730 11.584  0.50 29.54 ?  104  GLU   B O    1 
ATOM   5535 C  CB   A GLU   B 1 104 ? 37.949 -26.050 12.225  0.50 27.66 ?  104  GLU   B CB   1 
ATOM   5536 C  CB   B GLU   B 1 104 ? 37.892 -26.076 12.196  0.50 27.17 ?  104  GLU   B CB   1 
ATOM   5537 C  CG   A GLU   B 1 104 ? 39.056 -25.404 13.051  0.50 26.50 ?  104  GLU   B CG   1 
ATOM   5538 C  CG   B GLU   B 1 104 ? 38.966 -25.409 13.046  0.50 25.93 ?  104  GLU   B CG   1 
ATOM   5539 C  CD   A GLU   B 1 104 ? 39.978 -24.516 12.242  0.50 25.29 ?  104  GLU   B CD   1 
ATOM   5540 C  CD   B GLU   B 1 104 ? 39.939 -24.567 12.249  0.50 24.66 ?  104  GLU   B CD   1 
ATOM   5541 O  OE1  A GLU   B 1 104 ? 39.971 -24.604 10.996  0.50 23.57 ?  104  GLU   B OE1  1 
ATOM   5542 O  OE1  B GLU   B 1 104 ? 39.914 -24.617 11.001  0.50 23.15 ?  104  GLU   B OE1  1 
ATOM   5543 O  OE2  A GLU   B 1 104 ? 40.717 -23.725 12.863  0.50 25.34 -1 104  GLU   B OE2  1 
ATOM   5544 O  OE2  B GLU   B 1 104 ? 40.739 -23.852 12.885  0.50 24.50 -1 104  GLU   B OE2  1 
ATOM   5545 H  H    A GLU   B 1 104 ? 38.712 -28.212 13.065  0.50 35.92 ?  104  GLU   B H    1 
ATOM   5546 H  H    B GLU   B 1 104 ? 38.687 -28.235 13.034  0.50 35.68 ?  104  GLU   B H    1 
ATOM   5547 H  HA   A GLU   B 1 104 ? 36.775 -26.583 13.811  0.50 34.68 ?  104  GLU   B HA   1 
ATOM   5548 H  HA   B GLU   B 1 104 ? 36.708 -26.640 13.764  0.50 34.18 ?  104  GLU   B HA   1 
ATOM   5549 H  HB2  A GLU   B 1 104 ? 38.363 -26.508 11.477  0.50 33.22 ?  104  GLU   B HB2  1 
ATOM   5550 H  HB2  B GLU   B 1 104 ? 38.328 -26.524 11.456  0.50 32.62 ?  104  GLU   B HB2  1 
ATOM   5551 H  HB3  A GLU   B 1 104 ? 37.368 -25.343 11.901  0.50 33.22 ?  104  GLU   B HB3  1 
ATOM   5552 H  HB3  B GLU   B 1 104 ? 37.297 -25.384 11.865  0.50 32.62 ?  104  GLU   B HB3  1 
ATOM   5553 H  HG2  A GLU   B 1 104 ? 38.657 -24.857 13.746  0.50 31.82 ?  104  GLU   B HG2  1 
ATOM   5554 H  HG2  B GLU   B 1 104 ? 38.537 -24.830 13.696  0.50 31.14 ?  104  GLU   B HG2  1 
ATOM   5555 H  HG3  A GLU   B 1 104 ? 39.601 -26.098 13.452  0.50 31.82 ?  104  GLU   B HG3  1 
ATOM   5556 H  HG3  B GLU   B 1 104 ? 39.478 -26.093 13.503  0.50 31.14 ?  104  GLU   B HG3  1 
ATOM   5557 N  N    A ASP   B 1 105 ? 34.865 -26.781 12.210  0.50 28.76 ?  105  ASP   B N    1 
ATOM   5558 N  N    B ASP   B 1 105 ? 34.826 -26.885 12.142  0.50 27.95 ?  105  ASP   B N    1 
ATOM   5559 C  CA   A ASP   B 1 105 ? 33.589 -27.227 11.663  0.50 28.98 ?  105  ASP   B CA   1 
ATOM   5560 C  CA   B ASP   B 1 105 ? 33.563 -27.358 11.586  0.50 27.95 ?  105  ASP   B CA   1 
ATOM   5561 C  C    A ASP   B 1 105 ? 33.651 -27.282 10.141  0.50 27.03 ?  105  ASP   B C    1 
ATOM   5562 C  C    B ASP   B 1 105 ? 33.627 -27.369 10.063  0.50 26.21 ?  105  ASP   B C    1 
ATOM   5563 O  O    A ASP   B 1 105 ? 33.839 -26.255 9.480   0.50 26.44 ?  105  ASP   B O    1 
ATOM   5564 O  O    B ASP   B 1 105 ? 33.791 -26.319 9.433   0.50 25.56 ?  105  ASP   B O    1 
ATOM   5565 C  CB   A ASP   B 1 105 ? 32.479 -26.279 12.114  0.50 31.21 ?  105  ASP   B CB   1 
ATOM   5566 C  CB   B ASP   B 1 105 ? 32.418 -26.465 12.064  0.50 29.75 ?  105  ASP   B CB   1 
ATOM   5567 C  CG   A ASP   B 1 105 ? 31.101 -26.753 11.696  0.50 33.36 ?  105  ASP   B CG   1 
ATOM   5568 C  CG   B ASP   B 1 105 ? 31.051 -27.040 11.732  0.50 31.47 ?  105  ASP   B CG   1 
ATOM   5569 O  OD1  A ASP   B 1 105 ? 30.990 -27.868 11.143  0.50 33.76 ?  105  ASP   B OD1  1 
ATOM   5570 O  OD1  B ASP   B 1 105 ? 30.988 -28.051 11.000  0.50 31.86 ?  105  ASP   B OD1  1 
ATOM   5571 O  OD2  A ASP   B 1 105 ? 30.124 -26.005 11.917  0.50 34.43 -1 105  ASP   B OD2  1 
ATOM   5572 O  OD2  B ASP   B 1 105 ? 30.037 -26.488 12.212  0.50 31.97 -1 105  ASP   B OD2  1 
ATOM   5573 H  H    A ASP   B 1 105 ? 34.855 -25.976 12.512  0.50 34.53 ?  105  ASP   B H    1 
ATOM   5574 H  H    B ASP   B 1 105 ? 34.792 -26.082 12.440  0.50 33.56 ?  105  ASP   B H    1 
ATOM   5575 H  HA   A ASP   B 1 105 ? 33.388 -28.115 11.995  0.50 34.80 ?  105  ASP   B HA   1 
ATOM   5576 H  HA   B ASP   B 1 105 ? 33.388 -28.262 11.892  0.50 33.57 ?  105  ASP   B HA   1 
ATOM   5577 H  HB2  A ASP   B 1 105 ? 32.501 -26.203 13.082  0.50 37.47 ?  105  ASP   B HB2  1 
ATOM   5578 H  HB2  B ASP   B 1 105 ? 32.473 -26.364 13.027  0.50 35.72 ?  105  ASP   B HB2  1 
ATOM   5579 H  HB3  A ASP   B 1 105 ? 32.620 -25.410 11.710  0.50 37.47 ?  105  ASP   B HB3  1 
ATOM   5580 H  HB3  B ASP   B 1 105 ? 32.495 -25.595 11.637  0.50 35.72 ?  105  ASP   B HB3  1 
ATOM   5581 N  N    A ILE   B 1 106 ? 33.468 -28.484 9.587   0.50 26.36 ?  106  ILE   B N    1 
ATOM   5582 N  N    B ILE   B 1 106 ? 33.471 -28.559 9.476   0.50 25.80 ?  106  ILE   B N    1 
ATOM   5583 C  CA   A ILE   B 1 106 ? 33.475 -28.671 8.141   0.50 25.51 ?  106  ILE   B CA   1 
ATOM   5584 C  CA   B ILE   B 1 106 ? 33.475 -28.706 8.026   0.50 25.38 ?  106  ILE   B CA   1 
ATOM   5585 C  C    A ILE   B 1 106 ? 32.378 -27.860 7.460   0.50 24.41 ?  106  ILE   B C    1 
ATOM   5586 C  C    B ILE   B 1 106 ? 32.370 -27.886 7.372   0.50 24.43 ?  106  ILE   B C    1 
ATOM   5587 O  O    A ILE   B 1 106 ? 32.487 -27.551 6.270   0.50 23.57 ?  106  ILE   B O    1 
ATOM   5588 O  O    B ILE   B 1 106 ? 32.448 -27.583 6.177   0.50 23.68 ?  106  ILE   B O    1 
ATOM   5589 C  CB   A ILE   B 1 106 ? 33.373 -30.179 7.814   0.50 26.01 ?  106  ILE   B CB   1 
ATOM   5590 C  CB   B ILE   B 1 106 ? 33.382 -30.206 7.660   0.50 26.09 ?  106  ILE   B CB   1 
ATOM   5591 C  CG1  A ILE   B 1 106 ? 33.619 -30.435 6.325   0.50 25.97 ?  106  ILE   B CG1  1 
ATOM   5592 C  CG1  B ILE   B 1 106 ? 33.662 -30.429 6.173   0.50 26.27 ?  106  ILE   B CG1  1 
ATOM   5593 C  CG2  A ILE   B 1 106 ? 32.013 -30.726 8.229   0.50 26.56 ?  106  ILE   B CG2  1 
ATOM   5594 C  CG2  B ILE   B 1 106 ? 32.016 -30.767 8.034   0.50 26.73 ?  106  ILE   B CG2  1 
ATOM   5595 C  CD1  A ILE   B 1 106 ? 34.978 -29.977 5.848   0.50 25.80 ?  106  ILE   B CD1  1 
ATOM   5596 C  CD1  B ILE   B 1 106 ? 35.020 -29.941 5.735   0.50 26.35 ?  106  ILE   B CD1  1 
ATOM   5597 H  H    A ILE   B 1 106 ? 33.341 -29.205 10.034  0.50 31.65 ?  106  ILE   B H    1 
ATOM   5598 H  H    B ILE   B 1 106 ? 33.365 -29.296 9.902   0.50 30.98 ?  106  ILE   B H    1 
ATOM   5599 H  HA   A ILE   B 1 106 ? 34.322 -28.353 7.802   0.50 30.64 ?  106  ILE   B HA   1 
ATOM   5600 H  HA   B ILE   B 1 106 ? 34.319 -28.371 7.693   0.50 30.48 ?  106  ILE   B HA   1 
ATOM   5601 H  HB   A ILE   B 1 106 ? 34.056 -30.649 8.319   0.50 31.24 ?  106  ILE   B HB   1 
ATOM   5602 H  HB   B ILE   B 1 106 ? 34.054 -30.685 8.169   0.50 31.32 ?  106  ILE   B HB   1 
ATOM   5603 H  HG12 A ILE   B 1 106 ? 33.556 -31.390 6.158   0.50 31.18 ?  106  ILE   B HG12 1 
ATOM   5604 H  HG12 B ILE   B 1 106 ? 33.618 -31.382 5.986   0.50 31.54 ?  106  ILE   B HG12 1 
ATOM   5605 H  HG13 A ILE   B 1 106 ? 32.947 -29.968 5.807   0.50 31.18 ?  106  ILE   B HG13 1 
ATOM   5606 H  HG13 B ILE   B 1 106 ? 32.994 -29.962 5.651   0.50 31.54 ?  106  ILE   B HG13 1 
ATOM   5607 H  HG21 A ILE   B 1 106 ? 32.026 -31.693 8.154   0.50 31.89 ?  106  ILE   B HG21 1 
ATOM   5608 H  HG21 B ILE   B 1 106 ? 32.039 -31.733 7.948   0.50 32.10 ?  106  ILE   B HG21 1 
ATOM   5609 H  HG22 A ILE   B 1 106 ? 31.837 -30.469 9.147   0.50 31.89 ?  106  ILE   B HG22 1 
ATOM   5610 H  HG22 B ILE   B 1 106 ? 31.816 -30.521 8.950   0.50 32.10 ?  106  ILE   B HG22 1 
ATOM   5611 H  HG23 A ILE   B 1 106 ? 31.332 -30.358 7.646   0.50 31.89 ?  106  ILE   B HG23 1 
ATOM   5612 H  HG23 B ILE   B 1 106 ? 31.347 -30.398 7.438   0.50 32.10 ?  106  ILE   B HG23 1 
ATOM   5613 H  HD11 A ILE   B 1 106 ? 35.163 -30.382 4.987   0.50 30.99 ?  106  ILE   B HD11 1 
ATOM   5614 H  HD11 B ILE   B 1 106 ? 35.238 -30.342 4.881   0.50 31.64 ?  106  ILE   B HD11 1 
ATOM   5615 H  HD12 A ILE   B 1 106 ? 34.974 -29.010 5.764   0.50 30.99 ?  106  ILE   B HD12 1 
ATOM   5616 H  HD12 B ILE   B 1 106 ? 34.996 -28.974 5.650   0.50 31.64 ?  106  ILE   B HD12 1 
ATOM   5617 H  HD13 A ILE   B 1 106 ? 35.649 -30.252 6.493   0.50 30.99 ?  106  ILE   B HD13 1 
ATOM   5618 H  HD13 B ILE   B 1 106 ? 35.678 -30.200 6.400   0.50 31.64 ?  106  ILE   B HD13 1 
ATOM   5619 N  N    A GLN   B 1 107 ? 31.318 -27.503 8.189   0.50 24.52 ?  107  GLN   B N    1 
ATOM   5620 N  N    B GLN   B 1 107 ? 31.337 -27.510 8.129   0.50 24.66 ?  107  GLN   B N    1 
ATOM   5621 C  CA   A GLN   B 1 107 ? 30.244 -26.703 7.609   0.50 25.08 ?  107  GLN   B CA   1 
ATOM   5622 C  CA   B GLN   B 1 107 ? 30.252 -26.710 7.572   0.50 25.16 ?  107  GLN   B CA   1 
ATOM   5623 C  C    A GLN   B 1 107 ? 30.732 -25.354 7.092   0.50 22.87 ?  107  GLN   B C    1 
ATOM   5624 C  C    B GLN   B 1 107 ? 30.724 -25.342 7.095   0.50 22.93 ?  107  GLN   B C    1 
ATOM   5625 O  O    A GLN   B 1 107 ? 30.093 -24.780 6.206   0.50 23.31 ?  107  GLN   B O    1 
ATOM   5626 O  O    B GLN   B 1 107 ? 30.066 -24.739 6.243   0.50 23.42 ?  107  GLN   B O    1 
ATOM   5627 C  CB   A GLN   B 1 107 ? 29.134 -26.496 8.642   0.50 28.35 ?  107  GLN   B CB   1 
ATOM   5628 C  CB   B GLN   B 1 107 ? 29.139 -26.553 8.612   0.50 28.35 ?  107  GLN   B CB   1 
ATOM   5629 C  CG   A GLN   B 1 107 ? 27.807 -25.996 8.069   0.50 31.31 ?  107  GLN   B CG   1 
ATOM   5630 C  CG   B GLN   B 1 107 ? 27.818 -26.025 8.062   0.50 31.28 ?  107  GLN   B CG   1 
ATOM   5631 C  CD   A GLN   B 1 107 ? 27.741 -24.483 7.947   0.50 33.56 ?  107  GLN   B CD   1 
ATOM   5632 C  CD   B GLN   B 1 107 ? 27.742 -24.508 8.056   0.50 33.51 ?  107  GLN   B CD   1 
ATOM   5633 O  OE1  A GLN   B 1 107 ? 28.574 -23.764 8.502   0.50 34.46 ?  107  GLN   B OE1  1 
ATOM   5634 O  OE1  B GLN   B 1 107 ? 28.569 -23.829 8.666   0.50 34.35 ?  107  GLN   B OE1  1 
ATOM   5635 N  NE2  A GLN   B 1 107 ? 26.741 -23.991 7.219   0.50 34.30 ?  107  GLN   B NE2  1 
ATOM   5636 N  NE2  B GLN   B 1 107 ? 26.741 -23.968 7.367   0.50 34.27 ?  107  GLN   B NE2  1 
ATOM   5637 H  H    A GLN   B 1 107 ? 31.197 -27.716 9.007   0.50 29.45 ?  107  GLN   B H    1 
ATOM   5638 H  H    B GLN   B 1 107 ? 31.244 -27.701 8.957   0.50 29.62 ?  107  GLN   B H    1 
ATOM   5639 H  HA   A GLN   B 1 107 ? 29.864 -27.186 6.859   0.50 30.12 ?  107  GLN   B HA   1 
ATOM   5640 H  HA   B GLN   B 1 107 ? 29.878 -27.178 6.808   0.50 30.21 ?  107  GLN   B HA   1 
ATOM   5641 H  HB2  A GLN   B 1 107 ? 28.962 -27.342 9.079   0.50 34.04 ?  107  GLN   B HB2  1 
ATOM   5642 H  HB2  B GLN   B 1 107 ? 28.964 -27.419 9.005   0.50 34.04 ?  107  GLN   B HB2  1 
ATOM   5643 H  HB3  A GLN   B 1 107 ? 29.437 -25.847 9.296   0.50 34.04 ?  107  GLN   B HB3  1 
ATOM   5644 H  HB3  B GLN   B 1 107 ? 29.441 -25.938 9.298   0.50 34.04 ?  107  GLN   B HB3  1 
ATOM   5645 H  HG2  A GLN   B 1 107 ? 27.682 -26.371 7.184   0.50 37.59 ?  107  GLN   B HG2  1 
ATOM   5646 H  HG2  B GLN   B 1 107 ? 27.709 -26.332 7.149   0.50 37.56 ?  107  GLN   B HG2  1 
ATOM   5647 H  HG3  A GLN   B 1 107 ? 27.085 -26.282 8.654   0.50 37.59 ?  107  GLN   B HG3  1 
ATOM   5648 H  HG3  B GLN   B 1 107 ? 27.091 -26.362 8.613   0.50 37.56 ?  107  GLN   B HG3  1 
ATOM   5649 H  HE21 A GLN   B 1 107 ? 26.177 -24.523 6.845   0.50 41.18 ?  107  GLN   B HE21 1 
ATOM   5650 H  HE21 B GLN   B 1 107 ? 26.181 -24.473 6.952   0.50 41.15 ?  107  GLN   B HE21 1 
ATOM   5651 H  HE22 A GLN   B 1 107 ? 26.655 -23.140 7.122   0.50 41.18 ?  107  GLN   B HE22 1 
ATOM   5652 H  HE22 B GLN   B 1 107 ? 26.652 -23.113 7.336   0.50 41.15 ?  107  GLN   B HE22 1 
ATOM   5653 N  N    . LEU   B 1 108 ? 31.852 -24.842 7.611   1.00 20.90 ?  108  LEU   B N    1 
ATOM   5654 C  CA   . LEU   B 1 108 ? 32.381 -23.539 7.199   1.00 18.08 ?  108  LEU   B CA   1 
ATOM   5655 C  C    . LEU   B 1 108 ? 33.032 -23.561 5.828   1.00 15.74 ?  108  LEU   B C    1 
ATOM   5656 O  O    . LEU   B 1 108 ? 33.469 -22.505 5.344   1.00 14.84 ?  108  LEU   B O    1 
ATOM   5657 C  CB   . LEU   B 1 108 ? 33.384 -23.032 8.232   1.00 18.57 ?  108  LEU   B CB   1 
ATOM   5658 C  CG   . LEU   B 1 108 ? 32.770 -22.535 9.540   1.00 20.08 ?  108  LEU   B CG   1 
ATOM   5659 C  CD1  . LEU   B 1 108 ? 33.786 -22.576 10.666  1.00 20.44 ?  108  LEU   B CD1  1 
ATOM   5660 C  CD2  . LEU   B 1 108 ? 32.249 -21.121 9.351   1.00 20.96 ?  108  LEU   B CD2  1 
ATOM   5661 H  H    A LEU   B 1 108 ? 32.318 -25.230 8.214   0.50 25.10 ?  108  LEU   B H    1 
ATOM   5662 H  H    B LEU   B 1 108 ? 32.319 -25.235 8.210   0.50 25.10 ?  108  LEU   B H    1 
ATOM   5663 H  HA   . LEU   B 1 108 ? 31.646 -22.907 7.167   1.00 21.72 ?  108  LEU   B HA   1 
ATOM   5664 H  HB2  . LEU   B 1 108 ? 33.991 -23.753 8.453   1.00 22.31 ?  108  LEU   B HB2  1 
ATOM   5665 H  HB3  . LEU   B 1 108 ? 33.877 -22.294 7.845   1.00 22.31 ?  108  LEU   B HB3  1 
ATOM   5666 H  HG   . LEU   B 1 108 ? 32.021 -23.104 9.783   1.00 24.11 ?  108  LEU   B HG   1 
ATOM   5667 H  HD11 . LEU   B 1 108 ? 33.364 -22.267 11.484  1.00 24.56 ?  108  LEU   B HD11 1 
ATOM   5668 H  HD12 . LEU   B 1 108 ? 34.097 -23.487 10.778  1.00 24.56 ?  108  LEU   B HD12 1 
ATOM   5669 H  HD13 . LEU   B 1 108 ? 34.530 -21.996 10.440  1.00 24.56 ?  108  LEU   B HD13 1 
ATOM   5670 H  HD21 . LEU   B 1 108 ? 31.855 -20.816 10.183  1.00 25.18 ?  108  LEU   B HD21 1 
ATOM   5671 H  HD22 . LEU   B 1 108 ? 32.988 -20.544 9.103   1.00 25.18 ?  108  LEU   B HD22 1 
ATOM   5672 H  HD23 . LEU   B 1 108 ? 31.580 -21.122 8.649   1.00 25.18 ?  108  LEU   B HD23 1 
ATOM   5673 N  N    . LEU   B 1 109 ? 33.099 -24.729 5.196   1.00 14.74 ?  109  LEU   B N    1 
ATOM   5674 C  CA   . LEU   B 1 109 ? 33.729 -24.836 3.890   1.00 13.55 ?  109  LEU   B CA   1 
ATOM   5675 C  C    . LEU   B 1 109 ? 32.970 -24.049 2.832   1.00 12.84 ?  109  LEU   B C    1 
ATOM   5676 O  O    . LEU   B 1 109 ? 33.588 -23.457 1.940   1.00 12.38 ?  109  LEU   B O    1 
ATOM   5677 C  CB   . LEU   B 1 109 ? 33.830 -26.311 3.511   1.00 13.78 ?  109  LEU   B CB   1 
ATOM   5678 C  CG   . LEU   B 1 109 ? 34.624 -26.650 2.254   1.00 13.60 ?  109  LEU   B CG   1 
ATOM   5679 C  CD1  . LEU   B 1 109 ? 36.011 -26.005 2.265   1.00 13.33 ?  109  LEU   B CD1  1 
ATOM   5680 C  CD2  . LEU   B 1 109 ? 34.737 -28.161 2.102   1.00 14.54 ?  109  LEU   B CD2  1 
ATOM   5681 H  H    . LEU   B 1 109 ? 32.799 -25.471 5.501   1.00 17.71 ?  109  LEU   B H    1 
ATOM   5682 H  HA   . LEU   B 1 109 ? 34.627 -24.475 3.938   1.00 16.28 ?  109  LEU   B HA   1 
ATOM   5683 H  HB2  . LEU   B 1 109 ? 34.247 -26.785 4.246   1.00 16.56 ?  109  LEU   B HB2  1 
ATOM   5684 H  HB3  . LEU   B 1 109 ? 32.932 -26.654 3.379   1.00 16.56 ?  109  LEU   B HB3  1 
ATOM   5685 H  HG   . LEU   B 1 109 ? 34.146 -26.323 1.477   1.00 16.34 ?  109  LEU   B HG   1 
ATOM   5686 H  HD11 . LEU   B 1 109 ? 36.540 -26.373 1.538   1.00 16.02 ?  109  LEU   B HD11 1 
ATOM   5687 H  HD12 . LEU   B 1 109 ? 35.910 -25.048 2.148   1.00 16.02 ?  109  LEU   B HD12 1 
ATOM   5688 H  HD13 . LEU   B 1 109 ? 36.441 -26.195 3.113   1.00 16.02 ?  109  LEU   B HD13 1 
ATOM   5689 H  HD21 . LEU   B 1 109 ? 35.314 -28.363 1.346   1.00 17.48 ?  109  LEU   B HD21 1 
ATOM   5690 H  HD22 . LEU   B 1 109 ? 35.113 -28.536 2.912   1.00 17.48 ?  109  LEU   B HD22 1 
ATOM   5691 H  HD23 . LEU   B 1 109 ? 33.852 -28.534 1.946   1.00 17.48 ?  109  LEU   B HD23 1 
ATOM   5692 N  N    . LYS   B 1 110 ? 31.638 -24.016 2.910   1.00 12.59 ?  110  LYS   B N    1 
ATOM   5693 C  CA   . LYS   B 1 110 ? 30.884 -23.259 1.917   1.00 12.17 ?  110  LYS   B CA   1 
ATOM   5694 C  C    . LYS   B 1 110 ? 31.221 -21.773 2.004   1.00 11.91 ?  110  LYS   B C    1 
ATOM   5695 O  O    . LYS   B 1 110 ? 31.476 -21.121 0.985   1.00 11.71 ?  110  LYS   B O    1 
ATOM   5696 C  CB   . LYS   B 1 110 ? 29.379 -23.507 2.069   1.00 12.77 ?  110  LYS   B CB   1 
ATOM   5697 C  CG   . LYS   B 1 110 ? 28.565 -22.874 0.943   1.00 13.04 ?  110  LYS   B CG   1 
ATOM   5698 C  CD   . LYS   B 1 110 ? 27.102 -23.317 0.952   1.00 13.28 ?  110  LYS   B CD   1 
ATOM   5699 C  CE   . LYS   B 1 110 ? 26.343 -22.779 -0.261  1.00 14.10 ?  110  LYS   B CE   1 
ATOM   5700 N  NZ   . LYS   B 1 110 ? 26.674 -23.495 -1.522  1.00 14.26 ?  110  LYS   B NZ   1 
ATOM   5701 H  H    . LYS   B 1 110 ? 31.164 -24.413 3.506   1.00 15.13 ?  110  LYS   B H    1 
ATOM   5702 H  HA   . LYS   B 1 110 ? 31.142 -23.564 1.032   1.00 14.62 ?  110  LYS   B HA   1 
ATOM   5703 H  HB2  . LYS   B 1 110 ? 29.215 -24.468 2.055   1.00 15.34 ?  110  LYS   B HB2  1 
ATOM   5704 H  HB3  . LYS   B 1 110 ? 29.077 -23.135 2.909   1.00 15.34 ?  110  LYS   B HB3  1 
ATOM   5705 H  HG2  . LYS   B 1 110 ? 28.578 -21.909 1.042   1.00 15.67 ?  110  LYS   B HG2  1 
ATOM   5706 H  HG3  . LYS   B 1 110 ? 28.942 -23.127 0.088   1.00 15.67 ?  110  LYS   B HG3  1 
ATOM   5707 H  HD2  . LYS   B 1 110 ? 27.058 -24.290 0.930   1.00 15.96 ?  110  LYS   B HD2  1 
ATOM   5708 H  HD3  . LYS   B 1 110 ? 26.667 -22.986 1.756   1.00 15.96 ?  110  LYS   B HD3  1 
ATOM   5709 H  HE2  . LYS   B 1 110 ? 25.389 -22.868 -0.108  1.00 16.94 ?  110  LYS   B HE2  1 
ATOM   5710 H  HE3  . LYS   B 1 110 ? 26.570 -21.842 -0.384  1.00 16.94 ?  110  LYS   B HE3  1 
ATOM   5711 H  HZ1  . LYS   B 1 110 ? 26.214 -23.149 -2.199  1.00 17.13 ?  110  LYS   B HZ1  1 
ATOM   5712 H  HZ2  . LYS   B 1 110 ? 27.543 -23.422 -1.692  1.00 17.13 ?  110  LYS   B HZ2  1 
ATOM   5713 H  HZ3  . LYS   B 1 110 ? 26.466 -24.358 -1.441  1.00 17.13 ?  110  LYS   B HZ3  1 
ATOM   5714 N  N    . SER   B 1 111 ? 31.236 -21.222 3.222   1.00 12.47 ?  111  SER   B N    1 
ATOM   5715 C  CA   . SER   B 1 111 ? 31.631 -19.825 3.399   1.00 12.40 ?  111  SER   B CA   1 
ATOM   5716 C  C    . SER   B 1 111 ? 33.011 -19.569 2.810   1.00 11.56 ?  111  SER   B C    1 
ATOM   5717 O  O    . SER   B 1 111 ? 33.240 -18.536 2.166   1.00 11.67 ?  111  SER   B O    1 
ATOM   5718 C  CB   . SER   B 1 111 ? 31.627 -19.468 4.884   1.00 13.54 ?  111  SER   B CB   1 
ATOM   5719 O  OG   . SER   B 1 111 ? 30.323 -19.457 5.421   1.00 14.79 ?  111  SER   B OG   1 
ATOM   5720 H  H    . SER   B 1 111 ? 31.032 -21.635 3.948   1.00 14.99 ?  111  SER   B H    1 
ATOM   5721 H  HA   . SER   B 1 111 ? 30.996 -19.255 2.943   1.00 14.90 ?  111  SER   B HA   1 
ATOM   5722 H  HB2  . SER   B 1 111 ? 32.148 -20.126 5.368   1.00 16.27 ?  111  SER   B HB2  1 
ATOM   5723 H  HB3  . SER   B 1 111 ? 32.017 -18.590 4.995   1.00 16.27 ?  111  SER   B HB3  1 
ATOM   5724 H  HG   . SER   B 1 111 ? 30.347 -19.249 6.242   1.00 17.78 ?  111  SER   B HG   1 
ATOM   5725 N  N    . ALA   B 1 112 ? 33.949 -20.487 3.040   1.00 11.72 ?  112  ALA   B N    1 
ATOM   5726 C  CA   . ALA   B 1 112 ? 35.293 -20.320 2.500   1.00 11.43 ?  112  ALA   B CA   1 
ATOM   5727 C  C    . ALA   B 1 112 ? 35.263 -20.224 0.978   1.00 10.73 ?  112  ALA   B C    1 
ATOM   5728 O  O    . ALA   B 1 112 ? 35.888 -19.335 0.388   1.00 11.23 ?  112  ALA   B O    1 
ATOM   5729 C  CB   . ALA   B 1 112 ? 36.193 -21.462 2.973   1.00 11.71 ?  112  ALA   B CB   1 
ATOM   5730 H  H    . ALA   B 1 112 ? 33.834 -21.204 3.509   1.00 14.09 ?  112  ALA   B H    1 
ATOM   5731 H  HA   . ALA   B 1 112 ? 35.661 -19.494 2.844   1.00 13.74 ?  112  ALA   B HA   1 
ATOM   5732 H  HB1  . ALA   B 1 112 ? 37.083 -21.329 2.610   1.00 14.08 ?  112  ALA   B HB1  1 
ATOM   5733 H  HB2  . ALA   B 1 112 ? 36.232 -21.452 3.945   1.00 14.08 ?  112  ALA   B HB2  1 
ATOM   5734 H  HB3  . ALA   B 1 112 ? 35.830 -22.303 2.666   1.00 14.08 ?  112  ALA   B HB3  1 
ATOM   5735 N  N    . TYR   B 1 113 ? 34.531 -21.123 0.320   1.00 10.73 ?  113  TYR   B N    1 
ATOM   5736 C  CA   . TYR   B 1 113 ? 34.457 -21.077 -1.134  1.00 10.47 ?  113  TYR   B CA   1 
ATOM   5737 C  C    . TYR   B 1 113 ? 33.751 -19.827 -1.651  1.00 10.24 ?  113  TYR   B C    1 
ATOM   5738 O  O    . TYR   B 1 113 ? 34.022 -19.396 -2.778  1.00 10.19 ?  113  TYR   B O    1 
ATOM   5739 C  CB   . TYR   B 1 113 ? 33.786 -22.337 -1.675  1.00 11.02 ?  113  TYR   B CB   1 
ATOM   5740 C  CG   . TYR   B 1 113 ? 34.744 -23.482 -1.935  1.00 11.36 ?  113  TYR   B CG   1 
ATOM   5741 C  CD1  . TYR   B 1 113 ? 35.744 -23.377 -2.895  1.00 12.06 ?  113  TYR   B CD1  1 
ATOM   5742 C  CD2  . TYR   B 1 113 ? 34.642 -24.673 -1.232  1.00 11.41 ?  113  TYR   B CD2  1 
ATOM   5743 C  CE1  . TYR   B 1 113 ? 36.620 -24.413 -3.138  1.00 12.08 ?  113  TYR   B CE1  1 
ATOM   5744 C  CE2  . TYR   B 1 113 ? 35.508 -25.727 -1.474  1.00 11.85 ?  113  TYR   B CE2  1 
ATOM   5745 C  CZ   . TYR   B 1 113 ? 36.494 -25.593 -2.431  1.00 11.94 ?  113  TYR   B CZ   1 
ATOM   5746 O  OH   . TYR   B 1 113 ? 37.375 -26.608 -2.708  1.00 12.69 ?  113  TYR   B OH   1 
ATOM   5747 H  H    . TYR   B 1 113 ? 34.071 -21.752 0.693   1.00 12.90 ?  113  TYR   B H    1 
ATOM   5748 H  HA   . TYR   B 1 113 ? 35.360 -21.061 -1.472  1.00 12.58 ?  113  TYR   B HA   1 
ATOM   5749 H  HB2  . TYR   B 1 113 ? 33.128 -22.646 -1.026  1.00 13.24 ?  113  TYR   B HB2  1 
ATOM   5750 H  HB3  . TYR   B 1 113 ? 33.344 -22.121 -2.508  1.00 13.24 ?  113  TYR   B HB3  1 
ATOM   5751 H  HD1  . TYR   B 1 113 ? 35.831 -22.583 -3.375  1.00 14.50 ?  113  TYR   B HD1  1 
ATOM   5752 H  HD2  . TYR   B 1 113 ? 33.972 -24.770 -0.595  1.00 13.72 ?  113  TYR   B HD2  1 
ATOM   5753 H  HE1  . TYR   B 1 113 ? 37.283 -24.323 -3.788  1.00 14.52 ?  113  TYR   B HE1  1 
ATOM   5754 H  HE2  . TYR   B 1 113 ? 35.422 -26.522 -1.001  1.00 14.25 ?  113  TYR   B HE2  1 
ATOM   5755 H  HH   . TYR   B 1 113 ? 37.203 -27.279 -2.230  1.00 15.25 ?  113  TYR   B HH   1 
ATOM   5756 N  N    . GLU   B 1 114 ? 32.826 -19.250 -0.875  1.00 10.45 ?  114  GLU   B N    1 
ATOM   5757 C  CA   . GLU   B 1 114 ? 32.146 -18.042 -1.332  1.00 10.53 ?  114  GLU   B CA   1 
ATOM   5758 C  C    . GLU   B 1 114 ? 33.130 -16.923 -1.629  1.00 10.44 ?  114  GLU   B C    1 
ATOM   5759 O  O    . GLU   B 1 114 ? 32.855 -16.062 -2.467  1.00 10.60 ?  114  GLU   B O    1 
ATOM   5760 C  CB   . GLU   B 1 114 ? 31.083 -17.609 -0.317  1.00 11.01 ?  114  GLU   B CB   1 
ATOM   5761 C  CG   . GLU   B 1 114 ? 29.863 -18.531 -0.380  1.00 11.36 ?  114  GLU   B CG   1 
ATOM   5762 C  CD   . GLU   B 1 114 ? 28.842 -18.341 0.722   1.00 11.51 ?  114  GLU   B CD   1 
ATOM   5763 O  OE1  . GLU   B 1 114 ? 29.136 -17.729 1.766   1.00 11.45 ?  114  GLU   B OE1  1 
ATOM   5764 O  OE2  . GLU   B 1 114 ? 27.720 -18.880 0.557   1.00 12.49 -1 114  GLU   B OE2  1 
ATOM   5765 H  H    . GLU   B 1 114 ? 32.570 -19.545 -0.105  1.00 12.56 ?  114  GLU   B H    1 
ATOM   5766 H  HA   . GLU   B 1 114 ? 31.689 -18.245 -2.158  1.00 12.66 ?  114  GLU   B HA   1 
ATOM   5767 H  HB2  . GLU   B 1 114 ? 31.453 -17.657 0.580   1.00 13.23 ?  114  GLU   B HB2  1 
ATOM   5768 H  HB3  . GLU   B 1 114 ? 30.795 -16.708 -0.517  1.00 13.23 ?  114  GLU   B HB3  1 
ATOM   5769 H  HG2  . GLU   B 1 114 ? 29.409 -18.382 -1.222  1.00 13.65 ?  114  GLU   B HG2  1 
ATOM   5770 H  HG3  . GLU   B 1 114 ? 30.168 -19.451 -0.334  1.00 13.65 ?  114  GLU   B HG3  1 
ATOM   5771 N  N    . ASN   B 1 115 ? 34.292 -16.920 -0.977  1.00 10.30 ?  115  ASN   B N    1 
ATOM   5772 C  CA   . ASN   B 1 115 ? 35.285 -15.892 -1.277  1.00 10.30 ?  115  ASN   B CA   1 
ATOM   5773 C  C    . ASN   B 1 115 ? 35.694 -15.916 -2.743  1.00 10.09 ?  115  ASN   B C    1 
ATOM   5774 O  O    . ASN   B 1 115 ? 36.087 -14.876 -3.298  1.00 10.48 ?  115  ASN   B O    1 
ATOM   5775 C  CB   . ASN   B 1 115 ? 36.525 -16.071 -0.397  1.00 10.71 ?  115  ASN   B CB   1 
ATOM   5776 C  CG   . ASN   B 1 115 ? 36.260 -15.794 1.062   1.00 11.02 ?  115  ASN   B CG   1 
ATOM   5777 O  OD1  . ASN   B 1 115 ? 36.271 -14.648 1.503   1.00 12.98 ?  115  ASN   B OD1  1 
ATOM   5778 N  ND2  . ASN   B 1 115 ? 36.077 -16.857 1.838   1.00 10.98 ?  115  ASN   B ND2  1 
ATOM   5779 H  H    . ASN   B 1 115 ? 34.529 -17.480 -0.362  1.00 12.39 ?  115  ASN   B H    1 
ATOM   5780 H  HA   . ASN   B 1 115 ? 34.911 -15.017 -1.086  1.00 12.38 ?  115  ASN   B HA   1 
ATOM   5781 H  HB2  . ASN   B 1 115 ? 36.841 -16.984 -0.476  1.00 12.88 ?  115  ASN   B HB2  1 
ATOM   5782 H  HB3  . ASN   B 1 115 ? 37.216 -15.455 -0.690  1.00 12.88 ?  115  ASN   B HB3  1 
ATOM   5783 H  HD21 . ASN   B 1 115 ? 35.938 -16.753 2.682   1.00 13.19 ?  115  ASN   B HD21 1 
ATOM   5784 H  HD22 . ASN   B 1 115 ? 36.098 -17.647 1.501   1.00 13.19 ?  115  ASN   B HD22 1 
ATOM   5785 N  N    . PHE   B 1 116 ? 35.662 -17.093 -3.376  1.00 9.96  ?  116  PHE   B N    1 
ATOM   5786 C  CA   . PHE   B 1 116 ? 36.097 -17.185 -4.764  1.00 10.11 ?  116  PHE   B CA   1 
ATOM   5787 C  C    . PHE   B 1 116 ? 35.195 -16.365 -5.678  1.00 9.82  ?  116  PHE   B C    1 
ATOM   5788 O  O    . PHE   B 1 116 ? 35.631 -15.937 -6.751  1.00 10.43 ?  116  PHE   B O    1 
ATOM   5789 C  CB   . PHE   B 1 116 ? 36.062 -18.632 -5.283  1.00 9.85  ?  116  PHE   B CB   1 
ATOM   5790 C  CG   . PHE   B 1 116 ? 37.132 -19.584 -4.734  1.00 9.83  ?  116  PHE   B CG   1 
ATOM   5791 C  CD1  . PHE   B 1 116 ? 37.779 -19.402 -3.520  1.00 10.83 ?  116  PHE   B CD1  1 
ATOM   5792 C  CD2  . PHE   B 1 116 ? 37.441 -20.715 -5.471  1.00 9.96  ?  116  PHE   B CD2  1 
ATOM   5793 C  CE1  . PHE   B 1 116 ? 38.712 -20.336 -3.068  1.00 10.83 ?  116  PHE   B CE1  1 
ATOM   5794 C  CE2  . PHE   B 1 116 ? 38.367 -21.641 -5.025  1.00 10.25 ?  116  PHE   B CE2  1 
ATOM   5795 C  CZ   . PHE   B 1 116 ? 39.003 -21.456 -3.827  1.00 10.42 ?  116  PHE   B CZ   1 
ATOM   5796 H  H    . PHE   B 1 116 ? 35.386 -17.836 -3.032  1.00 11.97 ?  116  PHE   B H    1 
ATOM   5797 H  HA   . PHE   B 1 116 ? 37.003 -16.852 -4.840  1.00 12.15 ?  116  PHE   B HA   1 
ATOM   5798 H  HB2  . PHE   B 1 116 ? 35.193 -19.008 -5.062  1.00 11.84 ?  116  PHE   B HB2  1 
ATOM   5799 H  HB3  . PHE   B 1 116 ? 36.162 -18.607 -6.246  1.00 11.84 ?  116  PHE   B HB3  1 
ATOM   5800 H  HD1  . PHE   B 1 116 ? 37.574 -18.658 -2.997  1.00 13.02 ?  116  PHE   B HD1  1 
ATOM   5801 H  HD2  . PHE   B 1 116 ? 37.009 -20.857 -6.281  1.00 11.98 ?  116  PHE   B HD2  1 
ATOM   5802 H  HE1  . PHE   B 1 116 ? 39.139 -20.198 -2.255  1.00 13.02 ?  116  PHE   B HE1  1 
ATOM   5803 H  HE2  . PHE   B 1 116 ? 38.566 -22.386 -5.541  1.00 12.32 ?  116  PHE   B HE2  1 
ATOM   5804 H  HZ   . PHE   B 1 116 ? 39.637 -22.063 -3.526  1.00 12.52 ?  116  PHE   B HZ   1 
ATOM   5805 N  N    . ASN   B 1 117 ? 33.927 -16.161 -5.292  1.00 10.10 ?  117  ASN   B N    1 
ATOM   5806 C  CA   . ASN   B 1 117 ? 32.981 -15.460 -6.155  1.00 10.13 ?  117  ASN   B CA   1 
ATOM   5807 C  C    . ASN   B 1 117 ? 33.294 -13.982 -6.303  1.00 10.76 ?  117  ASN   B C    1 
ATOM   5808 O  O    . ASN   B 1 117 ? 32.692 -13.322 -7.154  1.00 11.78 ?  117  ASN   B O    1 
ATOM   5809 C  CB   . ASN   B 1 117 ? 31.559 -15.681 -5.658  1.00 10.33 ?  117  ASN   B CB   1 
ATOM   5810 C  CG   . ASN   B 1 117 ? 31.111 -17.084 -5.909  1.00 10.70 ?  117  ASN   B CG   1 
ATOM   5811 O  OD1  . ASN   B 1 117 ? 31.463 -17.674 -6.930  1.00 11.70 ?  117  ASN   B OD1  1 
ATOM   5812 N  ND2  . ASN   B 1 117 ? 30.372 -17.649 -4.975  1.00 11.08 ?  117  ASN   B ND2  1 
ATOM   5813 H  H    . ASN   B 1 117 ? 33.600 -16.419 -4.534  1.00 12.14 ?  117  ASN   B H    1 
ATOM   5814 H  HA   . ASN   B 1 117 ? 33.040 -15.855 -7.033  1.00 12.18 ?  117  ASN   B HA   1 
ATOM   5815 H  HB2  . ASN   B 1 117 ? 31.522 -15.513 -4.700  1.00 12.42 ?  117  ASN   B HB2  1 
ATOM   5816 H  HB3  . ASN   B 1 117 ? 30.961 -15.074 -6.124  1.00 12.42 ?  117  ASN   B HB3  1 
ATOM   5817 H  HD21 . ASN   B 1 117 ? 30.095 -18.452 -5.078  1.00 13.32 ?  117  ASN   B HD21 1 
ATOM   5818 H  HD22 . ASN   B 1 117 ? 30.157 -17.201 -4.272  1.00 13.32 ?  117  ASN   B HD22 1 
ATOM   5819 N  N    . GLN   B 1 118 ? 34.231 -13.455 -5.527  1.00 10.35 ?  118  GLN   B N    1 
ATOM   5820 C  CA   . GLN   B 1 118 ? 34.658 -12.070 -5.664  1.00 11.17 ?  118  GLN   B CA   1 
ATOM   5821 C  C    . GLN   B 1 118 ? 35.727 -11.874 -6.732  1.00 11.32 ?  118  GLN   B C    1 
ATOM   5822 O  O    . GLN   B 1 118 ? 36.204 -10.746 -6.906  1.00 12.43 ?  118  GLN   B O    1 
ATOM   5823 C  CB   . GLN   B 1 118 ? 35.134 -11.538 -4.308  1.00 11.80 ?  118  GLN   B CB   1 
ATOM   5824 C  CG   . GLN   B 1 118 ? 34.050 -11.575 -3.244  1.00 11.74 ?  118  GLN   B CG   1 
ATOM   5825 C  CD   . GLN   B 1 118 ? 32.882 -10.672 -3.584  1.00 11.42 ?  118  GLN   B CD   1 
ATOM   5826 O  OE1  . GLN   B 1 118 ? 33.072 -9.532  -4.022  1.00 12.24 ?  118  GLN   B OE1  1 
ATOM   5827 N  NE2  . GLN   B 1 118 ? 31.667 -11.170 -3.391  1.00 11.85 ?  118  GLN   B NE2  1 
ATOM   5828 H  H    . GLN   B 1 118 ? 34.651 -13.879 -4.908  1.00 12.45 ?  118  GLN   B H    1 
ATOM   5829 H  HA   . GLN   B 1 118 ? 33.893 -11.536 -5.932  1.00 13.42 ?  118  GLN   B HA   1 
ATOM   5830 H  HB2  . GLN   B 1 118 ? 35.878 -12.070 -3.998  1.00 14.19 ?  118  GLN   B HB2  1 
ATOM   5831 H  HB3  . GLN   B 1 118 ? 35.413 -10.608 -4.409  1.00 14.19 ?  118  GLN   B HB3  1 
ATOM   5832 H  HG2  . GLN   B 1 118 ? 33.719 -12.484 -3.162  1.00 14.11 ?  118  GLN   B HG2  1 
ATOM   5833 H  HG3  . GLN   B 1 118 ? 34.425 -11.282 -2.397  1.00 14.11 ?  118  GLN   B HG3  1 
ATOM   5834 H  HE21 . GLN   B 1 118 ? 31.576 -11.971 -3.084  1.00 14.24 ?  118  GLN   B HE21 1 
ATOM   5835 H  HE22 . GLN   B 1 118 ? 30.978 -10.696 -3.569  1.00 14.24 ?  118  GLN   B HE22 1 
ATOM   5836 N  N    . HIS   B 1 119 ? 36.080 -12.931 -7.465  1.00 10.82 ?  119  HIS   B N    1 
ATOM   5837 C  CA   . HIS   B 1 119 ? 37.125 -12.889 -8.480  1.00 11.08 ?  119  HIS   B CA   1 
ATOM   5838 C  C    . HIS   B 1 119 ? 36.641 -13.620 -9.718  1.00 11.16 ?  119  HIS   B C    1 
ATOM   5839 O  O    . HIS   B 1 119 ? 36.127 -14.734 -9.618  1.00 11.65 ?  119  HIS   B O    1 
ATOM   5840 C  CB   . HIS   B 1 119 ? 38.401 -13.526 -7.928  1.00 11.61 ?  119  HIS   B CB   1 
ATOM   5841 C  CG   . HIS   B 1 119 ? 38.883 -12.829 -6.705  1.00 12.87 ?  119  HIS   B CG   1 
ATOM   5842 N  ND1  . HIS   B 1 119 ? 39.680 -11.705 -6.761  1.00 14.32 ?  119  HIS   B ND1  1 
ATOM   5843 C  CD2  . HIS   B 1 119 ? 38.589 -13.022 -5.399  1.00 13.98 ?  119  HIS   B CD2  1 
ATOM   5844 C  CE1  . HIS   B 1 119 ? 39.893 -11.265 -5.535  1.00 15.06 ?  119  HIS   B CE1  1 
ATOM   5845 N  NE2  . HIS   B 1 119 ? 39.237 -12.041 -4.691  1.00 15.20 ?  119  HIS   B NE2  1 
ATOM   5846 H  H    . HIS   B 1 119 ? 35.707 -13.709 -7.400  1.00 13.01 ?  119  HIS   B H    1 
ATOM   5847 H  HA   . HIS   B 1 119 ? 37.313 -11.963 -8.716  1.00 13.31 ?  119  HIS   B HA   1 
ATOM   5848 H  HB2  . HIS   B 1 119 ? 38.220 -14.450 -7.702  1.00 13.96 ?  119  HIS   B HB2  1 
ATOM   5849 H  HB3  . HIS   B 1 119 ? 39.097 -13.475 -8.602  1.00 13.96 ?  119  HIS   B HB3  1 
ATOM   5850 H  HD2  . HIS   B 1 119 ? 38.059 -13.698 -5.044  1.00 16.79 ?  119  HIS   B HD2  1 
ATOM   5851 H  HE1  . HIS   B 1 119 ? 40.424 -10.537 -5.301  1.00 18.10 ?  119  HIS   B HE1  1 
ATOM   5852 H  HE2  . HIS   B 1 119 ? 39.241 -11.962 -3.831  1.00 18.27 ?  119  HIS   B HE2  1 
ATOM   5853 N  N    . GLU   B 1 120 ? 36.799 -13.000 -10.887 1.00 11.96 ?  120  GLU   B N    1 
ATOM   5854 C  CA   . GLU   B 1 120 ? 36.208 -13.579 -12.088 1.00 13.15 ?  120  GLU   B CA   1 
ATOM   5855 C  C    . GLU   B 1 120 ? 36.883 -14.879 -12.504 1.00 12.10 ?  120  GLU   B C    1 
ATOM   5856 O  O    . GLU   B 1 120 ? 36.219 -15.754 -13.076 1.00 12.35 ?  120  GLU   B O    1 
ATOM   5857 C  CB   . GLU   B 1 120 ? 36.232 -12.569 -13.232 1.00 17.77 ?  120  GLU   B CB   1 
ATOM   5858 C  CG   . GLU   B 1 120 ? 35.254 -11.423 -13.035 1.00 23.70 ?  120  GLU   B CG   1 
ATOM   5859 C  CD   . GLU   B 1 120 ? 35.088 -10.564 -14.271 1.00 29.71 ?  120  GLU   B CD   1 
ATOM   5860 O  OE1  . GLU   B 1 120 ? 36.082 -10.374 -15.004 1.00 32.33 ?  120  GLU   B OE1  1 
ATOM   5861 O  OE2  . GLU   B 1 120 ? 33.960 -10.082 -14.508 1.00 32.38 -1 120  GLU   B OE2  1 
ATOM   5862 H  H    . GLU   B 1 120 ? 37.230 -12.260 -11.012 1.00 14.38 ?  120  GLU   B H    1 
ATOM   5863 H  HA   . GLU   B 1 120 ? 35.283 -13.782 -11.902 1.00 15.80 ?  120  GLU   B HA   1 
ATOM   5864 H  HB2  . GLU   B 1 120 ? 37.119 -12.189 -13.308 1.00 21.34 ?  120  GLU   B HB2  1 
ATOM   5865 H  HB3  . GLU   B 1 120 ? 35.993 -13.020 -14.059 1.00 21.34 ?  120  GLU   B HB3  1 
ATOM   5866 H  HG2  . GLU   B 1 120 ? 34.381 -11.784 -12.813 1.00 28.47 ?  120  GLU   B HG2  1 
ATOM   5867 H  HG3  . GLU   B 1 120 ? 35.570 -10.853 -12.320 1.00 28.47 ?  120  GLU   B HG3  1 
ATOM   5868 N  N    . VAL   B 1 121 ? 38.183 -15.022 -12.243 1.00 11.78 ?  121  VAL   B N    1 
ATOM   5869 C  CA   . VAL   B 1 121 ? 38.928 -16.230 -12.591 1.00 11.56 ?  121  VAL   B CA   1 
ATOM   5870 C  C    . VAL   B 1 121 ? 40.040 -16.435 -11.571 1.00 10.97 ?  121  VAL   B C    1 
ATOM   5871 O  O    . VAL   B 1 121 ? 40.722 -15.481 -11.178 1.00 11.74 ?  121  VAL   B O    1 
ATOM   5872 C  CB   . VAL   B 1 121 ? 39.443 -16.186 -14.049 1.00 13.47 ?  121  VAL   B CB   1 
ATOM   5873 C  CG1  . VAL   B 1 121 ? 40.305 -14.956 -14.305 1.00 14.73 ?  121  VAL   B CG1  1 
ATOM   5874 C  CG2  . VAL   B 1 121 ? 40.181 -17.468 -14.406 1.00 14.79 ?  121  VAL   B CG2  1 
ATOM   5875 H  H    . VAL   B 1 121 ? 38.667 -14.418 -11.865 1.00 14.15 ?  121  VAL   B H    1 
ATOM   5876 H  HA   . VAL   B 1 121 ? 38.322 -16.983 -12.524 1.00 13.89 ?  121  VAL   B HA   1 
ATOM   5877 H  HB   . VAL   B 1 121 ? 38.672 -16.125 -14.641 1.00 16.19 ?  121  VAL   B HB   1 
ATOM   5878 H  HG11 . VAL   B 1 121 ? 40.614 -14.971 -15.224 1.00 17.70 ?  121  VAL   B HG11 1 
ATOM   5879 H  HG12 . VAL   B 1 121 ? 39.772 -14.158 -14.150 1.00 17.70 ?  121  VAL   B HG12 1 
ATOM   5880 H  HG13 . VAL   B 1 121 ? 41.062 -14.969 -13.700 1.00 17.70 ?  121  VAL   B HG13 1 
ATOM   5881 H  HG21 . VAL   B 1 121 ? 40.384 -17.461 -15.357 1.00 17.77 ?  121  VAL   B HG21 1 
ATOM   5882 H  HG22 . VAL   B 1 121 ? 41.004 -17.514 -13.895 1.00 17.77 ?  121  VAL   B HG22 1 
ATOM   5883 H  HG23 . VAL   B 1 121 ? 39.617 -18.229 -14.197 1.00 17.77 ?  121  VAL   B HG23 1 
ATOM   5884 N  N    . LEU   B 1 122 ? 40.219 -17.688 -11.138 1.00 10.48 ?  122  LEU   B N    1 
ATOM   5885 C  CA   . LEU   B 1 122 ? 41.202 -18.037 -10.115 1.00 10.23 ?  122  LEU   B CA   1 
ATOM   5886 C  C    . LEU   B 1 122 ? 41.856 -19.369 -10.440 1.00 10.08 ?  122  LEU   B C    1 
ATOM   5887 O  O    . LEU   B 1 122 ? 41.196 -20.288 -10.937 1.00 11.33 ?  122  LEU   B O    1 
ATOM   5888 C  CB   . LEU   B 1 122 ? 40.548 -18.276 -8.743  1.00 12.04 ?  122  LEU   B CB   1 
ATOM   5889 C  CG   . LEU   B 1 122 ? 39.522 -17.249 -8.261  1.00 12.17 ?  122  LEU   B CG   1 
ATOM   5890 C  CD1  . LEU   B 1 122 ? 38.123 -17.607 -8.737  1.00 12.61 ?  122  LEU   B CD1  1 
ATOM   5891 C  CD2  . LEU   B 1 122 ? 39.558 -17.139 -6.752  1.00 11.45 ?  122  LEU   B CD2  1 
ATOM   5892 H  H    . LEU   B 1 122 ? 39.778 -18.368 -11.431 1.00 12.60 ?  122  LEU   B H    1 
ATOM   5893 H  HA   . LEU   B 1 122 ? 41.878 -17.346 -10.036 1.00 12.30 ?  122  LEU   B HA   1 
ATOM   5894 H  HB2  . LEU   B 1 122 ? 40.100 -19.133 -8.767  1.00 14.48 ?  122  LEU   B HB2  1 
ATOM   5895 H  HB3  . LEU   B 1 122 ? 41.250 -18.300 -8.075  1.00 14.48 ?  122  LEU   B HB3  1 
ATOM   5896 H  HG   . LEU   B 1 122 ? 39.743 -16.380 -8.628  1.00 14.63 ?  122  LEU   B HG   1 
ATOM   5897 H  HD11 . LEU   B 1 122 ? 37.493 -16.963 -8.377  1.00 15.16 ?  122  LEU   B HD11 1 
ATOM   5898 H  HD12 . LEU   B 1 122 ? 38.103 -17.577 -9.708  1.00 15.16 ?  122  LEU   B HD12 1 
ATOM   5899 H  HD13 . LEU   B 1 122 ? 37.901 -18.497 -8.429  1.00 15.16 ?  122  LEU   B HD13 1 
ATOM   5900 H  HD21 . LEU   B 1 122 ? 38.877 -16.511 -6.460  1.00 13.76 ?  122  LEU   B HD21 1 
ATOM   5901 H  HD22 . LEU   B 1 122 ? 39.389 -18.012 -6.364  1.00 13.76 ?  122  LEU   B HD22 1 
ATOM   5902 H  HD23 . LEU   B 1 122 ? 40.435 -16.822 -6.480  1.00 13.76 ?  122  LEU   B HD23 1 
ATOM   5903 N  N    . LEU   B 1 123 ? 43.142 -19.478 -10.085 1.00 9.77  ?  123  LEU   B N    1 
ATOM   5904 C  CA   . LEU   B 1 123 ? 43.854 -20.746 -9.961  1.00 10.04 ?  123  LEU   B CA   1 
ATOM   5905 C  C    . LEU   B 1 123 ? 43.824 -21.136 -8.487  1.00 9.84  ?  123  LEU   B C    1 
ATOM   5906 O  O    . LEU   B 1 123 ? 44.182 -20.314 -7.638  1.00 10.35 ?  123  LEU   B O    1 
ATOM   5907 C  CB   . LEU   B 1 123 ? 45.303 -20.566 -10.423 1.00 10.81 ?  123  LEU   B CB   1 
ATOM   5908 C  CG   . LEU   B 1 123 ? 46.245 -21.749 -10.178 1.00 11.08 ?  123  LEU   B CG   1 
ATOM   5909 C  CD1  . LEU   B 1 123 ? 45.822 -22.992 -10.947 1.00 11.45 ?  123  LEU   B CD1  1 
ATOM   5910 C  CD2  . LEU   B 1 123 ? 47.660 -21.361 -10.558 1.00 11.91 ?  123  LEU   B CD2  1 
ATOM   5911 H  H    . LEU   B 1 123 ? 43.637 -18.800 -9.887  1.00 11.75 ?  123  LEU   B H    1 
ATOM   5912 H  HA   . LEU   B 1 123 ? 43.418 -21.437 -10.489 1.00 12.07 ?  123  LEU   B HA   1 
ATOM   5913 H  HB2  . LEU   B 1 123 ? 45.293 -20.399 -11.379 1.00 12.99 ?  123  LEU   B HB2  1 
ATOM   5914 H  HB3  . LEU   B 1 123 ? 45.673 -19.800 -9.964  1.00 12.99 ?  123  LEU   B HB3  1 
ATOM   5915 H  HG   . LEU   B 1 123 ? 46.243 -21.969 -9.232  1.00 13.32 ?  123  LEU   B HG   1 
ATOM   5916 H  HD11 . LEU   B 1 123 ? 46.459 -23.699 -10.774 1.00 13.76 ?  123  LEU   B HD11 1 
ATOM   5917 H  HD12 . LEU   B 1 123 ? 44.938 -23.258 -10.650 1.00 13.76 ?  123  LEU   B HD12 1 
ATOM   5918 H  HD13 . LEU   B 1 123 ? 45.804 -22.782 -11.893 1.00 13.76 ?  123  LEU   B HD13 1 
ATOM   5919 H  HD21 . LEU   B 1 123 ? 48.246 -22.118 -10.399 1.00 14.32 ?  123  LEU   B HD21 1 
ATOM   5920 H  HD22 . LEU   B 1 123 ? 47.677 -21.122 -11.498 1.00 14.32 ?  123  LEU   B HD22 1 
ATOM   5921 H  HD23 . LEU   B 1 123 ? 47.936 -20.607 -10.018 1.00 14.32 ?  123  LEU   B HD23 1 
ATOM   5922 N  N    . ALA   B 1 124 ? 43.394 -22.364 -8.173  1.00 9.64  ?  124  ALA   B N    1 
ATOM   5923 C  CA   . ALA   B 1 124 ? 43.136 -22.674 -6.776  1.00 9.90  ?  124  ALA   B CA   1 
ATOM   5924 C  C    . ALA   B 1 124 ? 43.411 -24.134 -6.458  1.00 9.77  ?  124  ALA   B C    1 
ATOM   5925 O  O    . ALA   B 1 124 ? 43.269 -25.009 -7.324  1.00 10.36 ?  124  ALA   B O    1 
ATOM   5926 C  CB   . ALA   B 1 124 ? 41.681 -22.367 -6.411  1.00 10.31 ?  124  ALA   B CB   1 
ATOM   5927 H  H    . ALA   B 1 124 ? 43.232 -23.004 -8.734  1.00 11.59 ?  124  ALA   B H    1 
ATOM   5928 H  HA   . ALA   B 1 124 ? 43.711 -22.126 -6.231  1.00 11.90 ?  124  ALA   B HA   1 
ATOM   5929 H  HB1  . ALA   B 1 124 ? 41.531 -22.580 -5.478  1.00 12.39 ?  124  ALA   B HB1  1 
ATOM   5930 H  HB2  . ALA   B 1 124 ? 41.515 -21.419 -6.562  1.00 12.39 ?  124  ALA   B HB2  1 
ATOM   5931 H  HB3  . ALA   B 1 124 ? 41.090 -22.894 -6.972  1.00 12.39 ?  124  ALA   B HB3  1 
ATOM   5932 N  N    . PRO   B 1 125 ? 43.711 -24.432 -5.196  1.00 9.89  ?  125  PRO   B N    1 
ATOM   5933 C  CA   . PRO   B 1 125 ? 43.642 -25.797 -4.674  1.00 10.62 ?  125  PRO   B CA   1 
ATOM   5934 C  C    . PRO   B 1 125 ? 42.240 -26.070 -4.132  1.00 10.43 ?  125  PRO   B C    1 
ATOM   5935 O  O    . PRO   B 1 125 ? 41.443 -25.154 -3.924  1.00 11.07 ?  125  PRO   B O    1 
ATOM   5936 C  CB   . PRO   B 1 125 ? 44.624 -25.726 -3.499  1.00 11.72 ?  125  PRO   B CB   1 
ATOM   5937 C  CG   . PRO   B 1 125 ? 44.365 -24.345 -2.923  1.00 11.65 ?  125  PRO   B CG   1 
ATOM   5938 C  CD   . PRO   B 1 125 ? 44.035 -23.466 -4.128  1.00 10.56 ?  125  PRO   B CD   1 
ATOM   5939 H  HA   . PRO   B 1 125 ? 43.918 -26.465 -5.319  1.00 12.77 ?  125  PRO   B HA   1 
ATOM   5940 H  HB2  . PRO   B 1 125 ? 44.420 -26.415 -2.842  1.00 14.08 ?  125  PRO   B HB2  1 
ATOM   5941 H  HB3  . PRO   B 1 125 ? 45.536 -25.803 -3.812  1.00 14.08 ?  125  PRO   B HB3  1 
ATOM   5942 H  HG2  . PRO   B 1 125 ? 43.612 -24.376 -2.306  1.00 14.00 ?  125  PRO   B HG2  1 
ATOM   5943 H  HG3  . PRO   B 1 125 ? 45.161 -24.021 -2.464  1.00 14.00 ?  125  PRO   B HG3  1 
ATOM   5944 H  HD2  . PRO   B 1 125 ? 43.275 -22.899 -3.936  1.00 12.69 ?  125  PRO   B HD2  1 
ATOM   5945 H  HD3  . PRO   B 1 125 ? 44.816 -22.938 -4.376  1.00 12.69 ?  125  PRO   B HD3  1 
ATOM   5946 N  N    . LEU   B 1 126 ? 41.969 -27.348 -3.856  1.00 11.19 ?  126  LEU   B N    1 
ATOM   5947 C  CA   . LEU   B 1 126 ? 40.752 -27.714 -3.141  1.00 11.74 ?  126  LEU   B CA   1 
ATOM   5948 C  C    . LEU   B 1 126 ? 40.873 -27.313 -1.679  1.00 12.01 ?  126  LEU   B C    1 
ATOM   5949 O  O    . LEU   B 1 126 ? 41.765 -27.775 -0.963  1.00 13.74 ?  126  LEU   B O    1 
ATOM   5950 C  CB   . LEU   B 1 126 ? 40.502 -29.210 -3.253  1.00 12.95 ?  126  LEU   B CB   1 
ATOM   5951 C  CG   . LEU   B 1 126 ? 39.963 -29.685 -4.605  1.00 13.82 ?  126  LEU   B CG   1 
ATOM   5952 C  CD1  . LEU   B 1 126 ? 40.017 -31.196 -4.698  1.00 15.67 ?  126  LEU   B CD1  1 
ATOM   5953 C  CD2  . LEU   B 1 126 ? 38.542 -29.193 -4.849  1.00 14.19 ?  126  LEU   B CD2  1 
ATOM   5954 H  H    . LEU   B 1 126 ? 42.474 -28.018 -4.061  1.00 13.45 ?  126  LEU   B H    1 
ATOM   5955 H  HA   . LEU   B 1 126 ? 39.998 -27.241 -3.531  1.00 14.11 ?  126  LEU   B HA   1 
ATOM   5956 H  HB2  . LEU   B 1 126 ? 41.339 -29.673 -3.096  1.00 15.56 ?  126  LEU   B HB2  1 
ATOM   5957 H  HB3  . LEU   B 1 126 ? 39.856 -29.465 -2.578  1.00 15.56 ?  126  LEU   B HB3  1 
ATOM   5958 H  HG   . LEU   B 1 126 ? 40.527 -29.326 -5.309  1.00 16.61 ?  126  LEU   B HG   1 
ATOM   5959 H  HD11 . LEU   B 1 126 ? 39.670 -31.472 -5.561  1.00 18.82 ?  126  LEU   B HD11 1 
ATOM   5960 H  HD12 . LEU   B 1 126 ? 40.935 -31.488 -4.599  1.00 18.82 ?  126  LEU   B HD12 1 
ATOM   5961 H  HD13 . LEU   B 1 126 ? 39.471 -31.575 -3.988  1.00 18.82 ?  126  LEU   B HD13 1 
ATOM   5962 H  HD21 . LEU   B 1 126 ? 38.200 -29.607 -5.658  1.00 17.05 ?  126  LEU   B HD21 1 
ATOM   5963 H  HD22 . LEU   B 1 126 ? 37.988 -29.437 -4.093  1.00 17.05 ?  126  LEU   B HD22 1 
ATOM   5964 H  HD23 . LEU   B 1 126 ? 38.553 -28.228 -4.954  1.00 17.05 ?  126  LEU   B HD23 1 
ATOM   5965 N  N    . LEU   B 1 127 ? 39.946 -26.482 -1.224  1.00 12.18 ?  127  LEU   B N    1 
ATOM   5966 C  CA   . LEU   B 1 127 ? 39.999 -25.991 0.139   1.00 12.56 ?  127  LEU   B CA   1 
ATOM   5967 C  C    . LEU   B 1 127 ? 39.725 -27.112 1.133   1.00 12.16 ?  127  LEU   B C    1 
ATOM   5968 O  O    . LEU   B 1 127 ? 38.906 -28.008 0.904   1.00 12.43 ?  127  LEU   B O    1 
ATOM   5969 C  CB   . LEU   B 1 127 ? 38.977 -24.874 0.344   1.00 12.86 ?  127  LEU   B CB   1 
ATOM   5970 C  CG   . LEU   B 1 127 ? 39.161 -23.604 -0.484  1.00 13.22 ?  127  LEU   B CG   1 
ATOM   5971 C  CD1  . LEU   B 1 127 ? 38.041 -22.628 -0.165  1.00 13.53 ?  127  LEU   B CD1  1 
ATOM   5972 C  CD2  . LEU   B 1 127 ? 40.527 -22.966 -0.236  1.00 13.81 ?  127  LEU   B CD2  1 
ATOM   5973 H  H    . LEU   B 1 127 ? 39.276 -26.186 -1.683  1.00 14.64 ?  127  LEU   B H    1 
ATOM   5974 H  HA   . LEU   B 1 127 ? 40.882 -25.632 0.314   1.00 15.10 ?  127  LEU   B HA   1 
ATOM   5975 H  HB2  . LEU   B 1 127 ? 38.097 -25.224 0.135   1.00 15.46 ?  127  LEU   B HB2  1 
ATOM   5976 H  HB3  . LEU   B 1 127 ? 39.001 -24.607 1.276   1.00 15.46 ?  127  LEU   B HB3  1 
ATOM   5977 H  HG   . LEU   B 1 127 ? 39.091 -23.821 -1.426  1.00 15.89 ?  127  LEU   B HG   1 
ATOM   5978 H  HD11 . LEU   B 1 127 ? 38.167 -21.814 -0.687  1.00 16.26 ?  127  LEU   B HD11 1 
ATOM   5979 H  HD12 . LEU   B 1 127 ? 37.188 -23.029 -0.387  1.00 16.26 ?  127  LEU   B HD12 1 
ATOM   5980 H  HD13 . LEU   B 1 127 ? 38.068 -22.410 0.782   1.00 16.26 ?  127  LEU   B HD13 1 
ATOM   5981 H  HD21 . LEU   B 1 127 ? 40.566 -22.107 -0.685  1.00 16.60 ?  127  LEU   B HD21 1 
ATOM   5982 H  HD22 . LEU   B 1 127 ? 40.649 -22.843 0.721   1.00 16.60 ?  127  LEU   B HD22 1 
ATOM   5983 H  HD23 . LEU   B 1 127 ? 41.214 -23.554 -0.583  1.00 16.60 ?  127  LEU   B HD23 1 
ATOM   5984 N  N    . SER   B 1 128 ? 40.402 -27.021 2.269   1.00 12.23 ?  128  SER   B N    1 
ATOM   5985 C  CA   . SER   B 1 128 ? 40.292 -27.938 3.393   1.00 12.85 ?  128  SER   B CA   1 
ATOM   5986 C  C    . SER   B 1 128 ? 40.784 -29.345 3.071   1.00 14.02 ?  128  SER   B C    1 
ATOM   5987 O  O    . SER   B 1 128 ? 40.685 -30.229 3.924   1.00 15.47 ?  128  SER   B O    1 
ATOM   5988 C  CB   . SER   B 1 128 ? 38.890 -27.945 4.018   1.00 13.00 ?  128  SER   B CB   1 
ATOM   5989 O  OG   . SER   B 1 128 ? 38.583 -26.663 4.562   1.00 13.63 ?  128  SER   B OG   1 
ATOM   5990 H  H    . SER   B 1 128 ? 40.964 -26.384 2.420   1.00 14.70 ?  128  SER   B H    1 
ATOM   5991 H  HA   . SER   B 1 128 ? 40.881 -27.602 4.078   1.00 15.44 ?  128  SER   B HA   1 
ATOM   5992 H  HB2  . SER   B 1 128 ? 38.234 -28.175 3.340   1.00 15.62 ?  128  SER   B HB2  1 
ATOM   5993 H  HB3  . SER   B 1 128 ? 38.867 -28.611 4.733   1.00 15.62 ?  128  SER   B HB3  1 
ATOM   5994 H  HG   . SER   B 1 128 ? 39.155 -26.466 5.146   1.00 16.38 ?  128  SER   B HG   1 
ATOM   5995 N  N    . ALA   B 1 129 ? 41.360 -29.564 1.887   1.00 15.15 ?  129  ALA   B N    1 
ATOM   5996 C  CA   . ALA   B 1 129 ? 41.896 -30.866 1.527   1.00 15.55 ?  129  ALA   B CA   1 
ATOM   5997 C  C    . ALA   B 1 129 ? 43.289 -31.048 2.115   1.00 14.77 ?  129  ALA   B C    1 
ATOM   5998 O  O    . ALA   B 1 129 ? 43.852 -30.149 2.755   1.00 14.51 ?  129  ALA   B O    1 
ATOM   5999 C  CB   . ALA   B 1 129 ? 41.944 -31.023 0.010   1.00 17.59 ?  129  ALA   B CB   1 
ATOM   6000 H  H    . ALA   B 1 129 ? 41.452 -28.966 1.269   1.00 18.20 ?  129  ALA   B H    1 
ATOM   6001 H  HA   . ALA   B 1 129 ? 41.321 -31.553 1.887   1.00 18.68 ?  129  ALA   B HA   1 
ATOM   6002 H  HB1  . ALA   B 1 129 ? 42.294 -31.902 -0.203  1.00 21.13 ?  129  ALA   B HB1  1 
ATOM   6003 H  HB2  . ALA   B 1 129 ? 41.048 -30.927 -0.342  1.00 21.13 ?  129  ALA   B HB2  1 
ATOM   6004 H  HB3  . ALA   B 1 129 ? 42.523 -30.338 -0.360  1.00 21.13 ?  129  ALA   B HB3  1 
ATOM   6005 N  N    . GLY   B 1 130 ? 43.852 -32.231 1.877   1.00 14.76 ?  130  GLY   B N    1 
ATOM   6006 C  CA   . GLY   B 1 130 ? 45.240 -32.471 2.222   1.00 15.22 ?  130  GLY   B CA   1 
ATOM   6007 C  C    . GLY   B 1 130 ? 45.458 -32.377 3.712   1.00 15.47 ?  130  GLY   B C    1 
ATOM   6008 O  O    . GLY   B 1 130 ? 44.761 -33.019 4.511   1.00 16.12 ?  130  GLY   B O    1 
ATOM   6009 H  H    . GLY   B 1 130 ? 43.455 -32.900 1.511   1.00 17.73 ?  130  GLY   B H    1 
ATOM   6010 H  HA2  . GLY   B 1 130 ? 45.501 -33.360 1.925   1.00 18.29 ?  130  GLY   B HA2  1 
ATOM   6011 H  HA3  . GLY   B 1 130 ? 45.806 -31.820 1.782   1.00 18.29 ?  130  GLY   B HA3  1 
ATOM   6012 N  N    . ILE   B 1 131 ? 46.437 -31.552 4.097   1.00 16.12 ?  131  ILE   B N    1 
ATOM   6013 C  CA   . ILE   B 1 131 ? 46.800 -31.420 5.501   1.00 17.02 ?  131  ILE   B CA   1 
ATOM   6014 C  C    . ILE   B 1 131 ? 45.688 -30.817 6.340   1.00 16.01 ?  131  ILE   B C    1 
ATOM   6015 O  O    . ILE   B 1 131 ? 45.759 -30.892 7.570   1.00 17.39 ?  131  ILE   B O    1 
ATOM   6016 C  CB   . ILE   B 1 131 ? 48.125 -30.648 5.697   1.00 18.74 ?  131  ILE   B CB   1 
ATOM   6017 C  CG1  . ILE   B 1 131 ? 47.966 -29.169 5.319   1.00 19.73 ?  131  ILE   B CG1  1 
ATOM   6018 C  CG2  . ILE   B 1 131 ? 49.243 -31.292 4.885   1.00 19.75 ?  131  ILE   B CG2  1 
ATOM   6019 C  CD1  . ILE   B 1 131 ? 49.186 -28.319 5.620   1.00 20.81 ?  131  ILE   B CD1  1 
ATOM   6020 H  H    . ILE   B 1 131 ? 46.907 -31.063 3.563   1.00 19.37 ?  131  ILE   B H    1 
ATOM   6021 H  HA   . ILE   B 1 131 ? 46.948 -32.310 5.847   1.00 20.44 ?  131  ILE   B HA   1 
ATOM   6022 H  HB   . ILE   B 1 131 ? 48.364 -30.695 6.637   1.00 22.51 ?  131  ILE   B HB   1 
ATOM   6023 H  HG12 . ILE   B 1 131 ? 47.788 -29.111 4.368   1.00 23.70 ?  131  ILE   B HG12 1 
ATOM   6024 H  HG13 . ILE   B 1 131 ? 47.220 -28.791 5.814   1.00 23.70 ?  131  ILE   B HG13 1 
ATOM   6025 H  HG21 . ILE   B 1 131 ? 50.088 -30.896 5.145   1.00 23.72 ?  131  ILE   B HG21 1 
ATOM   6026 H  HG22 . ILE   B 1 131 ? 49.250 -32.243 5.065   1.00 23.72 ?  131  ILE   B HG22 1 
ATOM   6027 H  HG23 . ILE   B 1 131 ? 49.075 -31.133 3.943   1.00 23.72 ?  131  ILE   B HG23 1 
ATOM   6028 H  HD11 . ILE   B 1 131 ? 48.970 -27.389 5.451   1.00 25.00 ?  131  ILE   B HD11 1 
ATOM   6029 H  HD12 . ILE   B 1 131 ? 49.430 -28.437 6.552   1.00 25.00 ?  131  ILE   B HD12 1 
ATOM   6030 H  HD13 . ILE   B 1 131 ? 49.916 -28.600 5.048   1.00 25.00 ?  131  ILE   B HD13 1 
ATOM   6031 N  N    . PHE   B 1 132 ? 44.656 -30.240 5.714   1.00 14.71 ?  132  PHE   B N    1 
ATOM   6032 C  CA   . PHE   B 1 132 ? 43.499 -29.738 6.446   1.00 14.82 ?  132  PHE   B CA   1 
ATOM   6033 C  C    . PHE   B 1 132 ? 42.472 -30.824 6.764   1.00 16.24 ?  132  PHE   B C    1 
ATOM   6034 O  O    . PHE   B 1 132 ? 41.560 -30.569 7.558   1.00 17.77 ?  132  PHE   B O    1 
ATOM   6035 C  CB   . PHE   B 1 132 ? 42.822 -28.605 5.667   1.00 13.98 ?  132  PHE   B CB   1 
ATOM   6036 C  CG   . PHE   B 1 132 ? 43.515 -27.261 5.780   1.00 13.49 ?  132  PHE   B CG   1 
ATOM   6037 C  CD1  . PHE   B 1 132 ? 44.809 -27.076 5.317   1.00 14.78 ?  132  PHE   B CD1  1 
ATOM   6038 C  CD2  . PHE   B 1 132 ? 42.836 -26.168 6.298   1.00 13.22 ?  132  PHE   B CD2  1 
ATOM   6039 C  CE1  . PHE   B 1 132 ? 45.427 -25.835 5.410   1.00 15.21 ?  132  PHE   B CE1  1 
ATOM   6040 C  CE2  . PHE   B 1 132 ? 43.440 -24.926 6.385   1.00 13.69 ?  132  PHE   B CE2  1 
ATOM   6041 C  CZ   . PHE   B 1 132 ? 44.736 -24.761 5.941   1.00 14.78 ?  132  PHE   B CZ   1 
ATOM   6042 H  H    . PHE   B 1 132 ? 44.603 -30.131 4.863   1.00 17.68 ?  132  PHE   B H    1 
ATOM   6043 H  HA   . PHE   B 1 132 ? 43.803 -29.374 7.289   1.00 17.80 ?  132  PHE   B HA   1 
ATOM   6044 H  HB2  . PHE   B 1 132 ? 42.808 -28.846 4.731   1.00 16.80 ?  132  PHE   B HB2  1 
ATOM   6045 H  HB3  . PHE   B 1 132 ? 41.915 -28.502 5.997   1.00 16.80 ?  132  PHE   B HB3  1 
ATOM   6046 H  HD1  . PHE   B 1 132 ? 45.277 -27.802 4.965   1.00 17.76 ?  132  PHE   B HD1  1 
ATOM   6047 H  HD2  . PHE   B 1 132 ? 41.961 -26.277 6.603   1.00 15.89 ?  132  PHE   B HD2  1 
ATOM   6048 H  HE1  . PHE   B 1 132 ? 46.298 -25.726 5.110   1.00 18.28 ?  132  PHE   B HE1  1 
ATOM   6049 H  HE2  . PHE   B 1 132 ? 42.972 -24.206 6.750   1.00 16.45 ?  132  PHE   B HE2  1 
ATOM   6050 H  HZ   . PHE   B 1 132 ? 45.141 -23.925 6.007   1.00 17.76 ?  132  PHE   B HZ   1 
ATOM   6051 N  N    . GLY   B 1 133 ? 42.576 -32.015 6.164   1.00 15.94 ?  133  GLY   B N    1 
ATOM   6052 C  CA   . GLY   B 1 133 ? 41.861 -33.179 6.653   1.00 17.00 ?  133  GLY   B CA   1 
ATOM   6053 C  C    . GLY   B 1 133 ? 40.469 -33.439 6.111   1.00 17.54 ?  133  GLY   B C    1 
ATOM   6054 O  O    . GLY   B 1 133 ? 39.887 -34.470 6.460   1.00 19.29 ?  133  GLY   B O    1 
ATOM   6055 H  H    . GLY   B 1 133 ? 43.064 -32.169 5.470   1.00 19.15 ?  133  GLY   B H    1 
ATOM   6056 H  HA2  . GLY   B 1 133 ? 42.395 -33.966 6.464   1.00 20.42 ?  133  GLY   B HA2  1 
ATOM   6057 H  HA3  . GLY   B 1 133 ? 41.780 -33.104 7.615   1.00 20.42 ?  133  GLY   B HA3  1 
ATOM   6058 N  N    . ALA   B 1 134 ? 39.900 -32.561 5.293   1.00 16.70 ?  134  ALA   B N    1 
ATOM   6059 C  CA   . ALA   B 1 134 ? 38.575 -32.848 4.765   1.00 16.60 ?  134  ALA   B CA   1 
ATOM   6060 C  C    . ALA   B 1 134 ? 38.658 -33.847 3.616   1.00 16.57 ?  134  ALA   B C    1 
ATOM   6061 O  O    . ALA   B 1 134 ? 39.714 -34.053 3.009   1.00 17.32 ?  134  ALA   B O    1 
ATOM   6062 C  CB   . ALA   B 1 134 ? 37.888 -31.569 4.288   1.00 17.26 ?  134  ALA   B CB   1 
ATOM   6063 H  H    . ALA   B 1 134 ? 40.242 -31.808 5.041   1.00 20.07 ?  134  ALA   B H    1 
ATOM   6064 H  HA   . ALA   B 1 134 ? 38.028 -33.233 5.469   1.00 19.94 ?  134  ALA   B HA   1 
ATOM   6065 H  HB1  . ALA   B 1 134 ? 37.001 -31.790 3.961   1.00 20.74 ?  134  ALA   B HB1  1 
ATOM   6066 H  HB2  . ALA   B 1 134 ? 37.818 -30.950 5.033   1.00 20.74 ?  134  ALA   B HB2  1 
ATOM   6067 H  HB3  . ALA   B 1 134 ? 38.414 -31.173 3.577   1.00 20.74 ?  134  ALA   B HB3  1 
ATOM   6068 N  N    . ASP   B 1 135 ? 37.522 -34.469 3.326   1.00 16.97 ?  135  ASP   B N    1 
ATOM   6069 C  CA   . ASP   B 1 135 ? 37.423 -35.364 2.185   1.00 17.54 ?  135  ASP   B CA   1 
ATOM   6070 C  C    . ASP   B 1 135 ? 37.526 -34.526 0.918   1.00 16.34 ?  135  ASP   B C    1 
ATOM   6071 O  O    . ASP   B 1 135 ? 36.668 -33.658 0.690   1.00 16.18 ?  135  ASP   B O    1 
ATOM   6072 C  CB   . ASP   B 1 135 ? 36.078 -36.088 2.236   1.00 19.25 ?  135  ASP   B CB   1 
ATOM   6073 C  CG   . ASP   B 1 135 ? 35.903 -37.087 1.112   1.00 21.25 ?  135  ASP   B CG   1 
ATOM   6074 O  OD1  . ASP   B 1 135 ? 36.765 -37.132 0.209   1.00 20.71 ?  135  ASP   B OD1  1 
ATOM   6075 O  OD2  . ASP   B 1 135 ? 34.908 -37.847 1.142   1.00 23.95 -1 135  ASP   B OD2  1 
ATOM   6076 H  H    . ASP   B 1 135 ? 36.790 -34.387 3.774   1.00 20.38 ?  135  ASP   B H    1 
ATOM   6077 H  HA   . ASP   B 1 135 ? 38.139 -36.020 2.218   1.00 21.07 ?  135  ASP   B HA   1 
ATOM   6078 H  HB2  . ASP   B 1 135 ? 36.013 -36.568 3.075   1.00 23.12 ?  135  ASP   B HB2  1 
ATOM   6079 H  HB3  . ASP   B 1 135 ? 35.370 -35.432 2.169   1.00 23.12 ?  135  ASP   B HB3  1 
ATOM   6080 N  N    . PRO   B 1 136 ? 38.543 -34.727 0.076   1.00 16.67 ?  136  PRO   B N    1 
ATOM   6081 C  CA   . PRO   B 1 136 ? 38.639 -33.906 -1.140  1.00 15.51 ?  136  PRO   B CA   1 
ATOM   6082 C  C    . PRO   B 1 136 ? 37.444 -34.059 -2.061  1.00 15.04 ?  136  PRO   B C    1 
ATOM   6083 O  O    . PRO   B 1 136 ? 37.118 -33.112 -2.784  1.00 14.27 ?  136  PRO   B O    1 
ATOM   6084 C  CB   . PRO   B 1 136 ? 39.948 -34.380 -1.790  1.00 16.85 ?  136  PRO   B CB   1 
ATOM   6085 C  CG   . PRO   B 1 136 ? 40.165 -35.759 -1.239  1.00 18.20 ?  136  PRO   B CG   1 
ATOM   6086 C  CD   . PRO   B 1 136 ? 39.635 -35.712 0.164   1.00 17.81 ?  136  PRO   B CD   1 
ATOM   6087 H  HA   . PRO   B 1 136 ? 38.728 -32.972 -0.905  1.00 18.63 ?  136  PRO   B HA   1 
ATOM   6088 H  HB2  . PRO   B 1 136 ? 39.848 -34.407 -2.756  1.00 20.24 ?  136  PRO   B HB2  1 
ATOM   6089 H  HB3  . PRO   B 1 136 ? 40.672 -33.788 -1.536  1.00 20.24 ?  136  PRO   B HB3  1 
ATOM   6090 H  HG2  . PRO   B 1 136 ? 39.673 -36.408 -1.768  1.00 21.87 ?  136  PRO   B HG2  1 
ATOM   6091 H  HG3  . PRO   B 1 136 ? 41.114 -35.968 -1.239  1.00 21.87 ?  136  PRO   B HG3  1 
ATOM   6092 H  HD2  . PRO   B 1 136 ? 39.290 -36.579 0.426   1.00 21.39 ?  136  PRO   B HD2  1 
ATOM   6093 H  HD3  . PRO   B 1 136 ? 40.320 -35.400 0.779   1.00 21.39 ?  136  PRO   B HD3  1 
ATOM   6094 N  N    . ILE   B 1 137 ? 36.783 -35.220 -2.058  1.00 15.50 ?  137  ILE   B N    1 
ATOM   6095 C  CA   . ILE   B 1 137 ? 35.567 -35.392 -2.848  1.00 15.92 ?  137  ILE   B CA   1 
ATOM   6096 C  C    . ILE   B 1 137 ? 34.493 -34.422 -2.375  1.00 15.51 ?  137  ILE   B C    1 
ATOM   6097 O  O    . ILE   B 1 137 ? 33.779 -33.811 -3.180  1.00 15.15 ?  137  ILE   B O    1 
ATOM   6098 C  CB   . ILE   B 1 137 ? 35.098 -36.861 -2.783  1.00 18.13 ?  137  ILE   B CB   1 
ATOM   6099 C  CG1  . ILE   B 1 137 ? 36.107 -37.768 -3.493  1.00 20.76 ?  137  ILE   B CG1  1 
ATOM   6100 C  CG2  . ILE   B 1 137 ? 33.705 -37.010 -3.393  1.00 18.65 ?  137  ILE   B CG2  1 
ATOM   6101 C  CD1  . ILE   B 1 137 ? 35.801 -39.248 -3.369  1.00 23.02 ?  137  ILE   B CD1  1 
ATOM   6102 H  H    . ILE   B 1 137 ? 37.018 -35.919 -1.616  1.00 18.62 ?  137  ILE   B H    1 
ATOM   6103 H  HA   . ILE   B 1 137 ? 35.761 -35.190 -3.778  1.00 19.12 ?  137  ILE   B HA   1 
ATOM   6104 H  HB   . ILE   B 1 137 ? 35.047 -37.126 -1.856  1.00 21.78 ?  137  ILE   B HB   1 
ATOM   6105 H  HG12 . ILE   B 1 137 ? 36.116 -37.549 -4.438  1.00 24.94 ?  137  ILE   B HG12 1 
ATOM   6106 H  HG13 . ILE   B 1 137 ? 36.983 -37.617 -3.111  1.00 24.94 ?  137  ILE   B HG13 1 
ATOM   6107 H  HG21 . ILE   B 1 137 ? 33.479 -37.951 -3.461  1.00 22.40 ?  137  ILE   B HG21 1 
ATOM   6108 H  HG22 . ILE   B 1 137 ? 33.056 -36.567 -2.824  1.00 22.40 ?  137  ILE   B HG22 1 
ATOM   6109 H  HG23 . ILE   B 1 137 ? 33.700 -36.608 -4.276  1.00 22.40 ?  137  ILE   B HG23 1 
ATOM   6110 H  HD11 . ILE   B 1 137 ? 36.539 -39.745 -3.749  1.00 27.65 ?  137  ILE   B HD11 1 
ATOM   6111 H  HD12 . ILE   B 1 137 ? 35.695 -39.473 -2.431  1.00 27.65 ?  137  ILE   B HD12 1 
ATOM   6112 H  HD13 . ILE   B 1 137 ? 34.986 -39.452 -3.854  1.00 27.65 ?  137  ILE   B HD13 1 
ATOM   6113 N  N    . HIS   B 1 138 ? 34.358 -34.272 -1.061  1.00 15.51 ?  138  HIS   B N    1 
ATOM   6114 C  CA   . HIS   B 1 138 ? 33.412 -33.304 -0.529  1.00 15.77 ?  138  HIS   B CA   1 
ATOM   6115 C  C    . HIS   B 1 138 ? 33.834 -31.875 -0.848  1.00 14.92 ?  138  HIS   B C    1 
ATOM   6116 O  O    . HIS   B 1 138 ? 32.989 -31.029 -1.151  1.00 15.36 ?  138  HIS   B O    1 
ATOM   6117 C  CB   . HIS   B 1 138 ? 33.283 -33.487 0.975   1.00 17.28 ?  138  HIS   B CB   1 
ATOM   6118 C  CG   . HIS   B 1 138 ? 32.358 -32.503 1.611   1.00 18.40 ?  138  HIS   B CG   1 
ATOM   6119 N  ND1  . HIS   B 1 138 ? 31.020 -32.423 1.287   1.00 19.83 ?  138  HIS   B ND1  1 
ATOM   6120 C  CD2  . HIS   B 1 138 ? 32.584 -31.531 2.525   1.00 18.95 ?  138  HIS   B CD2  1 
ATOM   6121 C  CE1  . HIS   B 1 138 ? 30.457 -31.456 1.990   1.00 19.89 ?  138  HIS   B CE1  1 
ATOM   6122 N  NE2  . HIS   B 1 138 ? 31.384 -30.899 2.750   1.00 19.18 ?  138  HIS   B NE2  1 
ATOM   6123 H  H    . HIS   B 1 138 ? 34.795 -34.717 -0.470  1.00 18.64 ?  138  HIS   B H    1 
ATOM   6124 H  HA   . HIS   B 1 138 ? 32.540 -33.463 -0.930  1.00 18.94 ?  138  HIS   B HA   1 
ATOM   6125 H  HB2  . HIS   B 1 138 ? 32.936 -34.377 1.154   1.00 20.76 ?  138  HIS   B HB2  1 
ATOM   6126 H  HB3  . HIS   B 1 138 ? 34.154 -33.383 1.380   1.00 20.76 ?  138  HIS   B HB3  1 
ATOM   6127 H  HD1  . HIS   B 1 138 ? 30.613 -32.929 0.720   1.00 23.81 ?  138  HIS   B HD1  1 
ATOM   6128 H  HD2  . HIS   B 1 138 ? 33.390 -31.337 2.937   1.00 22.77 ?  138  HIS   B HD2  1 
ATOM   6129 H  HE1  . HIS   B 1 138 ? 29.557 -31.216 1.957   1.00 23.90 ?  138  HIS   B HE1  1 
ATOM   6130 N  N    . SER   B 1 139 ? 35.130 -31.580 -0.779  1.00 14.39 ?  139  SER   B N    1 
ATOM   6131 C  CA   . SER   B 1 139 ? 35.573 -30.231 -1.099  1.00 13.83 ?  139  SER   B CA   1 
ATOM   6132 C  C    . SER   B 1 139 ? 35.239 -29.881 -2.538  1.00 12.89 ?  139  SER   B C    1 
ATOM   6133 O  O    . SER   B 1 139 ? 34.793 -28.768 -2.817  1.00 12.99 ?  139  SER   B O    1 
ATOM   6134 C  CB   . SER   B 1 139 ? 37.068 -30.095 -0.838  1.00 14.21 ?  139  SER   B CB   1 
ATOM   6135 O  OG   . SER   B 1 139 ? 37.475 -28.758 -1.076  1.00 14.21 ?  139  SER   B OG   1 
ATOM   6136 H  H    . SER   B 1 139 ? 35.750 -32.127 -0.569  1.00 17.29 ?  139  SER   B H    1 
ATOM   6137 H  HA   . SER   B 1 139 ? 35.101 -29.606 -0.533  1.00 16.62 ?  139  SER   B HA   1 
ATOM   6138 H  HB2  . SER   B 1 139 ? 37.245 -30.324 0.086   1.00 17.08 ?  139  SER   B HB2  1 
ATOM   6139 H  HB3  . SER   B 1 139 ? 37.552 -30.686 -1.433  1.00 17.08 ?  139  SER   B HB3  1 
ATOM   6140 H  HG   . SER   B 1 139 ? 38.300 -28.681 -0.926  1.00 17.07 ?  139  SER   B HG   1 
ATOM   6141 N  N    . LEU   B 1 140 ? 35.425 -30.823 -3.463  1.00 12.73 ?  140  LEU   B N    1 
ATOM   6142 C  CA   . LEU   B 1 140 ? 35.059 -30.575 -4.849  1.00 13.16 ?  140  LEU   B CA   1 
ATOM   6143 C  C    . LEU   B 1 140 ? 33.557 -30.351 -4.980  1.00 13.15 ?  140  LEU   B C    1 
ATOM   6144 O  O    . LEU   B 1 140 ? 33.120 -29.466 -5.719  1.00 13.02 ?  140  LEU   B O    1 
ATOM   6145 C  CB   . LEU   B 1 140 ? 35.527 -31.738 -5.721  1.00 12.88 ?  140  LEU   B CB   1 
ATOM   6146 C  CG   . LEU   B 1 140 ? 35.167 -31.636 -7.193  1.00 13.13 ?  140  LEU   B CG   1 
ATOM   6147 C  CD1  . LEU   B 1 140 ? 35.735 -30.374 -7.794  1.00 14.21 ?  140  LEU   B CD1  1 
ATOM   6148 C  CD2  . LEU   B 1 140 ? 35.647 -32.869 -7.930  1.00 14.81 ?  140  LEU   B CD2  1 
ATOM   6149 H  H    . LEU   B 1 140 ? 35.747 -31.602 -3.318  1.00 15.30 ?  140  LEU   B H    1 
ATOM   6150 H  HA   . LEU   B 1 140 ? 35.511 -29.772 -5.158  1.00 15.82 ?  140  LEU   B HA   1 
ATOM   6151 H  HB2  . LEU   B 1 140 ? 36.494 -31.800 -5.665  1.00 15.48 ?  140  LEU   B HB2  1 
ATOM   6152 H  HB3  . LEU   B 1 140 ? 35.129 -32.556 -5.390  1.00 15.48 ?  140  LEU   B HB3  1 
ATOM   6153 H  HG   . LEU   B 1 140 ? 34.206 -31.589 -7.282  1.00 15.78 ?  140  LEU   B HG   1 
ATOM   6154 H  HD11 . LEU   B 1 140 ? 35.627 -30.409 -8.756  1.00 17.07 ?  140  LEU   B HD11 1 
ATOM   6155 H  HD12 . LEU   B 1 140 ? 35.253 -29.609 -7.435  1.00 17.07 ?  140  LEU   B HD12 1 
ATOM   6156 H  HD13 . LEU   B 1 140 ? 36.674 -30.310 -7.566  1.00 17.07 ?  140  LEU   B HD13 1 
ATOM   6157 H  HD21 . LEU   B 1 140 ? 35.408 -32.787 -8.867  1.00 17.80 ?  140  LEU   B HD21 1 
ATOM   6158 H  HD22 . LEU   B 1 140 ? 36.605 -32.942 -7.834  1.00 17.80 ?  140  LEU   B HD22 1 
ATOM   6159 H  HD23 . LEU   B 1 140 ? 35.210 -33.645 -7.545  1.00 17.80 ?  140  LEU   B HD23 1 
ATOM   6160 N  N    . ARG   B 1 141 ? 32.756 -31.142 -4.263  1.00 13.23 ?  141  ARG   B N    1 
ATOM   6161 C  CA   . ARG   B 1 141 ? 31.307 -30.965 -4.243  1.00 14.40 ?  141  ARG   B CA   1 
ATOM   6162 C  C    . ARG   B 1 141 ? 30.931 -29.553 -3.818  1.00 13.95 ?  141  ARG   B C    1 
ATOM   6163 O  O    . ARG   B 1 141 ? 30.132 -28.876 -4.482  1.00 13.84 ?  141  ARG   B O    1 
ATOM   6164 C  CB   . ARG   B 1 141 ? 30.725 -31.990 -3.261  1.00 15.76 ?  141  ARG   B CB   1 
ATOM   6165 C  CG   . ARG   B 1 141 ? 29.262 -31.875 -2.938  1.00 17.37 ?  141  ARG   B CG   1 
ATOM   6166 C  CD   . ARG   B 1 141 ? 28.472 -32.518 -4.004  1.00 18.80 ?  141  ARG   B CD   1 
ATOM   6167 N  NE   . ARG   B 1 141 ? 28.214 -31.607 -5.107  1.00 19.01 ?  141  ARG   B NE   1 
ATOM   6168 C  CZ   . ARG   B 1 141 ? 28.196 -31.958 -6.385  1.00 18.35 ?  141  ARG   B CZ   1 
ATOM   6169 N  NH1  . ARG   B 1 141 ? 28.599 -33.155 -6.781  1.00 17.87 ?  141  ARG   B NH1  1 
ATOM   6170 N  NH2  . ARG   B 1 141 ? 27.760 -31.087 -7.288  1.00 19.38 ?  141  ARG   B NH2  1 
ATOM   6171 H  H    . ARG   B 1 141 ? 33.037 -31.789 -3.780  1.00 15.90 ?  141  ARG   B H    1 
ATOM   6172 H  HA   . ARG   B 1 141 ? 30.942 -31.128 -5.123  1.00 17.30 ?  141  ARG   B HA   1 
ATOM   6173 H  HB2  . ARG   B 1 141 ? 30.883 -32.875 -3.626  1.00 18.94 ?  141  ARG   B HB2  1 
ATOM   6174 H  HB3  . ARG   B 1 141 ? 31.208 -31.909 -2.424  1.00 18.94 ?  141  ARG   B HB3  1 
ATOM   6175 H  HG2  . ARG   B 1 141 ? 29.089 -32.321 -2.098  1.00 20.87 ?  141  ARG   B HG2  1 
ATOM   6176 H  HG3  . ARG   B 1 141 ? 29.007 -30.936 -2.878  1.00 20.87 ?  141  ARG   B HG3  1 
ATOM   6177 H  HD2  . ARG   B 1 141 ? 28.957 -33.294 -4.336  1.00 22.59 ?  141  ARG   B HD2  1 
ATOM   6178 H  HD3  . ARG   B 1 141 ? 27.628 -32.797 -3.635  1.00 22.59 ?  141  ARG   B HD3  1 
ATOM   6179 H  HE   . ARG   B 1 141 ? 28.053 -30.785 -4.915  1.00 22.83 ?  141  ARG   B HE   1 
ATOM   6180 H  HH11 . ARG   B 1 141 ? 28.875 -33.738 -6.210  1.00 21.47 ?  141  ARG   B HH11 1 
ATOM   6181 H  HH12 . ARG   B 1 141 ? 28.584 -33.358 -7.615  1.00 21.47 ?  141  ARG   B HH12 1 
ATOM   6182 H  HH21 . ARG   B 1 141 ? 27.508 -30.303 -7.043  1.00 23.28 ?  141  ARG   B HH21 1 
ATOM   6183 H  HH22 . ARG   B 1 141 ? 27.762 -31.297 -8.123  1.00 23.28 ?  141  ARG   B HH22 1 
ATOM   6184 N  N    . VAL   B 1 142 ? 31.475 -29.104 -2.691  1.00 13.66 ?  142  VAL   B N    1 
ATOM   6185 C  CA   . VAL   B 1 142 ? 31.138 -27.772 -2.208  1.00 13.49 ?  142  VAL   B CA   1 
ATOM   6186 C  C    . VAL   B 1 142 ? 31.618 -26.714 -3.194  1.00 13.14 ?  142  VAL   B C    1 
ATOM   6187 O  O    . VAL   B 1 142 ? 30.919 -25.729 -3.456  1.00 13.47 ?  142  VAL   B O    1 
ATOM   6188 C  CB   . VAL   B 1 142 ? 31.687 -27.548 -0.788  1.00 14.06 ?  142  VAL   B CB   1 
ATOM   6189 C  CG1  . VAL   B 1 142 ? 31.364 -26.134 -0.305  1.00 13.64 ?  142  VAL   B CG1  1 
ATOM   6190 C  CG2  . VAL   B 1 142 ? 31.115 -28.584 0.162   1.00 14.89 ?  142  VAL   B CG2  1 
ATOM   6191 H  H    . VAL   B 1 142 ? 32.032 -29.534 -2.199  1.00 16.41 ?  142  VAL   B H    1 
ATOM   6192 H  HA   . VAL   B 1 142 ? 30.175 -27.698 -2.156  1.00 16.21 ?  142  VAL   B HA   1 
ATOM   6193 H  HB   . VAL   B 1 142 ? 32.653 -27.647 -0.799  1.00 16.89 ?  142  VAL   B HB   1 
ATOM   6194 H  HG11 . VAL   B 1 142 ? 31.555 -26.077 0.643   1.00 16.39 ?  142  VAL   B HG11 1 
ATOM   6195 H  HG12 . VAL   B 1 142 ? 31.911 -25.499 -0.792  1.00 16.39 ?  142  VAL   B HG12 1 
ATOM   6196 H  HG13 . VAL   B 1 142 ? 30.424 -25.957 -0.465  1.00 16.39 ?  142  VAL   B HG13 1 
ATOM   6197 H  HG21 . VAL   B 1 142 ? 31.426 -28.392 1.058   1.00 17.89 ?  142  VAL   B HG21 1 
ATOM   6198 H  HG22 . VAL   B 1 142 ? 30.148 -28.537 0.127   1.00 17.89 ?  142  VAL   B HG22 1 
ATOM   6199 H  HG23 . VAL   B 1 142 ? 31.416 -29.463 -0.115  1.00 17.89 ?  142  VAL   B HG23 1 
ATOM   6200 N  N    . CYS   B 1 143 ? 32.801 -26.911 -3.774  1.00 12.63 ?  143  CYS   B N    1 
ATOM   6201 C  CA   . CYS   B 1 143 ? 33.294 -25.974 -4.779  1.00 12.58 ?  143  CYS   B CA   1 
ATOM   6202 C  C    . CYS   B 1 143 ? 32.294 -25.834 -5.919  1.00 12.55 ?  143  CYS   B C    1 
ATOM   6203 O  O    . CYS   B 1 143 ? 31.893 -24.724 -6.282  1.00 12.71 ?  143  CYS   B O    1 
ATOM   6204 C  CB   . CYS   B 1 143 ? 34.650 -26.458 -5.304  1.00 12.69 ?  143  CYS   B CB   1 
ATOM   6205 S  SG   . CYS   B 1 143 ? 35.396 -25.368 -6.519  1.00 12.96 ?  143  CYS   B SG   1 
ATOM   6206 H  H    . CYS   B 1 143 ? 33.330 -27.563 -3.604  1.00 15.17 ?  143  CYS   B H    1 
ATOM   6207 H  HA   . CYS   B 1 143 ? 33.423 -25.101 -4.377  1.00 15.12 ?  143  CYS   B HA   1 
ATOM   6208 H  HB2  . CYS   B 1 143 ? 35.272 -26.537 -4.563  1.00 15.25 ?  143  CYS   B HB2  1 
ATOM   6209 H  HB3  . CYS   B 1 143 ? 34.535 -27.323 -5.721  1.00 15.25 ?  143  CYS   B HB3  1 
ATOM   6210 H  HG   . CYS   B 1 143 ? 36.469 -25.801 -6.838  1.00 15.58 ?  143  CYS   B HG   1 
ATOM   6211 N  N    . VAL   B 1 144 ? 31.892 -26.957 -6.509  1.00 12.85 ?  144  VAL   B N    1 
ATOM   6212 C  CA   . VAL   B 1 144 ? 30.983 -26.902 -7.648  1.00 13.99 ?  144  VAL   B CA   1 
ATOM   6213 C  C    . VAL   B 1 144 ? 29.642 -26.289 -7.272  1.00 14.24 ?  144  VAL   B C    1 
ATOM   6214 O  O    . VAL   B 1 144 ? 29.031 -25.578 -8.076  1.00 15.36 ?  144  VAL   B O    1 
ATOM   6215 C  CB   . VAL   B 1 144 ? 30.822 -28.316 -8.211  1.00 16.42 ?  144  VAL   B CB   1 
ATOM   6216 C  CG1  . VAL   B 1 144 ? 29.542 -28.447 -9.035  1.00 18.72 ?  144  VAL   B CG1  1 
ATOM   6217 C  CG2  . VAL   B 1 144 ? 32.067 -28.715 -9.003  1.00 16.58 ?  144  VAL   B CG2  1 
ATOM   6218 H  H    . VAL   B 1 144 ? 32.124 -27.750 -6.274  1.00 15.44 ?  144  VAL   B H    1 
ATOM   6219 H  HA   . VAL   B 1 144 ? 31.372 -26.350 -8.343  1.00 16.81 ?  144  VAL   B HA   1 
ATOM   6220 H  HB   . VAL   B 1 144 ? 30.747 -28.936 -7.467  1.00 19.73 ?  144  VAL   B HB   1 
ATOM   6221 H  HG11 . VAL   B 1 144 ? 29.614 -29.240 -9.595  1.00 22.48 ?  144  VAL   B HG11 1 
ATOM   6222 H  HG12 . VAL   B 1 144 ? 28.787 -28.541 -8.434  1.00 22.48 ?  144  VAL   B HG12 1 
ATOM   6223 H  HG13 . VAL   B 1 144 ? 29.440 -27.662 -9.589  1.00 22.48 ?  144  VAL   B HG13 1 
ATOM   6224 H  HG21 . VAL   B 1 144 ? 31.950 -29.614 -9.346  1.00 19.92 ?  144  VAL   B HG21 1 
ATOM   6225 H  HG22 . VAL   B 1 144 ? 32.181 -28.093 -9.740  1.00 19.92 ?  144  VAL   B HG22 1 
ATOM   6226 H  HG23 . VAL   B 1 144 ? 32.837 -28.679 -8.417  1.00 19.92 ?  144  VAL   B HG23 1 
ATOM   6227 N  N    . ASP   B 1 145 ? 29.177 -26.529 -6.052  1.00 14.41 ?  145  ASP   B N    1 
ATOM   6228 C  CA   . ASP   B 1 145 ? 27.869 -26.064 -5.616  1.00 15.20 ?  145  ASP   B CA   1 
ATOM   6229 C  C    . ASP   B 1 145 ? 27.895 -24.637 -5.080  1.00 14.59 ?  145  ASP   B C    1 
ATOM   6230 O  O    . ASP   B 1 145 ? 26.831 -24.101 -4.745  1.00 16.36 ?  145  ASP   B O    1 
ATOM   6231 C  CB   . ASP   B 1 145 ? 27.295 -26.984 -4.531  1.00 16.39 ?  145  ASP   B CB   1 
ATOM   6232 C  CG   . ASP   B 1 145 ? 26.929 -28.357 -5.041  1.00 17.94 ?  145  ASP   B CG   1 
ATOM   6233 O  OD1  . ASP   B 1 145 ? 26.815 -28.545 -6.268  1.00 18.14 ?  145  ASP   B OD1  1 
ATOM   6234 O  OD2  . ASP   B 1 145 ? 26.742 -29.246 -4.189  1.00 19.70 -1 145  ASP   B OD2  1 
ATOM   6235 H  H    . ASP   B 1 145 ? 29.616 -26.946 -5.448  1.00 17.32 ?  145  ASP   B H    1 
ATOM   6236 H  HA   . ASP   B 1 145 ? 27.267 -26.064 -6.373  1.00 18.27 ?  145  ASP   B HA   1 
ATOM   6237 H  HB2  . ASP   B 1 145 ? 27.952 -27.100 -3.836  1.00 19.69 ?  145  ASP   B HB2  1 
ATOM   6238 H  HB3  . ASP   B 1 145 ? 26.490 -26.577 -4.171  1.00 19.69 ?  145  ASP   B HB3  1 
ATOM   6239 N  N    . THR   B 1 146 ? 29.071 -24.022 -4.974  1.00 12.91 ?  146  THR   B N    1 
ATOM   6240 C  CA   . THR   B 1 146 ? 29.204 -22.702 -4.369  1.00 12.42 ?  146  THR   B CA   1 
ATOM   6241 C  C    . THR   B 1 146 ? 29.837 -21.672 -5.288  1.00 12.05 ?  146  THR   B C    1 
ATOM   6242 O  O    . THR   B 1 146 ? 29.382 -20.515 -5.337  1.00 12.11 ?  146  THR   B O    1 
ATOM   6243 C  CB   . THR   B 1 146 ? 30.041 -22.805 -3.090  1.00 12.79 ?  146  THR   B CB   1 
ATOM   6244 O  OG1  . THR   B 1 146 ? 29.463 -23.790 -2.227  1.00 13.24 ?  146  THR   B OG1  1 
ATOM   6245 C  CG2  . THR   B 1 146 ? 30.116 -21.468 -2.373  1.00 13.17 ?  146  THR   B CG2  1 
ATOM   6246 H  H    . THR   B 1 146 ? 29.820 -24.346 -5.251  1.00 15.52 ?  146  THR   B H    1 
ATOM   6247 H  HA   . THR   B 1 146 ? 28.332 -22.370 -4.127  1.00 14.92 ?  146  THR   B HA   1 
ATOM   6248 H  HB   . THR   B 1 146 ? 30.949 -23.066 -3.316  1.00 15.37 ?  146  THR   B HB   1 
ATOM   6249 H  HG1  . THR   B 1 146 ? 29.494 -24.550 -2.602  1.00 15.92 ?  146  THR   B HG1  1 
ATOM   6250 H  HG21 . THR   B 1 146 ? 30.468 -21.589 -1.479  1.00 15.82 ?  146  THR   B HG21 1 
ATOM   6251 H  HG22 . THR   B 1 146 ? 30.701 -20.862 -2.860  1.00 15.82 ?  146  THR   B HG22 1 
ATOM   6252 H  HG23 . THR   B 1 146 ? 29.233 -21.074 -2.317  1.00 15.82 ?  146  THR   B HG23 1 
ATOM   6253 N  N    . VAL   B 1 147 ? 30.907 -22.046 -5.979  1.00 11.90 ?  147  VAL   B N    1 
ATOM   6254 C  CA   . VAL   B 1 147 ? 31.628 -21.107 -6.823  1.00 11.65 ?  147  VAL   B CA   1 
ATOM   6255 C  C    . VAL   B 1 147 ? 30.892 -20.976 -8.143  1.00 11.93 ?  147  VAL   B C    1 
ATOM   6256 O  O    . VAL   B 1 147 ? 30.525 -21.982 -8.769  1.00 12.72 ?  147  VAL   B O    1 
ATOM   6257 C  CB   . VAL   B 1 147 ? 33.081 -21.565 -7.030  1.00 11.72 ?  147  VAL   B CB   1 
ATOM   6258 C  CG1  . VAL   B 1 147 ? 33.836 -20.541 -7.850  1.00 11.88 ?  147  VAL   B CG1  1 
ATOM   6259 C  CG2  . VAL   B 1 147 ? 33.764 -21.773 -5.691  1.00 11.93 ?  147  VAL   B CG2  1 
ATOM   6260 H  H    . VAL   B 1 147 ? 31.237 -22.845 -5.985  1.00 14.31 ?  147  VAL   B H    1 
ATOM   6261 H  HA   . VAL   B 1 147 ? 31.646 -20.239 -6.395  1.00 14.00 ?  147  VAL   B HA   1 
ATOM   6262 H  HB   . VAL   B 1 147 ? 33.090 -22.409 -7.515  1.00 14.08 ?  147  VAL   B HB   1 
ATOM   6263 H  HG11 . VAL   B 1 147 ? 34.779 -20.760 -7.837  1.00 14.28 ?  147  VAL   B HG11 1 
ATOM   6264 H  HG12 . VAL   B 1 147 ? 33.504 -20.554 -8.761  1.00 14.28 ?  147  VAL   B HG12 1 
ATOM   6265 H  HG13 . VAL   B 1 147 ? 33.694 -19.663 -7.458  1.00 14.28 ?  147  VAL   B HG13 1 
ATOM   6266 H  HG21 . VAL   B 1 147 ? 34.702 -21.968 -5.842  1.00 14.34 ?  147  VAL   B HG21 1 
ATOM   6267 H  HG22 . VAL   B 1 147 ? 33.675 -20.962 -5.166  1.00 14.34 ?  147  VAL   B HG22 1 
ATOM   6268 H  HG23 . VAL   B 1 147 ? 33.341 -22.514 -5.231  1.00 14.34 ?  147  VAL   B HG23 1 
ATOM   6269 N  N    . ARG   B 1 148 ? 30.688 -19.727 -8.567  1.00 11.85 ?  148  ARG   B N    1 
ATOM   6270 C  CA   . ARG   B 1 148 ? 30.064 -19.412 -9.840  1.00 12.11 ?  148  ARG   B CA   1 
ATOM   6271 C  C    . ARG   B 1 148 ? 31.020 -18.741 -10.814 1.00 12.22 ?  148  ARG   B C    1 
ATOM   6272 O  O    . ARG   B 1 148 ? 30.736 -18.725 -12.016 1.00 13.53 ?  148  ARG   B O    1 
ATOM   6273 C  CB   . ARG   B 1 148 ? 28.827 -18.526 -9.622  1.00 12.10 ?  148  ARG   B CB   1 
ATOM   6274 C  CG   . ARG   B 1 148 ? 27.753 -19.233 -8.811  1.00 13.04 ?  148  ARG   B CG   1 
ATOM   6275 C  CD   . ARG   B 1 148 ? 26.541 -18.355 -8.502  1.00 14.24 ?  148  ARG   B CD   1 
ATOM   6276 N  NE   . ARG   B 1 148 ? 26.922 -17.149 -7.777  1.00 13.68 ?  148  ARG   B NE   1 
ATOM   6277 C  CZ   . ARG   B 1 148 ? 27.227 -17.107 -6.486  1.00 12.91 ?  148  ARG   B CZ   1 
ATOM   6278 N  NH1  . ARG   B 1 148 ? 27.169 -18.190 -5.724  1.00 12.95 ?  148  ARG   B NH1  1 
ATOM   6279 N  NH2  . ARG   B 1 148 ? 27.625 -15.954 -5.952  1.00 13.03 ?  148  ARG   B NH2  1 
ATOM   6280 H  H    . ARG   B 1 148 ? 30.910 -19.027 -8.112  1.00 14.25 ?  148  ARG   B H    1 
ATOM   6281 H  HA   . ARG   B 1 148 ? 29.762 -20.236 -10.247 1.00 14.55 ?  148  ARG   B HA   1 
ATOM   6282 H  HB2  . ARG   B 1 148 ? 29.087 -17.724 -9.141  1.00 14.55 ?  148  ARG   B HB2  1 
ATOM   6283 H  HB3  . ARG   B 1 148 ? 28.448 -18.290 -10.483 1.00 14.55 ?  148  ARG   B HB3  1 
ATOM   6284 H  HG2  . ARG   B 1 148 ? 27.438 -20.004 -9.311  1.00 15.67 ?  148  ARG   B HG2  1 
ATOM   6285 H  HG3  . ARG   B 1 148 ? 28.131 -19.520 -7.967  1.00 15.67 ?  148  ARG   B HG3  1 
ATOM   6286 H  HD2  . ARG   B 1 148 ? 26.120 -18.088 -9.334  1.00 17.11 ?  148  ARG   B HD2  1 
ATOM   6287 H  HD3  . ARG   B 1 148 ? 25.914 -18.855 -7.956  1.00 17.11 ?  148  ARG   B HD3  1 
ATOM   6288 H  HE   . ARG   B 1 148 ? 26.958 -16.413 -8.217  1.00 16.44 ?  148  ARG   B HE   1 
ATOM   6289 H  HH11 . ARG   B 1 148 ? 26.908 -18.942 -6.055  1.00 15.56 ?  148  ARG   B HH11 1 
ATOM   6290 H  HH12 . ARG   B 1 148 ? 27.365 -18.139 -4.887  1.00 15.56 ?  148  ARG   B HH12 1 
ATOM   6291 H  HH21 . ARG   B 1 148 ? 27.675 -15.252 -6.441  1.00 15.66 ?  148  ARG   B HH21 1 
ATOM   6292 H  HH22 . ARG   B 1 148 ? 27.827 -15.916 -5.117  1.00 15.66 ?  148  ARG   B HH22 1 
ATOM   6293 N  N    . THR   B 1 149 ? 32.123 -18.184 -10.325 1.00 12.20 ?  149  THR   B N    1 
ATOM   6294 C  CA   . THR   B 1 149 ? 33.162 -17.626 -11.173 1.00 12.26 ?  149  THR   B CA   1 
ATOM   6295 C  C    . THR   B 1 149 ? 34.046 -18.764 -11.680 1.00 11.61 ?  149  THR   B C    1 
ATOM   6296 O  O    . THR   B 1 149 ? 33.847 -19.934 -11.345 1.00 12.18 ?  149  THR   B O    1 
ATOM   6297 C  CB   . THR   B 1 149 ? 33.929 -16.568 -10.393 1.00 12.08 ?  149  THR   B CB   1 
ATOM   6298 O  OG1  . THR   B 1 149 ? 34.386 -17.170 -9.179  1.00 11.93 ?  149  THR   B OG1  1 
ATOM   6299 C  CG2  . THR   B 1 149 ? 33.033 -15.365 -10.096 1.00 12.72 ?  149  THR   B CG2  1 
ATOM   6300 H  H    . THR   B 1 149 ? 32.286 -18.112 -9.482  1.00 14.66 ?  149  THR   B H    1 
ATOM   6301 H  HA   . THR   B 1 149 ? 32.751 -17.195 -11.937 1.00 14.73 ?  149  THR   B HA   1 
ATOM   6302 H  HB   . THR   B 1 149 ? 34.690 -16.275 -10.910 1.00 14.52 ?  149  THR   B HB   1 
ATOM   6303 H  HG1  . THR   B 1 149 ? 34.806 -16.602 -8.717  1.00 14.34 ?  149  THR   B HG1  1 
ATOM   6304 H  HG21 . THR   B 1 149 ? 33.536 -14.689 -9.614  1.00 15.29 ?  149  THR   B HG21 1 
ATOM   6305 H  HG22 . THR   B 1 149 ? 32.709 -14.982 -10.927 1.00 15.29 ?  149  THR   B HG22 1 
ATOM   6306 H  HG23 . THR   B 1 149 ? 32.274 -15.636 -9.557  1.00 15.29 ?  149  THR   B HG23 1 
ATOM   6307 N  N    . ASN   B 1 150 ? 35.015 -18.442 -12.521 1.00 11.72 ?  150  ASN   B N    1 
ATOM   6308 C  CA   . ASN   B 1 150 ? 35.775 -19.463 -13.229 1.00 12.15 ?  150  ASN   B CA   1 
ATOM   6309 C  C    . ASN   B 1 150 ? 36.940 -19.914 -12.360 1.00 11.82 ?  150  ASN   B C    1 
ATOM   6310 O  O    . ASN   B 1 150 ? 37.869 -19.144 -12.102 1.00 12.36 ?  150  ASN   B O    1 
ATOM   6311 C  CB   . ASN   B 1 150 ? 36.245 -18.921 -14.570 1.00 13.80 ?  150  ASN   B CB   1 
ATOM   6312 C  CG   . ASN   B 1 150 ? 35.105 -18.719 -15.521 1.00 16.37 ?  150  ASN   B CG   1 
ATOM   6313 O  OD1  . ASN   B 1 150 ? 34.222 -19.561 -15.617 1.00 17.21 ?  150  ASN   B OD1  1 
ATOM   6314 N  ND2  . ASN   B 1 150 ? 35.094 -17.593 -16.210 1.00 18.28 ?  150  ASN   B ND2  1 
ATOM   6315 H  H    . ASN   B 1 150 ? 35.266 -17.633 -12.688 1.00 14.08 ?  150  ASN   B H    1 
ATOM   6316 H  HA   . ASN   B 1 150 ? 35.196 -20.227 -13.394 1.00 14.61 ?  150  ASN   B HA   1 
ATOM   6317 H  HB2  . ASN   B 1 150 ? 36.673 -18.061 -14.428 1.00 16.58 ?  150  ASN   B HB2  1 
ATOM   6318 H  HB3  . ASN   B 1 150 ? 36.862 -19.545 -14.967 1.00 16.58 ?  150  ASN   B HB3  1 
ATOM   6319 H  HD21 . ASN   B 1 150 ? 34.456 -17.431 -16.768 1.00 21.96 ?  150  ASN   B HD21 1 
ATOM   6320 H  HD22 . ASN   B 1 150 ? 35.729 -17.020 -16.111 1.00 21.96 ?  150  ASN   B HD22 1 
ATOM   6321 N  N    . VAL   B 1 151 ? 36.895 -21.163 -11.905 1.00 11.56 ?  151  VAL   B N    1 
ATOM   6322 C  CA   . VAL   B 1 151 ? 37.911 -21.689 -11.009 1.00 11.70 ?  151  VAL   B CA   1 
ATOM   6323 C  C    . VAL   B 1 151 ? 38.615 -22.859 -11.681 1.00 11.37 ?  151  VAL   B C    1 
ATOM   6324 O  O    . VAL   B 1 151 ? 37.972 -23.793 -12.184 1.00 12.71 ?  151  VAL   B O    1 
ATOM   6325 C  CB   . VAL   B 1 151 ? 37.346 -22.027 -9.614  1.00 12.67 ?  151  VAL   B CB   1 
ATOM   6326 C  CG1  . VAL   B 1 151 ? 36.187 -23.021 -9.695  1.00 13.68 ?  151  VAL   B CG1  1 
ATOM   6327 C  CG2  . VAL   B 1 151 ? 38.455 -22.525 -8.699  1.00 13.22 ?  151  VAL   B CG2  1 
ATOM   6328 H  H    . VAL   B 1 151 ? 36.273 -21.728 -12.103 1.00 13.90 ?  151  VAL   B H    1 
ATOM   6329 H  HA   . VAL   B 1 151 ? 38.577 -20.994 -10.875 1.00 14.06 ?  151  VAL   B HA   1 
ATOM   6330 H  HB   . VAL   B 1 151 ? 36.998 -21.211 -9.221  1.00 15.22 ?  151  VAL   B HB   1 
ATOM   6331 H  HG11 . VAL   B 1 151 ? 35.867 -23.210 -8.798  1.00 16.44 ?  151  VAL   B HG11 1 
ATOM   6332 H  HG12 . VAL   B 1 151 ? 35.470 -22.633 -10.223 1.00 16.44 ?  151  VAL   B HG12 1 
ATOM   6333 H  HG13 . VAL   B 1 151 ? 36.497 -23.841 -10.113 1.00 16.44 ?  151  VAL   B HG13 1 
ATOM   6334 H  HG21 . VAL   B 1 151 ? 38.105 -22.600 -7.795  1.00 15.89 ?  151  VAL   B HG21 1 
ATOM   6335 H  HG22 . VAL   B 1 151 ? 38.756 -23.393 -9.007  1.00 15.89 ?  151  VAL   B HG22 1 
ATOM   6336 H  HG23 . VAL   B 1 151 ? 39.188 -21.891 -8.715  1.00 15.89 ?  151  VAL   B HG23 1 
ATOM   6337 N  N    . TYR   B 1 152 ? 39.945 -22.772 -11.698 1.00 10.73 ?  152  TYR   B N    1 
ATOM   6338 C  CA   . TYR   B 1 152 ? 40.848 -23.752 -12.281 1.00 11.25 ?  152  TYR   B CA   1 
ATOM   6339 C  C    . TYR   B 1 152 ? 41.568 -24.428 -11.122 1.00 10.45 ?  152  TYR   B C    1 
ATOM   6340 O  O    . TYR   B 1 152 ? 42.414 -23.809 -10.467 1.00 11.22 ?  152  TYR   B O    1 
ATOM   6341 C  CB   . TYR   B 1 152 ? 41.818 -23.042 -13.227 1.00 12.13 ?  152  TYR   B CB   1 
ATOM   6342 C  CG   . TYR   B 1 152 ? 41.137 -22.581 -14.493 1.00 12.49 ?  152  TYR   B CG   1 
ATOM   6343 C  CD1  . TYR   B 1 152 ? 40.474 -21.357 -14.561 1.00 12.96 ?  152  TYR   B CD1  1 
ATOM   6344 C  CD2  . TYR   B 1 152 ? 41.132 -23.390 -15.618 1.00 13.77 ?  152  TYR   B CD2  1 
ATOM   6345 C  CE1  . TYR   B 1 152 ? 39.835 -20.958 -15.720 1.00 14.57 ?  152  TYR   B CE1  1 
ATOM   6346 C  CE2  . TYR   B 1 152 ? 40.494 -23.007 -16.776 1.00 14.81 ?  152  TYR   B CE2  1 
ATOM   6347 C  CZ   . TYR   B 1 152 ? 39.848 -21.790 -16.827 1.00 15.15 ?  152  TYR   B CZ   1 
ATOM   6348 O  OH   . TYR   B 1 152 ? 39.217 -21.419 -17.989 1.00 17.72 ?  152  TYR   B OH   1 
ATOM   6349 H  H    . TYR   B 1 152 ? 40.375 -22.108 -11.349 1.00 12.90 ?  152  TYR   B H    1 
ATOM   6350 H  HA   . TYR   B 1 152 ? 40.342 -24.419 -12.776 1.00 13.52 ?  152  TYR   B HA   1 
ATOM   6351 H  HB2  . TYR   B 1 152 ? 42.183 -22.266 -12.775 1.00 14.58 ?  152  TYR   B HB2  1 
ATOM   6352 H  HB3  . TYR   B 1 152 ? 42.531 -23.654 -13.468 1.00 14.58 ?  152  TYR   B HB3  1 
ATOM   6353 H  HD1  . TYR   B 1 152 ? 40.457 -20.799 -13.814 1.00 15.58 ?  152  TYR   B HD1  1 
ATOM   6354 H  HD2  . TYR   B 1 152 ? 41.563 -24.216 -15.585 1.00 16.54 ?  152  TYR   B HD2  1 
ATOM   6355 H  HE1  . TYR   B 1 152 ? 39.397 -20.139 -15.755 1.00 17.50 ?  152  TYR   B HE1  1 
ATOM   6356 H  HE2  . TYR   B 1 152 ? 40.508 -23.562 -17.523 1.00 17.79 ?  152  TYR   B HE2  1 
ATOM   6357 H  HH   . TYR   B 1 152 ? 38.869 -20.658 -17.895 1.00 21.29 ?  152  TYR   B HH   1 
ATOM   6358 N  N    . LEU   B 1 153 ? 41.200 -25.681 -10.850 1.00 10.68 ?  153  LEU   B N    1 
ATOM   6359 C  CA   . LEU   B 1 153 ? 41.709 -26.435 -9.712  1.00 10.62 ?  153  LEU   B CA   1 
ATOM   6360 C  C    . LEU   B 1 153 ? 42.942 -27.230 -10.110 1.00 11.08 ?  153  LEU   B C    1 
ATOM   6361 O  O    . LEU   B 1 153 ? 42.925 -27.950 -11.110 1.00 12.23 ?  153  LEU   B O    1 
ATOM   6362 C  CB   . LEU   B 1 153 ? 40.633 -27.394 -9.195  1.00 11.35 ?  153  LEU   B CB   1 
ATOM   6363 C  CG   . LEU   B 1 153 ? 39.374 -26.742 -8.626  1.00 12.20 ?  153  LEU   B CG   1 
ATOM   6364 C  CD1  . LEU   B 1 153 ? 38.287 -27.778 -8.457  1.00 13.07 ?  153  LEU   B CD1  1 
ATOM   6365 C  CD2  . LEU   B 1 153 ? 39.675 -26.073 -7.295  1.00 12.65 ?  153  LEU   B CD2  1 
ATOM   6366 H  H    . LEU   B 1 153 ? 40.626 -26.127 -11.323 1.00 12.84 ?  153  LEU   B H    1 
ATOM   6367 H  HA   . LEU   B 1 153 ? 41.937 -25.826 -8.999  1.00 12.77 ?  153  LEU   B HA   1 
ATOM   6368 H  HB2  . LEU   B 1 153 ? 40.350 -27.969 -9.923  1.00 13.64 ?  153  LEU   B HB2  1 
ATOM   6369 H  HB3  . LEU   B 1 153 ? 41.016 -27.938 -8.487  1.00 13.64 ?  153  LEU   B HB3  1 
ATOM   6370 H  HG   . LEU   B 1 153 ? 39.051 -26.063 -9.238  1.00 14.66 ?  153  LEU   B HG   1 
ATOM   6371 H  HD11 . LEU   B 1 153 ? 37.480 -27.339 -8.133  1.00 15.71 ?  153  LEU   B HD11 1 
ATOM   6372 H  HD12 . LEU   B 1 153 ? 38.114 -28.193 -9.312  1.00 15.71 ?  153  LEU   B HD12 1 
ATOM   6373 H  HD13 . LEU   B 1 153 ? 38.581 -28.440 -7.814  1.00 15.71 ?  153  LEU   B HD13 1 
ATOM   6374 H  HD21 . LEU   B 1 153 ? 38.857 -25.707 -6.925  1.00 15.20 ?  153  LEU   B HD21 1 
ATOM   6375 H  HD22 . LEU   B 1 153 ? 40.046 -26.732 -6.685  1.00 15.20 ?  153  LEU   B HD22 1 
ATOM   6376 H  HD23 . LEU   B 1 153 ? 40.320 -25.361 -7.438  1.00 15.20 ?  153  LEU   B HD23 1 
ATOM   6377 N  N    . ALA   B 1 154 ? 43.993 -27.126 -9.303  1.00 11.19 ?  154  ALA   B N    1 
ATOM   6378 C  CA   . ALA   B 1 154 ? 45.224 -27.883 -9.488  1.00 12.46 ?  154  ALA   B CA   1 
ATOM   6379 C  C    . ALA   B 1 154 ? 45.286 -28.960 -8.415  1.00 13.00 ?  154  ALA   B C    1 
ATOM   6380 O  O    . ALA   B 1 154 ? 45.201 -28.663 -7.216  1.00 14.03 ?  154  ALA   B O    1 
ATOM   6381 C  CB   . ALA   B 1 154 ? 46.447 -26.971 -9.417  1.00 13.28 ?  154  ALA   B CB   1 
ATOM   6382 H  H    . ALA   B 1 154 ? 44.010 -26.597 -8.618  1.00 13.45 ?  154  ALA   B H    1 
ATOM   6383 H  HA   . ALA   B 1 154 ? 45.209 -28.308 -10.355 1.00 14.98 ?  154  ALA   B HA   1 
ATOM   6384 H  HB1  . ALA   B 1 154 ? 47.247 -27.505 -9.544  1.00 15.96 ?  154  ALA   B HB1  1 
ATOM   6385 H  HB2  . ALA   B 1 154 ? 46.385 -26.299 -10.116 1.00 15.96 ?  154  ALA   B HB2  1 
ATOM   6386 H  HB3  . ALA   B 1 154 ? 46.474 -26.538 -8.548  1.00 15.96 ?  154  ALA   B HB3  1 
ATOM   6387 N  N    . VAL   B 1 155 ? 45.405 -30.208 -8.848  1.00 12.44 ?  155  VAL   B N    1 
ATOM   6388 C  CA   . VAL   B 1 155 ? 45.511 -31.353 -7.954  1.00 12.87 ?  155  VAL   B CA   1 
ATOM   6389 C  C    . VAL   B 1 155 ? 46.850 -32.019 -8.236  1.00 12.58 ?  155  VAL   B C    1 
ATOM   6390 O  O    . VAL   B 1 155 ? 47.082 -32.512 -9.347  1.00 14.57 ?  155  VAL   B O    1 
ATOM   6391 C  CB   . VAL   B 1 155 ? 44.359 -32.347 -8.158  1.00 14.23 ?  155  VAL   B CB   1 
ATOM   6392 C  CG1  . VAL   B 1 155 ? 44.550 -33.550 -7.256  1.00 14.05 ?  155  VAL   B CG1  1 
ATOM   6393 C  CG2  . VAL   B 1 155 ? 43.024 -31.671 -7.882  1.00 15.20 ?  155  VAL   B CG2  1 
ATOM   6394 H  H    . VAL   B 1 155 ? 45.435 -30.423 -9.682  1.00 14.95 ?  155  VAL   B H    1 
ATOM   6395 H  HA   . VAL   B 1 155 ? 45.501 -31.052 -7.032  1.00 15.46 ?  155  VAL   B HA   1 
ATOM   6396 H  HB   . VAL   B 1 155 ? 44.360 -32.649 -9.080  1.00 17.10 ?  155  VAL   B HB   1 
ATOM   6397 H  HG11 . VAL   B 1 155 ? 43.722 -34.055 -7.219  1.00 16.89 ?  155  VAL   B HG11 1 
ATOM   6398 H  HG12 . VAL   B 1 155 ? 45.258 -34.114 -7.616  1.00 16.89 ?  155  VAL   B HG12 1 
ATOM   6399 H  HG13 . VAL   B 1 155 ? 44.791 -33.250 -6.366  1.00 16.89 ?  155  VAL   B HG13 1 
ATOM   6400 H  HG21 . VAL   B 1 155 ? 42.315 -32.326 -7.980  1.00 18.26 ?  155  VAL   B HG21 1 
ATOM   6401 H  HG22 . VAL   B 1 155 ? 43.029 -31.324 -6.976  1.00 18.26 ?  155  VAL   B HG22 1 
ATOM   6402 H  HG23 . VAL   B 1 155 ? 42.897 -30.948 -8.514  1.00 18.26 ?  155  VAL   B HG23 1 
ATOM   6403 N  N    . PHE   B 1 156 ? 47.714 -32.061 -7.223  1.00 13.19 ?  156  PHE   B N    1 
ATOM   6404 C  CA   . PHE   B 1 156 ? 49.092 -32.510 -7.429  1.00 14.41 ?  156  PHE   B CA   1 
ATOM   6405 C  C    . PHE   B 1 156 ? 49.191 -34.009 -7.711  1.00 15.57 ?  156  PHE   B C    1 
ATOM   6406 O  O    . PHE   B 1 156 ? 49.917 -34.437 -8.619  1.00 17.29 ?  156  PHE   B O    1 
ATOM   6407 C  CB   . PHE   B 1 156 ? 49.922 -32.139 -6.203  1.00 14.15 ?  156  PHE   B CB   1 
ATOM   6408 C  CG   . PHE   B 1 156 ? 51.344 -32.605 -6.260  1.00 14.67 ?  156  PHE   B CG   1 
ATOM   6409 C  CD1  . PHE   B 1 156 ? 52.223 -32.067 -7.180  1.00 16.39 ?  156  PHE   B CD1  1 
ATOM   6410 C  CD2  . PHE   B 1 156 ? 51.805 -33.563 -5.380  1.00 15.28 ?  156  PHE   B CD2  1 
ATOM   6411 C  CE1  . PHE   B 1 156 ? 53.541 -32.477 -7.227  1.00 17.19 ?  156  PHE   B CE1  1 
ATOM   6412 C  CE2  . PHE   B 1 156 ? 53.121 -33.980 -5.423  1.00 16.71 ?  156  PHE   B CE2  1 
ATOM   6413 C  CZ   . PHE   B 1 156 ? 53.983 -33.440 -6.355  1.00 17.00 ?  156  PHE   B CZ   1 
ATOM   6414 H  H    . PHE   B 1 156 ? 47.527 -31.849 -6.409  1.00 15.85 ?  156  PHE   B H    1 
ATOM   6415 H  HA   . PHE   B 1 156 ? 49.458 -32.040 -8.190  1.00 17.31 ?  156  PHE   B HA   1 
ATOM   6416 H  HB2  . PHE   B 1 156 ? 49.937 -31.171 -6.121  1.00 17.01 ?  156  PHE   B HB2  1 
ATOM   6417 H  HB3  . PHE   B 1 156 ? 49.518 -32.529 -5.415  1.00 17.01 ?  156  PHE   B HB3  1 
ATOM   6418 H  HD1  . PHE   B 1 156 ? 51.928 -31.412 -7.774  1.00 19.69 ?  156  PHE   B HD1  1 
ATOM   6419 H  HD2  . PHE   B 1 156 ? 51.222 -33.933 -4.756  1.00 18.36 ?  156  PHE   B HD2  1 
ATOM   6420 H  HE1  . PHE   B 1 156 ? 54.125 -32.110 -7.855  1.00 20.65 ?  156  PHE   B HE1  1 
ATOM   6421 H  HE2  . PHE   B 1 156 ? 53.419 -34.636 -4.832  1.00 20.07 ?  156  PHE   B HE2  1 
ATOM   6422 H  HZ   . PHE   B 1 156 ? 54.872 -33.723 -6.385  1.00 20.42 ?  156  PHE   B HZ   1 
ATOM   6423 N  N    . ASP   B 1 157 ? 48.523 -34.829 -6.914  1.00 15.90 ?  157  ASP   B N    1 
ATOM   6424 C  CA   . ASP   B 1 157 ? 48.673 -36.277 -7.018  1.00 17.17 ?  157  ASP   B CA   1 
ATOM   6425 C  C    . ASP   B 1 157 ? 47.757 -36.821 -8.109  1.00 17.30 ?  157  ASP   B C    1 
ATOM   6426 O  O    . ASP   B 1 157 ? 46.531 -36.706 -8.004  1.00 16.83 ?  157  ASP   B O    1 
ATOM   6427 C  CB   . ASP   B 1 157 ? 48.315 -36.895 -5.673  1.00 18.63 ?  157  ASP   B CB   1 
ATOM   6428 C  CG   . ASP   B 1 157 ? 48.445 -38.406 -5.663  1.00 20.44 ?  157  ASP   B CG   1 
ATOM   6429 O  OD1  . ASP   B 1 157 ? 48.789 -39.011 -6.707  1.00 20.78 ?  157  ASP   B OD1  1 
ATOM   6430 O  OD2  . ASP   B 1 157 ? 48.210 -38.990 -4.588  1.00 22.23 -1 157  ASP   B OD2  1 
ATOM   6431 H  H    . ASP   B 1 157 ? 47.978 -34.577 -6.306  1.00 19.10 ?  157  ASP   B H    1 
ATOM   6432 H  HA   . ASP   B 1 157 ? 49.594 -36.504 -7.237  1.00 20.63 ?  157  ASP   B HA   1 
ATOM   6433 H  HB2  . ASP   B 1 157 ? 48.899 -36.526 -4.995  1.00 22.37 ?  157  ASP   B HB2  1 
ATOM   6434 H  HB3  . ASP   B 1 157 ? 47.392 -36.675 -5.467  1.00 22.37 ?  157  ASP   B HB3  1 
ATOM   6435 N  N    . LYS   B 1 158 ? 48.349 -37.441 -9.140  1.00 18.35 ?  158  LYS   B N    1 
ATOM   6436 C  CA   . LYS   B 1 158 ? 47.566 -38.049 -10.219 1.00 19.39 ?  158  LYS   B CA   1 
ATOM   6437 C  C    . LYS   B 1 158 ? 46.506 -39.011 -9.683  1.00 18.98 ?  158  LYS   B C    1 
ATOM   6438 O  O    . LYS   B 1 158 ? 45.397 -39.099 -10.229 1.00 18.90 ?  158  LYS   B O    1 
ATOM   6439 C  CB   . LYS   B 1 158 ? 48.505 -38.770 -11.197 1.00 20.78 ?  158  LYS   B CB   1 
ATOM   6440 C  CG   . LYS   B 1 158 ? 47.814 -39.663 -12.219 1.00 22.84 ?  158  LYS   B CG   1 
ATOM   6441 C  CD   . LYS   B 1 158 ? 46.965 -38.869 -13.191 1.00 24.86 ?  158  LYS   B CD   1 
ATOM   6442 C  CE   . LYS   B 1 158 ? 46.362 -39.775 -14.253 1.00 26.46 ?  158  LYS   B CE   1 
ATOM   6443 N  NZ   . LYS   B 1 158 ? 45.301 -39.087 -15.042 1.00 26.90 ?  158  LYS   B NZ   1 
ATOM   6444 H  H    . LYS   B 1 158 ? 49.205 -37.520 -9.237  1.00 22.04 ?  158  LYS   B H    1 
ATOM   6445 H  HA   . LYS   B 1 158 ? 47.117 -37.348 -10.717 1.00 23.30 ?  158  LYS   B HA   1 
ATOM   6446 H  HB2  . LYS   B 1 158 ? 49.012 -38.105 -11.697 1.00 24.96 ?  158  LYS   B HB2  1 
ATOM   6447 H  HB3  . LYS   B 1 158 ? 49.117 -39.327 -10.692 1.00 24.96 ?  158  LYS   B HB3  1 
ATOM   6448 H  HG2  . LYS   B 1 158 ? 48.490 -40.132 -12.734 1.00 27.43 ?  158  LYS   B HG2  1 
ATOM   6449 H  HG3  . LYS   B 1 158 ? 47.245 -40.310 -11.770 1.00 27.43 ?  158  LYS   B HG3  1 
ATOM   6450 H  HD2  . LYS   B 1 158 ? 46.241 -38.438 -12.710 1.00 29.85 ?  158  LYS   B HD2  1 
ATOM   6451 H  HD3  . LYS   B 1 158 ? 47.517 -38.206 -13.634 1.00 29.85 ?  158  LYS   B HD3  1 
ATOM   6452 H  HE2  . LYS   B 1 158 ? 47.058 -40.055 -14.866 1.00 31.78 ?  158  LYS   B HE2  1 
ATOM   6453 H  HE3  . LYS   B 1 158 ? 45.964 -40.549 -13.824 1.00 31.78 ?  158  LYS   B HE3  1 
ATOM   6454 H  HZ1  . LYS   B 1 158 ? 44.967 -39.641 -15.653 1.00 32.31 ?  158  LYS   B HZ1  1 
ATOM   6455 H  HZ2  . LYS   B 1 158 ? 44.643 -38.822 -14.503 1.00 32.31 ?  158  LYS   B HZ2  1 
ATOM   6456 H  HZ3  . LYS   B 1 158 ? 45.641 -38.374 -15.453 1.00 32.31 ?  158  LYS   B HZ3  1 
ATOM   6457 N  N    . ASN   B 1 159 ? 46.834 -39.771 -8.637  1.00 19.54 ?  159  ASN   B N    1 
ATOM   6458 C  CA   . ASN   B 1 159 ? 45.879 -40.750 -8.125  1.00 20.19 ?  159  ASN   B CA   1 
ATOM   6459 C  C    . ASN   B 1 159 ? 44.686 -40.078 -7.446  1.00 19.34 ?  159  ASN   B C    1 
ATOM   6460 O  O    . ASN   B 1 159 ? 43.552 -40.567 -7.541  1.00 19.88 ?  159  ASN   B O    1 
ATOM   6461 C  CB   . ASN   B 1 159 ? 46.585 -41.724 -7.188  1.00 21.36 ?  159  ASN   B CB   1 
ATOM   6462 C  CG   . ASN   B 1 159 ? 47.613 -42.572 -7.906  1.00 23.14 ?  159  ASN   B CG   1 
ATOM   6463 O  OD1  . ASN   B 1 159 ? 47.357 -43.082 -9.001  1.00 23.81 ?  159  ASN   B OD1  1 
ATOM   6464 N  ND2  . ASN   B 1 159 ? 48.786 -42.733 -7.291  1.00 23.57 ?  159  ASN   B ND2  1 
ATOM   6465 H  H    . ASN   B 1 159 ? 47.587 -39.735 -8.225  1.00 23.47 ?  159  ASN   B H    1 
ATOM   6466 H  HA   . ASN   B 1 159 ? 45.541 -41.260 -8.880  1.00 24.25 ?  159  ASN   B HA   1 
ATOM   6467 H  HB2  . ASN   B 1 159 ? 47.037 -41.226 -6.494  1.00 25.65 ?  159  ASN   B HB2  1 
ATOM   6468 H  HB3  . ASN   B 1 159 ? 45.926 -42.320 -6.806  1.00 25.65 ?  159  ASN   B HB3  1 
ATOM   6469 H  HD21 . ASN   B 1 159 ? 49.407 -43.211 -7.656  1.00 28.31 ?  159  ASN   B HD21 1 
ATOM   6470 H  HD22 . ASN   B 1 159 ? 48.924 -42.374 -6.522  1.00 28.31 ?  159  ASN   B HD22 1 
ATOM   6471 N  N    . LEU   B 1 160 ? 44.907 -38.947 -6.770  1.00 18.27 ?  160  LEU   B N    1 
ATOM   6472 C  CA   . LEU   B 1 160 ? 43.775 -38.218 -6.213  1.00 16.98 ?  160  LEU   B CA   1 
ATOM   6473 C  C    . LEU   B 1 160 ? 42.980 -37.548 -7.319  1.00 16.36 ?  160  LEU   B C    1 
ATOM   6474 O  O    . LEU   B 1 160 ? 41.743 -37.552 -7.292  1.00 16.06 ?  160  LEU   B O    1 
ATOM   6475 C  CB   . LEU   B 1 160 ? 44.244 -37.191 -5.187  1.00 16.78 ?  160  LEU   B CB   1 
ATOM   6476 C  CG   . LEU   B 1 160 ? 43.119 -36.292 -4.659  1.00 16.53 ?  160  LEU   B CG   1 
ATOM   6477 C  CD1  . LEU   B 1 160 ? 42.011 -37.133 -4.043  1.00 16.80 ?  160  LEU   B CD1  1 
ATOM   6478 C  CD2  . LEU   B 1 160 ? 43.652 -35.286 -3.653  1.00 16.65 ?  160  LEU   B CD2  1 
ATOM   6479 H  H    . LEU   B 1 160 ? 45.682 -38.590 -6.634  1.00 21.95 ?  160  LEU   B H    1 
ATOM   6480 H  HA   . LEU   B 1 160 ? 43.195 -38.851 -5.770  1.00 20.39 ?  160  LEU   B HA   1 
ATOM   6481 H  HB2  . LEU   B 1 160 ? 44.637 -37.664 -4.435  1.00 20.16 ?  160  LEU   B HB2  1 
ATOM   6482 H  HB3  . LEU   B 1 160 ? 44.918 -36.623 -5.601  1.00 20.16 ?  160  LEU   B HB3  1 
ATOM   6483 H  HG   . LEU   B 1 160 ? 42.742 -35.799 -5.401  1.00 19.86 ?  160  LEU   B HG   1 
ATOM   6484 H  HD11 . LEU   B 1 160 ? 41.392 -36.548 -3.588  1.00 20.18 ?  160  LEU   B HD11 1 
ATOM   6485 H  HD12 . LEU   B 1 160 ? 41.550 -37.623 -4.745  1.00 20.18 ?  160  LEU   B HD12 1 
ATOM   6486 H  HD13 . LEU   B 1 160 ? 42.402 -37.760 -3.410  1.00 20.18 ?  160  LEU   B HD13 1 
ATOM   6487 H  HD21 . LEU   B 1 160 ? 42.920 -34.721 -3.363  1.00 20.00 ?  160  LEU   B HD21 1 
ATOM   6488 H  HD22 . LEU   B 1 160 ? 44.025 -35.763 -2.897  1.00 20.00 ?  160  LEU   B HD22 1 
ATOM   6489 H  HD23 . LEU   B 1 160 ? 44.338 -34.748 -4.079  1.00 20.00 ?  160  LEU   B HD23 1 
ATOM   6490 N  N    . TYR   B 1 161 ? 43.675 -36.985 -8.310  1.00 16.71 ?  161  TYR   B N    1 
ATOM   6491 C  CA   . TYR   B 1 161 ? 43.000 -36.416 -9.470  1.00 16.56 ?  161  TYR   B CA   1 
ATOM   6492 C  C    . TYR   B 1 161 ? 42.055 -37.435 -10.089 1.00 16.37 ?  161  TYR   B C    1 
ATOM   6493 O  O    . TYR   B 1 161 ? 40.883 -37.139 -10.344 1.00 16.12 ?  161  TYR   B O    1 
ATOM   6494 C  CB   . TYR   B 1 161 ? 44.039 -35.944 -10.494 1.00 17.03 ?  161  TYR   B CB   1 
ATOM   6495 C  CG   . TYR   B 1 161 ? 43.456 -35.473 -11.808 1.00 17.34 ?  161  TYR   B CG   1 
ATOM   6496 C  CD1  . TYR   B 1 161 ? 43.072 -34.149 -11.980 1.00 17.19 ?  161  TYR   B CD1  1 
ATOM   6497 C  CD2  . TYR   B 1 161 ? 43.277 -36.351 -12.872 1.00 17.73 ?  161  TYR   B CD2  1 
ATOM   6498 C  CE1  . TYR   B 1 161 ? 42.536 -33.714 -13.166 1.00 18.11 ?  161  TYR   B CE1  1 
ATOM   6499 C  CE2  . TYR   B 1 161 ? 42.735 -35.923 -14.066 1.00 19.01 ?  161  TYR   B CE2  1 
ATOM   6500 C  CZ   . TYR   B 1 161 ? 42.369 -34.601 -14.207 1.00 19.02 ?  161  TYR   B CZ   1 
ATOM   6501 O  OH   . TYR   B 1 161 ? 41.828 -34.155 -15.386 1.00 20.92 ?  161  TYR   B OH   1 
ATOM   6502 H  H    . TYR   B 1 161 ? 44.530 -36.929 -8.341  1.00 20.07 ?  161  TYR   B H    1 
ATOM   6503 H  HA   . TYR   B 1 161 ? 42.477 -35.646 -9.197  1.00 19.89 ?  161  TYR   B HA   1 
ATOM   6504 H  HB2  . TYR   B 1 161 ? 44.537 -35.201 -10.114 1.00 20.46 ?  161  TYR   B HB2  1 
ATOM   6505 H  HB3  . TYR   B 1 161 ? 44.644 -36.676 -10.689 1.00 20.46 ?  161  TYR   B HB3  1 
ATOM   6506 H  HD1  . TYR   B 1 161 ? 43.186 -33.543 -11.285 1.00 20.65 ?  161  TYR   B HD1  1 
ATOM   6507 H  HD2  . TYR   B 1 161 ? 43.518 -37.246 -12.781 1.00 21.30 ?  161  TYR   B HD2  1 
ATOM   6508 H  HE1  . TYR   B 1 161 ? 42.290 -32.819 -13.264 1.00 21.76 ?  161  TYR   B HE1  1 
ATOM   6509 H  HE2  . TYR   B 1 161 ? 42.617 -36.520 -14.771 1.00 22.83 ?  161  TYR   B HE2  1 
ATOM   6510 H  HH   . TYR   B 1 161 ? 41.777 -34.788 -15.936 1.00 25.13 ?  161  TYR   B HH   1 
ATOM   6511 N  N    . ASP   B 1 162 ? 42.551 -38.653 -10.321 1.00 16.80 ?  162  ASP   B N    1 
ATOM   6512 C  CA   . ASP   B 1 162 ? 41.722 -39.688 -10.930 1.00 17.38 ?  162  ASP   B CA   1 
ATOM   6513 C  C    . ASP   B 1 162 ? 40.520 -40.023 -10.055 1.00 16.80 ?  162  ASP   B C    1 
ATOM   6514 O  O    . ASP   B 1 162 ? 39.416 -40.235 -10.566 1.00 16.91 ?  162  ASP   B O    1 
ATOM   6515 C  CB   . ASP   B 1 162 ? 42.551 -40.948 -11.191 1.00 18.63 ?  162  ASP   B CB   1 
ATOM   6516 C  CG   . ASP   B 1 162 ? 43.545 -40.781 -12.326 1.00 19.96 ?  162  ASP   B CG   1 
ATOM   6517 O  OD1  . ASP   B 1 162 ? 43.407 -39.840 -13.130 1.00 20.42 ?  162  ASP   B OD1  1 
ATOM   6518 O  OD2  . ASP   B 1 162 ? 44.456 -41.629 -12.434 1.00 21.67 -1 162  ASP   B OD2  1 
ATOM   6519 H  H    . ASP   B 1 162 ? 43.354 -38.896 -10.138 1.00 20.19 ?  162  ASP   B H    1 
ATOM   6520 H  HA   . ASP   B 1 162 ? 41.392 -39.367 -11.783 1.00 20.87 ?  162  ASP   B HA   1 
ATOM   6521 H  HB2  . ASP   B 1 162 ? 43.057 -41.168 -10.396 1.00 22.38 ?  162  ASP   B HB2  1 
ATOM   6522 H  HB3  . ASP   B 1 162 ? 41.956 -41.676 -11.424 1.00 22.38 ?  162  ASP   B HB3  1 
ATOM   6523 N  N    . LYS   B 1 163 ? 40.716 -40.099 -8.738  1.00 16.52 ?  163  LYS   B N    1 
ATOM   6524 C  CA   . LYS   B 1 163 ? 39.594 -40.372 -7.845  1.00 17.23 ?  163  LYS   B CA   1 
ATOM   6525 C  C    . LYS   B 1 163 ? 38.549 -39.265 -7.914  1.00 15.69 ?  163  LYS   B C    1 
ATOM   6526 O  O    . LYS   B 1 163 ? 37.339 -39.538 -7.917  1.00 16.45 ?  163  LYS   B O    1 
ATOM   6527 C  CB   . LYS   B 1 163 ? 40.084 -40.536 -6.409  1.00 20.87 ?  163  LYS   B CB   1 
ATOM   6528 C  CG   . LYS   B 1 163 ? 39.008 -41.074 -5.492  1.00 27.25 ?  163  LYS   B CG   1 
ATOM   6529 C  CD   . LYS   B 1 163 ? 39.463 -41.204 -4.054  1.00 33.48 ?  163  LYS   B CD   1 
ATOM   6530 C  CE   . LYS   B 1 163 ? 38.384 -41.889 -3.226  1.00 38.68 ?  163  LYS   B CE   1 
ATOM   6531 N  NZ   . LYS   B 1 163 ? 38.492 -41.573 -1.776  1.00 41.89 ?  163  LYS   B NZ   1 
ATOM   6532 H  H    . LYS   B 1 163 ? 41.479 -39.999 -8.349  1.00 19.85 ?  163  LYS   B H    1 
ATOM   6533 H  HA   . LYS   B 1 163 ? 39.176 -41.200 -8.117  1.00 20.70 ?  163  LYS   B HA   1 
ATOM   6534 H  HB2  . LYS   B 1 163 ? 40.831 -41.156 -6.398  1.00 25.07 ?  163  LYS   B HB2  1 
ATOM   6535 H  HB3  . LYS   B 1 163 ? 40.366 -39.671 -6.070  1.00 25.07 ?  163  LYS   B HB3  1 
ATOM   6536 H  HG2  . LYS   B 1 163 ? 38.247 -40.474 -5.511  1.00 32.72 ?  163  LYS   B HG2  1 
ATOM   6537 H  HG3  . LYS   B 1 163 ? 38.742 -41.955 -5.804  1.00 32.72 ?  163  LYS   B HG3  1 
ATOM   6538 H  HD2  . LYS   B 1 163 ? 40.269 -41.744 -4.016  1.00 40.20 ?  163  LYS   B HD2  1 
ATOM   6539 H  HD3  . LYS   B 1 163 ? 39.626 -40.323 -3.684  1.00 40.20 ?  163  LYS   B HD3  1 
ATOM   6540 H  HE2  . LYS   B 1 163 ? 37.510 -41.606 -3.539  1.00 46.43 ?  163  LYS   B HE2  1 
ATOM   6541 H  HE3  . LYS   B 1 163 ? 38.472 -42.848 -3.330  1.00 46.43 ?  163  LYS   B HE3  1 
ATOM   6542 H  HZ1  . LYS   B 1 163 ? 37.845 -41.988 -1.327  1.00 50.29 ?  163  LYS   B HZ1  1 
ATOM   6543 H  HZ2  . LYS   B 1 163 ? 39.280 -41.843 -1.466  1.00 50.29 ?  163  LYS   B HZ2  1 
ATOM   6544 H  HZ3  . LYS   B 1 163 ? 38.415 -40.695 -1.650  1.00 50.29 ?  163  LYS   B HZ3  1 
ATOM   6545 N  N    . LEU   B 1 164 ? 38.999 -38.011 -7.960  1.00 14.75 ?  164  LEU   B N    1 
ATOM   6546 C  CA   . LEU   B 1 164 ? 38.089 -36.874 -8.023  1.00 14.31 ?  164  LEU   B CA   1 
ATOM   6547 C  C    . LEU   B 1 164 ? 37.310 -36.861 -9.332  1.00 14.26 ?  164  LEU   B C    1 
ATOM   6548 O  O    . LEU   B 1 164 ? 36.086 -36.667 -9.337  1.00 15.12 ?  164  LEU   B O    1 
ATOM   6549 C  CB   . LEU   B 1 164 ? 38.886 -35.579 -7.862  1.00 13.57 ?  164  LEU   B CB   1 
ATOM   6550 C  CG   . LEU   B 1 164 ? 39.426 -35.302 -6.460  1.00 14.33 ?  164  LEU   B CG   1 
ATOM   6551 C  CD1  . LEU   B 1 164 ? 40.509 -34.236 -6.509  1.00 14.45 ?  164  LEU   B CD1  1 
ATOM   6552 C  CD2  . LEU   B 1 164 ? 38.320 -34.880 -5.517  1.00 16.15 ?  164  LEU   B CD2  1 
ATOM   6553 H  H    . LEU   B 1 164 ? 39.836 -37.794 -7.963  1.00 17.72 ?  164  LEU   B H    1 
ATOM   6554 H  HA   . LEU   B 1 164 ? 37.459 -36.935 -7.298  1.00 17.20 ?  164  LEU   B HA   1 
ATOM   6555 H  HB2  . LEU   B 1 164 ? 39.651 -35.613 -8.466  1.00 16.31 ?  164  LEU   B HB2  1 
ATOM   6556 H  HB3  . LEU   B 1 164 ? 38.318 -34.837 -8.108  1.00 16.31 ?  164  LEU   B HB3  1 
ATOM   6557 H  HG   . LEU   B 1 164 ? 39.830 -36.110 -6.113  1.00 17.22 ?  164  LEU   B HG   1 
ATOM   6558 H  HD11 . LEU   B 1 164 ? 40.833 -34.070 -5.607  1.00 17.37 ?  164  LEU   B HD11 1 
ATOM   6559 H  HD12 . LEU   B 1 164 ? 41.243 -34.547 -7.066  1.00 17.37 ?  164  LEU   B HD12 1 
ATOM   6560 H  HD13 . LEU   B 1 164 ? 40.140 -33.419 -6.879  1.00 17.37 ?  164  LEU   B HD13 1 
ATOM   6561 H  HD21 . LEU   B 1 164 ? 38.705 -34.654 -4.657  1.00 19.40 ?  164  LEU   B HD21 1 
ATOM   6562 H  HD22 . LEU   B 1 164 ? 37.863 -34.109 -5.888  1.00 19.40 ?  164  LEU   B HD22 1 
ATOM   6563 H  HD23 . LEU   B 1 164 ? 37.696 -35.617 -5.417  1.00 19.40 ?  164  LEU   B HD23 1 
ATOM   6564 N  N    . VAL   B 1 165 ? 38.006 -37.032 -10.457 1.00 15.93 ?  165  VAL   B N    1 
ATOM   6565 C  CA   . VAL   B 1 165 ? 37.355 -36.970 -11.760 1.00 17.31 ?  165  VAL   B CA   1 
ATOM   6566 C  C    . VAL   B 1 165 ? 36.434 -38.167 -11.946 1.00 18.93 ?  165  VAL   B C    1 
ATOM   6567 O  O    . VAL   B 1 165 ? 35.273 -38.025 -12.349 1.00 19.67 ?  165  VAL   B O    1 
ATOM   6568 C  CB   . VAL   B 1 165 ? 38.406 -36.887 -12.882 1.00 18.09 ?  165  VAL   B CB   1 
ATOM   6569 C  CG1  . VAL   B 1 165 ? 37.746 -37.011 -14.239 1.00 19.29 ?  165  VAL   B CG1  1 
ATOM   6570 C  CG2  . VAL   B 1 165 ? 39.187 -35.595 -12.785 1.00 17.78 ?  165  VAL   B CG2  1 
ATOM   6571 H  H    . VAL   B 1 165 ? 38.855 -37.180 -10.494 1.00 19.14 ?  165  VAL   B H    1 
ATOM   6572 H  HA   . VAL   B 1 165 ? 36.813 -36.170 -11.808 1.00 20.79 ?  165  VAL   B HA   1 
ATOM   6573 H  HB   . VAL   B 1 165 ? 39.036 -37.621 -12.784 1.00 21.73 ?  165  VAL   B HB   1 
ATOM   6574 H  HG11 . VAL   B 1 165 ? 38.365 -36.710 -14.920 1.00 23.17 ?  165  VAL   B HG11 1 
ATOM   6575 H  HG12 . VAL   B 1 165 ? 37.521 -37.944 -14.394 1.00 23.17 ?  165  VAL   B HG12 1 
ATOM   6576 H  HG13 . VAL   B 1 165 ? 36.945 -36.470 -14.251 1.00 23.17 ?  165  VAL   B HG13 1 
ATOM   6577 H  HG21 . VAL   B 1 165 ? 39.819 -35.549 -13.521 1.00 21.36 ?  165  VAL   B HG21 1 
ATOM   6578 H  HG22 . VAL   B 1 165 ? 38.569 -34.848 -12.837 1.00 21.36 ?  165  VAL   B HG22 1 
ATOM   6579 H  HG23 . VAL   B 1 165 ? 39.662 -35.572 -11.940 1.00 21.36 ?  165  VAL   B HG23 1 
ATOM   6580 N  N    . SER   B 1 166 ? 36.943 -39.368 -11.652 1.00 19.75 ?  166  SER   B N    1 
ATOM   6581 C  CA   . SER   B 1 166 ? 36.190 -40.583 -11.935 1.00 20.92 ?  166  SER   B CA   1 
ATOM   6582 C  C    . SER   B 1 166 ? 34.927 -40.677 -11.090 1.00 21.04 ?  166  SER   B C    1 
ATOM   6583 O  O    . SER   B 1 166 ? 33.960 -41.311 -11.513 1.00 22.47 ?  166  SER   B O    1 
ATOM   6584 C  CB   . SER   B 1 166 ? 37.059 -41.833 -11.745 1.00 21.74 ?  166  SER   B CB   1 
ATOM   6585 O  OG   . SER   B 1 166 ? 37.398 -42.039 -10.383 1.00 21.63 ?  166  SER   B OG   1 
ATOM   6586 H  H    . SER   B 1 166 ? 37.719 -39.502 -11.297 1.00 23.73 ?  166  SER   B H    1 
ATOM   6587 H  HA   . SER   B 1 166 ? 35.920 -40.566 -12.867 1.00 25.13 ?  166  SER   B HA   1 
ATOM   6588 H  HB2  . SER   B 1 166 ? 36.568 -42.607 -12.064 1.00 26.12 ?  166  SER   B HB2  1 
ATOM   6589 H  HB3  . SER   B 1 166 ? 37.876 -41.730 -12.261 1.00 26.12 ?  166  SER   B HB3  1 
ATOM   6590 H  HG   . SER   B 1 166 ? 37.828 -41.374 -10.097 1.00 25.98 ?  166  SER   B HG   1 
ATOM   6591 N  N    . SER   B 1 167 ? 34.908 -40.064 -9.906  1.00 19.58 ?  167  SER   B N    1 
ATOM   6592 C  CA   . SER   B 1 167 ? 33.749 -40.125 -9.020  1.00 19.07 ?  167  SER   B CA   1 
ATOM   6593 C  C    . SER   B 1 167 ? 32.831 -38.907 -9.116  1.00 18.37 ?  167  SER   B C    1 
ATOM   6594 O  O    . SER   B 1 167 ? 31.751 -38.914 -8.513  1.00 18.72 ?  167  SER   B O    1 
ATOM   6595 C  CB   . SER   B 1 167 ? 34.198 -40.303 -7.564  1.00 18.96 ?  167  SER   B CB   1 
ATOM   6596 O  OG   . SER   B 1 167 ? 34.867 -39.141 -7.096  1.00 18.52 ?  167  SER   B OG   1 
ATOM   6597 H  H    . SER   B 1 167 ? 35.562 -39.618 -9.590  1.00 23.52 ?  167  SER   B H    1 
ATOM   6598 H  HA   . SER   B 1 167 ? 33.220 -40.906 -9.258  1.00 22.90 ?  167  SER   B HA   1 
ATOM   6599 H  HB2  . SER   B 1 167 ? 33.414 -40.470 -7.013  1.00 22.78 ?  167  SER   B HB2  1 
ATOM   6600 H  HB3  . SER   B 1 167 ? 34.797 -41.071 -7.514  1.00 22.78 ?  167  SER   B HB3  1 
ATOM   6601 H  HG   . SER   B 1 167 ? 35.549 -39.006 -7.564  1.00 22.25 ?  167  SER   B HG   1 
ATOM   6602 N  N    . PHE   B 1 168 ? 33.211 -37.870 -9.863  1.00 18.02 ?  168  PHE   B N    1 
ATOM   6603 C  CA   . PHE   B 1 168 ? 32.378 -36.668 -9.920  1.00 17.27 ?  168  PHE   B CA   1 
ATOM   6604 C  C    . PHE   B 1 168 ? 31.062 -36.926 -10.650 1.00 15.32 ?  168  PHE   B C    1 
ATOM   6605 O  O    . PHE   B 1 168 ? 30.020 -36.334 -10.306 1.00 15.83 ?  168  PHE   B O    1 
ATOM   6606 C  CB   . PHE   B 1 168 ? 33.141 -35.527 -10.586 1.00 18.10 ?  168  PHE   B CB   1 
ATOM   6607 C  CG   . PHE   B 1 168 ? 32.332 -34.278 -10.723 1.00 18.15 ?  168  PHE   B CG   1 
ATOM   6608 C  CD1  . PHE   B 1 168 ? 31.994 -33.539 -9.599  1.00 19.17 ?  168  PHE   B CD1  1 
ATOM   6609 C  CD2  . PHE   B 1 168 ? 31.892 -33.851 -11.958 1.00 17.69 ?  168  PHE   B CD2  1 
ATOM   6610 C  CE1  . PHE   B 1 168 ? 31.231 -32.393 -9.703  1.00 19.36 ?  168  PHE   B CE1  1 
ATOM   6611 C  CE2  . PHE   B 1 168 ? 31.142 -32.688 -12.077 1.00 18.58 ?  168  PHE   B CE2  1 
ATOM   6612 C  CZ   . PHE   B 1 168 ? 30.806 -31.959 -10.943 1.00 18.73 ?  168  PHE   B CZ   1 
ATOM   6613 H  H    . PHE   B 1 168 ? 33.932 -37.835 -10.333 1.00 21.65 ?  168  PHE   B H    1 
ATOM   6614 H  HA   . PHE   B 1 168 ? 32.163 -36.395 -9.019  1.00 20.74 ?  168  PHE   B HA   1 
ATOM   6615 H  HB2  . PHE   B 1 168 ? 33.923 -35.316 -10.051 1.00 21.75 ?  168  PHE   B HB2  1 
ATOM   6616 H  HB3  . PHE   B 1 168 ? 33.413 -35.799 -11.475 1.00 21.75 ?  168  PHE   B HB3  1 
ATOM   6617 H  HD1  . PHE   B 1 168 ? 32.274 -33.828 -8.760  1.00 23.03 ?  168  PHE   B HD1  1 
ATOM   6618 H  HD2  . PHE   B 1 168 ? 32.118 -34.327 -12.719 1.00 21.25 ?  168  PHE   B HD2  1 
ATOM   6619 H  HE1  . PHE   B 1 168 ? 31.011 -31.909 -8.940  1.00 23.26 ?  168  PHE   B HE1  1 
ATOM   6620 H  HE2  . PHE   B 1 168 ? 30.851 -32.401 -12.915 1.00 22.32 ?  168  PHE   B HE2  1 
ATOM   6621 H  HZ   . PHE   B 1 168 ? 30.292 -31.184 -11.019 1.00 22.50 ?  168  PHE   B HZ   1 
ATOM   6622 N  N    . LEU   B 1 169 ? 31.094 -37.803 -11.650 1.00 15.61 ?  169  LEU   B N    1 
ATOM   6623 C  CA   . LEU   B 1 169 ? 29.920 -38.106 -12.454 1.00 17.44 ?  169  LEU   B CA   1 
ATOM   6624 C  C    . LEU   B 1 169 ? 29.912 -39.540 -12.960 1.00 20.02 ?  169  LEU   B C    1 
ATOM   6625 O  O    . LEU   B 1 169 ? 28.996 -39.960 -13.668 1.00 22.32 ?  169  LEU   B O    1 
ATOM   6626 C  CB   . LEU   B 1 169 ? 29.849 -37.161 -13.651 1.00 19.34 ?  169  LEU   B CB   1 
ATOM   6627 C  CG   . LEU   B 1 169 ? 28.590 -36.300 -13.746 1.00 22.31 ?  169  LEU   B CG   1 
ATOM   6628 C  CD1  . LEU   B 1 169 ? 28.529 -35.634 -15.102 1.00 23.28 ?  169  LEU   B CD1  1 
ATOM   6629 C  CD2  . LEU   B 1 169 ? 27.338 -37.120 -13.489 1.00 22.35 ?  169  LEU   B CD2  1 
ATOM   6630 O  OXT  . LEU   B 1 169 ? 30.836 -40.294 -12.679 1.00 20.81 -1 169  LEU   B OXT  1 
ATOM   6631 H  H    . LEU   B 1 169 ? 31.799 -38.236 -11.892 1.00 18.76 ?  169  LEU   B H    1 
ATOM   6632 H  HA   . LEU   B 1 169 ? 29.138 -37.971 -11.905 1.00 20.96 ?  169  LEU   B HA   1 
ATOM   6633 H  HB2  . LEU   B 1 169 ? 30.608 -36.557 -13.618 1.00 23.23 ?  169  LEU   B HB2  1 
ATOM   6634 H  HB3  . LEU   B 1 169 ? 29.895 -37.689 -14.465 1.00 23.23 ?  169  LEU   B HB3  1 
ATOM   6635 H  HG   . LEU   B 1 169 ? 28.634 -35.601 -13.074 1.00 26.80 ?  169  LEU   B HG   1 
ATOM   6636 H  HD11 . LEU   B 1 169 ? 27.741 -35.070 -15.140 1.00 27.96 ?  169  LEU   B HD11 1 
ATOM   6637 H  HD12 . LEU   B 1 169 ? 29.327 -35.097 -15.225 1.00 27.96 ?  169  LEU   B HD12 1 
ATOM   6638 H  HD13 . LEU   B 1 169 ? 28.481 -36.319 -15.786 1.00 27.96 ?  169  LEU   B HD13 1 
ATOM   6639 H  HD21 . LEU   B 1 169 ? 26.584 -36.694 -13.921 1.00 26.84 ?  169  LEU   B HD21 1 
ATOM   6640 H  HD22 . LEU   B 1 169 ? 27.466 -38.013 -13.852 1.00 26.84 ?  169  LEU   B HD22 1 
ATOM   6641 H  HD23 . LEU   B 1 169 ? 27.188 -37.173 -12.533 1.00 26.84 ?  169  LEU   B HD23 1 
HETATM 6642 C  C1   T TFA   C 2 .   ? 12.113 -1.369  1.452   0.20 10.05 ?  201  TFA   A C1   1 
HETATM 6643 C  C2   T TFA   C 2 .   ? 12.731 -1.768  0.082   0.20 12.22 ?  201  TFA   A C2   1 
HETATM 6644 O  O    T TFA   C 2 .   ? 12.848 -1.607  2.417   0.20 8.88  ?  201  TFA   A O    1 
HETATM 6645 F  F1   T TFA   C 2 .   ? 12.815 -3.104  -0.052  0.20 13.09 ?  201  TFA   A F1   1 
HETATM 6646 F  F2   T TFA   C 2 .   ? 11.994 -1.360  -0.964  0.20 12.49 ?  201  TFA   A F2   1 
HETATM 6647 F  F3   T TFA   C 2 .   ? 13.962 -1.274  -0.102  0.20 13.38 ?  201  TFA   A F3   1 
HETATM 6648 O  OXT  T TFA   C 2 .   ? 10.987 -0.869  1.411   0.20 9.33  ?  201  TFA   A OXT  1 
HETATM 6649 S  S    B DMS   D 3 .   ? 10.756 -1.060  -3.701  0.50 23.85 ?  202  DMS   A S    1 
HETATM 6650 O  O    B DMS   D 3 .   ? 12.067 -1.711  -3.342  0.50 22.90 ?  202  DMS   A O    1 
HETATM 6651 C  C1   B DMS   D 3 .   ? 10.397 -1.595  -5.398  0.50 23.67 ?  202  DMS   A C1   1 
HETATM 6652 C  C2   B DMS   D 3 .   ? 11.023 0.710   -4.032  0.50 23.98 ?  202  DMS   A C2   1 
HETATM 6653 H  H11  B DMS   D 3 .   ? 11.277 -1.422  -5.910  0.50 28.43 ?  202  DMS   A H11  1 
HETATM 6654 H  H12  B DMS   D 3 .   ? 9.613  -1.003  -5.715  0.50 28.43 ?  202  DMS   A H12  1 
HETATM 6655 H  H13  B DMS   D 3 .   ? 10.142 -2.606  -5.354  0.50 28.43 ?  202  DMS   A H13  1 
HETATM 6656 H  H21  B DMS   D 3 .   ? 10.084 1.121   -4.209  0.50 28.80 ?  202  DMS   A H21  1 
HETATM 6657 H  H22  B DMS   D 3 .   ? 11.478 1.120   -3.186  0.50 28.80 ?  202  DMS   A H22  1 
HETATM 6658 H  H23  B DMS   D 3 .   ? 11.635 0.721   -4.862  0.50 28.80 ?  202  DMS   A H23  1 
HETATM 6659 S  S    B DMS   E 3 .   ? 11.197 6.284   6.512   0.50 41.71 ?  203  DMS   A S    1 
HETATM 6660 O  O    B DMS   E 3 .   ? 12.333 5.357   6.152   0.50 41.42 ?  203  DMS   A O    1 
HETATM 6661 C  C1   B DMS   E 3 .   ? 11.921 7.685   7.415   0.50 41.47 ?  203  DMS   A C1   1 
HETATM 6662 C  C2   B DMS   E 3 .   ? 10.239 5.471   7.823   0.50 41.45 ?  203  DMS   A C2   1 
HETATM 6663 H  H11  B DMS   E 3 .   ? 11.149 8.365   7.523   0.50 49.79 ?  203  DMS   A H11  1 
HETATM 6664 H  H12  B DMS   E 3 .   ? 12.709 8.054   6.847   0.50 49.79 ?  203  DMS   A H12  1 
HETATM 6665 H  H13  B DMS   E 3 .   ? 12.231 7.271   8.312   0.50 49.79 ?  203  DMS   A H13  1 
HETATM 6666 H  H21  B DMS   E 3 .   ? 9.421  6.081   7.982   0.50 49.76 ?  203  DMS   A H21  1 
HETATM 6667 H  H22  B DMS   E 3 .   ? 10.891 5.441   8.626   0.50 49.76 ?  203  DMS   A H22  1 
HETATM 6668 H  H23  B DMS   E 3 .   ? 9.978  4.526   7.478   0.50 49.76 ?  203  DMS   A H23  1 
HETATM 6669 N  N2   B A1BAO F 4 .   ? 14.760 -0.161  3.812   0.50 9.98  ?  204  A1BAO A N2   1 
HETATM 6670 C  C3   B A1BAO F 4 .   ? 14.150 0.107   -0.467  0.50 11.23 ?  204  A1BAO A C3   1 
HETATM 6671 C  C6   B A1BAO F 4 .   ? 11.355 2.804   -0.534  0.50 15.81 ?  204  A1BAO A C6   1 
HETATM 6672 C  C9   B A1BAO F 4 .   ? 11.581 0.019   -0.476  0.50 14.81 ?  204  A1BAO A C9   1 
HETATM 6673 C  C12  B A1BAO F 4 .   ? 15.247 2.079   5.150   0.50 9.91  ?  204  A1BAO A C12  1 
HETATM 6674 C  C14  B A1BAO F 4 .   ? 15.620 3.533   3.462   0.50 8.93  ?  204  A1BAO A C14  1 
HETATM 6675 C  C1   B A1BAO F 4 .   ? 15.941 -1.176  0.773   0.50 10.51 ?  204  A1BAO A C1   1 
HETATM 6676 C  C10  B A1BAO F 4 .   ? 15.027 0.968   3.078   0.50 9.25  ?  204  A1BAO A C10  1 
HETATM 6677 C  C11  B A1BAO F 4 .   ? 14.749 -0.087  5.188   0.50 10.58 ?  204  A1BAO A C11  1 
HETATM 6678 C  C13  B A1BAO F 4 .   ? 15.293 2.177   3.757   0.50 9.13  ?  204  A1BAO A C13  1 
HETATM 6679 C  C15  B A1BAO F 4 .   ? 15.743 4.218   4.647   0.50 9.27  ?  204  A1BAO A C15  1 
HETATM 6680 C  C2   B A1BAO F 4 .   ? 14.687 -0.265  0.933   0.50 9.89  ?  204  A1BAO A C2   1 
HETATM 6681 C  C4   B A1BAO F 4 .   ? 12.768 0.777   -0.482  0.50 12.86 ?  204  A1BAO A C4   1 
HETATM 6682 C  C5   B A1BAO F 4 .   ? 12.617 2.181   -0.514  0.50 14.66 ?  204  A1BAO A C5   1 
HETATM 6683 C  C7   B A1BAO F 4 .   ? 10.187 2.017   -0.520  0.50 15.45 ?  204  A1BAO A C7   1 
HETATM 6684 C  C8   B A1BAO F 4 .   ? 10.310 0.618   -0.492  0.50 15.75 ?  204  A1BAO A C8   1 
HETATM 6685 N  N1   B A1BAO F 4 .   ? 15.034 0.905   1.714   0.50 8.80  ?  204  A1BAO A N1   1 
HETATM 6686 N  N3   B A1BAO F 4 .   ? 14.977 0.994   5.945   0.50 10.44 ?  204  A1BAO A N3   1 
HETATM 6687 N  N4   B A1BAO F 4 .   ? 15.521 3.319   5.727   0.50 9.54  ?  204  A1BAO A N4   1 
HETATM 6688 O  O1   B A1BAO F 4 .   ? 15.550 -2.342  0.114   0.50 11.49 ?  204  A1BAO A O1   1 
HETATM 6689 O  O2   B A1BAO F 4 .   ? 8.959  2.611   -0.544  0.50 16.02 ?  204  A1BAO A O2   1 
HETATM 6690 H  H6   B A1BAO F 4 .   ? 14.914 0.737   -0.929  0.50 13.50 ?  204  A1BAO A H6   1 
HETATM 6691 H  H5   B A1BAO F 4 .   ? 14.171 -0.814  -1.118  0.50 13.50 ?  204  A1BAO A H5   1 
HETATM 6692 H  H8   B A1BAO F 4 .   ? 11.273 3.923   -0.559  0.50 19.00 ?  204  A1BAO A H8   1 
HETATM 6693 H  H11  B A1BAO F 4 .   ? 11.649 -1.102  -0.451  0.50 17.80 ?  204  A1BAO A H11  1 
HETATM 6694 H  H14  B A1BAO F 4 .   ? 15.749 4.043   2.512   0.50 10.74 ?  204  A1BAO A H14  1 
HETATM 6695 H  H4   B A1BAO F 4 .   ? 16.751 -0.634  0.215   0.50 12.64 ?  204  A1BAO A H4   1 
HETATM 6696 H  H3   B A1BAO F 4 .   ? 16.365 -1.395  1.788   0.50 12.64 ?  204  A1BAO A H3   1 
HETATM 6697 H  H13  B A1BAO F 4 .   ? 14.517 -1.018  5.789   0.50 12.72 ?  204  A1BAO A H13  1 
HETATM 6698 H  H15  B A1BAO F 4 .   ? 15.973 5.207   5.006   0.50 11.15 ?  204  A1BAO A H15  1 
HETATM 6699 H  H1   B A1BAO F 4 .   ? 13.856 -0.832  1.451   0.50 11.89 ?  204  A1BAO A H1   1 
HETATM 6700 H  H7   B A1BAO F 4 .   ? 13.547 2.817   -0.523  0.50 17.61 ?  204  A1BAO A H7   1 
HETATM 6701 H  H10  B A1BAO F 4 .   ? 9.391  -0.021  -0.487  0.50 18.93 ?  204  A1BAO A H10  1 
HETATM 6702 H  H12  B A1BAO F 4 .   ? 15.299 1.721   1.157   0.50 10.59 ?  204  A1BAO A H12  1 
HETATM 6703 H  H16  B A1BAO F 4 .   ? 15.556 3.538   6.659   0.50 11.47 ?  204  A1BAO A H16  1 
HETATM 6704 H  H2   B A1BAO F 4 .   ? 16.234 -3.014  0.178   0.50 13.81 ?  204  A1BAO A H2   1 
HETATM 6705 H  H9   B A1BAO F 4 .   ? 8.573  2.794   0.344   0.50 19.24 ?  204  A1BAO A H9   1 
HETATM 6706 CL CL   B CL    G 5 .   ? 16.236 2.861   -1.105  0.50 15.30 ?  205  CL    A CL   1 
HETATM 6707 O  O    . HOH   H 6 .   ? 11.645 -10.810 -10.093 1.00 42.31 ?  1301 HOH   A O    1 
HETATM 6708 O  O    . HOH   H 6 .   ? 18.554 -2.374  -16.433 1.00 46.60 ?  1302 HOH   A O    1 
HETATM 6709 O  O    . HOH   H 6 .   ? 14.742 -4.632  20.470  1.00 42.13 ?  1303 HOH   A O    1 
HETATM 6710 O  O    . HOH   H 6 .   ? 7.930  -12.644 -0.885  1.00 22.93 ?  1304 HOH   A O    1 
HETATM 6711 O  O    A HOH   H 6 .   ? 4.659  3.927   0.588   0.50 21.77 ?  1305 HOH   A O    1 
HETATM 6712 O  O    B HOH   H 6 .   ? 13.612 -1.016  -6.826  0.50 24.67 ?  1306 HOH   A O    1 
HETATM 6713 O  O    . HOH   H 6 .   ? 15.134 -12.222 18.604  1.00 35.03 ?  1307 HOH   A O    1 
HETATM 6714 O  O    . HOH   H 6 .   ? 28.313 -0.147  -13.419 1.00 35.54 ?  1308 HOH   A O    1 
HETATM 6715 O  O    B HOH   H 6 .   ? 14.862 -2.666  3.463   0.50 16.02 ?  1309 HOH   A O    1 
HETATM 6716 O  O    . HOH   H 6 .   ? 34.270 -1.825  12.509  1.00 34.04 ?  1310 HOH   A O    1 
HETATM 6717 O  O    . HOH   H 6 .   ? 14.177 -4.496  -11.877 1.00 34.74 ?  1311 HOH   A O    1 
HETATM 6718 O  O    . HOH   H 6 .   ? 28.908 0.397   -9.731  1.00 20.11 ?  1312 HOH   A O    1 
HETATM 6719 O  O    . HOH   H 6 .   ? 14.679 -13.945 16.623  1.00 23.64 ?  1313 HOH   A O    1 
HETATM 6720 O  O    . HOH   H 6 .   ? 30.219 -13.310 -8.458  1.00 18.63 ?  1314 HOH   A O    1 
HETATM 6721 O  O    . HOH   H 6 .   ? 14.889 3.992   17.510  1.00 36.00 ?  1315 HOH   A O    1 
HETATM 6722 O  O    . HOH   H 6 .   ? 42.384 10.544  5.122   1.00 19.17 ?  1316 HOH   A O    1 
HETATM 6723 O  O    . HOH   H 6 .   ? 9.199  -10.045 19.422  1.00 39.79 ?  1317 HOH   A O    1 
HETATM 6724 O  O    . HOH   H 6 .   ? 13.580 -15.219 -7.444  1.00 23.64 ?  1318 HOH   A O    1 
HETATM 6725 O  O    . HOH   H 6 .   ? 36.125 -5.095  -0.486  1.00 29.24 ?  1319 HOH   A O    1 
HETATM 6726 O  O    . HOH   H 6 .   ? 11.979 0.323   14.709  1.00 29.00 ?  1320 HOH   A O    1 
HETATM 6727 O  O    A HOH   H 6 .   ? 3.560  -9.453  9.704   0.50 24.96 ?  1321 HOH   A O    1 
HETATM 6728 O  O    . HOH   H 6 .   ? 7.600  -6.285  -6.547  1.00 38.77 ?  1322 HOH   A O    1 
HETATM 6729 O  O    . HOH   H 6 .   ? 19.924 -12.613 -8.784  1.00 23.93 ?  1323 HOH   A O    1 
HETATM 6730 O  O    A HOH   H 6 .   ? 14.237 0.585   6.780   0.50 19.11 ?  1324 HOH   A O    1 
HETATM 6731 O  O    B HOH   H 6 .   ? 21.541 2.949   -0.058  0.50 13.02 ?  1325 HOH   A O    1 
HETATM 6732 O  O    . HOH   H 6 .   ? 28.131 -6.254  19.622  1.00 38.73 ?  1326 HOH   A O    1 
HETATM 6733 O  O    . HOH   H 6 .   ? 26.474 -19.303 -1.780  1.00 13.02 ?  1327 HOH   A O    1 
HETATM 6734 O  O    . HOH   H 6 .   ? 30.887 6.236   -12.183 1.00 26.21 ?  1328 HOH   A O    1 
HETATM 6735 O  O    . HOH   H 6 .   ? 0.639  -4.509  0.053   1.00 28.74 ?  1329 HOH   A O    1 
HETATM 6736 O  O    . HOH   H 6 .   ? 30.990 -18.101 7.796   1.00 18.36 ?  1330 HOH   A O    1 
HETATM 6737 O  O    . HOH   H 6 .   ? 18.668 -19.342 13.517  1.00 31.00 ?  1331 HOH   A O    1 
HETATM 6738 O  O    . HOH   H 6 .   ? 38.217 10.168  7.144   1.00 37.50 ?  1332 HOH   A O    1 
HETATM 6739 O  O    . HOH   H 6 .   ? -0.736 -8.509  1.951   1.00 38.82 ?  1333 HOH   A O    1 
HETATM 6740 O  O    . HOH   H 6 .   ? 37.480 2.785   10.212  1.00 24.49 ?  1334 HOH   A O    1 
HETATM 6741 O  O    . HOH   H 6 .   ? 22.200 5.369   18.906  1.00 44.08 ?  1335 HOH   A O    1 
HETATM 6742 O  O    . HOH   H 6 .   ? 25.714 -0.858  -7.437  1.00 15.55 ?  1336 HOH   A O    1 
HETATM 6743 O  O    . HOH   H 6 .   ? 44.280 7.140   6.421   1.00 25.76 ?  1337 HOH   A O    1 
HETATM 6744 O  O    . HOH   H 6 .   ? 27.252 13.758  2.848   1.00 26.60 ?  1338 HOH   A O    1 
HETATM 6745 O  O    . HOH   H 6 .   ? 17.167 -18.045 14.950  1.00 25.39 ?  1339 HOH   A O    1 
HETATM 6746 O  O    . HOH   H 6 .   ? 39.695 -1.040  -5.177  1.00 20.37 ?  1340 HOH   A O    1 
HETATM 6747 O  O    . HOH   H 6 .   ? 31.656 8.206   14.811  1.00 21.79 ?  1341 HOH   A O    1 
HETATM 6748 O  O    . HOH   H 6 .   ? 20.616 -19.689 -5.065  1.00 24.07 ?  1342 HOH   A O    1 
HETATM 6749 O  O    . HOH   H 6 .   ? 18.900 -21.967 6.893   1.00 27.76 ?  1343 HOH   A O    1 
HETATM 6750 O  O    A HOH   H 6 .   ? 14.600 -3.643  3.078   0.50 15.39 ?  1344 HOH   A O    1 
HETATM 6751 O  O    B HOH   H 6 .   ? 15.293 6.747   6.996   0.50 18.89 ?  1345 HOH   A O    1 
HETATM 6752 O  O    . HOH   H 6 .   ? 38.505 4.977   7.000   1.00 14.47 ?  1346 HOH   A O    1 
HETATM 6753 O  O    . HOH   H 6 .   ? 33.960 -1.037  -8.944  1.00 24.69 ?  1347 HOH   A O    1 
HETATM 6754 O  O    . HOH   H 6 .   ? 17.117 -17.771 -5.038  1.00 25.25 ?  1348 HOH   A O    1 
HETATM 6755 O  O    A HOH   H 6 .   ? 13.280 -1.426  -6.544  0.50 13.01 ?  1349 HOH   A O    1 
HETATM 6756 O  O    . HOH   H 6 .   ? 14.339 -21.137 -4.290  1.00 27.17 ?  1350 HOH   A O    1 
HETATM 6757 O  O    . HOH   H 6 .   ? 22.738 12.522  1.617   1.00 13.36 ?  1351 HOH   A O    1 
HETATM 6758 O  O    . HOH   H 6 .   ? 26.817 11.416  1.658   1.00 14.88 ?  1352 HOH   A O    1 
HETATM 6759 O  O    . HOH   H 6 .   ? 42.526 4.290   5.395   1.00 31.28 ?  1353 HOH   A O    1 
HETATM 6760 O  O    . HOH   H 6 .   ? 21.327 -2.261  -2.493  1.00 15.07 ?  1354 HOH   A O    1 
HETATM 6761 O  O    A HOH   H 6 .   ? 17.462 -1.702  0.425   0.50 17.64 ?  1355 HOH   A O    1 
HETATM 6762 O  O    . HOH   H 6 .   ? 35.749 -12.636 6.849   1.00 14.66 ?  1356 HOH   A O    1 
HETATM 6763 O  O    . HOH   H 6 .   ? 27.880 0.808   -7.139  1.00 13.41 ?  1357 HOH   A O    1 
HETATM 6764 O  O    . HOH   H 6 .   ? 24.017 -2.104  -2.128  1.00 9.97  ?  1358 HOH   A O    1 
HETATM 6765 O  O    . HOH   H 6 .   ? 30.737 3.095   8.278   1.00 11.11 ?  1359 HOH   A O    1 
HETATM 6766 O  O    . HOH   H 6 .   ? 22.614 -11.927 21.794  1.00 46.34 ?  1360 HOH   A O    1 
HETATM 6767 O  O    . HOH   H 6 .   ? 18.524 9.451   8.940   1.00 20.29 ?  1361 HOH   A O    1 
HETATM 6768 O  O    . HOH   H 6 .   ? 22.158 -19.234 11.405  1.00 32.62 ?  1362 HOH   A O    1 
HETATM 6769 O  O    A HOH   H 6 .   ? -0.513 -3.082  3.069   0.50 28.42 ?  1363 HOH   A O    1 
HETATM 6770 O  O    . HOH   H 6 .   ? 33.607 -7.155  4.311   1.00 15.46 ?  1364 HOH   A O    1 
HETATM 6771 O  O    . HOH   H 6 .   ? 37.255 11.990  4.954   1.00 28.59 ?  1365 HOH   A O    1 
HETATM 6772 O  O    . HOH   H 6 .   ? 31.070 -13.935 -2.431  1.00 12.37 ?  1366 HOH   A O    1 
HETATM 6773 O  O    . HOH   H 6 .   ? 15.148 -8.053  -9.723  1.00 21.18 ?  1367 HOH   A O    1 
HETATM 6774 O  O    . HOH   H 6 .   ? 15.446 11.900  7.793   1.00 32.73 ?  1368 HOH   A O    1 
HETATM 6775 O  O    . HOH   H 6 .   ? 43.292 7.809   2.679   1.00 26.84 ?  1369 HOH   A O    1 
HETATM 6776 O  O    . HOH   H 6 .   ? 43.892 8.438   -3.071  1.00 25.94 ?  1370 HOH   A O    1 
HETATM 6777 O  O    . HOH   H 6 .   ? 21.882 -21.893 8.410   1.00 27.85 ?  1371 HOH   A O    1 
HETATM 6778 O  O    . HOH   H 6 .   ? 16.999 -19.266 4.887   1.00 13.90 ?  1372 HOH   A O    1 
HETATM 6779 O  O    . HOH   H 6 .   ? 37.219 -2.837  9.712   1.00 39.07 ?  1373 HOH   A O    1 
HETATM 6780 O  O    . HOH   H 6 .   ? 27.411 -10.596 14.065  1.00 16.17 ?  1374 HOH   A O    1 
HETATM 6781 O  O    A HOH   H 6 .   ? 11.032 -0.369  1.912   0.30 17.71 ?  1375 HOH   A O    1 
HETATM 6782 O  O    . HOH   H 6 .   ? 14.561 -0.517  -12.189 1.00 24.20 ?  1376 HOH   A O    1 
HETATM 6783 O  O    T HOH   H 6 .   ? 15.372 -0.410  2.368   0.20 9.98  ?  1377 HOH   A O    1 
HETATM 6784 O  O    A HOH   H 6 .   ? 6.908  -8.150  11.824  0.50 14.72 ?  1378 HOH   A O    1 
HETATM 6785 O  O    . HOH   H 6 .   ? 31.941 -9.320  -6.593  1.00 21.13 ?  1379 HOH   A O    1 
HETATM 6786 O  O    . HOH   H 6 .   ? 9.911  -21.421 5.697   1.00 17.39 ?  1380 HOH   A O    1 
HETATM 6787 O  O    . HOH   H 6 .   ? 21.142 10.196  15.000  1.00 36.41 ?  1381 HOH   A O    1 
HETATM 6788 O  O    . HOH   H 6 .   ? 24.107 -7.719  14.398  1.00 15.10 ?  1382 HOH   A O    1 
HETATM 6789 O  O    . HOH   H 6 .   ? 31.815 -7.284  -9.820  1.00 20.31 ?  1383 HOH   A O    1 
HETATM 6790 O  O    . HOH   H 6 .   ? 24.577 2.006   -7.091  1.00 24.74 ?  1384 HOH   A O    1 
HETATM 6791 O  O    . HOH   H 6 .   ? 13.916 -4.968  17.395  1.00 23.67 ?  1385 HOH   A O    1 
HETATM 6792 O  O    . HOH   H 6 .   ? 16.567 -22.044 1.000   1.00 26.86 ?  1386 HOH   A O    1 
HETATM 6793 O  O    B HOH   H 6 .   ? 13.010 -3.019  -1.026  0.50 24.20 ?  1387 HOH   A O    1 
HETATM 6794 O  O    . HOH   H 6 .   ? 8.532  -21.128 4.029   1.00 50.74 ?  1388 HOH   A O    1 
HETATM 6795 O  O    B HOH   H 6 .   ? 22.634 5.589   -1.925  0.50 22.06 ?  1389 HOH   A O    1 
HETATM 6796 O  O    . HOH   H 6 .   ? 14.481 -24.651 11.573  1.00 35.29 ?  1390 HOH   A O    1 
HETATM 6797 O  O    A HOH   H 6 .   ? 8.963  -12.110 17.166  0.50 29.44 ?  1391 HOH   A O    1 
HETATM 6798 O  O    . HOH   H 6 .   ? 24.630 -17.508 12.689  1.00 22.15 ?  1392 HOH   A O    1 
HETATM 6799 O  O    . HOH   H 6 .   ? 24.434 3.572   -1.823  1.00 12.97 ?  1393 HOH   A O    1 
HETATM 6800 O  O    . HOH   H 6 .   ? 37.467 -1.981  5.782   1.00 25.37 ?  1394 HOH   A O    1 
HETATM 6801 O  O    B HOH   H 6 .   ? 11.015 2.175   12.119  0.50 25.45 ?  1395 HOH   A O    1 
HETATM 6802 O  O    . HOH   H 6 .   ? 27.206 2.373   18.671  1.00 25.62 ?  1396 HOH   A O    1 
HETATM 6803 O  O    . HOH   H 6 .   ? 23.463 11.380  4.044   1.00 10.94 ?  1397 HOH   A O    1 
HETATM 6804 O  O    . HOH   H 6 .   ? 32.733 -9.249  5.949   1.00 19.58 ?  1398 HOH   A O    1 
HETATM 6805 O  O    . HOH   H 6 .   ? 30.001 -10.058 13.018  1.00 20.71 ?  1399 HOH   A O    1 
HETATM 6806 O  O    . HOH   H 6 .   ? 15.242 -21.558 14.211  1.00 17.00 ?  1400 HOH   A O    1 
HETATM 6807 O  O    . HOH   H 6 .   ? 28.571 -10.639 -14.032 1.00 39.92 ?  1401 HOH   A O    1 
HETATM 6808 O  O    . HOH   H 6 .   ? 20.549 -19.984 2.743   1.00 17.00 ?  1402 HOH   A O    1 
HETATM 6809 O  O    . HOH   H 6 .   ? 27.454 -6.240  -14.028 1.00 35.38 ?  1403 HOH   A O    1 
HETATM 6810 O  O    A HOH   H 6 .   ? 18.927 -0.657  -1.642  0.50 10.16 ?  1404 HOH   A O    1 
HETATM 6811 O  O    . HOH   H 6 .   ? 14.101 -23.060 7.420   1.00 17.33 ?  1405 HOH   A O    1 
HETATM 6812 O  O    . HOH   H 6 .   ? 23.928 -15.721 -9.154  1.00 34.79 ?  1406 HOH   A O    1 
HETATM 6813 O  O    . HOH   H 6 .   ? 30.644 1.898   16.655  1.00 19.86 ?  1407 HOH   A O    1 
HETATM 6814 O  O    . HOH   H 6 .   ? 6.655  -3.388  12.799  1.00 28.97 ?  1408 HOH   A O    1 
HETATM 6815 O  O    . HOH   H 6 .   ? 23.905 -20.238 -1.325  1.00 15.23 ?  1409 HOH   A O    1 
HETATM 6816 O  O    . HOH   H 6 .   ? 38.041 -1.332  -1.913  1.00 17.70 ?  1410 HOH   A O    1 
HETATM 6817 O  O    . HOH   H 6 .   ? 26.939 4.140   -0.668  1.00 11.53 ?  1411 HOH   A O    1 
HETATM 6818 O  O    . HOH   H 6 .   ? 32.509 -10.632 3.204   1.00 30.14 ?  1412 HOH   A O    1 
HETATM 6819 O  O    . HOH   H 6 .   ? 40.908 -8.291  -6.716  1.00 34.93 ?  1413 HOH   A O    1 
HETATM 6820 O  O    . HOH   H 6 .   ? 30.264 -12.867 13.547  1.00 18.56 ?  1414 HOH   A O    1 
HETATM 6821 O  O    A HOH   H 6 .   ? 20.070 4.554   -7.561  0.50 15.18 ?  1415 HOH   A O    1 
HETATM 6822 O  O    A HOH   H 6 .   ? 21.314 3.168   -0.363  0.50 8.94  ?  1416 HOH   A O    1 
HETATM 6823 O  O    A HOH   H 6 .   ? 15.763 -0.933  5.252   0.50 17.86 ?  1417 HOH   A O    1 
HETATM 6824 O  O    . HOH   H 6 .   ? 26.948 -3.141  19.376  1.00 35.60 ?  1418 HOH   A O    1 
HETATM 6825 O  O    . HOH   H 6 .   ? 32.683 -4.339  -9.868  1.00 27.58 ?  1419 HOH   A O    1 
HETATM 6826 O  O    . HOH   H 6 .   ? 35.060 -5.232  -3.077  1.00 16.61 ?  1420 HOH   A O    1 
HETATM 6827 O  O    A HOH   H 6 .   ? 24.061 3.971   -4.928  0.50 18.06 ?  1421 HOH   A O    1 
HETATM 6828 O  O    A HOH   H 6 .   ? 6.426  -5.594  11.153  0.50 16.26 ?  1422 HOH   A O    1 
HETATM 6829 O  O    . HOH   H 6 .   ? 15.865 2.171   24.674  1.00 41.65 ?  1423 HOH   A O    1 
HETATM 6830 O  O    . HOH   H 6 .   ? 36.680 -4.932  5.400   1.00 22.21 ?  1424 HOH   A O    1 
HETATM 6831 O  O    . HOH   H 6 .   ? 10.399 -13.745 -1.727  1.00 16.30 ?  1425 HOH   A O    1 
HETATM 6832 O  O    B HOH   H 6 .   ? 18.757 -1.107  -1.626  0.50 12.59 ?  1426 HOH   A O    1 
HETATM 6833 O  O    . HOH   H 6 .   ? 16.213 -14.201 20.143  1.00 42.86 ?  1427 HOH   A O    1 
HETATM 6834 O  O    . HOH   H 6 .   ? 5.267  2.711   5.066   1.00 32.10 ?  1428 HOH   A O    1 
HETATM 6835 O  O    . HOH   H 6 .   ? 41.589 1.500   5.046   1.00 36.07 ?  1429 HOH   A O    1 
HETATM 6836 O  O    . HOH   H 6 .   ? 16.177 16.722  8.640   1.00 29.55 ?  1430 HOH   A O    1 
HETATM 6837 O  O    . HOH   H 6 .   ? 22.574 8.145   18.308  1.00 46.44 ?  1431 HOH   A O    1 
HETATM 6838 O  O    A HOH   H 6 .   ? 10.992 1.564   12.729  0.50 17.63 ?  1432 HOH   A O    1 
HETATM 6839 O  O    . HOH   H 6 .   ? 21.700 -13.915 -8.180  1.00 47.08 ?  1433 HOH   A O    1 
HETATM 6840 O  O    . HOH   H 6 .   ? 15.997 6.888   2.907   1.00 17.95 ?  1434 HOH   A O    1 
HETATM 6841 O  O    . HOH   H 6 .   ? 10.374 -22.147 -1.238  1.00 51.24 ?  1435 HOH   A O    1 
HETATM 6842 O  O    . HOH   H 6 .   ? 11.741 -10.743 16.936  1.00 23.44 ?  1436 HOH   A O    1 
HETATM 6843 O  O    . HOH   H 6 .   ? 44.927 -0.571  3.094   1.00 39.85 ?  1437 HOH   A O    1 
HETATM 6844 O  O    . HOH   H 6 .   ? 18.541 4.938   -15.103 1.00 45.30 ?  1438 HOH   A O    1 
HETATM 6845 O  O    . HOH   H 6 .   ? 23.429 -7.974  17.050  1.00 19.67 ?  1439 HOH   A O    1 
HETATM 6846 O  O    . HOH   H 6 .   ? 19.346 -11.094 24.068  1.00 65.24 ?  1440 HOH   A O    1 
HETATM 6847 O  O    A HOH   H 6 .   ? 16.225 2.959   -1.459  0.50 9.70  ?  1441 HOH   A O    1 
HETATM 6848 O  O    . HOH   H 6 .   ? 18.320 -15.993 16.314  1.00 35.18 ?  1442 HOH   A O    1 
HETATM 6849 O  O    . HOH   H 6 .   ? 23.333 -20.909 1.343   1.00 16.96 ?  1443 HOH   A O    1 
HETATM 6850 O  O    A HOH   H 6 .   ? 18.830 2.045   -0.767  0.50 8.64  ?  1444 HOH   A O    1 
HETATM 6851 O  O    . HOH   H 6 .   ? -1.693 -4.906  7.616   1.00 42.07 ?  1445 HOH   A O    1 
HETATM 6852 O  O    A HOH   H 6 .   ? 23.168 7.525   -3.250  0.50 20.83 ?  1446 HOH   A O    1 
HETATM 6853 O  O    . HOH   H 6 .   ? 21.335 -9.222  21.274  1.00 44.84 ?  1447 HOH   A O    1 
HETATM 6854 O  O    . HOH   H 6 .   ? 37.702 -8.826  -3.408  1.00 22.25 ?  1448 HOH   A O    1 
HETATM 6855 O  O    . HOH   H 6 .   ? 29.715 -1.948  -12.763 1.00 48.35 ?  1449 HOH   A O    1 
HETATM 6856 O  O    . HOH   H 6 .   ? 20.524 -17.723 24.798  1.00 55.19 ?  1450 HOH   A O    1 
HETATM 6857 O  O    . HOH   H 6 .   ? 34.370 -8.110  -0.493  1.00 26.42 ?  1451 HOH   A O    1 
HETATM 6858 O  O    A HOH   H 6 .   ? 9.358  -16.316 -2.005  0.50 29.72 ?  1452 HOH   A O    1 
HETATM 6859 O  O    A HOH   H 6 .   ? 13.991 -0.327  3.442   0.30 28.88 ?  1453 HOH   A O    1 
HETATM 6860 O  O    . HOH   H 6 .   ? 21.444 -14.780 17.914  1.00 51.87 ?  1454 HOH   A O    1 
HETATM 6861 O  O    . HOH   H 6 .   ? 31.310 -12.762 0.013   1.00 18.25 ?  1455 HOH   A O    1 
HETATM 6862 O  O    . HOH   H 6 .   ? 30.566 14.757  2.786   1.00 18.29 ?  1456 HOH   A O    1 
HETATM 6863 O  O    B HOH   H 6 .   ? 23.270 7.940   -3.304  0.50 27.28 ?  1457 HOH   A O    1 
HETATM 6864 O  O    B HOH   H 6 .   ? 11.087 -0.857  2.555   0.50 18.61 ?  1458 HOH   A O    1 
HETATM 6865 O  O    B HOH   H 6 .   ? 5.327  3.886   1.029   0.50 31.61 ?  1459 HOH   A O    1 
HETATM 6866 O  O    . HOH   H 6 .   ? 29.782 -16.023 10.656  1.00 29.91 ?  1460 HOH   A O    1 
HETATM 6867 O  O    . HOH   H 6 .   ? 27.663 6.997   -6.421  1.00 31.86 ?  1461 HOH   A O    1 
HETATM 6868 O  O    B HOH   H 6 .   ? 19.048 1.490   -0.508  0.50 12.63 ?  1462 HOH   A O    1 
HETATM 6869 O  O    . HOH   H 6 .   ? 32.394 -15.909 10.848  1.00 29.98 ?  1463 HOH   A O    1 
HETATM 6870 O  O    . HOH   H 6 .   ? 24.758 5.578   20.713  1.00 50.45 ?  1464 HOH   A O    1 
HETATM 6871 O  O    . HOH   H 6 .   ? 25.440 8.324   -4.896  1.00 25.58 ?  1465 HOH   A O    1 
HETATM 6872 O  O    . HOH   H 6 .   ? 19.848 -17.283 -5.058  1.00 23.05 ?  1466 HOH   A O    1 
HETATM 6873 O  O    B HOH   H 6 .   ? 12.466 -3.028  1.731   0.50 16.72 ?  1467 HOH   A O    1 
HETATM 6874 O  O    . HOH   H 6 .   ? 24.603 14.551  7.797   1.00 31.97 ?  1468 HOH   A O    1 
HETATM 6875 O  O    . HOH   H 6 .   ? 23.221 -22.331 -3.336  1.00 33.17 ?  1469 HOH   A O    1 
HETATM 6876 O  O    . HOH   H 6 .   ? 39.598 -7.076  -3.496  1.00 42.95 ?  1470 HOH   A O    1 
HETATM 6877 O  O    . HOH   H 6 .   ? 15.719 -21.457 3.683   1.00 20.75 ?  1471 HOH   A O    1 
HETATM 6878 O  O    . HOH   H 6 .   ? 18.732 10.960  11.179  1.00 30.55 ?  1472 HOH   A O    1 
HETATM 6879 O  O    . HOH   H 6 .   ? 26.897 11.650  -1.308  1.00 30.75 ?  1473 HOH   A O    1 
HETATM 6880 O  O    . HOH   H 6 .   ? 27.391 -11.413 16.522  1.00 37.81 ?  1474 HOH   A O    1 
HETATM 6881 O  O    A HOH   H 6 .   ? 21.935 5.279   -5.850  0.50 22.81 ?  1475 HOH   A O    1 
HETATM 6882 O  O    . HOH   H 6 .   ? 11.886 -13.421 16.366  1.00 51.15 ?  1476 HOH   A O    1 
HETATM 6883 O  O    . HOH   H 6 .   ? 23.466 13.713  5.485   1.00 17.19 ?  1477 HOH   A O    1 
HETATM 6884 O  O    . HOH   H 6 .   ? 11.116 -15.018 -6.173  1.00 30.96 ?  1478 HOH   A O    1 
HETATM 6885 O  O    . HOH   H 6 .   ? 18.119 -16.215 -8.879  1.00 37.75 ?  1479 HOH   A O    1 
HETATM 6886 O  O    . HOH   H 6 .   ? 25.863 10.802  -3.683  1.00 22.36 ?  1480 HOH   A O    1 
HETATM 6887 O  O    . HOH   H 6 .   ? 12.230 1.518   17.286  1.00 37.09 ?  1481 HOH   A O    1 
HETATM 6888 O  O    . HOH   H 6 .   ? 15.693 -17.164 -7.015  1.00 29.36 ?  1482 HOH   A O    1 
HETATM 6889 O  O    . HOH   H 6 .   ? 14.033 -10.361 -10.870 1.00 30.17 ?  1483 HOH   A O    1 
HETATM 6890 O  O    B HOH   H 6 .   ? 14.892 8.232   4.915   0.50 19.60 ?  1484 HOH   A O    1 
HETATM 6891 O  O    . HOH   H 6 .   ? 28.577 -4.687  -12.315 1.00 35.04 ?  1485 HOH   A O    1 
HETATM 6892 O  O    . HOH   H 6 .   ? 35.141 7.469   12.248  1.00 41.42 ?  1486 HOH   A O    1 
HETATM 6893 O  O    . HOH   H 6 .   ? 20.495 -15.968 -7.434  1.00 27.10 ?  1487 HOH   A O    1 
HETATM 6894 O  O    . HOH   H 6 .   ? 28.806 9.043   17.515  1.00 36.48 ?  1488 HOH   A O    1 
HETATM 6895 O  O    . HOH   H 6 .   ? 17.315 -18.677 19.781  1.00 48.99 ?  1489 HOH   A O    1 
HETATM 6896 O  O    . HOH   H 6 .   ? 40.993 -3.966  -0.362  1.00 37.06 ?  1490 HOH   A O    1 
HETATM 6897 O  O    . HOH   H 6 .   ? 23.248 -12.862 19.315  1.00 41.25 ?  1491 HOH   A O    1 
HETATM 6898 O  O    . HOH   H 6 .   ? 30.810 0.780   19.081  1.00 36.99 ?  1492 HOH   A O    1 
HETATM 6899 O  O    . HOH   H 6 .   ? 23.171 11.892  -4.065  1.00 18.81 ?  1493 HOH   A O    1 
HETATM 6900 O  O    . HOH   H 6 .   ? 15.888 -6.982  -11.785 1.00 42.90 ?  1494 HOH   A O    1 
HETATM 6901 O  O    . HOH   H 6 .   ? 16.863 -20.540 16.127  1.00 26.57 ?  1495 HOH   A O    1 
HETATM 6902 O  O    . HOH   H 6 .   ? 44.456 10.414  -1.631  1.00 28.71 ?  1496 HOH   A O    1 
HETATM 6903 O  O    . HOH   H 6 .   ? 41.668 9.334   -3.957  1.00 29.89 ?  1497 HOH   A O    1 
HETATM 6904 O  O    . HOH   H 6 .   ? 30.705 5.836   -14.699 1.00 33.37 ?  1498 HOH   A O    1 
HETATM 6905 O  O    . HOH   H 6 .   ? 7.675  -3.401  -5.815  1.00 45.19 ?  1499 HOH   A O    1 
HETATM 6906 O  O    . HOH   H 6 .   ? 39.138 2.432   7.431   1.00 32.23 ?  1500 HOH   A O    1 
HETATM 6907 O  O    . HOH   H 6 .   ? 28.696 -7.947  -15.257 1.00 48.72 ?  1501 HOH   A O    1 
HETATM 6908 O  O    . HOH   H 6 .   ? 31.480 -0.611  -10.537 1.00 26.82 ?  1502 HOH   A O    1 
HETATM 6909 O  O    . HOH   H 6 .   ? 40.520 -0.257  -7.801  1.00 33.55 ?  1503 HOH   A O    1 
HETATM 6910 O  O    . HOH   H 6 .   ? 13.984 -25.278 8.892   1.00 31.76 ?  1504 HOH   A O    1 
HETATM 6911 O  O    . HOH   H 6 .   ? 20.028 -22.303 4.179   1.00 26.77 ?  1505 HOH   A O    1 
HETATM 6912 O  O    . HOH   H 6 .   ? 18.508 -23.266 1.859   1.00 40.56 ?  1506 HOH   A O    1 
HETATM 6913 O  O    . HOH   H 6 .   ? 16.199 -23.362 5.722   1.00 26.42 ?  1507 HOH   A O    1 
HETATM 6914 O  O    . HOH   H 6 .   ? 30.708 -5.861  -11.854 1.00 45.15 ?  1508 HOH   A O    1 
HETATM 6915 O  O    . HOH   H 6 .   ? 37.349 -6.640  7.578   1.00 23.97 ?  1509 HOH   A O    1 
HETATM 6916 O  O    . HOH   H 6 .   ? 23.227 -23.793 1.627   1.00 29.19 ?  1510 HOH   A O    1 
HETATM 6917 O  O    . HOH   H 6 .   ? 39.481 -0.037  6.576   1.00 30.41 ?  1511 HOH   A O    1 
HETATM 6918 O  O    . HOH   H 6 .   ? 28.974 14.480  0.857   1.00 45.43 ?  1512 HOH   A O    1 
HETATM 6919 O  O    . HOH   H 6 .   ? 37.984 13.966  6.673   1.00 38.25 ?  1513 HOH   A O    1 
HETATM 6920 O  O    . HOH   H 6 .   ? 36.471 -6.444  10.188  1.00 42.84 ?  1514 HOH   A O    1 
HETATM 6921 O  O    . HOH   H 6 .   ? 22.002 -24.002 4.493   1.00 24.61 ?  1515 HOH   A O    1 
HETATM 6922 O  O    . HOH   H 6 .   ? 17.386 -6.591  -14.182 1.00 42.08 ?  1516 HOH   A O    1 
HETATM 6923 O  O    T HOH   H 6 .   ? 11.891 -2.138  -3.675  0.20 10.69 ?  1517 HOH   A O    1 
HETATM 6924 O  O    B HOH   H 6 .   ? 5.985  6.525   1.507   0.50 29.45 ?  1518 HOH   A O    1 
HETATM 6925 O  O    B HOH   H 6 .   ? 8.353  7.173   2.317   0.50 30.34 ?  1519 HOH   A O    1 
HETATM 6926 O  O    A HOH   H 6 .   ? 14.811 8.663   4.869   0.50 36.87 ?  1520 HOH   A O    1 
HETATM 6927 O  O    . HOH   H 6 .   ? 24.101 9.093   -7.257  1.00 34.00 ?  1521 HOH   A O    1 
HETATM 6928 O  O    . HOH   H 6 .   ? 15.797 -12.231 27.379  1.00 45.79 ?  1522 HOH   A O    1 
HETATM 6929 O  O    . HOH   H 6 .   ? 16.356 -21.126 18.764  1.00 38.62 ?  1523 HOH   A O    1 
HETATM 6930 O  O    . HOH   H 6 .   ? 14.714 -22.733 19.810  1.00 32.88 ?  1524 HOH   A O    1 
HETATM 6931 O  O    . HOH   I 6 .   ? 29.811 -22.415 5.507   1.00 19.16 ?  201  HOH   B O    1 
HETATM 6932 O  O    . HOH   I 6 .   ? 27.677 -29.137 -1.859  1.00 33.77 ?  202  HOH   B O    1 
HETATM 6933 O  O    . HOH   I 6 .   ? 41.695 -35.987 -17.141 1.00 32.07 ?  203  HOH   B O    1 
HETATM 6934 O  O    . HOH   I 6 .   ? 52.954 -13.496 -20.235 1.00 30.76 ?  204  HOH   B O    1 
HETATM 6935 O  O    . HOH   I 6 .   ? 27.860 -41.786 -15.099 1.00 35.78 ?  205  HOH   B O    1 
HETATM 6936 O  O    . HOH   I 6 .   ? 48.056 -6.881  15.557  1.00 31.31 ?  206  HOH   B O    1 
HETATM 6937 O  O    . HOH   I 6 .   ? 41.310 -7.851  5.504   1.00 35.25 ?  207  HOH   B O    1 
HETATM 6938 O  O    . HOH   I 6 .   ? 44.433 -7.212  2.009   1.00 33.36 ?  208  HOH   B O    1 
HETATM 6939 O  O    . HOH   I 6 .   ? 54.496 -9.384  -8.709  1.00 17.90 ?  209  HOH   B O    1 
HETATM 6940 O  O    . HOH   I 6 .   ? 38.010 -39.397 -0.197  1.00 37.70 ?  210  HOH   B O    1 
HETATM 6941 O  O    . HOH   I 6 .   ? 47.458 -7.379  -3.932  1.00 39.48 ?  211  HOH   B O    1 
HETATM 6942 O  O    . HOH   I 6 .   ? 30.202 -40.989 -8.070  1.00 16.26 ?  212  HOH   B O    1 
HETATM 6943 O  O    . HOH   I 6 .   ? 59.093 -18.792 6.835   1.00 34.22 ?  213  HOH   B O    1 
HETATM 6944 O  O    . HOH   I 6 .   ? 29.889 -26.274 4.046   1.00 26.31 ?  214  HOH   B O    1 
HETATM 6945 O  O    . HOH   I 6 .   ? 56.640 -30.728 -7.769  1.00 31.16 ?  215  HOH   B O    1 
HETATM 6946 O  O    . HOH   I 6 .   ? 55.362 -16.530 -14.300 1.00 32.77 ?  216  HOH   B O    1 
HETATM 6947 O  O    . HOH   I 6 .   ? 30.904 -28.733 4.361   1.00 25.81 ?  217  HOH   B O    1 
HETATM 6948 O  O    . HOH   I 6 .   ? 56.322 -19.726 7.296   1.00 30.88 ?  218  HOH   B O    1 
HETATM 6949 O  O    . HOH   I 6 .   ? 57.701 -24.458 5.040   1.00 35.45 ?  219  HOH   B O    1 
HETATM 6950 O  O    . HOH   I 6 .   ? 50.180 -3.394  7.142   1.00 33.57 ?  220  HOH   B O    1 
HETATM 6951 O  O    . HOH   I 6 .   ? 58.218 -12.907 8.421   1.00 29.84 ?  221  HOH   B O    1 
HETATM 6952 O  O    . HOH   I 6 .   ? 37.108 -19.788 -18.054 1.00 36.80 ?  222  HOH   B O    1 
HETATM 6953 O  O    . HOH   I 6 .   ? 57.121 -26.825 -7.606  1.00 37.93 ?  223  HOH   B O    1 
HETATM 6954 O  O    . HOH   I 6 .   ? 34.527 -36.361 -7.175  1.00 17.49 ?  224  HOH   B O    1 
HETATM 6955 O  O    . HOH   I 6 .   ? 34.876 -24.623 13.807  1.00 34.61 ?  225  HOH   B O    1 
HETATM 6956 O  O    . HOH   I 6 .   ? 41.457 -39.144 -14.844 1.00 22.16 ?  226  HOH   B O    1 
HETATM 6957 O  O    . HOH   I 6 .   ? 50.733 -6.106  0.159   1.00 24.70 ?  227  HOH   B O    1 
HETATM 6958 O  O    . HOH   I 6 .   ? 57.365 -16.264 -12.183 1.00 17.91 ?  228  HOH   B O    1 
HETATM 6959 O  O    . HOH   I 6 .   ? 35.961 -43.283 -8.479  1.00 31.23 ?  229  HOH   B O    1 
HETATM 6960 O  O    . HOH   I 6 .   ? 45.141 -34.918 6.825   1.00 41.19 ?  230  HOH   B O    1 
HETATM 6961 O  O    . HOH   I 6 .   ? 51.647 -6.481  4.405   1.00 18.95 ?  231  HOH   B O    1 
HETATM 6962 O  O    . HOH   I 6 .   ? 49.365 -22.811 -19.741 1.00 48.74 ?  232  HOH   B O    1 
HETATM 6963 O  O    . HOH   I 6 .   ? 41.355 -9.622  13.029  1.00 21.00 ?  233  HOH   B O    1 
HETATM 6964 O  O    . HOH   I 6 .   ? 44.895 -43.542 -10.577 1.00 27.42 ?  234  HOH   B O    1 
HETATM 6965 O  O    . HOH   I 6 .   ? 29.768 -34.131 -0.409  1.00 33.72 ?  235  HOH   B O    1 
HETATM 6966 O  O    . HOH   I 6 .   ? 40.629 -16.051 14.102  1.00 22.06 ?  236  HOH   B O    1 
HETATM 6967 O  O    . HOH   I 6 .   ? 32.784 -43.768 -11.300 1.00 19.42 ?  237  HOH   B O    1 
HETATM 6968 O  O    . HOH   I 6 .   ? 38.470 -11.037 -2.266  1.00 17.78 ?  238  HOH   B O    1 
HETATM 6969 O  O    . HOH   I 6 .   ? 46.351 -1.549  13.211  1.00 26.26 ?  239  HOH   B O    1 
HETATM 6970 O  O    . HOH   I 6 .   ? 44.486 -27.726 -0.649  1.00 21.42 ?  240  HOH   B O    1 
HETATM 6971 O  O    . HOH   I 6 .   ? 35.087 -8.007  -2.964  1.00 16.85 ?  241  HOH   B O    1 
HETATM 6972 O  O    . HOH   I 6 .   ? 42.547 -25.356 2.638   1.00 14.33 ?  242  HOH   B O    1 
HETATM 6973 O  O    . HOH   I 6 .   ? 25.373 -25.903 -1.280  1.00 31.42 ?  243  HOH   B O    1 
HETATM 6974 O  O    . HOH   I 6 .   ? 50.712 -12.982 -0.444  1.00 10.94 ?  244  HOH   B O    1 
HETATM 6975 O  O    . HOH   I 6 .   ? 28.408 -19.717 -13.092 1.00 23.20 ?  245  HOH   B O    1 
HETATM 6976 O  O    . HOH   I 6 .   ? 38.938 -11.935 12.321  1.00 31.49 ?  246  HOH   B O    1 
HETATM 6977 O  O    . HOH   I 6 .   ? 39.496 -11.117 0.326   1.00 15.25 ?  247  HOH   B O    1 
HETATM 6978 O  O    . HOH   I 6 .   ? 39.276 -10.840 6.138   1.00 23.58 ?  248  HOH   B O    1 
HETATM 6979 O  O    . HOH   I 6 .   ? 41.850 -23.490 9.311   1.00 16.83 ?  249  HOH   B O    1 
HETATM 6980 O  O    . HOH   I 6 .   ? 42.628 -22.844 3.871   1.00 10.92 ?  250  HOH   B O    1 
HETATM 6981 O  O    . HOH   I 6 .   ? 43.062 -43.209 -8.201  1.00 28.44 ?  251  HOH   B O    1 
HETATM 6982 O  O    . HOH   I 6 .   ? 50.930 -39.925 -8.204  1.00 30.41 ?  252  HOH   B O    1 
HETATM 6983 O  O    . HOH   I 6 .   ? 34.220 -18.486 11.424  1.00 24.19 ?  253  HOH   B O    1 
HETATM 6984 O  O    . HOH   I 6 .   ? 33.513 -16.981 8.099   1.00 18.26 ?  254  HOH   B O    1 
HETATM 6985 O  O    . HOH   I 6 .   ? 57.592 -24.380 -3.773  1.00 20.69 ?  255  HOH   B O    1 
HETATM 6986 O  O    . HOH   I 6 .   ? 40.320 -12.750 -11.477 1.00 14.22 ?  256  HOH   B O    1 
HETATM 6987 O  O    . HOH   I 6 .   ? 58.166 -10.642 -4.031  1.00 19.06 ?  257  HOH   B O    1 
HETATM 6988 O  O    . HOH   I 6 .   ? 29.710 -25.209 -10.747 1.00 16.18 ?  258  HOH   B O    1 
HETATM 6989 O  O    . HOH   I 6 .   ? 51.528 -13.844 11.032  1.00 25.35 ?  259  HOH   B O    1 
HETATM 6990 O  O    . HOH   I 6 .   ? 43.158 -32.356 -17.049 1.00 22.98 ?  260  HOH   B O    1 
HETATM 6991 O  O    . HOH   I 6 .   ? 30.835 -15.713 2.698   1.00 12.37 ?  261  HOH   B O    1 
HETATM 6992 O  O    . HOH   I 6 .   ? 48.590 -36.481 -15.531 1.00 42.96 ?  262  HOH   B O    1 
HETATM 6993 O  O    . HOH   I 6 .   ? 27.104 -31.816 -9.911  1.00 18.71 ?  263  HOH   B O    1 
HETATM 6994 O  O    . HOH   I 6 .   ? 47.986 -22.762 5.845   1.00 16.02 ?  264  HOH   B O    1 
HETATM 6995 O  O    . HOH   I 6 .   ? 49.686 -0.485  10.222  1.00 28.78 ?  265  HOH   B O    1 
HETATM 6996 O  O    . HOH   I 6 .   ? 43.351 -15.784 -12.117 1.00 13.55 ?  266  HOH   B O    1 
HETATM 6997 O  O    . HOH   I 6 .   ? 56.119 -23.512 -14.714 1.00 28.02 ?  267  HOH   B O    1 
HETATM 6998 O  O    . HOH   I 6 .   ? 42.344 -9.941  9.349   1.00 19.53 ?  268  HOH   B O    1 
HETATM 6999 O  O    . HOH   I 6 .   ? 49.297 -28.680 -6.871  1.00 14.51 ?  269  HOH   B O    1 
HETATM 7000 O  O    . HOH   I 6 .   ? 28.468 -30.922 -14.691 1.00 29.97 ?  270  HOH   B O    1 
HETATM 7001 O  O    . HOH   I 6 .   ? 57.478 -9.221  1.470   1.00 18.49 ?  271  HOH   B O    1 
HETATM 7002 O  O    . HOH   I 6 .   ? 56.922 -8.641  8.454   1.00 17.82 ?  272  HOH   B O    1 
HETATM 7003 O  O    . HOH   I 6 .   ? 57.077 -12.151 12.351  1.00 34.48 ?  273  HOH   B O    1 
HETATM 7004 O  O    . HOH   I 6 .   ? 34.893 -33.357 -19.114 1.00 34.21 ?  274  HOH   B O    1 
HETATM 7005 O  O    . HOH   I 6 .   ? 46.575 -31.260 -4.765  1.00 19.73 ?  275  HOH   B O    1 
HETATM 7006 O  O    . HOH   I 6 .   ? 31.819 -17.929 -14.505 1.00 29.93 ?  276  HOH   B O    1 
HETATM 7007 O  O    . HOH   I 6 .   ? 28.253 -34.331 -9.374  1.00 18.39 ?  277  HOH   B O    1 
HETATM 7008 O  O    . HOH   I 6 .   ? 34.464 -12.776 2.631   1.00 22.57 ?  278  HOH   B O    1 
HETATM 7009 O  O    . HOH   I 6 .   ? 42.376 -34.677 3.773   1.00 26.84 ?  279  HOH   B O    1 
HETATM 7010 O  O    . HOH   I 6 .   ? 46.850 -29.498 9.797   1.00 29.49 ?  280  HOH   B O    1 
HETATM 7011 O  O    . HOH   I 6 .   ? 48.032 -24.511 -17.766 1.00 31.70 ?  281  HOH   B O    1 
HETATM 7012 O  O    . HOH   I 6 .   ? 27.944 -22.864 -7.951  1.00 16.37 ?  282  HOH   B O    1 
HETATM 7013 O  O    . HOH   I 6 .   ? 48.387 -25.029 3.129   1.00 12.76 ?  283  HOH   B O    1 
HETATM 7014 O  O    . HOH   I 6 .   ? 27.602 -26.740 -15.610 1.00 31.94 ?  284  HOH   B O    1 
HETATM 7015 O  O    . HOH   I 6 .   ? 52.501 -10.376 12.990  1.00 20.85 ?  285  HOH   B O    1 
HETATM 7016 O  O    . HOH   I 6 .   ? 51.184 -37.563 -9.578  1.00 24.92 ?  286  HOH   B O    1 
HETATM 7017 O  O    . HOH   I 6 .   ? 48.681 -20.008 5.950   1.00 12.90 ?  287  HOH   B O    1 
HETATM 7018 O  O    . HOH   I 6 .   ? 59.765 -15.263 8.187   1.00 28.43 ?  288  HOH   B O    1 
HETATM 7019 O  O    . HOH   I 6 .   ? 41.085 -5.534  11.564  1.00 42.11 ?  289  HOH   B O    1 
HETATM 7020 O  O    . HOH   I 6 .   ? 51.668 -5.946  -7.921  1.00 44.87 ?  290  HOH   B O    1 
HETATM 7021 O  O    . HOH   I 6 .   ? 47.052 -33.961 -4.595  1.00 16.92 ?  291  HOH   B O    1 
HETATM 7022 O  O    . HOH   I 6 .   ? 36.818 -12.763 -1.482  1.00 25.31 ?  292  HOH   B O    1 
HETATM 7023 O  O    . HOH   I 6 .   ? 42.722 -12.208 -18.420 1.00 28.05 ?  293  HOH   B O    1 
HETATM 7024 O  O    . HOH   I 6 .   ? 33.484 -15.284 -13.916 1.00 20.68 ?  294  HOH   B O    1 
HETATM 7025 O  O    . HOH   I 6 .   ? 37.453 -18.102 13.104  1.00 29.68 ?  295  HOH   B O    1 
HETATM 7026 O  O    . HOH   I 6 .   ? 52.569 -35.613 -8.654  1.00 28.64 ?  296  HOH   B O    1 
HETATM 7027 O  O    . HOH   I 6 .   ? 49.884 -24.672 5.798   1.00 30.54 ?  297  HOH   B O    1 
HETATM 7028 O  O    . HOH   I 6 .   ? 30.512 -42.253 -10.559 1.00 29.92 ?  298  HOH   B O    1 
HETATM 7029 O  O    . HOH   I 6 .   ? 42.861 -20.261 -20.671 1.00 35.33 ?  299  HOH   B O    1 
HETATM 7030 O  O    . HOH   I 6 .   ? 44.612 -27.428 2.028   1.00 14.55 ?  300  HOH   B O    1 
HETATM 7031 O  O    . HOH   I 6 .   ? 25.936 -21.456 -3.479  1.00 15.29 ?  301  HOH   B O    1 
HETATM 7032 O  O    . HOH   I 6 .   ? 45.318 -33.339 -15.940 1.00 23.55 ?  302  HOH   B O    1 
HETATM 7033 O  O    . HOH   I 6 .   ? 40.250 -10.849 -9.496  1.00 16.33 ?  303  HOH   B O    1 
HETATM 7034 O  O    . HOH   I 6 .   ? 45.859 -40.363 -3.527  1.00 28.38 ?  304  HOH   B O    1 
HETATM 7035 O  O    . HOH   I 6 .   ? 53.011 -16.003 -12.721 1.00 25.10 ?  305  HOH   B O    1 
HETATM 7036 O  O    . HOH   I 6 .   ? 43.989 -29.345 -4.640  1.00 23.13 ?  306  HOH   B O    1 
HETATM 7037 O  O    . HOH   I 6 .   ? 35.019 -33.536 4.543   1.00 27.84 ?  307  HOH   B O    1 
HETATM 7038 O  O    . HOH   I 6 .   ? 42.268 -9.907  -14.856 1.00 37.68 ?  308  HOH   B O    1 
HETATM 7039 O  O    . HOH   I 6 .   ? 53.439 -30.196 4.545   1.00 18.12 ?  309  HOH   B O    1 
HETATM 7040 O  O    . HOH   I 6 .   ? 52.494 -29.198 -13.021 1.00 24.76 ?  310  HOH   B O    1 
HETATM 7041 O  O    . HOH   I 6 .   ? 43.214 -21.407 10.682  1.00 15.45 ?  311  HOH   B O    1 
HETATM 7042 O  O    . HOH   I 6 .   ? 37.092 -30.548 -20.955 1.00 29.34 ?  312  HOH   B O    1 
HETATM 7043 O  O    . HOH   I 6 .   ? 37.843 -10.240 -10.691 1.00 16.19 ?  313  HOH   B O    1 
HETATM 7044 O  O    . HOH   I 6 .   ? 62.696 -13.580 4.772   1.00 25.01 ?  314  HOH   B O    1 
HETATM 7045 O  O    . HOH   I 6 .   ? 37.283 -35.623 7.268   1.00 32.65 ?  315  HOH   B O    1 
HETATM 7046 O  O    . HOH   I 6 .   ? 41.740 -8.055  1.373   1.00 21.50 ?  316  HOH   B O    1 
HETATM 7047 O  O    . HOH   I 6 .   ? 32.778 -34.565 -5.877  1.00 16.11 ?  317  HOH   B O    1 
HETATM 7048 O  O    . HOH   I 6 .   ? 62.843 -20.096 -0.766  1.00 37.17 ?  318  HOH   B O    1 
HETATM 7049 O  O    . HOH   I 6 .   ? 57.650 -22.041 3.184   1.00 26.92 ?  319  HOH   B O    1 
HETATM 7050 O  O    . HOH   I 6 .   ? 53.653 -12.590 -22.134 1.00 30.12 ?  320  HOH   B O    1 
HETATM 7051 O  O    . HOH   I 6 .   ? 51.361 -32.982 -10.791 1.00 39.99 ?  321  HOH   B O    1 
HETATM 7052 O  O    . HOH   I 6 .   ? 26.334 -21.014 -6.222  1.00 15.43 ?  322  HOH   B O    1 
HETATM 7053 O  O    . HOH   I 6 .   ? 38.307 -12.680 7.958   1.00 17.47 ?  323  HOH   B O    1 
HETATM 7054 O  O    . HOH   I 6 .   ? 44.611 -24.587 9.576   1.00 19.47 ?  324  HOH   B O    1 
HETATM 7055 O  O    . HOH   I 6 .   ? 43.481 -15.363 18.144  1.00 25.38 ?  325  HOH   B O    1 
HETATM 7056 O  O    . HOH   I 6 .   ? 36.709 -12.401 4.271   1.00 17.34 ?  326  HOH   B O    1 
HETATM 7057 O  O    . HOH   I 6 .   ? 59.927 -17.177 -10.470 1.00 33.33 ?  327  HOH   B O    1 
HETATM 7058 O  O    . HOH   I 6 .   ? 47.162 -24.469 8.210   1.00 25.87 ?  328  HOH   B O    1 
HETATM 7059 O  O    . HOH   I 6 .   ? 44.100 -1.723  7.644   1.00 44.26 ?  329  HOH   B O    1 
HETATM 7060 O  O    . HOH   I 6 .   ? 27.890 -14.769 -9.403  1.00 32.82 ?  330  HOH   B O    1 
HETATM 7061 O  O    . HOH   I 6 .   ? 43.103 -34.602 0.116   1.00 19.40 ?  331  HOH   B O    1 
HETATM 7062 O  O    . HOH   I 6 .   ? 48.113 -32.625 -16.654 1.00 41.91 ?  332  HOH   B O    1 
HETATM 7063 O  O    . HOH   I 6 .   ? 48.588 -11.983 -14.081 1.00 26.68 ?  333  HOH   B O    1 
HETATM 7064 O  O    . HOH   I 6 .   ? 41.257 -24.519 15.821  1.00 41.90 ?  334  HOH   B O    1 
HETATM 7065 O  O    . HOH   I 6 .   ? 45.708 -36.244 -16.091 1.00 34.43 ?  335  HOH   B O    1 
HETATM 7066 O  O    . HOH   I 6 .   ? 33.635 -31.162 11.098  1.00 34.26 ?  336  HOH   B O    1 
HETATM 7067 O  O    . HOH   I 6 .   ? 38.379 -9.338  -13.235 1.00 25.58 ?  337  HOH   B O    1 
HETATM 7068 O  O    . HOH   I 6 .   ? 42.832 -43.473 -14.341 1.00 42.14 ?  338  HOH   B O    1 
HETATM 7069 O  O    . HOH   I 6 .   ? 47.452 -27.417 2.055   1.00 14.18 ?  339  HOH   B O    1 
HETATM 7070 O  O    . HOH   I 6 .   ? 39.514 -23.509 -20.332 1.00 36.09 ?  340  HOH   B O    1 
HETATM 7071 O  O    . HOH   I 6 .   ? 46.812 -19.881 12.265  1.00 28.98 ?  341  HOH   B O    1 
HETATM 7072 O  O    . HOH   I 6 .   ? 37.000 -15.058 -16.479 1.00 36.70 ?  342  HOH   B O    1 
HETATM 7073 O  O    . HOH   I 6 .   ? 28.864 -42.897 -12.329 1.00 32.51 ?  343  HOH   B O    1 
HETATM 7074 O  O    . HOH   I 6 .   ? 38.447 -12.235 -16.227 1.00 40.70 ?  344  HOH   B O    1 
HETATM 7075 O  O    . HOH   I 6 .   ? 33.004 -14.681 1.073   1.00 17.64 ?  345  HOH   B O    1 
HETATM 7076 O  O    . HOH   I 6 .   ? 39.785 -44.189 -11.185 1.00 39.35 ?  346  HOH   B O    1 
HETATM 7077 O  O    . HOH   I 6 .   ? 38.570 -22.389 15.034  1.00 38.81 ?  347  HOH   B O    1 
HETATM 7078 O  O    . HOH   I 6 .   ? 37.069 -45.318 -9.648  1.00 36.61 ?  348  HOH   B O    1 
HETATM 7079 O  O    . HOH   I 6 .   ? 62.501 -20.076 -4.792  1.00 45.73 ?  349  HOH   B O    1 
HETATM 7080 O  O    . HOH   I 6 .   ? 40.423 -43.464 -9.070  1.00 26.00 ?  350  HOH   B O    1 
HETATM 7081 O  O    . HOH   I 6 .   ? 55.603 -8.236  10.785  1.00 24.11 ?  351  HOH   B O    1 
HETATM 7082 O  O    . HOH   I 6 .   ? 33.701 -9.461  -8.820  1.00 29.86 ?  352  HOH   B O    1 
HETATM 7083 O  O    . HOH   I 6 .   ? 27.766 -26.580 -0.575  1.00 28.69 ?  353  HOH   B O    1 
HETATM 7084 O  O    . HOH   I 6 .   ? 44.145 -37.364 -17.748 1.00 32.85 ?  354  HOH   B O    1 
HETATM 7085 O  O    . HOH   I 6 .   ? 34.546 -10.325 7.598   1.00 23.17 ?  355  HOH   B O    1 
HETATM 7086 O  O    . HOH   I 6 .   ? 56.587 -7.288  3.122   1.00 25.75 ?  356  HOH   B O    1 
HETATM 7087 O  O    . HOH   I 6 .   ? 23.220 -23.623 6.772   1.00 35.18 ?  357  HOH   B O    1 
HETATM 7088 O  O    . HOH   I 6 .   ? 36.089 -8.506  -9.692  1.00 33.87 ?  358  HOH   B O    1 
HETATM 7089 O  O    . HOH   I 6 .   ? 34.038 -7.769  11.438  1.00 40.01 ?  359  HOH   B O    1 
HETATM 7090 O  O    . HOH   I 6 .   ? 61.467 -19.900 1.742   1.00 35.61 ?  360  HOH   B O    1 
HETATM 7091 O  O    . HOH   I 6 .   ? 56.879 -21.532 -16.315 1.00 37.45 ?  361  HOH   B O    1 
HETATM 7092 O  O    . HOH   I 6 .   ? 43.117 -12.669 -21.187 1.00 37.71 ?  362  HOH   B O    1 
HETATM 7093 O  O    . HOH   I 6 .   ? 40.247 -8.806  9.867   1.00 35.78 ?  363  HOH   B O    1 
HETATM 7094 O  O    . HOH   I 6 .   ? 27.166 -25.941 -11.351 1.00 32.82 ?  364  HOH   B O    1 
HETATM 7095 O  O    . HOH   I 6 .   ? 32.520 -23.573 14.067  1.00 37.02 ?  365  HOH   B O    1 
HETATM 7096 O  O    . HOH   I 6 .   ? 58.926 -10.525 9.198   1.00 39.37 ?  366  HOH   B O    1 
HETATM 7097 O  O    . HOH   I 6 .   ? 54.229 -5.784  2.983   1.00 34.89 ?  367  HOH   B O    1 
HETATM 7098 O  O    . HOH   I 6 .   ? 40.132 -11.359 -13.920 1.00 28.68 ?  368  HOH   B O    1 
HETATM 7099 O  O    . HOH   I 6 .   ? 48.372 -26.483 8.851   1.00 39.95 ?  369  HOH   B O    1 
HETATM 7100 O  O    . HOH   I 6 .   ? 36.134 -8.617  8.957   1.00 32.13 ?  370  HOH   B O    1 
HETATM 7101 O  O    . HOH   I 6 .   ? 39.823 -7.039  7.838   1.00 35.82 ?  371  HOH   B O    1 
HETATM 7102 O  O    . HOH   I 6 .   ? 56.014 -7.833  -0.561  1.00 31.91 ?  372  HOH   B O    1 
HETATM 7103 O  O    . HOH   I 6 .   ? 41.784 -10.018 -17.440 1.00 52.54 ?  373  HOH   B O    1 
HETATM 7104 O  O    . HOH   I 6 .   ? 51.997 -12.931 13.360  1.00 27.38 ?  374  HOH   B O    1 
HETATM 7105 O  O    . HOH   I 6 .   ? 41.840 -6.800  -4.901  1.00 46.32 ?  375  HOH   B O    1 
HETATM 7106 O  O    . HOH   I 6 .   ? 62.984 -12.341 6.918   1.00 35.53 ?  376  HOH   B O    1 
HETATM 7107 O  O    . HOH   I 6 .   ? 38.012 -10.533 10.009  1.00 27.17 ?  377  HOH   B O    1 
HETATM 7108 O  O    . HOH   I 6 .   ? 36.506 -22.799 13.279  1.00 26.65 ?  378  HOH   B O    1 
HETATM 7109 O  O    . HOH   I 6 .   ? 40.132 -7.685  3.161   1.00 35.37 ?  379  HOH   B O    1 
HETATM 7110 O  O    . HOH   I 6 .   ? 42.654 -17.045 -23.157 1.00 41.83 ?  380  HOH   B O    1 
HETATM 7111 O  O    . HOH   I 6 .   ? 44.003 -5.609  -3.426  1.00 43.15 ?  381  HOH   B O    1 
HETATM 7112 O  O    . HOH   I 6 .   ? 39.603 -13.975 15.653  1.00 45.21 ?  382  HOH   B O    1 
HETATM 7113 O  O    . HOH   I 6 .   ? 52.835 -29.856 7.207   1.00 22.29 ?  383  HOH   B O    1 
HETATM 7114 O  O    . HOH   I 6 .   ? 46.770 -5.343  2.867   1.00 38.31 ?  384  HOH   B O    1 
HETATM 7115 O  O    . HOH   I 6 .   ? 60.469 -22.299 2.896   1.00 44.51 ?  385  HOH   B O    1 
HETATM 7116 O  O    . HOH   I 6 .   ? 35.392 -33.729 7.343   1.00 39.84 ?  386  HOH   B O    1 
HETATM 7117 O  O    . HOH   I 6 .   ? 25.833 -18.918 -11.892 1.00 37.47 ?  387  HOH   B O    1 
HETATM 7118 O  O    . HOH   I 6 .   ? 35.259 -20.312 13.300  1.00 30.48 ?  388  HOH   B O    1 
HETATM 7119 O  O    . HOH   I 6 .   ? 23.933 -20.901 -7.662  1.00 26.92 ?  389  HOH   B O    1 
HETATM 7120 O  O    . HOH   I 6 .   ? 40.917 -9.710  15.813  1.00 44.27 ?  390  HOH   B O    1 
HETATM 7121 O  O    . HOH   I 6 .   ? 44.151 -31.687 -3.791  1.00 35.13 ?  391  HOH   B O    1 
HETATM 7122 O  O    . HOH   I 6 .   ? 40.745 -6.577  -0.799  1.00 23.33 ?  392  HOH   B O    1 
HETATM 7123 O  O    . HOH   I 6 .   ? 27.928 -27.063 2.239   1.00 30.18 ?  393  HOH   B O    1 
HETATM 7124 O  O    . HOH   I 6 .   ? 26.626 -27.922 -13.437 1.00 33.89 ?  394  HOH   B O    1 
HETATM 7125 O  O    . HOH   I 6 .   ? 24.605 -20.637 -10.474 1.00 36.08 ?  395  HOH   B O    1 
HETATM 7126 O  O    . HOH   I 6 .   ? 50.627 -30.818 8.677   1.00 28.47 ?  396  HOH   B O    1 
HETATM 7127 O  O    . HOH   I 6 .   ? 34.375 -33.468 9.660   1.00 35.02 ?  397  HOH   B O    1 
HETATM 7128 O  O    . HOH   I 6 .   ? 26.842 -30.643 -12.605 1.00 27.91 ?  398  HOH   B O    1 
HETATM 7129 O  O    . HOH   I 6 .   ? 57.648 -6.550  -2.364  1.00 32.00 ?  399  HOH   B O    1 
HETATM 7130 O  O    . HOH   I 6 .   ? 45.726 -20.169 15.214  1.00 45.84 ?  400  HOH   B O    1 
HETATM 7131 O  O    . HOH   I 6 .   ? 40.874 -11.755 -22.275 1.00 39.07 ?  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   ? 0.5645 0.5710 0.6494 0.0104  -0.0431 0.0603  3    VAL   A N   
2    N  N   B VAL   A 3   ? 0.5628 0.5707 0.6460 0.0122  -0.0433 0.0622  3    VAL   A N   
3    C  CA  A VAL   A 3   ? 0.5640 0.5705 0.6397 0.0089  -0.0398 0.0603  3    VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.5622 0.5702 0.6362 0.0107  -0.0402 0.0621  3    VAL   A CA  
5    C  C   A VAL   A 3   ? 0.5537 0.5637 0.6105 0.0022  -0.0408 0.0624  3    VAL   A C   
6    C  C   B VAL   A 3   ? 0.5519 0.5633 0.6079 0.0042  -0.0409 0.0638  3    VAL   A C   
7    O  O   A VAL   A 3   ? 0.5555 0.5653 0.6218 0.0042  -0.0451 0.0636  3    VAL   A O   
8    O  O   B VAL   A 3   ? 0.5533 0.5647 0.6177 0.0065  -0.0447 0.0652  3    VAL   A O   
9    C  CB  A VAL   A 3   ? 0.5721 0.5760 0.6531 0.0125  -0.0370 0.0583  3    VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.5704 0.5757 0.6486 0.0144  -0.0377 0.0601  3    VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.5751 0.5778 0.6544 0.0148  -0.0369 0.0578  3    VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.5732 0.5771 0.6497 0.0164  -0.0376 0.0596  3    VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.5746 0.5781 0.6545 0.0132  -0.0364 0.0578  3    VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.5730 0.5780 0.6499 0.0154  -0.0370 0.0597  3    VAL   A CG2 
31   N  N   A ASN   A 4   ? 0.5393 0.5534 0.5615 -0.0071 -0.0373 0.0622  4    ASN   A N   
32   N  N   B ASN   A 4   ? 0.5380 0.5532 0.5614 -0.0051 -0.0373 0.0629  4    ASN   A N   
33   C  CA  A ASN   A 4   ? 0.5220 0.5409 0.5071 -0.0169 -0.0334 0.0602  4    ASN   A CA  
34   C  CA  B ASN   A 4   ? 0.5211 0.5408 0.5095 -0.0149 -0.0332 0.0601  4    ASN   A CA  
35   C  C   A ASN   A 4   ? 0.4967 0.5256 0.4785 -0.0294 -0.0236 0.0428  4    ASN   A C   
36   C  C   B ASN   A 4   ? 0.4964 0.5257 0.4816 -0.0274 -0.0238 0.0423  4    ASN   A C   
37   O  O   A ASN   A 4   ? 0.4966 0.5264 0.4766 -0.0296 -0.0240 0.0431  4    ASN   A O   
38   O  O   B ASN   A 4   ? 0.4963 0.5266 0.4811 -0.0275 -0.0243 0.0426  4    ASN   A O   
39   C  CB  A ASN   A 4   ? 0.5266 0.5417 0.4754 -0.0144 -0.0378 0.0760  4    ASN   A CB  
40   C  CB  B ASN   A 4   ? 0.5255 0.5414 0.4788 -0.0123 -0.0372 0.0755  4    ASN   A CB  
41   C  CG  A ASN   A 4   ? 0.5286 0.5406 0.4437 -0.0125 -0.0416 0.0916  4    ASN   A CG  
42   C  CG  B ASN   A 4   ? 0.5274 0.5403 0.4477 -0.0103 -0.0404 0.0909  4    ASN   A CG  
43   O  OD1 A ASN   A 4   ? 0.5302 0.5401 0.4324 -0.0123 -0.0439 0.0975  4    ASN   A OD1 
44   O  OD1 B ASN   A 4   ? 0.5290 0.5398 0.4372 -0.0102 -0.0418 0.0967  4    ASN   A OD1 
45   N  ND2 A ASN   A 4   ? 0.5279 0.5397 0.4366 -0.0109 -0.0433 0.0986  4    ASN   A ND2 
46   N  ND2 B ASN   A 4   ? 0.5268 0.5394 0.4401 -0.0087 -0.0422 0.0977  4    ASN   A ND2 
59   N  N   A SER   A 5   ? 0.4695 0.5074 0.4416 -0.0428 -0.0123 0.0262  5    SER   A N   
60   N  N   B SER   A 5   ? 0.4697 0.5076 0.4427 -0.0408 -0.0129 0.0254  5    SER   A N   
61   C  CA  A SER   A 5   ? 0.4404 0.4885 0.4059 -0.0565 0.0025  0.0093  5    SER   A CA  
62   C  CA  B SER   A 5   ? 0.4410 0.4889 0.4036 -0.0544 0.0016  0.0079  5    SER   A CA  
63   C  C   A SER   A 5   ? 0.4066 0.4619 0.3656 -0.0671 0.0155  0.0020  5    SER   A C   
64   C  C   B SER   A 5   ? 0.4071 0.4622 0.3654 -0.0657 0.0156  0.0016  5    SER   A C   
65   O  O   A SER   A 5   ? 0.4102 0.4656 0.3608 -0.0639 0.0161  -0.0030 5    SER   A O   
66   O  O   B SER   A 5   ? 0.4110 0.4660 0.3621 -0.0622 0.0170  -0.0030 5    SER   A O   
67   C  CB  A SER   A 5   ? 0.4447 0.4954 0.4204 -0.0592 0.0049  0.0023  5    SER   A CB  
68   C  CB  B SER   A 5   ? 0.4457 0.4959 0.4140 -0.0567 0.0024  -0.0007 5    SER   A CB  
69   O  OG  A SER   A 5   ? 0.4471 0.4997 0.4235 -0.0606 0.0060  -0.0002 5    SER   A OG  
70   O  OG  B SER   A 5   ? 0.4481 0.5000 0.4122 -0.0578 0.0030  -0.0046 5    SER   A OG  
81   N  N   . PHE   A 6   ? 0.3670 0.4300 0.3157 -0.0796 0.0285  0.0066  6    PHE   A N   
82   C  CA  . PHE   A 6   ? 0.2941 0.3653 0.2330 -0.0985 0.0454  0.0249  6    PHE   A CA  
83   C  C   . PHE   A 6   ? 0.2833 0.3579 0.2375 -0.1074 0.0642  0.0185  6    PHE   A C   
84   O  O   . PHE   A 6   ? 0.2917 0.3599 0.2858 -0.1122 0.0702  0.0282  6    PHE   A O   
85   C  CB  . PHE   A 6   ? 0.2509 0.3135 0.1872 -0.0906 0.0268  0.0371  6    PHE   A CB  
86   C  CG  . PHE   A 6   ? 0.2214 0.2735 0.1593 -0.0757 0.0078  0.0418  6    PHE   A CG  
87   C  CD1 . PHE   A 6   ? 0.2115 0.2596 0.1537 -0.0642 -0.0033 0.0423  6    PHE   A CD1 
88   C  CD2 . PHE   A 6   ? 0.2262 0.2652 0.1931 -0.0522 0.0126  0.0390  6    PHE   A CD2 
89   C  CE1 . PHE   A 6   ? 0.2097 0.2522 0.1736 -0.0608 0.0020  0.0420  6    PHE   A CE1 
90   C  CE2 . PHE   A 6   ? 0.2233 0.2590 0.2092 -0.0438 0.0120  0.0349  6    PHE   A CE2 
91   C  CZ  . PHE   A 6   ? 0.2166 0.2536 0.1931 -0.0524 0.0048  0.0374  6    PHE   A CZ  
102  N  N   . SER   A 7   ? 0.2648 0.3458 0.2187 -0.1079 0.0731  0.0083  7    SER   A N   
103  C  CA  . SER   A 7   ? 0.2595 0.3380 0.2339 -0.0931 0.0727  -0.0136 7    SER   A CA  
104  C  C   . SER   A 7   ? 0.2393 0.2986 0.2172 -0.0882 0.0727  -0.0047 7    SER   A C   
105  O  O   . SER   A 7   ? 0.2506 0.2874 0.2209 -0.0963 0.0708  -0.0058 7    SER   A O   
106  C  CB  . SER   A 7   ? 0.2802 0.3644 0.2739 -0.0766 0.0746  -0.0194 7    SER   A CB  
107  O  OG  . SER   A 7   ? 0.3009 0.3790 0.3192 -0.0647 0.0654  -0.0249 7    SER   A OG  
113  N  N   . GLY   A 8   ? 0.2160 0.2681 0.2142 -0.0781 0.0704  -0.0091 8    GLY   A N   
114  C  CA  . GLY   A 8   ? 0.2001 0.2413 0.2327 -0.0585 0.0626  -0.0050 8    GLY   A CA  
115  C  C   . GLY   A 8   ? 0.1755 0.2207 0.2130 -0.0438 0.0489  0.0082  8    GLY   A C   
116  O  O   . GLY   A 8   ? 0.1755 0.2280 0.2400 -0.0243 0.0454  -0.0093 8    GLY   A O   
120  N  N   . TYR   A 9   ? 0.1601 0.2118 0.1987 -0.0287 0.0398  0.0222  9    TYR   A N   
121  C  CA  . TYR   A 9   ? 0.1466 0.1980 0.1779 -0.0286 0.0301  0.0347  9    TYR   A CA  
122  C  C   . TYR   A 9   ? 0.1501 0.1899 0.1819 -0.0212 0.0300  0.0487  9    TYR   A C   
123  O  O   . TYR   A 9   ? 0.1811 0.2056 0.2014 -0.0289 0.0220  0.0473  9    TYR   A O   
124  C  CB  . TYR   A 9   ? 0.1390 0.2061 0.1817 -0.0202 0.0208  0.0213  9    TYR   A CB  
125  C  CG  . TYR   A 9   ? 0.1382 0.2059 0.1680 -0.0145 0.0233  0.0159  9    TYR   A CG  
126  C  CD1 . TYR   A 9   ? 0.1429 0.2147 0.1820 -0.0238 0.0347  0.0070  9    TYR   A CD1 
127  C  CD2 . TYR   A 9   ? 0.1363 0.1980 0.1715 -0.0053 0.0176  0.0245  9    TYR   A CD2 
128  C  CE1 . TYR   A 9   ? 0.1517 0.2182 0.1884 -0.0232 0.0317  -0.0054 9    TYR   A CE1 
129  C  CE2 . TYR   A 9   ? 0.1384 0.2030 0.1672 -0.0090 0.0264  0.0129  9    TYR   A CE2 
130  C  CZ  . TYR   A 9   ? 0.1422 0.2150 0.1942 -0.0268 0.0415  0.0016  9    TYR   A CZ  
131  O  OH  . TYR   A 9   ? 0.1513 0.2276 0.2214 -0.0445 0.0417  -0.0066 9    TYR   A OH  
141  N  N   . LEU   A 10  ? 0.1435 0.1771 0.1729 -0.0206 0.0216  0.0434  10   LEU   A N   
142  C  CA  . LEU   A 10  ? 0.1348 0.1738 0.1824 -0.0331 0.0171  0.0532  10   LEU   A CA  
143  C  C   . LEU   A 10  ? 0.1282 0.1618 0.1752 -0.0350 0.0094  0.0472  10   LEU   A C   
144  O  O   . LEU   A 10  ? 0.1371 0.1598 0.1696 -0.0257 0.0174  0.0475  10   LEU   A O   
145  C  CB  . LEU   A 10  ? 0.1386 0.1889 0.2143 -0.0348 0.0025  0.0643  10   LEU   A CB  
146  C  CG  . LEU   A 10  ? 0.1591 0.2055 0.2530 -0.0342 -0.0116 0.0645  10   LEU   A CG  
147  C  CD1 . LEU   A 10  ? 0.1752 0.2118 0.2878 -0.0466 -0.0037 0.0620  10   LEU   A CD1 
148  C  CD2 . LEU   A 10  ? 0.1784 0.2324 0.2731 -0.0275 -0.0026 0.0444  10   LEU   A CD2 
160  N  N   . LYS   A 11  ? 0.1421 0.1608 0.1817 -0.0336 0.0118  0.0503  11   LYS   A N   
161  C  CA  . LYS   A 11  ? 0.1386 0.1590 0.1732 -0.0362 0.0063  0.0472  11   LYS   A CA  
162  C  C   . LYS   A 11  ? 0.1303 0.1715 0.1758 -0.0385 0.0056  0.0417  11   LYS   A C   
163  O  O   . LYS   A 11  ? 0.1381 0.2088 0.1914 -0.0624 0.0068  0.0256  11   LYS   A O   
164  C  CB  . LYS   A 11  ? 0.1514 0.1529 0.1705 -0.0363 0.0010  0.0322  11   LYS   A CB  
165  C  CG  . LYS   A 11  ? 0.1677 0.1434 0.1607 -0.0401 -0.0002 0.0386  11   LYS   A CG  
166  C  CD  . LYS   A 11  ? 0.1869 0.1497 0.1547 -0.0346 -0.0005 0.0350  11   LYS   A CD  
167  C  CE  . LYS   A 11  ? 0.1991 0.1444 0.1549 -0.0251 0.0052  0.0386  11   LYS   A CE  
168  N  NZ  . LYS   A 11  ? 0.1935 0.1465 0.1587 -0.0121 -0.0059 0.0362  11   LYS   A NZ  
182  N  N   . LEU   A 12  ? 0.1248 0.1593 0.1686 -0.0355 0.0023  0.0346  12   LEU   A N   
183  C  CA  . LEU   A 12  ? 0.1285 0.1780 0.1638 -0.0328 0.0001  0.0380  12   LEU   A CA  
184  C  C   . LEU   A 12  ? 0.1343 0.1722 0.1522 -0.0348 0.0100  0.0461  12   LEU   A C   
185  O  O   . LEU   A 12  ? 0.1421 0.1761 0.1646 -0.0386 0.0065  0.0293  12   LEU   A O   
186  C  CB  . LEU   A 12  ? 0.1350 0.1768 0.1681 -0.0284 -0.0040 0.0489  12   LEU   A CB  
187  C  CG  . LEU   A 12  ? 0.1475 0.1876 0.1891 -0.0248 0.0053  0.0455  12   LEU   A CG  
188  C  CD1 . LEU   A 12  ? 0.1605 0.1955 0.1948 -0.0189 0.0114  0.0459  12   LEU   A CD1 
189  C  CD2 . LEU   A 12  ? 0.1478 0.1957 0.2252 -0.0225 -0.0038 0.0416  12   LEU   A CD2 
201  N  N   . THR   A 13  ? 0.1329 0.1655 0.1562 -0.0314 0.0028  0.0326  13   THR   A N   
202  C  CA  . THR   A 13  ? 0.1375 0.1591 0.1723 -0.0377 0.0052  0.0249  13   THR   A CA  
203  C  C   . THR   A 13  ? 0.1425 0.1526 0.1746 -0.0399 0.0031  0.0345  13   THR   A C   
204  O  O   . THR   A 13  ? 0.1459 0.1526 0.1726 -0.0284 -0.0040 0.0380  13   THR   A O   
205  C  CB  . THR   A 13  ? 0.1451 0.1694 0.1802 -0.0352 0.0124  0.0304  13   THR   A CB  
206  O  OG1 . THR   A 13  ? 0.1430 0.1676 0.1873 -0.0355 0.0092  0.0388  13   THR   A OG1 
207  C  CG2 . THR   A 13  ? 0.1532 0.1866 0.1902 -0.0331 0.0189  0.0183  13   THR   A CG2 
215  N  N   . ASP   A 14  ? 0.1505 0.1485 0.1843 -0.0414 0.0025  0.0430  14   ASP   A N   
216  C  CA  . ASP   A 14  ? 0.1537 0.1616 0.2018 -0.0316 -0.0021 0.0552  14   ASP   A CA  
217  C  C   . ASP   A 14  ? 0.1488 0.1627 0.1964 -0.0311 -0.0081 0.0551  14   ASP   A C   
218  O  O   . ASP   A 14  ? 0.1668 0.1721 0.2029 -0.0453 -0.0201 0.0618  14   ASP   A O   
219  C  CB  . ASP   A 14  ? 0.1738 0.1770 0.2647 -0.0325 0.0003  0.0698  14   ASP   A CB  
220  C  CG  . ASP   A 14  ? 0.1848 0.2284 0.3385 -0.0295 -0.0014 0.0707  14   ASP   A CG  
221  O  OD1 . ASP   A 14  ? 0.1995 0.2477 0.3642 -0.0153 -0.0136 0.0758  14   ASP   A OD1 
222  O  OD2 . ASP   A 14  ? 0.2023 0.2707 0.3879 -0.0234 -0.0048 0.0516  14   ASP   A OD2 
227  N  N   . ASN   A 15  ? 0.1338 0.1471 0.1865 -0.0266 -0.0044 0.0549  15   ASN   A N   
228  C  CA  . ASN   A 15  ? 0.1312 0.1421 0.1992 -0.0291 -0.0091 0.0429  15   ASN   A CA  
229  C  C   . ASN   A 15  ? 0.1264 0.1378 0.2200 -0.0295 -0.0070 0.0384  15   ASN   A C   
230  O  O   . ASN   A 15  ? 0.1329 0.1388 0.2677 -0.0242 -0.0290 0.0453  15   ASN   A O   
231  C  CB  . ASN   A 15  ? 0.1292 0.1436 0.1871 -0.0195 -0.0039 0.0412  15   ASN   A CB  
232  C  CG  . ASN   A 15  ? 0.1252 0.1528 0.1973 -0.0151 -0.0003 0.0303  15   ASN   A CG  
233  O  OD1 . ASN   A 15  ? 0.1419 0.1640 0.2142 -0.0309 0.0027  0.0362  15   ASN   A OD1 
234  N  ND2 . ASN   A 15  ? 0.1290 0.1572 0.1927 -0.0201 0.0078  0.0261  15   ASN   A ND2 
241  N  N   . VAL   A 16  ? 0.1262 0.1410 0.1999 -0.0275 -0.0029 0.0398  16   VAL   A N   
242  C  CA  . VAL   A 16  ? 0.1211 0.1391 0.1869 -0.0235 0.0041  0.0495  16   VAL   A CA  
243  C  C   . VAL   A 16  ? 0.1187 0.1420 0.1720 -0.0239 -0.0078 0.0450  16   VAL   A C   
244  O  O   . VAL   A 16  ? 0.1183 0.1431 0.1939 -0.0256 0.0089  0.0369  16   VAL   A O   
245  C  CB  . VAL   A 16  ? 0.1330 0.1557 0.1771 -0.0054 0.0193  0.0475  16   VAL   A CB  
246  C  CG1 . VAL   A 16  ? 0.1460 0.1723 0.1897 0.0012  0.0137  0.0472  16   VAL   A CG1 
247  C  CG2 . VAL   A 16  ? 0.1444 0.1641 0.1965 0.0006  0.0288  0.0411  16   VAL   A CG2 
257  N  N   . TYR   A 17  ? 0.1138 0.1416 0.1710 -0.0181 0.0045  0.0459  17   TYR   A N   
258  C  CA  . TYR   A 17  ? 0.1186 0.1413 0.1597 -0.0205 0.0016  0.0462  17   TYR   A CA  
259  C  C   . TYR   A 17  ? 0.1176 0.1388 0.1777 -0.0190 0.0058  0.0421  17   TYR   A C   
260  O  O   . TYR   A 17  ? 0.1175 0.1473 0.1861 -0.0156 0.0077  0.0537  17   TYR   A O   
261  C  CB  . TYR   A 17  ? 0.1366 0.1430 0.1683 -0.0257 -0.0052 0.0416  17   TYR   A CB  
262  C  CG  . TYR   A 17  ? 0.1544 0.1494 0.1683 -0.0308 -0.0143 0.0419  17   TYR   A CG  
263  C  CD1 . TYR   A 17  ? 0.1678 0.1612 0.1774 -0.0111 -0.0149 0.0378  17   TYR   A CD1 
264  C  CD2 . TYR   A 17  ? 0.1689 0.1626 0.1588 -0.0432 -0.0147 0.0384  17   TYR   A CD2 
265  C  CE1 . TYR   A 17  ? 0.1835 0.1595 0.1885 -0.0227 -0.0141 0.0406  17   TYR   A CE1 
266  C  CE2 . TYR   A 17  ? 0.1868 0.1639 0.1727 -0.0482 -0.0139 0.0250  17   TYR   A CE2 
267  C  CZ  . TYR   A 17  ? 0.1974 0.1610 0.1780 -0.0335 -0.0290 0.0408  17   TYR   A CZ  
268  O  OH  . TYR   A 17  ? 0.2184 0.1566 0.1900 -0.0310 -0.0354 0.0477  17   TYR   A OH  
278  N  N   A ILE   A 18  ? 0.1211 0.1377 0.1712 -0.0141 0.0044  0.0407  18   ILE   A N   
279  N  N   B ILE   A 18  ? 0.1174 0.1423 0.1661 -0.0210 0.0149  0.0503  18   ILE   A N   
280  C  CA  A ILE   A 18  ? 0.1265 0.1327 0.1620 -0.0099 0.0092  0.0294  18   ILE   A CA  
281  C  CA  B ILE   A 18  ? 0.1164 0.1415 0.1484 -0.0183 0.0156  0.0377  18   ILE   A CA  
282  C  C   A ILE   A 18  ? 0.1346 0.1376 0.1608 -0.0223 0.0082  0.0258  18   ILE   A C   
283  C  C   B ILE   A 18  ? 0.1114 0.1562 0.1322 -0.0258 0.0030  0.0374  18   ILE   A C   
284  O  O   A ILE   A 18  ? 0.1338 0.1465 0.1568 -0.0287 0.0031  0.0318  18   ILE   A O   
285  O  O   B ILE   A 18  ? 0.1080 0.1667 0.1486 -0.0296 0.0147  0.0365  18   ILE   A O   
286  C  CB  A ILE   A 18  ? 0.1323 0.1254 0.1475 0.0051  0.0126  0.0199  18   ILE   A CB  
287  C  CB  B ILE   A 18  ? 0.1323 0.1380 0.1406 -0.0067 0.0238  0.0362  18   ILE   A CB  
288  C  CG1 A ILE   A 18  ? 0.1383 0.1163 0.1263 0.0176  0.0069  0.0200  18   ILE   A CG1 
289  C  CG1 B ILE   A 18  ? 0.1545 0.1479 0.1498 -0.0079 0.0266  0.0332  18   ILE   A CG1 
290  C  CG2 A ILE   A 18  ? 0.1301 0.1271 0.1390 0.0117  0.0084  0.0096  18   ILE   A CG2 
291  C  CG2 B ILE   A 18  ? 0.1376 0.1438 0.1419 -0.0077 0.0204  0.0367  18   ILE   A CG2 
292  C  CD1 A ILE   A 18  ? 0.1605 0.1216 0.1347 0.0285  0.0130  0.0174  18   ILE   A CD1 
293  C  CD1 B ILE   A 18  ? 0.1729 0.1634 0.1654 0.0015  0.0385  0.0153  18   ILE   A CD1 
316  N  N   A LYS   A 19  ? 0.1348 0.1358 0.1493 -0.0200 0.0150  0.0202  19   LYS   A N   
317  N  N   B LYS   A 19  ? 0.1118 0.1609 0.1271 -0.0124 0.0180  0.0338  19   LYS   A N   
318  C  CA  A LYS   A 19  ? 0.1430 0.1452 0.1543 -0.0138 0.0136  0.0256  19   LYS   A CA  
319  C  CA  B LYS   A 19  ? 0.1268 0.1808 0.1511 -0.0011 0.0291  0.0281  19   LYS   A CA  
320  C  C   A LYS   A 19  ? 0.1355 0.1434 0.1607 -0.0050 0.0210  0.0391  19   LYS   A C   
321  C  C   B LYS   A 19  ? 0.1346 0.1861 0.1733 0.0107  0.0263  0.0272  19   LYS   A C   
322  O  O   A LYS   A 19  ? 0.1332 0.1346 0.1539 -0.0045 0.0185  0.0400  19   LYS   A O   
323  O  O   B LYS   A 19  ? 0.1367 0.1798 0.1812 0.0044  0.0231  0.0312  19   LYS   A O   
324  C  CB  A LYS   A 19  ? 0.1620 0.1589 0.1588 -0.0188 0.0087  0.0171  19   LYS   A CB  
325  C  CB  B LYS   A 19  ? 0.1351 0.1970 0.1637 -0.0031 0.0393  0.0139  19   LYS   A CB  
326  C  CG  A LYS   A 19  ? 0.1888 0.1740 0.1763 -0.0224 0.0034  0.0081  19   LYS   A CG  
327  C  CG  B LYS   A 19  ? 0.1664 0.2137 0.1824 0.0039  0.0387  0.0100  19   LYS   A CG  
328  C  CD  A LYS   A 19  ? 0.2145 0.1909 0.1832 -0.0286 0.0078  -0.0012 19   LYS   A CD  
329  C  CD  B LYS   A 19  ? 0.1924 0.2309 0.1838 0.0042  0.0424  0.0153  19   LYS   A CD  
330  C  CE  A LYS   A 19  ? 0.2337 0.1993 0.1911 -0.0409 0.0118  -0.0064 19   LYS   A CE  
331  C  CE  B LYS   A 19  ? 0.2127 0.2455 0.1985 -0.0018 0.0432  0.0149  19   LYS   A CE  
332  N  NZ  A LYS   A 19  ? 0.2459 0.2054 0.1856 -0.0538 0.0147  -0.0132 19   LYS   A NZ  
333  N  NZ  B LYS   A 19  ? 0.2284 0.2541 0.2072 -0.0113 0.0474  0.0107  19   LYS   A NZ  
360  N  N   A ASN   A 20  ? 0.1373 0.1517 0.1825 0.0003  0.0269  0.0550  20   ASN   A N   
361  N  N   B ASN   A 20  ? 0.1429 0.1994 0.1996 0.0194  0.0207  0.0274  20   ASN   A N   
362  C  CA  A ASN   A 20  ? 0.1439 0.1661 0.2078 0.0220  0.0462  0.0496  20   ASN   A CA  
363  C  CA  B ASN   A 20  ? 0.1499 0.2143 0.2253 0.0247  0.0099  0.0191  20   ASN   A CA  
364  C  C   A ASN   A 20  ? 0.1655 0.1630 0.2115 0.0212  0.0564  0.0356  20   ASN   A C   
365  C  C   B ASN   A 20  ? 0.1657 0.2117 0.2372 0.0205  0.0262  0.0049  20   ASN   A C   
366  O  O   A ASN   A 20  ? 0.1852 0.1566 0.2101 0.0186  0.0605  0.0200  20   ASN   A O   
367  O  O   B ASN   A 20  ? 0.1818 0.2120 0.2512 0.0225  0.0367  -0.0082 20   ASN   A O   
368  C  CB  A ASN   A 20  ? 0.1422 0.1841 0.2255 0.0319  0.0566  0.0639  20   ASN   A CB  
369  C  CB  B ASN   A 20  ? 0.1462 0.2280 0.2567 0.0307  -0.0128 0.0211  20   ASN   A CB  
370  C  CG  A ASN   A 20  ? 0.1474 0.1964 0.2695 0.0376  0.0610  0.0781  20   ASN   A CG  
371  C  CG  B ASN   A 20  ? 0.1495 0.2388 0.2927 0.0387  -0.0241 0.0156  20   ASN   A CG  
372  O  OD1 A ASN   A 20  ? 0.1650 0.2101 0.3160 0.0339  0.0701  0.0608  20   ASN   A OD1 
373  O  OD1 B ASN   A 20  ? 0.1441 0.2404 0.3324 0.0424  -0.0146 -0.0057 20   ASN   A OD1 
374  N  ND2 A ASN   A 20  ? 0.1559 0.1932 0.2758 0.0383  0.0379  0.1070  20   ASN   A ND2 
375  N  ND2 B ASN   A 20  ? 0.1645 0.2435 0.3014 0.0384  -0.0296 0.0308  20   ASN   A ND2 
388  N  N   A ALA   A 21  ? 0.1702 0.1661 0.2106 0.0209  0.0463  0.0311  21   ALA   A N   
389  N  N   B ALA   A 21  ? 0.1679 0.2059 0.2304 0.0135  0.0114  0.0029  21   ALA   A N   
390  C  CA  A ALA   A 21  ? 0.1798 0.1728 0.2085 0.0169  0.0417  0.0339  21   ALA   A CA  
391  C  CA  B ALA   A 21  ? 0.1710 0.2035 0.2144 0.0064  0.0181  0.0025  21   ALA   A CA  
392  C  C   A ALA   A 21  ? 0.1807 0.1779 0.2106 0.0158  0.0330  0.0346  21   ALA   A C   
393  C  C   B ALA   A 21  ? 0.1527 0.1887 0.1851 0.0023  0.0243  0.0042  21   ALA   A C   
394  O  O   A ALA   A 21  ? 0.1828 0.1823 0.2231 0.0184  0.0303  0.0304  21   ALA   A O   
395  O  O   B ALA   A 21  ? 0.1504 0.1816 0.1954 0.0086  0.0246  0.0023  21   ALA   A O   
396  C  CB  A ALA   A 21  ? 0.1931 0.1781 0.2150 0.0139  0.0385  0.0294  21   ALA   A CB  
397  C  CB  B ALA   A 21  ? 0.1896 0.2133 0.2415 0.0059  0.0132  -0.0053 21   ALA   A CB  
408  N  N   A ASP   A 22  ? 0.1851 0.1767 0.2138 0.0110  0.0215  0.0386  22   ASP   A N   
409  N  N   B ASP   A 22  ? 0.1458 0.1838 0.1581 -0.0047 0.0292  0.0096  22   ASP   A N   
410  C  CA  A ASP   A 22  ? 0.1896 0.1749 0.2144 0.0097  0.0126  0.0390  22   ASP   A CA  
411  C  CA  B ASP   A 22  ? 0.1459 0.1795 0.1516 -0.0044 0.0239  0.0056  22   ASP   A CA  
412  C  C   A ASP   A 22  ? 0.1794 0.1755 0.1851 0.0072  0.0205  0.0345  22   ASP   A C   
413  C  C   B ASP   A 22  ? 0.1323 0.1727 0.1172 -0.0151 0.0277  0.0057  22   ASP   A C   
414  O  O   A ASP   A 22  ? 0.1807 0.1794 0.1937 0.0018  0.0194  0.0288  22   ASP   A O   
415  O  O   B ASP   A 22  ? 0.1328 0.1800 0.1098 -0.0228 0.0225  -0.0025 22   ASP   A O   
416  C  CB  A ASP   A 22  ? 0.2055 0.1745 0.2458 0.0066  0.0060  0.0350  22   ASP   A CB  
417  C  CB  B ASP   A 22  ? 0.1686 0.1836 0.1819 0.0064  0.0243  0.0033  22   ASP   A CB  
418  C  CG  A ASP   A 22  ? 0.2235 0.1806 0.2755 -0.0007 0.0025  0.0347  22   ASP   A CG  
419  C  CG  B ASP   A 22  ? 0.1876 0.1882 0.2029 0.0158  0.0304  0.0015  22   ASP   A CG  
420  O  OD1 A ASP   A 22  ? 0.2187 0.1743 0.2977 -0.0118 -0.0061 0.0447  22   ASP   A OD1 
421  O  OD1 B ASP   A 22  ? 0.1826 0.1827 0.1623 0.0159  0.0258  -0.0020 22   ASP   A OD1 
422  O  OD2 A ASP   A 22  ? 0.2457 0.1923 0.2935 -0.0003 0.0089  0.0182  22   ASP   A OD2 
423  O  OD2 B ASP   A 22  ? 0.2122 0.2035 0.2596 0.0140  0.0465  0.0061  22   ASP   A OD2 
432  N  N   A ILE   A 23  ? 0.1760 0.1696 0.1598 0.0078  0.0234  0.0248  23   ILE   A N   
433  N  N   B ILE   A 23  ? 0.1314 0.1611 0.1261 -0.0112 0.0172  0.0047  23   ILE   A N   
434  C  CA  A ILE   A 23  ? 0.1701 0.1595 0.1441 0.0016  0.0259  0.0208  23   ILE   A CA  
435  C  CA  B ILE   A 23  ? 0.1325 0.1608 0.1162 -0.0144 0.0081  0.0128  23   ILE   A CA  
436  C  C   A ILE   A 23  ? 0.1636 0.1674 0.1441 0.0044  0.0405  0.0128  23   ILE   A C   
437  C  C   B ILE   A 23  ? 0.1379 0.1668 0.1202 -0.0179 0.0063  0.0064  23   ILE   A C   
438  O  O   A ILE   A 23  ? 0.1684 0.1753 0.1490 0.0030  0.0368  0.0051  23   ILE   A O   
439  O  O   B ILE   A 23  ? 0.1433 0.1637 0.1276 -0.0186 0.0018  0.0083  23   ILE   A O   
440  C  CB  A ILE   A 23  ? 0.1781 0.1534 0.1254 0.0052  0.0205  0.0102  23   ILE   A CB  
441  C  CB  B ILE   A 23  ? 0.1437 0.1581 0.1163 -0.0052 0.0084  0.0158  23   ILE   A CB  
442  C  CG1 A ILE   A 23  ? 0.1823 0.1511 0.1313 0.0067  0.0126  0.0016  23   ILE   A CG1 
443  C  CG1 B ILE   A 23  ? 0.1502 0.1585 0.1248 -0.0102 0.0034  0.0077  23   ILE   A CG1 
444  C  CG2 A ILE   A 23  ? 0.1781 0.1569 0.1270 0.0135  0.0280  0.0160  23   ILE   A CG2 
445  C  CG2 B ILE   A 23  ? 0.1486 0.1548 0.1137 0.0004  0.0101  0.0190  23   ILE   A CG2 
446  C  CD1 A ILE   A 23  ? 0.1865 0.1531 0.1435 0.0043  0.0058  -0.0084 23   ILE   A CD1 
447  C  CD1 B ILE   A 23  ? 0.1516 0.1612 0.1386 -0.0101 0.0009  -0.0047 23   ILE   A CD1 
470  N  N   A VAL   A 24  ? 0.1646 0.1712 0.1526 -0.0018 0.0326  0.0098  24   VAL   A N   
471  N  N   B VAL   A 24  ? 0.1477 0.1717 0.1264 -0.0254 -0.0028 0.0043  24   VAL   A N   
472  C  CA  A VAL   A 24  ? 0.1722 0.1857 0.1626 -0.0069 0.0239  0.0010  24   VAL   A CA  
473  C  CA  B VAL   A 24  ? 0.1653 0.1750 0.1397 -0.0309 0.0012  -0.0011 24   VAL   A CA  
474  C  C   A VAL   A 24  ? 0.1713 0.2032 0.1600 -0.0151 0.0090  0.0007  24   VAL   A C   
475  C  C   B VAL   A 24  ? 0.1717 0.1933 0.1380 -0.0307 0.0004  -0.0133 24   VAL   A C   
476  O  O   A VAL   A 24  ? 0.1795 0.2066 0.1694 -0.0155 0.0088  0.0062  24   VAL   A O   
477  O  O   B VAL   A 24  ? 0.1845 0.1975 0.1505 -0.0307 -0.0010 -0.0150 24   VAL   A O   
478  C  CB  A VAL   A 24  ? 0.1798 0.1872 0.1851 -0.0032 0.0319  0.0028  24   VAL   A CB  
479  C  CB  B VAL   A 24  ? 0.1755 0.1718 0.1709 -0.0336 0.0056  0.0071  24   VAL   A CB  
480  C  CG1 A VAL   A 24  ? 0.1841 0.1957 0.1943 0.0049  0.0359  -0.0060 24   VAL   A CG1 
481  C  CG1 B VAL   A 24  ? 0.1911 0.1819 0.2017 -0.0263 -0.0023 0.0055  24   VAL   A CG1 
482  C  CG2 A VAL   A 24  ? 0.1908 0.1874 0.1948 -0.0009 0.0377  0.0083  24   VAL   A CG2 
483  C  CG2 B VAL   A 24  ? 0.1862 0.1701 0.1805 -0.0401 0.0113  0.0058  24   VAL   A CG2 
502  N  N   A GLU   A 25  ? 0.1725 0.2240 0.1554 -0.0214 0.0086  -0.0138 25   GLU   A N   
503  N  N   B GLU   A 25  ? 0.1733 0.2148 0.1350 -0.0265 0.0174  -0.0261 25   GLU   A N   
504  C  CA  A GLU   A 25  ? 0.1861 0.2478 0.1639 -0.0151 0.0191  -0.0176 25   GLU   A CA  
505  C  CA  B GLU   A 25  ? 0.1831 0.2344 0.1387 -0.0323 0.0242  -0.0314 25   GLU   A CA  
506  C  C   A GLU   A 25  ? 0.1693 0.2491 0.1235 -0.0227 0.0318  -0.0239 25   GLU   A C   
507  C  C   B GLU   A 25  ? 0.1798 0.2407 0.1236 -0.0347 0.0253  -0.0274 25   GLU   A C   
508  O  O   A GLU   A 25  ? 0.1690 0.2585 0.1286 -0.0197 0.0295  -0.0239 25   GLU   A O   
509  O  O   B GLU   A 25  ? 0.1865 0.2487 0.1299 -0.0336 0.0254  -0.0305 25   GLU   A O   
510  C  CB  A GLU   A 25  ? 0.2143 0.2712 0.2152 -0.0108 0.0155  -0.0146 25   GLU   A CB  
511  C  CB  B GLU   A 25  ? 0.2003 0.2470 0.1854 -0.0348 0.0305  -0.0337 25   GLU   A CB  
512  C  CG  A GLU   A 25  ? 0.2413 0.2923 0.2759 -0.0154 0.0022  -0.0205 25   GLU   A CG  
513  C  CG  B GLU   A 25  ? 0.2287 0.2643 0.2625 -0.0349 0.0311  -0.0353 25   GLU   A CG  
514  C  CD  A GLU   A 25  ? 0.2611 0.3113 0.3227 -0.0168 -0.0121 -0.0234 25   GLU   A CD  
515  C  CD  B GLU   A 25  ? 0.2520 0.2828 0.3346 -0.0364 0.0239  -0.0304 25   GLU   A CD  
516  O  OE1 A GLU   A 25  ? 0.2700 0.3212 0.3237 -0.0134 -0.0218 -0.0282 25   GLU   A OE1 
517  O  OE1 B GLU   A 25  ? 0.2627 0.2909 0.3635 -0.0355 0.0207  -0.0268 25   GLU   A OE1 
518  O  OE2 A GLU   A 25  ? 0.2681 0.3180 0.3501 -0.0196 -0.0168 -0.0265 25   GLU   A OE2 
519  O  OE2 B GLU   A 25  ? 0.2602 0.2904 0.3634 -0.0376 0.0190  -0.0258 25   GLU   A OE2 
532  N  N   A GLU   A 26  ? 0.1593 0.2417 0.1302 -0.0369 0.0372  -0.0271 26   GLU   A N   
533  N  N   B GLU   A 26  ? 0.1763 0.2335 0.1264 -0.0403 0.0284  -0.0236 26   GLU   A N   
534  C  CA  A GLU   A 26  ? 0.1701 0.2429 0.1160 -0.0524 0.0354  -0.0168 26   GLU   A CA  
535  C  CA  B GLU   A 26  ? 0.1840 0.2262 0.1402 -0.0447 0.0319  -0.0088 26   GLU   A CA  
536  C  C   A GLU   A 26  ? 0.1781 0.2297 0.1065 -0.0561 0.0271  -0.0151 26   GLU   A C   
537  C  C   B GLU   A 26  ? 0.1734 0.2149 0.1222 -0.0326 0.0183  0.0020  26   GLU   A C   
538  O  O   A GLU   A 26  ? 0.1843 0.2323 0.0992 -0.0589 0.0375  -0.0221 26   GLU   A O   
539  O  O   B GLU   A 26  ? 0.1800 0.2188 0.1161 -0.0331 0.0222  -0.0011 26   GLU   A O   
540  C  CB  A GLU   A 26  ? 0.1832 0.2533 0.1363 -0.0563 0.0301  -0.0180 26   GLU   A CB  
541  C  CB  B GLU   A 26  ? 0.2086 0.2237 0.1870 -0.0571 0.0262  -0.0110 26   GLU   A CB  
542  C  CG  A GLU   A 26  ? 0.2006 0.2682 0.2113 -0.0553 0.0299  -0.0201 26   GLU   A CG  
543  C  CG  B GLU   A 26  ? 0.2299 0.2189 0.2391 -0.0697 0.0512  -0.0118 26   GLU   A CG  
544  C  CD  A GLU   A 26  ? 0.2057 0.2785 0.2473 -0.0593 0.0348  -0.0228 26   GLU   A CD  
545  C  CD  B GLU   A 26  ? 0.2414 0.2096 0.2583 -0.0933 0.0869  -0.0103 26   GLU   A CD  
546  O  OE1 A GLU   A 26  ? 0.2032 0.2838 0.2422 -0.0549 0.0484  -0.0348 26   GLU   A OE1 
547  O  OE1 B GLU   A 26  ? 0.2408 0.2018 0.2587 -0.1062 0.1020  -0.0358 26   GLU   A OE1 
548  O  OE2 A GLU   A 26  ? 0.2095 0.2797 0.2612 -0.0656 0.0259  -0.0324 26   GLU   A OE2 
549  O  OE2 B GLU   A 26  ? 0.2494 0.2151 0.2541 -0.0925 0.1118  -0.0069 26   GLU   A OE2 
562  N  N   A ALA   A 27  ? 0.1742 0.2130 0.1213 -0.0597 0.0253  -0.0065 27   ALA   A N   
563  N  N   B ALA   A 27  ? 0.1541 0.1981 0.1221 -0.0187 0.0124  0.0218  27   ALA   A N   
564  C  CA  A ALA   A 27  ? 0.1796 0.2095 0.1262 -0.0565 0.0282  -0.0045 27   ALA   A CA  
565  C  CA  B ALA   A 27  ? 0.1488 0.1960 0.1162 -0.0049 0.0063  0.0256  27   ALA   A CA  
566  C  C   A ALA   A 27  ? 0.1959 0.2257 0.1471 -0.0602 0.0222  -0.0133 27   ALA   A C   
567  C  C   B ALA   A 27  ? 0.1553 0.2068 0.1040 -0.0052 0.0011  0.0167  27   ALA   A C   
568  O  O   A ALA   A 27  ? 0.2015 0.2245 0.1540 -0.0649 0.0111  -0.0143 27   ALA   A O   
569  O  O   B ALA   A 27  ? 0.1553 0.2045 0.1108 -0.0015 -0.0010 0.0127  27   ALA   A O   
570  C  CB  A ALA   A 27  ? 0.1750 0.1978 0.1262 -0.0541 0.0248  0.0013  27   ALA   A CB  
571  C  CB  B ALA   A 27  ? 0.1447 0.1904 0.1225 -0.0071 0.0107  0.0311  27   ALA   A CB  
582  N  N   A LYS   A 28  ? 0.2198 0.2512 0.1721 -0.0494 0.0195  -0.0289 28   LYS   A N   
583  N  N   B LYS   A 28  ? 0.1809 0.2264 0.1175 0.0029  -0.0133 -0.0054 28   LYS   A N   
584  C  CA  A LYS   A 28  ? 0.2478 0.2804 0.2086 -0.0371 0.0173  -0.0346 28   LYS   A CA  
585  C  CA  B LYS   A 28  ? 0.2117 0.2568 0.1389 0.0176  -0.0276 -0.0311 28   LYS   A CA  
586  C  C   A LYS   A 28  ? 0.2607 0.3043 0.1946 -0.0431 0.0302  -0.0295 28   LYS   A C   
587  C  C   B LYS   A 28  ? 0.2388 0.2827 0.1161 0.0121  -0.0216 -0.0231 28   LYS   A C   
588  O  O   A LYS   A 28  ? 0.2669 0.3137 0.2269 -0.0425 0.0171  -0.0269 28   LYS   A O   
589  O  O   B LYS   A 28  ? 0.2547 0.2935 0.1151 0.0125  -0.0295 -0.0175 28   LYS   A O   
590  C  CB  A LYS   A 28  ? 0.2636 0.2907 0.2545 -0.0177 0.0074  -0.0372 28   LYS   A CB  
591  C  CB  B LYS   A 28  ? 0.2252 0.2693 0.1880 0.0355  -0.0411 -0.0541 28   LYS   A CB  
592  C  CG  A LYS   A 28  ? 0.2795 0.3007 0.2989 -0.0021 -0.0001 -0.0365 28   LYS   A CG  
593  C  CG  B LYS   A 28  ? 0.2422 0.2863 0.2376 0.0428  -0.0510 -0.0617 28   LYS   A CG  
594  C  CD  A LYS   A 28  ? 0.2929 0.3133 0.3460 0.0098  -0.0137 -0.0316 28   LYS   A CD  
595  C  CD  B LYS   A 28  ? 0.2662 0.3085 0.3085 0.0493  -0.0529 -0.0567 28   LYS   A CD  
596  C  CE  A LYS   A 28  ? 0.3042 0.3234 0.3760 0.0177  -0.0254 -0.0303 28   LYS   A CE  
597  C  CE  B LYS   A 28  ? 0.2885 0.3257 0.3540 0.0517  -0.0567 -0.0595 28   LYS   A CE  
598  N  NZ  A LYS   A 28  ? 0.3112 0.3278 0.4011 0.0246  -0.0259 -0.0356 28   LYS   A NZ  
599  N  NZ  B LYS   A 28  ? 0.2989 0.3340 0.3695 0.0540  -0.0675 -0.0648 28   LYS   A NZ  
626  N  N   A LYS   A 29  ? 0.2659 0.3194 0.1770 -0.0499 0.0641  -0.0151 29   LYS   A N   
627  N  N   B LYS   A 29  ? 0.2473 0.3005 0.1198 0.0051  0.0080  -0.0040 29   LYS   A N   
628  C  CA  A LYS   A 29  ? 0.2820 0.3374 0.1918 -0.0544 0.0811  -0.0098 29   LYS   A CA  
629  C  CA  B LYS   A 29  ? 0.2666 0.3223 0.1491 -0.0032 0.0344  0.0161  29   LYS   A CA  
630  C  C   A LYS   A 29  ? 0.2780 0.3306 0.1649 -0.0654 0.0616  -0.0066 29   LYS   A C   
631  C  C   B LYS   A 29  ? 0.2678 0.3188 0.1309 -0.0135 0.0222  0.0306  29   LYS   A C   
632  O  O   A LYS   A 29  ? 0.2911 0.3394 0.1637 -0.0596 0.0556  -0.0107 29   LYS   A O   
633  O  O   B LYS   A 29  ? 0.2816 0.3311 0.1454 -0.0082 0.0154  0.0328  29   LYS   A O   
634  C  CB  A LYS   A 29  ? 0.3026 0.3631 0.2617 -0.0457 0.0981  -0.0062 29   LYS   A CB  
635  C  CB  B LYS   A 29  ? 0.2877 0.3470 0.2163 -0.0015 0.0612  0.0231  29   LYS   A CB  
636  C  CG  A LYS   A 29  ? 0.3257 0.3864 0.3341 -0.0375 0.1009  -0.0001 29   LYS   A CG  
637  C  CG  B LYS   A 29  ? 0.3117 0.3689 0.2928 0.0032  0.0749  0.0274  29   LYS   A CG  
638  C  CD  A LYS   A 29  ? 0.3463 0.4058 0.4000 -0.0310 0.0998  0.0012  29   LYS   A CD  
639  C  CD  B LYS   A 29  ? 0.3326 0.3869 0.3683 0.0094  0.0814  0.0253  29   LYS   A CD  
640  C  CE  A LYS   A 29  ? 0.3604 0.4193 0.4430 -0.0266 0.1009  0.0003  29   LYS   A CE  
641  C  CE  B LYS   A 29  ? 0.3478 0.3999 0.4184 0.0132  0.0872  0.0197  29   LYS   A CE  
642  N  NZ  A LYS   A 29  ? 0.3666 0.4261 0.4742 -0.0233 0.0999  0.0003  29   LYS   A NZ  
643  N  NZ  B LYS   A 29  ? 0.3552 0.4066 0.4518 0.0160  0.0871  0.0202  29   LYS   A NZ  
670  N  N   A VAL   A 30  ? 0.2600 0.3136 0.1529 -0.0802 0.0480  0.0003  30   VAL   A N   
671  N  N   B VAL   A 30  ? 0.2556 0.3027 0.1351 -0.0244 0.0158  0.0358  30   VAL   A N   
672  C  CA  A VAL   A 30  ? 0.2528 0.2944 0.1390 -0.0920 0.0247  0.0183  30   VAL   A CA  
673  C  CA  B VAL   A 30  ? 0.2463 0.2837 0.1313 -0.0373 -0.0069 0.0484  30   VAL   A CA  
674  C  C   A VAL   A 30  ? 0.2509 0.2784 0.1054 -0.0885 0.0166  0.0368  30   VAL   A C   
675  C  C   B VAL   A 30  ? 0.2480 0.2741 0.1247 -0.0350 -0.0143 0.0417  30   VAL   A C   
676  O  O   A VAL   A 30  ? 0.2611 0.2823 0.1152 -0.0847 0.0164  0.0385  30   VAL   A O   
677  O  O   B VAL   A 30  ? 0.2546 0.2716 0.1323 -0.0329 -0.0183 0.0505  30   VAL   A O   
678  C  CB  A VAL   A 30  ? 0.2499 0.2908 0.1734 -0.1022 0.0031  0.0098  30   VAL   A CB  
679  C  CB  B VAL   A 30  ? 0.2421 0.2740 0.1496 -0.0463 -0.0287 0.0551  30   VAL   A CB  
680  C  CG1 A VAL   A 30  ? 0.2519 0.2908 0.1928 -0.1003 -0.0089 0.0018  30   VAL   A CG1 
681  C  CG1 B VAL   A 30  ? 0.2453 0.2726 0.1692 -0.0452 -0.0384 0.0553  30   VAL   A CG1 
682  C  CG2 A VAL   A 30  ? 0.2507 0.2924 0.1962 -0.1081 0.0018  0.0086  30   VAL   A CG2 
683  C  CG2 B VAL   A 30  ? 0.2408 0.2721 0.1737 -0.0536 -0.0276 0.0600  30   VAL   A CG2 
702  N  N   A LYS   A 31  ? 0.2374 0.2578 0.0952 -0.0866 0.0058  0.0335  31   LYS   A N   
703  N  N   B LYS   A 31  ? 0.2455 0.2660 0.1317 -0.0344 -0.0252 0.0236  31   LYS   A N   
704  C  CA  A LYS   A 31  ? 0.2454 0.2563 0.1092 -0.0735 -0.0145 0.0280  31   LYS   A CA  
705  C  CA  B LYS   A 31  ? 0.2509 0.2631 0.1506 -0.0281 -0.0394 0.0116  31   LYS   A CA  
706  C  C   A LYS   A 31  ? 0.2260 0.2348 0.0970 -0.0589 -0.0209 0.0574  31   LYS   A C   
707  C  C   B LYS   A 31  ? 0.2301 0.2500 0.1421 -0.0181 -0.0341 0.0330  31   LYS   A C   
708  O  O   A LYS   A 31  ? 0.2283 0.2444 0.1067 -0.0481 -0.0276 0.0693  31   LYS   A O   
709  O  O   B LYS   A 31  ? 0.2385 0.2598 0.1570 -0.0080 -0.0407 0.0342  31   LYS   A O   
710  C  CB  A LYS   A 31  ? 0.2800 0.2823 0.1984 -0.0664 -0.0270 0.0062  31   LYS   A CB  
711  C  CB  B LYS   A 31  ? 0.2824 0.2798 0.2083 -0.0262 -0.0506 -0.0146 31   LYS   A CB  
712  C  CG  A LYS   A 31  ? 0.3209 0.3076 0.3171 -0.0482 -0.0360 -0.0076 31   LYS   A CG  
713  C  CG  B LYS   A 31  ? 0.3196 0.3042 0.3123 -0.0180 -0.0539 -0.0283 31   LYS   A CG  
714  C  CD  A LYS   A 31  ? 0.3543 0.3275 0.4022 -0.0312 -0.0422 -0.0185 31   LYS   A CD  
715  C  CD  B LYS   A 31  ? 0.3491 0.3259 0.3919 -0.0119 -0.0564 -0.0394 31   LYS   A CD  
716  C  CE  A LYS   A 31  ? 0.3748 0.3402 0.4538 -0.0182 -0.0490 -0.0279 31   LYS   A CE  
717  C  CE  B LYS   A 31  ? 0.3689 0.3422 0.4469 -0.0091 -0.0600 -0.0477 31   LYS   A CE  
718  N  NZ  A LYS   A 31  ? 0.3845 0.3462 0.4850 -0.0097 -0.0560 -0.0333 31   LYS   A NZ  
719  N  NZ  B LYS   A 31  ? 0.3806 0.3513 0.4820 -0.0069 -0.0626 -0.0547 31   LYS   A NZ  
746  N  N   A PRO   A 32  ? 0.2068 0.2120 0.0929 -0.0571 -0.0172 0.0502  32   PRO   A N   
747  N  N   B PRO   A 32  ? 0.2024 0.2268 0.1225 -0.0164 -0.0131 0.0314  32   PRO   A N   
748  C  CA  A PRO   A 32  ? 0.2044 0.2027 0.1224 -0.0518 -0.0218 0.0546  32   PRO   A CA  
749  C  CA  B PRO   A 32  ? 0.1925 0.2168 0.1355 -0.0104 -0.0105 0.0373  32   PRO   A CA  
750  C  C   A PRO   A 32  ? 0.1995 0.1994 0.1230 -0.0426 -0.0259 0.0540  32   PRO   A C   
751  C  C   B PRO   A 32  ? 0.1897 0.2142 0.1381 -0.0049 -0.0218 0.0418  32   PRO   A C   
752  O  O   A PRO   A 32  ? 0.1935 0.1973 0.1125 -0.0543 -0.0248 0.0416  32   PRO   A O   
753  O  O   B PRO   A 32  ? 0.1864 0.2163 0.1426 -0.0066 -0.0225 0.0325  32   PRO   A O   
754  C  CB  A PRO   A 32  ? 0.2017 0.2100 0.1437 -0.0507 -0.0259 0.0393  32   PRO   A CB  
755  C  CB  B PRO   A 32  ? 0.1848 0.2199 0.1447 -0.0102 -0.0031 0.0227  32   PRO   A CB  
756  C  CG  A PRO   A 32  ? 0.1988 0.2118 0.1070 -0.0463 -0.0328 0.0367  32   PRO   A CG  
757  C  CG  B PRO   A 32  ? 0.1850 0.2228 0.1165 -0.0095 -0.0112 0.0178  32   PRO   A CG  
758  C  CD  A PRO   A 32  ? 0.1993 0.2081 0.0962 -0.0505 -0.0246 0.0487  32   PRO   A CD  
759  C  CD  B PRO   A 32  ? 0.1890 0.2245 0.1199 -0.0123 -0.0047 0.0248  32   PRO   A CD  
774  N  N   A THR   A 33  ? 0.2018 0.1992 0.1137 -0.0320 -0.0274 0.0591  33   THR   A N   
775  N  N   B THR   A 33  ? 0.1914 0.2102 0.1367 -0.0067 -0.0253 0.0496  33   THR   A N   
776  C  CA  A THR   A 33  ? 0.2003 0.2022 0.1383 -0.0197 -0.0301 0.0569  33   THR   A CA  
777  C  CA  B THR   A 33  ? 0.1932 0.2079 0.1421 -0.0070 -0.0311 0.0544  33   THR   A CA  
778  C  C   A THR   A 33  ? 0.1769 0.1891 0.1333 -0.0213 -0.0294 0.0447  33   THR   A C   
779  C  C   B THR   A 33  ? 0.1752 0.1855 0.1417 -0.0182 -0.0368 0.0405  33   THR   A C   
780  O  O   A THR   A 33  ? 0.1663 0.1836 0.1425 -0.0167 -0.0388 0.0482  33   THR   A O   
781  O  O   B THR   A 33  ? 0.1697 0.1684 0.1557 -0.0219 -0.0455 0.0342  33   THR   A O   
782  C  CB  A THR   A 33  ? 0.2200 0.2205 0.1687 -0.0066 -0.0360 0.0660  33   THR   A CB  
783  C  CB  B THR   A 33  ? 0.2144 0.2281 0.1564 0.0038  -0.0252 0.0755  33   THR   A CB  
784  O  OG1 A THR   A 33  ? 0.2398 0.2314 0.2016 0.0026  -0.0260 0.0706  33   THR   A OG1 
785  O  OG1 B THR   A 33  ? 0.2270 0.2434 0.1672 0.0140  -0.0270 0.0905  33   THR   A OG1 
786  C  CG2 A THR   A 33  ? 0.2228 0.2284 0.1742 -0.0018 -0.0416 0.0593  33   THR   A CG2 
787  C  CG2 B THR   A 33  ? 0.2208 0.2359 0.1690 0.0043  -0.0197 0.0656  33   THR   A CG2 
802  N  N   . VAL   A 34  ? 0.1632 0.1799 0.1275 -0.0276 -0.0275 0.0444  34   VAL   A N   
803  C  CA  . VAL   A 34  ? 0.1495 0.1644 0.1198 -0.0273 -0.0210 0.0329  34   VAL   A CA  
804  C  C   . VAL   A 34  ? 0.1460 0.1605 0.1048 -0.0223 -0.0080 0.0248  34   VAL   A C   
805  O  O   . VAL   A 34  ? 0.1427 0.1639 0.1388 -0.0334 -0.0146 0.0352  34   VAL   A O   
806  C  CB  . VAL   A 34  ? 0.1569 0.1664 0.1441 -0.0252 -0.0113 0.0268  34   VAL   A CB  
807  C  CG1 . VAL   A 34  ? 0.1697 0.1708 0.1432 -0.0199 -0.0004 0.0190  34   VAL   A CG1 
808  C  CG2 . VAL   A 34  ? 0.1617 0.1781 0.1745 -0.0196 -0.0152 0.0231  34   VAL   A CG2 
819  N  N   . VAL   A 35  ? 0.1347 0.1513 0.1051 -0.0267 -0.0115 0.0218  35   VAL   A N   
820  C  CA  . VAL   A 35  ? 0.1278 0.1480 0.1038 -0.0196 -0.0070 0.0177  35   VAL   A CA  
821  C  C   . VAL   A 35  ? 0.1223 0.1297 0.1045 -0.0135 0.0012  0.0165  35   VAL   A C   
822  O  O   . VAL   A 35  ? 0.1158 0.1437 0.1234 -0.0228 0.0063  0.0142  35   VAL   A O   
823  C  CB  . VAL   A 35  ? 0.1323 0.1525 0.1152 -0.0103 0.0024  0.0081  35   VAL   A CB  
824  C  CG1 . VAL   A 35  ? 0.1420 0.1560 0.1293 -0.0069 -0.0005 0.0027  35   VAL   A CG1 
825  C  CG2 . VAL   A 35  ? 0.1295 0.1526 0.1443 -0.0082 0.0050  0.0066  35   VAL   A CG2 
835  N  N   . VAL   A 36  ? 0.1096 0.1284 0.1034 -0.0166 0.0032  0.0198  36   VAL   A N   
836  C  CA  . VAL   A 36  ? 0.1085 0.1212 0.1021 -0.0067 0.0013  0.0160  36   VAL   A CA  
837  C  C   . VAL   A 36  ? 0.1018 0.1239 0.1087 -0.0120 0.0007  0.0120  36   VAL   A C   
838  O  O   . VAL   A 36  ? 0.1091 0.1247 0.1267 -0.0089 0.0086  0.0198  36   VAL   A O   
839  C  CB  . VAL   A 36  ? 0.1062 0.1160 0.1204 -0.0106 0.0053  0.0190  36   VAL   A CB  
840  C  CG1 . VAL   A 36  ? 0.1152 0.1208 0.1335 -0.0149 0.0057  0.0059  36   VAL   A CG1 
841  C  CG2 . VAL   A 36  ? 0.1144 0.1205 0.1308 -0.0073 -0.0073 0.0223  36   VAL   A CG2 
851  N  N   . ASN   A 37  ? 0.1009 0.1098 0.1082 -0.0032 -0.0002 0.0193  37   ASN   A N   
852  C  CA  . ASN   A 37  ? 0.1025 0.1146 0.1146 -0.0012 0.0018  0.0173  37   ASN   A CA  
853  C  C   . ASN   A 37  ? 0.1004 0.1098 0.1084 -0.0003 0.0103  0.0214  37   ASN   A C   
854  O  O   . ASN   A 37  ? 0.1121 0.1169 0.1118 0.0056  0.0075  0.0094  37   ASN   A O   
855  C  CB  . ASN   A 37  ? 0.1069 0.1122 0.1183 0.0034  0.0007  0.0085  37   ASN   A CB  
856  C  CG  . ASN   A 37  ? 0.1093 0.1088 0.1124 0.0081  0.0018  0.0102  37   ASN   A CG  
857  O  OD1 . ASN   A 37  ? 0.1087 0.1082 0.1431 0.0009  0.0008  0.0226  37   ASN   A OD1 
858  N  ND2 . ASN   A 37  ? 0.1092 0.1086 0.1339 -0.0009 -0.0029 0.0210  37   ASN   A ND2 
865  N  N   A ALA   A 38  ? 0.0998 0.1135 0.1126 -0.0007 0.0110  0.0098  38   ALA   A N   
866  N  N   B ALA   A 38  ? 0.1037 0.1191 0.1126 -0.0014 0.0064  0.0134  38   ALA   A N   
867  C  CA  A ALA   A 38  ? 0.1095 0.1159 0.1073 -0.0008 0.0020  0.0056  38   ALA   A CA  
868  C  CA  B ALA   A 38  ? 0.1141 0.1267 0.1107 -0.0020 -0.0043 0.0132  38   ALA   A CA  
869  C  C   A ALA   A 38  ? 0.1113 0.1152 0.1159 0.0033  -0.0000 0.0050  38   ALA   A C   
870  C  C   B ALA   A 38  ? 0.1103 0.1217 0.1135 0.0008  -0.0072 0.0066  38   ALA   A C   
871  O  O   A ALA   A 38  ? 0.1185 0.1044 0.1056 0.0055  -0.0068 0.0003  38   ALA   A O   
872  O  O   B ALA   A 38  ? 0.1127 0.1196 0.1163 -0.0010 -0.0135 0.0110  38   ALA   A O   
873  C  CB  A ALA   A 38  ? 0.1136 0.1340 0.1165 -0.0117 -0.0062 0.0043  38   ALA   A CB  
874  C  CB  B ALA   A 38  ? 0.1239 0.1453 0.1247 -0.0091 -0.0118 0.0106  38   ALA   A CB  
885  N  N   . ALA   A 39  ? 0.1110 0.1178 0.1276 -0.0007 0.0000  0.0129  39   ALA   A N   
886  C  CA  . ALA   A 39  ? 0.1117 0.1185 0.1243 -0.0046 0.0068  0.0064  39   ALA   A CA  
887  C  C   . ALA   A 39  ? 0.1152 0.1109 0.1278 -0.0021 0.0049  0.0095  39   ALA   A C   
888  O  O   . ALA   A 39  ? 0.1253 0.1160 0.1258 -0.0040 0.0102  0.0080  39   ALA   A O   
889  C  CB  . ALA   A 39  ? 0.1197 0.1419 0.1374 -0.0067 0.0011  -0.0032 39   ALA   A CB  
896  N  N   A ASN   A 40  ? 0.1189 0.1198 0.1269 -0.0062 0.0118  0.0040  40   ASN   A N   
897  N  N   B ASN   A 40  ? 0.1242 0.1128 0.1275 -0.0051 0.0196  0.0062  40   ASN   A N   
898  C  CA  A ASN   A 40  ? 0.1203 0.1195 0.1169 -0.0022 0.0084  0.0062  40   ASN   A CA  
899  C  CA  B ASN   A 40  ? 0.1294 0.1080 0.1190 0.0004  0.0196  0.0076  40   ASN   A CA  
900  C  C   A ASN   A 40  ? 0.1214 0.1113 0.1135 -0.0003 0.0126  0.0180  40   ASN   A C   
901  C  C   B ASN   A 40  ? 0.1318 0.1002 0.1021 -0.0007 0.0216  0.0143  40   ASN   A C   
902  O  O   A ASN   A 40  ? 0.1229 0.1123 0.1118 -0.0052 0.0150  0.0161  40   ASN   A O   
903  O  O   B ASN   A 40  ? 0.1315 0.1092 0.1099 -0.0020 0.0158  0.0145  40   ASN   A O   
904  C  CB  A ASN   A 40  ? 0.1302 0.1260 0.1219 0.0078  -0.0028 0.0102  40   ASN   A CB  
905  C  CB  B ASN   A 40  ? 0.1367 0.1108 0.1345 0.0030  0.0123  0.0088  40   ASN   A CB  
906  C  CG  A ASN   A 40  ? 0.1468 0.1265 0.1332 0.0115  -0.0071 0.0151  40   ASN   A CG  
907  C  CG  B ASN   A 40  ? 0.1465 0.1179 0.1572 -0.0022 0.0110  0.0080  40   ASN   A CG  
908  O  OD1 A ASN   A 40  ? 0.1546 0.1256 0.1466 0.0085  -0.0106 0.0213  40   ASN   A OD1 
909  O  OD1 B ASN   A 40  ? 0.1504 0.1179 0.1609 -0.0102 0.0237  -0.0011 40   ASN   A OD1 
910  N  ND2 A ASN   A 40  ? 0.1498 0.1343 0.1405 0.0168  0.0049  -0.0099 40   ASN   A ND2 
911  N  ND2 B ASN   A 40  ? 0.1470 0.1360 0.1762 -0.0088 0.0214  -0.0037 40   ASN   A ND2 
924  N  N   A VAL   A 41  ? 0.1192 0.1188 0.1109 0.0016  0.0128  0.0208  41   VAL   A N   
925  N  N   B VAL   A 41  ? 0.1338 0.1076 0.1102 -0.0011 0.0161  0.0188  41   VAL   A N   
926  C  CA  A VAL   A 41  ? 0.1170 0.1209 0.1118 -0.0022 0.0176  0.0234  41   VAL   A CA  
927  C  CA  B VAL   A 41  ? 0.1369 0.1153 0.1284 0.0001  0.0228  0.0207  41   VAL   A CA  
928  C  C   A VAL   A 41  ? 0.1185 0.1178 0.1101 -0.0024 0.0245  0.0192  41   VAL   A C   
929  C  C   B VAL   A 41  ? 0.1357 0.1154 0.1257 0.0002  0.0328  0.0140  41   VAL   A C   
930  O  O   A VAL   A 41  ? 0.1268 0.1183 0.1084 0.0036  0.0074  0.0130  41   VAL   A O   
931  O  O   B VAL   A 41  ? 0.1401 0.1099 0.1033 0.0035  0.0194  0.0014  41   VAL   A O   
932  C  CB  A VAL   A 41  ? 0.1187 0.1228 0.1100 -0.0021 0.0174  0.0177  41   VAL   A CB  
933  C  CB  B VAL   A 41  ? 0.1484 0.1249 0.1400 -0.0003 0.0251  0.0174  41   VAL   A CB  
934  C  CG1 A VAL   A 41  ? 0.1253 0.1242 0.1260 0.0001  0.0120  0.0174  41   VAL   A CG1 
935  C  CG1 B VAL   A 41  ? 0.1684 0.1308 0.1566 -0.0030 0.0295  0.0093  41   VAL   A CG1 
936  C  CG2 A VAL   A 41  ? 0.1185 0.1245 0.0986 -0.0036 0.0243  0.0208  41   VAL   A CG2 
937  C  CG2 B VAL   A 41  ? 0.1523 0.1343 0.1386 -0.0024 0.0133  0.0067  41   VAL   A CG2 
956  N  N   A TYR   A 42  ? 0.1130 0.1103 0.1507 -0.0085 0.0255  0.0250  42   TYR   A N   
957  N  N   B TYR   A 42  ? 0.1296 0.1153 0.1521 0.0029  0.0370  0.0210  42   TYR   A N   
958  C  CA  A TYR   A 42  ? 0.1185 0.1095 0.1510 -0.0125 0.0256  0.0236  42   TYR   A CA  
959  C  CA  B TYR   A 42  ? 0.1321 0.1140 0.1518 0.0005  0.0401  0.0222  42   TYR   A CA  
960  C  C   A TYR   A 42  ? 0.1130 0.1098 0.1471 -0.0117 0.0185  0.0213  42   TYR   A C   
961  C  C   B TYR   A 42  ? 0.1263 0.1162 0.1521 0.0011  0.0282  0.0244  42   TYR   A C   
962  O  O   A TYR   A 42  ? 0.1178 0.1115 0.1608 -0.0191 0.0197  0.0101  42   TYR   A O   
963  O  O   B TYR   A 42  ? 0.1306 0.1228 0.1681 -0.0036 0.0302  0.0115  42   TYR   A O   
964  C  CB  A TYR   A 42  ? 0.1325 0.1171 0.1523 -0.0140 0.0303  0.0309  42   TYR   A CB  
965  C  CB  B TYR   A 42  ? 0.1468 0.1210 0.1494 0.0010  0.0377  0.0321  42   TYR   A CB  
966  C  CG  A TYR   A 42  ? 0.1422 0.1245 0.1520 -0.0135 0.0279  0.0347  42   TYR   A CG  
967  C  CG  B TYR   A 42  ? 0.1569 0.1300 0.1499 0.0038  0.0305  0.0349  42   TYR   A CG  
968  C  CD1 A TYR   A 42  ? 0.1508 0.1371 0.1546 -0.0159 0.0278  0.0309  42   TYR   A CD1 
969  C  CD1 B TYR   A 42  ? 0.1591 0.1392 0.1485 0.0010  0.0322  0.0378  42   TYR   A CD1 
970  C  CD2 A TYR   A 42  ? 0.1453 0.1401 0.1652 0.0003  0.0296  0.0267  42   TYR   A CD2 
971  C  CD2 B TYR   A 42  ? 0.1690 0.1504 0.1745 0.0126  0.0263  0.0258  42   TYR   A CD2 
972  C  CE1 A TYR   A 42  ? 0.1550 0.1483 0.1473 -0.0154 0.0270  0.0220  42   TYR   A CE1 
973  C  CE1 B TYR   A 42  ? 0.1611 0.1516 0.1467 0.0003  0.0370  0.0412  42   TYR   A CE1 
974  C  CE2 A TYR   A 42  ? 0.1542 0.1521 0.1704 -0.0077 0.0245  0.0293  42   TYR   A CE2 
975  C  CE2 B TYR   A 42  ? 0.1751 0.1619 0.1752 0.0104  0.0278  0.0303  42   TYR   A CE2 
976  C  CZ  A TYR   A 42  ? 0.1614 0.1521 0.1532 -0.0133 0.0256  0.0249  42   TYR   A CZ  
977  C  CZ  B TYR   A 42  ? 0.1724 0.1617 0.1649 0.0033  0.0340  0.0315  42   TYR   A CZ  
978  O  OH  A TYR   A 42  ? 0.1728 0.1650 0.1678 -0.0132 0.0224  0.0096  42   TYR   A OH  
979  O  OH  B TYR   A 42  ? 0.1763 0.1762 0.1781 -0.0012 0.0324  0.0181  42   TYR   A OH  
998  N  N   A LEU   A 43  ? 0.1120 0.1073 0.1442 -0.0101 0.0159  0.0063  43   LEU   A N   
999  N  N   B LEU   A 43  ? 0.1241 0.1143 0.1480 0.0006  0.0173  0.0161  43   LEU   A N   
1000 C  CA  A LEU   A 43  ? 0.1067 0.1098 0.1407 -0.0115 0.0180  0.0099  43   LEU   A CA  
1001 C  CA  B LEU   A 43  ? 0.1217 0.1174 0.1366 -0.0028 0.0074  0.0136  43   LEU   A CA  
1002 C  C   A LEU   A 43  ? 0.1069 0.1115 0.1487 -0.0090 0.0177  0.0092  43   LEU   A C   
1003 C  C   B LEU   A 43  ? 0.1214 0.1195 0.1403 0.0035  -0.0020 0.0074  43   LEU   A C   
1004 O  O   A LEU   A 43  ? 0.1232 0.1132 0.1647 -0.0061 0.0066  0.0124  43   LEU   A O   
1005 O  O   B LEU   A 43  ? 0.1386 0.1248 0.1392 0.0103  -0.0154 0.0065  43   LEU   A O   
1006 C  CB  A LEU   A 43  ? 0.1173 0.1060 0.1576 -0.0103 0.0062  0.0054  43   LEU   A CB  
1007 C  CB  B LEU   A 43  ? 0.1170 0.1062 0.1359 -0.0070 0.0102  0.0139  43   LEU   A CB  
1008 C  CG  A LEU   A 43  ? 0.1260 0.1134 0.1611 -0.0051 0.0026  0.0018  43   LEU   A CG  
1009 C  CG  B LEU   A 43  ? 0.1192 0.1117 0.1335 -0.0031 0.0125  0.0146  43   LEU   A CG  
1010 C  CD1 A LEU   A 43  ? 0.1283 0.1190 0.1708 -0.0018 -0.0058 0.0046  43   LEU   A CD1 
1011 C  CD1 B LEU   A 43  ? 0.1200 0.1200 0.1510 -0.0024 0.0098  0.0113  43   LEU   A CD1 
1012 C  CD2 A LEU   A 43  ? 0.1371 0.1175 0.1599 -0.0069 -0.0021 0.0045  43   LEU   A CD2 
1013 C  CD2 B LEU   A 43  ? 0.1341 0.1126 0.1269 -0.0022 0.0070  0.0249  43   LEU   A CD2 
1036 N  N   A LYS   A 44  ? 0.1153 0.1088 0.1496 -0.0066 0.0207  0.0147  44   LYS   A N   
1037 N  N   B LYS   A 44  ? 0.1210 0.1178 0.1401 0.0073  -0.0042 0.0128  44   LYS   A N   
1038 C  CA  A LYS   A 44  ? 0.1284 0.1154 0.1514 -0.0064 0.0262  0.0176  44   LYS   A CA  
1039 C  CA  B LYS   A 44  ? 0.1309 0.1206 0.1370 0.0073  -0.0007 0.0150  44   LYS   A CA  
1040 C  C   A LYS   A 44  ? 0.1203 0.1148 0.1412 -0.0014 0.0109  0.0072  44   LYS   A C   
1041 C  C   B LYS   A 44  ? 0.1212 0.1183 0.1248 0.0056  -0.0003 0.0100  44   LYS   A C   
1042 O  O   A LYS   A 44  ? 0.1224 0.1289 0.1580 -0.0009 0.0087  -0.0012 44   LYS   A O   
1043 O  O   B LYS   A 44  ? 0.1234 0.1358 0.1319 0.0031  0.0021  -0.0010 44   LYS   A O   
1044 C  CB  A LYS   A 44  ? 0.1576 0.1264 0.1679 -0.0072 0.0365  0.0377  44   LYS   A CB  
1045 C  CB  B LYS   A 44  ? 0.1572 0.1343 0.1747 0.0146  0.0055  0.0128  44   LYS   A CB  
1046 C  CG  A LYS   A 44  ? 0.1814 0.1464 0.2074 -0.0064 0.0581  0.0550  44   LYS   A CG  
1047 C  CG  B LYS   A 44  ? 0.1767 0.1553 0.2370 0.0201  0.0174  0.0151  44   LYS   A CG  
1048 C  CD  A LYS   A 44  ? 0.2090 0.1887 0.2997 -0.0000 0.0483  0.0394  44   LYS   A CD  
1049 C  CD  B LYS   A 44  ? 0.1972 0.1862 0.3133 0.0163  0.0109  0.0144  44   LYS   A CD  
1050 C  CE  A LYS   A 44  ? 0.2284 0.2191 0.3578 -0.0036 0.0448  0.0276  44   LYS   A CE  
1051 C  CE  B LYS   A 44  ? 0.2089 0.2092 0.3575 0.0079  0.0066  0.0164  44   LYS   A CE  
1052 N  NZ  A LYS   A 44  ? 0.2398 0.2412 0.3869 -0.0131 0.0420  0.0201  44   LYS   A NZ  
1053 N  NZ  B LYS   A 44  ? 0.2181 0.2191 0.3769 -0.0067 0.0027  0.0120  44   LYS   A NZ  
1080 N  N   . HIS   A 45  ? 0.1101 0.1112 0.1324 -0.0018 0.0029  0.0142  45   HIS   A N   
1081 C  CA  . HIS   A 45  ? 0.1131 0.1119 0.1278 0.0004  -0.0099 0.0075  45   HIS   A CA  
1082 C  C   . HIS   A 45  ? 0.1174 0.1282 0.1358 0.0031  0.0005  0.0083  45   HIS   A C   
1083 O  O   . HIS   A 45  ? 0.1346 0.1372 0.1570 0.0196  -0.0048 -0.0096 45   HIS   A O   
1084 C  CB  . HIS   A 45  ? 0.1138 0.1137 0.1274 -0.0007 -0.0021 -0.0000 45   HIS   A CB  
1085 C  CG  . HIS   A 45  ? 0.1131 0.1124 0.1162 -0.0044 -0.0012 0.0071  45   HIS   A CG  
1086 N  ND1 . HIS   A 45  ? 0.1063 0.1197 0.1327 -0.0025 -0.0075 0.0140  45   HIS   A ND1 
1087 C  CD2 . HIS   A 45  ? 0.1116 0.1186 0.1324 -0.0078 -0.0051 0.0141  45   HIS   A CD2 
1088 C  CE1 . HIS   A 45  ? 0.1136 0.1220 0.1260 -0.0091 -0.0011 0.0220  45   HIS   A CE1 
1089 N  NE2 . HIS   A 45  ? 0.1129 0.1260 0.1289 -0.0044 -0.0022 0.0224  45   HIS   A NE2 
1098 N  N   A GLY   A 46  ? 0.1290 0.1342 0.1431 0.0046  -0.0133 0.0094  46   GLY   A N   
1099 N  N   B GLY   A 46  ? 0.1305 0.1297 0.1400 0.0116  -0.0168 0.0117  46   GLY   A N   
1100 C  CA  A GLY   A 46  ? 0.1341 0.1410 0.1633 0.0080  -0.0136 0.0144  46   GLY   A CA  
1101 C  CA  B GLY   A 46  ? 0.1373 0.1299 0.1553 0.0200  -0.0198 0.0215  46   GLY   A CA  
1102 C  C   A GLY   A 46  ? 0.1362 0.1428 0.1632 0.0114  -0.0193 0.0186  46   GLY   A C   
1103 C  C   B GLY   A 46  ? 0.1417 0.1244 0.1483 0.0283  -0.0308 0.0333  46   GLY   A C   
1104 O  O   A GLY   A 46  ? 0.1347 0.1512 0.1984 0.0008  -0.0222 0.0003  46   GLY   A O   
1105 O  O   B GLY   A 46  ? 0.1474 0.1283 0.1935 0.0345  -0.0372 0.0251  46   GLY   A O   
1112 N  N   A GLY   A 47  ? 0.1369 0.1421 0.1435 0.0185  -0.0145 0.0099  47   GLY   A N   
1113 N  N   B GLY   A 47  ? 0.1362 0.1271 0.1290 0.0221  -0.0194 0.0147  47   GLY   A N   
1114 C  CA  A GLY   A 47  ? 0.1348 0.1370 0.1263 0.0251  -0.0284 -0.0002 47   GLY   A CA  
1115 C  CA  B GLY   A 47  ? 0.1385 0.1311 0.1298 0.0178  -0.0275 0.0079  47   GLY   A CA  
1116 C  C   A GLY   A 47  ? 0.1336 0.1274 0.1329 0.0208  -0.0384 -0.0064 47   GLY   A C   
1117 C  C   B GLY   A 47  ? 0.1357 0.1264 0.1345 0.0169  -0.0235 -0.0043 47   GLY   A C   
1118 O  O   A GLY   A 47  ? 0.1358 0.1251 0.1221 0.0281  -0.0373 -0.0054 47   GLY   A O   
1119 O  O   B GLY   A 47  ? 0.1397 0.1239 0.1372 0.0233  -0.0169 0.0053  47   GLY   A O   
1126 N  N   A GLY   A 48  ? 0.1345 0.1205 0.1429 0.0200  -0.0419 -0.0080 48   GLY   A N   
1127 N  N   B GLY   A 48  ? 0.1349 0.1283 0.1541 0.0110  -0.0287 -0.0024 48   GLY   A N   
1128 C  CA  A GLY   A 48  ? 0.1374 0.1198 0.1628 0.0108  -0.0423 -0.0075 48   GLY   A CA  
1129 C  CA  B GLY   A 48  ? 0.1323 0.1274 0.1652 0.0099  -0.0256 -0.0050 48   GLY   A CA  
1130 C  C   A GLY   A 48  ? 0.1286 0.1186 0.1463 -0.0004 -0.0274 -0.0065 48   GLY   A C   
1131 C  C   B GLY   A 48  ? 0.1206 0.1297 0.1555 0.0067  -0.0058 -0.0020 48   GLY   A C   
1132 O  O   A GLY   A 48  ? 0.1401 0.1164 0.1391 0.0009  -0.0233 0.0052  48   GLY   A O   
1133 O  O   B GLY   A 48  ? 0.1375 0.1330 0.1534 0.0100  0.0005  -0.0040 48   GLY   A O   
1140 N  N   A VAL   A 49  ? 0.1259 0.1150 0.1400 -0.0074 -0.0154 -0.0059 49   VAL   A N   
1141 N  N   B VAL   A 49  ? 0.1075 0.1241 0.1480 -0.0007 0.0003  0.0038  49   VAL   A N   
1142 C  CA  A VAL   A 49  ? 0.1341 0.1133 0.1389 -0.0106 -0.0003 -0.0070 49   VAL   A CA  
1143 C  CA  B VAL   A 49  ? 0.1057 0.1246 0.1417 -0.0004 0.0087  0.0131  49   VAL   A CA  
1144 C  C   A VAL   A 49  ? 0.1276 0.1066 0.1215 -0.0040 0.0006  0.0084  49   VAL   A C   
1145 C  C   B VAL   A 49  ? 0.1078 0.1183 0.1196 0.0048  0.0112  0.0086  49   VAL   A C   
1146 O  O   A VAL   A 49  ? 0.1337 0.1113 0.1245 -0.0105 0.0041  0.0073  49   VAL   A O   
1147 O  O   B VAL   A 49  ? 0.1125 0.1246 0.1214 0.0041  0.0152  0.0088  49   VAL   A O   
1148 C  CB  A VAL   A 49  ? 0.1479 0.1179 0.1447 -0.0161 0.0026  -0.0145 49   VAL   A CB  
1149 C  CB  B VAL   A 49  ? 0.1016 0.1216 0.1354 0.0043  0.0019  0.0169  49   VAL   A CB  
1150 C  CG1 A VAL   A 49  ? 0.1465 0.1143 0.1647 -0.0084 0.0101  -0.0144 49   VAL   A CG1 
1151 C  CG1 B VAL   A 49  ? 0.0999 0.1117 0.1148 0.0099  0.0054  0.0220  49   VAL   A CG1 
1152 C  CG2 A VAL   A 49  ? 0.1586 0.1268 0.1836 -0.0236 0.0027  -0.0136 49   VAL   A CG2 
1153 C  CG2 B VAL   A 49  ? 0.1042 0.1282 0.1582 0.0053  0.0015  0.0117  49   VAL   A CG2 
1172 N  N   A ALA   A 50  ? 0.1166 0.1026 0.1237 -0.0037 -0.0126 0.0187  50   ALA   A N   
1173 N  N   B ALA   A 50  ? 0.1106 0.1112 0.1151 0.0061  0.0036  0.0008  50   ALA   A N   
1174 C  CA  A ALA   A 50  ? 0.1067 0.1055 0.1312 -0.0106 -0.0101 0.0217  50   ALA   A CA  
1175 C  CA  B ALA   A 50  ? 0.1115 0.1093 0.1222 0.0014  -0.0040 -0.0020 50   ALA   A CA  
1176 C  C   A ALA   A 50  ? 0.1039 0.1107 0.1244 -0.0098 -0.0012 0.0164  50   ALA   A C   
1177 C  C   B ALA   A 50  ? 0.1164 0.1103 0.1045 0.0026  -0.0013 -0.0024 50   ALA   A C   
1178 O  O   A ALA   A 50  ? 0.0976 0.1131 0.1334 -0.0081 -0.0015 0.0125  50   ALA   A O   
1179 O  O   B ALA   A 50  ? 0.1175 0.1127 0.0989 0.0068  -0.0048 -0.0020 50   ALA   A O   
1180 C  CB  A ALA   A 50  ? 0.1045 0.1077 0.1278 -0.0170 -0.0069 0.0148  50   ALA   A CB  
1181 C  CB  B ALA   A 50  ? 0.1120 0.1090 0.1139 0.0037  0.0035  -0.0118 50   ALA   A CB  
1192 N  N   A GLY   A 51  ? 0.1099 0.1074 0.1287 -0.0013 -0.0057 0.0161  51   GLY   A N   
1193 N  N   B GLY   A 51  ? 0.1188 0.1048 0.1127 0.0037  -0.0113 -0.0062 51   GLY   A N   
1194 C  CA  A GLY   A 51  ? 0.1199 0.1064 0.1340 0.0024  -0.0095 0.0096  51   GLY   A CA  
1195 C  CA  B GLY   A 51  ? 0.1288 0.1044 0.1044 0.0054  -0.0124 -0.0089 51   GLY   A CA  
1196 C  C   A GLY   A 51  ? 0.1106 0.1102 0.1307 0.0066  -0.0073 0.0006  51   GLY   A C   
1197 C  C   B GLY   A 51  ? 0.1219 0.1148 0.1193 0.0067  -0.0080 -0.0041 51   GLY   A C   
1198 O  O   A GLY   A 51  ? 0.1089 0.1230 0.1345 0.0066  -0.0092 -0.0057 51   GLY   A O   
1199 O  O   B GLY   A 51  ? 0.1246 0.1263 0.1297 0.0020  -0.0094 -0.0118 51   GLY   A O   
1206 N  N   A ALA   A 52  ? 0.1093 0.1176 0.1229 0.0011  -0.0061 -0.0078 52   ALA   A N   
1207 N  N   B ALA   A 52  ? 0.1210 0.1244 0.1185 -0.0001 -0.0019 -0.0069 52   ALA   A N   
1208 C  CA  A ALA   A 52  ? 0.1151 0.1285 0.1308 -0.0045 -0.0025 -0.0103 52   ALA   A CA  
1209 C  CA  B ALA   A 52  ? 0.1202 0.1352 0.1285 -0.0021 -0.0020 -0.0082 52   ALA   A CA  
1210 C  C   A ALA   A 52  ? 0.1144 0.1292 0.1174 -0.0134 0.0030  -0.0043 52   ALA   A C   
1211 C  C   B ALA   A 52  ? 0.1141 0.1370 0.1211 -0.0044 -0.0014 -0.0013 52   ALA   A C   
1212 O  O   A ALA   A 52  ? 0.1230 0.1374 0.1278 -0.0070 -0.0013 -0.0115 52   ALA   A O   
1213 O  O   B ALA   A 52  ? 0.1212 0.1428 0.1307 0.0006  -0.0052 -0.0077 52   ALA   A O   
1214 C  CB  A ALA   A 52  ? 0.1264 0.1516 0.1541 -0.0052 -0.0051 -0.0052 52   ALA   A CB  
1215 C  CB  B ALA   A 52  ? 0.1269 0.1559 0.1448 -0.0033 -0.0016 -0.0031 52   ALA   A CB  
1226 N  N   A LEU   A 53  ? 0.1127 0.1235 0.1134 -0.0143 0.0066  -0.0028 53   LEU   A N   
1227 N  N   B LEU   A 53  ? 0.1080 0.1325 0.1199 0.0034  -0.0004 -0.0004 53   LEU   A N   
1228 C  CA  A LEU   A 53  ? 0.1255 0.1296 0.1118 -0.0145 0.0093  0.0012  53   LEU   A CA  
1229 C  CA  B LEU   A 53  ? 0.1147 0.1339 0.1167 0.0046  -0.0022 0.0028  53   LEU   A CA  
1230 C  C   A LEU   A 53  ? 0.1270 0.1315 0.0973 -0.0077 0.0097  0.0055  53   LEU   A C   
1231 C  C   B LEU   A 53  ? 0.1174 0.1351 0.1052 0.0134  -0.0049 0.0045  53   LEU   A C   
1232 O  O   A LEU   A 53  ? 0.1331 0.1388 0.0942 -0.0177 0.0061  0.0011  53   LEU   A O   
1233 O  O   B LEU   A 53  ? 0.1272 0.1429 0.1166 0.0059  -0.0094 0.0071  53   LEU   A O   
1234 C  CB  A LEU   A 53  ? 0.1310 0.1318 0.1135 -0.0142 0.0014  0.0086  53   LEU   A CB  
1235 C  CB  B LEU   A 53  ? 0.1138 0.1308 0.1149 0.0029  -0.0124 0.0064  53   LEU   A CB  
1236 C  CG  A LEU   A 53  ? 0.1334 0.1334 0.1225 -0.0094 0.0011  0.0077  53   LEU   A CG  
1237 C  CG  B LEU   A 53  ? 0.1173 0.1309 0.1224 0.0008  -0.0104 0.0055  53   LEU   A CG  
1238 C  CD1 A LEU   A 53  ? 0.1338 0.1416 0.1152 -0.0006 0.0015  0.0052  53   LEU   A CD1 
1239 C  CD1 B LEU   A 53  ? 0.1287 0.1381 0.1340 -0.0014 -0.0084 0.0080  53   LEU   A CD1 
1240 C  CD2 A LEU   A 53  ? 0.1354 0.1434 0.1195 -0.0146 0.0002  0.0160  53   LEU   A CD2 
1241 C  CD2 B LEU   A 53  ? 0.1208 0.1361 0.1261 -0.0028 -0.0030 -0.0018 53   LEU   A CD2 
1264 N  N   A ASN   A 54  ? 0.1199 0.1245 0.1036 -0.0101 0.0004  0.0099  54   ASN   A N   
1265 N  N   B ASN   A 54  ? 0.1108 0.1285 0.1069 0.0109  -0.0115 -0.0032 54   ASN   A N   
1266 C  CA  A ASN   A 54  ? 0.1120 0.1188 0.1274 -0.0067 -0.0066 0.0040  54   ASN   A CA  
1267 C  CA  B ASN   A 54  ? 0.1017 0.1246 0.1123 0.0103  -0.0105 -0.0104 54   ASN   A CA  
1268 C  C   A ASN   A 54  ? 0.1171 0.1207 0.1304 -0.0114 0.0011  0.0034  54   ASN   A C   
1269 C  C   B ASN   A 54  ? 0.1123 0.1242 0.1211 -0.0011 -0.0001 -0.0043 54   ASN   A C   
1270 O  O   A ASN   A 54  ? 0.1218 0.1305 0.1340 -0.0108 -0.0067 -0.0078 54   ASN   A O   
1271 O  O   B ASN   A 54  ? 0.1162 0.1329 0.1172 0.0018  -0.0058 -0.0173 54   ASN   A O   
1272 C  CB  A ASN   A 54  ? 0.1114 0.1166 0.1436 -0.0144 -0.0125 0.0122  54   ASN   A CB  
1273 C  CB  B ASN   A 54  ? 0.0989 0.1293 0.1051 0.0086  -0.0067 -0.0074 54   ASN   A CB  
1274 C  CG  A ASN   A 54  ? 0.1187 0.1157 0.1645 -0.0112 -0.0105 0.0143  54   ASN   A CG  
1275 C  CG  B ASN   A 54  ? 0.0983 0.1310 0.1008 0.0093  0.0034  -0.0159 54   ASN   A CG  
1276 O  OD1 A ASN   A 54  ? 0.1182 0.1161 0.1880 -0.0076 -0.0147 0.0238  54   ASN   A OD1 
1277 O  OD1 B ASN   A 54  ? 0.0922 0.1309 0.0931 0.0057  -0.0019 -0.0234 54   ASN   A OD1 
1278 N  ND2 A ASN   A 54  ? 0.1282 0.1174 0.1731 -0.0155 -0.0198 0.0204  54   ASN   A ND2 
1279 N  ND2 B ASN   A 54  ? 0.1104 0.1361 0.1235 0.0034  -0.0040 0.0009  54   ASN   A ND2 
1292 N  N   . LYS   A 55  ? 0.1136 0.1248 0.1281 -0.0024 -0.0054 -0.0033 55   LYS   A N   
1293 C  CA  . LYS   A 55  ? 0.1220 0.1316 0.1306 0.0088  -0.0069 -0.0099 55   LYS   A CA  
1294 C  C   . LYS   A 55  ? 0.1202 0.1385 0.1371 0.0004  -0.0043 -0.0173 55   LYS   A C   
1295 O  O   . LYS   A 55  ? 0.1300 0.1508 0.1352 0.0053  -0.0100 -0.0221 55   LYS   A O   
1296 C  CB  . LYS   A 55  ? 0.1331 0.1363 0.1415 0.0159  -0.0081 -0.0119 55   LYS   A CB  
1297 C  CG  . LYS   A 55  ? 0.1475 0.1631 0.1519 0.0264  -0.0172 -0.0206 55   LYS   A CG  
1298 C  CD  . LYS   A 55  ? 0.1622 0.1886 0.1611 0.0381  -0.0132 -0.0194 55   LYS   A CD  
1299 C  CE  . LYS   A 55  ? 0.1827 0.2219 0.1974 0.0531  -0.0243 -0.0248 55   LYS   A CE  
1300 N  NZ  . LYS   A 55  ? 0.1903 0.2399 0.2058 0.0642  -0.0292 -0.0217 55   LYS   A NZ  
1315 N  N   . ALA   A 56  ? 0.1251 0.1460 0.1333 -0.0093 -0.0056 -0.0129 56   ALA   A N   
1316 C  CA  . ALA   A 56  ? 0.1313 0.1650 0.1280 -0.0120 0.0078  -0.0150 56   ALA   A CA  
1317 C  C   . ALA   A 56  ? 0.1391 0.1734 0.1222 -0.0129 0.0094  -0.0213 56   ALA   A C   
1318 O  O   . ALA   A 56  ? 0.1465 0.2089 0.1284 0.0028  0.0076  -0.0100 56   ALA   A O   
1319 C  CB  . ALA   A 56  ? 0.1383 0.1858 0.1401 -0.0119 0.0047  -0.0030 56   ALA   A CB  
1325 N  N   . THR   A 57  ? 0.1262 0.1550 0.1178 -0.0091 -0.0003 -0.0167 57   THR   A N   
1326 C  CA  . THR   A 57  ? 0.1334 0.1524 0.1140 -0.0094 -0.0058 -0.0105 57   THR   A CA  
1327 C  C   . THR   A 57  ? 0.1329 0.1552 0.1253 -0.0050 -0.0063 -0.0162 57   THR   A C   
1328 O  O   . THR   A 57  ? 0.1320 0.1638 0.1430 -0.0139 -0.0140 -0.0253 57   THR   A O   
1329 C  CB  . THR   A 57  ? 0.1293 0.1528 0.1155 -0.0074 -0.0027 -0.0110 57   THR   A CB  
1330 O  OG1 . THR   A 57  ? 0.1215 0.1484 0.1183 -0.0026 -0.0051 -0.0058 57   THR   A OG1 
1331 C  CG2 . THR   A 57  ? 0.1355 0.1543 0.1244 -0.0071 -0.0069 -0.0007 57   THR   A CG2 
1339 N  N   . ASN   A 58  ? 0.1364 0.1524 0.1470 -0.0052 -0.0004 -0.0214 58   ASN   A N   
1340 C  CA  . ASN   A 58  ? 0.1525 0.1501 0.1686 -0.0106 0.0081  -0.0351 58   ASN   A CA  
1341 C  C   . ASN   A 58  ? 0.1325 0.1391 0.1618 -0.0071 -0.0067 -0.0167 58   ASN   A C   
1342 O  O   . ASN   A 58  ? 0.1360 0.1497 0.1788 -0.0152 -0.0048 -0.0268 58   ASN   A O   
1343 C  CB  . ASN   A 58  ? 0.2029 0.1703 0.2039 -0.0175 0.0370  -0.0508 58   ASN   A CB  
1344 C  CG  . ASN   A 58  ? 0.2546 0.1956 0.2818 -0.0185 0.0379  -0.0370 58   ASN   A CG  
1345 O  OD1 . ASN   A 58  ? 0.2828 0.1893 0.3201 0.0138  0.0688  -0.0246 58   ASN   A OD1 
1346 N  ND2 . ASN   A 58  ? 0.2695 0.2120 0.3065 -0.0260 0.0241  -0.0451 58   ASN   A ND2 
1353 N  N   . ASN   A 59  ? 0.1184 0.1298 0.1403 -0.0064 -0.0173 -0.0073 59   ASN   A N   
1354 C  CA  . ASN   A 59  ? 0.1186 0.1197 0.1441 -0.0030 -0.0122 -0.0051 59   ASN   A CA  
1355 C  C   . ASN   A 59  ? 0.1195 0.1228 0.1348 -0.0007 -0.0131 -0.0094 59   ASN   A C   
1356 O  O   . ASN   A 59  ? 0.1190 0.1265 0.1513 -0.0039 -0.0034 0.0012  59   ASN   A O   
1357 C  CB  . ASN   A 59  ? 0.1214 0.1215 0.1528 0.0028  -0.0211 -0.0148 59   ASN   A CB  
1358 C  CG  . ASN   A 59  ? 0.1247 0.1252 0.1530 -0.0002 -0.0307 -0.0022 59   ASN   A CG  
1359 O  OD1 . ASN   A 59  ? 0.1367 0.1340 0.1372 -0.0099 -0.0227 0.0029  59   ASN   A OD1 
1360 N  ND2 . ASN   A 59  ? 0.1309 0.1289 0.1736 -0.0113 -0.0182 -0.0016 59   ASN   A ND2 
1367 N  N   . ALA   A 60  ? 0.1123 0.1295 0.1439 -0.0013 -0.0125 -0.0038 60   ALA   A N   
1368 C  CA  . ALA   A 60  ? 0.1147 0.1316 0.1424 -0.0030 -0.0147 -0.0051 60   ALA   A CA  
1369 C  C   . ALA   A 60  ? 0.1173 0.1254 0.1483 -0.0053 -0.0072 -0.0021 60   ALA   A C   
1370 O  O   . ALA   A 60  ? 0.1134 0.1268 0.1701 -0.0040 -0.0127 -0.0025 60   ALA   A O   
1371 C  CB  . ALA   A 60  ? 0.1249 0.1406 0.1584 -0.0011 -0.0185 -0.0114 60   ALA   A CB  
1377 N  N   . MET   A 61  ? 0.1117 0.1227 0.1367 -0.0060 -0.0059 -0.0027 61   MET   A N   
1378 C  CA  . MET   A 61  ? 0.1146 0.1118 0.1298 -0.0013 -0.0016 0.0028  61   MET   A CA  
1379 C  C   . MET   A 61  ? 0.1137 0.1103 0.1411 -0.0017 -0.0034 -0.0015 61   MET   A C   
1380 O  O   . MET   A 61  ? 0.1142 0.1125 0.1466 -0.0045 0.0073  0.0077  61   MET   A O   
1381 C  CB  . MET   A 61  ? 0.1148 0.1215 0.1249 -0.0026 0.0010  0.0001  61   MET   A CB  
1382 C  CG  . MET   A 61  ? 0.1113 0.1242 0.1488 -0.0011 -0.0005 -0.0006 61   MET   A CG  
1383 S  SD  . MET   A 61  ? 0.1211 0.1286 0.1635 -0.0083 -0.0038 -0.0122 61   MET   A SD  
1384 C  CE  . MET   A 61  ? 0.1371 0.1337 0.1731 -0.0123 0.0109  -0.0099 61   MET   A CE  
1394 N  N   . GLN   A 62  ? 0.1105 0.1164 0.1416 -0.0083 -0.0078 -0.0031 62   GLN   A N   
1395 C  CA  . GLN   A 62  ? 0.1151 0.1104 0.1426 -0.0058 -0.0004 0.0020  62   GLN   A CA  
1396 C  C   . GLN   A 62  ? 0.1148 0.1063 0.1433 -0.0010 0.0003  0.0028  62   GLN   A C   
1397 O  O   . GLN   A 62  ? 0.1207 0.1181 0.1478 -0.0044 0.0051  0.0018  62   GLN   A O   
1398 C  CB  . GLN   A 62  ? 0.1161 0.1132 0.1518 0.0004  0.0042  0.0024  62   GLN   A CB  
1399 C  CG  . GLN   A 62  ? 0.1177 0.1091 0.1479 -0.0042 -0.0068 0.0081  62   GLN   A CG  
1400 C  CD  . GLN   A 62  ? 0.1261 0.1132 0.1432 -0.0030 -0.0003 0.0177  62   GLN   A CD  
1401 O  OE1 . GLN   A 62  ? 0.1244 0.1279 0.1417 -0.0046 -0.0027 0.0047  62   GLN   A OE1 
1402 N  NE2 . GLN   A 62  ? 0.1281 0.1176 0.1482 0.0011  0.0048  -0.0018 62   GLN   A NE2 
1411 N  N   . VAL   A 63  ? 0.1079 0.1144 0.1652 -0.0041 0.0030  -0.0130 63   VAL   A N   
1412 C  CA  . VAL   A 63  ? 0.1133 0.1236 0.1838 -0.0090 0.0011  -0.0118 63   VAL   A CA  
1413 C  C   . VAL   A 63  ? 0.1048 0.1228 0.1733 -0.0139 -0.0063 -0.0128 63   VAL   A C   
1414 O  O   . VAL   A 63  ? 0.1087 0.1267 0.1903 -0.0105 -0.0049 -0.0084 63   VAL   A O   
1415 C  CB  . VAL   A 63  ? 0.1198 0.1374 0.2121 -0.0144 -0.0043 -0.0349 63   VAL   A CB  
1416 C  CG1 . VAL   A 63  ? 0.1390 0.1570 0.2364 -0.0126 -0.0070 -0.0572 63   VAL   A CG1 
1417 C  CG2 . VAL   A 63  ? 0.1301 0.1318 0.2357 -0.0084 0.0063  -0.0326 63   VAL   A CG2 
1427 N  N   . GLU   A 64  ? 0.1068 0.1289 0.1585 -0.0064 -0.0053 -0.0036 64   GLU   A N   
1428 C  CA  . GLU   A 64  ? 0.1083 0.1293 0.1630 -0.0063 -0.0089 0.0048  64   GLU   A CA  
1429 C  C   . GLU   A 64  ? 0.1047 0.1214 0.1603 -0.0086 0.0003  0.0092  64   GLU   A C   
1430 O  O   . GLU   A 64  ? 0.1178 0.1251 0.1584 -0.0013 -0.0010 0.0041  64   GLU   A O   
1431 C  CB  . GLU   A 64  ? 0.1161 0.1389 0.1611 -0.0064 -0.0027 -0.0025 64   GLU   A CB  
1432 C  CG  . GLU   A 64  ? 0.1243 0.1417 0.1790 -0.0132 -0.0008 -0.0019 64   GLU   A CG  
1433 C  CD  . GLU   A 64  ? 0.1351 0.1463 0.1662 -0.0212 0.0038  -0.0048 64   GLU   A CD  
1434 O  OE1 . GLU   A 64  ? 0.1311 0.1582 0.1912 -0.0234 0.0069  0.0005  64   GLU   A OE1 
1435 O  OE2 . GLU   A 64  ? 0.1532 0.1452 0.1647 -0.0231 -0.0081 0.0067  64   GLU   A OE2 
1442 N  N   . SER   A 65  ? 0.0985 0.1213 0.1498 -0.0000 0.0008  0.0045  65   SER   A N   
1443 C  CA  . SER   A 65  ? 0.1074 0.1176 0.1528 -0.0023 -0.0031 0.0020  65   SER   A CA  
1444 C  C   . SER   A 65  ? 0.1105 0.1199 0.1551 -0.0009 -0.0040 -0.0014 65   SER   A C   
1445 O  O   . SER   A 65  ? 0.1183 0.1276 0.1703 0.0007  0.0150  -0.0037 65   SER   A O   
1446 C  CB  . SER   A 65  ? 0.1110 0.1153 0.1444 -0.0085 0.0032  0.0059  65   SER   A CB  
1447 O  OG  . SER   A 65  ? 0.1092 0.1293 0.1510 -0.0082 -0.0063 0.0097  65   SER   A OG  
1453 N  N   . ASP   A 66  ? 0.1168 0.1240 0.1541 -0.0032 0.0084  0.0072  66   ASP   A N   
1454 C  CA  . ASP   A 66  ? 0.1227 0.1294 0.1661 -0.0040 0.0114  0.0179  66   ASP   A CA  
1455 C  C   . ASP   A 66  ? 0.1186 0.1258 0.1675 -0.0025 0.0109  0.0150  66   ASP   A C   
1456 O  O   . ASP   A 66  ? 0.1243 0.1384 0.1951 0.0002  0.0246  0.0240  66   ASP   A O   
1457 C  CB  . ASP   A 66  ? 0.1324 0.1383 0.1896 0.0041  0.0178  0.0294  66   ASP   A CB  
1458 C  CG  . ASP   A 66  ? 0.1558 0.1502 0.2071 -0.0015 -0.0004 0.0462  66   ASP   A CG  
1459 O  OD1 . ASP   A 66  ? 0.1566 0.1757 0.1923 -0.0080 -0.0091 0.0425  66   ASP   A OD1 
1460 O  OD2 . ASP   A 66  ? 0.1719 0.1593 0.2850 0.0135  -0.0157 0.0288  66   ASP   A OD2 
1465 N  N   . ASP   A 67  ? 0.1133 0.1262 0.1834 -0.0028 0.0080  0.0184  67   ASP   A N   
1466 C  CA  . ASP   A 67  ? 0.1154 0.1423 0.2079 -0.0020 0.0022  0.0244  67   ASP   A CA  
1467 C  C   . ASP   A 67  ? 0.1176 0.1436 0.1974 0.0025  0.0093  0.0269  67   ASP   A C   
1468 O  O   . ASP   A 67  ? 0.1168 0.1495 0.2123 0.0023  0.0208  0.0285  67   ASP   A O   
1469 C  CB  . ASP   A 67  ? 0.1252 0.1554 0.2380 -0.0056 -0.0104 0.0375  67   ASP   A CB  
1470 C  CG  . ASP   A 67  ? 0.1241 0.1663 0.2765 -0.0105 -0.0229 0.0437  67   ASP   A CG  
1471 O  OD1 . ASP   A 67  ? 0.1297 0.1822 0.3580 -0.0163 -0.0371 0.0573  67   ASP   A OD1 
1472 O  OD2 . ASP   A 67  ? 0.1310 0.1716 0.2512 -0.0037 -0.0149 0.0356  67   ASP   A OD2 
1477 N  N   . TYR   A 68  ? 0.1213 0.1313 0.1940 0.0037  0.0181  0.0279  68   TYR   A N   
1478 C  CA  . TYR   A 68  ? 0.1295 0.1306 0.1882 0.0039  0.0251  0.0281  68   TYR   A CA  
1479 C  C   . TYR   A 68  ? 0.1213 0.1275 0.1892 0.0004  0.0239  0.0204  68   TYR   A C   
1480 O  O   . TYR   A 68  ? 0.1290 0.1343 0.1950 0.0110  0.0273  0.0214  68   TYR   A O   
1481 C  CB  . TYR   A 68  ? 0.1328 0.1281 0.2033 0.0078  0.0436  0.0307  68   TYR   A CB  
1482 C  CG  . TYR   A 68  ? 0.1423 0.1426 0.2229 0.0060  0.0553  0.0294  68   TYR   A CG  
1483 C  CD1 . TYR   A 68  ? 0.1517 0.1525 0.2538 -0.0173 0.0459  -0.0014 68   TYR   A CD1 
1484 C  CD2 . TYR   A 68  ? 0.1592 0.1449 0.2635 0.0125  0.0599  0.0370  68   TYR   A CD2 
1485 C  CE1 . TYR   A 68  ? 0.1535 0.1586 0.2821 -0.0152 0.0515  -0.0073 68   TYR   A CE1 
1486 C  CE2 . TYR   A 68  ? 0.1552 0.1516 0.2829 0.0037  0.0633  0.0189  68   TYR   A CE2 
1487 C  CZ  . TYR   A 68  ? 0.1546 0.1562 0.2995 -0.0170 0.0487  -0.0104 68   TYR   A CZ  
1488 O  OH  . TYR   A 68  ? 0.1783 0.1555 0.3243 -0.0146 0.0289  -0.0263 68   TYR   A OH  
1498 N  N   . ILE   A 69  ? 0.1141 0.1213 0.1909 -0.0006 0.0183  0.0163  69   ILE   A N   
1499 C  CA  . ILE   A 69  ? 0.1246 0.1233 0.1799 0.0032  0.0147  0.0052  69   ILE   A CA  
1500 C  C   . ILE   A 69  ? 0.1299 0.1260 0.1690 0.0057  0.0178  0.0196  69   ILE   A C   
1501 O  O   . ILE   A 69  ? 0.1354 0.1376 0.1642 -0.0014 0.0242  0.0155  69   ILE   A O   
1502 C  CB  . ILE   A 69  ? 0.1286 0.1465 0.1804 0.0049  0.0166  0.0011  69   ILE   A CB  
1503 C  CG1 . ILE   A 69  ? 0.1272 0.1587 0.1901 0.0060  0.0168  -0.0155 69   ILE   A CG1 
1504 C  CG2 . ILE   A 69  ? 0.1449 0.1661 0.1929 0.0123  0.0056  -0.0109 69   ILE   A CG2 
1505 C  CD1 . ILE   A 69  ? 0.1250 0.1677 0.2091 -0.0032 0.0169  -0.0208 69   ILE   A CD1 
1517 N  N   . ALA   A 70  ? 0.1316 0.1292 0.1802 -0.0050 0.0218  0.0169  70   ALA   A N   
1518 C  CA  . ALA   A 70  ? 0.1334 0.1424 0.2032 -0.0146 0.0280  0.0262  70   ALA   A CA  
1519 C  C   . ALA   A 70  ? 0.1297 0.1602 0.1989 -0.0074 0.0255  0.0270  70   ALA   A C   
1520 O  O   . ALA   A 70  ? 0.1482 0.1945 0.2129 0.0122  0.0468  0.0421  70   ALA   A O   
1521 C  CB  . ALA   A 70  ? 0.1391 0.1371 0.2225 -0.0172 0.0244  0.0210  70   ALA   A CB  
1527 N  N   . THR   A 71  ? 0.1271 0.1558 0.1886 -0.0000 0.0230  0.0277  71   THR   A N   
1528 C  CA  . THR   A 71  ? 0.1386 0.1701 0.2227 0.0100  0.0194  0.0278  71   THR   A CA  
1529 C  C   . THR   A 71  ? 0.1258 0.1607 0.2440 0.0174  0.0294  0.0223  71   THR   A C   
1530 O  O   . THR   A 71  ? 0.1378 0.1873 0.2842 0.0139  0.0425  -0.0036 71   THR   A O   
1531 C  CB  . THR   A 71  ? 0.1643 0.2003 0.2441 0.0153  -0.0144 0.0418  71   THR   A CB  
1532 O  OG1 . THR   A 71  ? 0.1868 0.2153 0.2469 0.0035  -0.0332 0.0393  71   THR   A OG1 
1533 C  CG2 . THR   A 71  ? 0.1765 0.2188 0.2792 0.0268  -0.0267 0.0538  71   THR   A CG2 
1541 N  N   . ASN   A 72  ? 0.1256 0.1464 0.2172 0.0140  0.0253  0.0299  72   ASN   A N   
1542 C  CA  . ASN   A 72  ? 0.1369 0.1471 0.2173 0.0194  0.0339  0.0290  72   ASN   A CA  
1543 C  C   . ASN   A 72  ? 0.1481 0.1449 0.2097 0.0173  0.0514  0.0223  72   ASN   A C   
1544 O  O   . ASN   A 72  ? 0.1667 0.1437 0.2486 0.0151  0.0518  0.0129  72   ASN   A O   
1545 C  CB  . ASN   A 72  ? 0.1564 0.1516 0.2166 0.0171  0.0404  0.0322  72   ASN   A CB  
1546 C  CG  . ASN   A 72  ? 0.1792 0.1628 0.2305 0.0227  0.0428  0.0343  72   ASN   A CG  
1547 O  OD1 . ASN   A 72  ? 0.1965 0.1970 0.2477 0.0281  0.0484  0.0311  72   ASN   A OD1 
1548 N  ND2 . ASN   A 72  ? 0.1945 0.1640 0.2431 0.0501  0.0225  0.0242  72   ASN   A ND2 
1555 N  N   . GLY   A 73  ? 0.1460 0.1422 0.1994 0.0074  0.0436  0.0157  73   GLY   A N   
1556 C  CA  . GLY   A 73  ? 0.1509 0.1442 0.1870 -0.0002 0.0429  0.0119  73   GLY   A CA  
1557 C  C   . GLY   A 73  ? 0.1510 0.1299 0.1731 0.0030  0.0558  0.0243  73   GLY   A C   
1558 O  O   . GLY   A 73  ? 0.1497 0.1390 0.1984 0.0086  0.0420  0.0339  73   GLY   A O   
1562 N  N   . PRO   A 74  ? 0.1596 0.1313 0.1814 -0.0130 0.0549  0.0151  74   PRO   A N   
1563 C  CA  . PRO   A 74  ? 0.1584 0.1321 0.1881 -0.0038 0.0477  0.0167  74   PRO   A CA  
1564 C  C   . PRO   A 74  ? 0.1515 0.1179 0.1827 -0.0014 0.0389  0.0057  74   PRO   A C   
1565 O  O   . PRO   A 74  ? 0.1549 0.1253 0.2013 0.0065  0.0394  -0.0005 74   PRO   A O   
1566 C  CB  . PRO   A 74  ? 0.1706 0.1642 0.2043 -0.0003 0.0462  0.0315  74   PRO   A CB  
1567 C  CG  . PRO   A 74  ? 0.1962 0.1960 0.2522 -0.0144 0.0391  0.0203  74   PRO   A CG  
1568 C  CD  . PRO   A 74  ? 0.1771 0.1709 0.1977 -0.0196 0.0447  0.0105  74   PRO   A CD  
1576 N  N   . LEU   A 75  ? 0.1476 0.1114 0.1668 -0.0013 0.0322  0.0049  75   LEU   A N   
1577 C  CA  . LEU   A 75  ? 0.1490 0.1153 0.1483 0.0035  0.0111  0.0152  75   LEU   A CA  
1578 C  C   . LEU   A 75  ? 0.1594 0.1258 0.1359 0.0066  0.0165  0.0143  75   LEU   A C   
1579 O  O   . LEU   A 75  ? 0.1954 0.1378 0.1494 0.0134  0.0104  0.0083  75   LEU   A O   
1580 C  CB  . LEU   A 75  ? 0.1503 0.1210 0.1387 -0.0040 0.0082  0.0249  75   LEU   A CB  
1581 C  CG  . LEU   A 75  ? 0.1691 0.1550 0.1461 -0.0334 0.0089  0.0142  75   LEU   A CG  
1582 C  CD1 . LEU   A 75  ? 0.1829 0.2039 0.1572 -0.0351 0.0101  -0.0040 75   LEU   A CD1 
1583 C  CD2 . LEU   A 75  ? 0.1912 0.1933 0.1986 -0.0089 0.0089  0.0132  75   LEU   A CD2 
1595 N  N   . LYS   A 76  ? 0.1548 0.1244 0.1515 -0.0010 0.0165  0.0035  76   LYS   A N   
1596 C  CA  . LYS   A 76  ? 0.1525 0.1419 0.1539 -0.0042 0.0113  -0.0084 76   LYS   A CA  
1597 C  C   . LYS   A 76  ? 0.1509 0.1285 0.1288 0.0023  0.0142  0.0094  76   LYS   A C   
1598 O  O   . LYS   A 76  ? 0.1550 0.1232 0.1315 -0.0012 0.0168  0.0190  76   LYS   A O   
1599 C  CB  . LYS   A 76  ? 0.1512 0.1617 0.1933 0.0033  0.0075  -0.0269 76   LYS   A CB  
1600 C  CG  . LYS   A 76  ? 0.1613 0.1598 0.2406 0.0087  0.0046  -0.0202 76   LYS   A CG  
1601 C  CD  . LYS   A 76  ? 0.1683 0.1619 0.2816 0.0151  -0.0013 -0.0314 76   LYS   A CD  
1602 C  CE  . LYS   A 76  ? 0.1850 0.1778 0.3407 0.0078  0.0091  -0.0367 76   LYS   A CE  
1603 N  NZ  . LYS   A 76  ? 0.1832 0.1698 0.3789 -0.0055 0.0109  -0.0482 76   LYS   A NZ  
1617 N  N   . VAL   A 77  ? 0.1581 0.1292 0.1336 -0.0016 0.0306  0.0142  77   VAL   A N   
1618 C  CA  . VAL   A 77  ? 0.1512 0.1320 0.1293 0.0074  0.0168  0.0125  77   VAL   A CA  
1619 C  C   . VAL   A 77  ? 0.1447 0.1255 0.1345 0.0079  0.0175  0.0120  77   VAL   A C   
1620 O  O   . VAL   A 77  ? 0.1530 0.1286 0.1368 0.0107  0.0301  0.0060  77   VAL   A O   
1621 C  CB  . VAL   A 77  ? 0.1672 0.1508 0.1391 0.0058  0.0107  0.0247  77   VAL   A CB  
1622 C  CG1 . VAL   A 77  ? 0.1627 0.1638 0.1587 0.0083  -0.0047 0.0072  77   VAL   A CG1 
1623 C  CG2 . VAL   A 77  ? 0.1940 0.1632 0.1551 0.0023  -0.0012 0.0303  77   VAL   A CG2 
1633 N  N   . GLY   A 78  ? 0.1415 0.1237 0.1329 0.0054  0.0227  0.0104  78   GLY   A N   
1634 C  CA  . GLY   A 78  ? 0.1413 0.1221 0.1421 0.0001  0.0230  0.0163  78   GLY   A CA  
1635 C  C   . GLY   A 78  ? 0.1309 0.1127 0.1393 0.0037  0.0260  0.0104  78   GLY   A C   
1636 O  O   . GLY   A 78  ? 0.1333 0.1217 0.1524 -0.0027 0.0172  0.0233  78   GLY   A O   
1640 N  N   . GLY   A 79  ? 0.1324 0.1132 0.1417 0.0028  0.0177  0.0137  79   GLY   A N   
1641 C  CA  . GLY   A 79  ? 0.1317 0.1180 0.1564 0.0016  0.0183  0.0160  79   GLY   A CA  
1642 C  C   . GLY   A 79  ? 0.1185 0.1159 0.1388 0.0022  0.0153  0.0122  79   GLY   A C   
1643 O  O   . GLY   A 79  ? 0.1233 0.1249 0.1432 0.0196  0.0111  0.0116  79   GLY   A O   
1647 N  N   . SER   A 80  ? 0.1138 0.1293 0.1609 -0.0004 0.0147  0.0042  80   SER   A N   
1648 C  CA  . SER   A 80  ? 0.1109 0.1244 0.1521 -0.0007 0.0075  0.0090  80   SER   A CA  
1649 C  C   . SER   A 80  ? 0.1091 0.1263 0.1410 -0.0012 0.0084  0.0150  80   SER   A C   
1650 O  O   . SER   A 80  ? 0.1143 0.1452 0.1801 0.0047  0.0128  0.0021  80   SER   A O   
1651 C  CB  . SER   A 80  ? 0.1213 0.1221 0.1714 -0.0050 0.0084  0.0029  80   SER   A CB  
1652 O  OG  . SER   A 80  ? 0.1473 0.1231 0.2068 0.0034  -0.0023 0.0249  80   SER   A OG  
1658 N  N   . CYS   A 81  ? 0.1087 0.1225 0.1429 -0.0028 0.0000  0.0105  81   CYS   A N   
1659 C  CA  . CYS   A 81  ? 0.1072 0.1288 0.1496 -0.0054 -0.0115 0.0222  81   CYS   A CA  
1660 C  C   . CYS   A 81  ? 0.1082 0.1237 0.1424 -0.0077 -0.0043 0.0258  81   CYS   A C   
1661 O  O   . CYS   A 81  ? 0.1075 0.1525 0.1628 0.0019  -0.0010 0.0322  81   CYS   A O   
1662 C  CB  . CYS   A 81  ? 0.1175 0.1317 0.1650 -0.0135 -0.0053 0.0283  81   CYS   A CB  
1663 S  SG  . CYS   A 81  ? 0.1304 0.1247 0.1501 -0.0137 0.0013  0.0148  81   CYS   A SG  
1669 N  N   . VAL   A 82  ? 0.1136 0.1294 0.1473 -0.0001 -0.0132 0.0224  82   VAL   A N   
1670 C  CA  . VAL   A 82  ? 0.1202 0.1317 0.1458 0.0009  -0.0114 0.0280  82   VAL   A CA  
1671 C  C   . VAL   A 82  ? 0.1165 0.1371 0.1575 -0.0013 -0.0068 0.0251  82   VAL   A C   
1672 O  O   . VAL   A 82  ? 0.1149 0.1482 0.1767 -0.0014 -0.0077 0.0033  82   VAL   A O   
1673 C  CB  . VAL   A 82  ? 0.1488 0.1495 0.1590 -0.0021 -0.0058 0.0319  82   VAL   A CB  
1674 C  CG1 . VAL   A 82  ? 0.1750 0.1581 0.1896 0.0048  0.0050  0.0301  82   VAL   A CG1 
1675 C  CG2 . VAL   A 82  ? 0.1573 0.1532 0.1838 -0.0044 -0.0070 0.0433  82   VAL   A CG2 
1685 N  N   . LEU   A 83  ? 0.1116 0.1334 0.1459 -0.0098 -0.0114 0.0160  83   LEU   A N   
1686 C  CA  . LEU   A 83  ? 0.1168 0.1379 0.1369 -0.0112 -0.0141 0.0091  83   LEU   A CA  
1687 C  C   . LEU   A 83  ? 0.1253 0.1418 0.1357 -0.0148 -0.0199 0.0168  83   LEU   A C   
1688 O  O   . LEU   A 83  ? 0.1308 0.1426 0.1487 -0.0183 -0.0119 0.0217  83   LEU   A O   
1689 C  CB  . LEU   A 83  ? 0.1267 0.1399 0.1471 -0.0125 -0.0157 0.0122  83   LEU   A CB  
1690 C  CG  . LEU   A 83  ? 0.1396 0.1496 0.1503 -0.0132 0.0047  0.0123  83   LEU   A CG  
1691 C  CD1 . LEU   A 83  ? 0.1566 0.1553 0.1586 -0.0215 0.0001  0.0218  83   LEU   A CD1 
1692 C  CD2 . LEU   A 83  ? 0.1384 0.1629 0.1678 -0.0130 0.0108  0.0181  83   LEU   A CD2 
1704 N  N   . SER   A 84  ? 0.1403 0.1472 0.1361 -0.0187 -0.0181 0.0204  84   SER   A N   
1705 C  CA  . SER   A 84  ? 0.1470 0.1557 0.1169 -0.0178 -0.0159 0.0235  84   SER   A CA  
1706 C  C   . SER   A 84  ? 0.1506 0.1504 0.1247 -0.0223 -0.0034 0.0156  84   SER   A C   
1707 O  O   . SER   A 84  ? 0.1397 0.1623 0.1246 -0.0171 -0.0124 0.0116  84   SER   A O   
1708 C  CB  . SER   A 84  ? 0.1500 0.1763 0.1289 -0.0154 -0.0137 0.0133  84   SER   A CB  
1709 O  OG  . SER   A 84  ? 0.1551 0.1957 0.1458 -0.0142 -0.0210 -0.0035 84   SER   A OG  
1715 N  N   . GLY   A 85  ? 0.1626 0.1627 0.1317 -0.0214 0.0027  0.0116  85   GLY   A N   
1716 C  CA  . GLY   A 85  ? 0.1646 0.1683 0.1514 -0.0258 0.0074  -0.0003 85   GLY   A CA  
1717 C  C   . GLY   A 85  ? 0.1617 0.1748 0.1175 -0.0204 -0.0105 0.0023  85   GLY   A C   
1718 O  O   . GLY   A 85  ? 0.1642 0.1817 0.1301 -0.0288 0.0011  -0.0109 85   GLY   A O   
1722 N  N   . HIS   A 86  ? 0.1640 0.1659 0.1153 -0.0165 -0.0161 0.0055  86   HIS   A N   
1723 C  CA  . HIS   A 86  ? 0.1808 0.1739 0.1133 -0.0184 -0.0142 0.0055  86   HIS   A CA  
1724 C  C   . HIS   A 86  ? 0.2003 0.1900 0.0968 -0.0233 -0.0206 0.0114  86   HIS   A C   
1725 O  O   . HIS   A 86  ? 0.2110 0.2134 0.1106 -0.0228 -0.0128 0.0132  86   HIS   A O   
1726 C  CB  . HIS   A 86  ? 0.1780 0.1631 0.1354 -0.0131 -0.0092 0.0038  86   HIS   A CB  
1727 C  CG  . HIS   A 86  ? 0.1723 0.1631 0.1255 -0.0048 -0.0030 0.0137  86   HIS   A CG  
1728 N  ND1 . HIS   A 86  ? 0.1788 0.1623 0.1587 -0.0192 -0.0088 0.0092  86   HIS   A ND1 
1729 C  CD2 . HIS   A 86  ? 0.1733 0.1581 0.1235 0.0052  0.0021  0.0115  86   HIS   A CD2 
1730 C  CE1 . HIS   A 86  ? 0.1748 0.1630 0.1574 -0.0168 0.0114  0.0131  86   HIS   A CE1 
1731 N  NE2 . HIS   A 86  ? 0.1713 0.1556 0.1316 0.0021  0.0083  0.0210  86   HIS   A NE2 
1739 N  N   . ASN   A 87  ? 0.2142 0.1993 0.1175 -0.0174 0.0006  -0.0031 87   ASN   A N   
1740 C  CA  . ASN   A 87  ? 0.2319 0.2125 0.1153 -0.0131 0.0223  -0.0074 87   ASN   A CA  
1741 C  C   . ASN   A 87  ? 0.2240 0.2227 0.1467 -0.0196 0.0334  -0.0029 87   ASN   A C   
1742 O  O   . ASN   A 87  ? 0.2523 0.2458 0.1911 -0.0328 0.0704  -0.0116 87   ASN   A O   
1743 C  CB  . ASN   A 87  ? 0.2516 0.2188 0.1214 -0.0008 0.0211  -0.0074 87   ASN   A CB  
1744 C  CG  . ASN   A 87  ? 0.2691 0.2272 0.1332 0.0082  0.0353  -0.0082 87   ASN   A CG  
1745 O  OD1 . ASN   A 87  ? 0.2869 0.2226 0.1414 0.0252  0.0346  0.0002  87   ASN   A OD1 
1746 N  ND2 . ASN   A 87  ? 0.2735 0.2514 0.1450 0.0066  0.0405  -0.0006 87   ASN   A ND2 
1753 N  N   A LEU   A 88  ? 0.1980 0.2069 0.1323 -0.0210 0.0157  0.0108  88   LEU   A N   
1754 N  N   B LEU   A 88  ? 0.2012 0.2122 0.1352 -0.0181 0.0211  0.0030  88   LEU   A N   
1755 C  CA  A LEU   A 88  ? 0.1799 0.2011 0.1436 -0.0239 0.0147  0.0303  88   LEU   A CA  
1756 C  CA  B LEU   A 88  ? 0.1854 0.2101 0.1466 -0.0187 0.0242  0.0167  88   LEU   A CA  
1757 C  C   A LEU   A 88  ? 0.1706 0.2078 0.1398 -0.0240 0.0218  0.0305  88   LEU   A C   
1758 C  C   B LEU   A 88  ? 0.1738 0.2126 0.1444 -0.0199 0.0207  0.0289  88   LEU   A C   
1759 O  O   A LEU   A 88  ? 0.1698 0.2121 0.1745 -0.0235 0.0272  0.0355  88   LEU   A O   
1760 O  O   B LEU   A 88  ? 0.1734 0.2166 0.1646 -0.0164 0.0231  0.0472  88   LEU   A O   
1761 C  CB  A LEU   A 88  ? 0.1774 0.1995 0.1509 -0.0273 -0.0177 0.0423  88   LEU   A CB  
1762 C  CB  B LEU   A 88  ? 0.1868 0.2147 0.1520 -0.0195 0.0085  0.0132  88   LEU   A CB  
1763 C  CG  A LEU   A 88  ? 0.1912 0.2101 0.1823 -0.0233 -0.0290 0.0474  88   LEU   A CG  
1764 C  CG  B LEU   A 88  ? 0.1977 0.2262 0.1690 -0.0125 0.0056  0.0064  88   LEU   A CG  
1765 C  CD1 A LEU   A 88  ? 0.1964 0.2128 0.1683 -0.0270 -0.0380 0.0450  88   LEU   A CD1 
1766 C  CD1 B LEU   A 88  ? 0.1990 0.2296 0.1576 -0.0119 0.0042  -0.0044 88   LEU   A CD1 
1767 C  CD2 A LEU   A 88  ? 0.2047 0.2208 0.2229 -0.0154 -0.0241 0.0385  88   LEU   A CD2 
1768 C  CD2 B LEU   A 88  ? 0.2083 0.2333 0.1931 -0.0056 0.0104  0.0048  88   LEU   A CD2 
1791 N  N   . ALA   A 89  ? 0.1649 0.2087 0.1371 -0.0207 0.0099  0.0139  89   ALA   A N   
1792 C  CA  . ALA   A 89  ? 0.1681 0.2077 0.1215 -0.0176 0.0000  0.0180  89   ALA   A CA  
1793 C  C   . ALA   A 89  ? 0.1758 0.2087 0.1229 -0.0159 -0.0107 0.0212  89   ALA   A C   
1794 O  O   . ALA   A 89  ? 0.1690 0.2003 0.1619 -0.0240 -0.0128 -0.0007 89   ALA   A O   
1795 C  CB  . ALA   A 89  ? 0.1631 0.2010 0.1202 -0.0205 0.0048  0.0156  89   ALA   A CB  
1802 N  N   A LYS   A 90  ? 0.1809 0.2177 0.1263 -0.0207 -0.0212 0.0237  90   LYS   A N   
1803 N  N   B LYS   A 90  ? 0.1811 0.2168 0.1252 -0.0190 -0.0206 0.0242  90   LYS   A N   
1804 C  CA  A LYS   A 90  ? 0.1856 0.2273 0.1354 -0.0202 -0.0387 0.0265  90   LYS   A CA  
1805 C  CA  B LYS   A 90  ? 0.1862 0.2254 0.1321 -0.0170 -0.0389 0.0273  90   LYS   A CA  
1806 C  C   A LYS   A 90  ? 0.1711 0.2134 0.1358 -0.0223 -0.0334 0.0176  90   LYS   A C   
1807 C  C   B LYS   A 90  ? 0.1727 0.2104 0.1295 -0.0182 -0.0346 0.0229  90   LYS   A C   
1808 O  O   A LYS   A 90  ? 0.1776 0.2261 0.1619 -0.0272 -0.0327 0.0035  90   LYS   A O   
1809 O  O   B LYS   A 90  ? 0.1818 0.2190 0.1465 -0.0185 -0.0364 0.0174  90   LYS   A O   
1810 C  CB  A LYS   A 90  ? 0.2077 0.2526 0.1734 -0.0176 -0.0504 0.0465  90   LYS   A CB  
1811 C  CB  B LYS   A 90  ? 0.2080 0.2508 0.1718 -0.0139 -0.0496 0.0432  90   LYS   A CB  
1812 C  CG  A LYS   A 90  ? 0.2372 0.2799 0.2549 -0.0158 -0.0512 0.0529  90   LYS   A CG  
1813 C  CG  B LYS   A 90  ? 0.2367 0.2780 0.2521 -0.0121 -0.0514 0.0452  90   LYS   A CG  
1814 C  CD  A LYS   A 90  ? 0.2648 0.3048 0.3412 -0.0163 -0.0367 0.0502  90   LYS   A CD  
1815 C  CD  B LYS   A 90  ? 0.2633 0.3021 0.3362 -0.0122 -0.0382 0.0396  90   LYS   A CD  
1816 C  CE  A LYS   A 90  ? 0.2916 0.3251 0.4040 -0.0167 -0.0242 0.0467  90   LYS   A CE  
1817 C  CE  B LYS   A 90  ? 0.2896 0.3210 0.3993 -0.0116 -0.0266 0.0341  90   LYS   A CE  
1818 N  NZ  A LYS   A 90  ? 0.3060 0.3379 0.4489 -0.0180 -0.0159 0.0456  90   LYS   A NZ  
1819 N  NZ  B LYS   A 90  ? 0.3037 0.3318 0.4431 -0.0114 -0.0185 0.0321  90   LYS   A NZ  
1846 N  N   . HIS   A 91  ? 0.1613 0.1897 0.1184 -0.0204 -0.0343 0.0242  91   HIS   A N   
1847 C  CA  . HIS   A 91  ? 0.1456 0.1677 0.1298 -0.0084 -0.0279 0.0167  91   HIS   A CA  
1848 C  C   . HIS   A 91  ? 0.1333 0.1540 0.1213 -0.0136 -0.0166 0.0167  91   HIS   A C   
1849 O  O   . HIS   A 91  ? 0.1336 0.1704 0.1282 -0.0209 -0.0090 0.0183  91   HIS   A O   
1850 C  CB  . HIS   A 91  ? 0.1638 0.1939 0.1664 0.0088  -0.0404 0.0181  91   HIS   A CB  
1851 C  CG  . HIS   A 91  ? 0.2055 0.2473 0.2257 0.0181  -0.0703 0.0107  91   HIS   A CG  
1852 N  ND1 . HIS   A 91  ? 0.2122 0.2768 0.2638 0.0203  -0.0820 -0.0097 91   HIS   A ND1 
1853 C  CD2 . HIS   A 91  ? 0.2341 0.2688 0.2463 0.0260  -0.0880 0.0207  91   HIS   A CD2 
1854 C  CE1 . HIS   A 91  ? 0.2229 0.2884 0.2634 0.0266  -0.0922 0.0087  91   HIS   A CE1 
1855 N  NE2 . HIS   A 91  ? 0.2424 0.2871 0.2658 0.0298  -0.0951 0.0169  91   HIS   A NE2 
1864 N  N   . CYS   A 92  ? 0.1269 0.1469 0.1200 -0.0189 -0.0173 0.0215  92   CYS   A N   
1865 C  CA  . CYS   A 92  ? 0.1238 0.1427 0.1309 -0.0170 -0.0059 0.0176  92   CYS   A CA  
1866 C  C   . CYS   A 92  ? 0.1223 0.1360 0.1142 -0.0164 -0.0024 0.0164  92   CYS   A C   
1867 O  O   . CYS   A 92  ? 0.1210 0.1411 0.1368 -0.0200 -0.0061 0.0103  92   CYS   A O   
1868 C  CB  . CYS   A 92  ? 0.1266 0.1418 0.1231 -0.0107 -0.0164 0.0085  92   CYS   A CB  
1869 S  SG  . CYS   A 92  ? 0.1242 0.1287 0.1241 -0.0122 -0.0085 0.0139  92   CYS   A SG  
1875 N  N   . LEU   A 93  ? 0.1183 0.1271 0.1203 -0.0112 0.0039  0.0138  93   LEU   A N   
1876 C  CA  . LEU   A 93  ? 0.1097 0.1211 0.1305 -0.0068 -0.0020 0.0149  93   LEU   A CA  
1877 C  C   . LEU   A 93  ? 0.1037 0.1109 0.1200 -0.0042 -0.0023 0.0138  93   LEU   A C   
1878 O  O   . LEU   A 93  ? 0.1037 0.1196 0.1215 0.0003  -0.0008 0.0135  93   LEU   A O   
1879 C  CB  . LEU   A 93  ? 0.1106 0.1213 0.1379 -0.0028 -0.0056 0.0286  93   LEU   A CB  
1880 C  CG  . LEU   A 93  ? 0.1204 0.1229 0.1345 -0.0010 0.0009  0.0219  93   LEU   A CG  
1881 C  CD1 . LEU   A 93  ? 0.1302 0.1275 0.1638 0.0018  0.0089  0.0189  93   LEU   A CD1 
1882 C  CD2 . LEU   A 93  ? 0.1335 0.1207 0.1493 -0.0103 -0.0013 0.0164  93   LEU   A CD2 
1894 N  N   . HIS   A 94  ? 0.1068 0.1099 0.1207 -0.0046 -0.0065 0.0211  94   HIS   A N   
1895 C  CA  . HIS   A 94  ? 0.1080 0.1090 0.1233 -0.0052 -0.0011 0.0155  94   HIS   A CA  
1896 C  C   . HIS   A 94  ? 0.1035 0.1090 0.1240 -0.0051 -0.0021 0.0166  94   HIS   A C   
1897 O  O   . HIS   A 94  ? 0.1061 0.1272 0.1546 0.0037  0.0035  0.0005  94   HIS   A O   
1898 C  CB  . HIS   A 94  ? 0.1058 0.1093 0.1299 -0.0036 -0.0020 0.0160  94   HIS   A CB  
1899 C  CG  . HIS   A 94  ? 0.1140 0.1080 0.1237 -0.0048 -0.0039 0.0156  94   HIS   A CG  
1900 N  ND1 . HIS   A 94  ? 0.1082 0.1068 0.1430 -0.0097 -0.0008 0.0220  94   HIS   A ND1 
1901 C  CD2 . HIS   A 94  ? 0.1184 0.1190 0.1365 -0.0057 -0.0098 0.0104  94   HIS   A CD2 
1902 C  CE1 . HIS   A 94  ? 0.1106 0.1117 0.1394 -0.0108 -0.0135 0.0118  94   HIS   A CE1 
1903 N  NE2 . HIS   A 94  ? 0.1186 0.1160 0.1405 -0.0070 -0.0103 0.0006  94   HIS   A NE2 
1911 N  N   . VAL   A 95  ? 0.1037 0.1047 0.1134 -0.0032 0.0042  0.0103  95   VAL   A N   
1912 C  CA  . VAL   A 95  ? 0.1121 0.1069 0.1166 -0.0064 0.0099  0.0149  95   VAL   A CA  
1913 C  C   . VAL   A 95  ? 0.1091 0.1030 0.1124 -0.0081 0.0103  0.0118  95   VAL   A C   
1914 O  O   . VAL   A 95  ? 0.1124 0.1149 0.1238 0.0082  0.0069  0.0112  95   VAL   A O   
1915 C  CB  . VAL   A 95  ? 0.1123 0.1116 0.1263 -0.0092 0.0015  0.0074  95   VAL   A CB  
1916 C  CG1 . VAL   A 95  ? 0.1268 0.1121 0.1393 -0.0130 0.0011  0.0070  95   VAL   A CG1 
1917 C  CG2 . VAL   A 95  ? 0.1092 0.1149 0.1326 -0.0109 0.0072  0.0206  95   VAL   A CG2 
1927 N  N   . VAL   A 96  ? 0.1097 0.1098 0.1149 -0.0025 0.0057  0.0155  96   VAL   A N   
1928 C  CA  . VAL   A 96  ? 0.1213 0.1087 0.1253 -0.0016 0.0077  0.0212  96   VAL   A CA  
1929 C  C   . VAL   A 96  ? 0.1210 0.1176 0.1153 0.0012  0.0114  0.0228  96   VAL   A C   
1930 O  O   . VAL   A 96  ? 0.1281 0.1241 0.1365 -0.0016 0.0160  0.0056  96   VAL   A O   
1931 C  CB  . VAL   A 96  ? 0.1235 0.1158 0.1300 0.0014  0.0192  0.0159  96   VAL   A CB  
1932 C  CG1 . VAL   A 96  ? 0.1285 0.1261 0.1196 -0.0008 0.0113  0.0157  96   VAL   A CG1 
1933 C  CG2 . VAL   A 96  ? 0.1275 0.1232 0.1351 -0.0127 0.0212  0.0084  96   VAL   A CG2 
1943 N  N   . GLY   A 97  ? 0.1208 0.1202 0.1260 -0.0036 0.0092  0.0195  97   GLY   A N   
1944 C  CA  . GLY   A 97  ? 0.1294 0.1320 0.1212 -0.0039 -0.0028 0.0168  97   GLY   A CA  
1945 C  C   . GLY   A 97  ? 0.1320 0.1477 0.1134 -0.0087 0.0007  0.0183  97   GLY   A C   
1946 O  O   . GLY   A 97  ? 0.1448 0.1452 0.1377 -0.0100 0.0003  0.0261  97   GLY   A O   
1950 N  N   A PRO   A 98  ? 0.1334 0.1569 0.0992 -0.0016 -0.0036 0.0215  98   PRO   A N   
1951 N  N   B PRO   A 98  ? 0.1426 0.1439 0.1205 -0.0014 0.0034  0.0202  98   PRO   A N   
1952 C  CA  A PRO   A 98  ? 0.1342 0.1752 0.1025 -0.0037 -0.0019 0.0242  98   PRO   A CA  
1953 C  CA  B PRO   A 98  ? 0.1565 0.1550 0.1428 -0.0009 0.0070  0.0159  98   PRO   A CA  
1954 C  C   A PRO   A 98  ? 0.1263 0.1844 0.0941 -0.0119 -0.0073 0.0342  98   PRO   A C   
1955 C  C   B PRO   A 98  ? 0.1762 0.1468 0.1504 -0.0022 0.0071  0.0231  98   PRO   A C   
1956 O  O   A PRO   A 98  ? 0.1166 0.1739 0.1171 -0.0092 -0.0009 0.0363  98   PRO   A O   
1957 O  O   B PRO   A 98  ? 0.1752 0.1327 0.1701 0.0027  0.0144  0.0247  98   PRO   A O   
1958 C  CB  A PRO   A 98  ? 0.1472 0.1787 0.0882 0.0087  -0.0074 0.0129  98   PRO   A CB  
1959 C  CB  B PRO   A 98  ? 0.1588 0.1558 0.1344 0.0084  0.0044  0.0165  98   PRO   A CB  
1960 C  CG  A PRO   A 98  ? 0.1473 0.1716 0.0989 0.0060  -0.0108 0.0078  98   PRO   A CG  
1961 C  CG  B PRO   A 98  ? 0.1611 0.1527 0.1388 0.0041  0.0036  0.0087  98   PRO   A CG  
1962 C  CD  A PRO   A 98  ? 0.1385 0.1583 0.1030 0.0040  -0.0080 0.0144  98   PRO   A CD  
1963 C  CD  B PRO   A 98  ? 0.1473 0.1388 0.1240 0.0038  0.0041  0.0153  98   PRO   A CD  
1978 N  N   A ASN   A 99  ? 0.1311 0.1999 0.0919 -0.0129 0.0045  0.0358  99   ASN   A N   
1979 N  N   B ASN   A 99  ? 0.2026 0.1505 0.1323 0.0022  0.0071  0.0296  99   ASN   A N   
1980 C  CA  A ASN   A 99  ? 0.1526 0.2137 0.0998 -0.0213 0.0007  0.0472  99   ASN   A CA  
1981 C  CA  B ASN   A 99  ? 0.2327 0.1550 0.1254 0.0079  0.0031  0.0398  99   ASN   A CA  
1982 C  C   A ASN   A 99  ? 0.1761 0.2363 0.1077 -0.0416 -0.0086 0.0557  99   ASN   A C   
1983 C  C   B ASN   A 99  ? 0.2553 0.1655 0.1228 0.0103  -0.0142 0.0454  99   ASN   A C   
1984 O  O   A ASN   A 99  ? 0.1875 0.2482 0.1133 -0.0393 -0.0101 0.0429  99   ASN   A O   
1985 O  O   B ASN   A 99  ? 0.2571 0.1537 0.1196 0.0195  -0.0262 0.0309  99   ASN   A O   
1986 C  CB  A ASN   A 99  ? 0.1534 0.2081 0.1112 -0.0156 -0.0054 0.0482  99   ASN   A CB  
1987 C  CB  B ASN   A 99  ? 0.2418 0.1551 0.1454 0.0134  0.0074  0.0364  99   ASN   A CB  
1988 C  CG  A ASN   A 99  ? 0.1585 0.2059 0.1263 -0.0041 -0.0126 0.0301  99   ASN   A CG  
1989 C  CG  B ASN   A 99  ? 0.2533 0.1589 0.1573 0.0147  0.0129  0.0488  99   ASN   A CG  
1990 O  OD1 A ASN   A 99  ? 0.1699 0.2135 0.1211 0.0080  -0.0031 0.0142  99   ASN   A OD1 
1991 O  OD1 B ASN   A 99  ? 0.2527 0.1664 0.1490 0.0213  0.0083  0.0579  99   ASN   A OD1 
1992 N  ND2 A ASN   A 99  ? 0.1609 0.1978 0.1475 -0.0087 -0.0169 0.0483  99   ASN   A ND2 
1993 N  ND2 B ASN   A 99  ? 0.2626 0.1600 0.2066 0.0184  0.0024  0.0260  99   ASN   A ND2 
2006 N  N   A VAL   A 100 ? 0.1905 0.2512 0.1333 -0.0507 -0.0300 0.0600  100  VAL   A N   
2007 N  N   B VAL   A 100 ? 0.2687 0.1878 0.1482 0.0114  -0.0280 0.0518  100  VAL   A N   
2008 C  CA  A VAL   A 100 ? 0.2094 0.2671 0.1597 -0.0522 -0.0343 0.0548  100  VAL   A CA  
2009 C  CA  B VAL   A 100 ? 0.2836 0.2046 0.1845 0.0135  -0.0343 0.0471  100  VAL   A CA  
2010 C  C   A VAL   A 100 ? 0.2148 0.2703 0.1594 -0.0534 -0.0277 0.0749  100  VAL   A C   
2011 C  C   B VAL   A 100 ? 0.2872 0.1966 0.1783 0.0233  -0.0417 0.0426  100  VAL   A C   
2012 O  O   A VAL   A 100 ? 0.2218 0.2726 0.1648 -0.0443 -0.0174 0.0886  100  VAL   A O   
2013 O  O   B VAL   A 100 ? 0.2898 0.1924 0.2012 0.0157  -0.0402 0.0376  100  VAL   A O   
2014 C  CB  A VAL   A 100 ? 0.2259 0.2770 0.1993 -0.0510 -0.0399 0.0318  100  VAL   A CB  
2015 C  CB  B VAL   A 100 ? 0.2939 0.2338 0.2387 0.0164  -0.0264 0.0335  100  VAL   A CB  
2016 C  CG1 A VAL   A 100 ? 0.2264 0.2823 0.2209 -0.0454 -0.0352 0.0239  100  VAL   A CG1 
2017 C  CG1 B VAL   A 100 ? 0.2979 0.2416 0.2672 0.0176  -0.0226 0.0276  100  VAL   A CG1 
2018 C  CG2 A VAL   A 100 ? 0.2301 0.2753 0.2021 -0.0577 -0.0516 0.0157  100  VAL   A CG2 
2019 C  CG2 B VAL   A 100 ? 0.2956 0.2449 0.2601 0.0156  -0.0244 0.0322  100  VAL   A CG2 
2038 N  N   A ASN   A 101 ? 0.2198 0.2761 0.1722 -0.0579 -0.0214 0.0893  101  ASN   A N   
2039 N  N   B ASN   A 101 ? 0.2911 0.1994 0.1595 0.0344  -0.0441 0.0395  101  ASN   A N   
2040 C  CA  A ASN   A 101 ? 0.2372 0.2834 0.1846 -0.0605 -0.0183 0.0957  101  ASN   A CA  
2041 C  CA  B ASN   A 101 ? 0.2991 0.2106 0.1640 0.0416  -0.0363 0.0387  101  ASN   A CA  
2042 C  C   A ASN   A 101 ? 0.2579 0.3096 0.2145 -0.0607 0.0067  0.1075  101  ASN   A C   
2043 C  C   B ASN   A 101 ? 0.3167 0.2265 0.1468 0.0404  -0.0165 0.0523  101  ASN   A C   
2044 O  O   A ASN   A 101 ? 0.2725 0.3172 0.2376 -0.0599 0.0055  0.0980  101  ASN   A O   
2045 O  O   B ASN   A 101 ? 0.3278 0.2341 0.1421 0.0359  -0.0089 0.0633  101  ASN   A O   
2046 C  CB  A ASN   A 101 ? 0.2345 0.2654 0.1661 -0.0608 -0.0380 0.0877  101  ASN   A CB  
2047 C  CB  B ASN   A 101 ? 0.2905 0.2102 0.1686 0.0413  -0.0393 0.0341  101  ASN   A CB  
2048 C  CG  A ASN   A 101 ? 0.2322 0.2501 0.1533 -0.0564 -0.0462 0.0613  101  ASN   A CG  
2049 C  CG  B ASN   A 101 ? 0.2869 0.2217 0.1916 0.0321  -0.0398 0.0318  101  ASN   A CG  
2050 O  OD1 A ASN   A 101 ? 0.2244 0.2469 0.1536 -0.0426 -0.0404 0.0268  101  ASN   A OD1 
2051 O  OD1 B ASN   A 101 ? 0.2910 0.2350 0.2152 0.0218  -0.0390 0.0296  101  ASN   A OD1 
2052 N  ND2 A ASN   A 101 ? 0.2390 0.2456 0.1620 -0.0617 -0.0529 0.0575  101  ASN   A ND2 
2053 N  ND2 B ASN   A 101 ? 0.2807 0.2172 0.2084 0.0351  -0.0307 0.0188  101  ASN   A ND2 
2066 N  N   A LYS   A 102 ? 0.2573 0.3288 0.2282 -0.0634 0.0267  0.1166  102  LYS   A N   
2067 N  N   B LYS   A 102 ? 0.3227 0.2391 0.1855 0.0420  -0.0014 0.0442  102  LYS   A N   
2068 C  CA  A LYS   A 102 ? 0.2647 0.3492 0.2316 -0.0605 0.0246  0.1050  102  LYS   A CA  
2069 C  CA  B LYS   A 102 ? 0.3325 0.2552 0.1942 0.0363  0.0139  0.0447  102  LYS   A CA  
2070 C  C   A LYS   A 102 ? 0.2767 0.3674 0.2227 -0.0485 0.0196  0.0892  102  LYS   A C   
2071 C  C   B LYS   A 102 ? 0.3258 0.2487 0.1737 0.0406  0.0031  0.0532  102  LYS   A C   
2072 O  O   A LYS   A 102 ? 0.2777 0.3763 0.2258 -0.0434 0.0255  0.0847  102  LYS   A O   
2073 O  O   B LYS   A 102 ? 0.3251 0.2456 0.1829 0.0429  0.0030  0.0577  102  LYS   A O   
2074 C  CB  A LYS   A 102 ? 0.2675 0.3538 0.2735 -0.0662 0.0186  0.0903  102  LYS   A CB  
2075 C  CB  B LYS   A 102 ? 0.3481 0.2784 0.2663 0.0277  0.0221  0.0233  102  LYS   A CB  
2076 C  CG  A LYS   A 102 ? 0.2728 0.3584 0.2981 -0.0688 0.0124  0.0795  102  LYS   A CG  
2077 C  CG  B LYS   A 102 ? 0.3621 0.3004 0.3251 0.0191  0.0256  0.0070  102  LYS   A CG  
2078 C  CD  A LYS   A 102 ? 0.2829 0.3640 0.3264 -0.0679 0.0074  0.0647  102  LYS   A CD  
2079 C  CD  B LYS   A 102 ? 0.3748 0.3220 0.3856 0.0105  0.0259  -0.0051 102  LYS   A CD  
2080 C  CE  A LYS   A 102 ? 0.2932 0.3678 0.3534 -0.0646 0.0055  0.0564  102  LYS   A CE  
2081 C  CE  B LYS   A 102 ? 0.3832 0.3364 0.4213 0.0029  0.0283  -0.0104 102  LYS   A CE  
2082 N  NZ  A LYS   A 102 ? 0.2991 0.3687 0.3644 -0.0641 0.0057  0.0516  102  LYS   A NZ  
2083 N  NZ  B LYS   A 102 ? 0.3865 0.3439 0.4438 -0.0013 0.0337  -0.0114 102  LYS   A NZ  
2110 N  N   A GLY   A 103 ? 0.2860 0.3772 0.2427 -0.0386 0.0083  0.0621  103  GLY   A N   
2111 N  N   B GLY   A 103 ? 0.3187 0.2506 0.1485 0.0404  -0.0139 0.0383  103  GLY   A N   
2112 C  CA  A GLY   A 103 ? 0.2964 0.3827 0.2425 -0.0291 0.0072  0.0470  103  GLY   A CA  
2113 C  CA  B GLY   A 103 ? 0.3102 0.2487 0.1577 0.0361  -0.0225 0.0431  103  GLY   A CA  
2114 C  C   A GLY   A 103 ? 0.3017 0.3882 0.2473 -0.0227 0.0117  0.0401  103  GLY   A C   
2115 C  C   B GLY   A 103 ? 0.2920 0.2409 0.1417 0.0289  -0.0200 0.0469  103  GLY   A C   
2116 O  O   A GLY   A 103 ? 0.3088 0.3911 0.2571 -0.0229 0.0122  0.0393  103  GLY   A O   
2117 O  O   B GLY   A 103 ? 0.3065 0.2461 0.1319 0.0277  -0.0269 0.0449  103  GLY   A O   
2124 N  N   A GLU   A 104 ? 0.2962 0.3878 0.2279 -0.0200 0.0213  0.0350  104  GLU   A N   
2125 N  N   B GLU   A 104 ? 0.2573 0.2285 0.1364 0.0218  -0.0194 0.0489  104  GLU   A N   
2126 C  CA  A GLU   A 104 ? 0.2879 0.3843 0.2102 -0.0225 0.0258  0.0320  104  GLU   A CA  
2127 C  CA  B GLU   A 104 ? 0.2246 0.2132 0.1167 0.0088  -0.0155 0.0419  104  GLU   A CA  
2128 C  C   A GLU   A 104 ? 0.2917 0.3908 0.2106 -0.0226 0.0195  0.0174  104  GLU   A C   
2129 C  C   B GLU   A 104 ? 0.2156 0.2040 0.1165 0.0126  -0.0130 0.0207  104  GLU   A C   
2130 O  O   A GLU   A 104 ? 0.2892 0.3946 0.2161 -0.0233 0.0069  0.0165  104  GLU   A O   
2131 O  O   B GLU   A 104 ? 0.2069 0.2024 0.1767 0.0116  -0.0089 0.0211  104  GLU   A O   
2132 C  CB  A GLU   A 104 ? 0.2720 0.3748 0.2008 -0.0270 0.0325  0.0458  104  GLU   A CB  
2133 C  CB  B GLU   A 104 ? 0.2036 0.2071 0.1179 -0.0089 -0.0101 0.0579  104  GLU   A CB  
2134 C  CG  A GLU   A 104 ? 0.2609 0.3659 0.1998 -0.0271 0.0366  0.0547  104  GLU   A CG  
2135 C  CG  B GLU   A 104 ? 0.1931 0.2120 0.1340 -0.0231 -0.0147 0.0579  104  GLU   A CG  
2136 C  CD  A GLU   A 104 ? 0.2520 0.3579 0.1988 -0.0235 0.0496  0.0629  104  GLU   A CD  
2137 C  CD  B GLU   A 104 ? 0.1855 0.2168 0.1390 -0.0297 -0.0177 0.0610  104  GLU   A CD  
2138 O  OE1 A GLU   A 104 ? 0.2428 0.3518 0.1761 -0.0245 0.0555  0.0685  104  GLU   A OE1 
2139 O  OE1 B GLU   A 104 ? 0.1735 0.2147 0.1466 -0.0339 -0.0214 0.0597  104  GLU   A OE1 
2140 O  OE2 A GLU   A 104 ? 0.2591 0.3583 0.2117 -0.0196 0.0524  0.0687  104  GLU   A OE2 
2141 O  OE2 B GLU   A 104 ? 0.1964 0.2245 0.1554 -0.0332 -0.0023 0.0615  104  GLU   A OE2 
2154 N  N   A ASP   A 105 ? 0.2973 0.3939 0.2196 -0.0194 0.0265  0.0021  105  ASP   A N   
2155 N  N   B ASP   A 105 ? 0.2340 0.1999 0.1238 0.0020  -0.0045 0.0178  105  ASP   A N   
2156 C  CA  A ASP   A 105 ? 0.2973 0.3971 0.2383 -0.0170 0.0301  -0.0144 105  ASP   A CA  
2157 C  CA  B ASP   A 105 ? 0.2437 0.1997 0.1582 0.0016  0.0059  -0.0115 105  ASP   A CA  
2158 C  C   A ASP   A 105 ? 0.2684 0.3886 0.2085 -0.0251 0.0240  -0.0312 105  ASP   A C   
2159 C  C   B ASP   A 105 ? 0.2226 0.1873 0.1426 -0.0057 0.0019  -0.0125 105  ASP   A C   
2160 O  O   A ASP   A 105 ? 0.2578 0.3890 0.1753 -0.0210 0.0251  -0.0481 105  ASP   A O   
2161 O  O   B ASP   A 105 ? 0.2038 0.1761 0.1128 -0.0030 -0.0062 -0.0180 105  ASP   A O   
2162 C  CB  A ASP   A 105 ? 0.3211 0.4085 0.2874 -0.0074 0.0342  -0.0123 105  ASP   A CB  
2163 C  CB  B ASP   A 105 ? 0.2705 0.2218 0.2190 0.0084  0.0171  -0.0334 105  ASP   A CB  
2164 C  CG  A ASP   A 105 ? 0.3394 0.4189 0.3296 0.0004  0.0317  -0.0105 105  ASP   A CG  
2165 C  CG  B ASP   A 105 ? 0.2915 0.2419 0.2684 0.0206  0.0153  -0.0571 105  ASP   A CG  
2166 O  OD1 A ASP   A 105 ? 0.3423 0.4228 0.3404 0.0042  0.0262  -0.0157 105  ASP   A OD1 
2167 O  OD1 B ASP   A 105 ? 0.2965 0.2446 0.2562 0.0138  0.0083  -0.0739 105  ASP   A OD1 
2168 O  OD2 A ASP   A 105 ? 0.3495 0.4237 0.3520 0.0012  0.0350  -0.0022 105  ASP   A OD2 
2169 O  OD2 B ASP   A 105 ? 0.3068 0.2574 0.3136 0.0269  0.0071  -0.0527 105  ASP   A OD2 
2178 N  N   A ILE   A 106 ? 0.2477 0.3764 0.2202 -0.0393 0.0061  -0.0347 106  ILE   A N   
2179 N  N   B ILE   A 106 ? 0.2206 0.1988 0.1608 -0.0083 -0.0086 0.0060  106  ILE   A N   
2180 C  CA  A ILE   A 106 ? 0.2196 0.3598 0.2280 -0.0540 -0.0063 -0.0474 106  ILE   A CA  
2181 C  CA  B ILE   A 106 ? 0.2139 0.2173 0.1701 -0.0183 -0.0170 0.0019  106  ILE   A CA  
2182 C  C   A ILE   A 106 ? 0.1970 0.3337 0.2245 -0.0758 -0.0069 -0.0779 106  ILE   A C   
2183 C  C   B ILE   A 106 ? 0.2061 0.2105 0.1566 -0.0217 -0.0186 0.0030  106  ILE   A C   
2184 O  O   A ILE   A 106 ? 0.1736 0.3243 0.2268 -0.0846 0.0072  -0.0795 106  ILE   A O   
2185 O  O   B ILE   A 106 ? 0.1943 0.2127 0.1729 -0.0156 -0.0100 0.0001  106  ILE   A O   
2186 C  CB  A ILE   A 106 ? 0.2187 0.3678 0.2569 -0.0416 -0.0179 -0.0219 106  ILE   A CB  
2187 C  CB  B ILE   A 106 ? 0.2229 0.2501 0.2322 -0.0212 -0.0283 0.0124  106  ILE   A CB  
2188 C  CG1 A ILE   A 106 ? 0.2043 0.3661 0.2742 -0.0297 -0.0236 -0.0020 106  ILE   A CG1 
2189 C  CG1 B ILE   A 106 ? 0.2212 0.2672 0.2703 -0.0121 -0.0330 0.0260  106  ILE   A CG1 
2190 C  CG2 A ILE   A 106 ? 0.2285 0.3724 0.2637 -0.0397 -0.0193 -0.0187 106  ILE   A CG2 
2191 C  CG2 B ILE   A 106 ? 0.2302 0.2572 0.2437 -0.0274 -0.0264 0.0118  106  ILE   A CG2 
2192 C  CD1 A ILE   A 106 ? 0.1964 0.3621 0.2823 -0.0184 -0.0150 0.0089  106  ILE   A CD1 
2193 C  CD1 B ILE   A 106 ? 0.2237 0.2718 0.2901 -0.0013 -0.0268 0.0341  106  ILE   A CD1 
2216 N  N   A GLN   A 107 ? 0.2108 0.3207 0.2454 -0.0771 0.0011  -0.0946 107  GLN   A N   
2217 N  N   B GLN   A 107 ? 0.2215 0.2010 0.1751 -0.0194 -0.0175 0.0074  107  GLN   A N   
2218 C  CA  A GLN   A 107 ? 0.2300 0.3068 0.2992 -0.0665 0.0156  -0.0888 107  GLN   A CA  
2219 C  CA  B GLN   A 107 ? 0.2429 0.2069 0.2290 -0.0228 -0.0038 0.0047  107  GLN   A CA  
2220 C  C   A GLN   A 107 ? 0.2030 0.2617 0.2749 -0.0540 0.0403  -0.0782 107  GLN   A C   
2221 C  C   B GLN   A 107 ? 0.2182 0.1767 0.2035 -0.0150 0.0146  0.0230  107  GLN   A C   
2222 O  O   A GLN   A 107 ? 0.2172 0.2662 0.3290 -0.0486 0.0534  -0.0746 107  GLN   A O   
2223 O  O   B GLN   A 107 ? 0.2245 0.1692 0.2076 -0.0144 0.0186  0.0185  107  GLN   A O   
2224 C  CB  A GLN   A 107 ? 0.2719 0.3367 0.3817 -0.0695 0.0104  -0.0811 107  GLN   A CB  
2225 C  CB  B GLN   A 107 ? 0.2865 0.2517 0.3127 -0.0337 -0.0119 -0.0029 107  GLN   A CB  
2226 C  CG  A GLN   A 107 ? 0.3114 0.3652 0.4653 -0.0678 0.0025  -0.0705 107  GLN   A CG  
2227 C  CG  B GLN   A 107 ? 0.3254 0.2911 0.3961 -0.0409 -0.0223 0.0022  107  GLN   A CG  
2228 C  CD  A GLN   A 107 ? 0.3441 0.3861 0.5325 -0.0664 -0.0039 -0.0597 107  GLN   A CD  
2229 C  CD  B GLN   A 107 ? 0.3608 0.3244 0.4699 -0.0449 -0.0291 0.0115  107  GLN   A CD  
2230 O  OE1 A GLN   A 107 ? 0.3566 0.3941 0.5602 -0.0673 -0.0056 -0.0570 107  GLN   A OE1 
2231 O  OE1 B GLN   A 107 ? 0.3730 0.3372 0.4887 -0.0479 -0.0293 0.0193  107  GLN   A OE1 
2232 N  NE2 A GLN   A 107 ? 0.3543 0.3921 0.5552 -0.0655 -0.0071 -0.0579 107  GLN   A NE2 
2233 N  NE2 B GLN   A 107 ? 0.3697 0.3348 0.4923 -0.0450 -0.0348 0.0130  107  GLN   A NE2 
2250 N  N   A LEU   A 108 ? 0.1666 0.2134 0.2097 -0.0451 0.0390  -0.0744 108  LEU   A N   
2251 N  N   B LEU   A 108 ? 0.1934 0.1666 0.1905 -0.0212 0.0248  0.0142  108  LEU   A N   
2252 C  CA  A LEU   A 108 ? 0.1538 0.1800 0.1929 -0.0158 0.0317  -0.0281 108  LEU   A CA  
2253 C  CA  B LEU   A 108 ? 0.1743 0.1554 0.1880 -0.0090 0.0279  0.0115  108  LEU   A CA  
2254 C  C   A LEU   A 108 ? 0.1438 0.1435 0.1745 -0.0049 0.0294  -0.0001 108  LEU   A C   
2255 C  C   B LEU   A 108 ? 0.1532 0.1300 0.1730 -0.0024 0.0296  0.0203  108  LEU   A C   
2256 O  O   A LEU   A 108 ? 0.1420 0.1453 0.1811 0.0020  0.0286  0.0046  108  LEU   A O   
2257 O  O   B LEU   A 108 ? 0.1507 0.1321 0.1809 0.0043  0.0343  0.0242  108  LEU   A O   
2258 C  CB  A LEU   A 108 ? 0.1550 0.1867 0.1716 -0.0105 0.0353  -0.0119 108  LEU   A CB  
2259 C  CB  B LEU   A 108 ? 0.1786 0.1725 0.1738 -0.0175 0.0374  0.0025  108  LEU   A CB  
2260 C  CG  A LEU   A 108 ? 0.1707 0.2016 0.1865 -0.0032 0.0403  -0.0037 108  LEU   A CG  
2261 C  CG  B LEU   A 108 ? 0.1910 0.1954 0.1943 -0.0217 0.0413  -0.0138 108  LEU   A CG  
2262 C  CD1 A LEU   A 108 ? 0.1828 0.2061 0.1865 -0.0062 0.0413  0.0073  108  LEU   A CD1 
2263 C  CD1 B LEU   A 108 ? 0.1982 0.2028 0.1984 -0.0277 0.0451  -0.0123 108  LEU   A CD1 
2264 C  CD2 A LEU   A 108 ? 0.1736 0.2078 0.2165 0.0054  0.0380  -0.0085 108  LEU   A CD2 
2265 C  CD2 B LEU   A 108 ? 0.1966 0.2060 0.2221 -0.0209 0.0349  -0.0228 108  LEU   A CD2 
2288 N  N   . LEU   A 109 ? 0.1384 0.1346 0.1711 0.0039  0.0245  0.0227  109  LEU   A N   
2289 C  CA  . LEU   A 109 ? 0.1350 0.1282 0.1539 0.0057  0.0112  0.0217  109  LEU   A CA  
2290 C  C   . LEU   A 109 ? 0.1250 0.1226 0.1541 -0.0059 0.0108  0.0160  109  LEU   A C   
2291 O  O   . LEU   A 109 ? 0.1287 0.1145 0.1726 -0.0045 -0.0010 0.0129  109  LEU   A O   
2292 C  CB  . LEU   A 109 ? 0.1409 0.1398 0.1787 0.0142  0.0110  0.0372  109  LEU   A CB  
2293 C  CG  . LEU   A 109 ? 0.1318 0.1450 0.1881 0.0144  0.0174  0.0409  109  LEU   A CG  
2294 C  CD1 . LEU   A 109 ? 0.1410 0.1363 0.2018 0.0083  0.0234  0.0253  109  LEU   A CD1 
2295 C  CD2 . LEU   A 109 ? 0.1322 0.1666 0.2055 0.0119  0.0159  0.0414  109  LEU   A CD2 
2308 N  N   . LYS   A 110 ? 0.1254 0.1227 0.1538 -0.0033 0.0039  0.0068  110  LYS   A N   
2309 C  CA  . LYS   A 110 ? 0.1235 0.1169 0.1690 -0.0058 0.0012  0.0124  110  LYS   A CA  
2310 C  C   . LYS   A 110 ? 0.1248 0.1076 0.1541 -0.0065 0.0075  0.0013  110  LYS   A C   
2311 O  O   . LYS   A 110 ? 0.1184 0.1144 0.1613 -0.0072 0.0088  -0.0000 110  LYS   A O   
2312 C  CB  . LYS   A 110 ? 0.1292 0.1240 0.1850 -0.0069 -0.0089 0.0052  110  LYS   A CB  
2313 C  CG  . LYS   A 110 ? 0.1269 0.1210 0.1910 -0.0029 -0.0038 0.0027  110  LYS   A CG  
2314 C  CD  . LYS   A 110 ? 0.1321 0.1247 0.2133 -0.0091 -0.0053 -0.0048 110  LYS   A CD  
2315 C  CE  . LYS   A 110 ? 0.1424 0.1263 0.2185 -0.0102 0.0164  -0.0058 110  LYS   A CE  
2316 N  NZ  . LYS   A 110 ? 0.1477 0.1320 0.2274 -0.0192 0.0181  0.0046  110  LYS   A NZ  
2330 N  N   . SER   A 111 ? 0.1254 0.1098 0.1540 -0.0030 0.0054  0.0088  111  SER   A N   
2331 C  CA  . SER   A 111 ? 0.1141 0.1188 0.1593 -0.0004 0.0054  0.0094  111  SER   A CA  
2332 C  C   . SER   A 111 ? 0.1120 0.1147 0.1572 -0.0051 0.0082  0.0067  111  SER   A C   
2333 O  O   . SER   A 111 ? 0.1236 0.1094 0.1710 -0.0019 0.0115  0.0120  111  SER   A O   
2334 C  CB  . SER   A 111 ? 0.1325 0.1426 0.1680 -0.0047 0.0155  -0.0087 111  SER   A CB  
2335 O  OG  . SER   A 111 ? 0.1777 0.1585 0.1758 0.0031  0.0263  -0.0096 111  SER   A OG  
2341 N  N   . ALA   A 112 ? 0.1189 0.1122 0.1573 -0.0008 0.0139  0.0117  112  ALA   A N   
2342 C  CA  . ALA   A 112 ? 0.1240 0.1075 0.1562 -0.0033 0.0165  0.0061  112  ALA   A CA  
2343 C  C   . ALA   A 112 ? 0.1172 0.1040 0.1561 0.0006  0.0091  0.0085  112  ALA   A C   
2344 O  O   . ALA   A 112 ? 0.1207 0.1069 0.1612 -0.0114 0.0153  0.0110  112  ALA   A O   
2345 C  CB  . ALA   A 112 ? 0.1283 0.1133 0.1542 -0.0032 0.0136  0.0065  112  ALA   A CB  
2351 N  N   . TYR   A 113 ? 0.1077 0.1068 0.1563 -0.0006 0.0080  0.0117  113  TYR   A N   
2352 C  CA  . TYR   A 113 ? 0.1123 0.1042 0.1529 -0.0038 0.0115  0.0172  113  TYR   A CA  
2353 C  C   . TYR   A 113 ? 0.1070 0.1051 0.1462 -0.0083 0.0099  0.0114  113  TYR   A C   
2354 O  O   . TYR   A 113 ? 0.1110 0.1123 0.1533 -0.0057 0.0114  0.0115  113  TYR   A O   
2355 C  CB  . TYR   A 113 ? 0.1103 0.1157 0.1579 -0.0042 0.0002  0.0239  113  TYR   A CB  
2356 C  CG  . TYR   A 113 ? 0.1122 0.1241 0.1446 -0.0108 0.0103  0.0266  113  TYR   A CG  
2357 C  CD1 . TYR   A 113 ? 0.1139 0.1362 0.1389 -0.0022 0.0084  0.0248  113  TYR   A CD1 
2358 C  CD2 . TYR   A 113 ? 0.1161 0.1311 0.1491 -0.0098 0.0068  0.0250  113  TYR   A CD2 
2359 C  CE1 . TYR   A 113 ? 0.1218 0.1444 0.1376 -0.0004 0.0095  0.0285  113  TYR   A CE1 
2360 C  CE2 . TYR   A 113 ? 0.1175 0.1405 0.1492 -0.0109 0.0102  0.0291  113  TYR   A CE2 
2361 C  CZ  . TYR   A 113 ? 0.1160 0.1469 0.1414 0.0041  0.0123  0.0344  113  TYR   A CZ  
2362 O  OH  . TYR   A 113 ? 0.1180 0.1623 0.1570 0.0156  0.0072  0.0324  113  TYR   A OH  
2372 N  N   . GLU   A 114 ? 0.1083 0.1061 0.1575 -0.0053 0.0119  0.0150  114  GLU   A N   
2373 C  CA  . GLU   A 114 ? 0.1145 0.0994 0.1686 0.0024  0.0063  0.0142  114  GLU   A CA  
2374 C  C   . GLU   A 114 ? 0.1096 0.1083 0.1588 -0.0019 0.0124  0.0135  114  GLU   A C   
2375 O  O   . GLU   A 114 ? 0.1206 0.1137 0.1517 -0.0001 -0.0000 0.0153  114  GLU   A O   
2376 C  CB  . GLU   A 114 ? 0.1119 0.1054 0.1672 -0.0036 0.0110  0.0148  114  GLU   A CB  
2377 C  CG  . GLU   A 114 ? 0.1188 0.1063 0.1725 -0.0003 0.0176  0.0052  114  GLU   A CG  
2378 C  CD  . GLU   A 114 ? 0.1269 0.1092 0.1796 -0.0037 0.0049  0.0079  114  GLU   A CD  
2379 O  OE1 . GLU   A 114 ? 0.1306 0.1133 0.1807 -0.0106 0.0128  -0.0018 114  GLU   A OE1 
2380 O  OE2 . GLU   A 114 ? 0.1447 0.1198 0.1954 -0.0127 0.0138  -0.0081 114  GLU   A OE2 
2387 N  N   . ASN   A 115 ? 0.1110 0.1124 0.1564 -0.0073 0.0108  0.0104  115  ASN   A N   
2388 C  CA  . ASN   A 115 ? 0.1125 0.1126 0.1595 -0.0104 0.0097  0.0165  115  ASN   A CA  
2389 C  C   . ASN   A 115 ? 0.1177 0.1080 0.1571 -0.0120 0.0022  0.0106  115  ASN   A C   
2390 O  O   . ASN   A 115 ? 0.1192 0.1189 0.1593 -0.0098 0.0093  0.0166  115  ASN   A O   
2391 C  CB  . ASN   A 115 ? 0.1238 0.1227 0.1475 -0.0113 0.0118  0.0128  115  ASN   A CB  
2392 C  CG  . ASN   A 115 ? 0.1219 0.1409 0.1582 -0.0150 0.0199  0.0194  115  ASN   A CG  
2393 O  OD1 . ASN   A 115 ? 0.1226 0.2403 0.1794 -0.0138 0.0263  0.0329  115  ASN   A OD1 
2394 N  ND2 . ASN   A 115 ? 0.1250 0.1206 0.1600 -0.0086 0.0236  0.0205  115  ASN   A ND2 
2401 N  N   . PHE   A 116 ? 0.1122 0.1114 0.1536 -0.0037 0.0081  0.0207  116  PHE   A N   
2402 C  CA  . PHE   A 116 ? 0.1116 0.1184 0.1407 -0.0016 0.0110  0.0173  116  PHE   A CA  
2403 C  C   . PHE   A 116 ? 0.1072 0.1249 0.1530 -0.0051 0.0126  0.0200  116  PHE   A C   
2404 O  O   . PHE   A 116 ? 0.1160 0.1287 0.1604 0.0023  0.0078  0.0277  116  PHE   A O   
2405 C  CB  . PHE   A 116 ? 0.1115 0.1115 0.1511 -0.0033 0.0152  0.0230  116  PHE   A CB  
2406 C  CG  . PHE   A 116 ? 0.1113 0.1179 0.1491 -0.0076 0.0075  0.0128  116  PHE   A CG  
2407 C  CD1 . PHE   A 116 ? 0.1122 0.1155 0.1486 -0.0087 0.0087  0.0115  116  PHE   A CD1 
2408 C  CD2 . PHE   A 116 ? 0.1172 0.1232 0.1606 -0.0056 0.0171  0.0175  116  PHE   A CD2 
2409 C  CE1 . PHE   A 116 ? 0.1181 0.1173 0.1608 -0.0148 0.0023  0.0094  116  PHE   A CE1 
2410 C  CE2 . PHE   A 116 ? 0.1151 0.1197 0.1689 -0.0027 0.0117  0.0107  116  PHE   A CE2 
2411 C  CZ  . PHE   A 116 ? 0.1213 0.1060 0.1514 -0.0032 0.0003  0.0132  116  PHE   A CZ  
2421 N  N   . ASN   A 117 ? 0.1125 0.1155 0.1665 -0.0022 0.0125  0.0250  117  ASN   A N   
2422 C  CA  . ASN   A 117 ? 0.1127 0.1159 0.1732 -0.0007 0.0141  0.0276  117  ASN   A CA  
2423 C  C   . ASN   A 117 ? 0.1140 0.1237 0.1865 -0.0008 0.0120  0.0243  117  ASN   A C   
2424 O  O   . ASN   A 117 ? 0.1269 0.1275 0.1977 -0.0043 -0.0067 0.0392  117  ASN   A O   
2425 C  CB  . ASN   A 117 ? 0.1155 0.1208 0.1673 0.0001  0.0139  0.0294  117  ASN   A CB  
2426 C  CG  . ASN   A 117 ? 0.1141 0.1193 0.1742 -0.0014 0.0095  0.0284  117  ASN   A CG  
2427 O  OD1 . ASN   A 117 ? 0.1172 0.1392 0.1841 -0.0119 0.0126  0.0215  117  ASN   A OD1 
2428 N  ND2 . ASN   A 117 ? 0.1110 0.1184 0.1859 -0.0041 0.0067  0.0273  117  ASN   A ND2 
2435 N  N   . GLN   A 118 ? 0.1110 0.1247 0.1839 -0.0037 0.0030  0.0320  118  GLN   A N   
2436 C  CA  . GLN   A 118 ? 0.1193 0.1378 0.1898 -0.0073 -0.0025 0.0203  118  GLN   A CA  
2437 C  C   . GLN   A 118 ? 0.1224 0.1469 0.1726 -0.0075 -0.0073 0.0292  118  GLN   A C   
2438 O  O   . GLN   A 118 ? 0.1217 0.1738 0.1905 -0.0014 -0.0188 0.0072  118  GLN   A O   
2439 C  CB  . GLN   A 118 ? 0.1181 0.1372 0.2017 -0.0042 0.0100  0.0244  118  GLN   A CB  
2440 C  CG  . GLN   A 118 ? 0.1163 0.1428 0.1984 -0.0010 0.0124  0.0301  118  GLN   A CG  
2441 C  CD  . GLN   A 118 ? 0.1137 0.1417 0.2158 0.0048  0.0086  0.0259  118  GLN   A CD  
2442 O  OE1 . GLN   A 118 ? 0.1161 0.1586 0.2257 0.0132  0.0003  0.0190  118  GLN   A OE1 
2443 N  NE2 . GLN   A 118 ? 0.1234 0.1359 0.2178 0.0051  0.0033  0.0269  118  GLN   A NE2 
2452 N  N   . HIS   A 119 ? 0.1288 0.1418 0.1636 -0.0033 -0.0051 0.0349  119  HIS   A N   
2453 C  CA  . HIS   A 119 ? 0.1297 0.1456 0.1733 -0.0076 -0.0038 0.0338  119  HIS   A CA  
2454 C  C   . HIS   A 119 ? 0.1385 0.1506 0.1636 -0.0073 0.0026  0.0356  119  HIS   A C   
2455 O  O   . HIS   A 119 ? 0.1384 0.1589 0.1637 -0.0210 0.0019  0.0350  119  HIS   A O   
2456 C  CB  . HIS   A 119 ? 0.1378 0.1399 0.1876 -0.0039 0.0128  0.0373  119  HIS   A CB  
2457 C  CG  . HIS   A 119 ? 0.1368 0.1430 0.2295 0.0020  0.0144  0.0442  119  HIS   A CG  
2458 N  ND1 . HIS   A 119 ? 0.1486 0.1629 0.2949 -0.0099 0.0048  0.0287  119  HIS   A ND1 
2459 C  CD2 . HIS   A 119 ? 0.1459 0.1555 0.2523 0.0164  0.0333  0.0685  119  HIS   A CD2 
2460 C  CE1 . HIS   A 119 ? 0.1449 0.1610 0.3116 -0.0082 0.0208  0.0525  119  HIS   A CE1 
2461 N  NE2 . HIS   A 119 ? 0.1545 0.1594 0.2992 0.0066  0.0412  0.0739  119  HIS   A NE2 
2469 N  N   . GLU   A 120 ? 0.1415 0.1733 0.1587 -0.0044 -0.0070 0.0596  120  GLU   A N   
2470 C  CA  . GLU   A 120 ? 0.1645 0.2047 0.1945 0.0076  -0.0126 0.0942  120  GLU   A CA  
2471 C  C   . GLU   A 120 ? 0.1485 0.1888 0.1706 -0.0047 -0.0096 0.0830  120  GLU   A C   
2472 O  O   . GLU   A 120 ? 0.1454 0.1808 0.1755 -0.0134 -0.0092 0.0760  120  GLU   A O   
2473 C  CB  . GLU   A 120 ? 0.2304 0.2766 0.2368 0.0282  -0.0079 0.1437  120  GLU   A CB  
2474 C  CG  . GLU   A 120 ? 0.3241 0.3526 0.3446 0.0432  -0.0094 0.1586  120  GLU   A CG  
2475 C  CD  . GLU   A 120 ? 0.4270 0.4337 0.4685 0.0516  0.0053  0.1456  120  GLU   A CD  
2476 O  OE1 . GLU   A 120 ? 0.4441 0.4434 0.4917 0.0514  0.0104  0.1412  120  GLU   A OE1 
2477 O  OE2 . GLU   A 120 ? 0.4761 0.4799 0.5228 0.0544  0.0119  0.1403  120  GLU   A OE2 
2484 N  N   . VAL   A 121 ? 0.1455 0.1855 0.1514 -0.0081 -0.0048 0.0630  121  VAL   A N   
2485 C  CA  . VAL   A 121 ? 0.1523 0.1923 0.1386 -0.0099 0.0047  0.0624  121  VAL   A CA  
2486 C  C   . VAL   A 121 ? 0.1416 0.1723 0.1318 -0.0190 -0.0007 0.0469  121  VAL   A C   
2487 O  O   . VAL   A 121 ? 0.1421 0.1751 0.1476 -0.0234 -0.0105 0.0394  121  VAL   A O   
2488 C  CB  . VAL   A 121 ? 0.1918 0.2340 0.1813 0.0031  0.0191  0.0756  121  VAL   A CB  
2489 C  CG1 . VAL   A 121 ? 0.1957 0.2475 0.1795 0.0174  0.0295  0.0803  121  VAL   A CG1 
2490 C  CG2 . VAL   A 121 ? 0.2120 0.2517 0.2208 -0.0066 0.0193  0.0644  121  VAL   A CG2 
2500 N  N   . LEU   A 122 ? 0.1285 0.1494 0.1360 -0.0168 0.0019  0.0434  122  LEU   A N   
2501 C  CA  . LEU   A 122 ? 0.1363 0.1387 0.1302 -0.0180 0.0098  0.0334  122  LEU   A CA  
2502 C  C   . LEU   A 122 ? 0.1319 0.1401 0.1131 -0.0214 0.0000  0.0304  122  LEU   A C   
2503 O  O   . LEU   A 122 ? 0.1311 0.1511 0.1489 -0.0236 -0.0017 0.0286  122  LEU   A O   
2504 C  CB  . LEU   A 122 ? 0.1512 0.1417 0.1635 -0.0017 0.0034  0.0412  122  LEU   A CB  
2505 C  CG  . LEU   A 122 ? 0.1548 0.1468 0.1556 -0.0046 0.0141  0.0317  122  LEU   A CG  
2506 C  CD1 . LEU   A 122 ? 0.1684 0.1488 0.1674 -0.0102 0.0196  0.0353  122  LEU   A CD1 
2507 C  CD2 . LEU   A 122 ? 0.1487 0.1420 0.1541 -0.0010 0.0230  0.0248  122  LEU   A CD2 
2519 N  N   . LEU   A 123 ? 0.1233 0.1409 0.1217 -0.0206 -0.0047 0.0284  123  LEU   A N   
2520 C  CA  . LEU   A 123 ? 0.1236 0.1377 0.1196 -0.0159 -0.0026 0.0239  123  LEU   A CA  
2521 C  C   . LEU   A 123 ? 0.1189 0.1341 0.1125 -0.0171 -0.0020 0.0254  123  LEU   A C   
2522 O  O   . LEU   A 123 ? 0.1179 0.1456 0.1288 -0.0242 -0.0006 0.0254  123  LEU   A O   
2523 C  CB  . LEU   A 123 ? 0.1314 0.1458 0.1178 -0.0192 0.0037  0.0288  123  LEU   A CB  
2524 C  CG  . LEU   A 123 ? 0.1377 0.1593 0.1325 -0.0114 0.0003  0.0127  123  LEU   A CG  
2525 C  CD1 . LEU   A 123 ? 0.1414 0.1723 0.1339 -0.0033 0.0049  0.0058  123  LEU   A CD1 
2526 C  CD2 . LEU   A 123 ? 0.1479 0.1640 0.1455 -0.0083 -0.0069 0.0064  123  LEU   A CD2 
2538 N  N   . ALA   A 124 ? 0.1171 0.1252 0.1098 -0.0163 0.0063  0.0248  124  ALA   A N   
2539 C  CA  . ALA   A 124 ? 0.1157 0.1247 0.1154 -0.0096 0.0017  0.0213  124  ALA   A CA  
2540 C  C   . ALA   A 124 ? 0.1109 0.1213 0.1174 -0.0102 0.0053  0.0230  124  ALA   A C   
2541 O  O   . ALA   A 124 ? 0.1110 0.1335 0.1350 -0.0106 0.0058  0.0280  124  ALA   A O   
2542 C  CB  . ALA   A 124 ? 0.1174 0.1246 0.1402 -0.0015 0.0049  0.0274  124  ALA   A CB  
2548 N  N   A PRO   A 125 ? 0.1066 0.1317 0.1221 -0.0030 0.0057  0.0247  125  PRO   A N   
2549 N  N   B PRO   A 125 ? 0.1086 0.1175 0.1116 -0.0093 0.0022  0.0274  125  PRO   A N   
2550 C  CA  A PRO   A 125 ? 0.1079 0.1285 0.1263 -0.0004 0.0037  0.0151  125  PRO   A CA  
2551 C  CA  B PRO   A 125 ? 0.1166 0.1205 0.1168 -0.0091 0.0022  0.0198  125  PRO   A CA  
2552 C  C   A PRO   A 125 ? 0.1013 0.1207 0.1178 0.0006  0.0007  0.0169  125  PRO   A C   
2553 C  C   B PRO   A 125 ? 0.1144 0.1270 0.1180 -0.0066 0.0006  0.0233  125  PRO   A C   
2554 O  O   A PRO   A 125 ? 0.1053 0.1221 0.1192 0.0079  0.0012  0.0080  125  PRO   A O   
2555 O  O   B PRO   A 125 ? 0.1214 0.1267 0.1334 -0.0079 0.0064  0.0225  125  PRO   A O   
2556 C  CB  A PRO   A 125 ? 0.1200 0.1290 0.1201 -0.0066 0.0001  0.0101  125  PRO   A CB  
2557 C  CB  B PRO   A 125 ? 0.1235 0.1160 0.1056 -0.0140 0.0026  0.0157  125  PRO   A CB  
2558 C  CG  A PRO   A 125 ? 0.1191 0.1351 0.1296 -0.0090 0.0028  0.0185  125  PRO   A CG  
2559 C  CG  B PRO   A 125 ? 0.1193 0.1134 0.1148 -0.0159 -0.0019 0.0197  125  PRO   A CG  
2560 C  CD  A PRO   A 125 ? 0.1101 0.1400 0.1302 -0.0085 0.0121  0.0186  125  PRO   A CD  
2561 C  CD  B PRO   A 125 ? 0.1052 0.1063 0.1087 -0.0173 0.0012  0.0193  125  PRO   A CD  
2576 N  N   A LEU   A 126 ? 0.0961 0.1243 0.1183 0.0007  0.0076  0.0162  126  LEU   A N   
2577 N  N   B LEU   A 126 ? 0.1119 0.1308 0.1227 -0.0043 -0.0028 0.0171  126  LEU   A N   
2578 C  CA  A LEU   A 126 ? 0.1103 0.1285 0.1359 -0.0011 0.0045  0.0112  126  LEU   A CA  
2579 C  CA  B LEU   A 126 ? 0.1138 0.1312 0.1225 -0.0047 0.0057  0.0172  126  LEU   A CA  
2580 C  C   A LEU   A 126 ? 0.1211 0.1284 0.1273 0.0061  -0.0077 0.0150  126  LEU   A C   
2581 C  C   B LEU   A 126 ? 0.1147 0.1258 0.1212 0.0006  0.0182  0.0086  126  LEU   A C   
2582 O  O   A LEU   A 126 ? 0.1329 0.1326 0.1534 0.0144  0.0053  0.0186  126  LEU   A O   
2583 O  O   B LEU   A 126 ? 0.1271 0.1321 0.1511 0.0021  0.0289  0.0251  126  LEU   A O   
2584 C  CB  A LEU   A 126 ? 0.1146 0.1261 0.1427 -0.0050 -0.0105 0.0155  126  LEU   A CB  
2585 C  CB  B LEU   A 126 ? 0.1187 0.1377 0.1380 -0.0096 0.0014  0.0138  126  LEU   A CB  
2586 C  CG  A LEU   A 126 ? 0.1107 0.1324 0.1676 0.0050  0.0021  0.0172  126  LEU   A CG  
2587 C  CG  B LEU   A 126 ? 0.1144 0.1378 0.1438 -0.0077 0.0074  0.0079  126  LEU   A CG  
2588 C  CD1 A LEU   A 126 ? 0.1134 0.1416 0.1879 0.0039  0.0040  0.0344  126  LEU   A CD1 
2589 C  CD1 B LEU   A 126 ? 0.1189 0.1406 0.1808 -0.0113 -0.0015 0.0082  126  LEU   A CD1 
2590 C  CD2 A LEU   A 126 ? 0.1194 0.1297 0.1628 0.0023  0.0052  0.0114  126  LEU   A CD2 
2591 C  CD2 B LEU   A 126 ? 0.1186 0.1407 0.1473 -0.0066 0.0095  0.0067  126  LEU   A CD2 
2614 N  N   A LEU   A 127 ? 0.1281 0.1325 0.1285 0.0015  -0.0060 0.0133  127  LEU   A N   
2615 N  N   B LEU   A 127 ? 0.1079 0.1205 0.1103 0.0024  0.0151  0.0121  127  LEU   A N   
2616 C  CA  A LEU   A 127 ? 0.1248 0.1268 0.1216 -0.0040 -0.0024 0.0187  127  LEU   A CA  
2617 C  CA  B LEU   A 127 ? 0.1075 0.1218 0.1179 0.0011  0.0135  0.0169  127  LEU   A CA  
2618 C  C   A LEU   A 127 ? 0.1218 0.1213 0.1118 -0.0008 -0.0075 0.0252  127  LEU   A C   
2619 C  C   B LEU   A 127 ? 0.1096 0.1206 0.1282 0.0015  0.0116  0.0038  127  LEU   A C   
2620 O  O   A LEU   A 127 ? 0.1284 0.1213 0.1098 -0.0052 -0.0174 0.0253  127  LEU   A O   
2621 O  O   B LEU   A 127 ? 0.1190 0.1248 0.1343 -0.0112 0.0266  0.0077  127  LEU   A O   
2622 C  CB  A LEU   A 127 ? 0.1218 0.1224 0.1139 0.0010  0.0048  0.0208  127  LEU   A CB  
2623 C  CB  B LEU   A 127 ? 0.1106 0.1408 0.1243 0.0040  0.0089  0.0224  127  LEU   A CB  
2624 C  CG  A LEU   A 127 ? 0.1224 0.1152 0.1254 -0.0010 -0.0063 0.0164  127  LEU   A CG  
2625 C  CG  B LEU   A 127 ? 0.1223 0.1633 0.1381 0.0014  0.0019  0.0323  127  LEU   A CG  
2626 C  CD1 A LEU   A 127 ? 0.1267 0.1056 0.1456 -0.0024 -0.0061 0.0071  127  LEU   A CD1 
2627 C  CD1 B LEU   A 127 ? 0.1255 0.1752 0.1741 0.0073  0.0017  0.0311  127  LEU   A CD1 
2628 C  CD2 A LEU   A 127 ? 0.1348 0.1192 0.1511 0.0035  -0.0127 0.0215  127  LEU   A CD2 
2629 C  CD2 B LEU   A 127 ? 0.1325 0.1737 0.1377 -0.0066 -0.0192 0.0149  127  LEU   A CD2 
2652 N  N   A SER   A 128 ? 0.1247 0.1219 0.1021 -0.0051 0.0025  0.0273  128  SER   A N   
2653 N  N   B SER   A 128 ? 0.1125 0.1223 0.1393 -0.0046 -0.0033 0.0020  128  SER   A N   
2654 C  CA  A SER   A 128 ? 0.1352 0.1221 0.1022 0.0022  0.0057  0.0228  128  SER   A CA  
2655 C  CA  B SER   A 128 ? 0.1208 0.1215 0.1338 -0.0042 -0.0106 -0.0000 128  SER   A CA  
2656 C  C   A SER   A 128 ? 0.1369 0.1251 0.1114 0.0083  0.0107  0.0196  128  SER   A C   
2657 C  C   B SER   A 128 ? 0.1278 0.1232 0.1337 -0.0004 -0.0216 0.0108  128  SER   A C   
2658 O  O   A SER   A 128 ? 0.1435 0.1440 0.1141 0.0083  0.0223  0.0215  128  SER   A O   
2659 O  O   B SER   A 128 ? 0.1295 0.1329 0.1299 0.0032  -0.0181 0.0157  128  SER   A O   
2660 C  CB  A SER   A 128 ? 0.1353 0.1225 0.1009 0.0015  0.0063  0.0297  128  SER   A CB  
2661 C  CB  B SER   A 128 ? 0.1226 0.1255 0.1371 -0.0011 -0.0094 0.0028  128  SER   A CB  
2662 O  OG  A SER   A 128 ? 0.1376 0.1333 0.1062 0.0003  0.0056  0.0183  128  SER   A OG  
2663 O  OG  B SER   A 128 ? 0.1192 0.1330 0.1497 0.0020  0.0028  0.0131  128  SER   A OG  
2674 N  N   A ALA   A 129 ? 0.1345 0.1260 0.1150 0.0043  0.0041  0.0125  129  ALA   A N   
2675 N  N   B ALA   A 129 ? 0.1293 0.1264 0.1394 0.0035  -0.0244 0.0175  129  ALA   A N   
2676 C  CA  A ALA   A 129 ? 0.1248 0.1310 0.1108 0.0097  0.0033  0.0126  129  ALA   A CA  
2677 C  CA  B ALA   A 129 ? 0.1265 0.1341 0.1428 0.0019  -0.0197 0.0083  129  ALA   A CA  
2678 C  C   A ALA   A 129 ? 0.1257 0.1232 0.0927 0.0055  0.0015  -0.0003 129  ALA   A C   
2679 C  C   B ALA   A 129 ? 0.1362 0.1411 0.1257 0.0003  -0.0139 0.0110  129  ALA   A C   
2680 O  O   A ALA   A 129 ? 0.1346 0.1308 0.0980 -0.0020 0.0083  0.0118  129  ALA   A O   
2681 O  O   B ALA   A 129 ? 0.1403 0.1460 0.1225 -0.0027 -0.0090 0.0052  129  ALA   A O   
2682 C  CB  A ALA   A 129 ? 0.1280 0.1413 0.1236 0.0090  0.0099  0.0204  129  ALA   A CB  
2683 C  CB  B ALA   A 129 ? 0.1247 0.1422 0.1662 0.0007  -0.0241 0.0060  129  ALA   A CB  
2694 N  N   A GLY   A 130 ? 0.1277 0.1232 0.1136 0.0032  0.0091  -0.0038 130  GLY   A N   
2695 N  N   B GLY   A 130 ? 0.1454 0.1455 0.1247 0.0021  -0.0088 0.0099  130  GLY   A N   
2696 C  CA  A GLY   A 130 ? 0.1501 0.1285 0.1196 0.0055  0.0155  -0.0067 130  GLY   A CA  
2697 C  CA  B GLY   A 130 ? 0.1599 0.1470 0.1431 0.0038  0.0006  0.0063  130  GLY   A CA  
2698 C  C   A GLY   A 130 ? 0.1513 0.1315 0.1103 0.0095  0.0079  0.0046  130  GLY   A C   
2699 C  C   B GLY   A 130 ? 0.1588 0.1480 0.1427 0.0070  -0.0149 0.0170  130  GLY   A C   
2700 O  O   A GLY   A 130 ? 0.1470 0.1276 0.1114 0.0029  -0.0033 0.0087  130  GLY   A O   
2701 O  O   B GLY   A 130 ? 0.1615 0.1512 0.1511 0.0079  -0.0075 0.0264  130  GLY   A O   
2708 N  N   A ILE   A 131 ? 0.1581 0.1300 0.1241 0.0034  0.0060  0.0062  131  ILE   A N   
2709 N  N   B ILE   A 131 ? 0.1577 0.1398 0.1581 0.0008  -0.0195 0.0223  131  ILE   A N   
2710 C  CA  A ILE   A 131 ? 0.1629 0.1307 0.1240 0.0020  -0.0080 0.0045  131  ILE   A CA  
2711 C  CA  B ILE   A 131 ? 0.1562 0.1335 0.1497 0.0044  -0.0276 0.0206  131  ILE   A CA  
2712 C  C   A ILE   A 131 ? 0.1536 0.1369 0.1273 0.0040  0.0015  0.0170  131  ILE   A C   
2713 C  C   B ILE   A 131 ? 0.1613 0.1370 0.1355 0.0100  -0.0282 0.0233  131  ILE   A C   
2714 O  O   A ILE   A 131 ? 0.1509 0.1419 0.1422 0.0053  0.0005  0.0214  131  ILE   A O   
2715 O  O   B ILE   A 131 ? 0.1795 0.1387 0.1433 0.0070  -0.0208 0.0185  131  ILE   A O   
2716 C  CB  A ILE   A 131 ? 0.1695 0.1384 0.1453 -0.0004 -0.0182 -0.0083 131  ILE   A CB  
2717 C  CB  B ILE   A 131 ? 0.1581 0.1431 0.1654 0.0059  -0.0348 0.0178  131  ILE   A CB  
2718 C  CG1 A ILE   A 131 ? 0.1765 0.1548 0.1587 -0.0054 -0.0299 -0.0127 131  ILE   A CG1 
2719 C  CG1 B ILE   A 131 ? 0.1644 0.1590 0.1788 0.0075  -0.0358 0.0152  131  ILE   A CG1 
2720 C  CG2 A ILE   A 131 ? 0.1703 0.1337 0.1545 0.0055  -0.0151 -0.0175 131  ILE   A CG2 
2721 C  CG2 B ILE   A 131 ? 0.1576 0.1411 0.1687 0.0047  -0.0284 0.0086  131  ILE   A CG2 
2722 C  CD1 A ILE   A 131 ? 0.1810 0.1597 0.1893 -0.0020 -0.0356 -0.0104 131  ILE   A CD1 
2723 C  CD1 B ILE   A 131 ? 0.1726 0.1683 0.2000 0.0023  -0.0439 0.0176  131  ILE   A CD1 
2746 N  N   A PHE   A 132 ? 0.1496 0.1366 0.1305 0.0049  0.0062  0.0182  132  PHE   A N   
2747 N  N   B PHE   A 132 ? 0.1557 0.1356 0.1367 0.0175  -0.0279 0.0149  132  PHE   A N   
2748 C  CA  A PHE   A 132 ? 0.1525 0.1445 0.1262 0.0011  0.0017  0.0111  132  PHE   A CA  
2749 C  CA  B PHE   A 132 ? 0.1559 0.1355 0.1393 0.0132  -0.0208 0.0101  132  PHE   A CA  
2750 C  C   A PHE   A 132 ? 0.1515 0.1608 0.1177 -0.0013 0.0016  0.0118  132  PHE   A C   
2751 C  C   B PHE   A 132 ? 0.1654 0.1520 0.1451 0.0207  -0.0209 0.0173  132  PHE   A C   
2752 O  O   A PHE   A 132 ? 0.1587 0.1736 0.1315 -0.0027 0.0009  0.0068  132  PHE   A O   
2753 O  O   B PHE   A 132 ? 0.1806 0.1667 0.1648 0.0185  -0.0131 0.0137  132  PHE   A O   
2754 C  CB  A PHE   A 132 ? 0.1550 0.1429 0.1321 -0.0012 -0.0041 0.0115  132  PHE   A CB  
2755 C  CB  B PHE   A 132 ? 0.1501 0.1280 0.1304 0.0045  -0.0144 0.0184  132  PHE   A CB  
2756 C  CG  A PHE   A 132 ? 0.1573 0.1447 0.1280 -0.0007 -0.0084 0.0151  132  PHE   A CG  
2757 C  CG  B PHE   A 132 ? 0.1498 0.1214 0.1201 0.0091  -0.0221 0.0169  132  PHE   A CG  
2758 C  CD1 A PHE   A 132 ? 0.1647 0.1542 0.1501 0.0015  -0.0103 0.0052  132  PHE   A CD1 
2759 C  CD1 B PHE   A 132 ? 0.1534 0.1323 0.1485 0.0153  -0.0174 -0.0008 132  PHE   A CD1 
2760 C  CD2 A PHE   A 132 ? 0.1555 0.1530 0.1469 -0.0068 -0.0041 0.0091  132  PHE   A CD2 
2761 C  CD2 B PHE   A 132 ? 0.1481 0.1323 0.1378 0.0110  -0.0285 -0.0055 132  PHE   A CD2 
2762 C  CE1 A PHE   A 132 ? 0.1683 0.1598 0.1536 -0.0010 -0.0166 0.0041  132  PHE   A CE1 
2763 C  CE1 B PHE   A 132 ? 0.1540 0.1396 0.1496 0.0171  -0.0284 -0.0061 132  PHE   A CE1 
2764 C  CE2 A PHE   A 132 ? 0.1589 0.1586 0.1628 -0.0049 -0.0119 0.0024  132  PHE   A CE2 
2765 C  CE2 B PHE   A 132 ? 0.1457 0.1418 0.1517 0.0177  -0.0361 -0.0128 132  PHE   A CE2 
2766 C  CZ  A PHE   A 132 ? 0.1655 0.1623 0.1641 -0.0029 -0.0206 0.0025  132  PHE   A CZ  
2767 C  CZ  B PHE   A 132 ? 0.1492 0.1430 0.1553 0.0164  -0.0400 -0.0107 132  PHE   A CZ  
2786 N  N   A GLY   A 133 ? 0.1491 0.1636 0.1261 -0.0028 -0.0050 0.0167  133  GLY   A N   
2787 N  N   B GLY   A 133 ? 0.1662 0.1522 0.1340 0.0184  -0.0216 0.0242  133  GLY   A N   
2788 C  CA  A GLY   A 133 ? 0.1573 0.1740 0.1351 -0.0056 -0.0213 0.0091  133  GLY   A CA  
2789 C  CA  B GLY   A 133 ? 0.1685 0.1556 0.1324 0.0118  -0.0276 0.0138  133  GLY   A CA  
2790 C  C   A GLY   A 133 ? 0.1635 0.1857 0.1363 -0.0097 -0.0319 0.0037  133  GLY   A C   
2791 C  C   B GLY   A 133 ? 0.1675 0.1649 0.1379 0.0128  -0.0418 0.0015  133  GLY   A C   
2792 O  O   A GLY   A 133 ? 0.1731 0.1950 0.1487 -0.0067 -0.0279 -0.0134 133  GLY   A O   
2793 O  O   B GLY   A 133 ? 0.1681 0.1739 0.1391 0.0213  -0.0457 -0.0099 133  GLY   A O   
2800 N  N   A ALA   A 134 ? 0.1624 0.1797 0.1284 -0.0174 -0.0244 0.0103  134  ALA   A N   
2801 N  N   B ALA   A 134 ? 0.1673 0.1555 0.1383 0.0063  -0.0303 -0.0008 134  ALA   A N   
2802 C  CA  A ALA   A 134 ? 0.1619 0.1840 0.1410 -0.0155 -0.0227 0.0045  134  ALA   A CA  
2803 C  CA  B ALA   A 134 ? 0.1652 0.1528 0.1548 0.0064  -0.0266 -0.0055 134  ALA   A CA  
2804 C  C   A ALA   A 134 ? 0.1635 0.1870 0.1424 -0.0177 -0.0233 0.0084  134  ALA   A C   
2805 C  C   B ALA   A 134 ? 0.1648 0.1470 0.1529 0.0039  -0.0190 0.0035  134  ALA   A C   
2806 O  O   A ALA   A 134 ? 0.1720 0.1948 0.1642 -0.0218 -0.0136 0.0031  134  ALA   A O   
2807 O  O   B ALA   A 134 ? 0.1650 0.1470 0.1769 0.0014  0.0015  0.0072  134  ALA   A O   
2808 C  CB  A ALA   A 134 ? 0.1684 0.1838 0.1647 -0.0113 -0.0214 0.0014  134  ALA   A CB  
2809 C  CB  B ALA   A 134 ? 0.1705 0.1532 0.1953 0.0084  -0.0264 -0.0100 134  ALA   A CB  
2820 N  N   A ASP   A 135 ? 0.1654 0.1856 0.1570 -0.0146 -0.0198 0.0150  135  ASP   A N   
2821 N  N   B ASP   A 135 ? 0.1747 0.1562 0.1598 -0.0060 -0.0200 0.0108  135  ASP   A N   
2822 C  CA  A ASP   A 135 ? 0.1642 0.1855 0.1706 -0.0159 -0.0296 0.0193  135  ASP   A CA  
2823 C  CA  B ASP   A 135 ? 0.1741 0.1611 0.1851 -0.0130 -0.0293 0.0090  135  ASP   A CA  
2824 C  C   A ASP   A 135 ? 0.1524 0.1737 0.1726 -0.0074 -0.0232 0.0347  135  ASP   A C   
2825 C  C   B ASP   A 135 ? 0.1583 0.1497 0.1826 -0.0073 -0.0225 0.0099  135  ASP   A C   
2826 O  O   A ASP   A 135 ? 0.1475 0.1725 0.1829 -0.0031 -0.0275 0.0408  135  ASP   A O   
2827 O  O   B ASP   A 135 ? 0.1539 0.1401 0.1871 -0.0094 -0.0130 0.0128  135  ASP   A O   
2828 C  CB  A ASP   A 135 ? 0.1843 0.2029 0.1992 -0.0282 -0.0387 0.0097  135  ASP   A CB  
2829 C  CB  B ASP   A 135 ? 0.1921 0.1823 0.2047 -0.0215 -0.0405 -0.0001 135  ASP   A CB  
2830 C  CG  A ASP   A 135 ? 0.2012 0.2176 0.2342 -0.0443 -0.0424 -0.0013 135  ASP   A CG  
2831 C  CG  B ASP   A 135 ? 0.2081 0.2054 0.2386 -0.0226 -0.0459 -0.0013 135  ASP   A CG  
2832 O  OD1 A ASP   A 135 ? 0.1976 0.2225 0.2347 -0.0535 -0.0580 0.0038  135  ASP   A OD1 
2833 O  OD1 B ASP   A 135 ? 0.2102 0.2078 0.2500 -0.0158 -0.0515 0.0002  135  ASP   A OD1 
2834 O  OD2 A ASP   A 135 ? 0.2240 0.2281 0.2723 -0.0473 -0.0175 -0.0068 135  ASP   A OD2 
2835 O  OD2 B ASP   A 135 ? 0.2200 0.2228 0.2736 -0.0261 -0.0447 -0.0008 135  ASP   A OD2 
2844 N  N   A PRO   A 136 ? 0.1445 0.1624 0.1739 -0.0054 -0.0123 0.0368  136  PRO   A N   
2845 N  N   B PRO   A 136 ? 0.1461 0.1469 0.1783 0.0022  -0.0182 0.0096  136  PRO   A N   
2846 C  CA  A PRO   A 136 ? 0.1376 0.1570 0.1758 -0.0101 -0.0059 0.0272  136  PRO   A CA  
2847 C  CA  B PRO   A 136 ? 0.1424 0.1499 0.1832 0.0005  -0.0081 -0.0003 136  PRO   A CA  
2848 C  C   A PRO   A 136 ? 0.1200 0.1516 0.1729 -0.0044 -0.0039 0.0224  136  PRO   A C   
2849 C  C   B PRO   A 136 ? 0.1269 0.1486 0.1819 0.0010  -0.0013 -0.0001 136  PRO   A C   
2850 O  O   A PRO   A 136 ? 0.1173 0.1599 0.1662 -0.0074 -0.0081 0.0263  136  PRO   A O   
2851 O  O   B PRO   A 136 ? 0.1234 0.1394 0.1546 0.0015  0.0145  0.0006  136  PRO   A O   
2852 C  CB  A PRO   A 136 ? 0.1523 0.1576 0.1903 -0.0084 -0.0032 0.0264  136  PRO   A CB  
2853 C  CB  B PRO   A 136 ? 0.1550 0.1498 0.1978 0.0044  -0.0086 -0.0042 136  PRO   A CB  
2854 C  CG  A PRO   A 136 ? 0.1583 0.1595 0.2050 -0.0045 -0.0061 0.0306  136  PRO   A CG  
2855 C  CG  B PRO   A 136 ? 0.1593 0.1477 0.2088 0.0094  -0.0144 -0.0052 136  PRO   A CG  
2856 C  CD  A PRO   A 136 ? 0.1526 0.1589 0.1928 -0.0019 -0.0063 0.0371  136  PRO   A CD  
2857 C  CD  B PRO   A 136 ? 0.1501 0.1430 0.1966 0.0081  -0.0148 0.0059  136  PRO   A CD  
2872 N  N   A ILE   A 137 ? 0.1183 0.1486 0.1728 -0.0036 -0.0115 0.0185  137  ILE   A N   
2873 N  N   B ILE   A 137 ? 0.1255 0.1498 0.1994 -0.0033 -0.0073 -0.0029 137  ILE   A N   
2874 C  CA  A ILE   A 137 ? 0.1194 0.1537 0.1771 -0.0111 -0.0149 0.0260  137  ILE   A CA  
2875 C  CA  B ILE   A 137 ? 0.1256 0.1569 0.1990 -0.0089 -0.0058 -0.0043 137  ILE   A CA  
2876 C  C   A ILE   A 137 ? 0.1274 0.1492 0.1491 -0.0109 -0.0162 0.0271  137  ILE   A C   
2877 C  C   B ILE   A 137 ? 0.1277 0.1474 0.1773 -0.0121 -0.0040 -0.0097 137  ILE   A C   
2878 O  O   A ILE   A 137 ? 0.1362 0.1423 0.1475 -0.0145 -0.0069 0.0214  137  ILE   A O   
2879 O  O   B ILE   A 137 ? 0.1348 0.1503 0.1761 -0.0143 -0.0039 -0.0060 137  ILE   A O   
2880 C  CB  A ILE   A 137 ? 0.1294 0.1733 0.2167 -0.0164 -0.0278 0.0306  137  ILE   A CB  
2881 C  CB  B ILE   A 137 ? 0.1370 0.1687 0.2319 -0.0114 -0.0202 0.0008  137  ILE   A CB  
2882 C  CG1 A ILE   A 137 ? 0.1401 0.1982 0.2604 -0.0147 -0.0259 0.0343  137  ILE   A CG1 
2883 C  CG1 B ILE   A 137 ? 0.1546 0.1897 0.2688 -0.0013 -0.0375 0.0167  137  ILE   A CG1 
2884 C  CG2 A ILE   A 137 ? 0.1401 0.1737 0.2268 -0.0205 -0.0351 0.0214  137  ILE   A CG2 
2885 C  CG2 B ILE   A 137 ? 0.1418 0.1640 0.2443 -0.0146 -0.0242 -0.0106 137  ILE   A CG2 
2886 C  CD1 A ILE   A 137 ? 0.1583 0.2183 0.2922 -0.0098 -0.0144 0.0340  137  ILE   A CD1 
2887 C  CD1 B ILE   A 137 ? 0.1734 0.2074 0.3029 0.0045  -0.0344 0.0230  137  ILE   A CD1 
2910 N  N   A HIS   A 138 ? 0.1285 0.1542 0.1352 -0.0096 -0.0108 0.0218  138  HIS   A N   
2911 N  N   B HIS   A 138 ? 0.1288 0.1483 0.1694 -0.0113 0.0134  -0.0107 138  HIS   A N   
2912 C  CA  A HIS   A 138 ? 0.1365 0.1670 0.1470 -0.0027 -0.0077 0.0143  138  HIS   A CA  
2913 C  CA  B HIS   A 138 ? 0.1309 0.1354 0.1587 -0.0119 0.0076  -0.0073 138  HIS   A CA  
2914 C  C   A HIS   A 138 ? 0.1240 0.1585 0.1432 -0.0015 -0.0017 0.0179  138  HIS   A C   
2915 C  C   B HIS   A 138 ? 0.1258 0.1281 0.1499 -0.0056 0.0026  -0.0034 138  HIS   A C   
2916 O  O   A HIS   A 138 ? 0.1323 0.1629 0.1555 -0.0061 0.0062  0.0226  138  HIS   A O   
2917 O  O   B HIS   A 138 ? 0.1367 0.1273 0.1440 -0.0021 0.0019  -0.0072 138  HIS   A O   
2918 C  CB  A HIS   A 138 ? 0.1538 0.1800 0.1417 -0.0022 -0.0141 0.0135  138  HIS   A CB  
2919 C  CB  B HIS   A 138 ? 0.1363 0.1452 0.1541 -0.0116 0.0080  -0.0171 138  HIS   A CB  
2920 C  CG  A HIS   A 138 ? 0.1697 0.1865 0.1463 -0.0073 -0.0112 0.0110  138  HIS   A CG  
2921 C  CG  B HIS   A 138 ? 0.1521 0.1563 0.1722 -0.0059 0.0047  -0.0197 138  HIS   A CG  
2922 N  ND1 A HIS   A 138 ? 0.1789 0.1933 0.1610 -0.0063 -0.0001 0.0072  138  HIS   A ND1 
2923 N  ND1 B HIS   A 138 ? 0.1650 0.1668 0.1946 0.0017  0.0030  -0.0246 138  HIS   A ND1 
2924 C  CD2 A HIS   A 138 ? 0.1744 0.1917 0.1516 -0.0047 -0.0120 0.0127  138  HIS   A CD2 
2925 C  CD2 B HIS   A 138 ? 0.1554 0.1592 0.1762 -0.0012 0.0063  -0.0125 138  HIS   A CD2 
2926 C  CE1 A HIS   A 138 ? 0.1871 0.2001 0.1722 0.0017  0.0006  0.0089  138  HIS   A CE1 
2927 C  CE1 B HIS   A 138 ? 0.1698 0.1696 0.1877 0.0070  0.0017  -0.0237 138  HIS   A CE1 
2928 N  NE2 A HIS   A 138 ? 0.1814 0.1996 0.1583 0.0019  -0.0034 0.0115  138  HIS   A NE2 
2929 N  NE2 B HIS   A 138 ? 0.1642 0.1680 0.1800 0.0047  0.0050  -0.0158 138  HIS   A NE2 
2944 N  N   A SER   A 139 ? 0.1121 0.1458 0.1311 0.0041  -0.0026 0.0157  139  SER   A N   
2945 N  N   B SER   A 139 ? 0.1197 0.1216 0.1554 -0.0054 -0.0008 0.0084  139  SER   A N   
2946 C  CA  A SER   A 139 ? 0.1134 0.1393 0.1303 -0.0012 0.0026  0.0159  139  SER   A CA  
2947 C  CA  B SER   A 139 ? 0.1190 0.1201 0.1400 -0.0036 0.0104  0.0015  139  SER   A CA  
2948 C  C   A SER   A 139 ? 0.1096 0.1320 0.1342 -0.0043 0.0090  0.0072  139  SER   A C   
2949 C  C   B SER   A 139 ? 0.1164 0.1170 0.1406 -0.0010 0.0129  -0.0023 139  SER   A C   
2950 O  O   A SER   A 139 ? 0.1084 0.1302 0.1252 -0.0080 0.0137  0.0024  139  SER   A O   
2951 O  O   B SER   A 139 ? 0.1199 0.1168 0.1550 -0.0007 -0.0075 0.0095  139  SER   A O   
2952 C  CB  A SER   A 139 ? 0.1084 0.1305 0.1197 -0.0016 0.0120  0.0066  139  SER   A CB  
2953 C  CB  B SER   A 139 ? 0.1224 0.1204 0.1560 -0.0049 0.0014  0.0046  139  SER   A CB  
2954 O  OG  A SER   A 139 ? 0.1025 0.1203 0.1111 0.0008  0.0067  0.0152  139  SER   A OG  
2955 O  OG  B SER   A 139 ? 0.1289 0.1147 0.1543 -0.0083 0.0014  -0.0050 139  SER   A OG  
2966 N  N   A LEU   A 140 ? 0.1094 0.1358 0.1327 -0.0004 -0.0002 0.0059  140  LEU   A N   
2967 N  N   B LEU   A 140 ? 0.1138 0.1231 0.1222 -0.0047 0.0130  0.0108  140  LEU   A N   
2968 C  CA  A LEU   A 140 ? 0.1116 0.1378 0.1305 -0.0028 -0.0002 0.0066  140  LEU   A CA  
2969 C  CA  B LEU   A 140 ? 0.1132 0.1174 0.1209 -0.0072 0.0192  0.0100  140  LEU   A CA  
2970 C  C   A LEU   A 140 ? 0.1076 0.1476 0.1285 -0.0071 0.0048  0.0013  140  LEU   A C   
2971 C  C   B LEU   A 140 ? 0.1095 0.1236 0.1353 -0.0103 0.0104  0.0142  140  LEU   A C   
2972 O  O   A LEU   A 140 ? 0.1071 0.1482 0.1366 0.0007  0.0129  0.0006  140  LEU   A O   
2973 O  O   B LEU   A 140 ? 0.1137 0.1240 0.1495 -0.0045 0.0093  0.0091  140  LEU   A O   
2974 C  CB  A LEU   A 140 ? 0.1148 0.1367 0.1430 -0.0043 -0.0090 -0.0014 140  LEU   A CB  
2975 C  CB  B LEU   A 140 ? 0.1148 0.1167 0.1362 -0.0091 0.0167  0.0059  140  LEU   A CB  
2976 C  CG  A LEU   A 140 ? 0.1129 0.1340 0.1431 -0.0062 0.0056  0.0033  140  LEU   A CG  
2977 C  CG  B LEU   A 140 ? 0.1121 0.1218 0.1480 -0.0114 0.0160  0.0172  140  LEU   A CG  
2978 C  CD1 A LEU   A 140 ? 0.1185 0.1305 0.1608 0.0088  0.0002  -0.0020 140  LEU   A CD1 
2979 C  CD1 B LEU   A 140 ? 0.1142 0.1252 0.1415 -0.0106 0.0224  0.0232  140  LEU   A CD1 
2980 C  CD2 A LEU   A 140 ? 0.1213 0.1348 0.1517 -0.0055 0.0063  -0.0041 140  LEU   A CD2 
2981 C  CD2 B LEU   A 140 ? 0.1127 0.1291 0.1687 -0.0048 0.0098  0.0245  140  LEU   A CD2 
3004 N  N   A ARG   A 141 ? 0.1179 0.1550 0.1359 -0.0106 0.0010  -0.0132 141  ARG   A N   
3005 N  N   B ARG   A 141 ? 0.1152 0.1324 0.1433 -0.0135 0.0072  0.0170  141  ARG   A N   
3006 C  CA  A ARG   A 141 ? 0.1324 0.1757 0.1494 -0.0203 -0.0017 -0.0193 141  ARG   A CA  
3007 C  CA  B ARG   A 141 ? 0.1178 0.1467 0.1413 -0.0187 0.0104  0.0048  141  ARG   A CA  
3008 C  C   A ARG   A 141 ? 0.1283 0.1628 0.1489 -0.0188 -0.0035 -0.0086 141  ARG   A C   
3009 C  C   B ARG   A 141 ? 0.1198 0.1368 0.1459 -0.0158 0.0049  0.0096  141  ARG   A C   
3010 O  O   A ARG   A 141 ? 0.1288 0.1530 0.1478 -0.0170 0.0103  -0.0144 141  ARG   A O   
3011 O  O   B ARG   A 141 ? 0.1229 0.1363 0.1584 -0.0176 0.0092  0.0041  141  ARG   A O   
3012 C  CB  A ARG   A 141 ? 0.1425 0.2081 0.1713 -0.0254 0.0079  -0.0293 141  ARG   A CB  
3013 C  CB  B ARG   A 141 ? 0.1243 0.1786 0.1351 -0.0284 0.0200  0.0047  141  ARG   A CB  
3014 C  CG  A ARG   A 141 ? 0.1642 0.2307 0.2026 -0.0327 0.0005  -0.0300 141  ARG   A CG  
3015 C  CG  B ARG   A 141 ? 0.1463 0.2008 0.1569 -0.0314 0.0102  -0.0000 141  ARG   A CG  
3016 C  CD  A ARG   A 141 ? 0.1699 0.2381 0.2166 -0.0462 -0.0083 -0.0189 141  ARG   A CD  
3017 C  CD  B ARG   A 141 ? 0.1608 0.1997 0.1896 -0.0312 0.0059  -0.0030 141  ARG   A CD  
3018 N  NE  A ARG   A 141 ? 0.1681 0.2452 0.2328 -0.0547 -0.0047 -0.0006 141  ARG   A NE  
3019 N  NE  B ARG   A 141 ? 0.1734 0.2109 0.1987 -0.0212 0.0133  0.0082  141  ARG   A NE  
3020 C  CZ  A ARG   A 141 ? 0.1648 0.2626 0.2358 -0.0647 -0.0071 0.0055  141  ARG   A CZ  
3021 C  CZ  B ARG   A 141 ? 0.1783 0.2153 0.1954 -0.0199 0.0232  0.0197  141  ARG   A CZ  
3022 N  NH1 A ARG   A 141 ? 0.1669 0.2664 0.2458 -0.0617 -0.0067 0.0049  141  ARG   A NH1 
3023 N  NH1 B ARG   A 141 ? 0.1830 0.2232 0.1940 -0.0258 0.0307  0.0212  141  ARG   A NH1 
3024 N  NH2 A ARG   A 141 ? 0.1635 0.2755 0.2428 -0.0647 -0.0125 0.0098  141  ARG   A NH2 
3025 N  NH2 B ARG   A 141 ? 0.1825 0.2236 0.2078 -0.0101 0.0269  0.0277  141  ARG   A NH2 
3052 N  N   A VAL   A 142 ? 0.1200 0.1577 0.1484 -0.0149 -0.0020 -0.0010 142  VAL   A N   
3053 N  N   B VAL   A 142 ? 0.1181 0.1425 0.1570 -0.0070 0.0051  0.0147  142  VAL   A N   
3054 C  CA  A VAL   A 142 ? 0.1152 0.1500 0.1610 -0.0153 0.0158  0.0109  142  VAL   A CA  
3055 C  CA  B VAL   A 142 ? 0.1243 0.1392 0.1620 -0.0043 0.0083  0.0178  142  VAL   A CA  
3056 C  C   A VAL   A 142 ? 0.1077 0.1460 0.1649 -0.0169 0.0148  0.0147  142  VAL   A C   
3057 C  C   B VAL   A 142 ? 0.1106 0.1401 0.1674 -0.0101 0.0077  0.0168  142  VAL   A C   
3058 O  O   A VAL   A 142 ? 0.1157 0.1513 0.1669 -0.0069 0.0154  0.0215  142  VAL   A O   
3059 O  O   B VAL   A 142 ? 0.1154 0.1458 0.1740 -0.0014 0.0039  0.0197  142  VAL   A O   
3060 C  CB  A VAL   A 142 ? 0.1158 0.1459 0.1640 -0.0126 0.0181  0.0170  142  VAL   A CB  
3061 C  CB  B VAL   A 142 ? 0.1365 0.1468 0.1604 0.0007  0.0059  0.0150  142  VAL   A CB  
3062 C  CG1 A VAL   A 142 ? 0.1054 0.1313 0.1651 -0.0165 0.0298  0.0168  142  VAL   A CG1 
3063 C  CG1 B VAL   A 142 ? 0.1408 0.1404 0.1666 0.0005  0.0047  0.0045  142  VAL   A CG1 
3064 C  CG2 A VAL   A 142 ? 0.1238 0.1592 0.1778 -0.0086 0.0214  0.0102  142  VAL   A CG2 
3065 C  CG2 B VAL   A 142 ? 0.1467 0.1596 0.1623 0.0057  0.0003  0.0237  142  VAL   A CG2 
3084 N  N   . CYS   A 143 ? 0.1127 0.1446 0.1606 -0.0126 0.0094  0.0192  143  CYS   A N   
3085 C  CA  . CYS   A 143 ? 0.1161 0.1451 0.1686 -0.0138 0.0064  0.0282  143  CYS   A CA  
3086 C  C   . CYS   A 143 ? 0.1125 0.1399 0.1747 -0.0113 0.0086  0.0279  143  CYS   A C   
3087 O  O   . CYS   A 143 ? 0.1140 0.1404 0.1662 -0.0083 0.0053  0.0297  143  CYS   A O   
3088 C  CB  . CYS   A 143 ? 0.1235 0.1440 0.1738 -0.0017 0.0061  0.0326  143  CYS   A CB  
3089 S  SG  . CYS   A 143 ? 0.1401 0.1526 0.1565 0.0037  0.0100  0.0204  143  CYS   A SG  
3096 N  N   . VAL   A 144 ? 0.1157 0.1507 0.1822 -0.0148 0.0089  0.0325  144  VAL   A N   
3097 C  CA  . VAL   A 144 ? 0.1196 0.1594 0.1999 -0.0177 0.0142  0.0306  144  VAL   A CA  
3098 C  C   . VAL   A 144 ? 0.1247 0.1467 0.1945 -0.0217 -0.0052 0.0266  144  VAL   A C   
3099 O  O   . VAL   A 144 ? 0.1419 0.1485 0.2073 -0.0130 -0.0033 0.0313  144  VAL   A O   
3100 C  CB  . VAL   A 144 ? 0.1388 0.1814 0.2518 -0.0122 0.0328  0.0332  144  VAL   A CB  
3101 C  CG1 . VAL   A 144 ? 0.1511 0.1935 0.2899 -0.0275 0.0187  0.0288  144  VAL   A CG1 
3102 C  CG2 . VAL   A 144 ? 0.1308 0.1868 0.2657 -0.0086 0.0333  0.0502  144  VAL   A CG2 
3112 N  N   . ASP   A 145 ? 0.1263 0.1436 0.1995 -0.0225 0.0001  0.0191  145  ASP   A N   
3113 C  CA  . ASP   A 145 ? 0.1390 0.1482 0.2167 -0.0250 0.0011  0.0083  145  ASP   A CA  
3114 C  C   . ASP   A 145 ? 0.1329 0.1389 0.2218 -0.0169 0.0066  0.0064  145  ASP   A C   
3115 O  O   . ASP   A 145 ? 0.1471 0.1455 0.2806 -0.0182 0.0013  -0.0217 145  ASP   A O   
3116 C  CB  . ASP   A 145 ? 0.1516 0.1765 0.2242 -0.0335 -0.0093 -0.0002 145  ASP   A CB  
3117 C  CG  . ASP   A 145 ? 0.1691 0.2204 0.2498 -0.0555 -0.0219 0.0107  145  ASP   A CG  
3118 O  OD1 . ASP   A 145 ? 0.1649 0.2358 0.2590 -0.0668 -0.0113 0.0198  145  ASP   A OD1 
3119 O  OD2 . ASP   A 145 ? 0.1912 0.2449 0.2587 -0.0622 -0.0421 0.0214  145  ASP   A OD2 
3124 N  N   . THR   A 146 ? 0.1259 0.1286 0.1858 -0.0149 0.0086  0.0151  146  THR   A N   
3125 C  CA  . THR   A 146 ? 0.1208 0.1248 0.1763 -0.0090 0.0030  0.0088  146  THR   A CA  
3126 C  C   . THR   A 146 ? 0.1184 0.1200 0.1829 -0.0039 0.0111  0.0185  146  THR   A C   
3127 O  O   . THR   A 146 ? 0.1281 0.1375 0.1926 0.0030  -0.0006 0.0150  146  THR   A O   
3128 C  CB  . THR   A 146 ? 0.1182 0.1275 0.1809 -0.0047 0.0065  0.0200  146  THR   A CB  
3129 O  OG1 . THR   A 146 ? 0.1165 0.1397 0.1880 -0.0013 0.0009  0.0106  146  THR   A OG1 
3130 C  CG2 . THR   A 146 ? 0.1156 0.1287 0.2038 -0.0087 0.0058  0.0204  146  THR   A CG2 
3138 N  N   . VAL   A 147 ? 0.1193 0.1258 0.1662 0.0001  0.0110  0.0203  147  VAL   A N   
3139 C  CA  . VAL   A 147 ? 0.1173 0.1321 0.1741 -0.0091 0.0141  0.0292  147  VAL   A CA  
3140 C  C   . VAL   A 147 ? 0.1194 0.1251 0.1958 -0.0132 0.0130  0.0361  147  VAL   A C   
3141 O  O   . VAL   A 147 ? 0.1204 0.1320 0.2111 -0.0157 0.0054  0.0318  147  VAL   A O   
3142 C  CB  . VAL   A 147 ? 0.1290 0.1272 0.1642 -0.0132 0.0110  0.0296  147  VAL   A CB  
3143 C  CG1 . VAL   A 147 ? 0.1551 0.1358 0.1724 -0.0077 0.0110  0.0403  147  VAL   A CG1 
3144 C  CG2 . VAL   A 147 ? 0.1320 0.1294 0.1713 -0.0096 0.0011  0.0204  147  VAL   A CG2 
3154 N  N   . ARG   A 148 ? 0.1203 0.1278 0.1979 -0.0147 0.0155  0.0456  148  ARG   A N   
3155 C  CA  . ARG   A 148 ? 0.1257 0.1372 0.1943 -0.0126 0.0101  0.0497  148  ARG   A CA  
3156 C  C   . ARG   A 148 ? 0.1363 0.1344 0.1876 -0.0141 0.0106  0.0590  148  ARG   A C   
3157 O  O   . ARG   A 148 ? 0.1645 0.1480 0.2001 -0.0200 0.0143  0.0521  148  ARG   A O   
3158 C  CB  . ARG   A 148 ? 0.1297 0.1367 0.2128 -0.0039 0.0116  0.0478  148  ARG   A CB  
3159 C  CG  . ARG   A 148 ? 0.1437 0.1323 0.2457 -0.0061 0.0330  0.0343  148  ARG   A CG  
3160 C  CD  . ARG   A 148 ? 0.1602 0.1298 0.2693 -0.0034 0.0423  0.0458  148  ARG   A CD  
3161 N  NE  . ARG   A 148 ? 0.1571 0.1356 0.2633 0.0099  0.0457  0.0527  148  ARG   A NE  
3162 C  CZ  . ARG   A 148 ? 0.1545 0.1274 0.2501 0.0106  0.0467  0.0472  148  ARG   A CZ  
3163 N  NH1 . ARG   A 148 ? 0.1593 0.1279 0.2584 -0.0064 0.0442  0.0271  148  ARG   A NH1 
3164 N  NH2 . ARG   A 148 ? 0.1477 0.1465 0.2467 0.0152  0.0448  0.0493  148  ARG   A NH2 
3178 N  N   . THR   A 149 ? 0.1323 0.1401 0.1823 -0.0180 0.0013  0.0473  149  THR   A N   
3179 C  CA  . THR   A 149 ? 0.1351 0.1487 0.1779 -0.0139 0.0000  0.0439  149  THR   A CA  
3180 C  C   . THR   A 149 ? 0.1273 0.1444 0.1583 -0.0195 0.0072  0.0494  149  THR   A C   
3181 O  O   . THR   A 149 ? 0.1270 0.1541 0.1852 -0.0203 0.0040  0.0427  149  THR   A O   
3182 C  CB  . THR   A 149 ? 0.1372 0.1609 0.1777 -0.0163 0.0027  0.0392  149  THR   A CB  
3183 O  OG1 . THR   A 149 ? 0.1366 0.1516 0.1917 -0.0257 0.0033  0.0373  149  THR   A OG1 
3184 C  CG2 . THR   A 149 ? 0.1321 0.1681 0.1998 -0.0090 -0.0057 0.0405  149  THR   A CG2 
3192 N  N   . ASN   A 150 ? 0.1305 0.1484 0.1621 -0.0098 -0.0008 0.0558  150  ASN   A N   
3193 C  CA  . ASN   A 150 ? 0.1445 0.1549 0.1635 -0.0131 0.0069  0.0477  150  ASN   A CA  
3194 C  C   . ASN   A 150 ? 0.1276 0.1474 0.1645 -0.0166 0.0024  0.0442  150  ASN   A C   
3195 O  O   . ASN   A 150 ? 0.1359 0.1597 0.1999 -0.0158 -0.0158 0.0445  150  ASN   A O   
3196 C  CB  . ASN   A 150 ? 0.1900 0.1818 0.1900 -0.0188 0.0202  0.0691  150  ASN   A CB  
3197 C  CG  . ASN   A 150 ? 0.2419 0.2190 0.2525 -0.0162 0.0108  0.0747  150  ASN   A CG  
3198 O  OD1 . ASN   A 150 ? 0.2661 0.2283 0.2714 -0.0236 0.0143  0.0871  150  ASN   A OD1 
3199 N  ND2 . ASN   A 150 ? 0.2666 0.2426 0.2838 -0.0112 0.0000  0.0762  150  ASN   A ND2 
3206 N  N   . VAL   A 151 ? 0.1276 0.1364 0.1691 -0.0151 0.0017  0.0380  151  VAL   A N   
3207 C  CA  . VAL   A 151 ? 0.1335 0.1370 0.1508 -0.0199 0.0003  0.0384  151  VAL   A CA  
3208 C  C   . VAL   A 151 ? 0.1253 0.1337 0.1582 -0.0270 0.0016  0.0464  151  VAL   A C   
3209 O  O   . VAL   A 151 ? 0.1323 0.1414 0.1936 -0.0211 0.0034  0.0375  151  VAL   A O   
3210 C  CB  . VAL   A 151 ? 0.1604 0.1554 0.1593 -0.0092 0.0057  0.0369  151  VAL   A CB  
3211 C  CG1 . VAL   A 151 ? 0.1533 0.1761 0.1809 -0.0180 0.0032  0.0387  151  VAL   A CG1 
3212 C  CG2 . VAL   A 151 ? 0.1717 0.1546 0.1622 -0.0066 0.0219  0.0387  151  VAL   A CG2 
3222 N  N   . TYR   A 152 ? 0.1220 0.1368 0.1582 -0.0251 -0.0004 0.0420  152  TYR   A N   
3223 C  CA  . TYR   A 152 ? 0.1229 0.1455 0.1435 -0.0185 -0.0027 0.0390  152  TYR   A CA  
3224 C  C   . TYR   A 152 ? 0.1211 0.1371 0.1375 -0.0183 0.0098  0.0369  152  TYR   A C   
3225 O  O   . TYR   A 152 ? 0.1304 0.1402 0.1457 -0.0266 0.0064  0.0332  152  TYR   A O   
3226 C  CB  . TYR   A 152 ? 0.1388 0.1551 0.1458 -0.0149 0.0081  0.0421  152  TYR   A CB  
3227 C  CG  . TYR   A 152 ? 0.1440 0.1739 0.1429 -0.0182 0.0143  0.0459  152  TYR   A CG  
3228 C  CD1 . TYR   A 152 ? 0.1612 0.1895 0.1692 -0.0023 0.0187  0.0502  152  TYR   A CD1 
3229 C  CD2 . TYR   A 152 ? 0.1543 0.1880 0.1465 -0.0273 0.0085  0.0384  152  TYR   A CD2 
3230 C  CE1 . TYR   A 152 ? 0.1962 0.2016 0.1787 -0.0006 0.0114  0.0650  152  TYR   A CE1 
3231 C  CE2 . TYR   A 152 ? 0.1818 0.2007 0.1480 -0.0323 0.0098  0.0474  152  TYR   A CE2 
3232 C  CZ  . TYR   A 152 ? 0.2099 0.2032 0.1641 -0.0224 0.0034  0.0670  152  TYR   A CZ  
3233 O  OH  . TYR   A 152 ? 0.2391 0.2192 0.1929 -0.0259 0.0051  0.0816  152  TYR   A OH  
3243 N  N   A LEU   A 153 ? 0.1123 0.1331 0.1449 -0.0187 0.0164  0.0317  153  LEU   A N   
3244 N  N   B LEU   A 153 ? 0.1198 0.1374 0.1423 -0.0151 0.0100  0.0408  153  LEU   A N   
3245 C  CA  A LEU   A 153 ? 0.1110 0.1275 0.1532 -0.0162 0.0079  0.0274  153  LEU   A CA  
3246 C  CA  B LEU   A 153 ? 0.1178 0.1345 0.1403 -0.0046 0.0105  0.0401  153  LEU   A CA  
3247 C  C   A LEU   A 153 ? 0.1122 0.1245 0.1436 -0.0159 0.0149  0.0187  153  LEU   A C   
3248 C  C   B LEU   A 153 ? 0.1223 0.1481 0.1413 0.0012  0.0224  0.0354  153  LEU   A C   
3249 O  O   A LEU   A 153 ? 0.1195 0.1346 0.1505 -0.0214 0.0232  0.0117  153  LEU   A O   
3250 O  O   B LEU   A 153 ? 0.1226 0.1584 0.1463 -0.0010 0.0200  0.0346  153  LEU   A O   
3251 C  CB  A LEU   A 153 ? 0.1114 0.1235 0.1646 -0.0169 0.0089  0.0224  153  LEU   A CB  
3252 C  CB  B LEU   A 153 ? 0.1146 0.1305 0.1520 -0.0014 0.0044  0.0377  153  LEU   A CB  
3253 C  CG  A LEU   A 153 ? 0.1199 0.1243 0.1640 -0.0132 0.0195  0.0161  153  LEU   A CG  
3254 C  CG  B LEU   A 153 ? 0.1212 0.1308 0.1487 -0.0001 0.0044  0.0333  153  LEU   A CG  
3255 C  CD1 A LEU   A 153 ? 0.1268 0.1220 0.1571 -0.0144 0.0164  0.0152  153  LEU   A CD1 
3256 C  CD1 B LEU   A 153 ? 0.1257 0.1351 0.1492 -0.0055 -0.0044 0.0292  153  LEU   A CD1 
3257 C  CD2 A LEU   A 153 ? 0.1286 0.1331 0.1682 -0.0143 0.0294  -0.0004 153  LEU   A CD2 
3258 C  CD2 B LEU   A 153 ? 0.1322 0.1339 0.1656 0.0036  0.0134  0.0263  153  LEU   A CD2 
3281 N  N   A ALA   A 154 ? 0.1117 0.1167 0.1588 -0.0106 0.0071  0.0277  154  ALA   A N   
3282 N  N   B ALA   A 154 ? 0.1288 0.1471 0.1329 0.0019  0.0322  0.0339  154  ALA   A N   
3283 C  CA  A ALA   A 154 ? 0.1159 0.1193 0.1482 -0.0065 0.0121  0.0208  154  ALA   A CA  
3284 C  CA  B ALA   A 154 ? 0.1434 0.1528 0.1421 0.0033  0.0271  0.0272  154  ALA   A CA  
3285 C  C   A ALA   A 154 ? 0.1091 0.1097 0.1490 -0.0039 0.0158  0.0228  154  ALA   A C   
3286 C  C   B ALA   A 154 ? 0.1461 0.1539 0.1436 0.0043  0.0211  0.0337  154  ALA   A C   
3287 O  O   A ALA   A 154 ? 0.1200 0.1178 0.1763 0.0008  0.0150  0.0321  154  ALA   A O   
3288 O  O   B ALA   A 154 ? 0.1481 0.1538 0.1435 0.0051  0.0276  0.0325  154  ALA   A O   
3289 C  CB  A ALA   A 154 ? 0.1224 0.1318 0.1721 0.0011  0.0056  0.0088  154  ALA   A CB  
3290 C  CB  B ALA   A 154 ? 0.1512 0.1580 0.1681 0.0064  0.0177  0.0122  154  ALA   A CB  
3301 N  N   A VAL   A 155 ? 0.0982 0.0998 0.1097 -0.0049 0.0226  0.0270  155  VAL   A N   
3302 N  N   B VAL   A 155 ? 0.1448 0.1577 0.1501 0.0068  0.0117  0.0437  155  VAL   A N   
3303 C  CA  A VAL   A 155 ? 0.1086 0.1160 0.1423 -0.0038 0.0178  0.0347  155  VAL   A CA  
3304 C  CA  B VAL   A 155 ? 0.1603 0.1870 0.1833 -0.0006 0.0038  0.0465  155  VAL   A CA  
3305 C  CA  T VAL   A 155 ? 0.1300 0.1362 0.1424 -0.0130 0.0164  0.0379  155  VAL   A CA  
3306 C  C   A VAL   A 155 ? 0.1102 0.1211 0.1510 0.0157  0.0234  0.0488  155  VAL   A C   
3307 C  C   B VAL   A 155 ? 0.1819 0.2136 0.2354 0.0145  -0.0097 0.0537  155  VAL   A C   
3308 C  C   T VAL   A 155 ? 0.1298 0.1341 0.1341 -0.0005 0.0217  0.0409  155  VAL   A C   
3309 O  O   A VAL   A 155 ? 0.1059 0.1241 0.1647 0.0178  0.0370  0.0439  155  VAL   A O   
3310 O  O   B VAL   A 155 ? 0.1799 0.2155 0.2604 0.0223  0.0051  0.0528  155  VAL   A O   
3311 O  O   T VAL   A 155 ? 0.1254 0.1382 0.1312 0.0030  0.0237  0.0382  155  VAL   A O   
3312 C  CB  A VAL   A 155 ? 0.1157 0.1239 0.1581 -0.0043 0.0027  0.0260  155  VAL   A CB  
3313 C  CB  B VAL   A 155 ? 0.1598 0.1904 0.1713 -0.0090 -0.0117 0.0428  155  VAL   A CB  
3314 C  CB  T VAL   A 155 ? 0.1318 0.1383 0.1506 -0.0154 0.0038  0.0340  155  VAL   A CB  
3315 C  CG1 A VAL   A 155 ? 0.1322 0.1350 0.1701 -0.0036 -0.0023 0.0211  155  VAL   A CG1 
3316 C  CG1 B VAL   A 155 ? 0.1731 0.1976 0.1724 -0.0136 -0.0146 0.0462  155  VAL   A CG1 
3317 C  CG1 T VAL   A 155 ? 0.1405 0.1438 0.1600 -0.0169 -0.0015 0.0320  155  VAL   A CG1 
3318 C  CG2 A VAL   A 155 ? 0.1227 0.1274 0.1696 -0.0040 -0.0105 0.0238  155  VAL   A CG2 
3319 C  CG2 B VAL   A 155 ? 0.1602 0.1932 0.1889 -0.0126 -0.0202 0.0318  155  VAL   A CG2 
3320 C  CG2 T VAL   A 155 ? 0.1349 0.1393 0.1574 -0.0142 -0.0039 0.0326  155  VAL   A CG2 
3346 N  N   A PHE   A 156 ? 0.1219 0.1319 0.1580 0.0262  0.0310  0.0543  156  PHE   A N   
3347 N  N   B PHE   A 156 ? 0.2049 0.2375 0.2580 0.0219  -0.0257 0.0553  156  PHE   A N   
3348 N  N   T PHE   A 156 ? 0.1379 0.1323 0.1320 0.0057  0.0308  0.0401  156  PHE   A N   
3349 C  CA  A PHE   A 156 ? 0.1391 0.1460 0.1776 0.0387  0.0373  0.0590  156  PHE   A CA  
3350 C  CA  B PHE   A 156 ? 0.2211 0.2572 0.2809 0.0304  -0.0296 0.0595  156  PHE   A CA  
3351 C  CA  T PHE   A 156 ? 0.1510 0.1340 0.1321 0.0132  0.0393  0.0441  156  PHE   A CA  
3352 C  C   A PHE   A 156 ? 0.1424 0.1484 0.1731 0.0433  0.0497  0.0865  156  PHE   A C   
3353 C  C   B PHE   A 156 ? 0.2223 0.2516 0.2985 0.0319  -0.0315 0.0737  156  PHE   A C   
3354 C  C   T PHE   A 156 ? 0.1584 0.1493 0.1439 0.0214  0.0476  0.0538  156  PHE   A C   
3355 O  O   A PHE   A 156 ? 0.1460 0.1585 0.1807 0.0383  0.0646  0.0723  156  PHE   A O   
3356 O  O   B PHE   A 156 ? 0.2341 0.2546 0.3168 0.0367  -0.0306 0.0708  156  PHE   A O   
3357 O  O   T PHE   A 156 ? 0.1672 0.1558 0.1426 0.0265  0.0556  0.0444  156  PHE   A O   
3358 C  CB  A PHE   A 156 ? 0.1611 0.1586 0.1997 0.0437  0.0268  0.0534  156  PHE   A CB  
3359 C  CB  B PHE   A 156 ? 0.2356 0.2858 0.2967 0.0317  -0.0220 0.0481  156  PHE   A CB  
3360 C  CB  T PHE   A 156 ? 0.1575 0.1209 0.1290 0.0103  0.0339  0.0494  156  PHE   A CB  
3361 C  CG  A PHE   A 156 ? 0.1892 0.1718 0.2192 0.0470  0.0125  0.0405  156  PHE   A CG  
3362 C  CG  B PHE   A 156 ? 0.2472 0.3115 0.3031 0.0351  -0.0182 0.0388  156  PHE   A CG  
3363 C  CG  T PHE   A 156 ? 0.1585 0.1111 0.1123 0.0097  0.0262  0.0573  156  PHE   A CG  
3364 C  CD1 A PHE   A 156 ? 0.2012 0.1792 0.2276 0.0468  0.0170  0.0326  156  PHE   A CD1 
3365 C  CD1 B PHE   A 156 ? 0.2504 0.3232 0.2999 0.0349  -0.0155 0.0364  156  PHE   A CD1 
3366 C  CD1 T PHE   A 156 ? 0.1603 0.1108 0.1181 0.0139  0.0161  0.0501  156  PHE   A CD1 
3367 C  CD2 A PHE   A 156 ? 0.1989 0.1813 0.2264 0.0495  0.0090  0.0338  156  PHE   A CD2 
3368 C  CD2 B PHE   A 156 ? 0.2567 0.3222 0.3140 0.0379  -0.0129 0.0366  156  PHE   A CD2 
3369 C  CD2 T PHE   A 156 ? 0.1626 0.1120 0.1271 0.0129  0.0150  0.0461  156  PHE   A CD2 
3370 C  CE1 A PHE   A 156 ? 0.2094 0.1830 0.2322 0.0446  0.0208  0.0251  156  PHE   A CE1 
3371 C  CE1 B PHE   A 156 ? 0.2552 0.3278 0.3127 0.0377  -0.0148 0.0349  156  PHE   A CE1 
3372 C  CE1 T PHE   A 156 ? 0.1658 0.1147 0.1439 0.0174  0.0118  0.0313  156  PHE   A CE1 
3373 C  CE2 A PHE   A 156 ? 0.2118 0.1865 0.2310 0.0470  0.0093  0.0217  156  PHE   A CE2 
3374 C  CE2 B PHE   A 156 ? 0.2600 0.3307 0.3155 0.0379  -0.0122 0.0340  156  PHE   A CE2 
3375 C  CE2 T PHE   A 156 ? 0.1711 0.1146 0.1418 0.0120  0.0079  0.0394  156  PHE   A CE2 
3376 C  CZ  A PHE   A 156 ? 0.2153 0.1878 0.2386 0.0458  0.0172  0.0168  156  PHE   A CZ  
3377 C  CZ  B PHE   A 156 ? 0.2568 0.3311 0.3143 0.0394  -0.0125 0.0331  156  PHE   A CZ  
3378 C  CZ  T PHE   A 156 ? 0.1688 0.1133 0.1438 0.0128  0.0090  0.0306  156  PHE   A CZ  
3406 N  N   A ASP   A 157 ? 0.1550 0.1562 0.1974 0.0419  0.0429  0.0980  157  ASP   A N   
3407 N  N   B ASP   A 157 ? 0.2101 0.2434 0.2876 0.0224  -0.0367 0.0922  157  ASP   A N   
3408 N  N   T ASP   A 157 ? 0.1617 0.1653 0.1707 0.0191  0.0467  0.0642  157  ASP   A N   
3409 C  CA  A ASP   A 157 ? 0.1686 0.1775 0.2214 0.0381  0.0327  0.0925  157  ASP   A CA  
3410 C  CA  B ASP   A 157 ? 0.1951 0.2457 0.2844 0.0087  -0.0384 0.0976  157  ASP   A CA  
3411 C  CA  T ASP   A 157 ? 0.1696 0.1840 0.1995 0.0192  0.0330  0.0672  157  ASP   A CA  
3412 C  C   A ASP   A 157 ? 0.1669 0.1893 0.2356 0.0338  0.0300  0.1053  157  ASP   A C   
3413 C  C   B ASP   A 157 ? 0.1902 0.2454 0.2943 0.0010  -0.0439 0.1009  157  ASP   A C   
3414 C  C   T ASP   A 157 ? 0.1739 0.2009 0.2117 0.0178  0.0323  0.0746  157  ASP   A C   
3415 O  O   A ASP   A 157 ? 0.1611 0.1814 0.2316 0.0285  0.0363  0.1147  157  ASP   A O   
3416 O  O   B ASP   A 157 ? 0.1854 0.2436 0.2967 -0.0056 -0.0402 0.0958  157  ASP   A O   
3417 O  O   T ASP   A 157 ? 0.1692 0.1999 0.2084 0.0154  0.0362  0.0761  157  ASP   A O   
3418 C  CB  A ASP   A 157 ? 0.1795 0.1862 0.2324 0.0442  0.0231  0.0851  157  ASP   A CB  
3419 C  CB  B ASP   A 157 ? 0.1811 0.2512 0.2750 0.0043  -0.0331 0.1033  157  ASP   A CB  
3420 C  CB  T ASP   A 157 ? 0.1719 0.1850 0.2172 0.0245  0.0196  0.0699  157  ASP   A CB  
3421 C  CG  A ASP   A 157 ? 0.1902 0.1988 0.2429 0.0472  0.0238  0.0753  157  ASP   A CG  
3422 C  CG  B ASP   A 157 ? 0.1666 0.2574 0.2730 0.0045  -0.0233 0.1060  157  ASP   A CG  
3423 C  CG  T ASP   A 157 ? 0.1723 0.1844 0.2297 0.0327  0.0126  0.0736  157  ASP   A CG  
3424 O  OD1 A ASP   A 157 ? 0.1992 0.2048 0.2492 0.0485  0.0229  0.0675  157  ASP   A OD1 
3425 O  OD1 B ASP   A 157 ? 0.1649 0.2524 0.2702 0.0035  -0.0072 0.1041  157  ASP   A OD1 
3426 O  OD1 T ASP   A 157 ? 0.1703 0.1836 0.2411 0.0358  0.0141  0.0680  157  ASP   A OD1 
3427 O  OD2 A ASP   A 157 ? 0.1875 0.2020 0.2530 0.0474  0.0274  0.0752  157  ASP   A OD2 
3428 O  OD2 B ASP   A 157 ? 0.1467 0.2634 0.2786 0.0029  -0.0252 0.1042  157  ASP   A OD2 
3429 O  OD2 T ASP   A 157 ? 0.1721 0.1815 0.2259 0.0372  0.0076  0.0796  157  ASP   A OD2 
3442 N  N   A LYS   A 158 ? 0.1717 0.2094 0.2621 0.0372  0.0264  0.1006  158  LYS   A N   
3443 N  N   B LYS   A 158 ? 0.1953 0.2478 0.3112 -0.0034 -0.0438 0.1036  158  LYS   A N   
3444 N  N   T LYS   A 158 ? 0.1833 0.2189 0.2325 0.0200  0.0315  0.0717  158  LYS   A N   
3445 C  CA  A LYS   A 158 ? 0.1715 0.2308 0.2813 0.0437  0.0319  0.0927  158  LYS   A CA  
3446 C  CA  B LYS   A 158 ? 0.2018 0.2591 0.3203 -0.0065 -0.0268 0.1038  158  LYS   A CA  
3447 C  CA  T LYS   A 158 ? 0.1913 0.2346 0.2526 0.0242  0.0310  0.0670  158  LYS   A CA  
3448 C  C   A LYS   A 158 ? 0.1626 0.2409 0.2671 0.0438  0.0210  0.1022  158  LYS   A C   
3449 C  C   B LYS   A 158 ? 0.1847 0.2629 0.2877 -0.0107 -0.0299 0.1167  158  LYS   A C   
3450 C  C   T LYS   A 158 ? 0.1917 0.2403 0.2475 0.0269  0.0225  0.0694  158  LYS   A C   
3451 O  O   A LYS   A 158 ? 0.1700 0.2464 0.2747 0.0388  0.0243  0.1022  158  LYS   A O   
3452 O  O   B LYS   A 158 ? 0.1820 0.2603 0.2758 -0.0245 -0.0202 0.1224  158  LYS   A O   
3453 O  O   T LYS   A 158 ? 0.1941 0.2441 0.2539 0.0281  0.0240  0.0676  158  LYS   A O   
3454 C  CB  A LYS   A 158 ? 0.1845 0.2410 0.3048 0.0461  0.0475  0.0865  158  LYS   A CB  
3455 C  CB  B LYS   A 158 ? 0.2258 0.2721 0.3500 -0.0083 -0.0077 0.0967  158  LYS   A CB  
3456 C  CB  T LYS   A 158 ? 0.2021 0.2431 0.2795 0.0215  0.0389  0.0613  158  LYS   A CB  
3457 C  CG  A LYS   A 158 ? 0.2009 0.2541 0.3308 0.0460  0.0529  0.0841  158  LYS   A CG  
3458 C  CG  B LYS   A 158 ? 0.2464 0.2871 0.3777 -0.0125 0.0064  0.0979  158  LYS   A CG  
3459 C  CG  T LYS   A 158 ? 0.2147 0.2530 0.3069 0.0180  0.0394  0.0578  158  LYS   A CG  
3460 C  CD  A LYS   A 158 ? 0.2168 0.2663 0.3550 0.0423  0.0618  0.0869  158  LYS   A CD  
3461 C  CD  B LYS   A 158 ? 0.2590 0.2981 0.4014 -0.0131 0.0199  0.1010  158  LYS   A CD  
3462 C  CD  T LYS   A 158 ? 0.2263 0.2616 0.3345 0.0146  0.0415  0.0584  158  LYS   A CD  
3463 C  CE  A LYS   A 158 ? 0.2288 0.2748 0.3674 0.0381  0.0688  0.0952  158  LYS   A CE  
3464 C  CE  B LYS   A 158 ? 0.2644 0.3022 0.4091 -0.0095 0.0279  0.1107  158  LYS   A CE  
3465 C  CE  T LYS   A 158 ? 0.2344 0.2678 0.3518 0.0124  0.0421  0.0631  158  LYS   A CE  
3466 N  NZ  A LYS   A 158 ? 0.2375 0.2793 0.3767 0.0365  0.0716  0.1000  158  LYS   A NZ  
3467 N  NZ  B LYS   A 158 ? 0.2646 0.3032 0.4114 -0.0052 0.0276  0.1170  158  LYS   A NZ  
3468 N  NZ  T LYS   A 158 ? 0.2399 0.2715 0.3613 0.0118  0.0426  0.0663  158  LYS   A NZ  
3508 N  N   A ASN   A 159 ? 0.1524 0.2473 0.2596 0.0371  0.0110  0.1051  159  ASN   A N   
3509 N  N   B ASN   A 159 ? 0.1836 0.2797 0.2991 -0.0004 -0.0341 0.1106  159  ASN   A N   
3510 N  N   T ASN   A 159 ? 0.1918 0.2415 0.2465 0.0206  0.0145  0.0695  159  ASN   A N   
3511 C  CA  A ASN   A 159 ? 0.1507 0.2534 0.2467 0.0244  0.0031  0.1061  159  ASN   A CA  
3512 C  CA  B ASN   A 159 ? 0.1861 0.2976 0.3092 0.0055  -0.0329 0.0995  159  ASN   A CA  
3513 C  CA  T ASN   A 159 ? 0.1962 0.2423 0.2412 0.0105  0.0087  0.0693  159  ASN   A CA  
3514 C  C   A ASN   A 159 ? 0.1401 0.2564 0.2354 0.0134  0.0053  0.0968  159  ASN   A C   
3515 C  C   B ASN   A 159 ? 0.1610 0.2986 0.2712 0.0039  -0.0257 0.1036  159  ASN   A C   
3516 C  C   T ASN   A 159 ? 0.1986 0.2442 0.2367 0.0032  0.0109  0.0593  159  ASN   A C   
3517 O  O   A ASN   A 159 ? 0.1382 0.2577 0.2356 0.0152  -0.0000 0.0871  159  ASN   A O   
3518 O  O   B ASN   A 159 ? 0.1530 0.3097 0.2675 0.0091  -0.0344 0.1038  159  ASN   A O   
3519 O  O   T ASN   A 159 ? 0.2002 0.2437 0.2379 0.0042  0.0102  0.0527  159  ASN   A O   
3520 C  CB  A ASN   A 159 ? 0.1586 0.2556 0.2608 0.0241  -0.0070 0.1113  159  ASN   A CB  
3521 C  CB  B ASN   A 159 ? 0.2172 0.3117 0.3692 0.0118  -0.0359 0.0803  159  ASN   A CB  
3522 C  CB  T ASN   A 159 ? 0.1978 0.2420 0.2513 0.0097  -0.0003 0.0760  159  ASN   A CB  
3523 C  CG  A ASN   A 159 ? 0.1689 0.2582 0.2885 0.0208  -0.0092 0.1080  159  ASN   A CG  
3524 C  CG  B ASN   A 159 ? 0.2489 0.3238 0.4245 0.0108  -0.0401 0.0517  159  ASN   A CG  
3525 C  CG  T ASN   A 159 ? 0.2007 0.2420 0.2688 0.0079  -0.0044 0.0777  159  ASN   A CG  
3526 O  OD1 A ASN   A 159 ? 0.1653 0.2619 0.2994 0.0154  -0.0060 0.1088  159  ASN   A OD1 
3527 O  OD1 B ASN   A 159 ? 0.2605 0.3303 0.4471 0.0090  -0.0415 0.0423  159  ASN   A OD1 
3528 O  OD1 T ASN   A 159 ? 0.1976 0.2452 0.2771 0.0048  -0.0008 0.0782  159  ASN   A OD1 
3529 N  ND2 A ASN   A 159 ? 0.1713 0.2574 0.2882 0.0242  -0.0153 0.1083  159  ASN   A ND2 
3530 N  ND2 B ASN   A 159 ? 0.2577 0.3253 0.4474 0.0092  -0.0422 0.0381  159  ASN   A ND2 
3531 N  ND2 T ASN   A 159 ? 0.2015 0.2406 0.2653 0.0099  -0.0108 0.0817  159  ASN   A ND2 
3550 N  N   A LEU   A 160 ? 0.1341 0.2534 0.2261 0.0031  0.0010  0.0983  160  LEU   A N   
3551 N  N   B LEU   A 160 ? 0.1451 0.2840 0.2517 -0.0032 -0.0261 0.1128  160  LEU   A N   
3552 N  N   T LEU   A 160 ? 0.1993 0.2443 0.2325 -0.0040 0.0077  0.0574  160  LEU   A N   
3553 C  CA  A LEU   A 160 ? 0.1377 0.2483 0.2154 -0.0095 0.0043  0.0964  160  LEU   A CA  
3554 C  CA  B LEU   A 160 ? 0.1423 0.2705 0.2300 -0.0134 -0.0105 0.1173  160  LEU   A CA  
3555 C  CA  T LEU   A 160 ? 0.2028 0.2422 0.2264 -0.0117 0.0079  0.0555  160  LEU   A CA  
3556 C  C   A LEU   A 160 ? 0.1283 0.2449 0.2025 -0.0124 0.0059  0.0958  160  LEU   A C   
3557 C  C   B LEU   A 160 ? 0.1242 0.2606 0.2032 -0.0207 -0.0042 0.1145  160  LEU   A C   
3558 O  O   A LEU   A 160 ? 0.1226 0.2497 0.2045 -0.0111 0.0043  0.0901  160  LEU   A O   
3559 O  O   B LEU   A 160 ? 0.1156 0.2666 0.2138 -0.0219 -0.0043 0.1036  160  LEU   A O   
3560 C  CB  A LEU   A 160 ? 0.1434 0.2456 0.2097 -0.0169 0.0018  0.0945  160  LEU   A CB  
3561 C  CB  B LEU   A 160 ? 0.1502 0.2662 0.2226 -0.0169 -0.0086 0.1198  160  LEU   A CB  
3562 C  CB  T LEU   A 160 ? 0.2033 0.2398 0.2190 -0.0171 0.0080  0.0544  160  LEU   A CB  
3563 C  CG  A LEU   A 160 ? 0.1478 0.2450 0.2198 -0.0277 0.0001  0.0826  160  LEU   A CG  
3564 C  CG  B LEU   A 160 ? 0.1556 0.2670 0.2413 -0.0264 -0.0065 0.0984  160  LEU   A CG  
3565 C  CG  T LEU   A 160 ? 0.2039 0.2385 0.2199 -0.0234 0.0087  0.0486  160  LEU   A CG  
3566 C  CD1 A LEU   A 160 ? 0.1550 0.2489 0.2291 -0.0294 0.0036  0.0769  160  LEU   A CD1 
3567 C  CD1 B LEU   A 160 ? 0.1612 0.2717 0.2553 -0.0313 -0.0002 0.0880  160  LEU   A CD1 
3568 C  CD1 T LEU   A 160 ? 0.2066 0.2406 0.2234 -0.0240 0.0101  0.0448  160  LEU   A CD1 
3569 C  CD2 A LEU   A 160 ? 0.1499 0.2405 0.2209 -0.0305 -0.0023 0.0783  160  LEU   A CD2 
3570 C  CD2 B LEU   A 160 ? 0.1589 0.2634 0.2434 -0.0268 -0.0074 0.0899  160  LEU   A CD2 
3571 C  CD2 T LEU   A 160 ? 0.2039 0.2350 0.2173 -0.0258 0.0091  0.0477  160  LEU   A CD2 
3604 N  N   A TYR   A 161 ? 0.1336 0.2371 0.2136 -0.0120 0.0036  0.0932  161  TYR   A N   
3605 N  N   B TYR   A 161 ? 0.1307 0.2474 0.2103 -0.0222 -0.0031 0.1051  161  TYR   A N   
3606 C  CA  A TYR   A 161 ? 0.1335 0.2302 0.2048 -0.0064 0.0099  0.0907  161  TYR   A CA  
3607 C  CA  B TYR   A 161 ? 0.1360 0.2336 0.1999 -0.0208 0.0050  0.1011  161  TYR   A CA  
3608 C  C   A TYR   A 161 ? 0.1336 0.2483 0.2088 -0.0044 0.0101  0.0823  161  TYR   A C   
3609 C  C   B TYR   A 161 ? 0.1295 0.2440 0.2015 -0.0263 0.0023  0.0954  161  TYR   A C   
3610 O  O   A TYR   A 161 ? 0.1273 0.2510 0.1994 -0.0044 0.0049  0.0748  161  TYR   A O   
3611 O  O   B TYR   A 161 ? 0.1262 0.2412 0.1909 -0.0320 0.0011  0.0908  161  TYR   A O   
3612 C  CB  A TYR   A 161 ? 0.1389 0.2109 0.2117 0.0011  0.0118  0.0792  161  TYR   A CB  
3613 C  CB  B TYR   A 161 ? 0.1528 0.2126 0.2102 -0.0101 0.0128  0.0841  161  TYR   A CB  
3614 C  CG  A TYR   A 161 ? 0.1339 0.1972 0.2041 0.0118  0.0131  0.0660  161  TYR   A CG  
3615 C  CG  B TYR   A 161 ? 0.1617 0.1990 0.2097 0.0048  0.0220  0.0684  161  TYR   A CG  
3616 C  CD1 A TYR   A 161 ? 0.1389 0.1999 0.2042 0.0205  0.0133  0.0534  161  TYR   A CD1 
3617 C  CD1 B TYR   A 161 ? 0.1669 0.2021 0.2089 0.0172  0.0280  0.0602  161  TYR   A CD1 
3618 C  CD2 A TYR   A 161 ? 0.1333 0.1936 0.2062 0.0199  0.0111  0.0553  161  TYR   A CD2 
3619 C  CD2 B TYR   A 161 ? 0.1711 0.1963 0.2216 0.0106  0.0267  0.0578  161  TYR   A CD2 
3620 C  CE1 A TYR   A 161 ? 0.1506 0.1964 0.2005 0.0274  0.0157  0.0543  161  TYR   A CE1 
3621 C  CE1 B TYR   A 161 ? 0.1781 0.2008 0.2112 0.0277  0.0247  0.0683  161  TYR   A CE1 
3622 C  CE2 A TYR   A 161 ? 0.1411 0.1913 0.2084 0.0188  0.0219  0.0526  161  TYR   A CE2 
3623 C  CE2 B TYR   A 161 ? 0.1837 0.1968 0.2229 0.0133  0.0299  0.0598  161  TYR   A CE2 
3624 C  CZ  A TYR   A 161 ? 0.1606 0.1905 0.2119 0.0222  0.0214  0.0553  161  TYR   A CZ  
3625 C  CZ  B TYR   A 161 ? 0.1924 0.1988 0.2240 0.0202  0.0332  0.0688  161  TYR   A CZ  
3626 O  OH  A TYR   A 161 ? 0.1790 0.1839 0.2212 0.0242  0.0248  0.0620  161  TYR   A OH  
3627 O  OH  B TYR   A 161 ? 0.2142 0.2008 0.2475 0.0170  0.0417  0.0750  161  TYR   A OH  
3646 N  N   A ASP   A 162 ? 0.1379 0.2627 0.2190 0.0018  0.0154  0.0821  162  ASP   A N   
3647 N  N   B ASP   A 162 ? 0.1238 0.2551 0.2142 -0.0260 0.0023  0.0970  162  ASP   A N   
3648 C  CA  A ASP   A 162 ? 0.1445 0.2814 0.2190 0.0004  0.0197  0.0765  162  ASP   A CA  
3649 C  CA  B ASP   A 162 ? 0.1229 0.2746 0.2198 -0.0321 0.0026  0.0849  162  ASP   A CA  
3650 C  C   A ASP   A 162 ? 0.1498 0.2970 0.2138 -0.0022 0.0247  0.0751  162  ASP   A C   
3651 C  C   B ASP   A 162 ? 0.1123 0.2876 0.2179 -0.0425 -0.0059 0.0819  162  ASP   A C   
3652 O  O   A ASP   A 162 ? 0.1564 0.2978 0.2188 0.0011  0.0255  0.0672  162  ASP   A O   
3653 O  O   B ASP   A 162 ? 0.1143 0.2871 0.2315 -0.0519 -0.0071 0.0615  162  ASP   A O   
3654 C  CB  A ASP   A 162 ? 0.1474 0.2859 0.2295 0.0027  0.0268  0.0694  162  ASP   A CB  
3655 C  CB  B ASP   A 162 ? 0.1364 0.2860 0.2442 -0.0237 0.0118  0.0694  162  ASP   A CB  
3656 C  CG  A ASP   A 162 ? 0.1536 0.2925 0.2436 0.0064  0.0348  0.0642  162  ASP   A CG  
3657 C  CG  B ASP   A 162 ? 0.1517 0.2982 0.2554 -0.0113 0.0157  0.0626  162  ASP   A CG  
3658 O  OD1 A ASP   A 162 ? 0.1607 0.2991 0.2556 0.0064  0.0265  0.0569  162  ASP   A OD1 
3659 O  OD1 B ASP   A 162 ? 0.1545 0.3000 0.2554 -0.0094 0.0157  0.0573  162  ASP   A OD1 
3660 O  OD2 A ASP   A 162 ? 0.1591 0.2921 0.2548 0.0093  0.0548  0.0658  162  ASP   A OD2 
3661 O  OD2 B ASP   A 162 ? 0.1654 0.3054 0.2608 -0.0027 0.0274  0.0638  162  ASP   A OD2 
3670 N  N   A LYS   A 163 ? 0.1564 0.3120 0.2206 -0.0059 0.0149  0.0662  163  LYS   A N   
3671 N  N   B LYS   A 163 ? 0.1153 0.3028 0.2204 -0.0432 -0.0302 0.0805  163  LYS   A N   
3672 C  CA  A LYS   A 163 ? 0.1730 0.3257 0.2292 -0.0090 0.0009  0.0576  163  LYS   A CA  
3673 C  CA  B LYS   A 163 ? 0.1374 0.3189 0.2323 -0.0412 -0.0299 0.0741  163  LYS   A CA  
3674 C  C   A LYS   A 163 ? 0.1556 0.3139 0.2176 -0.0113 0.0090  0.0587  163  LYS   A C   
3675 C  C   B LYS   A 163 ? 0.1311 0.3033 0.2210 -0.0487 -0.0083 0.0688  163  LYS   A C   
3676 O  O   A LYS   A 163 ? 0.1486 0.3199 0.2245 -0.0075 0.0041  0.0443  163  LYS   A O   
3677 O  O   B LYS   A 163 ? 0.1334 0.3160 0.2419 -0.0497 -0.0097 0.0587  163  LYS   A O   
3678 C  CB  A LYS   A 163 ? 0.2088 0.3479 0.2666 -0.0051 -0.0152 0.0511  163  LYS   A CB  
3679 C  CB  B LYS   A 163 ? 0.1733 0.3485 0.2753 -0.0317 -0.0439 0.0732  163  LYS   A CB  
3680 C  CG  A LYS   A 163 ? 0.2442 0.3682 0.3225 -0.0069 -0.0156 0.0451  163  LYS   A CG  
3681 C  CG  B LYS   A 163 ? 0.2191 0.3738 0.3358 -0.0306 -0.0331 0.0743  163  LYS   A CG  
3682 C  CD  A LYS   A 163 ? 0.2732 0.3841 0.3798 -0.0100 -0.0175 0.0407  163  LYS   A CD  
3683 C  CD  B LYS   A 163 ? 0.2625 0.3927 0.3983 -0.0326 -0.0224 0.0765  163  LYS   A CD  
3684 C  CE  A LYS   A 163 ? 0.3030 0.3948 0.4260 -0.0113 -0.0162 0.0410  163  LYS   A CE  
3685 C  CE  B LYS   A 163 ? 0.2999 0.4049 0.4419 -0.0344 -0.0173 0.0797  163  LYS   A CE  
3686 N  NZ  A LYS   A 163 ? 0.3171 0.4006 0.4519 -0.0118 -0.0184 0.0442  163  LYS   A NZ  
3687 N  NZ  B LYS   A 163 ? 0.3208 0.4122 0.4701 -0.0347 -0.0159 0.0786  163  LYS   A NZ  
3714 N  N   A LEU   A 164 ? 0.1402 0.2906 0.1953 -0.0167 0.0085  0.0618  164  LEU   A N   
3715 N  N   B LEU   A 164 ? 0.1206 0.2755 0.1922 -0.0552 -0.0123 0.0668  164  LEU   A N   
3716 C  CA  A LEU   A 164 ? 0.1429 0.2718 0.1870 -0.0265 0.0187  0.0525  164  LEU   A CA  
3717 C  CA  B LEU   A 164 ? 0.1248 0.2531 0.1858 -0.0544 0.0004  0.0557  164  LEU   A CA  
3718 C  C   A LEU   A 164 ? 0.1483 0.2657 0.1908 -0.0349 0.0110  0.0459  164  LEU   A C   
3719 C  C   B LEU   A 164 ? 0.1350 0.2475 0.1833 -0.0462 0.0037  0.0455  164  LEU   A C   
3720 O  O   A LEU   A 164 ? 0.1529 0.2672 0.2002 -0.0364 0.0176  0.0424  164  LEU   A O   
3721 O  O   B LEU   A 164 ? 0.1360 0.2507 0.1768 -0.0488 0.0150  0.0390  164  LEU   A O   
3722 C  CB  A LEU   A 164 ? 0.1420 0.2620 0.1742 -0.0206 0.0223  0.0533  164  LEU   A CB  
3723 C  CB  B LEU   A 164 ? 0.1272 0.2394 0.1839 -0.0585 0.0015  0.0587  164  LEU   A CB  
3724 C  CG  A LEU   A 164 ? 0.1470 0.2556 0.1724 -0.0152 0.0185  0.0611  164  LEU   A CG  
3725 C  CG  B LEU   A 164 ? 0.1370 0.2362 0.1953 -0.0541 0.0037  0.0508  164  LEU   A CG  
3726 C  CD1 A LEU   A 164 ? 0.1381 0.2481 0.1554 -0.0087 0.0072  0.0761  164  LEU   A CD1 
3727 C  CD1 B LEU   A 164 ? 0.1314 0.2313 0.1967 -0.0488 0.0047  0.0488  164  LEU   A CD1 
3728 C  CD2 A LEU   A 164 ? 0.1582 0.2566 0.1840 -0.0166 0.0275  0.0512  164  LEU   A CD2 
3729 C  CD2 B LEU   A 164 ? 0.1518 0.2391 0.2091 -0.0516 0.0087  0.0360  164  LEU   A CD2 
3752 N  N   A VAL   A 165 ? 0.1350 0.2561 0.1719 -0.0440 0.0117  0.0546  165  VAL   A N   
3753 N  N   B VAL   A 165 ? 0.1336 0.2385 0.1867 -0.0416 0.0048  0.0446  165  VAL   A N   
3754 C  CA  A VAL   A 165 ? 0.1429 0.2542 0.1719 -0.0411 0.0172  0.0585  165  VAL   A CA  
3755 C  CA  B VAL   A 165 ? 0.1430 0.2315 0.1807 -0.0377 0.0125  0.0497  165  VAL   A CA  
3756 C  C   A VAL   A 165 ? 0.1349 0.2563 0.1731 -0.0362 0.0264  0.0552  165  VAL   A C   
3757 C  C   B VAL   A 165 ? 0.1406 0.2285 0.1850 -0.0357 0.0060  0.0504  165  VAL   A C   
3758 O  O   A VAL   A 165 ? 0.1422 0.2613 0.1748 -0.0308 0.0240  0.0579  165  VAL   A O   
3759 O  O   B VAL   A 165 ? 0.1458 0.2259 0.1921 -0.0373 0.0027  0.0568  165  VAL   A O   
3760 C  CB  A VAL   A 165 ? 0.1578 0.2537 0.1767 -0.0388 0.0176  0.0556  165  VAL   A CB  
3761 C  CB  B VAL   A 165 ? 0.1557 0.2335 0.1855 -0.0288 0.0183  0.0447  165  VAL   A CB  
3762 C  CG1 A VAL   A 165 ? 0.1635 0.2593 0.1815 -0.0413 0.0202  0.0514  165  VAL   A CG1 
3763 C  CG1 B VAL   A 165 ? 0.1590 0.2388 0.1963 -0.0313 0.0233  0.0410  165  VAL   A CG1 
3764 C  CG2 A VAL   A 165 ? 0.1664 0.2509 0.1728 -0.0331 0.0068  0.0666  165  VAL   A CG2 
3765 C  CG2 B VAL   A 165 ? 0.1638 0.2322 0.1772 -0.0186 0.0081  0.0579  165  VAL   A CG2 
3784 N  N   A SER   A 166 ? 0.1210 0.2561 0.1908 -0.0290 0.0250  0.0378  166  SER   A N   
3785 N  N   B SER   A 166 ? 0.1381 0.2297 0.1969 -0.0312 -0.0062 0.0432  166  SER   A N   
3786 C  CA  A SER   A 166 ? 0.1209 0.2627 0.2090 -0.0246 0.0184  0.0305  166  SER   A CA  
3787 C  CA  B SER   A 166 ? 0.1421 0.2373 0.2051 -0.0320 -0.0030 0.0465  166  SER   A CA  
3788 C  C   A SER   A 166 ? 0.1197 0.2654 0.2065 -0.0163 -0.0084 0.0307  166  SER   A C   
3789 C  C   B SER   A 166 ? 0.1424 0.2386 0.2250 -0.0408 -0.0016 0.0420  166  SER   A C   
3790 O  O   A SER   A 166 ? 0.1310 0.2688 0.2314 -0.0176 -0.0138 0.0228  166  SER   A O   
3791 O  O   B SER   A 166 ? 0.1453 0.2323 0.2392 -0.0445 -0.0024 0.0307  166  SER   A O   
3792 C  CB  A SER   A 166 ? 0.1373 0.2736 0.2338 -0.0096 0.0171  0.0151  166  SER   A CB  
3793 C  CB  B SER   A 166 ? 0.1615 0.2483 0.1945 -0.0249 0.0031  0.0523  166  SER   A CB  
3794 O  OG  A SER   A 166 ? 0.1569 0.2861 0.2622 -0.0065 0.0271  0.0190  166  SER   A OG  
3795 O  OG  B SER   A 166 ? 0.1885 0.2590 0.2044 -0.0216 0.0073  0.0546  166  SER   A OG  
3806 N  N   A SER   A 167 ? 0.1255 0.2693 0.1832 -0.0047 -0.0134 0.0267  167  SER   A N   
3807 N  N   B SER   A 167 ? 0.1548 0.2489 0.2336 -0.0381 0.0091  0.0424  167  SER   A N   
3808 C  CA  A SER   A 167 ? 0.1415 0.2721 0.1727 0.0034  -0.0142 0.0156  167  SER   A CA  
3809 C  CA  B SER   A 167 ? 0.1866 0.2637 0.2508 -0.0231 0.0169  0.0351  167  SER   A CA  
3810 C  C   A SER   A 167 ? 0.1457 0.2790 0.1672 0.0059  -0.0055 0.0106  167  SER   A C   
3811 C  C   B SER   A 167 ? 0.1981 0.2738 0.2882 -0.0069 0.0287  0.0300  167  SER   A C   
3812 O  O   A SER   A 167 ? 0.1553 0.2908 0.1479 0.0011  -0.0158 0.0034  167  SER   A O   
3813 O  O   B SER   A 167 ? 0.2239 0.2889 0.3376 -0.0007 0.0342  0.0259  167  SER   A O   
3814 C  CB  A SER   A 167 ? 0.1486 0.2681 0.1701 0.0051  -0.0058 0.0120  167  SER   A CB  
3815 C  CB  B SER   A 167 ? 0.1977 0.2711 0.2398 -0.0207 0.0279  0.0240  167  SER   A CB  
3816 O  OG  A SER   A 167 ? 0.1580 0.2645 0.1724 -0.0036 0.0056  0.0031  167  SER   A OG  
3817 O  OG  B SER   A 167 ? 0.2050 0.2778 0.2278 -0.0150 0.0515  0.0141  167  SER   A OG  
3828 N  N   A PHE   A 168 ? 0.1449 0.2683 0.1599 0.0090  0.0085  0.0173  168  PHE   A N   
3829 N  N   B PHE   A 168 ? 0.1727 0.2612 0.2505 -0.0091 0.0375  0.0271  168  PHE   A N   
3830 C  CA  A PHE   A 168 ? 0.1463 0.2598 0.1837 0.0035  0.0213  0.0252  168  PHE   A CA  
3831 C  CA  B PHE   A 168 ? 0.1603 0.2591 0.2138 -0.0124 0.0368  0.0198  168  PHE   A CA  
3832 C  C   A PHE   A 168 ? 0.1578 0.2638 0.2239 -0.0023 0.0490  0.0176  168  PHE   A C   
3833 C  C   B PHE   A 168 ? 0.1648 0.2599 0.2262 -0.0181 0.0411  0.0155  168  PHE   A C   
3834 O  O   A PHE   A 168 ? 0.1654 0.2710 0.2687 -0.0089 0.0507  0.0256  168  PHE   A O   
3835 O  O   B PHE   A 168 ? 0.1545 0.2563 0.2160 -0.0157 0.0429  0.0120  168  PHE   A O   
3836 C  CB  A PHE   A 168 ? 0.1398 0.2512 0.1648 -0.0035 0.0101  0.0328  168  PHE   A CB  
3837 C  CB  B PHE   A 168 ? 0.1579 0.2639 0.2040 -0.0168 0.0197  0.0227  168  PHE   A CB  
3838 C  CG  A PHE   A 168 ? 0.1356 0.2501 0.1475 -0.0096 0.0060  0.0408  168  PHE   A CG  
3839 C  CG  B PHE   A 168 ? 0.1573 0.2638 0.1918 -0.0220 0.0100  0.0355  168  PHE   A CG  
3840 C  CD1 A PHE   A 168 ? 0.1375 0.2548 0.1507 -0.0173 0.0065  0.0502  168  PHE   A CD1 
3841 C  CD1 B PHE   A 168 ? 0.1595 0.2668 0.1930 -0.0204 0.0076  0.0506  168  PHE   A CD1 
3842 C  CD2 A PHE   A 168 ? 0.1378 0.2492 0.1390 -0.0098 0.0168  0.0389  168  PHE   A CD2 
3843 C  CD2 B PHE   A 168 ? 0.1619 0.2627 0.1831 -0.0180 0.0015  0.0390  168  PHE   A CD2 
3844 C  CE1 A PHE   A 168 ? 0.1302 0.2525 0.1496 -0.0211 0.0082  0.0586  168  PHE   A CE1 
3845 C  CE1 B PHE   A 168 ? 0.1607 0.2700 0.1934 -0.0178 0.0000  0.0524  168  PHE   A CE1 
3846 C  CE2 A PHE   A 168 ? 0.1409 0.2454 0.1485 -0.0149 0.0169  0.0438  168  PHE   A CE2 
3847 C  CE2 B PHE   A 168 ? 0.1680 0.2660 0.1778 -0.0136 -0.0136 0.0475  168  PHE   A CE2 
3848 C  CZ  A PHE   A 168 ? 0.1335 0.2474 0.1494 -0.0197 0.0059  0.0497  168  PHE   A CZ  
3849 C  CZ  B PHE   A 168 ? 0.1690 0.2698 0.1879 -0.0152 -0.0076 0.0491  168  PHE   A CZ  
3868 N  N   A LEU   A 169 ? 0.1773 0.2576 0.2407 -0.0113 0.0542  0.0026  169  LEU   A N   
3869 N  N   B LEU   A 169 ? 0.1748 0.2669 0.2496 -0.0216 0.0413  0.0130  169  LEU   A N   
3870 C  CA  A LEU   A 169 ? 0.2082 0.2584 0.2862 -0.0119 0.0379  -0.0005 169  LEU   A CA  
3871 C  CA  B LEU   A 169 ? 0.1978 0.2833 0.2701 -0.0238 0.0354  0.0018  169  LEU   A CA  
3872 C  C   A LEU   A 169 ? 0.2042 0.2507 0.2915 -0.0160 0.0515  0.0101  169  LEU   A C   
3873 C  C   B LEU   A 169 ? 0.2123 0.2968 0.2761 -0.0175 0.0254  -0.0129 169  LEU   A C   
3874 O  O   A LEU   A 169 ? 0.2153 0.2513 0.3016 -0.0126 0.0411  0.0082  169  LEU   A O   
3875 O  O   B LEU   A 169 ? 0.2072 0.2992 0.2739 -0.0208 0.0129  -0.0163 169  LEU   A O   
3876 C  CB  A LEU   A 169 ? 0.2357 0.2673 0.2936 -0.0041 0.0316  -0.0100 169  LEU   A CB  
3877 C  CB  B LEU   A 169 ? 0.2081 0.2908 0.2802 -0.0260 0.0442  0.0067  169  LEU   A CB  
3878 C  CG  A LEU   A 169 ? 0.2599 0.2734 0.3036 0.0007  0.0249  -0.0230 169  LEU   A CG  
3879 C  CG  B LEU   A 169 ? 0.2239 0.2994 0.2915 -0.0271 0.0548  0.0099  169  LEU   A CG  
3880 C  CD1 A LEU   A 169 ? 0.2678 0.2749 0.3052 0.0011  0.0201  -0.0271 169  LEU   A CD1 
3881 C  CD1 B LEU   A 169 ? 0.2408 0.3115 0.3191 -0.0222 0.0520  0.0098  169  LEU   A CD1 
3882 C  CD2 A LEU   A 169 ? 0.2679 0.2757 0.2990 0.0001  0.0241  -0.0306 169  LEU   A CD2 
3883 C  CD2 B LEU   A 169 ? 0.2237 0.2984 0.2870 -0.0304 0.0640  0.0112  169  LEU   A CD2 
3884 O  OXT A LEU   A 169 ? 0.1895 0.2524 0.2802 -0.0241 0.0760  0.0072  169  LEU   A OXT 
3885 O  OXT B LEU   A 169 ? 0.2312 0.3085 0.2940 -0.0125 0.0243  -0.0147 169  LEU   A OXT 
3908 N  N   A SER   B 1   ? 0.3444 0.3344 0.3204 -0.1005 -0.0804 0.0445  1    SER   B N   
3909 N  N   B SER   B 1   ? 0.3189 0.3144 0.3050 -0.1034 -0.0532 0.0477  1    SER   B N   
3910 C  CA  A SER   B 1   ? 0.3369 0.3380 0.3298 -0.1038 -0.0842 0.0396  1    SER   B CA  
3911 C  CA  B SER   B 1   ? 0.3099 0.3212 0.3151 -0.1071 -0.0566 0.0421  1    SER   B CA  
3912 C  C   A SER   B 1   ? 0.3149 0.3379 0.3117 -0.1065 -0.0926 0.0557  1    SER   B C   
3913 C  C   B SER   B 1   ? 0.2854 0.3240 0.2927 -0.1077 -0.0687 0.0615  1    SER   B C   
3914 O  O   A SER   B 1   ? 0.3210 0.3409 0.2876 -0.1042 -0.0911 0.0543  1    SER   B O   
3915 O  O   B SER   B 1   ? 0.2905 0.3267 0.2648 -0.1061 -0.0607 0.0582  1    SER   B O   
3916 C  CB  A SER   B 1   ? 0.3482 0.3391 0.3393 -0.1037 -0.0759 0.0236  1    SER   B CB  
3917 C  CB  B SER   B 1   ? 0.3206 0.3215 0.3310 -0.1090 -0.0454 0.0218  1    SER   B CB  
3918 O  OG  A SER   B 1   ? 0.3610 0.3471 0.3848 -0.1004 -0.0700 0.0183  1    SER   B OG  
3919 O  OG  B SER   B 1   ? 0.3327 0.3294 0.3797 -0.1075 -0.0425 0.0123  1    SER   B OG  
3934 N  N   A MET   B 2   ? 0.2924 0.3331 0.3175 -0.1068 -0.0890 0.0854  2    MET   B N   
3935 N  N   B MET   B 2   ? 0.2631 0.3220 0.2928 -0.1034 -0.0732 0.1014  2    MET   B N   
3936 C  CA  A MET   B 2   ? 0.2757 0.3334 0.3404 -0.0926 -0.0845 0.1005  2    MET   B CA  
3937 C  CA  B MET   B 2   ? 0.2472 0.3237 0.3044 -0.0816 -0.0796 0.1244  2    MET   B CA  
3938 C  C   A MET   B 2   ? 0.2411 0.3135 0.3092 -0.0809 -0.0970 0.1210  2    MET   B C   
3939 C  C   B MET   B 2   ? 0.2186 0.3083 0.2848 -0.0653 -0.0854 0.1452  2    MET   B C   
3940 O  O   A MET   B 2   ? 0.2370 0.3245 0.3085 -0.0688 -0.1078 0.1258  2    MET   B O   
3941 O  O   B MET   B 2   ? 0.2139 0.3219 0.2940 -0.0530 -0.0900 0.1408  2    MET   B O   
3942 C  CB  A MET   B 2   ? 0.3010 0.3607 0.4172 -0.0776 -0.0604 0.0788  2    MET   B CB  
3943 C  CB  B MET   B 2   ? 0.2682 0.3478 0.3565 -0.0625 -0.0708 0.1122  2    MET   B CB  
3944 C  CG  A MET   B 2   ? 0.3266 0.3855 0.4857 -0.0605 -0.0374 0.0622  2    MET   B CG  
3945 C  CG  B MET   B 2   ? 0.2874 0.3693 0.3919 -0.0421 -0.0597 0.1162  2    MET   B CG  
3946 S  SD  A MET   B 2   ? 0.3514 0.4084 0.5554 -0.0441 -0.0221 0.0517  2    MET   B SD  
3947 S  SD  B MET   B 2   ? 0.3071 0.3925 0.4230 -0.0222 -0.0588 0.1219  2    MET   B SD  
3948 C  CE  A MET   B 2   ? 0.3559 0.4148 0.5600 -0.0422 -0.0166 0.0531  2    MET   B CE  
3949 C  CE  B MET   B 2   ? 0.3100 0.3973 0.4317 -0.0227 -0.0550 0.1150  2    MET   B CE  
3968 N  N   A VAL   B 3   ? 0.2146 0.2791 0.2863 -0.0867 -0.0918 0.1281  3    VAL   B N   
3969 N  N   B VAL   B 3   ? 0.2005 0.2779 0.2702 -0.0659 -0.0779 0.1552  3    VAL   B N   
3970 C  CA  A VAL   B 3   ? 0.2056 0.2497 0.2802 -0.0810 -0.0824 0.1176  3    VAL   B CA  
3971 C  CA  B VAL   B 3   ? 0.2004 0.2548 0.2758 -0.0587 -0.0713 0.1367  3    VAL   B CA  
3972 C  C   A VAL   B 3   ? 0.1864 0.2348 0.2502 -0.0715 -0.0748 0.1056  3    VAL   B C   
3973 C  C   B VAL   B 3   ? 0.1871 0.2439 0.2512 -0.0550 -0.0671 0.1191  3    VAL   B C   
3974 O  O   A VAL   B 3   ? 0.1803 0.2322 0.2468 -0.0726 -0.0763 0.1106  3    VAL   B O   
3975 O  O   B VAL   B 3   ? 0.1851 0.2540 0.2601 -0.0425 -0.0709 0.1276  3    VAL   B O   
3976 C  CB  A VAL   B 3   ? 0.2197 0.2469 0.3197 -0.0789 -0.0722 0.1009  3    VAL   B CB  
3977 C  CB  B VAL   B 3   ? 0.2177 0.2521 0.3172 -0.0544 -0.0596 0.1181  3    VAL   B CB  
3978 C  CG1 A VAL   B 3   ? 0.2279 0.2431 0.3366 -0.0825 -0.0671 0.0983  3    VAL   B CG1 
3979 C  CG1 B VAL   B 3   ? 0.2277 0.2481 0.3345 -0.0582 -0.0537 0.1121  3    VAL   B CG1 
3980 C  CG2 A VAL   B 3   ? 0.2202 0.2505 0.3338 -0.0745 -0.0602 0.1026  3    VAL   B CG2 
3981 C  CG2 B VAL   B 3   ? 0.2192 0.2556 0.3275 -0.0490 -0.0508 0.1194  3    VAL   B CG2 
4000 N  N   . ASN   B 4   ? 0.1779 0.2209 0.2310 -0.0623 -0.0624 0.0928  4    ASN   B N   
4001 C  CA  . ASN   B 4   ? 0.1738 0.2099 0.1846 -0.0612 -0.0486 0.0554  4    ASN   B CA  
4002 C  C   . ASN   B 4   ? 0.1770 0.2274 0.1712 -0.0601 -0.0420 0.0404  4    ASN   B C   
4003 O  O   . ASN   B 4   ? 0.1769 0.2312 0.1930 -0.0565 -0.0310 0.0191  4    ASN   B O   
4004 C  CB  . ASN   B 4   ? 0.1739 0.2051 0.1622 -0.0549 -0.0513 0.0369  4    ASN   B CB  
4005 C  CG  . ASN   B 4   ? 0.1775 0.1899 0.1550 -0.0523 -0.0523 0.0341  4    ASN   B CG  
4006 O  OD1 . ASN   B 4   ? 0.1813 0.1758 0.1630 -0.0501 -0.0539 0.0353  4    ASN   B OD1 
4007 N  ND2 . ASN   B 4   ? 0.1965 0.1953 0.1674 -0.0307 -0.0341 0.0303  4    ASN   B ND2 
4015 N  N   . SER   B 5   ? 0.1930 0.2465 0.1787 -0.0625 -0.0316 0.0369  5    SER   B N   
4016 C  CA  . SER   B 5   ? 0.2182 0.2826 0.2028 -0.0509 -0.0158 0.0343  5    SER   B CA  
4017 C  C   . SER   B 5   ? 0.2399 0.2902 0.2426 -0.0713 0.0096  0.0296  5    SER   B C   
4018 O  O   . SER   B 5   ? 0.2600 0.2818 0.3075 -0.0679 0.0477  0.0277  5    SER   B O   
4019 C  CB  . SER   B 5   ? 0.2286 0.2977 0.2266 -0.0384 -0.0067 0.0484  5    SER   B CB  
4020 O  OG  . SER   B 5   ? 0.2515 0.3203 0.2783 -0.0248 0.0007  0.0489  5    SER   B OG  
4026 N  N   . PHE   B 6   ? 0.2572 0.3116 0.2254 -0.0796 0.0233  0.0404  6    PHE   B N   
4027 C  CA  . PHE   B 6   ? 0.2683 0.3203 0.1941 -0.1003 0.0320  0.0202  6    PHE   B CA  
4028 C  C   . PHE   B 6   ? 0.3269 0.3634 0.2406 -0.1052 0.0655  -0.0023 6    PHE   B C   
4029 O  O   . PHE   B 6   ? 0.3407 0.3950 0.2825 -0.0958 0.0519  -0.0130 6    PHE   B O   
4030 C  CB  . PHE   B 6   ? 0.2400 0.2930 0.1717 -0.0921 0.0126  0.0184  6    PHE   B CB  
4031 C  CG  . PHE   B 6   ? 0.2110 0.2608 0.1674 -0.0850 -0.0051 0.0186  6    PHE   B CG  
4032 C  CD1 . PHE   B 6   ? 0.2129 0.2325 0.1535 -0.0754 -0.0148 0.0140  6    PHE   B CD1 
4033 C  CD2 . PHE   B 6   ? 0.1862 0.2591 0.1709 -0.0706 -0.0057 0.0463  6    PHE   B CD2 
4034 C  CE1 . PHE   B 6   ? 0.2040 0.2099 0.1562 -0.0654 -0.0162 0.0206  6    PHE   B CE1 
4035 C  CE2 . PHE   B 6   ? 0.1876 0.2437 0.2045 -0.0591 -0.0004 0.0473  6    PHE   B CE2 
4036 C  CZ  . PHE   B 6   ? 0.1921 0.2198 0.1850 -0.0593 -0.0098 0.0253  6    PHE   B CZ  
4046 N  N   . SER   B 7   ? 0.3666 0.3551 0.2611 -0.1264 0.1083  -0.0202 7    SER   B N   
4047 C  CA  . SER   B 7   ? 0.4010 0.3679 0.3174 -0.1249 0.1380  -0.0279 7    SER   B CA  
4048 C  C   . SER   B 7   ? 0.4005 0.3472 0.2997 -0.1293 0.1521  -0.0467 7    SER   B C   
4049 O  O   . SER   B 7   ? 0.4046 0.3450 0.3249 -0.1325 0.1505  -0.0539 7    SER   B O   
4050 C  CB  . SER   B 7   ? 0.4246 0.3995 0.3939 -0.1188 0.1500  -0.0204 7    SER   B CB  
4051 O  OG  . SER   B 7   ? 0.4368 0.4215 0.4477 -0.1147 0.1485  -0.0147 7    SER   B OG  
4057 N  N   . GLY   B 8   ? 0.4005 0.3343 0.3055 -0.1171 0.1563  -0.0637 8    GLY   B N   
4058 C  CA  . GLY   B 8   ? 0.3839 0.3124 0.2937 -0.1101 0.1574  -0.0811 8    GLY   B CA  
4059 C  C   . GLY   B 8   ? 0.3585 0.2817 0.2809 -0.1055 0.1569  -0.0811 8    GLY   B C   
4060 O  O   . GLY   B 8   ? 0.3661 0.2853 0.3215 -0.0964 0.1568  -0.0876 8    GLY   B O   
4064 N  N   . TYR   B 9   ? 0.3397 0.2544 0.2578 -0.0952 0.1246  -0.0908 9    TYR   B N   
4065 C  CA  . TYR   B 9   ? 0.3190 0.2229 0.2289 -0.0843 0.0942  -0.0671 9    TYR   B CA  
4066 C  C   . TYR   B 9   ? 0.3178 0.2175 0.2201 -0.0785 0.0651  -0.0510 9    TYR   B C   
4067 O  O   . TYR   B 9   ? 0.3338 0.2375 0.2623 -0.0827 0.0618  -0.0369 9    TYR   B O   
4068 C  CB  . TYR   B 9   ? 0.3074 0.2007 0.2437 -0.0741 0.0845  -0.0631 9    TYR   B CB  
4069 C  CG  . TYR   B 9   ? 0.2972 0.1808 0.2427 -0.0753 0.0782  -0.0622 9    TYR   B CG  
4070 C  CD1 . TYR   B 9   ? 0.3014 0.1783 0.2584 -0.0922 0.0813  -0.0531 9    TYR   B CD1 
4071 C  CD2 . TYR   B 9   ? 0.2835 0.1756 0.2318 -0.0646 0.0691  -0.0630 9    TYR   B CD2 
4072 C  CE1 . TYR   B 9   ? 0.2965 0.1888 0.2530 -0.0958 0.0833  -0.0641 9    TYR   B CE1 
4073 C  CE2 . TYR   B 9   ? 0.2827 0.1782 0.2367 -0.0674 0.0700  -0.0602 9    TYR   B CE2 
4074 C  CZ  . TYR   B 9   ? 0.2874 0.1934 0.2466 -0.0852 0.0791  -0.0708 9    TYR   B CZ  
4075 O  OH  . TYR   B 9   ? 0.2851 0.2080 0.2580 -0.0978 0.0775  -0.0860 9    TYR   B OH  
4085 N  N   . LEU   B 10  ? 0.2985 0.1891 0.2034 -0.0737 0.0415  -0.0465 10   LEU   B N   
4086 C  CA  . LEU   B 10  ? 0.2915 0.1884 0.1952 -0.0773 -0.0008 -0.0379 10   LEU   B CA  
4087 C  C   . LEU   B 10  ? 0.2721 0.1877 0.1906 -0.0760 -0.0232 -0.0353 10   LEU   B C   
4088 O  O   . LEU   B 10  ? 0.2535 0.1899 0.1901 -0.0600 -0.0142 -0.0210 10   LEU   B O   
4089 C  CB  . LEU   B 10  ? 0.3061 0.1874 0.2228 -0.0802 -0.0178 -0.0181 10   LEU   B CB  
4090 C  CG  . LEU   B 10  ? 0.3234 0.1957 0.2582 -0.0813 -0.0473 -0.0089 10   LEU   B CG  
4091 C  CD1 . LEU   B 10  ? 0.3369 0.2079 0.2777 -0.0783 -0.0433 -0.0113 10   LEU   B CD1 
4092 C  CD2 . LEU   B 10  ? 0.3321 0.2014 0.2853 -0.0785 -0.0491 0.0125  10   LEU   B CD2 
4104 N  N   . LYS   B 11  ? 0.2866 0.2132 0.1994 -0.0758 -0.0400 -0.0268 11   LYS   B N   
4105 C  CA  . LYS   B 11  ? 0.3076 0.2416 0.2437 -0.0631 -0.0458 -0.0318 11   LYS   B CA  
4106 C  C   . LYS   B 11  ? 0.2879 0.2192 0.2494 -0.0815 -0.0395 -0.0417 11   LYS   B C   
4107 O  O   . LYS   B 11  ? 0.3041 0.2360 0.2863 -0.0962 -0.0324 -0.0740 11   LYS   B O   
4108 C  CB  . LYS   B 11  ? 0.3433 0.2933 0.3157 -0.0354 -0.0506 -0.0321 11   LYS   B CB  
4109 C  CG  . LYS   B 11  ? 0.3716 0.3260 0.3888 -0.0176 -0.0509 -0.0324 11   LYS   B CG  
4110 C  CD  . LYS   B 11  ? 0.3934 0.3462 0.4579 -0.0064 -0.0471 -0.0322 11   LYS   B CD  
4111 C  CE  . LYS   B 11  ? 0.4091 0.3594 0.5084 -0.0056 -0.0467 -0.0366 11   LYS   B CE  
4112 N  NZ  . LYS   B 11  ? 0.4179 0.3674 0.5354 -0.0074 -0.0485 -0.0362 11   LYS   B NZ  
4126 N  N   . LEU   B 12  ? 0.2509 0.1935 0.2441 -0.0719 -0.0461 -0.0391 12   LEU   B N   
4127 C  CA  . LEU   B 12  ? 0.2290 0.1714 0.2557 -0.0590 -0.0311 -0.0365 12   LEU   B CA  
4128 C  C   . LEU   B 12  ? 0.2103 0.1720 0.2627 -0.0596 -0.0350 -0.0274 12   LEU   B C   
4129 O  O   . LEU   B 12  ? 0.2101 0.1745 0.2813 -0.0657 -0.0480 -0.0238 12   LEU   B O   
4130 C  CB  . LEU   B 12  ? 0.2272 0.1548 0.2529 -0.0439 -0.0204 -0.0316 12   LEU   B CB  
4131 C  CG  . LEU   B 12  ? 0.2257 0.1474 0.2470 -0.0437 -0.0063 -0.0241 12   LEU   B CG  
4132 C  CD1 . LEU   B 12  ? 0.2352 0.1507 0.2466 -0.0282 -0.0054 -0.0048 12   LEU   B CD1 
4133 C  CD2 . LEU   B 12  ? 0.2332 0.1538 0.2623 -0.0460 -0.0054 -0.0337 12   LEU   B CD2 
4145 N  N   . THR   B 13  ? 0.2026 0.1797 0.2553 -0.0581 -0.0419 -0.0369 13   THR   B N   
4146 C  CA  . THR   B 13  ? 0.2019 0.1875 0.2395 -0.0646 -0.0556 -0.0269 13   THR   B CA  
4147 C  C   . THR   B 13  ? 0.2421 0.2077 0.2556 -0.0720 -0.0701 -0.0137 13   THR   B C   
4148 O  O   . THR   B 13  ? 0.2584 0.2086 0.2715 -0.0695 -0.0441 -0.0104 13   THR   B O   
4149 C  CB  . THR   B 13  ? 0.1876 0.1860 0.2405 -0.0555 -0.0478 -0.0154 13   THR   B CB  
4150 O  OG1 . THR   B 13  ? 0.1770 0.1778 0.2541 -0.0520 -0.0331 -0.0139 13   THR   B OG1 
4151 C  CG2 . THR   B 13  ? 0.1948 0.1907 0.2487 -0.0483 -0.0388 -0.0086 13   THR   B CG2 
4159 N  N   A ASP   B 14  ? 0.2514 0.2167 0.2674 -0.0766 -0.0952 -0.0088 14   ASP   B N   
4160 N  N   B ASP   B 14  ? 0.2529 0.2181 0.2643 -0.0742 -0.0916 -0.0021 14   ASP   B N   
4161 C  CA  A ASP   B 14  ? 0.2624 0.2268 0.2980 -0.0738 -0.0982 0.0063  14   ASP   B CA  
4162 C  CA  B ASP   B 14  ? 0.2647 0.2291 0.2901 -0.0699 -0.0934 0.0166  14   ASP   B CA  
4163 C  C   A ASP   B 14  ? 0.2515 0.2077 0.2615 -0.0714 -0.0833 0.0146  14   ASP   B C   
4164 C  C   B ASP   B 14  ? 0.2519 0.2101 0.2603 -0.0684 -0.0854 0.0193  14   ASP   B C   
4165 O  O   A ASP   B 14  ? 0.2691 0.2133 0.2608 -0.0727 -0.0803 0.0185  14   ASP   B O   
4166 O  O   B ASP   B 14  ? 0.2681 0.2147 0.2630 -0.0691 -0.0916 0.0203  14   ASP   B O   
4167 C  CB  A ASP   B 14  ? 0.2817 0.2563 0.3709 -0.0713 -0.1084 0.0042  14   ASP   B CB  
4168 C  CB  B ASP   B 14  ? 0.2873 0.2596 0.3534 -0.0648 -0.0948 0.0232  14   ASP   B CB  
4169 C  CG  A ASP   B 14  ? 0.3053 0.2814 0.4416 -0.0635 -0.1001 -0.0071 14   ASP   B CG  
4170 C  CG  B ASP   B 14  ? 0.3114 0.2861 0.4168 -0.0577 -0.0839 0.0181  14   ASP   B CG  
4171 O  OD1 A ASP   B 14  ? 0.3188 0.2885 0.4576 -0.0646 -0.1000 -0.0185 14   ASP   B OD1 
4172 O  OD1 B ASP   B 14  ? 0.3237 0.2968 0.4286 -0.0569 -0.0772 0.0117  14   ASP   B OD1 
4173 O  OD2 A ASP   B 14  ? 0.3083 0.2912 0.4708 -0.0596 -0.0930 -0.0062 14   ASP   B OD2 
4174 O  OD2 B ASP   B 14  ? 0.3159 0.2937 0.4393 -0.0582 -0.0803 0.0199  14   ASP   B OD2 
4183 N  N   . ASN   B 15  ? 0.2219 0.1858 0.2365 -0.0597 -0.0762 0.0191  15   ASN   B N   
4184 C  CA  . ASN   B 15  ? 0.1766 0.1629 0.2216 -0.0432 -0.0579 0.0063  15   ASN   B CA  
4185 C  C   . ASN   B 15  ? 0.1596 0.1483 0.2124 -0.0327 -0.0401 -0.0002 15   ASN   B C   
4186 O  O   . ASN   B 15  ? 0.1571 0.1414 0.2199 -0.0309 -0.0470 -0.0099 15   ASN   B O   
4187 C  CB  . ASN   B 15  ? 0.1668 0.1589 0.2384 -0.0218 -0.0623 0.0142  15   ASN   B CB  
4188 C  CG  . ASN   B 15  ? 0.1538 0.1550 0.2426 -0.0267 -0.0314 0.0145  15   ASN   B CG  
4189 O  OD1 . ASN   B 15  ? 0.1589 0.1796 0.2760 -0.0437 -0.0406 0.0240  15   ASN   B OD1 
4190 N  ND2 . ASN   B 15  ? 0.1565 0.1351 0.2228 -0.0172 -0.0040 -0.0102 15   ASN   B ND2 
4198 N  N   . VAL   B 16  ? 0.1632 0.1406 0.2131 -0.0336 -0.0458 -0.0040 16   VAL   B N   
4199 C  CA  . VAL   B 16  ? 0.1620 0.1442 0.1983 -0.0330 -0.0376 -0.0172 16   VAL   B CA  
4200 C  C   . VAL   B 16  ? 0.1631 0.1548 0.2017 -0.0403 -0.0341 -0.0080 16   VAL   B C   
4201 O  O   . VAL   B 16  ? 0.1645 0.1670 0.2220 -0.0405 -0.0281 -0.0271 16   VAL   B O   
4202 C  CB  . VAL   B 16  ? 0.1649 0.1377 0.2126 -0.0223 -0.0252 -0.0219 16   VAL   B CB  
4203 C  CG1 . VAL   B 16  ? 0.1712 0.1327 0.2041 -0.0029 -0.0201 -0.0138 16   VAL   B CG1 
4204 C  CG2 . VAL   B 16  ? 0.1708 0.1460 0.2358 -0.0122 -0.0261 -0.0217 16   VAL   B CG2 
4214 N  N   . TYR   B 17  ? 0.1710 0.1571 0.1958 -0.0343 -0.0302 -0.0141 17   TYR   B N   
4215 C  CA  . TYR   B 17  ? 0.1775 0.1709 0.1921 -0.0457 -0.0324 0.0006  17   TYR   B CA  
4216 C  C   . TYR   B 17  ? 0.1704 0.1481 0.1942 -0.0500 -0.0199 -0.0105 17   TYR   B C   
4217 O  O   . TYR   B 17  ? 0.1707 0.1526 0.1983 -0.0388 -0.0252 -0.0338 17   TYR   B O   
4218 C  CB  . TYR   B 17  ? 0.2085 0.2152 0.2030 -0.0345 -0.0313 0.0279  17   TYR   B CB  
4219 C  CG  . TYR   B 17  ? 0.2371 0.2682 0.2413 -0.0224 -0.0477 0.0367  17   TYR   B CG  
4220 C  CD1 . TYR   B 17  ? 0.2548 0.2877 0.2695 -0.0183 -0.0564 0.0535  17   TYR   B CD1 
4221 C  CD2 . TYR   B 17  ? 0.2570 0.2956 0.2730 -0.0118 -0.0548 0.0358  17   TYR   B CD2 
4222 C  CE1 . TYR   B 17  ? 0.2729 0.3116 0.2914 -0.0075 -0.0650 0.0466  17   TYR   B CE1 
4223 C  CE2 . TYR   B 17  ? 0.2723 0.3149 0.2943 0.0008  -0.0672 0.0425  17   TYR   B CE2 
4224 C  CZ  . TYR   B 17  ? 0.2836 0.3285 0.3054 0.0042  -0.0711 0.0452  17   TYR   B CZ  
4225 O  OH  . TYR   B 17  ? 0.2985 0.3473 0.3202 0.0139  -0.0772 0.0437  17   TYR   B OH  
4235 N  N   . ILE   B 18  ? 0.1774 0.1488 0.1880 -0.0431 -0.0041 -0.0209 18   ILE   B N   
4236 C  CA  . ILE   B 18  ? 0.1848 0.1440 0.1807 -0.0419 -0.0002 -0.0272 18   ILE   B CA  
4237 C  C   . ILE   B 18  ? 0.1956 0.1490 0.1845 -0.0499 0.0053  -0.0381 18   ILE   B C   
4238 O  O   . ILE   B 18  ? 0.2187 0.1662 0.1975 -0.0433 0.0074  -0.0405 18   ILE   B O   
4239 C  CB  . ILE   B 18  ? 0.1855 0.1484 0.1885 -0.0448 -0.0035 -0.0214 18   ILE   B CB  
4240 C  CG1 . ILE   B 18  ? 0.1850 0.1497 0.2067 -0.0423 0.0011  -0.0114 18   ILE   B CG1 
4241 C  CG2 . ILE   B 18  ? 0.1873 0.1580 0.1889 -0.0418 -0.0019 -0.0122 18   ILE   B CG2 
4242 C  CD1 . ILE   B 18  ? 0.1960 0.1787 0.2223 -0.0391 -0.0135 0.0141  18   ILE   B CD1 
4254 N  N   . LYS   B 19  ? 0.1981 0.1479 0.2014 -0.0323 0.0385  -0.0420 19   LYS   B N   
4255 C  CA  . LYS   B 19  ? 0.2072 0.1558 0.2261 -0.0371 0.0351  -0.0499 19   LYS   B CA  
4256 C  C   . LYS   B 19  ? 0.1873 0.1514 0.2393 -0.0329 0.0408  -0.0548 19   LYS   B C   
4257 O  O   . LYS   B 19  ? 0.1829 0.1550 0.2144 -0.0222 0.0273  -0.0495 19   LYS   B O   
4258 C  CB  . LYS   B 19  ? 0.2321 0.1782 0.2271 -0.0464 0.0458  -0.0403 19   LYS   B CB  
4259 C  CG  . LYS   B 19  ? 0.2586 0.2029 0.2473 -0.0616 0.0605  -0.0418 19   LYS   B CG  
4260 C  CD  . LYS   B 19  ? 0.2863 0.2336 0.2527 -0.0672 0.0706  -0.0418 19   LYS   B CD  
4261 C  CE  . LYS   B 19  ? 0.3122 0.2565 0.2723 -0.0653 0.0688  -0.0454 19   LYS   B CE  
4262 N  NZ  . LYS   B 19  ? 0.3260 0.2712 0.2737 -0.0651 0.0690  -0.0404 19   LYS   B NZ  
4276 N  N   . ASN   B 20  ? 0.1841 0.1667 0.2742 -0.0251 0.0466  -0.0699 20   ASN   B N   
4277 C  CA  . ASN   B 20  ? 0.1850 0.1782 0.2896 -0.0180 0.0480  -0.0903 20   ASN   B CA  
4278 C  C   . ASN   B 20  ? 0.1829 0.1921 0.2920 -0.0234 0.0611  -0.0961 20   ASN   B C   
4279 O  O   . ASN   B 20  ? 0.2006 0.2258 0.3151 -0.0377 0.0610  -0.0974 20   ASN   B O   
4280 C  CB  . ASN   B 20  ? 0.2144 0.1857 0.3199 0.0038  0.0311  -0.0897 20   ASN   B CB  
4281 C  CG  . ASN   B 20  ? 0.2411 0.1913 0.3467 0.0305  0.0293  -0.0895 20   ASN   B CG  
4282 O  OD1 . ASN   B 20  ? 0.2737 0.2138 0.3652 0.0460  0.0254  -0.0889 20   ASN   B OD1 
4283 N  ND2 . ASN   B 20  ? 0.2330 0.1886 0.3445 0.0301  0.0170  -0.0828 20   ASN   B ND2 
4290 N  N   . ALA   B 21  ? 0.1840 0.1819 0.2863 -0.0276 0.0587  -0.0766 21   ALA   B N   
4291 C  CA  . ALA   B 21  ? 0.1932 0.1854 0.2920 -0.0314 0.0425  -0.0650 21   ALA   B CA  
4292 C  C   . ALA   B 21  ? 0.1914 0.1611 0.2789 -0.0197 0.0432  -0.0479 21   ALA   B C   
4293 O  O   . ALA   B 21  ? 0.1970 0.1531 0.2645 -0.0289 0.0433  -0.0406 21   ALA   B O   
4294 C  CB  . ALA   B 21  ? 0.2054 0.2083 0.2987 -0.0435 0.0440  -0.0551 21   ALA   B CB  
4300 N  N   . ASP   B 22  ? 0.1804 0.1550 0.2682 -0.0188 0.0321  -0.0342 22   ASP   B N   
4301 C  CA  . ASP   B 22  ? 0.1756 0.1492 0.2547 -0.0094 0.0266  -0.0296 22   ASP   B CA  
4302 C  C   . ASP   B 22  ? 0.1662 0.1438 0.2063 -0.0168 0.0203  -0.0142 22   ASP   B C   
4303 O  O   . ASP   B 22  ? 0.1736 0.1478 0.2074 -0.0167 0.0149  -0.0089 22   ASP   B O   
4304 C  CB  . ASP   B 22  ? 0.1788 0.1540 0.2946 -0.0059 0.0320  -0.0153 22   ASP   B CB  
4305 C  CG  . ASP   B 22  ? 0.1787 0.1707 0.3422 0.0009  0.0117  -0.0120 22   ASP   B CG  
4306 O  OD1 . ASP   B 22  ? 0.1873 0.1648 0.3415 0.0045  -0.0111 -0.0141 22   ASP   B OD1 
4307 O  OD2 . ASP   B 22  ? 0.1884 0.2028 0.4010 0.0121  -0.0122 -0.0255 22   ASP   B OD2 
4312 N  N   . ILE   B 23  ? 0.1703 0.1371 0.1828 -0.0142 0.0133  0.0106  23   ILE   B N   
4313 C  CA  . ILE   B 23  ? 0.1612 0.1339 0.1740 -0.0119 0.0034  0.0039  23   ILE   B CA  
4314 C  C   . ILE   B 23  ? 0.1546 0.1338 0.1646 -0.0059 -0.0061 -0.0019 23   ILE   B C   
4315 O  O   . ILE   B 23  ? 0.1469 0.1334 0.1597 -0.0091 -0.0047 0.0067  23   ILE   B O   
4316 C  CB  . ILE   B 23  ? 0.1605 0.1396 0.1763 -0.0199 0.0053  0.0129  23   ILE   B CB  
4317 C  CG1 . ILE   B 23  ? 0.1588 0.1516 0.1883 -0.0145 0.0045  0.0279  23   ILE   B CG1 
4318 C  CG2 . ILE   B 23  ? 0.1694 0.1580 0.1753 -0.0156 0.0035  0.0100  23   ILE   B CG2 
4319 C  CD1 . ILE   B 23  ? 0.1665 0.1662 0.1916 -0.0119 0.0019  0.0249  23   ILE   B CD1 
4331 N  N   . VAL   B 24  ? 0.1547 0.1349 0.1744 -0.0077 -0.0076 0.0042  24   VAL   B N   
4332 C  CA  . VAL   B 24  ? 0.1501 0.1395 0.1917 -0.0057 -0.0164 0.0008  24   VAL   B CA  
4333 C  C   . VAL   B 24  ? 0.1469 0.1440 0.1918 -0.0117 -0.0082 0.0006  24   VAL   B C   
4334 O  O   . VAL   B 24  ? 0.1482 0.1515 0.2082 -0.0197 -0.0087 0.0125  24   VAL   B O   
4335 C  CB  . VAL   B 24  ? 0.1604 0.1565 0.1997 -0.0045 -0.0204 0.0011  24   VAL   B CB  
4336 C  CG1 . VAL   B 24  ? 0.1606 0.1604 0.2353 -0.0081 -0.0261 -0.0051 24   VAL   B CG1 
4337 C  CG2 . VAL   B 24  ? 0.1702 0.1887 0.2068 0.0050  -0.0169 -0.0093 24   VAL   B CG2 
4347 N  N   . GLU   B 25  ? 0.1658 0.1581 0.1999 -0.0107 0.0029  0.0008  25   GLU   B N   
4348 C  CA  . GLU   B 25  ? 0.1788 0.1872 0.2209 -0.0016 0.0155  -0.0076 25   GLU   B CA  
4349 C  C   . GLU   B 25  ? 0.1759 0.1786 0.1862 -0.0135 0.0149  -0.0044 25   GLU   B C   
4350 O  O   . GLU   B 25  ? 0.1815 0.1900 0.1998 -0.0144 0.0182  0.0035  25   GLU   B O   
4351 C  CB  . GLU   B 25  ? 0.2142 0.2354 0.2903 0.0232  0.0319  -0.0117 25   GLU   B CB  
4352 C  CG  . GLU   B 25  ? 0.2612 0.2976 0.4009 0.0331  0.0226  -0.0192 25   GLU   B CG  
4353 C  CD  . GLU   B 25  ? 0.3001 0.3652 0.4923 0.0303  0.0135  -0.0270 25   GLU   B CD  
4354 O  OE1 . GLU   B 25  ? 0.3259 0.3916 0.5166 0.0360  0.0176  -0.0308 25   GLU   B OE1 
4355 O  OE2 . GLU   B 25  ? 0.3230 0.3875 0.5187 0.0263  0.0047  -0.0317 25   GLU   B OE2 
4362 N  N   A GLU   B 26  ? 0.1762 0.1725 0.1679 -0.0267 0.0092  -0.0064 26   GLU   B N   
4363 N  N   B GLU   B 26  ? 0.1729 0.1743 0.1782 -0.0227 0.0104  0.0035  26   GLU   B N   
4364 C  CA  A GLU   B 26  ? 0.1768 0.1806 0.1677 -0.0387 -0.0041 -0.0045 26   GLU   B CA  
4365 C  CA  B GLU   B 26  ? 0.1689 0.1837 0.1912 -0.0303 -0.0031 0.0118  26   GLU   B CA  
4366 C  C   A GLU   B 26  ? 0.1594 0.1827 0.1617 -0.0314 -0.0017 0.0118  26   GLU   B C   
4367 C  C   B GLU   B 26  ? 0.1549 0.1840 0.1707 -0.0258 -0.0002 0.0204  26   GLU   B C   
4368 O  O   A GLU   B 26  ? 0.1716 0.2037 0.1740 -0.0293 -0.0052 0.0178  26   GLU   B O   
4369 O  O   B GLU   B 26  ? 0.1666 0.2048 0.1786 -0.0222 -0.0028 0.0261  26   GLU   B O   
4370 C  CB  A GLU   B 26  ? 0.2053 0.1916 0.1711 -0.0440 -0.0006 -0.0033 26   GLU   B CB  
4371 C  CB  B GLU   B 26  ? 0.1872 0.1970 0.2219 -0.0294 -0.0032 0.0234  26   GLU   B CB  
4372 C  CG  A GLU   B 26  ? 0.2386 0.2076 0.2032 -0.0473 0.0074  -0.0145 26   GLU   B CG  
4373 C  CG  B GLU   B 26  ? 0.2080 0.2167 0.2785 -0.0262 0.0030  0.0190  26   GLU   B CG  
4374 C  CD  A GLU   B 26  ? 0.2576 0.2140 0.1910 -0.0594 0.0259  -0.0288 26   GLU   B CD  
4375 C  CD  B GLU   B 26  ? 0.2108 0.2228 0.2894 -0.0325 0.0162  0.0082  26   GLU   B CD  
4376 O  OE1 A GLU   B 26  ? 0.2625 0.2058 0.1777 -0.0575 0.0577  -0.0357 26   GLU   B OE1 
4377 O  OE1 B GLU   B 26  ? 0.2061 0.2224 0.3241 -0.0404 0.0452  -0.0035 26   GLU   B OE1 
4378 O  OE2 A GLU   B 26  ? 0.2682 0.2316 0.1973 -0.0653 0.0312  -0.0064 26   GLU   B OE2 
4379 O  OE2 B GLU   B 26  ? 0.2092 0.2246 0.2744 -0.0293 0.0162  0.0004  26   GLU   B OE2 
4392 N  N   . ALA   B 27  ? 0.1437 0.1682 0.1579 -0.0253 0.0043  0.0199  27   ALA   B N   
4393 C  CA  . ALA   B 27  ? 0.1451 0.1628 0.1787 -0.0199 -0.0004 0.0304  27   ALA   B CA  
4394 C  C   . ALA   B 27  ? 0.1466 0.1727 0.2053 -0.0181 0.0102  0.0419  27   ALA   B C   
4395 O  O   . ALA   B 27  ? 0.1543 0.1838 0.2125 -0.0063 0.0041  0.0481  27   ALA   B O   
4396 C  CB  . ALA   B 27  ? 0.1555 0.1507 0.1756 -0.0194 0.0028  0.0326  27   ALA   B CB  
4403 N  N   . LYS   B 28  ? 0.1422 0.1861 0.2468 -0.0207 0.0134  0.0609  28   LYS   B N   
4404 C  CA  . LYS   B 28  ? 0.1555 0.2289 0.2668 -0.0128 0.0426  0.0885  28   LYS   B CA  
4405 C  C   . LYS   B 28  ? 0.1777 0.2468 0.2567 -0.0028 0.0502  0.0763  28   LYS   B C   
4406 O  O   . LYS   B 28  ? 0.2067 0.2516 0.2710 -0.0028 0.0574  0.0768  28   LYS   B O   
4407 C  CB  . LYS   B 28  ? 0.1801 0.2687 0.3219 -0.0002 0.0626  0.1159  28   LYS   B CB  
4408 C  CG  . LYS   B 28  ? 0.2119 0.3181 0.3644 0.0090  0.0679  0.1338  28   LYS   B CG  
4409 C  CD  . LYS   B 28  ? 0.2690 0.3755 0.4215 0.0131  0.0864  0.1376  28   LYS   B CD  
4410 C  CE  . LYS   B 28  ? 0.3269 0.4244 0.4765 0.0176  0.0888  0.1420  28   LYS   B CE  
4411 N  NZ  . LYS   B 28  ? 0.3643 0.4513 0.4945 0.0207  0.0833  0.1489  28   LYS   B NZ  
4425 N  N   . LYS   B 29  ? 0.1900 0.2773 0.2513 0.0146  0.0583  0.0583  29   LYS   B N   
4426 C  CA  . LYS   B 29  ? 0.2402 0.3141 0.2813 0.0129  0.0624  0.0591  29   LYS   B CA  
4427 C  C   . LYS   B 29  ? 0.2332 0.3128 0.2497 0.0135  0.0452  0.0692  29   LYS   B C   
4428 O  O   . LYS   B 29  ? 0.2513 0.3338 0.2616 0.0203  0.0414  0.0752  29   LYS   B O   
4429 C  CB  . LYS   B 29  ? 0.3002 0.3522 0.3612 0.0101  0.0665  0.0444  29   LYS   B CB  
4430 C  CG  . LYS   B 29  ? 0.3514 0.3835 0.4566 0.0060  0.0659  0.0346  29   LYS   B CG  
4431 C  CD  . LYS   B 29  ? 0.3957 0.4058 0.5204 -0.0003 0.0734  0.0257  29   LYS   B CD  
4432 C  CE  . LYS   B 29  ? 0.4338 0.4200 0.5618 -0.0058 0.0842  0.0199  29   LYS   B CE  
4433 N  NZ  . LYS   B 29  ? 0.4564 0.4277 0.5931 -0.0092 0.0873  0.0155  29   LYS   B NZ  
4447 N  N   . VAL   B 30  ? 0.2050 0.2891 0.2306 0.0004  0.0328  0.0746  30   VAL   B N   
4448 C  CA  . VAL   B 30  ? 0.1915 0.2779 0.2522 -0.0129 -0.0009 0.0790  30   VAL   B CA  
4449 C  C   . VAL   B 30  ? 0.1706 0.2687 0.2369 -0.0166 0.0032  0.0934  30   VAL   B C   
4450 O  O   . VAL   B 30  ? 0.1852 0.2805 0.2433 -0.0138 -0.0052 0.1059  30   VAL   B O   
4451 C  CB  . VAL   B 30  ? 0.1948 0.2757 0.3089 -0.0296 -0.0295 0.0751  30   VAL   B CB  
4452 C  CG1 . VAL   B 30  ? 0.2022 0.2836 0.3155 -0.0296 -0.0195 0.0719  30   VAL   B CG1 
4453 C  CG2 . VAL   B 30  ? 0.2026 0.2753 0.3299 -0.0387 -0.0421 0.0600  30   VAL   B CG2 
4463 N  N   . LYS   B 31  ? 0.1644 0.2327 0.2652 -0.0309 -0.0045 0.0991  31   LYS   B N   
4464 C  CA  . LYS   B 31  ? 0.1485 0.2290 0.3022 -0.0399 -0.0158 0.1022  31   LYS   B CA  
4465 C  C   . LYS   B 31  ? 0.1415 0.1939 0.2623 -0.0368 -0.0335 0.0884  31   LYS   B C   
4466 O  O   . LYS   B 31  ? 0.1487 0.2066 0.2720 -0.0302 -0.0284 0.1088  31   LYS   B O   
4467 C  CB  . LYS   B 31  ? 0.1681 0.2735 0.3640 -0.0396 0.0103  0.1185  31   LYS   B CB  
4468 C  CG  . LYS   B 31  ? 0.1998 0.3174 0.4132 -0.0382 0.0290  0.1152  31   LYS   B CG  
4469 C  CD  . LYS   B 31  ? 0.2417 0.3667 0.4638 -0.0308 0.0300  0.0983  31   LYS   B CD  
4470 C  CE  . LYS   B 31  ? 0.2756 0.4028 0.5094 -0.0280 0.0259  0.0860  31   LYS   B CE  
4471 N  NZ  . LYS   B 31  ? 0.3048 0.4287 0.5213 -0.0213 0.0177  0.0793  31   LYS   B NZ  
4485 N  N   . PRO   B 32  ? 0.1609 0.1527 0.1994 -0.0400 -0.0441 0.0528  32   PRO   B N   
4486 C  CA  . PRO   B 32  ? 0.1732 0.1490 0.1672 -0.0410 -0.0464 0.0298  32   PRO   B CA  
4487 C  C   . PRO   B 32  ? 0.1809 0.1417 0.1680 -0.0418 -0.0556 0.0344  32   PRO   B C   
4488 O  O   . PRO   B 32  ? 0.1925 0.1429 0.1965 -0.0458 -0.0743 0.0330  32   PRO   B O   
4489 C  CB  . PRO   B 32  ? 0.1863 0.1427 0.1664 -0.0451 -0.0335 0.0170  32   PRO   B CB  
4490 C  CG  . PRO   B 32  ? 0.1995 0.1341 0.1739 -0.0366 -0.0483 0.0267  32   PRO   B CG  
4491 C  CD  . PRO   B 32  ? 0.1844 0.1397 0.1982 -0.0309 -0.0601 0.0304  32   PRO   B CD  
4499 N  N   . THR   B 33  ? 0.1849 0.1297 0.1578 -0.0378 -0.0490 0.0278  33   THR   B N   
4500 C  CA  . THR   B 33  ? 0.1920 0.1352 0.1460 -0.0427 -0.0451 0.0315  33   THR   B CA  
4501 C  C   . THR   B 33  ? 0.1942 0.1273 0.1505 -0.0405 -0.0460 0.0234  33   THR   B C   
4502 O  O   . THR   B 33  ? 0.2177 0.1315 0.1557 -0.0472 -0.0539 0.0186  33   THR   B O   
4503 C  CB  . THR   B 33  ? 0.1980 0.1476 0.1570 -0.0288 -0.0531 0.0278  33   THR   B CB  
4504 O  OG1 . THR   B 33  ? 0.1867 0.1561 0.1632 -0.0270 -0.0503 0.0286  33   THR   B OG1 
4505 C  CG2 . THR   B 33  ? 0.2235 0.1554 0.1725 -0.0180 -0.0499 0.0247  33   THR   B CG2 
4513 N  N   . VAL   B 34  ? 0.1789 0.1252 0.1311 -0.0365 -0.0418 0.0167  34   VAL   B N   
4514 C  CA  . VAL   B 34  ? 0.1607 0.1220 0.1287 -0.0264 -0.0352 0.0084  34   VAL   B CA  
4515 C  C   . VAL   B 34  ? 0.1448 0.1194 0.1198 -0.0305 -0.0203 0.0077  34   VAL   B C   
4516 O  O   . VAL   B 34  ? 0.1602 0.1215 0.1331 -0.0259 -0.0303 0.0073  34   VAL   B O   
4517 C  CB  . VAL   B 34  ? 0.1667 0.1311 0.1556 -0.0089 -0.0263 0.0076  34   VAL   B CB  
4518 C  CG1 . VAL   B 34  ? 0.1611 0.1459 0.1687 -0.0124 -0.0168 0.0005  34   VAL   B CG1 
4519 C  CG2 . VAL   B 34  ? 0.1723 0.1338 0.1842 -0.0138 -0.0276 0.0114  34   VAL   B CG2 
4529 N  N   . VAL   B 35  ? 0.1372 0.1136 0.1174 -0.0240 -0.0130 0.0070  35   VAL   B N   
4530 C  CA  . VAL   B 35  ? 0.1331 0.1142 0.1187 -0.0210 -0.0132 0.0067  35   VAL   B CA  
4531 C  C   . VAL   B 35  ? 0.1238 0.1094 0.1208 -0.0166 -0.0137 0.0048  35   VAL   B C   
4532 O  O   . VAL   B 35  ? 0.1263 0.1161 0.1297 -0.0218 -0.0023 -0.0025 35   VAL   B O   
4533 C  CB  . VAL   B 35  ? 0.1303 0.1302 0.1309 -0.0204 0.0012  0.0068  35   VAL   B CB  
4534 C  CG1 . VAL   B 35  ? 0.1268 0.1431 0.1515 -0.0227 -0.0011 0.0042  35   VAL   B CG1 
4535 C  CG2 . VAL   B 35  ? 0.1351 0.1311 0.1409 -0.0118 0.0012  -0.0014 35   VAL   B CG2 
4545 N  N   . VAL   B 36  ? 0.1248 0.1077 0.1220 -0.0182 -0.0135 0.0048  36   VAL   B N   
4546 C  CA  . VAL   B 36  ? 0.1202 0.1048 0.1200 -0.0118 -0.0086 0.0080  36   VAL   B CA  
4547 C  C   . VAL   B 36  ? 0.1138 0.1079 0.1116 -0.0112 -0.0049 0.0044  36   VAL   B C   
4548 O  O   . VAL   B 36  ? 0.1230 0.1195 0.1384 -0.0084 -0.0042 -0.0017 36   VAL   B O   
4549 C  CB  . VAL   B 36  ? 0.1224 0.1108 0.1200 -0.0139 -0.0033 0.0039  36   VAL   B CB  
4550 C  CG1 . VAL   B 36  ? 0.1207 0.1213 0.1279 -0.0156 -0.0020 0.0109  36   VAL   B CG1 
4551 C  CG2 . VAL   B 36  ? 0.1322 0.1199 0.1356 -0.0141 -0.0176 0.0094  36   VAL   B CG2 
4561 N  N   . ASN   B 37  ? 0.1194 0.1156 0.1128 0.0006  -0.0054 0.0046  37   ASN   B N   
4562 C  CA  . ASN   B 37  ? 0.1200 0.1153 0.1149 0.0024  -0.0072 0.0035  37   ASN   B CA  
4563 C  C   . ASN   B 37  ? 0.1197 0.1148 0.1106 0.0023  -0.0062 0.0065  37   ASN   B C   
4564 O  O   . ASN   B 37  ? 0.1285 0.1210 0.1255 0.0017  0.0028  0.0097  37   ASN   B O   
4565 C  CB  . ASN   B 37  ? 0.1191 0.1171 0.1210 0.0009  -0.0076 -0.0035 37   ASN   B CB  
4566 C  CG  . ASN   B 37  ? 0.1202 0.1204 0.1195 0.0025  -0.0076 0.0036  37   ASN   B CG  
4567 O  OD1 . ASN   B 37  ? 0.1313 0.1233 0.1379 0.0116  -0.0183 0.0000  37   ASN   B OD1 
4568 N  ND2 . ASN   B 37  ? 0.1302 0.1178 0.1254 0.0028  -0.0186 0.0060  37   ASN   B ND2 
4575 N  N   . ALA   B 38  ? 0.1253 0.1169 0.1168 0.0050  0.0060  0.0072  38   ALA   B N   
4576 C  CA  . ALA   B 38  ? 0.1389 0.1199 0.1196 -0.0012 0.0022  0.0074  38   ALA   B CA  
4577 C  C   . ALA   B 38  ? 0.1331 0.1149 0.1216 0.0031  0.0009  0.0120  38   ALA   B C   
4578 O  O   . ALA   B 38  ? 0.1473 0.1249 0.1315 0.0076  -0.0025 0.0067  38   ALA   B O   
4579 C  CB  . ALA   B 38  ? 0.1617 0.1274 0.1345 -0.0041 0.0075  0.0076  38   ALA   B CB  
4585 N  N   . ALA   B 39  ? 0.1314 0.1191 0.1219 0.0082  -0.0045 0.0078  39   ALA   B N   
4586 C  CA  . ALA   B 39  ? 0.1413 0.1207 0.1203 0.0058  -0.0113 0.0068  39   ALA   B CA  
4587 C  C   . ALA   B 39  ? 0.1465 0.1293 0.1130 0.0113  -0.0042 0.0118  39   ALA   B C   
4588 O  O   . ALA   B 39  ? 0.1490 0.1359 0.1341 0.0026  -0.0019 0.0085  39   ALA   B O   
4589 C  CB  . ALA   B 39  ? 0.1406 0.1233 0.1419 -0.0047 -0.0045 0.0015  39   ALA   B CB  
4595 N  N   . ASN   B 40  ? 0.1478 0.1515 0.1177 0.0021  -0.0033 -0.0033 40   ASN   B N   
4596 C  CA  . ASN   B 40  ? 0.1550 0.1500 0.1253 0.0075  -0.0019 -0.0062 40   ASN   B CA  
4597 C  C   . ASN   B 40  ? 0.1608 0.1546 0.1106 0.0127  -0.0060 0.0097  40   ASN   B C   
4598 O  O   . ASN   B 40  ? 0.1539 0.1468 0.1145 0.0130  -0.0120 0.0007  40   ASN   B O   
4599 C  CB  . ASN   B 40  ? 0.1689 0.1462 0.1416 0.0146  -0.0087 0.0098  40   ASN   B CB  
4600 C  CG  . ASN   B 40  ? 0.1754 0.1567 0.1733 0.0077  -0.0233 0.0149  40   ASN   B CG  
4601 O  OD1 . ASN   B 40  ? 0.1717 0.1569 0.2588 0.0030  -0.0365 0.0212  40   ASN   B OD1 
4602 N  ND2 . ASN   B 40  ? 0.1759 0.1609 0.1665 0.0081  -0.0143 0.0145  40   ASN   B ND2 
4609 N  N   . VAL   B 41  ? 0.1714 0.1596 0.1108 0.0177  0.0005  0.0037  41   VAL   B N   
4610 C  CA  . VAL   B 41  ? 0.1773 0.1744 0.1224 0.0109  0.0006  -0.0055 41   VAL   B CA  
4611 C  C   . VAL   B 41  ? 0.1749 0.1696 0.1110 0.0224  -0.0089 -0.0075 41   VAL   B C   
4612 O  O   . VAL   B 41  ? 0.1697 0.1678 0.1243 0.0199  -0.0092 -0.0092 41   VAL   B O   
4613 C  CB  . VAL   B 41  ? 0.1897 0.1935 0.1405 -0.0014 0.0240  -0.0111 41   VAL   B CB  
4614 C  CG1 . VAL   B 41  ? 0.1834 0.1936 0.1557 -0.0069 0.0309  -0.0147 41   VAL   B CG1 
4615 C  CG2 . VAL   B 41  ? 0.2057 0.2100 0.1436 -0.0103 0.0192  -0.0116 41   VAL   B CG2 
4625 N  N   . TYR   B 42  ? 0.1845 0.1669 0.1128 0.0229  -0.0222 -0.0046 42   TYR   B N   
4626 C  CA  . TYR   B 42  ? 0.1842 0.1721 0.1214 0.0220  -0.0249 -0.0188 42   TYR   B CA  
4627 C  C   . TYR   B 42  ? 0.1653 0.1599 0.1347 0.0253  -0.0277 -0.0123 42   TYR   B C   
4628 O  O   . TYR   B 42  ? 0.1650 0.1666 0.1613 0.0216  -0.0319 -0.0154 42   TYR   B O   
4629 C  CB  . TYR   B 42  ? 0.2037 0.1942 0.1437 0.0132  -0.0303 -0.0022 42   TYR   B CB  
4630 C  CG  . TYR   B 42  ? 0.2024 0.1996 0.1333 -0.0028 -0.0326 0.0080  42   TYR   B CG  
4631 C  CD1 . TYR   B 42  ? 0.1951 0.1976 0.0996 -0.0070 -0.0177 0.0050  42   TYR   B CD1 
4632 C  CD2 . TYR   B 42  ? 0.2161 0.2101 0.1740 -0.0061 -0.0147 0.0114  42   TYR   B CD2 
4633 C  CE1 . TYR   B 42  ? 0.2100 0.2150 0.1134 -0.0017 -0.0100 0.0006  42   TYR   B CE1 
4634 C  CE2 . TYR   B 42  ? 0.2197 0.2252 0.1604 -0.0023 0.0072  0.0241  42   TYR   B CE2 
4635 C  CZ  . TYR   B 42  ? 0.2318 0.2373 0.1365 0.0134  0.0126  0.0082  42   TYR   B CZ  
4636 O  OH  . TYR   B 42  ? 0.2662 0.2633 0.1772 0.0329  0.0228  0.0117  42   TYR   B OH  
4646 N  N   . LEU   B 43  ? 0.1587 0.1409 0.1166 0.0158  -0.0194 -0.0080 43   LEU   B N   
4647 C  CA  . LEU   B 43  ? 0.1557 0.1398 0.1168 0.0086  -0.0154 -0.0059 43   LEU   B CA  
4648 C  C   . LEU   B 43  ? 0.1571 0.1426 0.1175 0.0049  -0.0172 0.0011  43   LEU   B C   
4649 O  O   . LEU   B 43  ? 0.1545 0.1436 0.1472 0.0056  -0.0192 0.0078  43   LEU   B O   
4650 C  CB  . LEU   B 43  ? 0.1496 0.1320 0.1343 0.0027  -0.0235 -0.0097 43   LEU   B CB  
4651 C  CG  . LEU   B 43  ? 0.1573 0.1279 0.1430 0.0024  -0.0265 -0.0082 43   LEU   B CG  
4652 C  CD1 . LEU   B 43  ? 0.1624 0.1394 0.1756 0.0029  -0.0345 -0.0083 43   LEU   B CD1 
4653 C  CD2 . LEU   B 43  ? 0.1582 0.1290 0.1553 -0.0028 -0.0302 -0.0043 43   LEU   B CD2 
4665 N  N   . LYS   B 44  ? 0.1567 0.1431 0.1279 0.0074  -0.0084 -0.0010 44   LYS   B N   
4666 C  CA  . LYS   B 44  ? 0.1685 0.1477 0.1354 0.0127  -0.0151 0.0089  44   LYS   B CA  
4667 C  C   . LYS   B 44  ? 0.1587 0.1426 0.1343 0.0180  -0.0120 -0.0002 44   LYS   B C   
4668 O  O   . LYS   B 44  ? 0.1767 0.1421 0.1564 0.0074  -0.0026 0.0004  44   LYS   B O   
4669 C  CB  . LYS   B 44  ? 0.1978 0.1725 0.1569 0.0220  -0.0269 0.0037  44   LYS   B CB  
4670 C  CG  . LYS   B 44  ? 0.2405 0.2005 0.1849 0.0168  -0.0585 0.0078  44   LYS   B CG  
4671 C  CD  . LYS   B 44  ? 0.2770 0.2213 0.2525 0.0008  -0.0655 0.0002  44   LYS   B CD  
4672 C  CE  . LYS   B 44  ? 0.3100 0.2468 0.3049 -0.0081 -0.0698 0.0147  44   LYS   B CE  
4673 N  NZ  . LYS   B 44  ? 0.3226 0.2563 0.3334 -0.0047 -0.0795 0.0356  44   LYS   B NZ  
4687 N  N   . HIS   B 45  ? 0.1479 0.1429 0.1360 0.0098  -0.0132 0.0045  45   HIS   B N   
4688 C  CA  . HIS   B 45  ? 0.1541 0.1424 0.1395 0.0086  -0.0105 -0.0038 45   HIS   B CA  
4689 C  C   . HIS   B 45  ? 0.1780 0.1563 0.1763 0.0186  -0.0210 -0.0087 45   HIS   B C   
4690 O  O   . HIS   B 45  ? 0.1896 0.1908 0.2156 0.0461  0.0030  -0.0026 45   HIS   B O   
4691 C  CB  . HIS   B 45  ? 0.1488 0.1497 0.1435 0.0050  -0.0099 -0.0051 45   HIS   B CB  
4692 C  CG  . HIS   B 45  ? 0.1456 0.1422 0.1340 -0.0031 -0.0081 -0.0009 45   HIS   B CG  
4693 N  ND1 . HIS   B 45  ? 0.1497 0.1342 0.1356 0.0006  -0.0168 -0.0074 45   HIS   B ND1 
4694 C  CD2 . HIS   B 45  ? 0.1549 0.1404 0.1502 -0.0053 -0.0141 -0.0015 45   HIS   B CD2 
4695 C  CE1 . HIS   B 45  ? 0.1596 0.1253 0.1273 0.0006  -0.0228 -0.0075 45   HIS   B CE1 
4696 N  NE2 . HIS   B 45  ? 0.1646 0.1330 0.1384 -0.0006 -0.0157 -0.0053 45   HIS   B NE2 
4704 N  N   A GLY   B 46  ? 0.1877 0.1533 0.2117 0.0169  -0.0377 0.0004  46   GLY   B N   
4705 N  N   B GLY   B 46  ? 0.1902 0.1596 0.2024 0.0165  -0.0341 0.0041  46   GLY   B N   
4706 C  CA  A GLY   B 46  ? 0.1973 0.1640 0.2525 0.0165  -0.0451 0.0053  46   GLY   B CA  
4707 C  CA  B GLY   B 46  ? 0.2026 0.1751 0.2322 0.0148  -0.0409 0.0128  46   GLY   B CA  
4708 C  C   A GLY   B 46  ? 0.1960 0.1758 0.2920 0.0265  -0.0400 0.0059  46   GLY   B C   
4709 C  C   B GLY   B 46  ? 0.2058 0.1926 0.2665 0.0225  -0.0352 0.0198  46   GLY   B C   
4710 O  O   A GLY   B 46  ? 0.1979 0.1779 0.3619 0.0356  -0.0320 -0.0153 46   GLY   B O   
4711 O  O   B GLY   B 46  ? 0.2181 0.2116 0.2979 0.0262  -0.0308 0.0280  46   GLY   B O   
4718 N  N   . GLY   B 47  ? 0.1982 0.1922 0.2657 0.0132  -0.0226 0.0040  47   GLY   B N   
4719 C  CA  . GLY   B 47  ? 0.1796 0.1664 0.2183 0.0036  -0.0140 0.0003  47   GLY   B CA  
4720 C  C   . GLY   B 47  ? 0.1630 0.1452 0.1769 0.0051  -0.0001 0.0059  47   GLY   B C   
4721 O  O   . GLY   B 47  ? 0.1754 0.1340 0.1852 0.0028  -0.0045 0.0132  47   GLY   B O   
4726 N  N   . GLY   B 48  ? 0.1474 0.1363 0.1782 0.0070  -0.0053 0.0137  48   GLY   B N   
4727 C  CA  . GLY   B 48  ? 0.1476 0.1346 0.1746 -0.0019 -0.0040 0.0040  48   GLY   B CA  
4728 C  C   . GLY   B 48  ? 0.1416 0.1313 0.1671 0.0041  0.0036  0.0009  48   GLY   B C   
4729 O  O   . GLY   B 48  ? 0.1362 0.1312 0.1936 0.0016  -0.0114 -0.0005 48   GLY   B O   
4733 N  N   . VAL   B 49  ? 0.1434 0.1358 0.1510 0.0121  0.0032  0.0016  49   VAL   B N   
4734 C  CA  . VAL   B 49  ? 0.1388 0.1449 0.1456 0.0127  -0.0097 -0.0093 49   VAL   B CA  
4735 C  C   . VAL   B 49  ? 0.1324 0.1333 0.1321 0.0104  -0.0034 0.0034  49   VAL   B C   
4736 O  O   . VAL   B 49  ? 0.1459 0.1354 0.1424 0.0043  -0.0036 0.0036  49   VAL   B O   
4737 C  CB  . VAL   B 49  ? 0.1451 0.1648 0.1687 0.0048  -0.0204 -0.0050 49   VAL   B CB  
4738 C  CG1 . VAL   B 49  ? 0.1390 0.1701 0.1687 0.0113  -0.0286 0.0003  49   VAL   B CG1 
4739 C  CG2 . VAL   B 49  ? 0.1639 0.1802 0.1898 -0.0068 -0.0364 -0.0072 49   VAL   B CG2 
4749 N  N   . ALA   B 50  ? 0.1272 0.1306 0.1347 0.0035  -0.0020 0.0038  50   ALA   B N   
4750 C  CA  . ALA   B 50  ? 0.1324 0.1263 0.1335 0.0055  -0.0043 0.0049  50   ALA   B CA  
4751 C  C   . ALA   B 50  ? 0.1348 0.1310 0.1302 0.0083  -0.0031 -0.0004 50   ALA   B C   
4752 O  O   . ALA   B 50  ? 0.1353 0.1283 0.1378 0.0037  -0.0042 0.0003  50   ALA   B O   
4753 C  CB  . ALA   B 50  ? 0.1403 0.1312 0.1298 0.0023  -0.0021 0.0106  50   ALA   B CB  
4759 N  N   . GLY   B 51  ? 0.1337 0.1410 0.1362 0.0141  -0.0124 0.0087  51   GLY   B N   
4760 C  CA  . GLY   B 51  ? 0.1377 0.1451 0.1666 0.0201  -0.0140 0.0083  51   GLY   B CA  
4761 C  C   . GLY   B 51  ? 0.1361 0.1386 0.1589 0.0193  -0.0046 0.0058  51   GLY   B C   
4762 O  O   . GLY   B 51  ? 0.1402 0.1495 0.1764 0.0121  -0.0073 -0.0054 51   GLY   B O   
4766 N  N   . ALA   B 52  ? 0.1364 0.1407 0.1534 0.0179  -0.0034 0.0046  52   ALA   B N   
4767 C  CA  . ALA   B 52  ? 0.1407 0.1449 0.1544 0.0177  0.0043  -0.0039 52   ALA   B CA  
4768 C  C   . ALA   B 52  ? 0.1309 0.1402 0.1503 0.0075  0.0037  0.0008  52   ALA   B C   
4769 O  O   . ALA   B 52  ? 0.1352 0.1437 0.1618 0.0111  0.0047  -0.0003 52   ALA   B O   
4770 C  CB  . ALA   B 52  ? 0.1571 0.1498 0.1613 0.0087  0.0110  -0.0057 52   ALA   B CB  
4776 N  N   . LEU   B 53  ? 0.1283 0.1381 0.1444 0.0176  0.0001  0.0052  53   LEU   B N   
4777 C  CA  . LEU   B 53  ? 0.1296 0.1475 0.1430 0.0130  -0.0039 0.0020  53   LEU   B CA  
4778 C  C   . LEU   B 53  ? 0.1333 0.1391 0.1386 0.0116  0.0033  0.0051  53   LEU   B C   
4779 O  O   . LEU   B 53  ? 0.1399 0.1453 0.1528 -0.0003 0.0053  0.0105  53   LEU   B O   
4780 C  CB  . LEU   B 53  ? 0.1323 0.1486 0.1476 0.0098  -0.0027 0.0133  53   LEU   B CB  
4781 C  CG  . LEU   B 53  ? 0.1279 0.1599 0.1478 0.0030  -0.0031 0.0150  53   LEU   B CG  
4782 C  CD1 . LEU   B 53  ? 0.1415 0.1767 0.1709 0.0134  -0.0030 0.0005  53   LEU   B CD1 
4783 C  CD2 . LEU   B 53  ? 0.1480 0.1945 0.1697 -0.0113 -0.0137 -0.0068 53   LEU   B CD2 
4795 N  N   . ASN   B 54  ? 0.1317 0.1286 0.1394 0.0074  0.0011  0.0064  54   ASN   B N   
4796 C  CA  . ASN   B 54  ? 0.1338 0.1397 0.1488 0.0021  -0.0035 -0.0014 54   ASN   B CA  
4797 C  C   . ASN   B 54  ? 0.1319 0.1442 0.1603 0.0024  0.0004  0.0003  54   ASN   B C   
4798 O  O   . ASN   B 54  ? 0.1284 0.1505 0.1743 -0.0044 0.0044  -0.0019 54   ASN   B O   
4799 C  CB  . ASN   B 54  ? 0.1426 0.1539 0.1578 0.0053  -0.0043 -0.0029 54   ASN   B CB  
4800 C  CG  . ASN   B 54  ? 0.1402 0.1597 0.1551 0.0038  -0.0100 -0.0014 54   ASN   B CG  
4801 O  OD1 . ASN   B 54  ? 0.1338 0.1604 0.1747 0.0010  -0.0147 -0.0190 54   ASN   B OD1 
4802 N  ND2 . ASN   B 54  ? 0.1543 0.1824 0.1858 -0.0056 -0.0313 0.0109  54   ASN   B ND2 
4809 N  N   . LYS   B 55  ? 0.1297 0.1505 0.1833 0.0102  -0.0018 0.0019  55   LYS   B N   
4810 C  CA  . LYS   B 55  ? 0.1332 0.1617 0.1942 0.0183  -0.0061 -0.0062 55   LYS   B CA  
4811 C  C   . LYS   B 55  ? 0.1357 0.1599 0.1971 0.0170  0.0055  -0.0102 55   LYS   B C   
4812 O  O   . LYS   B 55  ? 0.1366 0.1713 0.2136 0.0096  0.0100  -0.0080 55   LYS   B O   
4813 C  CB  . LYS   B 55  ? 0.1448 0.1727 0.2398 0.0288  0.0073  0.0061  55   LYS   B CB  
4814 C  CG  . LYS   B 55  ? 0.1908 0.2003 0.3233 0.0369  0.0277  0.0243  55   LYS   B CG  
4815 C  CD  . LYS   B 55  ? 0.2317 0.2223 0.3920 0.0437  0.0391  0.0375  55   LYS   B CD  
4816 C  CE  . LYS   B 55  ? 0.2565 0.2470 0.4640 0.0406  0.0531  0.0383  55   LYS   B CE  
4817 N  NZ  . LYS   B 55  ? 0.2630 0.2629 0.4993 0.0367  0.0404  0.0473  55   LYS   B NZ  
4831 N  N   . ALA   B 56  ? 0.1362 0.1639 0.1755 0.0117  0.0079  -0.0114 56   ALA   B N   
4832 C  CA  . ALA   B 56  ? 0.1460 0.1813 0.1714 0.0079  0.0094  -0.0096 56   ALA   B CA  
4833 C  C   . ALA   B 56  ? 0.1477 0.1792 0.1683 0.0055  0.0136  -0.0021 56   ALA   B C   
4834 O  O   . ALA   B 56  ? 0.1581 0.1916 0.1845 0.0048  0.0281  0.0031  56   ALA   B O   
4835 C  CB  . ALA   B 56  ? 0.1561 0.1971 0.1865 -0.0103 0.0063  -0.0139 56   ALA   B CB  
4841 N  N   . THR   B 57  ? 0.1419 0.1662 0.1706 0.0020  0.0219  -0.0019 57   THR   B N   
4842 C  CA  . THR   B 57  ? 0.1469 0.1650 0.1689 -0.0025 0.0227  0.0058  57   THR   B CA  
4843 C  C   . THR   B 57  ? 0.1447 0.1755 0.1842 -0.0053 0.0250  0.0017  57   THR   B C   
4844 O  O   . THR   B 57  ? 0.1565 0.1753 0.1947 -0.0160 0.0203  -0.0008 57   THR   B O   
4845 C  CB  . THR   B 57  ? 0.1539 0.1493 0.1492 0.0009  0.0143  0.0106  57   THR   B CB  
4846 O  OG1 . THR   B 57  ? 0.1509 0.1404 0.1705 -0.0030 0.0145  -0.0001 57   THR   B OG1 
4847 C  CG2 . THR   B 57  ? 0.1476 0.1561 0.1606 -0.0042 0.0162  0.0103  57   THR   B CG2 
4855 N  N   . ASN   B 58  ? 0.1361 0.1951 0.2073 -0.0106 0.0097  -0.0183 58   ASN   B N   
4856 C  CA  . ASN   B 58  ? 0.1563 0.2335 0.2545 -0.0274 0.0287  -0.0103 58   ASN   B CA  
4857 C  C   . ASN   B 58  ? 0.1413 0.2103 0.2063 -0.0194 -0.0005 -0.0097 58   ASN   B C   
4858 O  O   . ASN   B 58  ? 0.1519 0.2232 0.2134 -0.0206 0.0016  -0.0172 58   ASN   B O   
4859 C  CB  . ASN   B 58  ? 0.2483 0.3117 0.3865 -0.0415 0.0648  0.0021  58   ASN   B CB  
4860 C  CG  . ASN   B 58  ? 0.3734 0.4000 0.5305 -0.0425 0.0872  0.0238  58   ASN   B CG  
4861 O  OD1 . ASN   B 58  ? 0.3954 0.4124 0.5804 -0.0430 0.0920  0.0285  58   ASN   B OD1 
4862 N  ND2 . ASN   B 58  ? 0.4432 0.4529 0.5789 -0.0424 0.0959  0.0300  58   ASN   B ND2 
4869 N  N   . ASN   B 59  ? 0.1408 0.1923 0.1817 -0.0157 -0.0058 -0.0024 59   ASN   B N   
4870 C  CA  . ASN   B 59  ? 0.1425 0.1978 0.1797 -0.0166 -0.0159 0.0116  59   ASN   B CA  
4871 C  C   . ASN   B 59  ? 0.1338 0.1885 0.1786 -0.0158 -0.0110 -0.0006 59   ASN   B C   
4872 O  O   . ASN   B 59  ? 0.1389 0.1882 0.1798 -0.0162 -0.0117 -0.0014 59   ASN   B O   
4873 C  CB  . ASN   B 59  ? 0.1543 0.2181 0.1904 -0.0047 -0.0219 0.0128  59   ASN   B CB  
4874 C  CG  . ASN   B 59  ? 0.1615 0.2278 0.2010 0.0015  -0.0405 0.0121  59   ASN   B CG  
4875 O  OD1 . ASN   B 59  ? 0.1634 0.2307 0.2073 0.0006  -0.0220 0.0228  59   ASN   B OD1 
4876 N  ND2 . ASN   B 59  ? 0.1699 0.2395 0.2044 -0.0022 -0.0438 0.0017  59   ASN   B ND2 
4883 N  N   . ALA   B 60  ? 0.1342 0.1755 0.1759 -0.0142 -0.0044 -0.0053 60   ALA   B N   
4884 C  CA  . ALA   B 60  ? 0.1447 0.1622 0.1765 -0.0184 -0.0040 0.0017  60   ALA   B CA  
4885 C  C   . ALA   B 60  ? 0.1490 0.1508 0.1514 -0.0101 -0.0029 0.0056  60   ALA   B C   
4886 O  O   . ALA   B 60  ? 0.1532 0.1533 0.1709 -0.0155 0.0010  -0.0065 60   ALA   B O   
4887 C  CB  . ALA   B 60  ? 0.1611 0.1625 0.1931 -0.0168 -0.0043 0.0046  60   ALA   B CB  
4893 N  N   . MET   B 61  ? 0.1400 0.1391 0.1539 -0.0111 -0.0013 0.0010  61   MET   B N   
4894 C  CA  . MET   B 61  ? 0.1330 0.1369 0.1506 -0.0091 -0.0069 0.0023  61   MET   B CA  
4895 C  C   . MET   B 61  ? 0.1369 0.1342 0.1541 -0.0117 -0.0117 0.0080  61   MET   B C   
4896 O  O   . MET   B 61  ? 0.1420 0.1366 0.1443 0.0002  -0.0093 -0.0128 61   MET   B O   
4897 C  CB  . MET   B 61  ? 0.1298 0.1418 0.1485 0.0008  -0.0065 -0.0033 61   MET   B CB  
4898 C  CG  . MET   B 61  ? 0.1284 0.1360 0.1459 0.0010  -0.0075 0.0013  61   MET   B CG  
4899 S  SD  . MET   B 61  ? 0.1316 0.1405 0.1585 -0.0026 -0.0061 -0.0099 61   MET   B SD  
4900 C  CE  . MET   B 61  ? 0.1418 0.1634 0.1585 0.0022  -0.0084 -0.0223 61   MET   B CE  
4910 N  N   . GLN   B 62  ? 0.1371 0.1415 0.1453 -0.0052 -0.0193 0.0023  62   GLN   B N   
4911 C  CA  . GLN   B 62  ? 0.1414 0.1456 0.1461 -0.0003 -0.0149 -0.0012 62   GLN   B CA  
4912 C  C   . GLN   B 62  ? 0.1402 0.1502 0.1547 -0.0010 -0.0306 -0.0103 62   GLN   B C   
4913 O  O   . GLN   B 62  ? 0.1515 0.1519 0.1584 0.0015  -0.0270 -0.0155 62   GLN   B O   
4914 C  CB  . GLN   B 62  ? 0.1470 0.1489 0.1584 0.0029  -0.0115 0.0009  62   GLN   B CB  
4915 C  CG  . GLN   B 62  ? 0.1503 0.1546 0.1534 0.0020  -0.0224 -0.0063 62   GLN   B CG  
4916 C  CD  . GLN   B 62  ? 0.1478 0.1526 0.1388 0.0058  -0.0240 0.0088  62   GLN   B CD  
4917 O  OE1 . GLN   B 62  ? 0.1471 0.1482 0.1631 0.0026  -0.0255 -0.0020 62   GLN   B OE1 
4918 N  NE2 . GLN   B 62  ? 0.1495 0.1576 0.1525 0.0057  -0.0176 -0.0103 62   GLN   B NE2 
4927 N  N   . VAL   B 63  ? 0.1414 0.1555 0.1687 -0.0053 -0.0310 -0.0130 63   VAL   B N   
4928 C  CA  . VAL   B 63  ? 0.1511 0.1569 0.1888 -0.0088 -0.0330 -0.0112 63   VAL   B CA  
4929 C  C   . VAL   B 63  ? 0.1514 0.1472 0.1779 -0.0147 -0.0334 -0.0191 63   VAL   B C   
4930 O  O   . VAL   B 63  ? 0.1628 0.1455 0.1846 -0.0080 -0.0452 -0.0140 63   VAL   B O   
4931 C  CB  . VAL   B 63  ? 0.1511 0.1697 0.2162 -0.0160 -0.0316 -0.0091 63   VAL   B CB  
4932 C  CG1 . VAL   B 63  ? 0.1583 0.1714 0.2292 -0.0312 -0.0234 -0.0069 63   VAL   B CG1 
4933 C  CG2 . VAL   B 63  ? 0.1449 0.1909 0.2306 -0.0090 -0.0318 -0.0147 63   VAL   B CG2 
4943 N  N   . GLU   B 64  ? 0.1476 0.1399 0.1652 -0.0082 -0.0266 -0.0138 64   GLU   B N   
4944 C  CA  . GLU   B 64  ? 0.1523 0.1350 0.1573 -0.0123 -0.0294 -0.0096 64   GLU   B CA  
4945 C  C   . GLU   B 64  ? 0.1468 0.1321 0.1443 -0.0031 -0.0342 -0.0110 64   GLU   B C   
4946 O  O   . GLU   B 64  ? 0.1582 0.1383 0.1478 -0.0073 -0.0275 -0.0141 64   GLU   B O   
4947 C  CB  . GLU   B 64  ? 0.1506 0.1423 0.1531 -0.0171 -0.0189 -0.0045 64   GLU   B CB  
4948 C  CG  . GLU   B 64  ? 0.1575 0.1512 0.1482 -0.0264 -0.0252 -0.0084 64   GLU   B CG  
4949 C  CD  . GLU   B 64  ? 0.1627 0.1585 0.1492 -0.0279 -0.0274 -0.0003 64   GLU   B CD  
4950 O  OE1 . GLU   B 64  ? 0.1662 0.1701 0.1706 -0.0339 -0.0184 -0.0211 64   GLU   B OE1 
4951 O  OE2 . GLU   B 64  ? 0.1787 0.1680 0.1591 -0.0302 -0.0406 -0.0061 64   GLU   B OE2 
4958 N  N   . SER   B 65  ? 0.1454 0.1291 0.1413 -0.0071 -0.0188 -0.0170 65   SER   B N   
4959 C  CA  . SER   B 65  ? 0.1457 0.1309 0.1448 0.0007  -0.0232 -0.0116 65   SER   B CA  
4960 C  C   . SER   B 65  ? 0.1494 0.1310 0.1457 0.0004  -0.0248 -0.0105 65   SER   B C   
4961 O  O   . SER   B 65  ? 0.1559 0.1419 0.1392 -0.0026 -0.0240 -0.0238 65   SER   B O   
4962 C  CB  . SER   B 65  ? 0.1497 0.1404 0.1385 -0.0074 -0.0175 -0.0080 65   SER   B CB  
4963 O  OG  . SER   B 65  ? 0.1513 0.1346 0.1461 -0.0061 -0.0143 -0.0187 65   SER   B OG  
4969 N  N   . ASP   B 66  ? 0.1603 0.1416 0.1461 0.0011  -0.0283 -0.0165 66   ASP   B N   
4970 C  CA  . ASP   B 66  ? 0.1655 0.1506 0.1324 0.0071  -0.0321 -0.0083 66   ASP   B CA  
4971 C  C   . ASP   B 66  ? 0.1677 0.1548 0.1313 -0.0035 -0.0274 -0.0147 66   ASP   B C   
4972 O  O   . ASP   B 66  ? 0.1734 0.1565 0.1422 0.0042  -0.0285 -0.0204 66   ASP   B O   
4973 C  CB  . ASP   B 66  ? 0.1747 0.1652 0.1517 0.0138  -0.0391 -0.0086 66   ASP   B CB  
4974 C  CG  . ASP   B 66  ? 0.2018 0.1800 0.1782 0.0221  -0.0542 -0.0055 66   ASP   B CG  
4975 O  OD1 . ASP   B 66  ? 0.2276 0.1679 0.1892 0.0170  -0.0516 0.0020  66   ASP   B OD1 
4976 O  OD2 . ASP   B 66  ? 0.2167 0.2011 0.2383 0.0422  -0.0494 -0.0125 66   ASP   B OD2 
4981 N  N   . ASP   B 67  ? 0.1613 0.1473 0.1345 -0.0089 -0.0251 -0.0186 67   ASP   B N   
4982 C  CA  . ASP   B 67  ? 0.1735 0.1418 0.1495 -0.0092 -0.0300 -0.0140 67   ASP   B CA  
4983 C  C   . ASP   B 67  ? 0.1711 0.1386 0.1584 -0.0026 -0.0294 -0.0140 67   ASP   B C   
4984 O  O   . ASP   B 67  ? 0.1768 0.1452 0.1761 0.0019  -0.0158 -0.0231 67   ASP   B O   
4985 C  CB  . ASP   B 67  ? 0.1955 0.1523 0.1635 -0.0188 -0.0398 -0.0071 67   ASP   B CB  
4986 C  CG  . ASP   B 67  ? 0.2336 0.1578 0.1669 -0.0171 -0.0650 -0.0091 67   ASP   B CG  
4987 O  OD1 . ASP   B 67  ? 0.2549 0.1645 0.1937 -0.0193 -0.0617 -0.0085 67   ASP   B OD1 
4988 O  OD2 . ASP   B 67  ? 0.2492 0.1682 0.1853 -0.0061 -0.0700 0.0013  67   ASP   B OD2 
4993 N  N   . TYR   B 68  ? 0.1641 0.1431 0.1453 0.0036  -0.0350 -0.0241 68   TYR   B N   
4994 C  CA  . TYR   B 68  ? 0.1614 0.1603 0.1648 0.0127  -0.0349 -0.0315 68   TYR   B CA  
4995 C  C   . TYR   B 68  ? 0.1546 0.1529 0.1728 0.0066  -0.0326 -0.0352 68   TYR   B C   
4996 O  O   . TYR   B 68  ? 0.1612 0.1608 0.1692 0.0097  -0.0315 -0.0422 68   TYR   B O   
4997 C  CB  . TYR   B 68  ? 0.1670 0.1816 0.1612 0.0150  -0.0380 -0.0379 68   TYR   B CB  
4998 C  CG  . TYR   B 68  ? 0.1794 0.1953 0.1686 0.0182  -0.0381 -0.0533 68   TYR   B CG  
4999 C  CD1 . TYR   B 68  ? 0.1819 0.1936 0.1898 0.0020  -0.0301 -0.0565 68   TYR   B CD1 
5000 C  CD2 . TYR   B 68  ? 0.1834 0.2107 0.1813 0.0246  -0.0455 -0.0471 68   TYR   B CD2 
5001 C  CE1 . TYR   B 68  ? 0.1891 0.2058 0.2186 0.0046  -0.0309 -0.0440 68   TYR   B CE1 
5002 C  CE2 . TYR   B 68  ? 0.1848 0.2121 0.1800 0.0229  -0.0360 -0.0553 68   TYR   B CE2 
5003 C  CZ  . TYR   B 68  ? 0.1812 0.2127 0.2066 0.0104  -0.0323 -0.0535 68   TYR   B CZ  
5004 O  OH  . TYR   B 68  ? 0.1743 0.2366 0.2309 0.0100  -0.0273 -0.0373 68   TYR   B OH  
5014 N  N   . ILE   B 69  ? 0.1523 0.1445 0.1607 0.0073  -0.0312 -0.0321 69   ILE   B N   
5015 C  CA  . ILE   B 69  ? 0.1632 0.1494 0.1618 0.0019  -0.0208 -0.0332 69   ILE   B CA  
5016 C  C   . ILE   B 69  ? 0.1620 0.1500 0.1648 0.0055  -0.0309 -0.0296 69   ILE   B C   
5017 O  O   . ILE   B 69  ? 0.1643 0.1595 0.1566 0.0036  -0.0164 -0.0290 69   ILE   B O   
5018 C  CB  . ILE   B 69  ? 0.1692 0.1529 0.1814 -0.0033 0.0034  -0.0319 69   ILE   B CB  
5019 C  CG1 . ILE   B 69  ? 0.1707 0.1564 0.1971 -0.0039 0.0062  -0.0270 69   ILE   B CG1 
5020 C  CG2 . ILE   B 69  ? 0.1831 0.1587 0.1900 -0.0045 0.0052  -0.0233 69   ILE   B CG2 
5021 C  CD1 . ILE   B 69  ? 0.1657 0.1599 0.2170 -0.0182 0.0080  -0.0276 69   ILE   B CD1 
5033 N  N   . ALA   B 70  ? 0.1601 0.1487 0.1599 0.0072  -0.0307 -0.0248 70   ALA   B N   
5034 C  CA  . ALA   B 70  ? 0.1615 0.1521 0.1476 0.0031  -0.0335 -0.0221 70   ALA   B CA  
5035 C  C   . ALA   B 70  ? 0.1683 0.1521 0.1652 -0.0001 -0.0379 -0.0272 70   ALA   B C   
5036 O  O   . ALA   B 70  ? 0.1738 0.1562 0.1618 0.0084  -0.0373 -0.0352 70   ALA   B O   
5037 C  CB  . ALA   B 70  ? 0.1674 0.1634 0.1615 0.0032  -0.0322 -0.0286 70   ALA   B CB  
5043 N  N   . THR   B 71  ? 0.1771 0.1524 0.1694 0.0045  -0.0511 -0.0272 71   THR   B N   
5044 C  CA  . THR   B 71  ? 0.1911 0.1543 0.1885 0.0096  -0.0689 -0.0286 71   THR   B CA  
5045 C  C   . THR   B 71  ? 0.1832 0.1581 0.2128 0.0283  -0.0605 -0.0423 71   THR   B C   
5046 O  O   . THR   B 71  ? 0.1932 0.1667 0.2507 0.0303  -0.0530 -0.0549 71   THR   B O   
5047 C  CB  . THR   B 71  ? 0.2177 0.1749 0.2145 0.0013  -0.0731 -0.0031 71   THR   B CB  
5048 O  OG1 . THR   B 71  ? 0.2307 0.1993 0.2402 -0.0181 -0.0717 0.0210  71   THR   B OG1 
5049 C  CG2 . THR   B 71  ? 0.2385 0.1707 0.2437 0.0070  -0.0614 0.0043  71   THR   B CG2 
5057 N  N   . ASN   B 72  ? 0.1669 0.1649 0.2083 0.0208  -0.0578 -0.0623 72   ASN   B N   
5058 C  CA  . ASN   B 72  ? 0.1690 0.1778 0.2256 0.0241  -0.0429 -0.0722 72   ASN   B CA  
5059 C  C   . ASN   B 72  ? 0.1711 0.1860 0.2258 0.0078  -0.0280 -0.0710 72   ASN   B C   
5060 O  O   . ASN   B 72  ? 0.1709 0.2019 0.2565 0.0079  -0.0146 -0.0707 72   ASN   B O   
5061 C  CB  . ASN   B 72  ? 0.1737 0.1926 0.2327 0.0160  -0.0575 -0.0626 72   ASN   B CB  
5062 C  CG  . ASN   B 72  ? 0.1938 0.2049 0.2444 0.0279  -0.0595 -0.0447 72   ASN   B CG  
5063 O  OD1 . ASN   B 72  ? 0.2145 0.2252 0.2433 0.0195  -0.0501 -0.0429 72   ASN   B OD1 
5064 N  ND2 . ASN   B 72  ? 0.2033 0.2102 0.2984 0.0433  -0.0452 -0.0097 72   ASN   B ND2 
5071 N  N   . GLY   B 73  ? 0.1776 0.1853 0.1968 0.0023  -0.0348 -0.0663 73   GLY   B N   
5072 C  CA  . GLY   B 73  ? 0.1722 0.1949 0.1835 0.0011  -0.0225 -0.0555 73   GLY   B CA  
5073 C  C   . GLY   B 73  ? 0.1638 0.1925 0.1436 0.0070  -0.0213 -0.0513 73   GLY   B C   
5074 O  O   . GLY   B 73  ? 0.1589 0.1761 0.1597 0.0072  -0.0197 -0.0300 73   GLY   B O   
5078 N  N   . PRO   B 74  ? 0.1625 0.2015 0.1384 0.0074  -0.0227 -0.0397 74   PRO   B N   
5079 C  CA  . PRO   B 74  ? 0.1594 0.2033 0.1271 0.0091  -0.0132 -0.0210 74   PRO   B CA  
5080 C  C   . PRO   B 74  ? 0.1503 0.1874 0.1242 0.0088  -0.0138 -0.0152 74   PRO   B C   
5081 O  O   . PRO   B 74  ? 0.1575 0.1918 0.1642 0.0099  -0.0079 -0.0267 74   PRO   B O   
5082 C  CB  . PRO   B 74  ? 0.1746 0.2238 0.1319 0.0058  -0.0065 -0.0105 74   PRO   B CB  
5083 C  CG  . PRO   B 74  ? 0.1919 0.2336 0.1564 0.0101  -0.0053 -0.0117 74   PRO   B CG  
5084 C  CD  . PRO   B 74  ? 0.1894 0.2226 0.1472 0.0103  -0.0045 -0.0251 74   PRO   B CD  
5092 N  N   . LEU   B 75  ? 0.1491 0.1748 0.1191 0.0125  -0.0152 -0.0156 75   LEU   B N   
5093 C  CA  . LEU   B 75  ? 0.1530 0.1779 0.1179 0.0044  -0.0178 -0.0063 75   LEU   B CA  
5094 C  C   . LEU   B 75  ? 0.1580 0.1887 0.1221 0.0075  -0.0090 -0.0018 75   LEU   B C   
5095 O  O   . LEU   B 75  ? 0.1750 0.2006 0.1273 0.0006  -0.0121 0.0073  75   LEU   B O   
5096 C  CB  . LEU   B 75  ? 0.1651 0.1814 0.1143 -0.0046 -0.0239 0.0113  75   LEU   B CB  
5097 C  CG  . LEU   B 75  ? 0.1974 0.1991 0.1260 -0.0264 -0.0140 0.0111  75   LEU   B CG  
5098 C  CD1 . LEU   B 75  ? 0.2266 0.2104 0.1341 -0.0358 0.0095  0.0042  75   LEU   B CD1 
5099 C  CD2 . LEU   B 75  ? 0.2308 0.2200 0.2052 -0.0171 0.0021  0.0151  75   LEU   B CD2 
5111 N  N   . LYS   B 76  ? 0.1535 0.2068 0.1445 0.0053  -0.0032 0.0137  76   LYS   B N   
5112 C  CA  . LYS   B 76  ? 0.1669 0.2115 0.1762 0.0005  0.0182  0.0041  76   LYS   B CA  
5113 C  C   . LYS   B 76  ? 0.1626 0.2003 0.1456 0.0048  0.0130  0.0224  76   LYS   B C   
5114 O  O   . LYS   B 76  ? 0.1639 0.1816 0.1485 0.0047  0.0090  0.0176  76   LYS   B O   
5115 C  CB  . LYS   B 76  ? 0.1825 0.2202 0.2413 -0.0064 0.0368  -0.0323 76   LYS   B CB  
5116 C  CG  . LYS   B 76  ? 0.1905 0.2404 0.2810 0.0025  0.0263  -0.0450 76   LYS   B CG  
5117 C  CD  . LYS   B 76  ? 0.1917 0.2518 0.3121 0.0080  0.0237  -0.0599 76   LYS   B CD  
5118 C  CE  . LYS   B 76  ? 0.1970 0.2691 0.3647 0.0081  0.0062  -0.0722 76   LYS   B CE  
5119 N  NZ  . LYS   B 76  ? 0.1928 0.2781 0.3769 0.0043  -0.0146 -0.0925 76   LYS   B NZ  
5133 N  N   . VAL   B 77  ? 0.1709 0.2115 0.1482 0.0130  0.0097  0.0276  77   VAL   B N   
5134 C  CA  . VAL   B 77  ? 0.1706 0.1999 0.1616 0.0182  0.0185  0.0530  77   VAL   B CA  
5135 C  C   . VAL   B 77  ? 0.1546 0.1759 0.1652 0.0181  0.0277  0.0402  77   VAL   B C   
5136 O  O   . VAL   B 77  ? 0.1590 0.1726 0.1633 0.0250  0.0286  0.0299  77   VAL   B O   
5137 C  CB  . VAL   B 77  ? 0.1824 0.2140 0.1985 0.0162  0.0325  0.0709  77   VAL   B CB  
5138 C  CG1 . VAL   B 77  ? 0.1874 0.2018 0.2268 0.0138  0.0359  0.0922  77   VAL   B CG1 
5139 C  CG2 . VAL   B 77  ? 0.1918 0.2339 0.2203 0.0151  0.0124  0.0739  77   VAL   B CG2 
5149 N  N   . GLY   B 78  ? 0.1479 0.1620 0.1590 0.0143  0.0170  0.0306  78   GLY   B N   
5150 C  CA  . GLY   B 78  ? 0.1477 0.1568 0.1477 0.0117  0.0226  0.0180  78   GLY   B CA  
5151 C  C   . GLY   B 78  ? 0.1419 0.1516 0.1401 0.0089  0.0204  0.0199  78   GLY   B C   
5152 O  O   . GLY   B 78  ? 0.1488 0.1488 0.1528 0.0185  0.0143  0.0244  78   GLY   B O   
5156 N  N   . GLY   B 79  ? 0.1366 0.1577 0.1369 0.0104  0.0128  0.0202  79   GLY   B N   
5157 C  CA  . GLY   B 79  ? 0.1368 0.1482 0.1418 0.0145  0.0082  0.0131  79   GLY   B CA  
5158 C  C   . GLY   B 79  ? 0.1279 0.1369 0.1403 0.0178  0.0057  0.0115  79   GLY   B C   
5159 O  O   . GLY   B 79  ? 0.1369 0.1378 0.1500 0.0132  0.0140  0.0195  79   GLY   B O   
5163 N  N   . SER   B 80  ? 0.1319 0.1325 0.1512 0.0077  0.0152  0.0092  80   SER   B N   
5164 C  CA  . SER   B 80  ? 0.1251 0.1296 0.1432 0.0052  0.0066  0.0059  80   SER   B CA  
5165 C  C   . SER   B 80  ? 0.1309 0.1244 0.1347 0.0082  -0.0029 0.0016  80   SER   B C   
5166 O  O   . SER   B 80  ? 0.1407 0.1287 0.1665 0.0086  0.0039  -0.0003 80   SER   B O   
5167 C  CB  . SER   B 80  ? 0.1352 0.1286 0.1465 0.0002  0.0020  0.0095  80   SER   B CB  
5168 O  OG  . SER   B 80  ? 0.1387 0.1477 0.1658 -0.0017 -0.0114 0.0144  80   SER   B OG  
5174 N  N   . CYS   B 81  ? 0.1284 0.1153 0.1411 0.0035  -0.0065 -0.0065 81   CYS   B N   
5175 C  CA  . CYS   B 81  ? 0.1321 0.1166 0.1503 0.0062  -0.0099 0.0000  81   CYS   B CA  
5176 C  C   . CYS   B 81  ? 0.1331 0.1156 0.1295 0.0018  -0.0156 -0.0034 81   CYS   B C   
5177 O  O   . CYS   B 81  ? 0.1541 0.1141 0.1356 0.0097  0.0006  -0.0041 81   CYS   B O   
5178 C  CB  . CYS   B 81  ? 0.1467 0.1294 0.1526 -0.0046 -0.0150 -0.0045 81   CYS   B CB  
5179 S  SG  . CYS   B 81  ? 0.1474 0.1442 0.1419 -0.0024 -0.0223 -0.0062 81   CYS   B SG  
5185 N  N   . VAL   B 82  ? 0.1370 0.1128 0.1399 0.0016  -0.0151 -0.0007 82   VAL   B N   
5186 C  CA  . VAL   B 82  ? 0.1427 0.1131 0.1309 -0.0008 -0.0100 0.0106  82   VAL   B CA  
5187 C  C   . VAL   B 82  ? 0.1492 0.1052 0.1505 -0.0040 -0.0064 0.0032  82   VAL   B C   
5188 O  O   . VAL   B 82  ? 0.1518 0.1094 0.1761 -0.0045 -0.0075 -0.0125 82   VAL   B O   
5189 C  CB  . VAL   B 82  ? 0.1495 0.1355 0.1548 -0.0020 -0.0140 0.0101  82   VAL   B CB  
5190 C  CG1 . VAL   B 82  ? 0.1704 0.1582 0.1533 0.0020  -0.0128 0.0183  82   VAL   B CG1 
5191 C  CG2 . VAL   B 82  ? 0.1572 0.1503 0.1680 -0.0040 -0.0342 0.0199  82   VAL   B CG2 
5201 N  N   . LEU   B 83  ? 0.1358 0.1090 0.1462 -0.0134 -0.0188 -0.0094 83   LEU   B N   
5202 C  CA  . LEU   B 83  ? 0.1430 0.1178 0.1323 -0.0124 -0.0160 -0.0050 83   LEU   B CA  
5203 C  C   . LEU   B 83  ? 0.1415 0.1158 0.1368 -0.0181 -0.0225 0.0016  83   LEU   B C   
5204 O  O   . LEU   B 83  ? 0.1412 0.1239 0.1235 -0.0222 -0.0138 -0.0000 83   LEU   B O   
5205 C  CB  . LEU   B 83  ? 0.1485 0.1281 0.1308 -0.0122 -0.0210 -0.0066 83   LEU   B CB  
5206 C  CG  . LEU   B 83  ? 0.1670 0.1506 0.1430 -0.0174 -0.0153 -0.0110 83   LEU   B CG  
5207 C  CD1 . LEU   B 83  ? 0.1768 0.1574 0.1396 -0.0115 -0.0209 -0.0059 83   LEU   B CD1 
5208 C  CD2 . LEU   B 83  ? 0.1810 0.1573 0.1613 -0.0076 -0.0174 -0.0190 83   LEU   B CD2 
5220 N  N   . SER   B 84  ? 0.1436 0.1274 0.1572 -0.0260 -0.0181 0.0047  84   SER   B N   
5221 C  CA  . SER   B 84  ? 0.1440 0.1497 0.1367 -0.0254 -0.0123 0.0180  84   SER   B CA  
5222 C  C   . SER   B 84  ? 0.1326 0.1650 0.1105 -0.0216 -0.0132 0.0167  84   SER   B C   
5223 O  O   . SER   B 84  ? 0.1421 0.1483 0.1153 -0.0202 -0.0150 0.0038  84   SER   B O   
5224 C  CB  . SER   B 84  ? 0.1631 0.1532 0.1799 -0.0305 0.0044  0.0121  84   SER   B CB  
5225 O  OG  . SER   B 84  ? 0.1603 0.1662 0.2213 -0.0398 0.0024  0.0219  84   SER   B OG  
5231 N  N   . GLY   B 85  ? 0.1395 0.1815 0.1256 -0.0264 -0.0153 0.0227  85   GLY   B N   
5232 C  CA  . GLY   B 85  ? 0.1376 0.1892 0.1464 -0.0374 -0.0102 -0.0064 85   GLY   B CA  
5233 C  C   . GLY   B 85  ? 0.1379 0.1749 0.1268 -0.0430 -0.0081 0.0047  85   GLY   B C   
5234 O  O   . GLY   B 85  ? 0.1492 0.1757 0.1381 -0.0548 0.0119  -0.0110 85   GLY   B O   
5238 N  N   . HIS   B 86  ? 0.1357 0.1635 0.1439 -0.0323 -0.0166 0.0190  86   HIS   B N   
5239 C  CA  . HIS   B 86  ? 0.1417 0.1654 0.1392 -0.0340 -0.0155 0.0216  86   HIS   B CA  
5240 C  C   . HIS   B 86  ? 0.1398 0.1773 0.1394 -0.0459 -0.0054 0.0305  86   HIS   B C   
5241 O  O   . HIS   B 86  ? 0.1543 0.1842 0.1406 -0.0396 0.0062  0.0262  86   HIS   B O   
5242 C  CB  . HIS   B 86  ? 0.1521 0.1643 0.1570 -0.0249 -0.0203 0.0085  86   HIS   B CB  
5243 C  CG  . HIS   B 86  ? 0.1492 0.1713 0.1431 -0.0167 -0.0138 0.0145  86   HIS   B CG  
5244 N  ND1 . HIS   B 86  ? 0.1608 0.1877 0.1591 -0.0247 -0.0226 -0.0004 86   HIS   B ND1 
5245 C  CD2 . HIS   B 86  ? 0.1558 0.1721 0.1437 -0.0095 -0.0199 0.0098  86   HIS   B CD2 
5246 C  CE1 . HIS   B 86  ? 0.1694 0.1823 0.1493 -0.0173 -0.0094 -0.0215 86   HIS   B CE1 
5247 N  NE2 . HIS   B 86  ? 0.1653 0.1741 0.1337 -0.0015 -0.0109 -0.0006 86   HIS   B NE2 
5255 N  N   . ASN   B 87  ? 0.1369 0.1798 0.1513 -0.0380 0.0022  0.0197  87   ASN   B N   
5256 C  CA  . ASN   B 87  ? 0.1512 0.1942 0.1536 -0.0382 0.0248  0.0167  87   ASN   B CA  
5257 C  C   . ASN   B 87  ? 0.1623 0.1813 0.1406 -0.0319 0.0278  0.0191  87   ASN   B C   
5258 O  O   . ASN   B 87  ? 0.1885 0.1870 0.1709 -0.0249 0.0486  0.0091  87   ASN   B O   
5259 C  CB  . ASN   B 87  ? 0.1513 0.2282 0.1918 -0.0292 0.0317  0.0117  87   ASN   B CB  
5260 C  CG  . ASN   B 87  ? 0.1618 0.2490 0.1935 0.0045  0.0377  0.0256  87   ASN   B CG  
5261 O  OD1 . ASN   B 87  ? 0.1537 0.2352 0.1782 0.0064  0.0453  0.0362  87   ASN   B OD1 
5262 N  ND2 . ASN   B 87  ? 0.1971 0.2629 0.2351 0.0152  0.0438  0.0303  87   ASN   B ND2 
5269 N  N   . LEU   B 88  ? 0.1513 0.1676 0.1303 -0.0346 0.0116  0.0096  88   LEU   B N   
5270 C  CA  . LEU   B 88  ? 0.1627 0.1593 0.1384 -0.0352 0.0067  -0.0026 88   LEU   B CA  
5271 C  C   . LEU   B 88  ? 0.1653 0.1485 0.1424 -0.0426 0.0023  0.0004  88   LEU   B C   
5272 O  O   . LEU   B 88  ? 0.1942 0.1553 0.1635 -0.0262 -0.0227 -0.0047 88   LEU   B O   
5273 C  CB  . LEU   B 88  ? 0.1777 0.1656 0.1533 -0.0402 -0.0085 0.0106  88   LEU   B CB  
5274 C  CG  . LEU   B 88  ? 0.2148 0.1965 0.1732 -0.0253 -0.0254 0.0320  88   LEU   B CG  
5275 C  CD1 . LEU   B 88  ? 0.2235 0.2260 0.1909 -0.0372 -0.0185 0.0475  88   LEU   B CD1 
5276 C  CD2 . LEU   B 88  ? 0.2518 0.2223 0.2349 0.0123  -0.0485 0.0130  88   LEU   B CD2 
5288 N  N   . ALA   B 89  ? 0.1498 0.1538 0.1262 -0.0429 0.0139  0.0030  89   ALA   B N   
5289 C  CA  . ALA   B 89  ? 0.1489 0.1437 0.1169 -0.0409 0.0040  0.0071  89   ALA   B CA  
5290 C  C   . ALA   B 89  ? 0.1630 0.1467 0.1175 -0.0438 0.0116  0.0018  89   ALA   B C   
5291 O  O   . ALA   B 89  ? 0.1476 0.1594 0.1466 -0.0456 0.0169  -0.0272 89   ALA   B O   
5292 C  CB  . ALA   B 89  ? 0.1430 0.1435 0.1336 -0.0371 -0.0003 0.0176  89   ALA   B CB  
5298 N  N   . LYS   B 90  ? 0.1968 0.1360 0.1282 -0.0517 -0.0076 0.0115  90   LYS   B N   
5299 C  CA  . LYS   B 90  ? 0.2108 0.1331 0.1185 -0.0485 -0.0152 0.0075  90   LYS   B CA  
5300 C  C   . LYS   B 90  ? 0.1914 0.1256 0.1378 -0.0469 -0.0125 0.0025  90   LYS   B C   
5301 O  O   . LYS   B 90  ? 0.1973 0.1427 0.1476 -0.0587 -0.0066 0.0066  90   LYS   B O   
5302 C  CB  . LYS   B 90  ? 0.2267 0.1425 0.1392 -0.0416 -0.0022 0.0157  90   LYS   B CB  
5303 C  CG  . LYS   B 90  ? 0.2256 0.1583 0.1481 -0.0231 0.0248  0.0119  90   LYS   B CG  
5304 C  CD  . LYS   B 90  ? 0.2506 0.1790 0.1965 -0.0137 0.0407  -0.0101 90   LYS   B CD  
5305 C  CE  . LYS   B 90  ? 0.2615 0.1912 0.2538 -0.0194 0.0538  -0.0154 90   LYS   B CE  
5306 N  NZ  . LYS   B 90  ? 0.2701 0.1803 0.2477 -0.0272 0.0722  -0.0041 90   LYS   B NZ  
5320 N  N   . HIS   B 91  ? 0.1633 0.1142 0.1239 -0.0343 -0.0190 0.0046  91   HIS   B N   
5321 C  CA  . HIS   B 91  ? 0.1495 0.1179 0.1237 -0.0234 -0.0157 0.0034  91   HIS   B CA  
5322 C  C   . HIS   B 91  ? 0.1410 0.1215 0.1171 -0.0275 -0.0005 -0.0012 91   HIS   B C   
5323 O  O   . HIS   B 91  ? 0.1537 0.1252 0.1158 -0.0266 -0.0183 0.0044  91   HIS   B O   
5324 C  CB  . HIS   B 91  ? 0.1675 0.1214 0.1602 -0.0114 -0.0080 0.0175  91   HIS   B CB  
5325 C  CG  . HIS   B 91  ? 0.2095 0.1425 0.2382 -0.0009 0.0257  0.0290  91   HIS   B CG  
5326 N  ND1 . HIS   B 91  ? 0.2399 0.1506 0.3063 -0.0064 0.0331  0.0191  91   HIS   B ND1 
5327 C  CD2 . HIS   B 91  ? 0.2179 0.1662 0.2907 0.0156  0.0170  0.0599  91   HIS   B CD2 
5328 C  CE1 . HIS   B 91  ? 0.2422 0.1665 0.3183 0.0101  0.0362  0.0251  91   HIS   B CE1 
5329 N  NE2 . HIS   B 91  ? 0.2340 0.1759 0.3128 0.0244  0.0286  0.0632  91   HIS   B NE2 
5337 N  N   . CYS   B 92  ? 0.1324 0.1166 0.1205 -0.0292 -0.0082 0.0008  92   CYS   B N   
5338 C  CA  . CYS   B 92  ? 0.1310 0.1163 0.1143 -0.0202 -0.0017 -0.0013 92   CYS   B CA  
5339 C  C   . CYS   B 92  ? 0.1297 0.1121 0.1076 -0.0155 -0.0045 0.0044  92   CYS   B C   
5340 O  O   . CYS   B 92  ? 0.1382 0.1179 0.1249 -0.0163 -0.0036 -0.0050 92   CYS   B O   
5341 C  CB  . CYS   B 92  ? 0.1324 0.1228 0.1180 -0.0139 -0.0053 -0.0015 92   CYS   B CB  
5342 S  SG  . CYS   B 92  ? 0.1310 0.1250 0.1241 -0.0113 -0.0094 0.0039  92   CYS   B SG  
5348 N  N   . LEU   B 93  ? 0.1202 0.1115 0.1152 -0.0169 -0.0088 -0.0029 93   LEU   B N   
5349 C  CA  . LEU   B 93  ? 0.1166 0.1157 0.1176 -0.0050 -0.0102 0.0052  93   LEU   B CA  
5350 C  C   . LEU   B 93  ? 0.1138 0.1102 0.1143 -0.0039 -0.0093 0.0080  93   LEU   B C   
5351 O  O   . LEU   B 93  ? 0.1217 0.1102 0.1284 -0.0078 -0.0047 0.0042  93   LEU   B O   
5352 C  CB  . LEU   B 93  ? 0.1262 0.1145 0.1296 -0.0023 -0.0081 0.0049  93   LEU   B CB  
5353 C  CG  . LEU   B 93  ? 0.1204 0.1282 0.1431 -0.0053 -0.0050 0.0147  93   LEU   B CG  
5354 C  CD1 . LEU   B 93  ? 0.1251 0.1364 0.1437 0.0011  -0.0044 0.0004  93   LEU   B CD1 
5355 C  CD2 . LEU   B 93  ? 0.1243 0.1226 0.1527 -0.0006 -0.0100 0.0059  93   LEU   B CD2 
5367 N  N   . HIS   B 94  ? 0.1190 0.1113 0.1139 -0.0056 -0.0161 0.0075  94   HIS   B N   
5368 C  CA  . HIS   B 94  ? 0.1234 0.1051 0.1176 0.0031  -0.0038 0.0110  94   HIS   B CA  
5369 C  C   . HIS   B 94  ? 0.1232 0.1103 0.1203 0.0035  -0.0002 0.0108  94   HIS   B C   
5370 O  O   . HIS   B 94  ? 0.1211 0.1214 0.1594 -0.0036 0.0071  -0.0033 94   HIS   B O   
5371 C  CB  . HIS   B 94  ? 0.1216 0.1129 0.1226 -0.0026 -0.0084 0.0028  94   HIS   B CB  
5372 C  CG  . HIS   B 94  ? 0.1255 0.1124 0.1274 -0.0067 -0.0163 -0.0007 94   HIS   B CG  
5373 N  ND1 . HIS   B 94  ? 0.1253 0.1171 0.1241 -0.0049 -0.0163 -0.0003 94   HIS   B ND1 
5374 C  CD2 . HIS   B 94  ? 0.1279 0.1149 0.1255 -0.0011 -0.0195 -0.0023 94   HIS   B CD2 
5375 C  CE1 . HIS   B 94  ? 0.1296 0.1154 0.1300 -0.0104 -0.0189 0.0106  94   HIS   B CE1 
5376 N  NE2 . HIS   B 94  ? 0.1245 0.1220 0.1272 -0.0159 -0.0145 0.0064  94   HIS   B NE2 
5384 N  N   . VAL   B 95  ? 0.1147 0.1064 0.1285 0.0035  0.0012  0.0082  95   VAL   B N   
5385 C  CA  . VAL   B 95  ? 0.1172 0.1150 0.1245 0.0009  0.0010  0.0154  95   VAL   B CA  
5386 C  C   . VAL   B 95  ? 0.1261 0.1169 0.1327 0.0044  0.0068  0.0047  95   VAL   B C   
5387 O  O   . VAL   B 95  ? 0.1305 0.1151 0.1529 0.0082  0.0083  0.0162  95   VAL   B O   
5388 C  CB  . VAL   B 95  ? 0.1186 0.1157 0.1351 -0.0029 -0.0047 0.0093  95   VAL   B CB  
5389 C  CG1 . VAL   B 95  ? 0.1319 0.1347 0.1428 -0.0104 -0.0017 0.0158  95   VAL   B CG1 
5390 C  CG2 . VAL   B 95  ? 0.1276 0.1140 0.1302 0.0008  -0.0134 0.0017  95   VAL   B CG2 
5400 N  N   . VAL   B 96  ? 0.1356 0.1215 0.1350 0.0137  0.0040  0.0159  96   VAL   B N   
5401 C  CA  . VAL   B 96  ? 0.1415 0.1355 0.1262 0.0156  0.0027  0.0224  96   VAL   B CA  
5402 C  C   . VAL   B 96  ? 0.1442 0.1390 0.1330 0.0125  0.0143  0.0171  96   VAL   B C   
5403 O  O   . VAL   B 96  ? 0.1447 0.1426 0.1487 0.0071  0.0228  0.0113  96   VAL   B O   
5404 C  CB  . VAL   B 96  ? 0.1488 0.1562 0.1292 0.0121  0.0071  0.0127  96   VAL   B CB  
5405 C  CG1 . VAL   B 96  ? 0.1463 0.1706 0.1429 0.0178  0.0139  0.0144  96   VAL   B CG1 
5406 C  CG2 . VAL   B 96  ? 0.1597 0.1553 0.1351 0.0067  0.0111  0.0006  96   VAL   B CG2 
5416 N  N   . GLY   B 97  ? 0.1481 0.1413 0.1294 0.0075  0.0066  0.0183  97   GLY   B N   
5417 C  CA  . GLY   B 97  ? 0.1630 0.1438 0.1372 0.0069  0.0071  0.0255  97   GLY   B CA  
5418 C  C   . GLY   B 97  ? 0.1850 0.1542 0.1416 0.0166  0.0087  0.0276  97   GLY   B C   
5419 O  O   . GLY   B 97  ? 0.2007 0.1592 0.1427 0.0130  0.0048  0.0175  97   GLY   B O   
5423 N  N   . PRO   B 98  ? 0.1990 0.1584 0.1695 0.0152  0.0317  0.0382  98   PRO   B N   
5424 C  CA  . PRO   B 98  ? 0.2125 0.1726 0.1797 0.0253  0.0500  0.0395  98   PRO   B CA  
5425 C  C   . PRO   B 98  ? 0.2262 0.1755 0.1485 0.0439  0.0530  0.0557  98   PRO   B C   
5426 O  O   . PRO   B 98  ? 0.2163 0.1734 0.1763 0.0378  0.0520  0.0487  98   PRO   B O   
5427 C  CB  . PRO   B 98  ? 0.2066 0.1790 0.2091 0.0157  0.0562  0.0385  98   PRO   B CB  
5428 C  CG  . PRO   B 98  ? 0.2003 0.1695 0.2057 0.0136  0.0472  0.0576  98   PRO   B CG  
5429 C  CD  . PRO   B 98  ? 0.1845 0.1607 0.1954 0.0154  0.0392  0.0459  98   PRO   B CD  
5437 N  N   . ASN   B 99  ? 0.2386 0.1923 0.1610 0.0594  0.0538  0.0336  99   ASN   B N   
5438 C  CA  . ASN   B 99  ? 0.2605 0.2073 0.1677 0.0641  0.0391  0.0559  99   ASN   B CA  
5439 C  C   . ASN   B 99  ? 0.2898 0.2415 0.1978 0.0621  0.0605  0.0902  99   ASN   B C   
5440 O  O   . ASN   B 99  ? 0.3024 0.2469 0.1977 0.0733  0.0559  0.0958  99   ASN   B O   
5441 C  CB  . ASN   B 99  ? 0.2653 0.2016 0.1633 0.0648  0.0326  0.0441  99   ASN   B CB  
5442 C  CG  . ASN   B 99  ? 0.2706 0.2041 0.1884 0.0612  0.0244  0.0390  99   ASN   B CG  
5443 O  OD1 . ASN   B 99  ? 0.2695 0.2031 0.2194 0.0677  0.0297  0.0517  99   ASN   B OD1 
5444 N  ND2 . ASN   B 99  ? 0.2755 0.2029 0.1979 0.0590  -0.0025 0.0316  99   ASN   B ND2 
5451 N  N   A VAL   B 100 ? 0.3090 0.2558 0.2455 0.0474  0.0569  0.1063  100  VAL   B N   
5452 N  N   B VAL   B 100 ? 0.3082 0.2550 0.2459 0.0463  0.0556  0.1059  100  VAL   B N   
5453 C  CA  A VAL   B 100 ? 0.3350 0.2723 0.2910 0.0349  0.0527  0.1189  100  VAL   B CA  
5454 C  CA  B VAL   B 100 ? 0.3335 0.2706 0.2910 0.0330  0.0505  0.1178  100  VAL   B CA  
5455 C  C   A VAL   B 100 ? 0.3529 0.2776 0.2852 0.0394  0.0515  0.1339  100  VAL   B C   
5456 C  C   B VAL   B 100 ? 0.3518 0.2758 0.2830 0.0377  0.0496  0.1328  100  VAL   B C   
5457 O  O   A VAL   B 100 ? 0.3590 0.2853 0.2912 0.0382  0.0574  0.1289  100  VAL   B O   
5458 O  O   B VAL   B 100 ? 0.3572 0.2815 0.2843 0.0354  0.0545  0.1272  100  VAL   B O   
5459 C  CB  A VAL   B 100 ? 0.3459 0.2858 0.3456 0.0165  0.0500  0.1186  100  VAL   B CB  
5460 C  CB  B VAL   B 100 ? 0.3434 0.2832 0.3454 0.0138  0.0473  0.1181  100  VAL   B CB  
5461 C  CG1 A VAL   B 100 ? 0.3514 0.2907 0.3675 0.0136  0.0484  0.1175  100  VAL   B CG1 
5462 C  CG1 B VAL   B 100 ? 0.3487 0.2875 0.3672 0.0109  0.0456  0.1185  100  VAL   B CG1 
5463 C  CG2 A VAL   B 100 ? 0.3477 0.2911 0.3620 0.0076  0.0502  0.1224  100  VAL   B CG2 
5464 C  CG2 B VAL   B 100 ? 0.3449 0.2884 0.3634 0.0044  0.0470  0.1206  100  VAL   B CG2 
5483 N  N   . ASN   B 101 ? 0.3654 0.2811 0.2878 0.0455  0.0400  0.1395  101  ASN   B N   
5484 C  CA  . ASN   B 101 ? 0.4008 0.2945 0.2947 0.0534  0.0122  0.1454  101  ASN   B CA  
5485 C  C   . ASN   B 101 ? 0.4450 0.3281 0.2971 0.0571  -0.0003 0.1649  101  ASN   B C   
5486 O  O   . ASN   B 101 ? 0.4523 0.3420 0.3258 0.0629  0.0023  0.1367  101  ASN   B O   
5487 C  CB  . ASN   B 101 ? 0.3960 0.2781 0.3182 0.0484  0.0105  0.1208  101  ASN   B CB  
5488 C  CG  . ASN   B 101 ? 0.3925 0.2586 0.3268 0.0474  0.0102  0.1152  101  ASN   B CG  
5489 O  OD1 . ASN   B 101 ? 0.3947 0.2567 0.3480 0.0378  0.0257  0.1099  101  ASN   B OD1 
5490 N  ND2 . ASN   B 101 ? 0.3903 0.2547 0.3159 0.0498  0.0047  0.1001  101  ASN   B ND2 
5498 N  N   . LYS   B 102 ? 0.4792 0.3609 0.3205 0.0458  0.0061  0.1611  102  LYS   B N   
5499 C  CA  . LYS   B 102 ? 0.5100 0.4047 0.3493 0.0297  0.0138  0.1234  102  LYS   B CA  
5500 C  C   . LYS   B 102 ? 0.5052 0.4080 0.3302 0.0268  0.0217  0.1297  102  LYS   B C   
5501 O  O   . LYS   B 102 ? 0.5160 0.4137 0.3486 0.0279  0.0034  0.1242  102  LYS   B O   
5502 C  CB  . LYS   B 102 ? 0.5416 0.4430 0.4159 0.0166  0.0233  0.0726  102  LYS   B CB  
5503 C  CG  . LYS   B 102 ? 0.5690 0.4777 0.4747 0.0052  0.0361  0.0257  102  LYS   B CG  
5504 C  CD  . LYS   B 102 ? 0.5917 0.5066 0.5385 -0.0025 0.0507  -0.0103 102  LYS   B CD  
5505 C  CE  . LYS   B 102 ? 0.6087 0.5266 0.5885 -0.0083 0.0589  -0.0357 102  LYS   B CE  
5506 N  NZ  . LYS   B 102 ? 0.6170 0.5378 0.6181 -0.0104 0.0599  -0.0485 102  LYS   B NZ  
5520 N  N   . GLY   B 103 ? 0.4855 0.4013 0.3273 0.0229  0.0461  0.1275  103  GLY   B N   
5521 C  CA  . GLY   B 103 ? 0.4638 0.3943 0.3428 0.0238  0.0634  0.1027  103  GLY   B CA  
5522 C  C   . GLY   B 103 ? 0.4392 0.3831 0.3453 0.0239  0.0769  0.0790  103  GLY   B C   
5523 O  O   . GLY   B 103 ? 0.4441 0.3901 0.3483 0.0250  0.0838  0.0824  103  GLY   B O   
5527 N  N   A GLU   B 104 ? 0.4237 0.3743 0.3388 0.0248  0.0806  0.0632  104  GLU   B N   
5528 N  N   B GLU   B 104 ? 0.4219 0.3702 0.3368 0.0212  0.0778  0.0645  104  GLU   B N   
5529 C  CA  A GLU   B 104 ? 0.4065 0.3642 0.3266 0.0283  0.0812  0.0451  104  GLU   B CA  
5530 C  CA  B GLU   B 104 ? 0.4031 0.3561 0.3224 0.0210  0.0756  0.0480  104  GLU   B CA  
5531 C  C   A GLU   B 104 ? 0.4080 0.3652 0.3452 0.0169  0.1083  0.0463  104  GLU   B C   
5532 C  C   B GLU   B 104 ? 0.4025 0.3555 0.3398 0.0122  0.1014  0.0501  104  GLU   B C   
5533 O  O   A GLU   B 104 ? 0.4110 0.3700 0.3609 0.0131  0.1058  0.0446  104  GLU   B O   
5534 O  O   B GLU   B 104 ? 0.4059 0.3593 0.3571 0.0088  0.0983  0.0467  104  GLU   B O   
5535 C  CB  A GLU   B 104 ? 0.3903 0.3510 0.3098 0.0440  0.0513  0.0187  104  GLU   B CB  
5536 C  CB  B GLU   B 104 ? 0.3873 0.3407 0.3041 0.0300  0.0439  0.0223  104  GLU   B CB  
5537 C  CG  A GLU   B 104 ? 0.3759 0.3413 0.2897 0.0603  0.0210  -0.0105 104  GLU   B CG  
5538 C  CG  B GLU   B 104 ? 0.3737 0.3288 0.2827 0.0397  0.0121  -0.0062 104  GLU   B CG  
5539 C  CD  A GLU   B 104 ? 0.3637 0.3318 0.2655 0.0756  -0.0066 -0.0288 104  GLU   B CD  
5540 C  CD  B GLU   B 104 ? 0.3632 0.3169 0.2568 0.0477  -0.0151 -0.0225 104  GLU   B CD  
5541 O  OE1 A GLU   B 104 ? 0.3526 0.3196 0.2233 0.0869  -0.0054 -0.0345 104  GLU   B OE1 
5542 O  OE1 B GLU   B 104 ? 0.3540 0.3052 0.2202 0.0540  -0.0149 -0.0258 104  GLU   B OE1 
5543 O  OE2 A GLU   B 104 ? 0.3629 0.3356 0.2645 0.0779  -0.0272 -0.0416 104  GLU   B OE2 
5544 O  OE2 B GLU   B 104 ? 0.3621 0.3186 0.2502 0.0478  -0.0361 -0.0348 104  GLU   B OE2 
5557 N  N   A ASP   B 105 ? 0.4036 0.3603 0.3289 0.0102  0.1344  0.0497  105  ASP   B N   
5558 N  N   B ASP   B 105 ? 0.3958 0.3497 0.3165 0.0071  0.1273  0.0563  105  ASP   B N   
5559 C  CA  A ASP   B 105 ? 0.4033 0.3581 0.3396 0.0037  0.1473  0.0404  105  ASP   B CA  
5560 C  CA  B ASP   B 105 ? 0.3935 0.3462 0.3224 0.0020  0.1409  0.0502  105  ASP   B CA  
5561 C  C   A ASP   B 105 ? 0.3909 0.3380 0.2981 -0.0064 0.1616  0.0449  105  ASP   B C   
5562 C  C   B ASP   B 105 ? 0.3829 0.3290 0.2841 -0.0082 0.1550  0.0533  105  ASP   B C   
5563 O  O   A ASP   B 105 ? 0.3863 0.3355 0.2829 -0.0052 0.1731  0.0504  105  ASP   B O   
5564 O  O   B ASP   B 105 ? 0.3773 0.3253 0.2688 -0.0090 0.1666  0.0613  105  ASP   B O   
5565 C  CB  A ASP   B 105 ? 0.4147 0.3748 0.3962 0.0091  0.1419  0.0240  105  ASP   B CB  
5566 C  CB  B ASP   B 105 ? 0.4015 0.3593 0.3696 0.0084  0.1351  0.0389  105  ASP   B CB  
5567 C  CG  A ASP   B 105 ? 0.4245 0.3894 0.4537 0.0100  0.1434  0.0128  105  ASP   B CG  
5568 C  CG  B ASP   B 105 ? 0.4084 0.3699 0.4175 0.0092  0.1374  0.0336  105  ASP   B CG  
5569 O  OD1 A ASP   B 105 ? 0.4255 0.3933 0.4640 0.0062  0.1523  0.0140  105  ASP   B OD1 
5570 O  OD1 B ASP   B 105 ? 0.4091 0.3750 0.4265 0.0042  0.1421  0.0347  105  ASP   B OD1 
5571 O  OD2 A ASP   B 105 ? 0.4293 0.3963 0.4826 0.0136  0.1360  0.0043  105  ASP   B OD2 
5572 O  OD2 B ASP   B 105 ? 0.4097 0.3730 0.4320 0.0112  0.1399  0.0325  105  ASP   B OD2 
5581 N  N   A ILE   B 106 ? 0.3819 0.3187 0.3007 -0.0149 0.1514  0.0443  106  ILE   B N   
5582 N  N   B ILE   B 106 ? 0.3770 0.3146 0.2888 -0.0140 0.1424  0.0474  106  ILE   B N   
5583 C  CA  A ILE   B 106 ? 0.3647 0.2962 0.3085 -0.0264 0.1519  0.0365  106  ILE   B CA  
5584 C  CA  B ILE   B 106 ? 0.3634 0.2987 0.3021 -0.0225 0.1401  0.0340  106  ILE   B CA  
5585 C  C   A ILE   B 106 ? 0.3376 0.2854 0.3046 -0.0211 0.1562  0.0276  106  ILE   B C   
5586 C  C   B ILE   B 106 ? 0.3380 0.2910 0.2993 -0.0174 0.1431  0.0208  106  ILE   B C   
5587 O  O   A ILE   B 106 ? 0.3301 0.2678 0.2977 -0.0242 0.1645  0.0301  106  ILE   B O   
5588 O  O   B ILE   B 106 ? 0.3318 0.2764 0.2916 -0.0213 0.1459  0.0204  106  ILE   B O   
5589 C  CB  A ILE   B 106 ? 0.3752 0.2882 0.3250 -0.0398 0.1451  0.0383  106  ILE   B CB  
5590 C  CB  B ILE   B 106 ? 0.3757 0.2951 0.3203 -0.0332 0.1329  0.0342  106  ILE   B CB  
5591 C  CG1 A ILE   B 106 ? 0.3779 0.2851 0.3236 -0.0368 0.1401  0.0326  106  ILE   B CG1 
5592 C  CG1 B ILE   B 106 ? 0.3804 0.2940 0.3236 -0.0284 0.1257  0.0294  106  ILE   B CG1 
5593 C  CG2 A ILE   B 106 ? 0.3795 0.2883 0.3414 -0.0486 0.1442  0.0418  106  ILE   B CG2 
5594 C  CG2 B ILE   B 106 ? 0.3803 0.2968 0.3387 -0.0414 0.1318  0.0352  106  ILE   B CG2 
5595 C  CD1 A ILE   B 106 ? 0.3786 0.2843 0.3176 -0.0334 0.1380  0.0331  106  ILE   B CD1 
5596 C  CD1 B ILE   B 106 ? 0.3823 0.2944 0.3242 -0.0237 0.1208  0.0282  106  ILE   B CD1 
5619 N  N   A GLN   B 107 ? 0.3213 0.2930 0.3175 -0.0172 0.1488  0.0276  107  GLN   B N   
5620 N  N   B GLN   B 107 ? 0.3224 0.2982 0.3165 -0.0128 0.1379  0.0191  107  GLN   B N   
5621 C  CA  A GLN   B 107 ? 0.3076 0.3034 0.3421 -0.0099 0.1257  0.0241  107  GLN   B CA  
5622 C  CA  B GLN   B 107 ? 0.3090 0.3073 0.3397 -0.0065 0.1208  0.0188  107  GLN   B CA  
5623 C  C   A GLN   B 107 ? 0.2732 0.2810 0.3149 -0.0002 0.1118  0.0174  107  GLN   B C   
5624 C  C   B GLN   B 107 ? 0.2744 0.2841 0.3128 0.0011  0.1104  0.0146  107  GLN   B C   
5625 O  O   A GLN   B 107 ? 0.2667 0.2801 0.3391 0.0040  0.0941  0.0021  107  GLN   B O   
5626 O  O   B GLN   B 107 ? 0.2691 0.2851 0.3357 0.0040  0.0941  -0.0010 107  GLN   B O   
5627 C  CB  A GLN   B 107 ? 0.3363 0.3355 0.4053 -0.0068 0.0977  0.0230  107  GLN   B CB  
5628 C  CB  B GLN   B 107 ? 0.3369 0.3389 0.4013 -0.0029 0.0966  0.0188  107  GLN   B CB  
5629 C  CG  A GLN   B 107 ? 0.3627 0.3637 0.4631 -0.0035 0.0681  0.0238  107  GLN   B CG  
5630 C  CG  B GLN   B 107 ? 0.3628 0.3670 0.4587 0.0006  0.0692  0.0203  107  GLN   B CG  
5631 C  CD  A GLN   B 107 ? 0.3823 0.3848 0.5080 -0.0033 0.0478  0.0270  107  GLN   B CD  
5632 C  CD  B GLN   B 107 ? 0.3821 0.3881 0.5031 0.0011  0.0498  0.0239  107  GLN   B CD  
5633 O  OE1 A GLN   B 107 ? 0.3905 0.3935 0.5252 -0.0048 0.0443  0.0260  107  GLN   B OE1 
5634 O  OE1 B GLN   B 107 ? 0.3901 0.3966 0.5184 -0.0003 0.0466  0.0239  107  GLN   B OE1 
5635 N  NE2 A GLN   B 107 ? 0.3892 0.3911 0.5228 -0.0003 0.0391  0.0308  107  GLN   B NE2 
5636 N  NE2 B GLN   B 107 ? 0.3889 0.3946 0.5187 0.0040  0.0414  0.0273  107  GLN   B NE2 
5653 N  N   . LEU   B 108 ? 0.2481 0.2595 0.2865 0.0162  0.1022  0.0194  108  LEU   B N   
5654 C  CA  . LEU   B 108 ? 0.2218 0.2307 0.2343 0.0295  0.0807  0.0356  108  LEU   B CA  
5655 C  C   . LEU   B 108 ? 0.1861 0.1871 0.2247 0.0304  0.0471  0.0392  108  LEU   B C   
5656 O  O   . LEU   B 108 ? 0.1847 0.1729 0.2063 0.0287  0.0369  0.0325  108  LEU   B O   
5657 C  CB  . LEU   B 108 ? 0.2374 0.2517 0.2165 0.0283  0.0811  0.0474  108  LEU   B CB  
5658 C  CG  . LEU   B 108 ? 0.2527 0.2841 0.2259 0.0289  0.0754  0.0230  108  LEU   B CG  
5659 C  CD1 . LEU   B 108 ? 0.2652 0.2967 0.2149 0.0182  0.0754  0.0241  108  LEU   B CD1 
5660 C  CD2 . LEU   B 108 ? 0.2635 0.2971 0.2360 0.0349  0.0591  0.0097  108  LEU   B CD2 
5673 N  N   . LEU   B 109 ? 0.1674 0.1671 0.2255 0.0202  0.0422  0.0299  109  LEU   B N   
5674 C  CA  . LEU   B 109 ? 0.1449 0.1381 0.2317 0.0140  0.0396  0.0321  109  LEU   B CA  
5675 C  C   . LEU   B 109 ? 0.1384 0.1246 0.2250 0.0064  0.0348  0.0242  109  LEU   B C   
5676 O  O   . LEU   B 109 ? 0.1376 0.1239 0.2088 0.0060  0.0319  0.0346  109  LEU   B O   
5677 C  CB  . LEU   B 109 ? 0.1519 0.1298 0.2419 0.0097  0.0260  0.0374  109  LEU   B CB  
5678 C  CG  . LEU   B 109 ? 0.1526 0.1260 0.2380 0.0060  0.0218  0.0267  109  LEU   B CG  
5679 C  CD1 . LEU   B 109 ? 0.1518 0.1355 0.2192 0.0122  0.0252  0.0261  109  LEU   B CD1 
5680 C  CD2 . LEU   B 109 ? 0.1660 0.1376 0.2489 0.0075  0.0116  0.0282  109  LEU   B CD2 
5692 N  N   . LYS   B 110 ? 0.1357 0.1266 0.2161 0.0005  0.0315  0.0229  110  LYS   B N   
5693 C  CA  . LYS   B 110 ? 0.1292 0.1232 0.2099 0.0003  0.0275  0.0191  110  LYS   B CA  
5694 C  C   . LYS   B 110 ? 0.1273 0.1264 0.1988 0.0060  0.0253  0.0182  110  LYS   B C   
5695 O  O   . LYS   B 110 ? 0.1210 0.1257 0.1982 -0.0043 0.0144  0.0083  110  LYS   B O   
5696 C  CB  . LYS   B 110 ? 0.1319 0.1237 0.2295 -0.0021 0.0308  0.0132  110  LYS   B CB  
5697 C  CG  . LYS   B 110 ? 0.1292 0.1229 0.2434 -0.0047 0.0195  0.0212  110  LYS   B CG  
5698 C  CD  . LYS   B 110 ? 0.1362 0.1262 0.2421 -0.0033 0.0179  0.0173  110  LYS   B CD  
5699 C  CE  . LYS   B 110 ? 0.1351 0.1383 0.2623 -0.0021 0.0157  0.0106  110  LYS   B CE  
5700 N  NZ  . LYS   B 110 ? 0.1327 0.1523 0.2568 -0.0004 0.0043  0.0039  110  LYS   B NZ  
5714 N  N   . SER   B 111 ? 0.1360 0.1267 0.2112 0.0009  0.0301  0.0174  111  SER   B N   
5715 C  CA  . SER   B 111 ? 0.1395 0.1290 0.2026 0.0041  0.0237  0.0208  111  SER   B CA  
5716 C  C   . SER   B 111 ? 0.1325 0.1185 0.1883 -0.0009 0.0143  0.0127  111  SER   B C   
5717 O  O   . SER   B 111 ? 0.1326 0.1251 0.1858 -0.0037 0.0102  0.0100  111  SER   B O   
5718 C  CB  . SER   B 111 ? 0.1529 0.1513 0.2101 0.0055  0.0360  0.0267  111  SER   B CB  
5719 O  OG  . SER   B 111 ? 0.1639 0.1812 0.2170 0.0108  0.0353  0.0259  111  SER   B OG  
5725 N  N   . ALA   B 112 ? 0.1267 0.1249 0.1937 0.0086  0.0205  0.0243  112  ALA   B N   
5726 C  CA  . ALA   B 112 ? 0.1246 0.1322 0.1777 0.0021  0.0066  0.0121  112  ALA   B CA  
5727 C  C   . ALA   B 112 ? 0.1173 0.1204 0.1700 0.0035  0.0070  0.0106  112  ALA   B C   
5728 O  O   . ALA   B 112 ? 0.1195 0.1229 0.1841 -0.0029 0.0068  0.0075  112  ALA   B O   
5729 C  CB  . ALA   B 112 ? 0.1233 0.1373 0.1844 0.0068  0.0106  0.0197  112  ALA   B CB  
5735 N  N   . TYR   B 113 ? 0.1162 0.1120 0.1794 0.0004  0.0156  0.0148  113  TYR   B N   
5736 C  CA  . TYR   B 113 ? 0.1138 0.1101 0.1738 -0.0026 0.0165  0.0065  113  TYR   B CA  
5737 C  C   . TYR   B 113 ? 0.1126 0.1072 0.1693 -0.0051 0.0057  0.0043  113  TYR   B C   
5738 O  O   . TYR   B 113 ? 0.1177 0.1130 0.1564 -0.0024 0.0047  0.0019  113  TYR   B O   
5739 C  CB  . TYR   B 113 ? 0.1207 0.1090 0.1889 -0.0022 0.0190  0.0105  113  TYR   B CB  
5740 C  CG  . TYR   B 113 ? 0.1219 0.1104 0.1991 -0.0048 0.0120  0.0165  113  TYR   B CG  
5741 C  CD1 . TYR   B 113 ? 0.1287 0.1120 0.2176 -0.0069 0.0133  0.0209  113  TYR   B CD1 
5742 C  CD2 . TYR   B 113 ? 0.1317 0.1109 0.1911 -0.0029 0.0067  0.0120  113  TYR   B CD2 
5743 C  CE1 . TYR   B 113 ? 0.1312 0.1135 0.2144 0.0019  0.0180  0.0137  113  TYR   B CE1 
5744 C  CE2 . TYR   B 113 ? 0.1349 0.1056 0.2099 0.0041  0.0183  0.0182  113  TYR   B CE2 
5745 C  CZ  . TYR   B 113 ? 0.1287 0.1089 0.2161 0.0074  0.0159  0.0139  113  TYR   B CZ  
5746 O  OH  . TYR   B 113 ? 0.1332 0.1088 0.2402 0.0116  0.0249  0.0104  113  TYR   B OH  
5756 N  N   . GLU   B 114 ? 0.1134 0.1044 0.1791 -0.0021 0.0105  0.0125  114  GLU   B N   
5757 C  CA  . GLU   B 114 ? 0.1136 0.1049 0.1814 0.0021  0.0052  0.0112  114  GLU   B CA  
5758 C  C   . GLU   B 114 ? 0.1136 0.1094 0.1737 -0.0026 0.0049  0.0087  114  GLU   B C   
5759 O  O   . GLU   B 114 ? 0.1145 0.1088 0.1796 -0.0015 0.0045  0.0119  114  GLU   B O   
5760 C  CB  . GLU   B 114 ? 0.1142 0.1099 0.1941 0.0009  0.0089  0.0111  114  GLU   B CB  
5761 C  CG  . GLU   B 114 ? 0.1200 0.1106 0.2011 -0.0002 0.0097  0.0080  114  GLU   B CG  
5762 C  CD  . GLU   B 114 ? 0.1170 0.1146 0.2058 -0.0049 0.0097  0.0080  114  GLU   B CD  
5763 O  OE1 . GLU   B 114 ? 0.1158 0.1303 0.1890 -0.0061 0.0179  0.0097  114  GLU   B OE1 
5764 O  OE2 . GLU   B 114 ? 0.1151 0.1340 0.2253 -0.0150 0.0131  0.0144  114  GLU   B OE2 
5771 N  N   . ASN   B 115 ? 0.1152 0.1079 0.1684 -0.0085 0.0043  0.0107  115  ASN   B N   
5772 C  CA  . ASN   B 115 ? 0.1199 0.1139 0.1575 -0.0054 -0.0019 0.0113  115  ASN   B CA  
5773 C  C   . ASN   B 115 ? 0.1148 0.1066 0.1621 -0.0090 -0.0047 0.0032  115  ASN   B C   
5774 O  O   . ASN   B 115 ? 0.1234 0.1102 0.1647 -0.0103 0.0033  0.0068  115  ASN   B O   
5775 C  CB  . ASN   B 115 ? 0.1281 0.1218 0.1571 -0.0091 0.0003  0.0065  115  ASN   B CB  
5776 C  CG  . ASN   B 115 ? 0.1353 0.1263 0.1573 -0.0009 -0.0004 0.0065  115  ASN   B CG  
5777 O  OD1 . ASN   B 115 ? 0.1730 0.1393 0.1807 -0.0015 0.0095  -0.0084 115  ASN   B OD1 
5778 N  ND2 . ASN   B 115 ? 0.1325 0.1355 0.1490 0.0001  0.0067  0.0041  115  ASN   B ND2 
5785 N  N   . PHE   B 116 ? 0.1161 0.1108 0.1516 -0.0060 -0.0030 0.0089  116  PHE   B N   
5786 C  CA  . PHE   B 116 ? 0.1178 0.1086 0.1577 -0.0083 -0.0002 0.0063  116  PHE   B CA  
5787 C  C   . PHE   B 116 ? 0.1192 0.0984 0.1555 -0.0071 -0.0007 0.0032  116  PHE   B C   
5788 O  O   . PHE   B 116 ? 0.1243 0.1109 0.1609 -0.0033 -0.0015 0.0059  116  PHE   B O   
5789 C  CB  . PHE   B 116 ? 0.1133 0.1101 0.1509 -0.0026 -0.0110 0.0071  116  PHE   B CB  
5790 C  CG  . PHE   B 116 ? 0.1147 0.1107 0.1480 -0.0051 -0.0001 0.0067  116  PHE   B CG  
5791 C  CD1 . PHE   B 116 ? 0.1209 0.1142 0.1764 -0.0036 0.0008  0.0080  116  PHE   B CD1 
5792 C  CD2 . PHE   B 116 ? 0.1209 0.1179 0.1398 -0.0045 -0.0020 0.0041  116  PHE   B CD2 
5793 C  CE1 . PHE   B 116 ? 0.1226 0.1152 0.1738 -0.0045 -0.0098 0.0064  116  PHE   B CE1 
5794 C  CE2 . PHE   B 116 ? 0.1227 0.1150 0.1518 0.0040  0.0025  -0.0011 116  PHE   B CE2 
5795 C  CZ  . PHE   B 116 ? 0.1161 0.1203 0.1595 -0.0016 -0.0032 0.0085  116  PHE   B CZ  
5805 N  N   . ASN   B 117 ? 0.1180 0.1051 0.1607 -0.0046 -0.0090 0.0066  117  ASN   B N   
5806 C  CA  . ASN   B 117 ? 0.1246 0.1052 0.1553 -0.0003 -0.0080 0.0030  117  ASN   B CA  
5807 C  C   . ASN   B 117 ? 0.1250 0.1083 0.1756 0.0002  -0.0108 0.0038  117  ASN   B C   
5808 O  O   . ASN   B 117 ? 0.1321 0.1145 0.2011 -0.0038 -0.0276 0.0123  117  ASN   B O   
5809 C  CB  . ASN   B 117 ? 0.1242 0.1103 0.1579 -0.0008 -0.0115 -0.0033 117  ASN   B CB  
5810 C  CG  . ASN   B 117 ? 0.1180 0.1101 0.1785 0.0036  -0.0008 0.0017  117  ASN   B CG  
5811 O  OD1 . ASN   B 117 ? 0.1372 0.1143 0.1930 -0.0131 0.0034  -0.0028 117  ASN   B OD1 
5812 N  ND2 . ASN   B 117 ? 0.1267 0.1159 0.1783 -0.0019 0.0003  -0.0001 117  ASN   B ND2 
5819 N  N   . GLN   B 118 ? 0.1265 0.1045 0.1624 -0.0081 -0.0071 0.0002  118  GLN   B N   
5820 C  CA  . GLN   B 118 ? 0.1317 0.1103 0.1824 0.0007  -0.0120 -0.0021 118  GLN   B CA  
5821 C  C   . GLN   B 118 ? 0.1352 0.1081 0.1867 0.0001  -0.0101 -0.0020 118  GLN   B C   
5822 O  O   . GLN   B 118 ? 0.1530 0.1062 0.2129 -0.0048 0.0037  0.0057  118  GLN   B O   
5823 C  CB  . GLN   B 118 ? 0.1374 0.1151 0.1960 -0.0004 -0.0128 -0.0002 118  GLN   B CB  
5824 C  CG  . GLN   B 118 ? 0.1429 0.1165 0.1867 0.0082  -0.0063 -0.0093 118  GLN   B CG  
5825 C  CD  . GLN   B 118 ? 0.1453 0.1114 0.1772 0.0039  -0.0044 -0.0166 118  GLN   B CD  
5826 O  OE1 . GLN   B 118 ? 0.1502 0.1073 0.2077 0.0029  0.0046  0.0026  118  GLN   B OE1 
5827 N  NE2 . GLN   B 118 ? 0.1523 0.1122 0.1858 0.0034  -0.0079 0.0053  118  GLN   B NE2 
5836 N  N   . HIS   B 119 ? 0.1330 0.1162 0.1620 -0.0082 -0.0112 0.0117  119  HIS   B N   
5837 C  CA  . HIS   B 119 ? 0.1424 0.1234 0.1550 -0.0078 -0.0125 0.0091  119  HIS   B CA  
5838 C  C   . HIS   B 119 ? 0.1433 0.1252 0.1554 -0.0043 -0.0269 0.0050  119  HIS   B C   
5839 O  O   . HIS   B 119 ? 0.1507 0.1246 0.1673 -0.0251 -0.0210 0.0122  119  HIS   B O   
5840 C  CB  . HIS   B 119 ? 0.1460 0.1369 0.1583 -0.0027 -0.0235 0.0030  119  HIS   B CB  
5841 C  CG  . HIS   B 119 ? 0.1545 0.1586 0.1760 0.0129  -0.0404 -0.0134 119  HIS   B CG  
5842 N  ND1 . HIS   B 119 ? 0.1627 0.1794 0.2020 0.0036  -0.0464 -0.0329 119  HIS   B ND1 
5843 C  CD2 . HIS   B 119 ? 0.1742 0.1759 0.1809 0.0420  -0.0465 -0.0151 119  HIS   B CD2 
5844 C  CE1 . HIS   B 119 ? 0.1766 0.1914 0.2043 0.0203  -0.0509 -0.0450 119  HIS   B CE1 
5845 N  NE2 . HIS   B 119 ? 0.1877 0.1978 0.1922 0.0340  -0.0520 -0.0365 119  HIS   B NE2 
5853 N  N   . GLU   B 120 ? 0.1630 0.1317 0.1600 -0.0112 -0.0305 0.0197  120  GLU   B N   
5854 C  CA  . GLU   B 120 ? 0.1941 0.1419 0.1637 -0.0058 -0.0462 0.0287  120  GLU   B CA  
5855 C  C   . GLU   B 120 ? 0.1707 0.1359 0.1532 -0.0175 -0.0372 0.0278  120  GLU   B C   
5856 O  O   . GLU   B 120 ? 0.1657 0.1453 0.1583 -0.0160 -0.0322 0.0168  120  GLU   B O   
5857 C  CB  . GLU   B 120 ? 0.2568 0.1743 0.2439 0.0127  -0.0742 0.0454  120  GLU   B CB  
5858 C  CG  . GLU   B 120 ? 0.3099 0.2490 0.3417 0.0237  -0.0958 0.0662  120  GLU   B CG  
5859 C  CD  . GLU   B 120 ? 0.3562 0.3223 0.4501 0.0253  -0.1034 0.0837  120  GLU   B CD  
5860 O  OE1 . GLU   B 120 ? 0.3816 0.3619 0.4847 0.0196  -0.1015 0.0998  120  GLU   B OE1 
5861 O  OE2 . GLU   B 120 ? 0.3693 0.3559 0.5052 0.0251  -0.1023 0.0768  120  GLU   B OE2 
5868 N  N   . VAL   B 121 ? 0.1615 0.1312 0.1548 -0.0262 -0.0264 0.0233  121  VAL   B N   
5869 C  CA  . VAL   B 121 ? 0.1580 0.1390 0.1420 -0.0225 -0.0269 0.0146  121  VAL   B CA  
5870 C  C   . VAL   B 121 ? 0.1497 0.1337 0.1336 -0.0253 -0.0153 0.0109  121  VAL   B C   
5871 O  O   . VAL   B 121 ? 0.1593 0.1310 0.1557 -0.0321 -0.0262 0.0108  121  VAL   B O   
5872 C  CB  . VAL   B 121 ? 0.1770 0.1736 0.1612 -0.0107 -0.0245 0.0225  121  VAL   B CB  
5873 C  CG1 . VAL   B 121 ? 0.1824 0.1855 0.1920 -0.0179 -0.0123 0.0179  121  VAL   B CG1 
5874 C  CG2 . VAL   B 121 ? 0.2012 0.1975 0.1632 -0.0024 -0.0202 0.0094  121  VAL   B CG2 
5884 N  N   . LEU   B 122 ? 0.1413 0.1243 0.1327 -0.0202 -0.0197 0.0059  122  LEU   B N   
5885 C  CA  . LEU   B 122 ? 0.1324 0.1381 0.1182 -0.0227 -0.0197 0.0077  122  LEU   B CA  
5886 C  C   . LEU   B 122 ? 0.1314 0.1273 0.1242 -0.0314 -0.0159 0.0085  122  LEU   B C   
5887 O  O   . LEU   B 122 ? 0.1375 0.1270 0.1658 -0.0334 -0.0237 0.0038  122  LEU   B O   
5888 C  CB  . LEU   B 122 ? 0.1558 0.1428 0.1590 -0.0052 -0.0258 0.0167  122  LEU   B CB  
5889 C  CG  . LEU   B 122 ? 0.1454 0.1475 0.1696 -0.0157 -0.0113 0.0131  122  LEU   B CG  
5890 C  CD1 . LEU   B 122 ? 0.1507 0.1698 0.1588 -0.0233 -0.0191 0.0049  122  LEU   B CD1 
5891 C  CD2 . LEU   B 122 ? 0.1463 0.1449 0.1439 -0.0094 -0.0124 0.0019  122  LEU   B CD2 
5903 N  N   . LEU   B 123 ? 0.1330 0.1150 0.1232 -0.0216 -0.0155 0.0059  123  LEU   B N   
5904 C  CA  . LEU   B 123 ? 0.1338 0.1149 0.1326 -0.0226 -0.0161 -0.0002 123  LEU   B CA  
5905 C  C   . LEU   B 123 ? 0.1267 0.1155 0.1316 -0.0268 -0.0145 0.0021  123  LEU   B C   
5906 O  O   . LEU   B 123 ? 0.1402 0.1173 0.1357 -0.0354 -0.0150 0.0042  123  LEU   B O   
5907 C  CB  . LEU   B 123 ? 0.1369 0.1224 0.1513 -0.0256 -0.0120 0.0004  123  LEU   B CB  
5908 C  CG  . LEU   B 123 ? 0.1372 0.1252 0.1585 -0.0179 -0.0087 0.0105  123  LEU   B CG  
5909 C  CD1 . LEU   B 123 ? 0.1518 0.1201 0.1630 -0.0194 -0.0040 -0.0088 123  LEU   B CD1 
5910 C  CD2 . LEU   B 123 ? 0.1512 0.1334 0.1680 -0.0185 -0.0015 0.0184  123  LEU   B CD2 
5922 N  N   . ALA   B 124 ? 0.1267 0.1125 0.1271 -0.0227 -0.0082 -0.0016 124  ALA   B N   
5923 C  CA  . ALA   B 124 ? 0.1221 0.1144 0.1396 -0.0151 -0.0116 -0.0005 124  ALA   B CA  
5924 C  C   . ALA   B 124 ? 0.1186 0.1144 0.1380 -0.0202 -0.0128 -0.0004 124  ALA   B C   
5925 O  O   . ALA   B 124 ? 0.1337 0.1122 0.1478 -0.0131 -0.0155 0.0029  124  ALA   B O   
5926 C  CB  . ALA   B 124 ? 0.1249 0.1218 0.1449 -0.0069 0.0027  -0.0008 124  ALA   B CB  
5932 N  N   . PRO   B 125 ? 0.1283 0.1125 0.1349 -0.0139 -0.0112 0.0131  125  PRO   B N   
5933 C  CA  . PRO   B 125 ? 0.1356 0.1146 0.1534 -0.0142 -0.0123 0.0200  125  PRO   B CA  
5934 C  C   . PRO   B 125 ? 0.1295 0.1098 0.1569 -0.0164 -0.0077 0.0065  125  PRO   B C   
5935 O  O   . PRO   B 125 ? 0.1312 0.1098 0.1798 -0.0084 -0.0006 0.0151  125  PRO   B O   
5936 C  CB  . PRO   B 125 ? 0.1386 0.1420 0.1647 -0.0179 -0.0201 0.0272  125  PRO   B CB  
5937 C  CG  . PRO   B 125 ? 0.1430 0.1437 0.1559 -0.0273 -0.0197 0.0133  125  PRO   B CG  
5938 C  CD  . PRO   B 125 ? 0.1378 0.1252 0.1381 -0.0218 -0.0091 0.0092  125  PRO   B CD  
5946 N  N   . LEU   B 126 ? 0.1334 0.1069 0.1849 -0.0116 0.0067  0.0127  126  LEU   B N   
5947 C  CA  . LEU   B 126 ? 0.1416 0.1160 0.1884 -0.0095 0.0219  0.0157  126  LEU   B CA  
5948 C  C   . LEU   B 126 ? 0.1377 0.1200 0.1986 0.0015  0.0284  0.0240  126  LEU   B C   
5949 O  O   . LEU   B 126 ? 0.1617 0.1542 0.2063 0.0231  -0.0021 0.0039  126  LEU   B O   
5950 C  CB  . LEU   B 126 ? 0.1595 0.1216 0.2107 -0.0157 0.0271  0.0082  126  LEU   B CB  
5951 C  CG  . LEU   B 126 ? 0.1759 0.1299 0.2195 -0.0252 0.0208  -0.0053 126  LEU   B CG  
5952 C  CD1 . LEU   B 126 ? 0.1888 0.1330 0.2735 -0.0210 0.0157  -0.0162 126  LEU   B CD1 
5953 C  CD2 . LEU   B 126 ? 0.1761 0.1415 0.2215 -0.0284 0.0138  -0.0102 126  LEU   B CD2 
5965 N  N   . LEU   B 127 ? 0.1365 0.1151 0.2112 0.0026  0.0263  0.0172  127  LEU   B N   
5966 C  CA  . LEU   B 127 ? 0.1355 0.1248 0.2170 -0.0039 0.0299  0.0259  127  LEU   B CA  
5967 C  C   . LEU   B 127 ? 0.1332 0.1183 0.2103 0.0021  0.0219  0.0252  127  LEU   B C   
5968 O  O   . LEU   B 127 ? 0.1368 0.1221 0.2134 -0.0121 0.0118  0.0239  127  LEU   B O   
5969 C  CB  . LEU   B 127 ? 0.1492 0.1203 0.2192 0.0028  0.0276  0.0242  127  LEU   B CB  
5970 C  CG  . LEU   B 127 ? 0.1616 0.1193 0.2214 0.0025  0.0249  0.0170  127  LEU   B CG  
5971 C  CD1 . LEU   B 127 ? 0.1658 0.1206 0.2276 0.0040  0.0191  0.0114  127  LEU   B CD1 
5972 C  CD2 . LEU   B 127 ? 0.1624 0.1284 0.2341 -0.0080 0.0277  0.0288  127  LEU   B CD2 
5984 N  N   . SER   B 128 ? 0.1391 0.1189 0.2067 0.0042  0.0081  0.0185  128  SER   B N   
5985 C  CA  . SER   B 128 ? 0.1498 0.1270 0.2113 0.0105  -0.0010 0.0267  128  SER   B CA  
5986 C  C   . SER   B 128 ? 0.1603 0.1318 0.2404 0.0081  -0.0209 0.0243  128  SER   B C   
5987 O  O   . SER   B 128 ? 0.1742 0.1356 0.2780 0.0075  -0.0172 0.0381  128  SER   B O   
5988 C  CB  . SER   B 128 ? 0.1603 0.1295 0.2042 0.0060  0.0023  0.0327  128  SER   B CB  
5989 O  OG  . SER   B 128 ? 0.1640 0.1494 0.2046 0.0106  0.0110  0.0373  128  SER   B OG  
5995 N  N   . ALA   B 129 ? 0.1724 0.1409 0.2623 0.0278  -0.0154 0.0066  129  ALA   B N   
5996 C  CA  . ALA   B 129 ? 0.1890 0.1447 0.2571 0.0325  -0.0114 0.0026  129  ALA   B CA  
5997 C  C   . ALA   B 129 ? 0.1740 0.1360 0.2512 0.0207  0.0035  0.0076  129  ALA   B C   
5998 O  O   . ALA   B 129 ? 0.1627 0.1419 0.2467 0.0163  0.0027  0.0072  129  ALA   B O   
5999 C  CB  . ALA   B 129 ? 0.2157 0.1680 0.2845 0.0320  -0.0001 -0.0004 129  ALA   B CB  
6005 N  N   . GLY   B 130 ? 0.1690 0.1346 0.2571 0.0271  0.0104  0.0050  130  GLY   B N   
6006 C  CA  . GLY   B 130 ? 0.1731 0.1482 0.2570 0.0242  0.0241  0.0010  130  GLY   B CA  
6007 C  C   . GLY   B 130 ? 0.1800 0.1508 0.2571 0.0210  0.0174  0.0159  130  GLY   B C   
6008 O  O   . GLY   B 130 ? 0.1934 0.1624 0.2569 0.0207  0.0162  0.0232  130  GLY   B O   
6012 N  N   . ILE   B 131 ? 0.1775 0.1636 0.2714 0.0336  0.0173  0.0091  131  ILE   B N   
6013 C  CA  . ILE   B 131 ? 0.1981 0.1771 0.2713 0.0315  0.0054  0.0210  131  ILE   B CA  
6014 C  C   . ILE   B 131 ? 0.2095 0.1668 0.2320 0.0254  0.0049  0.0260  131  ILE   B C   
6015 O  O   . ILE   B 131 ? 0.2349 0.1834 0.2423 0.0258  -0.0130 0.0276  131  ILE   B O   
6016 C  CB  . ILE   B 131 ? 0.1967 0.2098 0.3053 0.0269  -0.0038 0.0272  131  ILE   B CB  
6017 C  CG1 . ILE   B 131 ? 0.1937 0.2361 0.3199 -0.0018 0.0025  0.0304  131  ILE   B CG1 
6018 C  CG2 . ILE   B 131 ? 0.1994 0.2245 0.3266 0.0345  0.0001  0.0217  131  ILE   B CG2 
6019 C  CD1 . ILE   B 131 ? 0.1959 0.2591 0.3358 -0.0201 -0.0000 0.0342  131  ILE   B CD1 
6031 N  N   . PHE   B 132 ? 0.1935 0.1488 0.2168 0.0194  0.0189  0.0312  132  PHE   B N   
6032 C  CA  . PHE   B 132 ? 0.2030 0.1519 0.2080 0.0104  0.0391  0.0207  132  PHE   B CA  
6033 C  C   . PHE   B 132 ? 0.2225 0.1705 0.2240 0.0110  0.0463  0.0191  132  PHE   B C   
6034 O  O   . PHE   B 132 ? 0.2382 0.1951 0.2419 0.0035  0.0587  0.0252  132  PHE   B O   
6035 C  CB  . PHE   B 132 ? 0.1878 0.1505 0.1929 0.0137  0.0408  0.0186  132  PHE   B CB  
6036 C  CG  . PHE   B 132 ? 0.1788 0.1520 0.1815 0.0131  0.0264  0.0193  132  PHE   B CG  
6037 C  CD1 . PHE   B 132 ? 0.1855 0.1558 0.2204 0.0128  0.0283  0.0142  132  PHE   B CD1 
6038 C  CD2 . PHE   B 132 ? 0.1791 0.1570 0.1662 0.0188  0.0185  0.0209  132  PHE   B CD2 
6039 C  CE1 . PHE   B 132 ? 0.1922 0.1596 0.2261 0.0038  0.0200  0.0128  132  PHE   B CE1 
6040 C  CE2 . PHE   B 132 ? 0.1865 0.1626 0.1712 0.0151  0.0098  0.0209  132  PHE   B CE2 
6041 C  CZ  . PHE   B 132 ? 0.1923 0.1610 0.2084 0.0069  0.0038  0.0283  132  PHE   B CZ  
6051 N  N   . GLY   B 133 ? 0.2182 0.1585 0.2290 0.0092  0.0266  0.0393  133  GLY   B N   
6052 C  CA  . GLY   B 133 ? 0.2275 0.1696 0.2488 -0.0127 0.0267  0.0481  133  GLY   B CA  
6053 C  C   . GLY   B 133 ? 0.2343 0.1793 0.2529 -0.0267 0.0354  0.0527  133  GLY   B C   
6054 O  O   . GLY   B 133 ? 0.2510 0.1880 0.2938 -0.0406 0.0419  0.0617  133  GLY   B O   
6058 N  N   . ALA   B 134 ? 0.2143 0.1759 0.2444 -0.0244 0.0415  0.0355  134  ALA   B N   
6059 C  CA  . ALA   B 134 ? 0.2026 0.1752 0.2529 -0.0155 0.0512  0.0219  134  ALA   B CA  
6060 C  C   . ALA   B 134 ? 0.2087 0.1617 0.2590 -0.0059 0.0456  0.0322  134  ALA   B C   
6061 O  O   . ALA   B 134 ? 0.2149 0.1830 0.2601 0.0022  0.0364  0.0250  134  ALA   B O   
6062 C  CB  . ALA   B 134 ? 0.1976 0.1798 0.2785 -0.0099 0.0335  0.0157  134  ALA   B CB  
6068 N  N   . ASP   B 135 ? 0.2207 0.1586 0.2653 -0.0113 0.0258  0.0343  135  ASP   B N   
6069 C  CA  . ASP   B 135 ? 0.2369 0.1516 0.2779 -0.0131 0.0090  0.0392  135  ASP   B CA  
6070 C  C   . ASP   B 135 ? 0.2191 0.1368 0.2651 -0.0011 0.0083  0.0354  135  ASP   B C   
6071 O  O   . ASP   B 135 ? 0.2081 0.1352 0.2714 -0.0014 0.0130  0.0340  135  ASP   B O   
6072 C  CB  . ASP   B 135 ? 0.2677 0.1632 0.3003 -0.0356 0.0038  0.0394  135  ASP   B CB  
6073 C  CG  . ASP   B 135 ? 0.2989 0.1642 0.3441 -0.0569 0.0039  0.0341  135  ASP   B CG  
6074 O  OD1 . ASP   B 135 ? 0.3061 0.1459 0.3350 -0.0378 -0.0016 0.0327  135  ASP   B OD1 
6075 O  OD2 . ASP   B 135 ? 0.3229 0.1980 0.3891 -0.0760 0.0017  0.0115  135  ASP   B OD2 
6080 N  N   . PRO   B 136 ? 0.2139 0.1388 0.2805 0.0171  -0.0043 0.0317  136  PRO   B N   
6081 C  CA  . PRO   B 136 ? 0.1935 0.1319 0.2638 0.0145  -0.0066 0.0215  136  PRO   B CA  
6082 C  C   . PRO   B 136 ? 0.1703 0.1222 0.2789 0.0147  -0.0017 0.0163  136  PRO   B C   
6083 O  O   . PRO   B 136 ? 0.1533 0.1235 0.2656 0.0094  0.0070  0.0162  136  PRO   B O   
6084 C  CB  . PRO   B 136 ? 0.2033 0.1537 0.2831 0.0299  -0.0086 0.0100  136  PRO   B CB  
6085 C  CG  . PRO   B 136 ? 0.2202 0.1632 0.3082 0.0369  -0.0025 0.0148  136  PRO   B CG  
6086 C  CD  . PRO   B 136 ? 0.2221 0.1563 0.2982 0.0359  -0.0004 0.0191  136  PRO   B CD  
6094 N  N   . ILE   B 137 ? 0.1860 0.1156 0.2873 0.0119  -0.0075 0.0147  137  ILE   B N   
6095 C  CA  . ILE   B 137 ? 0.1894 0.1142 0.3011 0.0012  -0.0040 0.0099  137  ILE   B CA  
6096 C  C   . ILE   B 137 ? 0.1798 0.1194 0.2901 -0.0080 0.0104  0.0161  137  ILE   B C   
6097 O  O   . ILE   B 137 ? 0.1757 0.1195 0.2804 -0.0083 0.0075  0.0145  137  ILE   B O   
6098 C  CB  . ILE   B 137 ? 0.2148 0.1191 0.3551 -0.0005 -0.0063 0.0100  137  ILE   B CB  
6099 C  CG1 . ILE   B 137 ? 0.2475 0.1399 0.4015 0.0107  0.0029  -0.0002 137  ILE   B CG1 
6100 C  CG2 . ILE   B 137 ? 0.2189 0.1230 0.3665 -0.0254 -0.0026 0.0073  137  ILE   B CG2 
6101 C  CD1 . ILE   B 137 ? 0.2699 0.1611 0.4437 0.0226  0.0054  -0.0022 137  ILE   B CD1 
6113 N  N   . HIS   B 138 ? 0.1832 0.1188 0.2874 -0.0083 0.0197  0.0198  138  HIS   B N   
6114 C  CA  . HIS   B 138 ? 0.1903 0.1277 0.2811 -0.0039 0.0369  0.0237  138  HIS   B CA  
6115 C  C   . HIS   B 138 ? 0.1725 0.1248 0.2694 -0.0039 0.0335  0.0287  138  HIS   B C   
6116 O  O   . HIS   B 138 ? 0.1654 0.1328 0.2854 0.0019  0.0385  0.0398  138  HIS   B O   
6117 C  CB  . HIS   B 138 ? 0.2208 0.1429 0.2930 -0.0055 0.0586  0.0248  138  HIS   B CB  
6118 C  CG  . HIS   B 138 ? 0.2475 0.1588 0.2928 -0.0059 0.0747  0.0389  138  HIS   B CG  
6119 N  ND1 . HIS   B 138 ? 0.2574 0.1729 0.3230 -0.0036 0.0883  0.0348  138  HIS   B ND1 
6120 C  CD2 . HIS   B 138 ? 0.2663 0.1612 0.2927 -0.0024 0.0794  0.0396  138  HIS   B CD2 
6121 C  CE1 . HIS   B 138 ? 0.2652 0.1737 0.3171 -0.0013 0.0943  0.0368  138  HIS   B CE1 
6122 N  NE2 . HIS   B 138 ? 0.2735 0.1592 0.2961 0.0035  0.0891  0.0278  138  HIS   B NE2 
6130 N  N   . SER   B 139 ? 0.1671 0.1167 0.2630 0.0039  0.0274  0.0203  139  SER   B N   
6131 C  CA  . SER   B 139 ? 0.1659 0.1116 0.2480 -0.0022 0.0249  0.0077  139  SER   B CA  
6132 C  C   . SER   B 139 ? 0.1438 0.1054 0.2406 -0.0025 0.0212  0.0092  139  SER   B C   
6133 O  O   . SER   B 139 ? 0.1471 0.1079 0.2387 0.0027  0.0072  0.0118  139  SER   B O   
6134 C  CB  . SER   B 139 ? 0.1695 0.1136 0.2569 0.0051  0.0166  0.0047  139  SER   B CB  
6135 O  OG  . SER   B 139 ? 0.1727 0.1147 0.2523 0.0011  -0.0005 0.0221  139  SER   B OG  
6141 N  N   . LEU   B 140 ? 0.1408 0.0990 0.2440 -0.0056 0.0228  0.0085  140  LEU   B N   
6142 C  CA  . LEU   B 140 ? 0.1413 0.1080 0.2508 -0.0004 0.0179  0.0074  140  LEU   B CA  
6143 C  C   . LEU   B 140 ? 0.1358 0.1076 0.2563 -0.0044 0.0046  -0.0022 140  LEU   B C   
6144 O  O   . LEU   B 140 ? 0.1388 0.1125 0.2434 -0.0030 0.0037  0.0089  140  LEU   B O   
6145 C  CB  . LEU   B 140 ? 0.1397 0.1051 0.2446 -0.0076 0.0232  -0.0030 140  LEU   B CB  
6146 C  CG  . LEU   B 140 ? 0.1482 0.1109 0.2398 -0.0121 0.0042  0.0004  140  LEU   B CG  
6147 C  CD1 . LEU   B 140 ? 0.1566 0.1198 0.2634 -0.0119 0.0135  0.0032  140  LEU   B CD1 
6148 C  CD2 . LEU   B 140 ? 0.1661 0.1242 0.2725 -0.0145 0.0053  -0.0092 140  LEU   B CD2 
6160 N  N   . ARG   B 141 ? 0.1290 0.1054 0.2683 -0.0116 0.0104  -0.0011 141  ARG   B N   
6161 C  CA  . ARG   B 141 ? 0.1286 0.1138 0.3047 -0.0131 0.0248  -0.0021 141  ARG   B CA  
6162 C  C   . ARG   B 141 ? 0.1231 0.1109 0.2960 -0.0156 0.0141  -0.0044 141  ARG   B C   
6163 O  O   . ARG   B 141 ? 0.1322 0.1102 0.2834 -0.0122 0.0083  -0.0108 141  ARG   B O   
6164 C  CB  . ARG   B 141 ? 0.1495 0.1204 0.3289 -0.0184 0.0289  -0.0042 141  ARG   B CB  
6165 C  CG  . ARG   B 141 ? 0.1780 0.1472 0.3348 -0.0183 0.0322  -0.0041 141  ARG   B CG  
6166 C  CD  . ARG   B 141 ? 0.2169 0.1704 0.3271 -0.0142 0.0156  -0.0202 141  ARG   B CD  
6167 N  NE  . ARG   B 141 ? 0.2334 0.1686 0.3201 -0.0314 0.0226  -0.0217 141  ARG   B NE  
6168 C  CZ  . ARG   B 141 ? 0.2455 0.1547 0.2971 -0.0234 0.0309  -0.0321 141  ARG   B CZ  
6169 N  NH1 . ARG   B 141 ? 0.2516 0.1439 0.2835 -0.0190 0.0290  -0.0330 141  ARG   B NH1 
6170 N  NH2 . ARG   B 141 ? 0.2564 0.1659 0.3140 -0.0096 0.0147  -0.0294 141  ARG   B NH2 
6184 N  N   . VAL   B 142 ? 0.1313 0.1085 0.2791 -0.0089 0.0190  -0.0026 142  VAL   B N   
6185 C  CA  . VAL   B 142 ? 0.1258 0.1113 0.2755 -0.0017 0.0213  0.0003  142  VAL   B CA  
6186 C  C   . VAL   B 142 ? 0.1252 0.1082 0.2660 -0.0040 0.0146  0.0003  142  VAL   B C   
6187 O  O   . VAL   B 142 ? 0.1358 0.1088 0.2671 0.0011  0.0140  0.0003  142  VAL   B O   
6188 C  CB  . VAL   B 142 ? 0.1398 0.1206 0.2737 0.0001  0.0242  0.0118  142  VAL   B CB  
6189 C  CG1 . VAL   B 142 ? 0.1383 0.1222 0.2578 0.0023  0.0226  0.0077  142  VAL   B CG1 
6190 C  CG2 . VAL   B 142 ? 0.1618 0.1220 0.2819 0.0016  0.0209  0.0161  142  VAL   B CG2 
6200 N  N   . CYS   B 143 ? 0.1241 0.1092 0.2464 -0.0018 0.0082  0.0032  143  CYS   B N   
6201 C  CA  . CYS   B 143 ? 0.1223 0.1108 0.2449 -0.0102 0.0103  0.0075  143  CYS   B CA  
6202 C  C   . CYS   B 143 ? 0.1180 0.1118 0.2469 -0.0086 0.0050  -0.0023 143  CYS   B C   
6203 O  O   . CYS   B 143 ? 0.1222 0.1149 0.2460 -0.0039 0.0024  -0.0034 143  CYS   B O   
6204 C  CB  . CYS   B 143 ? 0.1277 0.1150 0.2395 -0.0054 0.0016  0.0046  143  CYS   B CB  
6205 S  SG  . CYS   B 143 ? 0.1313 0.1301 0.2311 -0.0054 0.0087  0.0039  143  CYS   B SG  
6211 N  N   . VAL   B 144 ? 0.1232 0.1115 0.2534 -0.0102 0.0041  -0.0125 144  VAL   B N   
6212 C  CA  . VAL   B 144 ? 0.1318 0.1208 0.2787 -0.0117 -0.0048 -0.0197 144  VAL   B CA  
6213 C  C   . VAL   B 144 ? 0.1278 0.1225 0.2908 -0.0106 -0.0080 -0.0037 144  VAL   B C   
6214 O  O   . VAL   B 144 ? 0.1380 0.1407 0.3051 0.0021  -0.0037 0.0162  144  VAL   B O   
6215 C  CB  . VAL   B 144 ? 0.1529 0.1321 0.3389 -0.0136 -0.0111 -0.0306 144  VAL   B CB  
6216 C  CG1 . VAL   B 144 ? 0.1771 0.1635 0.3705 -0.0136 -0.0145 -0.0177 144  VAL   B CG1 
6217 C  CG2 . VAL   B 144 ? 0.1646 0.1308 0.3347 -0.0012 -0.0265 -0.0412 144  VAL   B CG2 
6227 N  N   . ASP   B 145 ? 0.1234 0.1164 0.3078 -0.0087 -0.0021 -0.0212 145  ASP   B N   
6228 C  CA  . ASP   B 145 ? 0.1253 0.1216 0.3307 -0.0087 0.0117  -0.0096 145  ASP   B CA  
6229 C  C   . ASP   B 145 ? 0.1246 0.1183 0.3115 -0.0079 0.0092  -0.0046 145  ASP   B C   
6230 O  O   . ASP   B 145 ? 0.1267 0.1364 0.3586 -0.0137 0.0107  -0.0256 145  ASP   B O   
6231 C  CB  . ASP   B 145 ? 0.1331 0.1311 0.3586 -0.0205 0.0241  -0.0077 145  ASP   B CB  
6232 C  CG  . ASP   B 145 ? 0.1510 0.1335 0.3970 -0.0265 0.0339  -0.0036 145  ASP   B CG  
6233 O  OD1 . ASP   B 145 ? 0.1571 0.1367 0.3956 -0.0224 0.0018  -0.0095 145  ASP   B OD1 
6234 O  OD2 . ASP   B 145 ? 0.1779 0.1417 0.4290 -0.0296 0.0584  0.0042  145  ASP   B OD2 
6239 N  N   . THR   B 146 ? 0.1188 0.1124 0.2593 -0.0130 -0.0014 0.0046  146  THR   B N   
6240 C  CA  . THR   B 146 ? 0.1262 0.1110 0.2346 -0.0064 0.0072  0.0008  146  THR   B CA  
6241 C  C   . THR   B 146 ? 0.1240 0.1098 0.2241 -0.0025 0.0026  0.0000  146  THR   B C   
6242 O  O   . THR   B 146 ? 0.1284 0.1115 0.2203 -0.0025 0.0041  -0.0011 146  THR   B O   
6243 C  CB  . THR   B 146 ? 0.1296 0.1131 0.2433 -0.0040 0.0188  0.0065  146  THR   B CB  
6244 O  OG1 . THR   B 146 ? 0.1361 0.1119 0.2552 -0.0054 0.0262  0.0136  146  THR   B OG1 
6245 C  CG2 . THR   B 146 ? 0.1376 0.1197 0.2430 -0.0060 0.0160  0.0016  146  THR   B CG2 
6253 N  N   . VAL   B 147 ? 0.1271 0.1159 0.2093 -0.0060 0.0102  -0.0011 147  VAL   B N   
6254 C  CA  . VAL   B 147 ? 0.1269 0.1112 0.2046 -0.0120 -0.0060 -0.0004 147  VAL   B CA  
6255 C  C   . VAL   B 147 ? 0.1231 0.1132 0.2171 -0.0155 -0.0062 -0.0018 147  VAL   B C   
6256 O  O   . VAL   B 147 ? 0.1362 0.1238 0.2235 -0.0174 -0.0267 -0.0058 147  VAL   B O   
6257 C  CB  . VAL   B 147 ? 0.1296 0.1244 0.1912 -0.0100 -0.0107 0.0029  147  VAL   B CB  
6258 C  CG1 . VAL   B 147 ? 0.1257 0.1399 0.1860 -0.0102 -0.0039 0.0023  147  VAL   B CG1 
6259 C  CG2 . VAL   B 147 ? 0.1321 0.1209 0.2004 -0.0114 -0.0021 0.0043  147  VAL   B CG2 
6269 N  N   . ARG   B 148 ? 0.1246 0.1149 0.2110 -0.0104 -0.0144 -0.0083 148  ARG   B N   
6270 C  CA  . ARG   B 148 ? 0.1290 0.1288 0.2022 -0.0088 -0.0231 -0.0113 148  ARG   B CA  
6271 C  C   . ARG   B 148 ? 0.1367 0.1319 0.1958 -0.0097 -0.0218 -0.0056 148  ARG   B C   
6272 O  O   . ARG   B 148 ? 0.1551 0.1654 0.1937 -0.0231 -0.0267 0.0034  148  ARG   B O   
6273 C  CB  . ARG   B 148 ? 0.1337 0.1308 0.1953 0.0001  -0.0238 -0.0152 148  ARG   B CB  
6274 C  CG  . ARG   B 148 ? 0.1342 0.1445 0.2166 -0.0078 -0.0298 -0.0274 148  ARG   B CG  
6275 C  CD  . ARG   B 148 ? 0.1395 0.1624 0.2391 0.0072  -0.0305 -0.0345 148  ARG   B CD  
6276 N  NE  . ARG   B 148 ? 0.1446 0.1581 0.2172 0.0210  -0.0273 -0.0291 148  ARG   B NE  
6277 C  CZ  . ARG   B 148 ? 0.1402 0.1473 0.2030 0.0136  -0.0196 -0.0186 148  ARG   B CZ  
6278 N  NH1 . ARG   B 148 ? 0.1293 0.1518 0.2108 -0.0074 0.0041  -0.0203 148  ARG   B NH1 
6279 N  NH2 . ARG   B 148 ? 0.1592 0.1337 0.2023 0.0152  -0.0179 -0.0122 148  ARG   B NH2 
6293 N  N   . THR   B 149 ? 0.1387 0.1239 0.2009 -0.0142 -0.0268 0.0002  149  THR   B N   
6294 C  CA  . THR   B 149 ? 0.1464 0.1275 0.1919 -0.0168 -0.0248 0.0085  149  THR   B CA  
6295 C  C   . THR   B 149 ? 0.1433 0.1275 0.1704 -0.0171 -0.0326 0.0041  149  THR   B C   
6296 O  O   . THR   B 149 ? 0.1495 0.1276 0.1858 -0.0221 -0.0128 0.0027  149  THR   B O   
6297 C  CB  . THR   B 149 ? 0.1469 0.1267 0.1853 -0.0166 -0.0293 0.0048  149  THR   B CB  
6298 O  OG1 . THR   B 149 ? 0.1468 0.1326 0.1738 -0.0244 -0.0213 0.0026  149  THR   B OG1 
6299 C  CG2 . THR   B 149 ? 0.1525 0.1283 0.2025 -0.0052 -0.0270 0.0001  149  THR   B CG2 
6307 N  N   . ASN   B 150 ? 0.1494 0.1297 0.1661 -0.0200 -0.0295 0.0048  150  ASN   B N   
6308 C  CA  . ASN   B 150 ? 0.1555 0.1452 0.1612 -0.0261 -0.0314 -0.0060 150  ASN   B CA  
6309 C  C   . ASN   B 150 ? 0.1476 0.1406 0.1610 -0.0206 -0.0194 -0.0037 150  ASN   B C   
6310 O  O   . ASN   B 150 ? 0.1528 0.1358 0.1811 -0.0286 -0.0372 0.0004  150  ASN   B O   
6311 C  CB  . ASN   B 150 ? 0.1765 0.1782 0.1696 -0.0278 -0.0353 0.0094  150  ASN   B CB  
6312 C  CG  . ASN   B 150 ? 0.2034 0.2170 0.2018 -0.0231 -0.0379 0.0248  150  ASN   B CG  
6313 O  OD1 . ASN   B 150 ? 0.2070 0.2357 0.2112 -0.0301 -0.0472 0.0196  150  ASN   B OD1 
6314 N  ND2 . ASN   B 150 ? 0.2168 0.2328 0.2450 -0.0139 -0.0461 0.0683  150  ASN   B ND2 
6321 N  N   . VAL   B 151 ? 0.1401 0.1355 0.1638 -0.0211 -0.0257 -0.0014 151  VAL   B N   
6322 C  CA  . VAL   B 151 ? 0.1420 0.1369 0.1656 -0.0209 -0.0196 0.0012  151  VAL   B CA  
6323 C  C   . VAL   B 151 ? 0.1425 0.1290 0.1605 -0.0306 -0.0265 0.0031  151  VAL   B C   
6324 O  O   . VAL   B 151 ? 0.1493 0.1403 0.1934 -0.0282 -0.0138 -0.0069 151  VAL   B O   
6325 C  CB  . VAL   B 151 ? 0.1624 0.1425 0.1763 -0.0082 -0.0159 -0.0033 151  VAL   B CB  
6326 C  CG1 . VAL   B 151 ? 0.1679 0.1484 0.2034 -0.0139 -0.0098 -0.0141 151  VAL   B CG1 
6327 C  CG2 . VAL   B 151 ? 0.1706 0.1608 0.1710 0.0033  -0.0195 0.0098  151  VAL   B CG2 
6337 N  N   . TYR   B 152 ? 0.1385 0.1185 0.1506 -0.0240 -0.0215 -0.0002 152  TYR   B N   
6338 C  CA  . TYR   B 152 ? 0.1422 0.1384 0.1467 -0.0302 -0.0112 -0.0084 152  TYR   B CA  
6339 C  C   . TYR   B 152 ? 0.1373 0.1228 0.1368 -0.0263 -0.0069 -0.0099 152  TYR   B C   
6340 O  O   . TYR   B 152 ? 0.1447 0.1236 0.1581 -0.0275 -0.0114 -0.0030 152  TYR   B O   
6341 C  CB  . TYR   B 152 ? 0.1563 0.1572 0.1474 -0.0298 -0.0161 0.0040  152  TYR   B CB  
6342 C  CG  . TYR   B 152 ? 0.1711 0.1633 0.1401 -0.0418 -0.0163 0.0053  152  TYR   B CG  
6343 C  CD1 . TYR   B 152 ? 0.1824 0.1744 0.1357 -0.0345 -0.0174 0.0114  152  TYR   B CD1 
6344 C  CD2 . TYR   B 152 ? 0.1918 0.1784 0.1529 -0.0428 -0.0071 -0.0034 152  TYR   B CD2 
6345 C  CE1 . TYR   B 152 ? 0.1978 0.1959 0.1596 -0.0348 -0.0256 0.0225  152  TYR   B CE1 
6346 C  CE2 . TYR   B 152 ? 0.2035 0.2024 0.1566 -0.0445 -0.0209 -0.0081 152  TYR   B CE2 
6347 C  CZ  . TYR   B 152 ? 0.2104 0.2192 0.1459 -0.0380 -0.0398 0.0221  152  TYR   B CZ  
6348 O  OH  . TYR   B 152 ? 0.2357 0.2543 0.1834 -0.0282 -0.0464 0.0277  152  TYR   B OH  
6358 N  N   . LEU   B 153 ? 0.1373 0.1192 0.1493 -0.0294 -0.0115 -0.0082 153  LEU   B N   
6359 C  CA  . LEU   B 153 ? 0.1428 0.1162 0.1446 -0.0253 -0.0050 -0.0079 153  LEU   B CA  
6360 C  C   . LEU   B 153 ? 0.1462 0.1189 0.1559 -0.0257 -0.0010 -0.0109 153  LEU   B C   
6361 O  O   . LEU   B 153 ? 0.1527 0.1390 0.1729 -0.0169 -0.0066 -0.0350 153  LEU   B O   
6362 C  CB  . LEU   B 153 ? 0.1460 0.1188 0.1664 -0.0256 -0.0011 -0.0084 153  LEU   B CB  
6363 C  CG  . LEU   B 153 ? 0.1454 0.1295 0.1886 -0.0239 -0.0034 -0.0009 153  LEU   B CG  
6364 C  CD1 . LEU   B 153 ? 0.1507 0.1415 0.2046 -0.0286 0.0047  0.0099  153  LEU   B CD1 
6365 C  CD2 . LEU   B 153 ? 0.1476 0.1383 0.1946 -0.0299 0.0090  0.0062  153  LEU   B CD2 
6377 N  N   . ALA   B 154 ? 0.1382 0.1193 0.1676 -0.0102 -0.0090 -0.0118 154  ALA   B N   
6378 C  CA  . ALA   B 154 ? 0.1494 0.1302 0.1939 -0.0042 -0.0114 -0.0199 154  ALA   B CA  
6379 C  C   . ALA   B 154 ? 0.1613 0.1308 0.2018 0.0024  -0.0201 -0.0213 154  ALA   B C   
6380 O  O   . ALA   B 154 ? 0.1878 0.1336 0.2118 0.0045  -0.0066 -0.0012 154  ALA   B O   
6381 C  CB  . ALA   B 154 ? 0.1474 0.1520 0.2053 -0.0031 -0.0020 -0.0296 154  ALA   B CB  
6387 N  N   . VAL   B 155 ? 0.1322 0.1222 0.2181 -0.0027 0.0007  -0.0171 155  VAL   B N   
6388 C  CA  . VAL   B 155 ? 0.1285 0.1214 0.2389 -0.0008 -0.0075 -0.0094 155  VAL   B CA  
6389 C  C   . VAL   B 155 ? 0.1268 0.1211 0.2300 -0.0060 -0.0084 -0.0229 155  VAL   B C   
6390 O  O   . VAL   B 155 ? 0.1457 0.1431 0.2647 0.0077  -0.0079 -0.0422 155  VAL   B O   
6391 C  CB  . VAL   B 155 ? 0.1323 0.1351 0.2734 -0.0037 -0.0154 -0.0039 155  VAL   B CB  
6392 C  CG1 . VAL   B 155 ? 0.1359 0.1313 0.2668 -0.0075 -0.0087 -0.0042 155  VAL   B CG1 
6393 C  CG2 . VAL   B 155 ? 0.1298 0.1469 0.3007 -0.0075 -0.0174 0.0252  155  VAL   B CG2 
6403 N  N   . PHE   B 156 ? 0.1201 0.1345 0.2465 0.0008  -0.0064 -0.0172 156  PHE   B N   
6404 C  CA  . PHE   B 156 ? 0.1302 0.1379 0.2793 0.0073  -0.0039 -0.0222 156  PHE   B CA  
6405 C  C   . PHE   B 156 ? 0.1296 0.1502 0.3118 0.0109  -0.0073 -0.0388 156  PHE   B C   
6406 O  O   . PHE   B 156 ? 0.1546 0.1675 0.3349 0.0216  0.0032  -0.0437 156  PHE   B O   
6407 C  CB  . PHE   B 156 ? 0.1365 0.1322 0.2690 0.0011  -0.0071 -0.0174 156  PHE   B CB  
6408 C  CG  . PHE   B 156 ? 0.1320 0.1458 0.2797 0.0023  -0.0127 0.0054  156  PHE   B CG  
6409 C  CD1 . PHE   B 156 ? 0.1339 0.1698 0.3190 0.0046  0.0008  0.0330  156  PHE   B CD1 
6410 C  CD2 . PHE   B 156 ? 0.1385 0.1594 0.2826 0.0086  -0.0139 0.0070  156  PHE   B CD2 
6411 C  CE1 . PHE   B 156 ? 0.1377 0.1827 0.3326 -0.0002 0.0005  0.0331  156  PHE   B CE1 
6412 C  CE2 . PHE   B 156 ? 0.1475 0.1797 0.3077 0.0136  -0.0151 0.0086  156  PHE   B CE2 
6413 C  CZ  . PHE   B 156 ? 0.1349 0.1853 0.3256 0.0112  -0.0182 0.0176  156  PHE   B CZ  
6423 N  N   . ASP   B 157 ? 0.1294 0.1398 0.3349 0.0107  -0.0270 -0.0208 157  ASP   B N   
6424 C  CA  . ASP   B 157 ? 0.1375 0.1495 0.3654 0.0085  -0.0280 -0.0329 157  ASP   B CA  
6425 C  C   . ASP   B 157 ? 0.1394 0.1454 0.3726 0.0101  -0.0179 -0.0514 157  ASP   B C   
6426 O  O   . ASP   B 157 ? 0.1309 0.1425 0.3659 0.0050  -0.0175 -0.0472 157  ASP   B O   
6427 C  CB  . ASP   B 157 ? 0.1619 0.1727 0.3732 0.0048  -0.0495 -0.0230 157  ASP   B CB  
6428 C  CG  . ASP   B 157 ? 0.1991 0.1841 0.3933 0.0004  -0.0346 -0.0231 157  ASP   B CG  
6429 O  OD1 . ASP   B 157 ? 0.2096 0.1722 0.4076 0.0096  -0.0219 -0.0151 157  ASP   B OD1 
6430 O  OD2 . ASP   B 157 ? 0.2322 0.2004 0.4118 -0.0027 -0.0262 -0.0142 157  ASP   B OD2 
6435 N  N   . LYS   B 158 ? 0.1459 0.1650 0.3861 0.0096  -0.0030 -0.0768 158  LYS   B N   
6436 C  CA  . LYS   B 158 ? 0.1616 0.1844 0.3909 0.0089  0.0044  -0.0887 158  LYS   B CA  
6437 C  C   . LYS   B 158 ? 0.1604 0.1682 0.3926 0.0073  -0.0013 -0.0828 158  LYS   B C   
6438 O  O   . LYS   B 158 ? 0.1640 0.1729 0.3812 -0.0030 0.0024  -0.0912 158  LYS   B O   
6439 C  CB  . LYS   B 158 ? 0.1866 0.2171 0.3860 0.0094  0.0176  -0.1119 158  LYS   B CB  
6440 C  CG  . LYS   B 158 ? 0.2202 0.2533 0.3944 0.0117  0.0263  -0.1174 158  LYS   B CG  
6441 C  CD  . LYS   B 158 ? 0.2451 0.2950 0.4044 0.0115  0.0286  -0.1118 158  LYS   B CD  
6442 C  CE  . LYS   B 158 ? 0.2642 0.3241 0.4172 0.0133  0.0233  -0.1048 158  LYS   B CE  
6443 N  NZ  . LYS   B 158 ? 0.2647 0.3395 0.4179 0.0083  0.0187  -0.1015 158  LYS   B NZ  
6457 N  N   . ASN   B 159 ? 0.1630 0.1559 0.4237 0.0053  -0.0170 -0.0626 159  ASN   B N   
6458 C  CA  . ASN   B 159 ? 0.1744 0.1527 0.4399 0.0173  -0.0333 -0.0546 159  ASN   B CA  
6459 C  C   . ASN   B 159 ? 0.1607 0.1397 0.4344 0.0135  -0.0438 -0.0483 159  ASN   B C   
6460 O  O   . ASN   B 159 ? 0.1629 0.1337 0.4586 -0.0011 -0.0503 -0.0348 159  ASN   B O   
6461 C  CB  . ASN   B 159 ? 0.1957 0.1621 0.4538 0.0239  -0.0363 -0.0570 159  ASN   B CB  
6462 C  CG  . ASN   B 159 ? 0.2242 0.1817 0.4732 0.0197  -0.0498 -0.0738 159  ASN   B CG  
6463 O  OD1 . ASN   B 159 ? 0.2406 0.1934 0.4706 0.0290  -0.0477 -0.0834 159  ASN   B OD1 
6464 N  ND2 . ASN   B 159 ? 0.2256 0.1889 0.4812 0.0197  -0.0544 -0.0644 159  ASN   B ND2 
6471 N  N   . LEU   B 160 ? 0.1472 0.1393 0.4076 0.0077  -0.0458 -0.0435 160  LEU   B N   
6472 C  CA  . LEU   B 160 ? 0.1425 0.1407 0.3618 0.0090  -0.0401 -0.0179 160  LEU   B CA  
6473 C  C   . LEU   B 160 ? 0.1403 0.1284 0.3530 -0.0015 -0.0241 -0.0250 160  LEU   B C   
6474 O  O   . LEU   B 160 ? 0.1312 0.1328 0.3463 -0.0043 -0.0242 -0.0125 160  LEU   B O   
6475 C  CB  . LEU   B 160 ? 0.1420 0.1517 0.3440 0.0067  -0.0379 -0.0099 160  LEU   B CB  
6476 C  CG  . LEU   B 160 ? 0.1468 0.1635 0.3178 0.0096  -0.0354 -0.0016 160  LEU   B CG  
6477 C  CD1 . LEU   B 160 ? 0.1604 0.1752 0.3027 0.0022  -0.0125 -0.0076 160  LEU   B CD1 
6478 C  CD2 . LEU   B 160 ? 0.1478 0.1690 0.3157 0.0211  -0.0356 -0.0076 160  LEU   B CD2 
6490 N  N   . TYR   B 161 ? 0.1414 0.1336 0.3598 -0.0101 -0.0016 -0.0383 161  TYR   B N   
6491 C  CA  . TYR   B 161 ? 0.1497 0.1364 0.3430 -0.0147 0.0204  -0.0441 161  TYR   B CA  
6492 C  C   . TYR   B 161 ? 0.1527 0.1380 0.3312 -0.0153 0.0191  -0.0428 161  TYR   B C   
6493 O  O   . TYR   B 161 ? 0.1532 0.1362 0.3230 -0.0210 0.0117  -0.0412 161  TYR   B O   
6494 C  CB  . TYR   B 161 ? 0.1633 0.1453 0.3385 -0.0278 0.0327  -0.0459 161  TYR   B CB  
6495 C  CG  . TYR   B 161 ? 0.1880 0.1504 0.3205 -0.0323 0.0371  -0.0512 161  TYR   B CG  
6496 C  CD1 . TYR   B 161 ? 0.1938 0.1497 0.3098 -0.0430 0.0465  -0.0491 161  TYR   B CD1 
6497 C  CD2 . TYR   B 161 ? 0.2070 0.1577 0.3090 -0.0305 0.0285  -0.0615 161  TYR   B CD2 
6498 C  CE1 . TYR   B 161 ? 0.2130 0.1671 0.3082 -0.0452 0.0470  -0.0505 161  TYR   B CE1 
6499 C  CE2 . TYR   B 161 ? 0.2263 0.1800 0.3159 -0.0333 0.0354  -0.0611 161  TYR   B CE2 
6500 C  CZ  . TYR   B 161 ? 0.2295 0.1837 0.3096 -0.0485 0.0342  -0.0545 161  TYR   B CZ  
6501 O  OH  . TYR   B 161 ? 0.2578 0.2063 0.3307 -0.0508 0.0304  -0.0501 161  TYR   B OH  
6511 N  N   . ASP   B 162 ? 0.1556 0.1371 0.3457 -0.0094 0.0062  -0.0562 162  ASP   B N   
6512 C  CA  . ASP   B 162 ? 0.1661 0.1428 0.3513 -0.0067 -0.0041 -0.0529 162  ASP   B CA  
6513 C  C   . ASP   B 162 ? 0.1602 0.1345 0.3435 -0.0071 -0.0090 -0.0427 162  ASP   B C   
6514 O  O   . ASP   B 162 ? 0.1671 0.1391 0.3362 -0.0148 -0.0252 -0.0373 162  ASP   B O   
6515 C  CB  . ASP   B 162 ? 0.1846 0.1597 0.3636 0.0005  -0.0137 -0.0716 162  ASP   B CB  
6516 C  CG  . ASP   B 162 ? 0.1877 0.1859 0.3849 0.0059  -0.0102 -0.0862 162  ASP   B CG  
6517 O  OD1 . ASP   B 162 ? 0.1878 0.2062 0.3817 -0.0015 0.0104  -0.0809 162  ASP   B OD1 
6518 O  OD2 . ASP   B 162 ? 0.2011 0.2091 0.4130 0.0254  -0.0091 -0.0857 162  ASP   B OD2 
6523 N  N   . LYS   B 163 ? 0.1593 0.1233 0.3453 -0.0099 -0.0168 -0.0269 163  LYS   B N   
6524 C  CA  . LYS   B 163 ? 0.1720 0.1331 0.3498 -0.0207 -0.0150 -0.0121 163  LYS   B CA  
6525 C  C   . LYS   B 163 ? 0.1401 0.1277 0.3282 -0.0178 -0.0220 -0.0003 163  LYS   B C   
6526 O  O   . LYS   B 163 ? 0.1388 0.1398 0.3467 -0.0204 -0.0182 0.0047  163  LYS   B O   
6527 C  CB  . LYS   B 163 ? 0.2211 0.1806 0.3914 -0.0236 -0.0067 0.0031  163  LYS   B CB  
6528 C  CG  . LYS   B 163 ? 0.3043 0.2713 0.4597 -0.0307 0.0035  0.0050  163  LYS   B CG  
6529 C  CD  . LYS   B 163 ? 0.3851 0.3596 0.5274 -0.0406 0.0040  0.0030  163  LYS   B CD  
6530 C  CE  . LYS   B 163 ? 0.4577 0.4418 0.5700 -0.0458 0.0090  0.0009  163  LYS   B CE  
6531 N  NZ  . LYS   B 163 ? 0.4983 0.4902 0.6033 -0.0477 0.0105  -0.0049 163  LYS   B NZ  
6545 N  N   . LEU   B 164 ? 0.1311 0.1240 0.3053 -0.0132 -0.0183 0.0039  164  LEU   B N   
6546 C  CA  . LEU   B 164 ? 0.1381 0.1232 0.2826 -0.0131 -0.0242 0.0040  164  LEU   B CA  
6547 C  C   . LEU   B 164 ? 0.1428 0.1216 0.2775 -0.0169 -0.0285 0.0019  164  LEU   B C   
6548 O  O   . LEU   B 164 ? 0.1430 0.1456 0.2859 -0.0156 -0.0311 0.0007  164  LEU   B O   
6549 C  CB  . LEU   B 164 ? 0.1316 0.1192 0.2649 -0.0086 -0.0194 0.0000  164  LEU   B CB  
6550 C  CG  . LEU   B 164 ? 0.1401 0.1375 0.2669 -0.0098 -0.0110 0.0042  164  LEU   B CG  
6551 C  CD1 . LEU   B 164 ? 0.1445 0.1382 0.2665 -0.0150 -0.0196 -0.0050 164  LEU   B CD1 
6552 C  CD2 . LEU   B 164 ? 0.1536 0.1731 0.2868 -0.0098 -0.0023 -0.0017 164  LEU   B CD2 
6564 N  N   . VAL   B 165 ? 0.1739 0.1329 0.2984 -0.0216 -0.0352 -0.0122 165  VAL   B N   
6565 C  CA  . VAL   B 165 ? 0.2055 0.1431 0.3090 -0.0302 -0.0484 -0.0102 165  VAL   B CA  
6566 C  C   . VAL   B 165 ? 0.2310 0.1553 0.3329 -0.0387 -0.0709 -0.0102 165  VAL   B C   
6567 O  O   . VAL   B 165 ? 0.2481 0.1687 0.3307 -0.0459 -0.0761 -0.0000 165  VAL   B O   
6568 C  CB  . VAL   B 165 ? 0.2262 0.1564 0.3048 -0.0144 -0.0160 -0.0114 165  VAL   B CB  
6569 C  CG1 . VAL   B 165 ? 0.2404 0.1690 0.3233 -0.0186 -0.0023 -0.0116 165  VAL   B CG1 
6570 C  CG2 . VAL   B 165 ? 0.2199 0.1583 0.2974 -0.0081 -0.0050 -0.0043 165  VAL   B CG2 
6580 N  N   . SER   B 166 ? 0.2371 0.1477 0.3657 -0.0354 -0.0808 -0.0297 166  SER   B N   
6581 C  CA  . SER   B 166 ? 0.2315 0.1511 0.4124 -0.0364 -0.0742 -0.0395 166  SER   B CA  
6582 C  C   . SER   B 166 ? 0.2177 0.1596 0.4220 -0.0423 -0.0770 -0.0186 166  SER   B C   
6583 O  O   . SER   B 166 ? 0.2197 0.1807 0.4533 -0.0568 -0.0807 -0.0336 166  SER   B O   
6584 C  CB  . SER   B 166 ? 0.2302 0.1597 0.4363 -0.0295 -0.0658 -0.0483 166  SER   B CB  
6585 O  OG  . SER   B 166 ? 0.2181 0.1540 0.4500 -0.0233 -0.0591 -0.0273 166  SER   B OG  
6591 N  N   . SER   B 167 ? 0.1988 0.1516 0.3936 -0.0428 -0.0825 0.0205  167  SER   B N   
6592 C  CA  . SER   B 167 ? 0.1899 0.1565 0.3780 -0.0415 -0.0525 0.0306  167  SER   B CA  
6593 C  C   . SER   B 167 ? 0.1832 0.1623 0.3524 -0.0489 -0.0462 0.0509  167  SER   B C   
6594 O  O   . SER   B 167 ? 0.1810 0.1785 0.3516 -0.0535 -0.0400 0.0492  167  SER   B O   
6595 C  CB  . SER   B 167 ? 0.1780 0.1649 0.3776 -0.0348 -0.0198 0.0223  167  SER   B CB  
6596 O  OG  . SER   B 167 ? 0.1666 0.1720 0.3650 -0.0174 -0.0032 0.0197  167  SER   B OG  
6602 N  N   . PHE   B 168 ? 0.1855 0.1614 0.3378 -0.0453 -0.0362 0.0507  168  PHE   B N   
6603 C  CA  . PHE   B 168 ? 0.1880 0.1620 0.3060 -0.0467 -0.0357 0.0306  168  PHE   B CA  
6604 C  C   . PHE   B 168 ? 0.1641 0.1493 0.2688 -0.0259 -0.0152 0.0105  168  PHE   B C   
6605 O  O   . PHE   B 168 ? 0.1930 0.1434 0.2651 -0.0024 -0.0102 0.0030  168  PHE   B O   
6606 C  CB  . PHE   B 168 ? 0.2064 0.1685 0.3129 -0.0555 -0.0499 0.0466  168  PHE   B CB  
6607 C  CG  . PHE   B 168 ? 0.2332 0.1539 0.3025 -0.0567 -0.0473 0.0195  168  PHE   B CG  
6608 C  CD1 . PHE   B 168 ? 0.2610 0.1600 0.3073 -0.0489 -0.0495 0.0145  168  PHE   B CD1 
6609 C  CD2 . PHE   B 168 ? 0.2273 0.1450 0.2997 -0.0462 -0.0445 0.0232  168  PHE   B CD2 
6610 C  CE1 . PHE   B 168 ? 0.2735 0.1645 0.2977 -0.0381 -0.0393 0.0194  168  PHE   B CE1 
6611 C  CE2 . PHE   B 168 ? 0.2520 0.1517 0.3022 -0.0354 -0.0511 0.0162  168  PHE   B CE2 
6612 C  CZ  . PHE   B 168 ? 0.2647 0.1494 0.2977 -0.0236 -0.0480 0.0298  168  PHE   B CZ  
6622 N  N   . LEU   B 169 ? 0.1647 0.1642 0.2643 -0.0066 -0.0021 -0.0071 169  LEU   B N   
6623 C  CA  . LEU   B 169 ? 0.1850 0.1940 0.2838 -0.0068 0.0019  -0.0300 169  LEU   B CA  
6624 C  C   . LEU   B 169 ? 0.2146 0.2202 0.3257 0.0083  -0.0064 -0.0525 169  LEU   B C   
6625 O  O   . LEU   B 169 ? 0.2324 0.2410 0.3746 0.0091  -0.0095 -0.0789 169  LEU   B O   
6626 C  CB  . LEU   B 169 ? 0.2007 0.2343 0.2998 -0.0114 -0.0070 0.0003  169  LEU   B CB  
6627 C  CG  . LEU   B 169 ? 0.2345 0.2763 0.3371 -0.0038 -0.0029 0.0058  169  LEU   B CG  
6628 C  CD1 . LEU   B 169 ? 0.2487 0.2947 0.3410 0.0019  -0.0067 0.0188  169  LEU   B CD1 
6629 C  CD2 . LEU   B 169 ? 0.2261 0.2858 0.3373 0.0041  0.0128  -0.0120 169  LEU   B CD2 
6630 O  OXT . LEU   B 169 ? 0.2352 0.2331 0.3226 0.0306  0.0017  -0.0478 169  LEU   B OXT 
6642 C  C1  T TFA   C .   ? 0.1234 0.1477 0.1106 0.0039  0.0130  0.0043  201  TFA   A C1  
6643 C  C2  T TFA   C .   ? 0.1404 0.1646 0.1594 -0.0111 0.0088  -0.0079 201  TFA   A C2  
6644 O  O   T TFA   C .   ? 0.1045 0.1376 0.0954 0.0096  0.0177  0.0126  201  TFA   A O   
6645 F  F1  T TFA   C .   ? 0.1339 0.1597 0.2037 -0.0231 0.0044  -0.0064 201  TFA   A F1  
6646 F  F2  T TFA   C .   ? 0.1474 0.1733 0.1538 -0.0137 0.0076  -0.0049 201  TFA   A F2  
6647 F  F3  T TFA   C .   ? 0.1565 0.1797 0.1723 -0.0129 0.0218  -0.0137 201  TFA   A F3  
6648 O  OXT T TFA   C .   ? 0.1228 0.1393 0.0923 0.0172  0.0174  0.0130  201  TFA   A OXT 
6649 S  S   B DMS   D .   ? 0.2347 0.2362 0.4354 -0.0323 -0.0857 0.0972  202  DMS   A S   
6650 O  O   B DMS   D .   ? 0.2284 0.2289 0.4128 -0.0452 -0.0911 0.1120  202  DMS   A O   
6651 C  C1  B DMS   D .   ? 0.2479 0.2407 0.4107 -0.0280 -0.0979 0.1052  202  DMS   A C1  
6652 C  C2  B DMS   D .   ? 0.2423 0.2459 0.4229 -0.0389 -0.0825 0.0979  202  DMS   A C2  
6659 S  S   B DMS   E .   ? 0.5120 0.4967 0.5759 0.0648  -0.0087 -0.0358 203  DMS   A S   
6660 O  O   B DMS   E .   ? 0.5114 0.4967 0.5656 0.0676  -0.0049 -0.0357 203  DMS   A O   
6661 C  C1  B DMS   E .   ? 0.5121 0.4980 0.5656 0.0623  -0.0110 -0.0370 203  DMS   A C1  
6662 C  C2  B DMS   E .   ? 0.5138 0.4970 0.5641 0.0644  -0.0084 -0.0346 203  DMS   A C2  
6669 N  N2  B A1BAO F .   ? 0.1248 0.1302 0.1241 -0.0030 -0.0141 0.0120  204  A1BAO A N2  
6670 C  C3  B A1BAO F .   ? 0.1330 0.1616 0.1319 -0.0161 -0.0093 0.0209  204  A1BAO A C3  
6671 C  C6  B A1BAO F .   ? 0.1588 0.2018 0.2401 0.0002  -0.0134 0.0263  204  A1BAO A C6  
6672 C  C9  B A1BAO F .   ? 0.1489 0.1912 0.2226 -0.0186 -0.0189 0.0486  204  A1BAO A C9  
6673 C  C12 B A1BAO F .   ? 0.1267 0.1314 0.1183 0.0049  -0.0102 0.0057  204  A1BAO A C12 
6674 C  C14 B A1BAO F .   ? 0.1041 0.1316 0.1036 -0.0022 -0.0031 0.0096  204  A1BAO A C14 
6675 C  C1  B A1BAO F .   ? 0.1157 0.1303 0.1534 -0.0099 0.0103  -0.0126 204  A1BAO A C1  
6676 C  C10 B A1BAO F .   ? 0.1115 0.1278 0.1121 -0.0038 -0.0076 0.0139  204  A1BAO A C10 
6677 C  C11 B A1BAO F .   ? 0.1338 0.1432 0.1250 0.0038  -0.0042 0.0172  204  A1BAO A C11 
6678 C  C13 B A1BAO F .   ? 0.1092 0.1325 0.1049 -0.0032 -0.0070 0.0063  204  A1BAO A C13 
6679 C  C15 B A1BAO F .   ? 0.1051 0.1243 0.1229 0.0001  -0.0101 0.0033  204  A1BAO A C15 
6680 C  C2  B A1BAO F .   ? 0.1169 0.1319 0.1270 -0.0101 -0.0015 0.0099  204  A1BAO A C2  
6681 C  C4  B A1BAO F .   ? 0.1409 0.1773 0.1702 -0.0174 -0.0139 0.0338  204  A1BAO A C4  
6682 C  C5  B A1BAO F .   ? 0.1531 0.1875 0.2162 -0.0045 -0.0122 0.0151  204  A1BAO A C5  
6683 C  C7  B A1BAO F .   ? 0.1477 0.2114 0.2281 -0.0009 -0.0209 0.0657  204  A1BAO A C7  
6684 C  C8  B A1BAO F .   ? 0.1503 0.2073 0.2410 -0.0093 -0.0218 0.0512  204  A1BAO A C8  
6685 N  N1  B A1BAO F .   ? 0.1058 0.1198 0.1088 -0.0036 -0.0108 0.0165  204  A1BAO A N1  
6686 N  N3  B A1BAO F .   ? 0.1347 0.1409 0.1211 0.0052  -0.0040 0.0164  204  A1BAO A N3  
6687 N  N4  B A1BAO F .   ? 0.1269 0.1276 0.1079 0.0071  -0.0130 0.0073  204  A1BAO A N4  
6688 O  O1  B A1BAO F .   ? 0.1142 0.1415 0.1810 -0.0128 0.0115  -0.0141 204  A1BAO A O1  
6689 O  O2  B A1BAO F .   ? 0.1409 0.2222 0.2454 0.0108  -0.0281 0.0955  204  A1BAO A O2  
6706 CL CL  B CL    G .   ? 0.1899 0.1484 0.2430 -0.0209 0.0292  -0.0067 205  CL    A CL  
6707 O  O   . HOH   H .   ? 0.5088 0.6115 0.4873 -0.1329 -0.1136 -0.1024 1301 HOH   A O   
6708 O  O   . HOH   H .   ? 0.6983 0.5774 0.4949 -0.1492 -0.0243 0.2219  1302 HOH   A O   
6709 O  O   . HOH   H .   ? 0.4285 0.7461 0.4262 -0.1158 0.0848  0.0554  1303 HOH   A O   
6710 O  O   . HOH   H .   ? 0.1443 0.5201 0.2069 -0.0332 0.0180  0.0431  1304 HOH   A O   
6711 O  O   A HOH   H .   ? 0.2524 0.2427 0.3318 -0.0637 -0.0132 0.0101  1305 HOH   A O   
6712 O  O   B HOH   H .   ? 0.2594 0.3919 0.2861 0.0523  0.0988  -0.0239 1306 HOH   A O   
6713 O  O   . HOH   H .   ? 0.5292 0.3406 0.4612 -0.0726 0.1135  0.1030  1307 HOH   A O   
6714 O  O   . HOH   H .   ? 0.4586 0.5699 0.3218 -0.1165 0.1575  0.1030  1308 HOH   A O   
6715 O  O   B HOH   H .   ? 0.1437 0.2683 0.1968 0.0260  0.0172  0.0463  1309 HOH   A O   
6716 O  O   . HOH   H .   ? 0.5631 0.4473 0.2830 0.1613  -0.1079 0.0501  1310 HOH   A O   
6717 O  O   . HOH   H .   ? 0.5945 0.3979 0.3275 -0.0839 -0.0763 0.0527  1311 HOH   A O   
6718 O  O   . HOH   H .   ? 0.2928 0.2986 0.1725 -0.0265 0.0488  0.0658  1312 HOH   A O   
6719 O  O   . HOH   H .   ? 0.3323 0.3119 0.2540 -0.1212 -0.0079 0.0717  1313 HOH   A O   
6720 O  O   . HOH   H .   ? 0.1650 0.2874 0.2553 0.0345  -0.0260 -0.0311 1314 HOH   A O   
6721 O  O   . HOH   H .   ? 0.4117 0.5179 0.4383 0.1673  0.0846  -0.1178 1315 HOH   A O   
6722 O  O   . HOH   H .   ? 0.2014 0.1770 0.3500 -0.0489 0.0101  -0.0171 1316 HOH   A O   
6723 O  O   . HOH   H .   ? 0.5806 0.4631 0.4681 -0.1182 0.1221  0.2052  1317 HOH   A O   
6724 O  O   . HOH   H .   ? 0.3105 0.2962 0.2917 -0.0855 0.0079  -0.0200 1318 HOH   A O   
6725 O  O   . HOH   H .   ? 0.2593 0.5044 0.3472 -0.1100 0.0660  0.0469  1319 HOH   A O   
6726 O  O   . HOH   H .   ? 0.3707 0.3325 0.3987 -0.0057 0.0566  0.0034  1320 HOH   A O   
6727 O  O   A HOH   H .   ? 0.2323 0.3037 0.4124 0.0274  0.0676  0.2008  1321 HOH   A O   
6728 O  O   . HOH   H .   ? 0.2800 0.6466 0.5464 -0.0613 -0.0757 0.1898  1322 HOH   A O   
6729 O  O   . HOH   H .   ? 0.1705 0.3295 0.4092 -0.0337 0.0502  -0.1004 1323 HOH   A O   
6730 O  O   A HOH   H .   ? 0.1804 0.3342 0.2116 0.0577  0.0342  0.0307  1324 HOH   A O   
6731 O  O   B HOH   H .   ? 0.2033 0.1230 0.1682 0.0295  -0.0284 0.0268  1325 HOH   A O   
6732 O  O   . HOH   H .   ? 0.6408 0.5017 0.3291 -0.0563 -0.0205 0.0518  1326 HOH   A O   
6733 O  O   . HOH   H .   ? 0.1411 0.1418 0.2119 -0.0241 0.0077  0.0083  1327 HOH   A O   
6734 O  O   . HOH   H .   ? 0.4674 0.2457 0.2828 -0.1150 0.0688  0.0259  1328 HOH   A O   
6735 O  O   . HOH   H .   ? 0.2166 0.5198 0.3554 -0.0280 -0.0571 0.1063  1329 HOH   A O   
6736 O  O   . HOH   H .   ? 0.2306 0.2103 0.2565 0.0466  0.0330  0.0458  1330 HOH   A O   
6737 O  O   . HOH   H .   ? 0.4051 0.3703 0.4024 -0.1746 -0.1091 0.1857  1331 HOH   A O   
6738 O  O   . HOH   H .   ? 0.5158 0.5205 0.3885 -0.1201 -0.1333 -0.1144 1332 HOH   A O   
6739 O  O   . HOH   H .   ? 0.5649 0.3893 0.5208 0.0153  -0.1013 0.0778  1333 HOH   A O   
6740 O  O   . HOH   H .   ? 0.2057 0.3683 0.3566 -0.0399 -0.0714 0.1348  1334 HOH   A O   
6741 O  O   . HOH   H .   ? 0.5978 0.5247 0.5525 -0.0190 0.2854  -0.1275 1335 HOH   A O   
6742 O  O   . HOH   H .   ? 0.1723 0.2215 0.1969 -0.0295 -0.0097 0.0834  1336 HOH   A O   
6743 O  O   . HOH   H .   ? 0.2331 0.4067 0.3390 0.0927  -0.0628 -0.0084 1337 HOH   A O   
6744 O  O   . HOH   H .   ? 0.3814 0.1704 0.4590 0.0202  -0.1762 0.0381  1338 HOH   A O   
6745 O  O   . HOH   H .   ? 0.2724 0.2651 0.4270 -0.0299 -0.1239 0.1361  1339 HOH   A O   
6746 O  O   . HOH   H .   ? 0.1867 0.1835 0.4036 0.0191  0.1013  -0.0188 1340 HOH   A O   
6747 O  O   . HOH   H .   ? 0.3044 0.3276 0.1958 -0.0838 -0.0283 -0.0549 1341 HOH   A O   
6748 O  O   . HOH   H .   ? 0.2374 0.3504 0.3267 -0.0823 -0.0299 -0.0487 1342 HOH   A O   
6749 O  O   . HOH   H .   ? 0.4440 0.1807 0.4301 0.0300  0.0375  0.0217  1343 HOH   A O   
6750 O  O   A HOH   H .   ? 0.1192 0.3143 0.1513 0.0712  0.0343  0.0925  1344 HOH   A O   
6751 O  O   B HOH   H .   ? 0.1907 0.2364 0.2906 -0.0391 0.0138  0.0073  1345 HOH   A O   
6752 O  O   . HOH   H .   ? 0.1358 0.2056 0.2084 0.0021  -0.0027 0.0509  1346 HOH   A O   
6753 O  O   . HOH   H .   ? 0.3126 0.4177 0.2079 -0.0234 0.0693  0.0279  1347 HOH   A O   
6754 O  O   . HOH   H .   ? 0.2512 0.4258 0.2825 -0.0494 0.0638  0.0188  1348 HOH   A O   
6755 O  O   A HOH   H .   ? 0.1469 0.1200 0.2273 0.0041  -0.0780 -0.0074 1349 HOH   A O   
6756 O  O   . HOH   H .   ? 0.2930 0.3221 0.4171 -0.0589 -0.1039 -0.0577 1350 HOH   A O   
6757 O  O   . HOH   H .   ? 0.1646 0.1556 0.1875 0.0168  -0.0242 0.0227  1351 HOH   A O   
6758 O  O   . HOH   H .   ? 0.1860 0.1499 0.2293 0.0202  -0.0288 0.0028  1352 HOH   A O   
6759 O  O   . HOH   H .   ? 0.3565 0.4525 0.3796 0.2079  0.0962  0.0915  1353 HOH   A O   
6760 O  O   . HOH   H .   ? 0.1500 0.1834 0.2392 0.0096  -0.0397 -0.0577 1354 HOH   A O   
6761 O  O   A HOH   H .   ? 0.3379 0.1539 0.1783 0.0364  0.0339  0.0087  1355 HOH   A O   
6762 O  O   . HOH   H .   ? 0.1321 0.1813 0.2435 0.0071  -0.0116 0.0006  1356 HOH   A O   
6763 O  O   . HOH   H .   ? 0.2058 0.1500 0.1536 -0.0093 0.0258  0.0141  1357 HOH   A O   
6764 O  O   . HOH   H .   ? 0.1226 0.1240 0.1322 -0.0015 0.0059  0.0124  1358 HOH   A O   
6765 O  O   . HOH   H .   ? 0.1327 0.1403 0.1491 -0.0062 -0.0125 -0.0006 1359 HOH   A O   
6766 O  O   . HOH   H .   ? 0.5927 0.5360 0.6320 -0.1248 -0.0671 0.1845  1360 HOH   A O   
6767 O  O   . HOH   H .   ? 0.1879 0.2435 0.3395 0.0230  0.0790  -0.0619 1361 HOH   A O   
6768 O  O   . HOH   H .   ? 0.6090 0.3718 0.2584 -0.0344 -0.0181 0.1471  1362 HOH   A O   
6769 O  O   A HOH   H .   ? 0.2147 0.4252 0.4401 0.0436  0.0554  0.1281  1363 HOH   A O   
6770 O  O   . HOH   H .   ? 0.1823 0.1738 0.2312 -0.0289 0.0102  0.0412  1364 HOH   A O   
6771 O  O   . HOH   H .   ? 0.4489 0.2580 0.3796 -0.1666 0.1432  -0.0776 1365 HOH   A O   
6772 O  O   . HOH   H .   ? 0.1405 0.1199 0.2094 -0.0051 0.0172  -0.0048 1366 HOH   A O   
6773 O  O   . HOH   H .   ? 0.2351 0.2526 0.3171 -0.0161 -0.0124 -0.0548 1367 HOH   A O   
6774 O  O   . HOH   H .   ? 0.2728 0.4830 0.4879 0.0423  0.0458  0.0918  1368 HOH   A O   
6775 O  O   . HOH   H .   ? 0.2184 0.4976 0.3038 -0.0742 -0.0127 0.0938  1369 HOH   A O   
6776 O  O   . HOH   H .   ? 0.2522 0.4287 0.3047 0.0751  0.0844  0.1928  1370 HOH   A O   
6777 O  O   . HOH   H .   ? 0.4004 0.2166 0.4412 -0.1170 0.0840  0.0248  1371 HOH   A O   
6778 O  O   . HOH   H .   ? 0.1597 0.1595 0.2087 -0.0277 0.0151  0.0292  1372 HOH   A O   
6779 O  O   . HOH   H .   ? 0.3777 0.6289 0.4781 -0.0667 -0.1259 0.0987  1373 HOH   A O   
6780 O  O   . HOH   H .   ? 0.1772 0.2162 0.2212 -0.0209 -0.0463 0.0370  1374 HOH   A O   
6781 O  O   A HOH   H .   ? 0.2113 0.2300 0.2315 0.0758  0.0541  0.0715  1375 HOH   A O   
6782 O  O   . HOH   H .   ? 0.3290 0.3964 0.1939 -0.0506 -0.0922 0.0601  1376 HOH   A O   
6783 O  O   T HOH   H .   ? 0.0973 0.0916 0.1902 -0.0175 0.0033  0.0339  1377 HOH   A O   
6784 O  O   A HOH   H .   ? 0.1810 0.1976 0.1806 -0.0194 0.0406  0.0582  1378 HOH   A O   
6785 O  O   . HOH   H .   ? 0.3873 0.1964 0.2190 0.1091  0.0535  0.0245  1379 HOH   A O   
6786 O  O   . HOH   H .   ? 0.2472 0.2092 0.2045 -0.0509 0.0237  -0.0018 1380 HOH   A O   
6787 O  O   . HOH   H .   ? 0.2976 0.6815 0.4044 0.1525  0.0630  -0.0467 1381 HOH   A O   
6788 O  O   . HOH   H .   ? 0.2179 0.1856 0.1701 -0.0435 0.0102  0.0342  1382 HOH   A O   
6789 O  O   . HOH   H .   ? 0.2883 0.2705 0.2131 0.0378  0.0789  0.0167  1383 HOH   A O   
6790 O  O   . HOH   H .   ? 0.2230 0.2013 0.5158 0.0092  -0.1129 0.0393  1384 HOH   A O   
6791 O  O   . HOH   H .   ? 0.2457 0.3313 0.3224 -0.1035 0.0549  -0.0064 1385 HOH   A O   
6792 O  O   . HOH   H .   ? 0.2953 0.2301 0.4951 -0.0764 -0.0294 0.0145  1386 HOH   A O   
6793 O  O   B HOH   H .   ? 0.3448 0.2828 0.2918 -0.1095 0.1258  0.0420  1387 HOH   A O   
6794 O  O   . HOH   H .   ? 0.7646 0.4727 0.6908 -0.0449 -0.1309 0.1039  1388 HOH   A O   
6795 O  O   B HOH   H .   ? 0.2648 0.3541 0.2195 0.1662  0.0661  0.1079  1389 HOH   A O   
6796 O  O   . HOH   H .   ? 0.4981 0.3403 0.5023 0.0433  0.1820  -0.1157 1390 HOH   A O   
6797 O  O   A HOH   H .   ? 0.3885 0.3863 0.3437 -0.0758 0.0353  0.1330  1391 HOH   A O   
6798 O  O   . HOH   H .   ? 0.3069 0.2381 0.2965 -0.0022 -0.0423 0.0729  1392 HOH   A O   
6799 O  O   . HOH   H .   ? 0.1687 0.1648 0.1594 0.0026  0.0072  0.0098  1393 HOH   A O   
6800 O  O   . HOH   H .   ? 0.2386 0.3659 0.3593 -0.0217 0.1052  -0.0797 1394 HOH   A O   
6801 O  O   B HOH   H .   ? 0.3027 0.5004 0.1638 -0.0605 0.0449  0.0385  1395 HOH   A O   
6802 O  O   . HOH   H .   ? 0.4201 0.3640 0.1895 -0.0513 0.0620  0.0532  1396 HOH   A O   
6803 O  O   . HOH   H .   ? 0.1246 0.1335 0.1576 0.0008  -0.0164 0.0049  1397 HOH   A O   
6804 O  O   . HOH   H .   ? 0.1746 0.1841 0.3853 0.0407  0.1021  0.1121  1398 HOH   A O   
6805 O  O   . HOH   H .   ? 0.1707 0.2526 0.3636 -0.0019 -0.0294 0.0281  1399 HOH   A O   
6806 O  O   . HOH   H .   ? 0.1940 0.2000 0.2521 -0.0256 -0.0237 0.0768  1400 HOH   A O   
6807 O  O   . HOH   H .   ? 0.5738 0.5649 0.3783 0.1793  -0.0434 -0.0482 1401 HOH   A O   
6808 O  O   . HOH   H .   ? 0.2080 0.1611 0.2768 -0.0043 -0.0309 0.0086  1402 HOH   A O   
6809 O  O   . HOH   H .   ? 0.2946 0.6311 0.4186 -0.0064 0.0209  0.2183  1403 HOH   A O   
6810 O  O   A HOH   H .   ? 0.1302 0.1110 0.1448 -0.0093 -0.0174 0.0070  1404 HOH   A O   
6811 O  O   . HOH   H .   ? 0.2474 0.1705 0.2407 -0.0143 0.0140  0.0259  1405 HOH   A O   
6812 O  O   . HOH   H .   ? 0.5973 0.2842 0.4405 0.1284  -0.1012 -0.0498 1406 HOH   A O   
6813 O  O   . HOH   H .   ? 0.2797 0.2508 0.2239 -0.0643 -0.1089 0.0444  1407 HOH   A O   
6814 O  O   . HOH   H .   ? 0.2937 0.3540 0.4529 -0.0428 0.1217  -0.0282 1408 HOH   A O   
6815 O  O   . HOH   H .   ? 0.1421 0.1507 0.2860 -0.0046 0.0030  0.0244  1409 HOH   A O   
6816 O  O   . HOH   H .   ? 0.2326 0.1993 0.2406 -0.0548 -0.0084 0.0536  1410 HOH   A O   
6817 O  O   . HOH   H .   ? 0.1588 0.1319 0.1472 -0.0188 0.0124  0.0009  1411 HOH   A O   
6818 O  O   . HOH   H .   ? 0.4034 0.2199 0.5220 -0.0728 -0.2115 0.1169  1412 HOH   A O   
6819 O  O   . HOH   H .   ? 0.2548 0.3364 0.7361 -0.0162 0.1218  -0.0442 1413 HOH   A O   
6820 O  O   . HOH   H .   ? 0.1891 0.2750 0.2410 -0.0128 -0.0553 0.0503  1414 HOH   A O   
6821 O  O   A HOH   H .   ? 0.2008 0.1760 0.2000 0.0203  -0.0028 0.0450  1415 HOH   A O   
6822 O  O   A HOH   H .   ? 0.0936 0.1424 0.1035 0.0278  -0.0321 -0.0171 1416 HOH   A O   
6823 O  O   A HOH   H .   ? 0.2033 0.2006 0.2745 -0.0295 0.0449  -0.0033 1417 HOH   A O   
6824 O  O   . HOH   H .   ? 0.4853 0.4693 0.3979 -0.0684 -0.1658 0.0402  1418 HOH   A O   
6825 O  O   . HOH   H .   ? 0.2617 0.6068 0.1792 -0.0244 0.0480  0.0376  1419 HOH   A O   
6826 O  O   . HOH   H .   ? 0.3145 0.1187 0.1980 -0.0021 -0.0461 0.0165  1420 HOH   A O   
6827 O  O   A HOH   H .   ? 0.1699 0.1876 0.3288 0.0126  -0.0426 -0.0723 1421 HOH   A O   
6828 O  O   A HOH   H .   ? 0.1174 0.2316 0.2687 -0.0030 0.0560  0.0732  1422 HOH   A O   
6829 O  O   . HOH   H .   ? 0.4925 0.5680 0.5219 0.0848  0.0501  0.0679  1423 HOH   A O   
6830 O  O   . HOH   H .   ? 0.2176 0.3820 0.2443 0.1501  0.0058  0.0363  1424 HOH   A O   
6831 O  O   . HOH   H .   ? 0.1555 0.2154 0.2483 -0.0204 -0.0032 0.0541  1425 HOH   A O   
6832 O  O   B HOH   H .   ? 0.1387 0.1773 0.1623 -0.0323 -0.0265 0.0199  1426 HOH   A O   
6833 O  O   . HOH   H .   ? 0.4970 0.5381 0.5933 -0.0765 -0.1144 -0.0652 1427 HOH   A O   
6834 O  O   . HOH   H .   ? 0.3824 0.2729 0.5645 0.0658  0.0548  0.0148  1428 HOH   A O   
6835 O  O   . HOH   H .   ? 0.4203 0.6442 0.3060 -0.1089 -0.0353 0.1265  1429 HOH   A O   
6836 O  O   . HOH   H .   ? 0.3849 0.4164 0.3216 0.1706  -0.0975 -0.1605 1430 HOH   A O   
6837 O  O   . HOH   H .   ? 0.6300 0.6811 0.4534 0.0671  0.3066  0.0407  1431 HOH   A O   
6838 O  O   A HOH   H .   ? 0.2047 0.2467 0.2183 -0.0298 0.0834  -0.0054 1432 HOH   A O   
6839 O  O   . HOH   H .   ? 0.5338 0.6995 0.5555 0.1743  0.0261  0.0633  1433 HOH   A O   
6840 O  O   . HOH   H .   ? 0.1941 0.1816 0.3063 0.0274  -0.0598 0.0233  1434 HOH   A O   
6841 O  O   . HOH   H .   ? 0.6565 0.6789 0.6116 -0.1261 0.0100  0.0460  1435 HOH   A O   
6842 O  O   . HOH   H .   ? 0.3763 0.2850 0.2292 -0.0386 -0.0295 0.0133  1436 HOH   A O   
6843 O  O   . HOH   H .   ? 0.6527 0.3814 0.4800 0.1783  -0.0875 0.1310  1437 HOH   A O   
6844 O  O   . HOH   H .   ? 0.5753 0.7326 0.4133 0.1406  -0.1059 0.1640  1438 HOH   A O   
6845 O  O   . HOH   H .   ? 0.3227 0.2619 0.1626 -0.0824 0.0092  0.0463  1439 HOH   A O   
6846 O  O   . HOH   H .   ? 0.8957 0.8869 0.6962 -0.0203 -0.1145 -0.0158 1440 HOH   A O   
6847 O  O   A HOH   H .   ? 0.1175 0.1431 0.1082 0.0147  -0.0228 0.0082  1441 HOH   A O   
6848 O  O   . HOH   H .   ? 0.3835 0.4679 0.4855 -0.1066 -0.0840 -0.1293 1442 HOH   A O   
6849 O  O   . HOH   H .   ? 0.2385 0.1503 0.2555 0.0116  0.0059  0.0078  1443 HOH   A O   
6850 O  O   A HOH   H .   ? 0.1459 0.0853 0.0971 0.0108  -0.0254 0.0171  1444 HOH   A O   
6851 O  O   . HOH   H .   ? 0.5876 0.4387 0.5722 0.1292  0.1096  0.2235  1445 HOH   A O   
6852 O  O   A HOH   H .   ? 0.2137 0.2298 0.3478 0.0449  0.0430  -0.0832 1446 HOH   A O   
6853 O  O   . HOH   H .   ? 0.5022 0.5904 0.6111 -0.1406 0.0505  -0.1283 1447 HOH   A O   
6854 O  O   . HOH   H .   ? 0.1834 0.2185 0.4437 -0.0293 -0.0915 0.0630  1448 HOH   A O   
6855 O  O   . HOH   H .   ? 0.6360 0.6750 0.5259 -0.0564 0.1085  0.2183  1449 HOH   A O   
6856 O  O   . HOH   H .   ? 0.7084 0.6956 0.6928 0.0684  -0.1153 0.0204  1450 HOH   A O   
6857 O  O   . HOH   H .   ? 0.3809 0.3509 0.2719 0.2133  -0.0317 -0.0151 1451 HOH   A O   
6858 O  O   A HOH   H .   ? 0.4420 0.2522 0.4351 0.0339  0.0834  -0.0491 1452 HOH   A O   
6859 O  O   A HOH   H .   ? 0.5245 0.2867 0.2861 -0.0501 0.0717  0.0430  1453 HOH   A O   
6860 O  O   . HOH   H .   ? 0.6696 0.5220 0.7793 0.0920  -0.1076 0.1376  1454 HOH   A O   
6861 O  O   . HOH   H .   ? 0.2007 0.2555 0.2372 0.0009  -0.0169 -0.0445 1455 HOH   A O   
6862 O  O   . HOH   H .   ? 0.2201 0.1985 0.2764 0.0186  0.0385  0.0387  1456 HOH   A O   
6863 O  O   B HOH   H .   ? 0.2613 0.4131 0.3621 0.0609  0.0208  -0.0361 1457 HOH   A O   
6864 O  O   B HOH   H .   ? 0.1688 0.2126 0.3257 -0.0291 -0.0614 0.1186  1458 HOH   A O   
6865 O  O   B HOH   H .   ? 0.5093 0.3028 0.3892 0.0889  0.0424  0.0574  1459 HOH   A O   
6866 O  O   . HOH   H .   ? 0.4395 0.3554 0.3415 0.0815  0.0443  0.0805  1460 HOH   A O   
6867 O  O   . HOH   H .   ? 0.3979 0.3881 0.4246 0.0864  -0.0389 0.0656  1461 HOH   A O   
6868 O  O   B HOH   H .   ? 0.1735 0.1256 0.1809 -0.0133 -0.0392 0.0592  1462 HOH   A O   
6869 O  O   . HOH   H .   ? 0.3841 0.3556 0.3994 -0.0081 0.0722  0.0439  1463 HOH   A O   
6870 O  O   . HOH   H .   ? 0.6803 0.7642 0.4722 0.0698  -0.0793 -0.0612 1464 HOH   A O   
6871 O  O   . HOH   H .   ? 0.2998 0.3700 0.3023 0.1509  -0.0386 -0.0318 1465 HOH   A O   
6872 O  O   . HOH   H .   ? 0.2380 0.2782 0.3597 -0.0558 0.0604  -0.0801 1466 HOH   A O   
6873 O  O   B HOH   H .   ? 0.2463 0.1554 0.2337 -0.0765 -0.0763 0.0625  1467 HOH   A O   
6874 O  O   . HOH   H .   ? 0.3095 0.4797 0.4257 0.0754  -0.1131 0.1449  1468 HOH   A O   
6875 O  O   . HOH   H .   ? 0.2878 0.4544 0.5179 -0.1495 0.1059  -0.2019 1469 HOH   A O   
6876 O  O   . HOH   H .   ? 0.6019 0.3440 0.6858 0.1136  -0.0027 0.2264  1470 HOH   A O   
6877 O  O   . HOH   H .   ? 0.2441 0.2421 0.3022 -0.0832 0.0374  -0.0164 1471 HOH   A O   
6878 O  O   . HOH   H .   ? 0.2709 0.4687 0.4212 0.0826  0.0031  -0.1880 1472 HOH   A O   
6879 O  O   . HOH   H .   ? 0.3453 0.4404 0.3828 -0.1134 -0.0324 -0.0117 1473 HOH   A O   
6880 O  O   . HOH   H .   ? 0.3905 0.6376 0.4084 -0.1090 -0.0971 0.2174  1474 HOH   A O   
6881 O  O   A HOH   H .   ? 0.2497 0.2112 0.4058 0.0379  -0.0768 -0.0552 1475 HOH   A O   
6882 O  O   . HOH   H .   ? 0.6427 0.5952 0.7057 0.0552  0.2370  0.2465  1476 HOH   A O   
6883 O  O   . HOH   H .   ? 0.2569 0.1653 0.2311 0.0378  -0.0867 -0.0351 1477 HOH   A O   
6884 O  O   . HOH   H .   ? 0.3578 0.4820 0.3366 0.0240  -0.0244 -0.0848 1478 HOH   A O   
6885 O  O   . HOH   H .   ? 0.5089 0.5436 0.3817 0.0848  -0.0478 -0.0442 1479 HOH   A O   
6886 O  O   . HOH   H .   ? 0.2982 0.2286 0.3229 0.0255  0.0690  -0.0093 1480 HOH   A O   
6887 O  O   . HOH   H .   ? 0.4978 0.4586 0.4529 0.0209  0.0808  0.0579  1481 HOH   A O   
6888 O  O   . HOH   H .   ? 0.3926 0.4507 0.2725 0.0077  -0.0064 0.0129  1482 HOH   A O   
6889 O  O   . HOH   H .   ? 0.4409 0.4031 0.3022 -0.0362 -0.0418 -0.0296 1483 HOH   A O   
6890 O  O   B HOH   H .   ? 0.3025 0.2120 0.2302 0.0534  0.0732  0.0185  1484 HOH   A O   
6891 O  O   . HOH   H .   ? 0.5254 0.4193 0.3865 -0.0273 0.1114  -0.0305 1485 HOH   A O   
6892 O  O   . HOH   H .   ? 0.4901 0.5469 0.5369 -0.1625 -0.1326 0.0258  1486 HOH   A O   
6893 O  O   . HOH   H .   ? 0.2855 0.4554 0.2885 -0.0345 0.0024  -0.0584 1487 HOH   A O   
6894 O  O   . HOH   H .   ? 0.4834 0.4058 0.4970 -0.1891 -0.0845 -0.0340 1488 HOH   A O   
6895 O  O   . HOH   H .   ? 0.6535 0.5376 0.6704 -0.0626 0.0401  -0.0810 1489 HOH   A O   
6896 O  O   . HOH   H .   ? 0.5319 0.4242 0.4519 -0.0303 -0.0029 -0.1011 1490 HOH   A O   
6897 O  O   . HOH   H .   ? 0.5998 0.5412 0.4262 -0.0929 0.1254  0.1053  1491 HOH   A O   
6898 O  O   . HOH   H .   ? 0.7136 0.3636 0.3284 -0.0561 -0.1274 0.0435  1492 HOH   A O   
6899 O  O   . HOH   H .   ? 0.2746 0.2201 0.2200 0.0498  0.0045  0.0029  1493 HOH   A O   
6900 O  O   . HOH   H .   ? 0.6288 0.5054 0.4959 -0.0932 -0.1063 -0.0782 1494 HOH   A O   
6901 O  O   . HOH   H .   ? 0.4266 0.2565 0.3263 -0.0662 -0.1343 0.0796  1495 HOH   A O   
6902 O  O   . HOH   H .   ? 0.2731 0.3853 0.4326 0.0098  0.1168  0.1049  1496 HOH   A O   
6903 O  O   . HOH   H .   ? 0.2465 0.5160 0.3731 0.1233  0.0992  0.2443  1497 HOH   A O   
6904 O  O   . HOH   H .   ? 0.6412 0.2295 0.3971 -0.0623 0.0905  0.0454  1498 HOH   A O   
6905 O  O   . HOH   H .   ? 0.5494 0.6693 0.4983 0.1193  -0.1177 -0.0682 1499 HOH   A O   
6906 O  O   . HOH   H .   ? 0.2466 0.2290 0.7489 0.0010  -0.1257 0.0155  1500 HOH   A O   
6907 O  O   . HOH   H .   ? 0.5775 0.5947 0.6788 0.1479  0.1845  -0.1080 1501 HOH   A O   
6908 O  O   . HOH   H .   ? 0.4388 0.3216 0.2588 -0.0697 0.1567  -0.0346 1502 HOH   A O   
6909 O  O   . HOH   H .   ? 0.4572 0.3259 0.4917 0.0032  0.2398  0.0618  1503 HOH   A O   
6910 O  O   . HOH   H .   ? 0.4293 0.3218 0.4554 -0.1109 0.0356  0.1036  1504 HOH   A O   
6911 O  O   . HOH   H .   ? 0.2880 0.1947 0.5346 0.0141  0.0798  0.0927  1505 HOH   A O   
6912 O  O   . HOH   H .   ? 0.4914 0.5647 0.4850 0.0591  -0.1163 0.0644  1506 HOH   A O   
6913 O  O   . HOH   H .   ? 0.2498 0.2835 0.4704 0.0089  0.0901  -0.0369 1507 HOH   A O   
6914 O  O   . HOH   H .   ? 0.3799 0.7466 0.5888 -0.1053 -0.0499 0.2137  1508 HOH   A O   
6915 O  O   . HOH   H .   ? 0.2281 0.3548 0.3278 0.0551  -0.0554 0.0594  1509 HOH   A O   
6916 O  O   . HOH   H .   ? 0.4435 0.2587 0.4069 -0.1461 -0.0062 0.0532  1510 HOH   A O   
6917 O  O   . HOH   H .   ? 0.2800 0.4448 0.4306 0.0318  -0.0727 -0.0287 1511 HOH   A O   
6918 O  O   . HOH   H .   ? 0.4916 0.6925 0.5420 0.1139  -0.0453 0.0716  1512 HOH   A O   
6919 O  O   . HOH   H .   ? 0.6191 0.3221 0.5123 -0.0144 -0.0302 0.1669  1513 HOH   A O   
6920 O  O   . HOH   H .   ? 0.4732 0.6778 0.4766 0.3087  0.0151  0.1160  1514 HOH   A O   
6921 O  O   . HOH   H .   ? 0.2787 0.2238 0.4327 -0.0022 0.0481  0.0343  1515 HOH   A O   
6922 O  O   . HOH   H .   ? 0.4972 0.6424 0.4592 -0.0951 -0.0735 -0.1361 1516 HOH   A O   
6923 O  O   T HOH   H .   ? 0.0665 0.1269 0.2126 -0.0057 0.0005  0.0783  1517 HOH   A O   
6924 O  O   B HOH   H .   ? 0.4719 0.2782 0.3689 0.1297  0.0702  0.1105  1518 HOH   A O   
6925 O  O   B HOH   H .   ? 0.4001 0.3557 0.3968 0.1081  0.0794  0.1049  1519 HOH   A O   
6926 O  O   A HOH   H .   ? 0.3873 0.6715 0.3420 0.1019  -0.0266 0.0080  1520 HOH   A O   
6927 O  O   . HOH   H .   ? 0.2387 0.6597 0.3934 0.0872  0.0188  -0.0292 1521 HOH   A O   
6928 O  O   . HOH   H .   ? 0.4987 0.6744 0.5668 -0.1042 -0.0704 0.0795  1522 HOH   A O   
6929 O  O   . HOH   H .   ? 0.4396 0.5321 0.4958 0.1661  -0.0278 0.1523  1523 HOH   A O   
6930 O  O   . HOH   H .   ? 0.3625 0.4221 0.4646 -0.0790 -0.1059 0.2347  1524 HOH   A O   
6931 O  O   . HOH   I .   ? 0.2374 0.2033 0.2872 0.0187  0.0847  0.0236  201  HOH   B O   
6932 O  O   . HOH   I .   ? 0.3172 0.3299 0.6360 -0.0348 0.0283  -0.0020 202  HOH   B O   
6933 O  O   . HOH   I .   ? 0.4439 0.3566 0.4181 -0.0221 -0.0200 -0.1452 203  HOH   B O   
6934 O  O   . HOH   I .   ? 0.2666 0.3667 0.5352 -0.0640 0.0319  -0.1321 204  HOH   B O   
6935 O  O   . HOH   I .   ? 0.3104 0.5031 0.5461 -0.0106 0.1818  -0.1797 205  HOH   B O   
6936 O  O   . HOH   I .   ? 0.4659 0.4790 0.2448 -0.0293 -0.0259 -0.1373 206  HOH   B O   
6937 O  O   . HOH   I .   ? 0.4611 0.5425 0.3358 0.2674  -0.1153 -0.0401 207  HOH   B O   
6938 O  O   . HOH   I .   ? 0.4339 0.4366 0.3969 0.0568  0.0591  -0.1573 208  HOH   B O   
6939 O  O   . HOH   I .   ? 0.1820 0.2049 0.2933 0.0026  0.0363  -0.0326 209  HOH   B O   
6940 O  O   . HOH   I .   ? 0.6878 0.3292 0.4154 0.0034  0.1013  -0.0247 210  HOH   B O   
6941 O  O   . HOH   I .   ? 0.5105 0.3931 0.5963 0.0810  -0.0709 0.2481  211  HOH   B O   
6942 O  O   . HOH   I .   ? 0.1536 0.1851 0.2790 -0.0195 -0.0096 0.0096  212  HOH   B O   
6943 O  O   . HOH   I .   ? 0.2791 0.6899 0.3313 0.0894  0.0234  0.2157  213  HOH   B O   
6944 O  O   . HOH   I .   ? 0.2812 0.1971 0.5213 0.0140  0.1766  0.0850  214  HOH   B O   
6945 O  O   . HOH   I .   ? 0.3169 0.3677 0.4992 0.0544  0.0039  -0.0321 215  HOH   B O   
6946 O  O   . HOH   I .   ? 0.5888 0.2932 0.3631 -0.1904 -0.0051 0.0138  216  HOH   B O   
6947 O  O   . HOH   I .   ? 0.2988 0.2051 0.4768 0.0065  0.1730  0.0277  217  HOH   B O   
6948 O  O   . HOH   I .   ? 0.2580 0.2634 0.6519 0.0443  -0.0986 0.0656  218  HOH   B O   
6949 O  O   . HOH   I .   ? 0.3195 0.5355 0.4918 0.2182  0.0377  -0.0553 219  HOH   B O   
6950 O  O   . HOH   I .   ? 0.3852 0.4969 0.3934 0.2222  -0.0447 0.0275  220  HOH   B O   
6951 O  O   . HOH   I .   ? 0.4151 0.3875 0.3312 0.0402  -0.1074 0.0676  221  HOH   B O   
6952 O  O   . HOH   I .   ? 0.4146 0.6593 0.3242 0.2142  0.0385  -0.0249 222  HOH   B O   
6953 O  O   . HOH   I .   ? 0.3925 0.4175 0.6311 0.0090  -0.1499 -0.0893 223  HOH   B O   
6954 O  O   . HOH   I .   ? 0.1607 0.2035 0.3001 -0.0176 0.0067  -0.0234 224  HOH   B O   
6955 O  O   . HOH   I .   ? 0.6676 0.3973 0.2503 -0.0143 0.0405  0.0247  225  HOH   B O   
6956 O  O   . HOH   I .   ? 0.2048 0.2108 0.4265 -0.0340 0.0019  -0.0551 226  HOH   B O   
6957 O  O   . HOH   I .   ? 0.4567 0.1975 0.2844 -0.0085 -0.1054 0.0146  227  HOH   B O   
6958 O  O   . HOH   I .   ? 0.2455 0.1767 0.2582 -0.0321 0.1051  -0.0133 228  HOH   B O   
6959 O  O   . HOH   I .   ? 0.2856 0.3466 0.5544 0.0165  0.0386  -0.0221 229  HOH   B O   
6960 O  O   . HOH   I .   ? 0.6236 0.5935 0.3481 0.0843  0.0503  0.0059  230  HOH   B O   
6961 O  O   . HOH   I .   ? 0.3725 0.1704 0.1771 0.0211  -0.0861 -0.0057 231  HOH   B O   
6962 O  O   . HOH   I .   ? 0.6743 0.6263 0.5511 0.1826  -0.0053 -0.0023 232  HOH   B O   
6963 O  O   . HOH   I .   ? 0.2548 0.2469 0.2963 0.0420  0.0129  -0.0928 233  HOH   B O   
6964 O  O   . HOH   I .   ? 0.3524 0.2956 0.3940 0.1093  -0.0239 -0.0431 234  HOH   B O   
6965 O  O   . HOH   I .   ? 0.3753 0.4223 0.4836 -0.1374 -0.0133 0.1200  235  HOH   B O   
6966 O  O   . HOH   I .   ? 0.3468 0.2928 0.1986 0.0309  0.0619  0.0474  236  HOH   B O   
6967 O  O   . HOH   I .   ? 0.1983 0.2386 0.3010 -0.0575 0.0068  -0.0141 237  HOH   B O   
6968 O  O   . HOH   I .   ? 0.2332 0.2148 0.2275 0.0845  -0.0794 -0.0699 238  HOH   B O   
6969 O  O   . HOH   I .   ? 0.3426 0.2471 0.4081 0.0204  -0.0794 -0.1234 239  HOH   B O   
6970 O  O   . HOH   I .   ? 0.2030 0.3723 0.2386 -0.0585 -0.0204 0.0776  240  HOH   B O   
6971 O  O   . HOH   I .   ? 0.1890 0.1290 0.3222 0.0076  -0.0544 -0.0112 241  HOH   B O   
6972 O  O   . HOH   I .   ? 0.1524 0.1342 0.2580 -0.0017 0.0102  -0.0056 242  HOH   B O   
6973 O  O   . HOH   I .   ? 0.5019 0.3077 0.3844 -0.2207 0.0318  0.0017  243  HOH   B O   
6974 O  O   . HOH   I .   ? 0.1362 0.1340 0.1453 -0.0147 -0.0051 0.0005  244  HOH   B O   
6975 O  O   . HOH   I .   ? 0.2071 0.3741 0.3002 -0.0604 -0.0491 -0.0679 245  HOH   B O   
6976 O  O   . HOH   I .   ? 0.2391 0.4190 0.5383 -0.0090 0.0021  -0.0848 246  HOH   B O   
6977 O  O   . HOH   I .   ? 0.1991 0.1830 0.1971 -0.0244 -0.0448 0.0149  247  HOH   B O   
6978 O  O   . HOH   I .   ? 0.2558 0.3361 0.3038 -0.0735 0.0375  -0.0703 248  HOH   B O   
6979 O  O   . HOH   I .   ? 0.2368 0.2149 0.1877 0.0219  -0.0133 0.0004  249  HOH   B O   
6980 O  O   . HOH   I .   ? 0.1383 0.1217 0.1551 0.0040  -0.0074 0.0142  250  HOH   B O   
6981 O  O   . HOH   I .   ? 0.2866 0.1741 0.6200 -0.0061 -0.1191 -0.0469 251  HOH   B O   
6982 O  O   . HOH   I .   ? 0.2434 0.3945 0.5175 0.1160  -0.0499 -0.1066 252  HOH   B O   
6983 O  O   . HOH   I .   ? 0.3701 0.3404 0.2086 0.0345  0.1167  0.0056  253  HOH   B O   
6984 O  O   . HOH   I .   ? 0.1728 0.2526 0.2684 0.0386  0.0414  0.0950  254  HOH   B O   
6985 O  O   . HOH   I .   ? 0.2785 0.2258 0.2818 0.0917  0.0810  0.0025  255  HOH   B O   
6986 O  O   . HOH   I .   ? 0.1996 0.1468 0.1940 -0.0279 -0.0348 0.0269  256  HOH   B O   
6987 O  O   . HOH   I .   ? 0.2157 0.3008 0.2077 -0.0607 0.0317  0.0414  257  HOH   B O   
6988 O  O   . HOH   I .   ? 0.1508 0.1539 0.3100 -0.0220 -0.0198 0.0088  258  HOH   B O   
6989 O  O   . HOH   I .   ? 0.2618 0.4018 0.2995 -0.0866 -0.0417 -0.0476 259  HOH   B O   
6990 O  O   . HOH   I .   ? 0.3273 0.2604 0.2854 -0.0526 0.0368  -0.0547 260  HOH   B O   
6991 O  O   . HOH   I .   ? 0.1280 0.1511 0.1909 -0.0078 0.0020  0.0152  261  HOH   B O   
6992 O  O   . HOH   I .   ? 0.6554 0.4709 0.5059 0.2055  -0.0081 -0.0874 262  HOH   B O   
6993 O  O   . HOH   I .   ? 0.2091 0.1772 0.3246 -0.0041 -0.0367 -0.0249 263  HOH   B O   
6994 O  O   . HOH   I .   ? 0.2348 0.1935 0.1803 0.0115  0.0040  0.0015  264  HOH   B O   
6995 O  O   . HOH   I .   ? 0.3804 0.2973 0.4157 -0.0118 -0.1372 -0.0588 265  HOH   B O   
6996 O  O   . HOH   I .   ? 0.1872 0.1673 0.1602 -0.0435 -0.0418 0.0104  266  HOH   B O   
6997 O  O   . HOH   I .   ? 0.2538 0.4219 0.3888 0.0274  0.1455  0.0237  267  HOH   B O   
6998 O  O   . HOH   I .   ? 0.2272 0.2806 0.2341 -0.0354 -0.0750 0.0158  268  HOH   B O   
6999 O  O   . HOH   I .   ? 0.1935 0.1448 0.2131 -0.0296 -0.0178 0.0193  269  HOH   B O   
7000 O  O   . HOH   I .   ? 0.2053 0.4247 0.5085 -0.0347 -0.0475 -0.1461 270  HOH   B O   
7001 O  O   . HOH   I .   ? 0.2386 0.1858 0.2782 -0.0637 0.0163  -0.0154 271  HOH   B O   
7002 O  O   . HOH   I .   ? 0.2227 0.2408 0.2135 -0.0339 -0.0576 -0.0393 272  HOH   B O   
7003 O  O   . HOH   I .   ? 0.4054 0.5074 0.3974 0.0417  -0.1297 0.0297  273  HOH   B O   
7004 O  O   . HOH   I .   ? 0.3256 0.4543 0.5198 0.0644  0.0081  0.0612  274  HOH   B O   
7005 O  O   . HOH   I .   ? 0.1998 0.3217 0.2280 0.0797  -0.0273 -0.0315 275  HOH   B O   
7006 O  O   . HOH   I .   ? 0.3025 0.4658 0.3687 -0.0305 -0.0803 0.1214  276  HOH   B O   
7007 O  O   . HOH   I .   ? 0.1691 0.1331 0.3964 -0.0076 -0.0232 -0.0169 277  HOH   B O   
7008 O  O   . HOH   I .   ? 0.2301 0.3362 0.2914 -0.0414 0.0590  -0.1089 278  HOH   B O   
7009 O  O   . HOH   I .   ? 0.2758 0.2025 0.5417 0.0136  0.0623  0.0671  279  HOH   B O   
7010 O  O   . HOH   I .   ? 0.3130 0.3700 0.4373 0.1201  -0.0496 -0.0880 280  HOH   B O   
7011 O  O   . HOH   I .   ? 0.4739 0.3404 0.3899 -0.1128 0.0718  -0.0993 281  HOH   B O   
7012 O  O   . HOH   I .   ? 0.1515 0.1463 0.3244 -0.0126 0.0089  -0.0079 282  HOH   B O   
7013 O  O   . HOH   I .   ? 0.1595 0.1447 0.1805 -0.0012 0.0079  0.0046  283  HOH   B O   
7014 O  O   . HOH   I .   ? 0.2640 0.4387 0.5109 -0.1028 -0.1448 0.0880  284  HOH   B O   
7015 O  O   . HOH   I .   ? 0.3533 0.2426 0.1965 0.0405  -0.0768 -0.0149 285  HOH   B O   
7016 O  O   . HOH   I .   ? 0.1622 0.3195 0.4653 0.0206  0.0063  -0.1346 286  HOH   B O   
7017 O  O   . HOH   I .   ? 0.1580 0.1923 0.1400 -0.0150 -0.0113 0.0071  287  HOH   B O   
7018 O  O   . HOH   I .   ? 0.2519 0.6038 0.2244 0.0750  -0.0429 -0.0104 288  HOH   B O   
7019 O  O   . HOH   I .   ? 0.2809 0.6545 0.6648 0.0874  -0.0344 -0.0759 289  HOH   B O   
7020 O  O   . HOH   I .   ? 0.5990 0.5704 0.5355 0.2671  0.0074  -0.0223 290  HOH   B O   
7021 O  O   . HOH   I .   ? 0.1582 0.1897 0.2948 0.0222  -0.0103 0.0115  291  HOH   B O   
7022 O  O   . HOH   I .   ? 0.3803 0.2172 0.3641 -0.1035 -0.2095 0.0942  292  HOH   B O   
7023 O  O   . HOH   I .   ? 0.4609 0.3795 0.2254 0.1248  -0.0716 0.0644  293  HOH   B O   
7024 O  O   . HOH   I .   ? 0.2454 0.2623 0.2782 0.0165  -0.0889 0.0136  294  HOH   B O   
7025 O  O   . HOH   I .   ? 0.4119 0.4896 0.2264 0.0208  0.0941  0.0682  295  HOH   B O   
7026 O  O   . HOH   I .   ? 0.1917 0.2778 0.6185 0.0381  -0.0462 -0.1376 296  HOH   B O   
7027 O  O   . HOH   I .   ? 0.5344 0.3351 0.2907 0.2296  0.0939  0.0835  297  HOH   B O   
7028 O  O   . HOH   I .   ? 0.4707 0.3816 0.2845 0.0159  -0.0227 -0.0714 298  HOH   B O   
7029 O  O   . HOH   I .   ? 0.4784 0.6289 0.2350 -0.0333 -0.1189 0.0481  299  HOH   B O   
7030 O  O   . HOH   I .   ? 0.1704 0.1545 0.2278 0.0080  -0.0022 0.0149  300  HOH   B O   
7031 O  O   . HOH   I .   ? 0.1521 0.1383 0.2907 0.0104  0.0043  0.0056  301  HOH   B O   
7032 O  O   . HOH   I .   ? 0.3073 0.2894 0.2982 -0.0232 0.0132  -0.1361 302  HOH   B O   
7033 O  O   . HOH   I .   ? 0.2072 0.1607 0.2527 -0.0236 -0.0206 -0.0091 303  HOH   B O   
7034 O  O   . HOH   I .   ? 0.3079 0.2623 0.5080 -0.0286 -0.0909 0.1238  304  HOH   B O   
7035 O  O   . HOH   I .   ? 0.4474 0.2790 0.2275 -0.1640 0.0522  -0.0294 305  HOH   B O   
7036 O  O   . HOH   I .   ? 0.3570 0.1733 0.3485 0.0657  0.1515  0.0475  306  HOH   B O   
7037 O  O   . HOH   I .   ? 0.3154 0.3651 0.3774 -0.1237 0.1146  -0.0488 307  HOH   B O   
7038 O  O   . HOH   I .   ? 0.3242 0.7239 0.3835 0.1947  0.0002  0.0948  308  HOH   B O   
7039 O  O   . HOH   I .   ? 0.1922 0.1486 0.3476 0.0284  -0.0911 0.0048  309  HOH   B O   
7040 O  O   . HOH   I .   ? 0.2882 0.2900 0.3624 -0.0603 0.1279  -0.1102 310  HOH   B O   
7041 O  O   . HOH   I .   ? 0.2185 0.1871 0.1815 -0.0147 0.0173  0.0237  311  HOH   B O   
7042 O  O   . HOH   I .   ? 0.4567 0.3983 0.2596 0.0431  -0.0338 -0.0493 312  HOH   B O   
7043 O  O   . HOH   I .   ? 0.2384 0.1477 0.2292 -0.0164 -0.0113 0.0299  313  HOH   B O   
7044 O  O   . HOH   I .   ? 0.2276 0.2948 0.4280 -0.0177 -0.0583 0.0136  314  HOH   B O   
7045 O  O   . HOH   I .   ? 0.4116 0.3824 0.4467 -0.0338 0.0429  0.1275  315  HOH   B O   
7046 O  O   . HOH   I .   ? 0.3533 0.2138 0.2500 0.1239  0.0890  0.0214  316  HOH   B O   
7047 O  O   . HOH   I .   ? 0.1469 0.1754 0.2899 -0.0225 -0.0044 0.0109  317  HOH   B O   
7048 O  O   . HOH   I .   ? 0.4183 0.4251 0.5689 0.0703  -0.0158 0.0066  318  HOH   B O   
7049 O  O   . HOH   I .   ? 0.2828 0.2885 0.4514 -0.0472 -0.1336 0.1103  319  HOH   B O   
7050 O  O   . HOH   I .   ? 0.1997 0.5111 0.4335 -0.0534 -0.0221 -0.0617 320  HOH   B O   
7051 O  O   . HOH   I .   ? 0.3672 0.4033 0.7490 -0.0219 -0.0985 0.1893  321  HOH   B O   
7052 O  O   . HOH   I .   ? 0.1462 0.1566 0.2837 -0.0138 -0.0072 -0.0039 322  HOH   B O   
7053 O  O   . HOH   I .   ? 0.1608 0.2761 0.2270 -0.0153 -0.0100 0.0719  323  HOH   B O   
7054 O  O   . HOH   I .   ? 0.2859 0.2253 0.2284 0.0196  -0.0318 0.0351  324  HOH   B O   
7055 O  O   . HOH   I .   ? 0.3895 0.3817 0.1930 0.0970  -0.0375 -0.0151 325  HOH   B O   
7056 O  O   . HOH   I .   ? 0.1741 0.1935 0.2914 0.0332  0.0379  0.0193  326  HOH   B O   
7057 O  O   . HOH   I .   ? 0.3975 0.3205 0.5483 0.0915  0.2026  0.1929  327  HOH   B O   
7058 O  O   . HOH   I .   ? 0.2501 0.1858 0.5469 -0.0014 0.0118  0.0290  328  HOH   B O   
7059 O  O   . HOH   I .   ? 0.5818 0.4759 0.6241 0.1642  -0.0667 0.1623  329  HOH   B O   
7060 O  O   . HOH   I .   ? 0.7532 0.1937 0.3002 0.0045  -0.0955 0.0062  330  HOH   B O   
7061 O  O   . HOH   I .   ? 0.1687 0.2605 0.3077 0.0306  -0.0075 -0.0737 331  HOH   B O   
7062 O  O   . HOH   I .   ? 0.5970 0.4847 0.5108 0.1306  0.1574  0.0384  332  HOH   B O   
7063 O  O   . HOH   I .   ? 0.2058 0.2419 0.5662 -0.0439 -0.0035 0.1438  333  HOH   B O   
7064 O  O   . HOH   I .   ? 0.5643 0.5273 0.5004 -0.1155 -0.0630 0.1284  334  HOH   B O   
7065 O  O   . HOH   I .   ? 0.5195 0.3379 0.4508 0.0283  0.0994  -0.1613 335  HOH   B O   
7066 O  O   . HOH   I .   ? 0.5521 0.3721 0.3775 0.0635  0.1416  0.1658  336  HOH   B O   
7067 O  O   . HOH   I .   ? 0.4229 0.2538 0.2950 0.0271  0.0423  0.0906  337  HOH   B O   
7068 O  O   . HOH   I .   ? 0.5642 0.3653 0.6714 -0.0427 -0.1005 -0.1333 338  HOH   B O   
7069 O  O   . HOH   I .   ? 0.1682 0.1368 0.2339 0.0062  -0.0215 0.0122  339  HOH   B O   
7070 O  O   . HOH   I .   ? 0.4808 0.5361 0.3545 0.0203  -0.1152 0.0312  340  HOH   B O   
7071 O  O   . HOH   I .   ? 0.4739 0.3226 0.3045 0.0869  -0.1373 -0.0976 341  HOH   B O   
7072 O  O   . HOH   I .   ? 0.3992 0.6578 0.3375 -0.0393 -0.0484 0.1843  342  HOH   B O   
7073 O  O   . HOH   I .   ? 0.2266 0.4654 0.5433 -0.0256 -0.0657 0.0352  343  HOH   B O   
7074 O  O   . HOH   I .   ? 0.6427 0.6023 0.3016 -0.0045 -0.0506 0.1225  344  HOH   B O   
7075 O  O   . HOH   I .   ? 0.2052 0.1765 0.2883 -0.0095 0.0533  -0.0055 345  HOH   B O   
7076 O  O   . HOH   I .   ? 0.3972 0.5256 0.5722 0.0103  -0.0984 0.0438  346  HOH   B O   
7077 O  O   . HOH   I .   ? 0.4601 0.5138 0.5008 -0.1214 0.0661  0.0890  347  HOH   B O   
7078 O  O   . HOH   I .   ? 0.3929 0.5367 0.4614 -0.1127 -0.0692 -0.0854 348  HOH   B O   
7079 O  O   . HOH   I .   ? 0.4635 0.6249 0.6490 0.0948  0.0427  -0.0254 349  HOH   B O   
7080 O  O   . HOH   I .   ? 0.2647 0.2271 0.4961 -0.0399 -0.0794 -0.0404 350  HOH   B O   
7081 O  O   . HOH   I .   ? 0.3657 0.2161 0.3344 -0.0906 0.0216  -0.0841 351  HOH   B O   
7082 O  O   . HOH   I .   ? 0.2335 0.6054 0.2955 0.1523  -0.0574 -0.1372 352  HOH   B O   
7083 O  O   . HOH   I .   ? 0.2128 0.3907 0.4864 0.0140  0.0537  0.0046  353  HOH   B O   
7084 O  O   . HOH   I .   ? 0.3159 0.4275 0.5048 -0.1347 0.0317  -0.0758 354  HOH   B O   
7085 O  O   . HOH   I .   ? 0.2739 0.1845 0.4220 0.0391  -0.1298 -0.0504 355  HOH   B O   
7086 O  O   . HOH   I .   ? 0.3294 0.2730 0.3761 -0.0836 0.0027  -0.0824 356  HOH   B O   
7087 O  O   . HOH   I .   ? 0.4879 0.2726 0.5760 -0.1158 0.1210  0.0760  357  HOH   B O   
7088 O  O   . HOH   I .   ? 0.5146 0.3466 0.4256 0.0243  0.1372  -0.0568 358  HOH   B O   
7089 O  O   . HOH   I .   ? 0.4780 0.5203 0.5220 0.1774  -0.1262 0.1741  359  HOH   B O   
7090 O  O   . HOH   I .   ? 0.5034 0.3476 0.5022 0.0032  -0.1510 -0.0694 360  HOH   B O   
7091 O  O   . HOH   I .   ? 0.4765 0.3594 0.5870 0.0347  0.1015  0.0740  361  HOH   B O   
7092 O  O   . HOH   I .   ? 0.5002 0.4527 0.4798 -0.0398 0.0041  0.0626  362  HOH   B O   
7093 O  O   . HOH   I .   ? 0.4932 0.6016 0.2646 0.2066  -0.0371 -0.0192 363  HOH   B O   
7094 O  O   . HOH   I .   ? 0.2229 0.3700 0.6542 -0.0846 -0.0458 -0.0924 364  HOH   B O   
7095 O  O   . HOH   I .   ? 0.5709 0.4248 0.4108 0.0944  -0.0031 0.0489  365  HOH   B O   
7096 O  O   . HOH   I .   ? 0.5574 0.5876 0.3510 0.1717  -0.1565 0.0666  366  HOH   B O   
7097 O  O   . HOH   I .   ? 0.4625 0.2931 0.5701 -0.1396 -0.0660 0.0323  367  HOH   B O   
7098 O  O   . HOH   I .   ? 0.6050 0.2225 0.2623 0.0065  -0.0186 0.0453  368  HOH   B O   
7099 O  O   . HOH   I .   ? 0.4821 0.5705 0.4655 -0.0693 -0.0522 -0.1112 369  HOH   B O   
7100 O  O   . HOH   I .   ? 0.3350 0.4019 0.4837 0.1049  -0.1389 -0.0470 370  HOH   B O   
7101 O  O   . HOH   I .   ? 0.3657 0.5423 0.4532 0.2233  0.0597  0.1220  371  HOH   B O   
7102 O  O   . HOH   I .   ? 0.5842 0.3475 0.2807 -0.0962 -0.0759 -0.0557 372  HOH   B O   
7103 O  O   . HOH   I .   ? 0.7495 0.7358 0.5110 0.2277  -0.1369 0.0857  373  HOH   B O   
7104 O  O   . HOH   I .   ? 0.3586 0.3373 0.3445 0.0792  -0.1065 -0.0801 374  HOH   B O   
7105 O  O   . HOH   I .   ? 0.4911 0.6970 0.5719 0.1783  0.0405  0.2631  375  HOH   B O   
7106 O  O   . HOH   I .   ? 0.4453 0.4361 0.4687 -0.0737 -0.0422 0.0219  376  HOH   B O   
7107 O  O   . HOH   I .   ? 0.2112 0.4473 0.3738 0.0516  -0.0658 -0.0688 377  HOH   B O   
7108 O  O   . HOH   I .   ? 0.3164 0.4705 0.2254 0.0278  0.0218  0.0175  378  HOH   B O   
7109 O  O   . HOH   I .   ? 0.3503 0.4814 0.5122 0.1030  0.0016  -0.0159 379  HOH   B O   
7110 O  O   . HOH   I .   ? 0.4942 0.7255 0.3697 -0.1387 0.0266  -0.1469 380  HOH   B O   
7111 O  O   . HOH   I .   ? 0.6973 0.3738 0.5683 -0.1065 -0.1119 -0.0520 381  HOH   B O   
7112 O  O   . HOH   I .   ? 0.5193 0.6035 0.5950 -0.0135 0.1672  0.1615  382  HOH   B O   
7113 O  O   . HOH   I .   ? 0.2958 0.2562 0.2950 0.0023  0.0171  0.0247  383  HOH   B O   
7114 O  O   . HOH   I .   ? 0.6712 0.3832 0.4012 0.0614  0.0582  -0.0990 384  HOH   B O   
7115 O  O   . HOH   I .   ? 0.4155 0.7286 0.5471 0.0636  0.1890  0.0844  385  HOH   B O   
7116 O  O   . HOH   I .   ? 0.5817 0.4159 0.5162 -0.0931 0.0117  -0.0108 386  HOH   B O   
7117 O  O   . HOH   I .   ? 0.4869 0.4852 0.4517 0.0148  -0.0355 -0.0700 387  HOH   B O   
7118 O  O   . HOH   I .   ? 0.4820 0.3645 0.3114 0.0169  0.0806  -0.0161 388  HOH   B O   
7119 O  O   . HOH   I .   ? 0.2362 0.4007 0.3858 -0.0577 -0.0950 -0.0476 389  HOH   B O   
7120 O  O   . HOH   I .   ? 0.7088 0.5593 0.4141 0.1890  0.0332  -0.0384 390  HOH   B O   
7121 O  O   . HOH   I .   ? 0.4667 0.4134 0.4548 0.0183  0.1021  0.0961  391  HOH   B O   
7122 O  O   . HOH   I .   ? 0.3571 0.2173 0.3119 0.0643  -0.0475 0.0057  392  HOH   B O   
7123 O  O   . HOH   I .   ? 0.4313 0.2124 0.5030 -0.0366 0.0635  0.0937  393  HOH   B O   
7124 O  O   . HOH   I .   ? 0.2409 0.3763 0.6703 -0.1167 -0.0448 -0.0212 394  HOH   B O   
7125 O  O   . HOH   I .   ? 0.4239 0.5754 0.3716 0.1300  -0.0315 -0.1109 395  HOH   B O   
7126 O  O   . HOH   I .   ? 0.3012 0.3662 0.4143 0.0204  0.0246  -0.0853 396  HOH   B O   
7127 O  O   . HOH   I .   ? 0.4384 0.4362 0.4560 0.0776  0.0871  0.0656  397  HOH   B O   
7128 O  O   . HOH   I .   ? 0.2057 0.2795 0.5751 -0.0601 -0.0872 0.0331  398  HOH   B O   
7129 O  O   . HOH   I .   ? 0.5462 0.3848 0.2848 -0.2221 -0.0318 0.0975  399  HOH   B O   
7130 O  O   . HOH   I .   ? 0.5603 0.5728 0.6087 0.0638  -0.1045 0.2906  400  HOH   B O   
7131 O  O   . HOH   I .   ? 0.5957 0.5484 0.3406 0.1808  0.0455  -0.0088 401  HOH   B O   
# 
