data_7HF7
# 
_entry.id   7HF7 
# 
_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   7HF7         pdb_00007hf7 10.2210/pdb7hf7/pdb 
WWPDB D_1001407397 ?            ?                   
# 
_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                        7HF7 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                     18178.766 2   
'3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'DIMETHYL SULFOXIDE'                                                           78.133    1   ? ? ? ? 
3 non-polymer syn '[(2R,5S)-5-methyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-2-yl]methanol' 246.308   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                                 35.453    1   ? ? ? ? 
5 water       nat water                                                                          18.015    427 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'DIMETHYL SULFOXIDE'                                                           DMS   
3 '[(2R,5S)-5-methyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-2-yl]methanol' A1BAR 
4 'CHLORIDE ION'                                                                 CL    
5 water                                                                          HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BAR non-polymer         . '[(2R,5S)-5-methyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-2-yl]methanol' ? 'C13 H18 N4 O'   
246.308 
ALA   'L-peptide linking' y ALANINE                                                                        ? 'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE                                                                       ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                     ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                ? 'C4 H7 N O4'     
133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                                 ? 'Cl -1'          
35.453  
CYS   'L-peptide linking' y CYSTEINE                                                                       ? 'C3 H7 N O2 S'   
121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                           ? 'C2 H6 O S'      
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                      ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                        ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                      ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                          ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                     ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                        ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                         ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                     ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                  ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                        ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                         ? 'C3 H7 N O3'     
105.093 
THR   'L-peptide linking' y THREONINE                                                                      ? 'C4 H9 N O3'     
119.119 
TYR   'L-peptide linking' y TYROSINE                                                                       ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                         ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 DMS   1   301  301  DMS   DMS A . 
D 3 A1BAR 1   302  201  A1BAR LA1 A . 
E 4 CL    1   303  1    CL    CL  A . 
F 5 HOH   1   1301 1301 HOH   HOH A . 
F 5 HOH   2   1302 196  HOH   HOH A . 
F 5 HOH   3   1303 292  HOH   HOH A . 
F 5 HOH   4   1304 109  HOH   HOH A . 
F 5 HOH   5   1305 209  HOH   HOH A . 
F 5 HOH   6   1306 461  HOH   HOH A . 
F 5 HOH   7   1307 625  HOH   HOH A . 
F 5 HOH   8   1308 199  HOH   HOH A . 
F 5 HOH   9   1309 153  HOH   HOH A . 
F 5 HOH   10  1310 20   HOH   HOH A . 
F 5 HOH   11  1311 76   HOH   HOH A . 
F 5 HOH   12  1312 493  HOH   HOH A . 
F 5 HOH   13  1313 964  HOH   HOH A . 
F 5 HOH   14  1314 1283 HOH   HOH A . 
F 5 HOH   15  1315 105  HOH   HOH A . 
F 5 HOH   16  1316 192  HOH   HOH A . 
F 5 HOH   17  1317 1295 HOH   HOH A . 
F 5 HOH   18  1318 1    HOH   HOH A . 
F 5 HOH   19  1319 247  HOH   HOH A . 
F 5 HOH   20  1320 57   HOH   HOH A . 
F 5 HOH   21  1321 124  HOH   HOH A . 
F 5 HOH   22  1322 93   HOH   HOH A . 
F 5 HOH   23  1323 393  HOH   HOH A . 
F 5 HOH   24  1324 136  HOH   HOH A . 
F 5 HOH   25  1325 151  HOH   HOH A . 
F 5 HOH   26  1326 155  HOH   HOH A . 
F 5 HOH   27  1327 661  HOH   HOH A . 
F 5 HOH   28  1328 13   HOH   HOH A . 
F 5 HOH   29  1329 281  HOH   HOH A . 
F 5 HOH   30  1330 1275 HOH   HOH A . 
F 5 HOH   31  1331 164  HOH   HOH A . 
F 5 HOH   32  1332 15   HOH   HOH A . 
F 5 HOH   33  1333 140  HOH   HOH A . 
F 5 HOH   34  1334 21   HOH   HOH A . 
F 5 HOH   35  1335 26   HOH   HOH A . 
F 5 HOH   36  1336 1094 HOH   HOH A . 
F 5 HOH   37  1337 225  HOH   HOH A . 
F 5 HOH   38  1338 630  HOH   HOH A . 
F 5 HOH   39  1339 36   HOH   HOH A . 
F 5 HOH   40  1340 236  HOH   HOH A . 
F 5 HOH   41  1341 86   HOH   HOH A . 
F 5 HOH   42  1342 11   HOH   HOH A . 
F 5 HOH   43  1343 337  HOH   HOH A . 
F 5 HOH   44  1344 56   HOH   HOH A . 
F 5 HOH   45  1345 42   HOH   HOH A . 
F 5 HOH   46  1346 162  HOH   HOH A . 
F 5 HOH   47  1347 241  HOH   HOH A . 
F 5 HOH   48  1348 165  HOH   HOH A . 
F 5 HOH   49  1349 469  HOH   HOH A . 
F 5 HOH   50  1350 1290 HOH   HOH A . 
F 5 HOH   51  1351 320  HOH   HOH A . 
F 5 HOH   52  1352 396  HOH   HOH A . 
F 5 HOH   53  1353 68   HOH   HOH A . 
F 5 HOH   54  1354 229  HOH   HOH A . 
F 5 HOH   55  1355 405  HOH   HOH A . 
F 5 HOH   56  1356 27   HOH   HOH A . 
F 5 HOH   57  1357 139  HOH   HOH A . 
F 5 HOH   58  1358 4    HOH   HOH A . 
F 5 HOH   59  1359 7    HOH   HOH A . 
F 5 HOH   60  1360 8    HOH   HOH A . 
F 5 HOH   61  1361 1310 HOH   HOH A . 
F 5 HOH   62  1362 169  HOH   HOH A . 
F 5 HOH   63  1363 662  HOH   HOH A . 
F 5 HOH   64  1364 2    HOH   HOH A . 
F 5 HOH   65  1365 66   HOH   HOH A . 
F 5 HOH   66  1366 354  HOH   HOH A . 
F 5 HOH   67  1367 102  HOH   HOH A . 
F 5 HOH   68  1368 351  HOH   HOH A . 
F 5 HOH   69  1369 92   HOH   HOH A . 
F 5 HOH   70  1370 18   HOH   HOH A . 
F 5 HOH   71  1371 1300 HOH   HOH A . 
F 5 HOH   72  1372 33   HOH   HOH A . 
F 5 HOH   73  1373 81   HOH   HOH A . 
F 5 HOH   74  1374 296  HOH   HOH A . 
F 5 HOH   75  1375 19   HOH   HOH A . 
F 5 HOH   76  1376 159  HOH   HOH A . 
F 5 HOH   77  1377 45   HOH   HOH A . 
F 5 HOH   78  1378 5    HOH   HOH A . 
F 5 HOH   79  1379 49   HOH   HOH A . 
F 5 HOH   80  1380 6    HOH   HOH A . 
F 5 HOH   81  1381 186  HOH   HOH A . 
F 5 HOH   82  1382 18   HOH   HOH A . 
F 5 HOH   83  1383 46   HOH   HOH A . 
F 5 HOH   84  1384 138  HOH   HOH A . 
F 5 HOH   85  1385 12   HOH   HOH A . 
F 5 HOH   86  1386 35   HOH   HOH A . 
F 5 HOH   87  1387 134  HOH   HOH A . 
F 5 HOH   88  1388 195  HOH   HOH A . 
F 5 HOH   89  1389 96   HOH   HOH A . 
F 5 HOH   90  1390 17   HOH   HOH A . 
F 5 HOH   91  1391 34   HOH   HOH A . 
F 5 HOH   92  1392 939  HOH   HOH A . 
F 5 HOH   93  1393 148  HOH   HOH A . 
F 5 HOH   94  1394 21   HOH   HOH A . 
F 5 HOH   95  1395 366  HOH   HOH A . 
F 5 HOH   96  1396 218  HOH   HOH A . 
F 5 HOH   97  1397 154  HOH   HOH A . 
F 5 HOH   98  1398 78   HOH   HOH A . 
F 5 HOH   99  1399 5    HOH   HOH A . 
F 5 HOH   100 1400 132  HOH   HOH A . 
F 5 HOH   101 1401 70   HOH   HOH A . 
F 5 HOH   102 1402 116  HOH   HOH A . 
F 5 HOH   103 1403 1315 HOH   HOH A . 
F 5 HOH   104 1404 67   HOH   HOH A . 
F 5 HOH   105 1405 1313 HOH   HOH A . 
F 5 HOH   106 1406 39   HOH   HOH A . 
F 5 HOH   107 1407 74   HOH   HOH A . 
F 5 HOH   108 1408 4    HOH   HOH A . 
F 5 HOH   109 1409 58   HOH   HOH A . 
F 5 HOH   110 1410 1308 HOH   HOH A . 
F 5 HOH   111 1411 8    HOH   HOH A . 
F 5 HOH   112 1412 83   HOH   HOH A . 
F 5 HOH   113 1413 85   HOH   HOH A . 
F 5 HOH   114 1414 6    HOH   HOH A . 
F 5 HOH   115 1415 3    HOH   HOH A . 
F 5 HOH   116 1416 409  HOH   HOH A . 
F 5 HOH   117 1417 25   HOH   HOH A . 
F 5 HOH   118 1418 303  HOH   HOH A . 
F 5 HOH   119 1419 123  HOH   HOH A . 
F 5 HOH   120 1420 121  HOH   HOH A . 
F 5 HOH   121 1421 53   HOH   HOH A . 
F 5 HOH   122 1422 24   HOH   HOH A . 
F 5 HOH   123 1423 51   HOH   HOH A . 
F 5 HOH   124 1424 1309 HOH   HOH A . 
F 5 HOH   125 1425 1068 HOH   HOH A . 
F 5 HOH   126 1426 115  HOH   HOH A . 
F 5 HOH   127 1427 95   HOH   HOH A . 
F 5 HOH   128 1428 156  HOH   HOH A . 
F 5 HOH   129 1429 278  HOH   HOH A . 
F 5 HOH   130 1430 1222 HOH   HOH A . 
F 5 HOH   131 1431 125  HOH   HOH A . 
F 5 HOH   132 1432 397  HOH   HOH A . 
F 5 HOH   133 1433 1289 HOH   HOH A . 
F 5 HOH   134 1434 381  HOH   HOH A . 
F 5 HOH   135 1435 1279 HOH   HOH A . 
F 5 HOH   136 1436 212  HOH   HOH A . 
F 5 HOH   137 1437 1296 HOH   HOH A . 
F 5 HOH   138 1438 1189 HOH   HOH A . 
F 5 HOH   139 1439 16   HOH   HOH A . 
F 5 HOH   140 1440 582  HOH   HOH A . 
F 5 HOH   141 1441 71   HOH   HOH A . 
F 5 HOH   142 1442 333  HOH   HOH A . 
F 5 HOH   143 1443 122  HOH   HOH A . 
F 5 HOH   144 1444 40   HOH   HOH A . 
F 5 HOH   145 1445 73   HOH   HOH A . 
F 5 HOH   146 1446 944  HOH   HOH A . 
F 5 HOH   147 1447 952  HOH   HOH A . 
F 5 HOH   148 1448 1119 HOH   HOH A . 
F 5 HOH   149 1449 7    HOH   HOH A . 
F 5 HOH   150 1450 80   HOH   HOH A . 
F 5 HOH   151 1451 188  HOH   HOH A . 
F 5 HOH   152 1452 94   HOH   HOH A . 
F 5 HOH   153 1453 97   HOH   HOH A . 
F 5 HOH   154 1454 1238 HOH   HOH A . 
F 5 HOH   155 1455 104  HOH   HOH A . 
F 5 HOH   156 1456 3    HOH   HOH A . 
F 5 HOH   157 1457 576  HOH   HOH A . 
F 5 HOH   158 1458 1286 HOH   HOH A . 
F 5 HOH   159 1459 79   HOH   HOH A . 
F 5 HOH   160 1460 330  HOH   HOH A . 
F 5 HOH   161 1461 14   HOH   HOH A . 
F 5 HOH   162 1462 1134 HOH   HOH A . 
F 5 HOH   163 1463 107  HOH   HOH A . 
F 5 HOH   164 1464 726  HOH   HOH A . 
F 5 HOH   165 1465 509  HOH   HOH A . 
F 5 HOH   166 1466 163  HOH   HOH A . 
F 5 HOH   167 1467 408  HOH   HOH A . 
F 5 HOH   168 1468 756  HOH   HOH A . 
F 5 HOH   169 1469 361  HOH   HOH A . 
F 5 HOH   170 1470 556  HOH   HOH A . 
F 5 HOH   171 1471 126  HOH   HOH A . 
F 5 HOH   172 1472 63   HOH   HOH A . 
F 5 HOH   173 1473 319  HOH   HOH A . 
F 5 HOH   174 1474 342  HOH   HOH A . 
F 5 HOH   175 1475 250  HOH   HOH A . 
F 5 HOH   176 1476 280  HOH   HOH A . 
F 5 HOH   177 1477 1276 HOH   HOH A . 
F 5 HOH   178 1478 801  HOH   HOH A . 
F 5 HOH   179 1479 17   HOH   HOH A . 
F 5 HOH   180 1480 19   HOH   HOH A . 
F 5 HOH   181 1481 1307 HOH   HOH A . 
F 5 HOH   182 1482 695  HOH   HOH A . 
F 5 HOH   183 1483 370  HOH   HOH A . 
F 5 HOH   184 1484 224  HOH   HOH A . 
F 5 HOH   185 1485 326  HOH   HOH A . 
F 5 HOH   186 1486 135  HOH   HOH A . 
F 5 HOH   187 1487 1287 HOH   HOH A . 
F 5 HOH   188 1488 202  HOH   HOH A . 
F 5 HOH   189 1489 1306 HOH   HOH A . 
F 5 HOH   190 1490 9    HOH   HOH A . 
F 5 HOH   191 1491 674  HOH   HOH A . 
F 5 HOH   192 1492 267  HOH   HOH A . 
F 5 HOH   193 1493 10   HOH   HOH A . 
F 5 HOH   194 1494 315  HOH   HOH A . 
F 5 HOH   195 1495 919  HOH   HOH A . 
F 5 HOH   196 1496 15   HOH   HOH A . 
F 5 HOH   197 1497 521  HOH   HOH A . 
F 5 HOH   198 1498 12   HOH   HOH A . 
F 5 HOH   199 1499 309  HOH   HOH A . 
F 5 HOH   200 1500 1314 HOH   HOH A . 
F 5 HOH   201 1501 318  HOH   HOH A . 
F 5 HOH   202 1502 1284 HOH   HOH A . 
F 5 HOH   203 1503 711  HOH   HOH A . 
F 5 HOH   204 1504 331  HOH   HOH A . 
F 5 HOH   205 1505 805  HOH   HOH A . 
F 5 HOH   206 1506 356  HOH   HOH A . 
F 5 HOH   207 1507 263  HOH   HOH A . 
F 5 HOH   208 1508 208  HOH   HOH A . 
F 5 HOH   209 1509 941  HOH   HOH A . 
F 5 HOH   210 1510 152  HOH   HOH A . 
F 5 HOH   211 1511 350  HOH   HOH A . 
F 5 HOH   212 1512 1299 HOH   HOH A . 
F 5 HOH   213 1513 1071 HOH   HOH A . 
F 5 HOH   214 1514 180  HOH   HOH A . 
F 5 HOH   215 1515 363  HOH   HOH A . 
F 5 HOH   216 1516 371  HOH   HOH A . 
F 5 HOH   217 1517 313  HOH   HOH A . 
F 5 HOH   218 1518 185  HOH   HOH A . 
F 5 HOH   219 1519 429  HOH   HOH A . 
F 5 HOH   220 1520 772  HOH   HOH A . 
F 5 HOH   221 1521 376  HOH   HOH A . 
F 5 HOH   222 1522 16   HOH   HOH A . 
F 5 HOH   223 1523 1074 HOH   HOH A . 
F 5 HOH   224 1524 346  HOH   HOH A . 
F 5 HOH   225 1525 1292 HOH   HOH A . 
F 5 HOH   226 1526 1078 HOH   HOH A . 
G 5 HOH   1   201  64   HOH   HOH B . 
G 5 HOH   2   202  549  HOH   HOH B . 
G 5 HOH   3   203  398  HOH   HOH B . 
G 5 HOH   4   204  900  HOH   HOH B . 
G 5 HOH   5   205  758  HOH   HOH B . 
G 5 HOH   6   206  358  HOH   HOH B . 
G 5 HOH   7   207  240  HOH   HOH B . 
G 5 HOH   8   208  232  HOH   HOH B . 
G 5 HOH   9   209  1249 HOH   HOH B . 
G 5 HOH   10  210  364  HOH   HOH B . 
G 5 HOH   11  211  743  HOH   HOH B . 
G 5 HOH   12  212  120  HOH   HOH B . 
G 5 HOH   13  213  531  HOH   HOH B . 
G 5 HOH   14  214  343  HOH   HOH B . 
G 5 HOH   15  215  264  HOH   HOH B . 
G 5 HOH   16  216  444  HOH   HOH B . 
G 5 HOH   17  217  654  HOH   HOH B . 
G 5 HOH   18  218  50   HOH   HOH B . 
G 5 HOH   19  219  276  HOH   HOH B . 
G 5 HOH   20  220  353  HOH   HOH B . 
G 5 HOH   21  221  452  HOH   HOH B . 
G 5 HOH   22  222  82   HOH   HOH B . 
G 5 HOH   23  223  1140 HOH   HOH B . 
G 5 HOH   24  224  128  HOH   HOH B . 
G 5 HOH   25  225  131  HOH   HOH B . 
G 5 HOH   26  226  75   HOH   HOH B . 
G 5 HOH   27  227  332  HOH   HOH B . 
G 5 HOH   28  228  54   HOH   HOH B . 
G 5 HOH   29  229  127  HOH   HOH B . 
G 5 HOH   30  230  172  HOH   HOH B . 
G 5 HOH   31  231  272  HOH   HOH B . 
G 5 HOH   32  232  282  HOH   HOH B . 
G 5 HOH   33  233  110  HOH   HOH B . 
G 5 HOH   34  234  69   HOH   HOH B . 
G 5 HOH   35  235  166  HOH   HOH B . 
G 5 HOH   36  236  60   HOH   HOH B . 
G 5 HOH   37  237  325  HOH   HOH B . 
G 5 HOH   38  238  1278 HOH   HOH B . 
G 5 HOH   39  239  1    HOH   HOH B . 
G 5 HOH   40  240  723  HOH   HOH B . 
G 5 HOH   41  241  300  HOH   HOH B . 
G 5 HOH   42  242  181  HOH   HOH B . 
G 5 HOH   43  243  205  HOH   HOH B . 
G 5 HOH   44  244  9    HOH   HOH B . 
G 5 HOH   45  245  41   HOH   HOH B . 
G 5 HOH   46  246  14   HOH   HOH B . 
G 5 HOH   47  247  52   HOH   HOH B . 
G 5 HOH   48  248  129  HOH   HOH B . 
G 5 HOH   49  249  72   HOH   HOH B . 
G 5 HOH   50  250  347  HOH   HOH B . 
G 5 HOH   51  251  30   HOH   HOH B . 
G 5 HOH   52  252  143  HOH   HOH B . 
G 5 HOH   53  253  133  HOH   HOH B . 
G 5 HOH   54  254  31   HOH   HOH B . 
G 5 HOH   55  255  150  HOH   HOH B . 
G 5 HOH   56  256  47   HOH   HOH B . 
G 5 HOH   57  257  144  HOH   HOH B . 
G 5 HOH   58  258  62   HOH   HOH B . 
G 5 HOH   59  259  10   HOH   HOH B . 
G 5 HOH   60  260  231  HOH   HOH B . 
G 5 HOH   61  261  243  HOH   HOH B . 
G 5 HOH   62  262  391  HOH   HOH B . 
G 5 HOH   63  263  84   HOH   HOH B . 
G 5 HOH   64  264  61   HOH   HOH B . 
G 5 HOH   65  265  271  HOH   HOH B . 
G 5 HOH   66  266  59   HOH   HOH B . 
G 5 HOH   67  267  117  HOH   HOH B . 
G 5 HOH   68  268  1312 HOH   HOH B . 
G 5 HOH   69  269  114  HOH   HOH B . 
G 5 HOH   70  270  20   HOH   HOH B . 
G 5 HOH   71  271  103  HOH   HOH B . 
G 5 HOH   72  272  1277 HOH   HOH B . 
G 5 HOH   73  273  175  HOH   HOH B . 
G 5 HOH   74  274  77   HOH   HOH B . 
G 5 HOH   75  275  11   HOH   HOH B . 
G 5 HOH   76  276  242  HOH   HOH B . 
G 5 HOH   77  277  221  HOH   HOH B . 
G 5 HOH   78  278  416  HOH   HOH B . 
G 5 HOH   79  279  302  HOH   HOH B . 
G 5 HOH   80  280  1305 HOH   HOH B . 
G 5 HOH   81  281  387  HOH   HOH B . 
G 5 HOH   82  282  43   HOH   HOH B . 
G 5 HOH   83  283  88   HOH   HOH B . 
G 5 HOH   84  284  1066 HOH   HOH B . 
G 5 HOH   85  285  22   HOH   HOH B . 
G 5 HOH   86  286  287  HOH   HOH B . 
G 5 HOH   87  287  216  HOH   HOH B . 
G 5 HOH   88  288  89   HOH   HOH B . 
G 5 HOH   89  289  13   HOH   HOH B . 
G 5 HOH   90  290  147  HOH   HOH B . 
G 5 HOH   91  291  235  HOH   HOH B . 
G 5 HOH   92  292  106  HOH   HOH B . 
G 5 HOH   93  293  252  HOH   HOH B . 
G 5 HOH   94  294  635  HOH   HOH B . 
G 5 HOH   95  295  99   HOH   HOH B . 
G 5 HOH   96  296  1106 HOH   HOH B . 
G 5 HOH   97  297  137  HOH   HOH B . 
G 5 HOH   98  298  341  HOH   HOH B . 
G 5 HOH   99  299  112  HOH   HOH B . 
G 5 HOH   100 300  38   HOH   HOH B . 
G 5 HOH   101 301  311  HOH   HOH B . 
G 5 HOH   102 302  101  HOH   HOH B . 
G 5 HOH   103 303  316  HOH   HOH B . 
G 5 HOH   104 304  141  HOH   HOH B . 
G 5 HOH   105 305  704  HOH   HOH B . 
G 5 HOH   106 306  297  HOH   HOH B . 
G 5 HOH   107 307  1285 HOH   HOH B . 
G 5 HOH   108 308  160  HOH   HOH B . 
G 5 HOH   109 309  32   HOH   HOH B . 
G 5 HOH   110 310  220  HOH   HOH B . 
G 5 HOH   111 311  142  HOH   HOH B . 
G 5 HOH   112 312  299  HOH   HOH B . 
G 5 HOH   113 313  170  HOH   HOH B . 
G 5 HOH   114 314  215  HOH   HOH B . 
G 5 HOH   115 315  91   HOH   HOH B . 
G 5 HOH   116 316  118  HOH   HOH B . 
G 5 HOH   117 317  445  HOH   HOH B . 
G 5 HOH   118 318  37   HOH   HOH B . 
G 5 HOH   119 319  48   HOH   HOH B . 
G 5 HOH   120 320  177  HOH   HOH B . 
G 5 HOH   121 321  23   HOH   HOH B . 
G 5 HOH   122 322  1126 HOH   HOH B . 
G 5 HOH   123 323  44   HOH   HOH B . 
G 5 HOH   124 324  28   HOH   HOH B . 
G 5 HOH   125 325  1291 HOH   HOH B . 
G 5 HOH   126 326  197  HOH   HOH B . 
G 5 HOH   127 327  100  HOH   HOH B . 
G 5 HOH   128 328  161  HOH   HOH B . 
G 5 HOH   129 329  29   HOH   HOH B . 
G 5 HOH   130 330  55   HOH   HOH B . 
G 5 HOH   131 331  182  HOH   HOH B . 
G 5 HOH   132 332  1274 HOH   HOH B . 
G 5 HOH   133 333  1294 HOH   HOH B . 
G 5 HOH   134 334  717  HOH   HOH B . 
G 5 HOH   135 335  98   HOH   HOH B . 
G 5 HOH   136 336  234  HOH   HOH B . 
G 5 HOH   137 337  334  HOH   HOH B . 
G 5 HOH   138 338  207  HOH   HOH B . 
G 5 HOH   139 339  65   HOH   HOH B . 
G 5 HOH   140 340  339  HOH   HOH B . 
G 5 HOH   141 341  619  HOH   HOH B . 
G 5 HOH   142 342  362  HOH   HOH B . 
G 5 HOH   143 343  1293 HOH   HOH B . 
G 5 HOH   144 344  960  HOH   HOH B . 
G 5 HOH   145 345  463  HOH   HOH B . 
G 5 HOH   146 346  90   HOH   HOH B . 
G 5 HOH   147 347  178  HOH   HOH B . 
G 5 HOH   148 348  1304 HOH   HOH B . 
G 5 HOH   149 349  1280 HOH   HOH B . 
G 5 HOH   150 350  623  HOH   HOH B . 
G 5 HOH   151 351  191  HOH   HOH B . 
G 5 HOH   152 352  335  HOH   HOH B . 
G 5 HOH   153 353  304  HOH   HOH B . 
G 5 HOH   154 354  1046 HOH   HOH B . 
G 5 HOH   155 355  203  HOH   HOH B . 
G 5 HOH   156 356  87   HOH   HOH B . 
G 5 HOH   157 357  290  HOH   HOH B . 
G 5 HOH   158 358  541  HOH   HOH B . 
G 5 HOH   159 359  1077 HOH   HOH B . 
G 5 HOH   160 360  479  HOH   HOH B . 
G 5 HOH   161 361  389  HOH   HOH B . 
G 5 HOH   162 362  718  HOH   HOH B . 
G 5 HOH   163 363  1072 HOH   HOH B . 
G 5 HOH   164 364  283  HOH   HOH B . 
G 5 HOH   165 365  898  HOH   HOH B . 
G 5 HOH   166 366  1316 HOH   HOH B . 
G 5 HOH   167 367  615  HOH   HOH B . 
G 5 HOH   168 368  373  HOH   HOH B . 
G 5 HOH   169 369  667  HOH   HOH B . 
G 5 HOH   170 370  291  HOH   HOH B . 
G 5 HOH   171 371  340  HOH   HOH B . 
G 5 HOH   172 372  1303 HOH   HOH B . 
G 5 HOH   173 373  190  HOH   HOH B . 
G 5 HOH   174 374  310  HOH   HOH B . 
G 5 HOH   175 375  1173 HOH   HOH B . 
G 5 HOH   176 376  431  HOH   HOH B . 
G 5 HOH   177 377  149  HOH   HOH B . 
G 5 HOH   178 378  1163 HOH   HOH B . 
G 5 HOH   179 379  183  HOH   HOH B . 
G 5 HOH   180 380  1000 HOH   HOH B . 
G 5 HOH   181 381  418  HOH   HOH B . 
G 5 HOH   182 382  1311 HOH   HOH B . 
G 5 HOH   183 383  176  HOH   HOH B . 
G 5 HOH   184 384  424  HOH   HOH B . 
G 5 HOH   185 385  470  HOH   HOH B . 
G 5 HOH   186 386  248  HOH   HOH B . 
G 5 HOH   187 387  981  HOH   HOH B . 
G 5 HOH   188 388  491  HOH   HOH B . 
G 5 HOH   189 389  265  HOH   HOH B . 
G 5 HOH   190 390  184  HOH   HOH B . 
G 5 HOH   191 391  360  HOH   HOH B . 
G 5 HOH   192 392  1298 HOH   HOH B . 
G 5 HOH   193 393  410  HOH   HOH B . 
G 5 HOH   194 394  355  HOH   HOH B . 
G 5 HOH   195 395  274  HOH   HOH B . 
G 5 HOH   196 396  314  HOH   HOH B . 
G 5 HOH   197 397  566  HOH   HOH B . 
G 5 HOH   198 398  157  HOH   HOH B . 
G 5 HOH   199 399  792  HOH   HOH B . 
G 5 HOH   200 400  321  HOH   HOH B . 
G 5 HOH   201 401  558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HF7 
_cell.length_a           88.718 
_cell.length_b           88.718 
_cell.length_c           39.537 
_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                         7HF7 
_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          7HF7 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.63 
_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                     7HF7 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.360 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   156310 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.900 
_reflns.pdbx_Rmerge_I_obs            0.040 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        18.700 
_reflns.B_iso_Wilson_estimate        11.350 
_reflns.pdbx_redundancy              6.500 
_reflns.pdbx_Rrim_I_all              0.043 
_reflns.pdbx_Rpim_I_all              0.017 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1016840 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.020 1.040  ? 43560 7573 ? 0.762 ? ? ? 5.800 ? 1.700  ? ? ? ? ? ? 98.000 0.839 0.343 0.839 
1 2 5.590 44.360 ? 7131  1038 ? 0.027 ? ? ? 6.900 ? 60.200 ? ? ? ? ? ? 99.800 0.029 0.011 0.999 
# 
_refine.entry_id                                 7HF7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             44.3600 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.8300 
_refine.ls_number_reflns_obs                     156246 
_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                          0.1383 
_refine.ls_R_factor_R_work                       0.1377 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1506 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7538 
_refine.ls_number_reflns_R_work                  148708 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               17.0748 
_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                            0.1000 
_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                                58.740 
_refine.B_iso_min                                7.640 
_refine.pdbx_overall_phase_error                 14.4400 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0200 
_refine_hist.d_res_low                        44.3600 
_refine_hist.pdbx_number_atoms_ligand         47 
_refine_hist.number_atoms_solvent             427 
_refine_hist.number_atoms_total               3016 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           16.95 
_refine_hist.pdbx_B_iso_mean_solvent          28.77 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0200 1.0300  30 97.0000  4866 . 0.3190 0.3266 . 200 0.0000 5066 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 4944 . 0.2456 0.2611 . 280 0.0000 5224 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 4856 . 0.2101 0.2154 . 281 0.0000 5137 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 4918 . 0.1942 0.1929 . 277 0.0000 5195 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 4923 . 0.1738 0.1935 . 231 0.0000 5154 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 4976 . 0.1604 0.1931 . 243 0.0000 5219 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 100.0000 4861 . 0.1455 0.1719 . 265 0.0000 5126 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5015 . 0.1360 0.1511 . 214 0.0000 5229 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 4929 . 0.1290 0.1525 . 239 0.0000 5168 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 4947 . 0.1197 0.1491 . 262 0.0000 5209 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 4903 . 0.1231 0.1522 . 250 0.0000 5153 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 4921 . 0.1168 0.1440 . 270 0.0000 5191 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5034 . 0.1144 0.1383 . 217 0.0000 5251 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 4887 . 0.1186 0.1276 . 251 0.0000 5138 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 4962 . 0.1196 0.1383 . 245 0.0000 5207 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 4933 . 0.1220 0.1353 . 270 0.0000 5203 . 'X-RAY DIFFRACTION' 
1.3200 1.3500  30 100.0000 4953 . 0.1280 0.1492 . 252 0.0000 5205 . 'X-RAY DIFFRACTION' 
1.3500 1.3800  30 100.0000 4936 . 0.1251 0.1540 . 257 0.0000 5193 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 4978 . 0.1236 0.1430 . 244 0.0000 5222 . 'X-RAY DIFFRACTION' 
1.4300 1.4700  30 100.0000 4963 . 0.1195 0.1255 . 244 0.0000 5207 . 'X-RAY DIFFRACTION' 
1.4700 1.5200  30 100.0000 4975 . 0.1153 0.1320 . 239 0.0000 5214 . 'X-RAY DIFFRACTION' 
1.5200 1.5800  30 100.0000 4962 . 0.1162 0.1238 . 261 0.0000 5223 . 'X-RAY DIFFRACTION' 
1.5800 1.6600  30 100.0000 4937 . 0.1183 0.1308 . 262 0.0000 5199 . 'X-RAY DIFFRACTION' 
1.6600 1.7400  30 100.0000 5014 . 0.1267 0.1352 . 204 0.0000 5218 . 'X-RAY DIFFRACTION' 
1.7400 1.8500  30 100.0000 4956 . 0.1293 0.1296 . 294 0.0000 5250 . 'X-RAY DIFFRACTION' 
1.8500 2.0000  30 100.0000 4990 . 0.1314 0.1343 . 244 0.0000 5234 . 'X-RAY DIFFRACTION' 
2.0000 2.2000  30 100.0000 4961 . 0.1346 0.1359 . 286 0.0000 5247 . 'X-RAY DIFFRACTION' 
2.2000 2.5200  30 100.0000 5003 . 0.1350 0.1406 . 256 0.0000 5259 . 'X-RAY DIFFRACTION' 
2.5200 3.1700  30 100.0000 5030 . 0.1477 0.1615 . 249 0.0000 5279 . 'X-RAY DIFFRACTION' 
3.1700 44.3600 30 100.0000 5175 . 0.1488 0.1727 . 251 0.0000 5426 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HF7 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0004063' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HF7 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HF7 A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HF7 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 7HF7 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HF7 MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HF7 SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HF7 MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F 
2 1 B,G       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O LEU A 93  ? O LEU A 93  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HF7 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.60 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 4   ? B -125.75 -144.14 
2 1 HIS A 86  ? ? 55.88   -133.39 
3 1 SER A 128 ? B 70.33   -7.06   
4 1 HIS B 86  ? ? 56.94   -127.74 
# 
_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 1524 ? 5.82 . 
2 1 O ? A HOH 1525 ? 6.02 . 
3 1 O ? A HOH 1526 ? 7.54 . 
4 1 O ? B HOH 401  ? 6.34 . 
# 
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 
A1BAR N2   N  Y N 1   
A1BAR C3   C  N N 2   
A1BAR C6   C  N N 3   
A1BAR C9   C  Y N 4   
A1BAR C12  C  Y N 5   
A1BAR C1   C  N N 6   
A1BAR C10  C  Y N 7   
A1BAR C11  C  Y N 8   
A1BAR C13  C  N N 9   
A1BAR C2   C  N S 10  
A1BAR C4   C  N N 11  
A1BAR C5   C  N R 12  
A1BAR C7   C  Y N 13  
A1BAR C8   C  Y N 14  
A1BAR N1   N  N N 15  
A1BAR N3   N  Y N 16  
A1BAR N4   N  Y N 17  
A1BAR O1   O  N N 18  
A1BAR H7   H  N N 19  
A1BAR H6   H  N N 20  
A1BAR H11  H  N N 21  
A1BAR H10  H  N N 22  
A1BAR H15  H  N N 23  
A1BAR H4   H  N N 24  
A1BAR H5   H  N N 25  
A1BAR H3   H  N N 26  
A1BAR H14  H  N N 27  
A1BAR H17  H  N N 28  
A1BAR H18  H  N N 29  
A1BAR H1   H  N N 30  
A1BAR H9   H  N N 31  
A1BAR H8   H  N N 32  
A1BAR H2   H  N N 33  
A1BAR H13  H  N N 34  
A1BAR H16  H  N N 35  
A1BAR H12  H  N N 36  
ALA   N    N  N N 37  
ALA   CA   C  N S 38  
ALA   C    C  N N 39  
ALA   O    O  N N 40  
ALA   CB   C  N N 41  
ALA   OXT  O  N N 42  
ALA   H    H  N N 43  
ALA   H2   H  N N 44  
ALA   HA   H  N N 45  
ALA   HB1  H  N N 46  
ALA   HB2  H  N N 47  
ALA   HB3  H  N N 48  
ALA   HXT  H  N N 49  
ARG   N    N  N N 50  
ARG   CA   C  N S 51  
ARG   C    C  N N 52  
ARG   O    O  N N 53  
ARG   CB   C  N N 54  
ARG   CG   C  N N 55  
ARG   CD   C  N N 56  
ARG   NE   N  N N 57  
ARG   CZ   C  N N 58  
ARG   NH1  N  N N 59  
ARG   NH2  N  N N 60  
ARG   OXT  O  N N 61  
ARG   H    H  N N 62  
ARG   H2   H  N N 63  
ARG   HA   H  N N 64  
ARG   HB2  H  N N 65  
ARG   HB3  H  N N 66  
ARG   HG2  H  N N 67  
ARG   HG3  H  N N 68  
ARG   HD2  H  N N 69  
ARG   HD3  H  N N 70  
ARG   HE   H  N N 71  
ARG   HH11 H  N N 72  
ARG   HH12 H  N N 73  
ARG   HH21 H  N N 74  
ARG   HH22 H  N N 75  
ARG   HXT  H  N N 76  
ASN   N    N  N N 77  
ASN   CA   C  N S 78  
ASN   C    C  N N 79  
ASN   O    O  N N 80  
ASN   CB   C  N N 81  
ASN   CG   C  N N 82  
ASN   OD1  O  N N 83  
ASN   ND2  N  N N 84  
ASN   OXT  O  N N 85  
ASN   H    H  N N 86  
ASN   H2   H  N N 87  
ASN   HA   H  N N 88  
ASN   HB2  H  N N 89  
ASN   HB3  H  N N 90  
ASN   HD21 H  N N 91  
ASN   HD22 H  N N 92  
ASN   HXT  H  N N 93  
ASP   N    N  N N 94  
ASP   CA   C  N S 95  
ASP   C    C  N N 96  
ASP   O    O  N N 97  
ASP   CB   C  N N 98  
ASP   CG   C  N N 99  
ASP   OD1  O  N N 100 
ASP   OD2  O  N N 101 
ASP   OXT  O  N N 102 
ASP   H    H  N N 103 
ASP   H2   H  N N 104 
ASP   HA   H  N N 105 
ASP   HB2  H  N N 106 
ASP   HB3  H  N N 107 
ASP   HD2  H  N N 108 
ASP   HXT  H  N N 109 
CL    CL   CL N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
DMS   S    S  N N 125 
DMS   O    O  N N 126 
DMS   C1   C  N N 127 
DMS   C2   C  N N 128 
DMS   H11  H  N N 129 
DMS   H12  H  N N 130 
DMS   H13  H  N N 131 
DMS   H21  H  N N 132 
DMS   H22  H  N N 133 
DMS   H23  H  N N 134 
GLN   N    N  N N 135 
GLN   CA   C  N S 136 
GLN   C    C  N N 137 
GLN   O    O  N N 138 
GLN   CB   C  N N 139 
GLN   CG   C  N N 140 
GLN   CD   C  N N 141 
GLN   OE1  O  N N 142 
GLN   NE2  N  N N 143 
GLN   OXT  O  N N 144 
GLN   H    H  N N 145 
GLN   H2   H  N N 146 
GLN   HA   H  N N 147 
GLN   HB2  H  N N 148 
GLN   HB3  H  N N 149 
GLN   HG2  H  N N 150 
GLN   HG3  H  N N 151 
GLN   HE21 H  N N 152 
GLN   HE22 H  N N 153 
GLN   HXT  H  N N 154 
GLU   N    N  N N 155 
GLU   CA   C  N S 156 
GLU   C    C  N N 157 
GLU   O    O  N N 158 
GLU   CB   C  N N 159 
GLU   CG   C  N N 160 
GLU   CD   C  N N 161 
GLU   OE1  O  N N 162 
GLU   OE2  O  N N 163 
GLU   OXT  O  N N 164 
GLU   H    H  N N 165 
GLU   H2   H  N N 166 
GLU   HA   H  N N 167 
GLU   HB2  H  N N 168 
GLU   HB3  H  N N 169 
GLU   HG2  H  N N 170 
GLU   HG3  H  N N 171 
GLU   HE2  H  N N 172 
GLU   HXT  H  N N 173 
GLY   N    N  N N 174 
GLY   CA   C  N N 175 
GLY   C    C  N N 176 
GLY   O    O  N N 177 
GLY   OXT  O  N N 178 
GLY   H    H  N N 179 
GLY   H2   H  N N 180 
GLY   HA2  H  N N 181 
GLY   HA3  H  N N 182 
GLY   HXT  H  N N 183 
HIS   N    N  N N 184 
HIS   CA   C  N S 185 
HIS   C    C  N N 186 
HIS   O    O  N N 187 
HIS   CB   C  N N 188 
HIS   CG   C  Y N 189 
HIS   ND1  N  Y N 190 
HIS   CD2  C  Y N 191 
HIS   CE1  C  Y N 192 
HIS   NE2  N  Y N 193 
HIS   OXT  O  N N 194 
HIS   H    H  N N 195 
HIS   H2   H  N N 196 
HIS   HA   H  N N 197 
HIS   HB2  H  N N 198 
HIS   HB3  H  N N 199 
HIS   HD1  H  N N 200 
HIS   HD2  H  N N 201 
HIS   HE1  H  N N 202 
HIS   HE2  H  N N 203 
HIS   HXT  H  N N 204 
HOH   O    O  N N 205 
HOH   H1   H  N N 206 
HOH   H2   H  N N 207 
ILE   N    N  N N 208 
ILE   CA   C  N S 209 
ILE   C    C  N N 210 
ILE   O    O  N N 211 
ILE   CB   C  N S 212 
ILE   CG1  C  N N 213 
ILE   CG2  C  N N 214 
ILE   CD1  C  N N 215 
ILE   OXT  O  N N 216 
ILE   H    H  N N 217 
ILE   H2   H  N N 218 
ILE   HA   H  N N 219 
ILE   HB   H  N N 220 
ILE   HG12 H  N N 221 
ILE   HG13 H  N N 222 
ILE   HG21 H  N N 223 
ILE   HG22 H  N N 224 
ILE   HG23 H  N N 225 
ILE   HD11 H  N N 226 
ILE   HD12 H  N N 227 
ILE   HD13 H  N N 228 
ILE   HXT  H  N N 229 
LEU   N    N  N N 230 
LEU   CA   C  N S 231 
LEU   C    C  N N 232 
LEU   O    O  N N 233 
LEU   CB   C  N N 234 
LEU   CG   C  N N 235 
LEU   CD1  C  N N 236 
LEU   CD2  C  N N 237 
LEU   OXT  O  N N 238 
LEU   H    H  N N 239 
LEU   H2   H  N N 240 
LEU   HA   H  N N 241 
LEU   HB2  H  N N 242 
LEU   HB3  H  N N 243 
LEU   HG   H  N N 244 
LEU   HD11 H  N N 245 
LEU   HD12 H  N N 246 
LEU   HD13 H  N N 247 
LEU   HD21 H  N N 248 
LEU   HD22 H  N N 249 
LEU   HD23 H  N N 250 
LEU   HXT  H  N N 251 
LYS   N    N  N N 252 
LYS   CA   C  N S 253 
LYS   C    C  N N 254 
LYS   O    O  N N 255 
LYS   CB   C  N N 256 
LYS   CG   C  N N 257 
LYS   CD   C  N N 258 
LYS   CE   C  N N 259 
LYS   NZ   N  N N 260 
LYS   OXT  O  N N 261 
LYS   H    H  N N 262 
LYS   H2   H  N N 263 
LYS   HA   H  N N 264 
LYS   HB2  H  N N 265 
LYS   HB3  H  N N 266 
LYS   HG2  H  N N 267 
LYS   HG3  H  N N 268 
LYS   HD2  H  N N 269 
LYS   HD3  H  N N 270 
LYS   HE2  H  N N 271 
LYS   HE3  H  N N 272 
LYS   HZ1  H  N N 273 
LYS   HZ2  H  N N 274 
LYS   HZ3  H  N N 275 
LYS   HXT  H  N N 276 
MET   N    N  N N 277 
MET   CA   C  N S 278 
MET   C    C  N N 279 
MET   O    O  N N 280 
MET   CB   C  N N 281 
MET   CG   C  N N 282 
MET   SD   S  N N 283 
MET   CE   C  N N 284 
MET   OXT  O  N N 285 
MET   H    H  N N 286 
MET   H2   H  N N 287 
MET   HA   H  N N 288 
MET   HB2  H  N N 289 
MET   HB3  H  N N 290 
MET   HG2  H  N N 291 
MET   HG3  H  N N 292 
MET   HE1  H  N N 293 
MET   HE2  H  N N 294 
MET   HE3  H  N N 295 
MET   HXT  H  N N 296 
PHE   N    N  N N 297 
PHE   CA   C  N S 298 
PHE   C    C  N N 299 
PHE   O    O  N N 300 
PHE   CB   C  N N 301 
PHE   CG   C  Y N 302 
PHE   CD1  C  Y N 303 
PHE   CD2  C  Y N 304 
PHE   CE1  C  Y N 305 
PHE   CE2  C  Y N 306 
PHE   CZ   C  Y N 307 
PHE   OXT  O  N N 308 
PHE   H    H  N N 309 
PHE   H2   H  N N 310 
PHE   HA   H  N N 311 
PHE   HB2  H  N N 312 
PHE   HB3  H  N N 313 
PHE   HD1  H  N N 314 
PHE   HD2  H  N N 315 
PHE   HE1  H  N N 316 
PHE   HE2  H  N N 317 
PHE   HZ   H  N N 318 
PHE   HXT  H  N N 319 
PRO   N    N  N N 320 
PRO   CA   C  N S 321 
PRO   C    C  N N 322 
PRO   O    O  N N 323 
PRO   CB   C  N N 324 
PRO   CG   C  N N 325 
PRO   CD   C  N N 326 
PRO   OXT  O  N N 327 
PRO   H    H  N N 328 
PRO   HA   H  N N 329 
PRO   HB2  H  N N 330 
PRO   HB3  H  N N 331 
PRO   HG2  H  N N 332 
PRO   HG3  H  N N 333 
PRO   HD2  H  N N 334 
PRO   HD3  H  N N 335 
PRO   HXT  H  N N 336 
SER   N    N  N N 337 
SER   CA   C  N S 338 
SER   C    C  N N 339 
SER   O    O  N N 340 
SER   CB   C  N N 341 
SER   OG   O  N N 342 
SER   OXT  O  N N 343 
SER   H    H  N N 344 
SER   H2   H  N N 345 
SER   HA   H  N N 346 
SER   HB2  H  N N 347 
SER   HB3  H  N N 348 
SER   HG   H  N N 349 
SER   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TYR   N    N  N N 368 
TYR   CA   C  N S 369 
TYR   C    C  N N 370 
TYR   O    O  N N 371 
TYR   CB   C  N N 372 
TYR   CG   C  Y N 373 
TYR   CD1  C  Y N 374 
TYR   CD2  C  Y N 375 
TYR   CE1  C  Y N 376 
TYR   CE2  C  Y N 377 
TYR   CZ   C  Y N 378 
TYR   OH   O  N N 379 
TYR   OXT  O  N N 380 
TYR   H    H  N N 381 
TYR   H2   H  N N 382 
TYR   HA   H  N N 383 
TYR   HB2  H  N N 384 
TYR   HB3  H  N N 385 
TYR   HD1  H  N N 386 
TYR   HD2  H  N N 387 
TYR   HE1  H  N N 388 
TYR   HE2  H  N N 389 
TYR   HH   H  N N 390 
TYR   HXT  H  N N 391 
VAL   N    N  N N 392 
VAL   CA   C  N S 393 
VAL   C    C  N N 394 
VAL   O    O  N N 395 
VAL   CB   C  N N 396 
VAL   CG1  C  N N 397 
VAL   CG2  C  N N 398 
VAL   OXT  O  N N 399 
VAL   H    H  N N 400 
VAL   H2   H  N N 401 
VAL   HA   H  N N 402 
VAL   HB   H  N N 403 
VAL   HG11 H  N N 404 
VAL   HG12 H  N N 405 
VAL   HG13 H  N N 406 
VAL   HG21 H  N N 407 
VAL   HG22 H  N N 408 
VAL   HG23 H  N N 409 
VAL   HXT  H  N N 410 
# 
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 
A1BAR C3  C2   sing N N 1   
A1BAR C3  C4   sing N N 2   
A1BAR C2  C1   sing N N 3   
A1BAR C2  C13  sing N N 4   
A1BAR C4  C5   sing N N 5   
A1BAR C13 N1   sing N N 6   
A1BAR C6  C5   sing N N 7   
A1BAR C6  O1   sing N N 8   
A1BAR C5  N1   sing N N 9   
A1BAR N1  C7   sing N N 10  
A1BAR C11 C10  sing Y N 11  
A1BAR C11 C12  doub Y N 12  
A1BAR C7  C10  doub Y N 13  
A1BAR C7  N2   sing Y N 14  
A1BAR C10 C9   sing Y N 15  
A1BAR C12 N4   sing Y N 16  
A1BAR N2  C8   doub Y N 17  
A1BAR C9  N4   sing Y N 18  
A1BAR C9  N3   doub Y N 19  
A1BAR C8  N3   sing Y N 20  
A1BAR C3  H7   sing N N 21  
A1BAR C3  H6   sing N N 22  
A1BAR C6  H11  sing N N 23  
A1BAR C6  H10  sing N N 24  
A1BAR C12 H15  sing N N 25  
A1BAR C1  H4   sing N N 26  
A1BAR C1  H5   sing N N 27  
A1BAR C1  H3   sing N N 28  
A1BAR C11 H14  sing N N 29  
A1BAR C13 H17  sing N N 30  
A1BAR C13 H18  sing N N 31  
A1BAR C2  H1   sing N N 32  
A1BAR C4  H9   sing N N 33  
A1BAR C4  H8   sing N N 34  
A1BAR C5  H2   sing N N 35  
A1BAR C8  H13  sing N N 36  
A1BAR N4  H16  sing N N 37  
A1BAR O1  H12  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
DMS   S   O    doub N N 121 
DMS   S   C1   sing N N 122 
DMS   S   C2   sing N N 123 
DMS   C1  H11  sing N N 124 
DMS   C1  H12  sing N N 125 
DMS   C1  H13  sing N N 126 
DMS   C2  H21  sing N N 127 
DMS   C2  H22  sing N N 128 
DMS   C2  H23  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
THR   N   CA   sing N N 337 
THR   N   H    sing N N 338 
THR   N   H2   sing N N 339 
THR   CA  C    sing N N 340 
THR   CA  CB   sing N N 341 
THR   CA  HA   sing N N 342 
THR   C   O    doub N N 343 
THR   C   OXT  sing N N 344 
THR   CB  OG1  sing N N 345 
THR   CB  CG2  sing N N 346 
THR   CB  HB   sing N N 347 
THR   OG1 HG1  sing N N 348 
THR   CG2 HG21 sing N N 349 
THR   CG2 HG22 sing N N 350 
THR   CG2 HG23 sing N N 351 
THR   OXT HXT  sing N N 352 
TYR   N   CA   sing N N 353 
TYR   N   H    sing N N 354 
TYR   N   H2   sing N N 355 
TYR   CA  C    sing N N 356 
TYR   CA  CB   sing N N 357 
TYR   CA  HA   sing N N 358 
TYR   C   O    doub N N 359 
TYR   C   OXT  sing N N 360 
TYR   CB  CG   sing N N 361 
TYR   CB  HB2  sing N N 362 
TYR   CB  HB3  sing N N 363 
TYR   CG  CD1  doub Y N 364 
TYR   CG  CD2  sing Y N 365 
TYR   CD1 CE1  sing Y N 366 
TYR   CD1 HD1  sing N N 367 
TYR   CD2 CE2  doub Y N 368 
TYR   CD2 HD2  sing N N 369 
TYR   CE1 CZ   doub Y N 370 
TYR   CE1 HE1  sing N N 371 
TYR   CE2 CZ   sing Y N 372 
TYR   CE2 HE2  sing N N 373 
TYR   CZ  OH   sing N N 374 
TYR   OH  HH   sing N N 375 
TYR   OXT HXT  sing N N 376 
VAL   N   CA   sing N N 377 
VAL   N   H    sing N N 378 
VAL   N   H2   sing N N 379 
VAL   CA  C    sing N N 380 
VAL   CA  CB   sing N N 381 
VAL   CA  HA   sing N N 382 
VAL   C   O    doub N N 383 
VAL   C   OXT  sing N N 384 
VAL   CB  CG1  sing N N 385 
VAL   CB  CG2  sing N N 386 
VAL   CB  HB   sing N N 387 
VAL   CG1 HG11 sing N N 388 
VAL   CG1 HG12 sing N N 389 
VAL   CG1 HG13 sing N N 390 
VAL   CG2 HG21 sing N N 391 
VAL   CG2 HG22 sing N N 392 
VAL   CG2 HG23 sing N N 393 
VAL   OXT HXT  sing N N 394 
# 
_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                    7HF7 
_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]   0.025293 
_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 
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   ? 19.768 -16.232 22.384  0.50 37.39 ?  3    VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 20.093 -16.161 21.130  0.50 45.94 ?  3    VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.753 -15.199 22.546  0.50 36.96 ?  3    VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 19.189 -15.021 21.225  0.50 45.87 ?  3    VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.349 -13.823 22.275  0.50 35.27 ?  3    VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.994 -13.729 21.208  0.50 45.20 ?  3    VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.407 -13.481 22.805  0.50 35.74 ?  3    VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 21.142 -13.697 21.654  0.50 45.49 ?  3    VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.122 -15.252 23.948  0.50 37.85 ?  3    VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.307 -15.106 22.484  0.50 46.33 ?  3    VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.113 -14.125 24.117  0.50 38.13 ?  3    VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.022 -14.309 22.289  0.50 46.48 ?  3    VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.467 -16.603 24.187  0.50 38.12 ?  3    VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 18.002 -16.557 22.824  0.50 46.51 ?  3    VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 18.046 -15.349 21.899  0.50 44.35 ?  3    VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 18.602 -15.013 20.454  0.50 55.04 ?  3    VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.819 -15.134 24.612  0.50 45.42 ?  3    VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.787 -14.718 23.232  0.50 55.60 ?  3    VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.582 -14.296 24.909  0.50 45.76 ?  3    VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.482 -14.378 23.093  0.50 55.77 ?  3    VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.587 -13.284 24.212  0.50 45.76 ?  3    VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.248 -13.381 22.121  0.50 55.77 ?  3    VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.539 -14.096 23.335  0.50 45.76 ?  3    VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.535 -14.674 21.533  0.50 55.77 ?  3    VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 17.038 -16.595 25.057  0.50 45.74 ?  3    VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 17.292 -16.583 23.484  0.50 55.81 ?  3    VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.807 -16.761 23.494  0.50 45.74 ?  3    VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 17.723 -17.017 22.018  0.50 55.81 ?  3    VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.147 -17.294 24.160  0.50 45.74 ?  3    VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.802 -16.972 23.183  0.50 55.81 ?  3    VAL   A HG23 1 
ATOM   31   N  N    A ASN   A 1 4   ? 18.659 -13.034 21.454  0.50 32.71 ?  4    ASN   A N    1 
ATOM   32   N  N    B ASN   A 1 4   ? 19.385 -12.663 20.689  0.50 44.03 ?  4    ASN   A N    1 
ATOM   33   C  CA   A ASN   A 1 4   ? 19.080 -11.680 21.126  0.50 29.93 ?  4    ASN   A CA   1 
ATOM   34   C  CA   B ASN   A 1 4   ? 20.038 -11.363 20.621  0.50 42.67 ?  4    ASN   A CA   1 
ATOM   35   C  C    A ASN   A 1 4   ? 17.916 -10.723 21.364  0.50 27.67 ?  4    ASN   A C    1 
ATOM   36   C  C    B ASN   A 1 4   ? 19.154 -10.317 21.289  0.50 40.68 ?  4    ASN   A C    1 
ATOM   37   O  O    A ASN   A 1 4   ? 16.795 -11.138 21.672  0.50 27.41 ?  4    ASN   A O    1 
ATOM   38   O  O    B ASN   A 1 4   ? 18.476 -10.615 22.278  0.50 40.83 ?  4    ASN   A O    1 
ATOM   39   C  CB   A ASN   A 1 4   ? 19.621 -11.578 19.689  0.50 29.24 ?  4    ASN   A CB   1 
ATOM   40   C  CB   B ASN   A 1 4   ? 20.310 -10.981 19.165  0.50 43.09 ?  4    ASN   A CB   1 
ATOM   41   C  CG   A ASN   A 1 4   ? 18.594 -11.957 18.644  0.50 28.48 ?  4    ASN   A CG   1 
ATOM   42   C  CG   B ASN   A 1 4   ? 20.585 -12.186 18.289  0.50 43.38 ?  4    ASN   A CG   1 
ATOM   43   O  OD1  A ASN   A 1 4   ? 17.482 -11.432 18.629  0.50 28.47 ?  4    ASN   A OD1  1 
ATOM   44   O  OD1  B ASN   A 1 4   ? 19.783 -12.531 17.420  0.50 43.55 ?  4    ASN   A OD1  1 
ATOM   45   N  ND2  A ASN   A 1 4   ? 18.966 -12.876 17.758  0.50 28.11 ?  4    ASN   A ND2  1 
ATOM   46   N  ND2  B ASN   A 1 4   ? 21.719 -12.835 18.512  0.50 43.41 ?  4    ASN   A ND2  1 
ATOM   47   H  H    A ASN   A 1 4   ? 17.921 -13.266 21.077  0.50 39.25 ?  4    ASN   A H    1 
ATOM   48   H  H    B ASN   A 1 4   ? 18.586 -12.667 20.372  0.50 52.84 ?  4    ASN   A H    1 
ATOM   49   H  HA   A ASN   A 1 4   ? 19.803 -11.433 21.719  0.50 35.92 ?  4    ASN   A HA   1 
ATOM   50   H  HA   B ASN   A 1 4   ? 20.887 -11.401 21.092  0.50 51.20 ?  4    ASN   A HA   1 
ATOM   51   H  HB2  A ASN   A 1 4   ? 19.895 -10.663 19.519  0.50 35.09 ?  4    ASN   A HB2  1 
ATOM   52   H  HB2  B ASN   A 1 4   ? 19.533 -10.526 18.807  0.50 51.71 ?  4    ASN   A HB2  1 
ATOM   53   H  HB3  A ASN   A 1 4   ? 20.379 -12.175 19.594  0.50 35.09 ?  4    ASN   A HB3  1 
ATOM   54   H  HB3  B ASN   A 1 4   ? 21.084 -10.394 19.134  0.50 51.71 ?  4    ASN   A HB3  1 
ATOM   55   H  HD21 A ASN   A 1 4   ? 18.420 -13.128 17.141  0.50 33.73 ?  4    ASN   A HD21 1 
ATOM   56   H  HD21 B ASN   A 1 4   ? 21.915 -13.525 18.039  0.50 52.09 ?  4    ASN   A HD21 1 
ATOM   57   H  HD22 A ASN   A 1 4   ? 19.754 -13.218 17.798  0.50 33.73 ?  4    ASN   A HD22 1 
ATOM   58   H  HD22 B ASN   A 1 4   ? 22.257 -12.566 19.126  0.50 52.09 ?  4    ASN   A HD22 1 
ATOM   59   N  N    A SER   A 1 5   ? 18.193 -9.427  21.215  0.50 25.65 ?  5    SER   A N    1 
ATOM   60   N  N    B SER   A 1 5   ? 19.141 -9.094  20.752  0.50 38.41 ?  5    SER   A N    1 
ATOM   61   C  CA   A SER   A 1 5   ? 17.251 -8.376  21.578  0.50 24.05 ?  5    SER   A CA   1 
ATOM   62   C  CA   B SER   A 1 5   ? 18.359 -8.001  21.321  0.50 35.97 ?  5    SER   A CA   1 
ATOM   63   C  C    A SER   A 1 5   ? 16.389 -7.907  20.409  0.50 22.05 ?  5    SER   A C    1 
ATOM   64   C  C    B SER   A 1 5   ? 17.251 -7.524  20.384  0.50 32.91 ?  5    SER   A C    1 
ATOM   65   O  O    A SER   A 1 5   ? 15.642 -6.936  20.562  0.50 22.37 ?  5    SER   A O    1 
ATOM   66   O  O    B SER   A 1 5   ? 16.682 -6.448  20.598  0.50 33.09 ?  5    SER   A O    1 
ATOM   67   C  CB   A SER   A 1 5   ? 17.992 -7.181  22.187  0.50 24.66 ?  5    SER   A CB   1 
ATOM   68   C  CB   B SER   A 1 5   ? 19.273 -6.847  21.746  0.50 36.54 ?  5    SER   A CB   1 
ATOM   69   O  OG   A SER   A 1 5   ? 18.911 -6.625  21.264  0.50 25.18 ?  5    SER   A OG   1 
ATOM   70   O  OG   B SER   A 1 5   ? 20.365 -6.694  20.855  0.50 36.74 ?  5    SER   A OG   1 
ATOM   71   H  H    A SER   A 1 5   ? 18.931 -9.129  20.890  0.50 30.78 ?  5    SER   A H    1 
ATOM   72   H  H    B SER   A 1 5   ? 19.580 -8.873  20.046  0.50 46.09 ?  5    SER   A H    1 
ATOM   73   H  HA   A SER   A 1 5   ? 16.652 -8.717  22.258  0.50 28.86 ?  5    SER   A HA   1 
ATOM   74   H  HA   B SER   A 1 5   ? 17.928 -8.325  22.120  0.50 43.16 ?  5    SER   A HA   1 
ATOM   75   H  HB2  A SER   A 1 5   ? 17.343 -6.501  22.441  0.50 29.59 ?  5    SER   A HB2  1 
ATOM   76   H  HB2  B SER   A 1 5   ? 18.766 -6.023  21.747  0.50 43.85 ?  5    SER   A HB2  1 
ATOM   77   H  HB3  A SER   A 1 5   ? 18.478 -7.477  22.974  0.50 29.59 ?  5    SER   A HB3  1 
ATOM   78   H  HB3  B SER   A 1 5   ? 19.609 -7.028  22.641  0.50 43.85 ?  5    SER   A HB3  1 
ATOM   79   H  HG   A SER   A 1 5   ? 19.304 -5.966  21.613  0.50 30.22 ?  5    SER   A HG   1 
ATOM   80   H  HG   B SER   A 1 5   ? 20.867 -6.071  21.119  0.50 44.09 ?  5    SER   A HG   1 
ATOM   81   N  N    A PHE   A 1 6   ? 16.462 -8.569  19.258  0.50 19.69 ?  6    PHE   A N    1 
ATOM   82   N  N    B PHE   A 1 6   ? 16.913 -8.313  19.366  0.50 29.50 ?  6    PHE   A N    1 
ATOM   83   C  CA   A PHE   A 1 6   ? 15.597 -8.212  18.139  0.50 17.64 ?  6    PHE   A CA   1 
ATOM   84   C  CA   B PHE   A 1 6   ? 15.869 -7.935  18.425  0.50 25.95 ?  6    PHE   A CA   1 
ATOM   85   C  C    A PHE   A 1 6   ? 14.156 -8.584  18.471  0.50 17.57 ?  6    PHE   A C    1 
ATOM   86   C  C    B PHE   A 1 6   ? 14.493 -8.283  18.984  0.50 25.18 ?  6    PHE   A C    1 
ATOM   87   O  O    A PHE   A 1 6   ? 13.889 -9.699  18.924  0.50 17.92 ?  6    PHE   A O    1 
ATOM   88   O  O    B PHE   A 1 6   ? 14.332 -9.239  19.747  0.50 25.57 ?  6    PHE   A O    1 
ATOM   89   C  CB   A PHE   A 1 6   ? 16.052 -8.933  16.873  0.50 16.39 ?  6    PHE   A CB   1 
ATOM   90   C  CB   B PHE   A 1 6   ? 16.072 -8.646  17.087  0.50 23.37 ?  6    PHE   A CB   1 
ATOM   91   C  CG   A PHE   A 1 6   ? 17.308 -8.360  16.266  0.50 15.39 ?  6    PHE   A CG   1 
ATOM   92   C  CG   B PHE   A 1 6   ? 17.337 -8.248  16.372  0.50 21.00 ?  6    PHE   A CG   1 
ATOM   93   C  CD1  A PHE   A 1 6   ? 17.270 -7.163  15.569  0.50 15.20 ?  6    PHE   A CD1  1 
ATOM   94   C  CD1  B PHE   A 1 6   ? 17.389 -7.084  15.620  0.50 19.86 ?  6    PHE   A CD1  1 
ATOM   95   C  CD2  A PHE   A 1 6   ? 18.517 -9.021  16.388  0.50 16.05 ?  6    PHE   A CD2  1 
ATOM   96   C  CD2  B PHE   A 1 6   ? 18.472 -9.038  16.452  0.50 20.59 ?  6    PHE   A CD2  1 
ATOM   97   C  CE1  A PHE   A 1 6   ? 18.418 -6.631  15.009  0.50 15.30 ?  6    PHE   A CE1  1 
ATOM   98   C  CE1  B PHE   A 1 6   ? 18.552 -6.715  14.962  0.50 19.32 ?  6    PHE   A CE1  1 
ATOM   99   C  CE2  A PHE   A 1 6   ? 19.667 -8.495  15.828  0.50 16.23 ?  6    PHE   A CE2  1 
ATOM   100  C  CE2  B PHE   A 1 6   ? 19.635 -8.675  15.795  0.50 20.04 ?  6    PHE   A CE2  1 
ATOM   101  C  CZ   A PHE   A 1 6   ? 19.616 -7.299  15.138  0.50 15.71 ?  6    PHE   A CZ   1 
ATOM   102  C  CZ   B PHE   A 1 6   ? 19.675 -7.511  15.050  0.50 19.43 ?  6    PHE   A CZ   1 
ATOM   103  H  H    A PHE   A 1 6   ? 16.986 -9.230  19.107  0.50 23.63 ?  6    PHE   A H    1 
ATOM   104  H  H    B PHE   A 1 6   ? 17.273 -9.076  19.204  0.50 35.40 ?  6    PHE   A H    1 
ATOM   105  H  HA   A PHE   A 1 6   ? 15.634 -7.263  17.991  0.50 21.16 ?  6    PHE   A HA   1 
ATOM   106  H  HA   B PHE   A 1 6   ? 15.908 -6.979  18.274  0.50 31.14 ?  6    PHE   A HA   1 
ATOM   107  H  HB2  A PHE   A 1 6   ? 16.218 -9.868  17.091  0.50 19.67 ?  6    PHE   A HB2  1 
ATOM   108  H  HB2  B PHE   A 1 6   ? 16.105 -9.603  17.247  0.50 28.04 ?  6    PHE   A HB2  1 
ATOM   109  H  HB3  A PHE   A 1 6   ? 15.342 -8.879  16.213  0.50 19.67 ?  6    PHE   A HB3  1 
ATOM   110  H  HB3  B PHE   A 1 6   ? 15.320 -8.439  16.510  0.50 28.04 ?  6    PHE   A HB3  1 
ATOM   111  H  HD1  A PHE   A 1 6   ? 16.456 -6.713  15.484  0.50 18.25 ?  6    PHE   A HD1  1 
ATOM   112  H  HD1  B PHE   A 1 6   ? 16.632 -6.545  15.560  0.50 23.83 ?  6    PHE   A HD1  1 
ATOM   113  H  HD2  A PHE   A 1 6   ? 18.556 -9.827  16.855  0.50 19.26 ?  6    PHE   A HD2  1 
ATOM   114  H  HD2  B PHE   A 1 6   ? 18.452 -9.821  16.953  0.50 24.71 ?  6    PHE   A HD2  1 
ATOM   115  H  HE1  A PHE   A 1 6   ? 18.374 -5.826  14.546  0.50 18.37 ?  6    PHE   A HE1  1 
ATOM   116  H  HE1  B PHE   A 1 6   ? 18.574 -5.932  14.461  0.50 23.18 ?  6    PHE   A HE1  1 
ATOM   117  H  HE2  A PHE   A 1 6   ? 20.477 -8.941  15.918  0.50 19.47 ?  6    PHE   A HE2  1 
ATOM   118  H  HE2  B PHE   A 1 6   ? 20.394 -9.210  15.856  0.50 24.04 ?  6    PHE   A HE2  1 
ATOM   119  H  HZ   A PHE   A 1 6   ? 20.386 -6.939  14.762  0.50 18.85 ?  6    PHE   A HZ   1 
ATOM   120  H  HZ   B PHE   A 1 6   ? 20.457 -7.264  14.608  0.50 23.32 ?  6    PHE   A HZ   1 
ATOM   121  N  N    A SER   A 1 7   ? 13.223 -7.653  18.242  0.50 17.58 ?  7    SER   A N    1 
ATOM   122  N  N    B SER   A 1 7   ? 13.491 -7.501  18.583  0.50 23.75 ?  7    SER   A N    1 
ATOM   123  C  CA   A SER   A 1 7   ? 11.847 -7.792  18.713  0.50 18.14 ?  7    SER   A CA   1 
ATOM   124  C  CA   B SER   A 1 7   ? 12.150 -7.619  19.136  0.50 23.03 ?  7    SER   A CA   1 
ATOM   125  C  C    A SER   A 1 7   ? 10.853 -7.506  17.594  0.50 16.46 ?  7    SER   A C    1 
ATOM   126  C  C    B SER   A 1 7   ? 11.122 -7.336  18.052  0.50 21.52 ?  7    SER   A C    1 
ATOM   127  O  O    A SER   A 1 7   ? 11.066 -6.605  16.779  0.50 16.41 ?  7    SER   A O    1 
ATOM   128  O  O    B SER   A 1 7   ? 11.290 -6.414  17.250  0.50 21.50 ?  7    SER   A O    1 
ATOM   129  C  CB   A SER   A 1 7   ? 11.585 -6.834  19.883  0.50 20.25 ?  7    SER   A CB   1 
ATOM   130  C  CB   B SER   A 1 7   ? 11.959 -6.638  20.302  0.50 23.72 ?  7    SER   A CB   1 
ATOM   131  O  OG   A SER   A 1 7   ? 10.266 -6.975  20.383  0.50 21.65 ?  7    SER   A OG   1 
ATOM   132  O  OG   B SER   A 1 7   ? 10.593 -6.311  20.481  0.50 24.24 ?  7    SER   A OG   1 
ATOM   133  H  H    A SER   A 1 7   ? 13.363 -6.931  17.799  0.50 21.10 ?  7    SER   A H    1 
ATOM   134  H  H    B SER   A 1 7   ? 13.563 -6.894  17.975  0.50 28.50 ?  7    SER   A H    1 
ATOM   135  H  HA   A SER   A 1 7   ? 11.694 -8.696  19.021  0.50 21.76 ?  7    SER   A HA   1 
ATOM   136  H  HA   B SER   A 1 7   ? 12.011 -8.519  19.469  0.50 27.64 ?  7    SER   A HA   1 
ATOM   137  H  HB2  A SER   A 1 7   ? 12.215 -7.031  20.595  0.50 24.30 ?  7    SER   A HB2  1 
ATOM   138  H  HB2  B SER   A 1 7   ? 12.287 -7.050  21.119  0.50 28.46 ?  7    SER   A HB2  1 
ATOM   139  H  HB3  A SER   A 1 7   ? 11.711 -5.920  19.578  0.50 24.30 ?  7    SER   A HB3  1 
ATOM   140  H  HB3  B SER   A 1 7   ? 12.459 -5.828  20.118  0.50 28.46 ?  7    SER   A HB3  1 
ATOM   141  H  HG   A SER   A 1 7   ? 10.146 -6.442  21.024  0.50 25.99 ?  7    SER   A HG   1 
ATOM   142  H  HG   B SER   A 1 7   ? 10.507 -5.768  21.117  0.50 29.09 ?  7    SER   A HG   1 
ATOM   143  N  N    A GLY   A 1 8   ? 9.760  -8.272  17.566  0.50 15.47 ?  8    GLY   A N    1 
ATOM   144  N  N    B GLY   A 1 8   ? 10.064 -8.144  18.026  0.50 20.28 ?  8    GLY   A N    1 
ATOM   145  C  CA   A GLY   A 1 8   ? 8.682  -8.012  16.628  0.50 14.70 ?  8    GLY   A CA   1 
ATOM   146  C  CA   B GLY   A 1 8   ? 8.948  -7.907  17.135  0.50 18.86 ?  8    GLY   A CA   1 
ATOM   147  C  C    A GLY   A 1 8   ? 8.897  -8.524  15.222  0.50 13.91 ?  8    GLY   A C    1 
ATOM   148  C  C    B GLY   A 1 8   ? 9.101  -8.430  15.727  0.50 17.34 ?  8    GLY   A C    1 
ATOM   149  O  O    A GLY   A 1 8   ? 8.186  -8.096  14.306  0.50 14.45 ?  8    GLY   A O    1 
ATOM   150  O  O    B GLY   A 1 8   ? 8.319  -8.035  14.855  0.50 18.03 ?  8    GLY   A O    1 
ATOM   151  H  H    A GLY   A 1 8   ? 9.624  -8.948  18.079  0.50 18.57 ?  8    GLY   A H    1 
ATOM   152  H  H    B GLY   A 1 8   ? 9.975  -8.839  18.519  0.50 24.33 ?  8    GLY   A H    1 
ATOM   153  H  HA2  A GLY   A 1 8   ? 7.864  -8.410  16.975  0.50 17.64 ?  8    GLY   A HA2  1 
ATOM   154  H  HA2  B GLY   A 1 8   ? 8.158  -8.318  17.510  0.50 22.63 ?  8    GLY   A HA2  1 
ATOM   155  H  HA3  A GLY   A 1 8   ? 8.539  -7.054  16.573  0.50 17.64 ?  8    GLY   A HA3  1 
ATOM   156  H  HA3  B GLY   A 1 8   ? 8.793  -6.953  17.075  0.50 22.63 ?  8    GLY   A HA3  1 
ATOM   157  N  N    A TYR   A 1 9   ? 9.854  -9.427  15.015  0.50 12.83 ?  9    TYR   A N    1 
ATOM   158  N  N    B TYR   A 1 9   ? 10.070 -9.304  15.469  0.50 15.62 ?  9    TYR   A N    1 
ATOM   159  C  CA   A TYR   A 1 9   ? 10.137 -9.975  13.694  0.50 12.24 ?  9    TYR   A CA   1 
ATOM   160  C  CA   B TYR   A 1 9   ? 10.260 -9.825  14.124  0.50 14.29 ?  9    TYR   A CA   1 
ATOM   161  C  C    A TYR   A 1 9   ? 9.304  -11.219 13.418  0.50 12.06 ?  9    TYR   A C    1 
ATOM   162  C  C    B TYR   A 1 9   ? 9.327  -10.999 13.854  0.50 13.47 ?  9    TYR   A C    1 
ATOM   163  O  O    A TYR   A 1 9   ? 9.070  -12.044 14.308  0.50 13.04 ?  9    TYR   A O    1 
ATOM   164  O  O    B TYR   A 1 9   ? 8.924  -11.732 14.762  0.50 14.35 ?  9    TYR   A O    1 
ATOM   165  C  CB   A TYR   A 1 9   ? 11.620 -10.339 13.564  0.50 12.77 ?  9    TYR   A CB   1 
ATOM   166  C  CB   B TYR   A 1 9   ? 11.714 -10.257 13.910  0.50 14.42 ?  9    TYR   A CB   1 
ATOM   167  C  CG   A TYR   A 1 9   ? 12.516 -9.136  13.395  0.50 13.22 ?  9    TYR   A CG   1 
ATOM   168  C  CG   B TYR   A 1 9   ? 12.646 -9.084  13.716  0.50 14.12 ?  9    TYR   A CG   1 
ATOM   169  C  CD1  A TYR   A 1 9   ? 12.855 -8.346  14.483  0.50 13.90 ?  9    TYR   A CD1  1 
ATOM   170  C  CD1  B TYR   A 1 9   ? 12.965 -8.250  14.778  0.50 14.48 ?  9    TYR   A CD1  1 
ATOM   171  C  CD2  A TYR   A 1 9   ? 13.005 -8.778  12.145  0.50 13.28 ?  9    TYR   A CD2  1 
ATOM   172  C  CD2  B TYR   A 1 9   ? 13.186 -8.794  12.469  0.50 13.94 ?  9    TYR   A CD2  1 
ATOM   173  C  CE1  A TYR   A 1 9   ? 13.656 -7.230  14.336  0.50 14.22 ?  9    TYR   A CE1  1 
ATOM   174  C  CE1  B TYR   A 1 9   ? 13.797 -7.166  14.610  0.50 14.92 ?  9    TYR   A CE1  1 
ATOM   175  C  CE2  A TYR   A 1 9   ? 13.810 -7.666  11.986  0.50 13.57 ?  9    TYR   A CE2  1 
ATOM   176  C  CE2  B TYR   A 1 9   ? 14.022 -7.709  12.291  0.50 14.27 ?  9    TYR   A CE2  1 
ATOM   177  C  CZ   A TYR   A 1 9   ? 14.132 -6.896  13.085  0.50 13.98 ?  9    TYR   A CZ   1 
ATOM   178  C  CZ   B TYR   A 1 9   ? 14.322 -6.900  13.366  0.50 15.02 ?  9    TYR   A CZ   1 
ATOM   179  O  OH   A TYR   A 1 9   ? 14.924 -5.786  12.924  0.50 14.61 ?  9    TYR   A OH   1 
ATOM   180  O  OH   B TYR   A 1 9   ? 15.151 -5.821  13.197  0.50 16.38 ?  9    TYR   A OH   1 
ATOM   181  H  H    A TYR   A 1 9   ? 10.352 -9.742  15.632  0.50 15.39 ?  9    TYR   A H    1 
ATOM   182  H  H    B TYR   A 1 9   ? 10.632 -9.606  16.051  0.50 18.74 ?  9    TYR   A H    1 
ATOM   183  H  HA   A TYR   A 1 9   ? 9.925  -9.317  13.015  0.50 14.68 ?  9    TYR   A HA   1 
ATOM   184  H  HA   B TYR   A 1 9   ? 10.068 -9.122  13.482  0.50 17.15 ?  9    TYR   A HA   1 
ATOM   185  H  HB2  A TYR   A 1 9   ? 11.899 -10.814 14.361  0.50 15.33 ?  9    TYR   A HB2  1 
ATOM   186  H  HB2  B TYR   A 1 9   ? 12.022 -10.764 14.678  0.50 17.30 ?  9    TYR   A HB2  1 
ATOM   187  H  HB3  A TYR   A 1 9   ? 11.731 -10.907 12.784  0.50 15.33 ?  9    TYR   A HB3  1 
ATOM   188  H  HB3  B TYR   A 1 9   ? 11.755 -10.806 13.112  0.50 17.30 ?  9    TYR   A HB3  1 
ATOM   189  H  HD1  A TYR   A 1 9   ? 12.526 -8.570  15.326  0.50 16.68 ?  9    TYR   A HD1  1 
ATOM   190  H  HD1  B TYR   A 1 9   ? 12.604 -8.427  15.616  0.50 17.38 ?  9    TYR   A HD1  1 
ATOM   191  H  HD2  A TYR   A 1 9   ? 12.785 -9.294  11.402  0.50 15.93 ?  9    TYR   A HD2  1 
ATOM   192  H  HD2  B TYR   A 1 9   ? 12.987 -9.340  11.742  0.50 16.72 ?  9    TYR   A HD2  1 
ATOM   193  H  HE1  A TYR   A 1 9   ? 13.875 -6.713  15.076  0.50 17.06 ?  9    TYR   A HE1  1 
ATOM   194  H  HE1  B TYR   A 1 9   ? 13.996 -6.618  15.333  0.50 17.90 ?  9    TYR   A HE1  1 
ATOM   195  H  HE2  A TYR   A 1 9   ? 14.135 -7.439  11.143  0.50 16.28 ?  9    TYR   A HE2  1 
ATOM   196  H  HE2  B TYR   A 1 9   ? 14.385 -7.527  11.453  0.50 17.13 ?  9    TYR   A HE2  1 
ATOM   197  H  HH   A TYR   A 1 9   ? 15.057 -5.414  13.665  0.50 17.54 ?  9    TYR   A HH   1 
ATOM   198  H  HH   B TYR   A 1 9   ? 15.247 -5.419  13.927  0.50 19.66 ?  9    TYR   A HH   1 
ATOM   199  N  N    A LEU   A 1 10  ? 8.888  -11.363 12.161  0.50 11.60 ?  10   LEU   A N    1 
ATOM   200  N  N    B LEU   A 1 10  ? 8.969  -11.149 12.583  0.50 12.63 ?  10   LEU   A N    1 
ATOM   201  C  CA   A LEU   A 1 10  ? 8.306  -12.602 11.671  0.50 11.11 ?  10   LEU   A CA   1 
ATOM   202  C  CA   B LEU   A 1 10  ? 8.301  -12.340 12.084  0.50 12.19 ?  10   LEU   A CA   1 
ATOM   203  C  C    A LEU   A 1 10  ? 9.430  -13.529 11.227  0.50 10.92 ?  10   LEU   A C    1 
ATOM   204  C  C    B LEU   A 1 10  ? 9.369  -13.300 11.574  0.50 11.46 ?  10   LEU   A C    1 
ATOM   205  O  O    A LEU   A 1 10  ? 10.372 -13.105 10.551  0.50 11.29 ?  10   LEU   A O    1 
ATOM   206  O  O    B LEU   A 1 10  ? 10.245 -12.907 10.798  0.50 12.04 ?  10   LEU   A O    1 
ATOM   207  C  CB   A LEU   A 1 10  ? 7.395  -12.309 10.480  0.50 11.87 ?  10   LEU   A CB   1 
ATOM   208  C  CB   B LEU   A 1 10  ? 7.351  -11.963 10.946  0.50 12.92 ?  10   LEU   A CB   1 
ATOM   209  C  CG   A LEU   A 1 10  ? 6.648  -13.490 9.858   0.50 13.35 ?  10   LEU   A CG   1 
ATOM   210  C  CG   B LEU   A 1 10  ? 6.651  -13.133 10.252  0.50 14.29 ?  10   LEU   A CG   1 
ATOM   211  C  CD1  A LEU   A 1 10  ? 5.544  -13.979 10.775  0.50 14.16 ?  10   LEU   A CD1  1 
ATOM   212  C  CD1  B LEU   A 1 10  ? 5.696  -13.840 11.201  0.50 15.22 ?  10   LEU   A CD1  1 
ATOM   213  C  CD2  A LEU   A 1 10  ? 6.092  -13.114 8.496   0.50 13.79 ?  10   LEU   A CD2  1 
ATOM   214  C  CD2  B LEU   A 1 10  ? 5.932  -12.654 9.000   0.50 15.70 ?  10   LEU   A CD2  1 
ATOM   215  H  H    A LEU   A 1 10  ? 8.936  -10.747 11.555  0.50 13.92 ?  10   LEU   A H    1 
ATOM   216  H  H    B LEU   A 1 10  ? 9.107  -10.551 11.977  0.50 15.15 ?  10   LEU   A H    1 
ATOM   217  H  HA   A LEU   A 1 10  ? 7.790  -13.035 12.371  0.50 13.34 ?  10   LEU   A HA   1 
ATOM   218  H  HA   B LEU   A 1 10  ? 7.791  -12.759 12.797  0.50 14.62 ?  10   LEU   A HA   1 
ATOM   219  H  HB2  A LEU   A 1 10  ? 6.727  -11.672 10.763  0.50 14.24 ?  10   LEU   A HB2  1 
ATOM   220  H  HB2  B LEU   A 1 10  ? 6.659  -11.376 11.298  0.50 15.50 ?  10   LEU   A HB2  1 
ATOM   221  H  HB3  A LEU   A 1 10  ? 7.938  -11.919 9.777   0.50 14.24 ?  10   LEU   A HB3  1 
ATOM   222  H  HB3  B LEU   A 1 10  ? 7.859  -11.485 10.270  0.50 15.50 ?  10   LEU   A HB3  1 
ATOM   223  H  HG   A LEU   A 1 10  ? 7.269  -14.226 9.725   0.50 16.02 ?  10   LEU   A HG   1 
ATOM   224  H  HG   B LEU   A 1 10  ? 7.318  -13.780 9.976   0.50 17.15 ?  10   LEU   A HG   1 
ATOM   225  H  HD11 A LEU   A 1 10  ? 5.132  -14.767 10.385  0.50 16.99 ?  10   LEU   A HD11 1 
ATOM   226  H  HD11 B LEU   A 1 10  ? 5.251  -14.558 10.723  0.50 18.26 ?  10   LEU   A HD11 1 
ATOM   227  H  HD12 A LEU   A 1 10  ? 5.925  -14.199 11.639  0.50 16.99 ?  10   LEU   A HD12 1 
ATOM   228  H  HD12 B LEU   A 1 10  ? 6.198  -14.203 11.948  0.50 18.26 ?  10   LEU   A HD12 1 
ATOM   229  H  HD13 A LEU   A 1 10  ? 4.883  -13.277 10.875  0.50 16.99 ?  10   LEU   A HD13 1 
ATOM   230  H  HD13 B LEU   A 1 10  ? 5.040  -13.202 11.523  0.50 18.26 ?  10   LEU   A HD13 1 
ATOM   231  H  HD21 A LEU   A 1 10  ? 5.618  -13.875 8.127   0.50 16.54 ?  10   LEU   A HD21 1 
ATOM   232  H  HD21 B LEU   A 1 10  ? 5.496  -13.412 8.580   0.50 18.84 ?  10   LEU   A HD21 1 
ATOM   233  H  HD22 A LEU   A 1 10  ? 5.486  -12.364 8.602   0.50 16.54 ?  10   LEU   A HD22 1 
ATOM   234  H  HD22 B LEU   A 1 10  ? 5.274  -11.989 9.252   0.50 18.84 ?  10   LEU   A HD22 1 
ATOM   235  H  HD23 A LEU   A 1 10  ? 6.828  -12.867 7.914   0.50 16.54 ?  10   LEU   A HD23 1 
ATOM   236  H  HD23 B LEU   A 1 10  ? 6.583  -12.267 8.395   0.50 18.84 ?  10   LEU   A HD23 1 
ATOM   237  N  N    A LYS   A 1 11  ? 9.320  -14.800 11.601  0.50 11.04 ?  11   LYS   A N    1 
ATOM   238  N  N    B LYS   A 1 11  ? 9.306  -14.547 12.026  0.50 11.25 ?  11   LYS   A N    1 
ATOM   239  C  CA   A LYS   A 1 11  ? 10.323 -15.802 11.271  0.50 11.08 ?  11   LYS   A CA   1 
ATOM   240  C  CA   B LYS   A 1 11  ? 10.248 -15.568 11.584  0.50 11.41 ?  11   LYS   A CA   1 
ATOM   241  C  C    A LYS   A 1 11  ? 9.971  -16.411 9.921   0.50 10.82 ?  11   LYS   A C    1 
ATOM   242  C  C    B LYS   A 1 11  ? 9.834  -16.068 10.206  0.50 10.57 ?  11   LYS   A C    1 
ATOM   243  O  O    A LYS   A 1 11  ? 8.914  -17.032 9.779   0.50 11.78 ?  11   LYS   A O    1 
ATOM   244  O  O    B LYS   A 1 11  ? 8.704  -16.530 10.026  0.50 11.22 ?  11   LYS   A O    1 
ATOM   245  C  CB   A LYS   A 1 11  ? 10.333 -16.872 12.362  0.50 11.49 ?  11   LYS   A CB   1 
ATOM   246  C  CB   B LYS   A 1 11  ? 10.274 -16.718 12.591  0.50 11.84 ?  11   LYS   A CB   1 
ATOM   247  C  CG   A LYS   A 1 11  ? 11.357 -17.969 12.189  0.50 11.92 ?  11   LYS   A CG   1 
ATOM   248  C  CG   B LYS   A 1 11  ? 11.346 -17.788 12.339  0.50 12.05 ?  11   LYS   A CG   1 
ATOM   249  C  CD   A LYS   A 1 11  ? 11.416 -18.803 13.458  0.50 12.58 ?  11   LYS   A CD   1 
ATOM   250  C  CD   B LYS   A 1 11  ? 11.461 -18.746 13.534  0.50 12.54 ?  11   LYS   A CD   1 
ATOM   251  C  CE   A LYS   A 1 11  ? 12.398 -19.946 13.340  0.50 12.59 ?  11   LYS   A CE   1 
ATOM   252  C  CE   B LYS   A 1 11  ? 12.501 -19.851 13.324  0.50 12.65 ?  11   LYS   A CE   1 
ATOM   253  N  NZ   A LYS   A 1 11  ? 13.762 -19.462 13.015  0.50 12.80 ?  11   LYS   A NZ   1 
ATOM   254  N  NZ   B LYS   A 1 11  ? 13.892 -19.333 13.233  0.50 12.83 ?  11   LYS   A NZ   1 
ATOM   255  H  H    A LYS   A 1 11  ? 8.651  -15.124 12.043  0.50 13.25 ?  11   LYS   A H    1 
ATOM   256  H  H    B LYS   A 1 11  ? 8.721  -14.823 12.595  0.50 13.50 ?  11   LYS   A H    1 
ATOM   257  H  HA   A LYS   A 1 11  ? 11.201 -15.394 11.220  0.50 13.30 ?  11   LYS   A HA   1 
ATOM   258  H  HA   B LYS   A 1 11  ? 11.132 -15.181 11.518  0.50 13.69 ?  11   LYS   A HA   1 
ATOM   259  H  HB2  A LYS   A 1 11  ? 10.514 -16.441 13.213  0.50 13.78 ?  11   LYS   A HB2  1 
ATOM   260  H  HB2  B LYS   A 1 11  ? 10.428 -16.340 13.470  0.50 14.21 ?  11   LYS   A HB2  1 
ATOM   261  H  HB3  A LYS   A 1 11  ? 9.459  -17.291 12.391  0.50 13.78 ?  11   LYS   A HB3  1 
ATOM   262  H  HB3  B LYS   A 1 11  ? 9.407  -17.152 12.572  0.50 14.21 ?  11   LYS   A HB3  1 
ATOM   263  H  HG2  A LYS   A 1 11  ? 11.097 -18.546 11.451  0.50 14.30 ?  11   LYS   A HG2  1 
ATOM   264  H  HG2  B LYS   A 1 11  ? 11.104 -18.304 11.554  0.50 14.46 ?  11   LYS   A HG2  1 
ATOM   265  H  HG3  A LYS   A 1 11  ? 12.230 -17.581 12.030  0.50 14.30 ?  11   LYS   A HG3  1 
ATOM   266  H  HG3  B LYS   A 1 11  ? 12.204 -17.358 12.209  0.50 14.46 ?  11   LYS   A HG3  1 
ATOM   267  H  HD2  A LYS   A 1 11  ? 11.690 -18.237 14.195  0.50 15.10 ?  11   LYS   A HD2  1 
ATOM   268  H  HD2  B LYS   A 1 11  ? 11.711 -18.241 14.321  0.50 15.05 ?  11   LYS   A HD2  1 
ATOM   269  H  HD3  A LYS   A 1 11  ? 10.534 -19.174 13.633  0.50 15.10 ?  11   LYS   A HD3  1 
ATOM   270  H  HD3  B LYS   A 1 11  ? 10.600 -19.173 13.676  0.50 15.05 ?  11   LYS   A HD3  1 
ATOM   271  H  HE2  A LYS   A 1 11  ? 12.436 -20.421 14.184  0.50 15.11 ?  11   LYS   A HE2  1 
ATOM   272  H  HE2  B LYS   A 1 11  ? 12.465 -20.469 14.074  0.50 15.18 ?  11   LYS   A HE2  1 
ATOM   273  H  HE3  A LYS   A 1 11  ? 12.110 -20.542 12.632  0.50 15.11 ?  11   LYS   A HE3  1 
ATOM   274  H  HE3  B LYS   A 1 11  ? 12.307 -20.323 12.500  0.50 15.18 ?  11   LYS   A HE3  1 
ATOM   275  H  HZ1  A LYS   A 1 11  ? 14.330 -20.146 12.997  0.50 15.35 ?  11   LYS   A HZ1  1 
ATOM   276  H  HZ1  B LYS   A 1 11  ? 14.460 -20.002 13.073  0.50 15.39 ?  11   LYS   A HZ1  1 
ATOM   277  H  HZ2  A LYS   A 1 11  ? 13.763 -19.064 12.219  0.50 15.35 ?  11   LYS   A HZ2  1 
ATOM   278  H  HZ2  B LYS   A 1 11  ? 13.954 -18.740 12.572  0.50 15.39 ?  11   LYS   A HZ2  1 
ATOM   279  H  HZ3  A LYS   A 1 11  ? 14.032 -18.877 13.630  0.50 15.35 ?  11   LYS   A HZ3  1 
ATOM   280  H  HZ3  B LYS   A 1 11  ? 14.123 -18.939 13.997  0.50 15.39 ?  11   LYS   A HZ3  1 
ATOM   281  N  N    A LEU   A 1 12  ? 10.851 -16.247 8.931   0.50 10.05 ?  12   LEU   A N    1 
ATOM   282  N  N    B LEU   A 1 12  ? 10.730 -15.956 9.229   0.50 10.47 ?  12   LEU   A N    1 
ATOM   283  C  CA   A LEU   A 1 12  ? 10.595 -16.833 7.618   0.50 10.27 ?  12   LEU   A CA   1 
ATOM   284  C  CA   B LEU   A 1 12  ? 10.476 -16.483 7.893   0.50 10.59 ?  12   LEU   A CA   1 
ATOM   285  C  C    A LEU   A 1 12  ? 11.191 -18.230 7.467   0.50 10.41 ?  12   LEU   A C    1 
ATOM   286  C  C    B LEU   A 1 12  ? 11.056 -17.875 7.694   0.50 10.64 ?  12   LEU   A C    1 
ATOM   287  O  O    A LEU   A 1 12  ? 10.552 -19.110 6.880   0.50 10.66 ?  12   LEU   A O    1 
ATOM   288  O  O    B LEU   A 1 12  ? 10.409 -18.732 7.080   0.50 10.74 ?  12   LEU   A O    1 
ATOM   289  C  CB   A LEU   A 1 12  ? 11.125 -15.926 6.502   0.50 10.54 ?  12   LEU   A CB   1 
ATOM   290  C  CB   B LEU   A 1 12  ? 11.040 -15.539 6.827   0.50 11.22 ?  12   LEU   A CB   1 
ATOM   291  C  CG   A LEU   A 1 12  ? 10.466 -14.555 6.329   0.50 11.25 ?  12   LEU   A CG   1 
ATOM   292  C  CG   B LEU   A 1 12  ? 10.379 -14.165 6.747   0.50 11.93 ?  12   LEU   A CG   1 
ATOM   293  C  CD1  A LEU   A 1 12  ? 11.178 -13.781 5.233   0.50 11.97 ?  12   LEU   A CD1  1 
ATOM   294  C  CD1  B LEU   A 1 12  ? 11.026 -13.337 5.649   0.50 12.80 ?  12   LEU   A CD1  1 
ATOM   295  C  CD2  A LEU   A 1 12  ? 8.985  -14.693 6.013   0.50 11.90 ?  12   LEU   A CD2  1 
ATOM   296  C  CD2  B LEU   A 1 12  ? 8.888  -14.313 6.505   0.50 12.36 ?  12   LEU   A CD2  1 
ATOM   297  H  H    A LEU   A 1 12  ? 11.592 -15.806 8.991   0.50 12.06 ?  12   LEU   A H    1 
ATOM   298  H  H    B LEU   A 1 12  ? 11.496 -15.568 9.314   0.50 12.56 ?  12   LEU   A H    1 
ATOM   299  H  HA   A LEU   A 1 12  ? 9.637  -16.915 7.503   0.50 12.33 ?  12   LEU   A HA   1 
ATOM   300  H  HA   B LEU   A 1 12  ? 9.517  -16.542 7.761   0.50 12.71 ?  12   LEU   A HA   1 
ATOM   301  H  HB2  A LEU   A 1 12  ? 12.065 -15.772 6.664   0.50 12.65 ?  12   LEU   A HB2  1 
ATOM   302  H  HB2  B LEU   A 1 12  ? 11.980 -15.395 7.009   0.50 13.47 ?  12   LEU   A HB2  1 
ATOM   303  H  HB3  A LEU   A 1 12  ? 11.019 -16.401 5.661   0.50 12.65 ?  12   LEU   A HB3  1 
ATOM   304  H  HB3  B LEU   A 1 12  ? 10.935 -15.957 5.960   0.50 13.47 ?  12   LEU   A HB3  1 
ATOM   305  H  HG   A LEU   A 1 12  ? 10.551 -14.059 7.155   0.50 13.50 ?  12   LEU   A HG   1 
ATOM   306  H  HG   B LEU   A 1 12  ? 10.504 -13.698 7.591   0.50 14.31 ?  12   LEU   A HG   1 
ATOM   307  H  HD11 A LEU   A 1 12  ? 10.750 -12.917 5.128   0.50 14.36 ?  12   LEU   A HD11 1 
ATOM   308  H  HD11 B LEU   A 1 12  ? 10.598 -12.468 5.615   0.50 15.36 ?  12   LEU   A HD11 1 
ATOM   309  H  HD12 A LEU   A 1 12  ? 12.107 -13.662 5.483   0.50 14.36 ?  12   LEU   A HD12 1 
ATOM   310  H  HD12 B LEU   A 1 12  ? 11.969 -13.236 5.847   0.50 15.36 ?  12   LEU   A HD12 1 
ATOM   311  H  HD13 A LEU   A 1 12  ? 11.121 -14.281 4.403   0.50 14.36 ?  12   LEU   A HD13 1 
ATOM   312  H  HD13 B LEU   A 1 12  ? 10.911 -13.797 4.803   0.50 15.36 ?  12   LEU   A HD13 1 
ATOM   313  H  HD21 A LEU   A 1 12  ? 8.621  -13.820 5.803   0.50 14.28 ?  12   LEU   A HD21 1 
ATOM   314  H  HD21 B LEU   A 1 12  ? 8.522  -13.459 6.230   0.50 14.83 ?  12   LEU   A HD21 1 
ATOM   315  H  HD22 A LEU   A 1 12  ? 8.876  -15.287 5.251   0.50 14.28 ?  12   LEU   A HD22 1 
ATOM   316  H  HD22 B LEU   A 1 12  ? 8.746  -14.975 5.810   0.50 14.83 ?  12   LEU   A HD22 1 
ATOM   317  H  HD23 A LEU   A 1 12  ? 8.527  -15.066 6.784   0.50 14.28 ?  12   LEU   A HD23 1 
ATOM   318  H  HD23 B LEU   A 1 12  ? 8.460  -14.605 7.328   0.50 14.83 ?  12   LEU   A HD23 1 
ATOM   319  N  N    A THR   A 1 13  ? 12.410 -18.438 7.958   0.50 10.42 ?  13   THR   A N    1 
ATOM   320  N  N    B THR   A 1 13  ? 12.269 -18.109 8.186   0.50 10.42 ?  13   THR   A N    1 
ATOM   321  C  CA   A THR   A 1 13  ? 13.102 -19.720 7.874   0.50 10.73 ?  13   THR   A CA   1 
ATOM   322  C  CA   B THR   A 1 13  ? 12.934 -19.399 8.070   0.50 10.76 ?  13   THR   A CA   1 
ATOM   323  C  C    A THR   A 1 13  ? 13.883 -19.919 9.167   0.50 10.77 ?  13   THR   A C    1 
ATOM   324  C  C    B THR   A 1 13  ? 13.711 -19.653 9.354   0.50 11.26 ?  13   THR   A C    1 
ATOM   325  O  O    A THR   A 1 13  ? 13.769 -19.135 10.115  0.50 10.95 ?  13   THR   A O    1 
ATOM   326  O  O    B THR   A 1 13  ? 13.653 -18.879 10.315  0.50 11.61 ?  13   THR   A O    1 
ATOM   327  C  CB   A THR   A 1 13  ? 14.073 -19.770 6.686   0.50 11.50 ?  13   THR   A CB   1 
ATOM   328  C  CB   B THR   A 1 13  ? 13.890 -19.440 6.871   0.50 11.16 ?  13   THR   A CB   1 
ATOM   329  O  OG1  A THR   A 1 13  ? 15.149 -18.856 6.924   0.50 11.84 ?  13   THR   A OG1  1 
ATOM   330  O  OG1  B THR   A 1 13  ? 14.969 -18.535 7.110   0.50 11.07 ?  13   THR   A OG1  1 
ATOM   331  C  CG2  A THR   A 1 13  ? 13.389 -19.416 5.380   0.50 12.22 ?  13   THR   A CG2  1 
ATOM   332  C  CG2  B THR   A 1 13  ? 13.186 -19.067 5.569   0.50 11.76 ?  13   THR   A CG2  1 
ATOM   333  H  H    A THR   A 1 13  ? 12.871 -17.833 8.349   0.50 12.50 ?  13   THR   A H    1 
ATOM   334  H  H    B THR   A 1 13  ? 12.741 -17.513 8.589   0.50 12.51 ?  13   THR   A H    1 
ATOM   335  H  HA   A THR   A 1 13  ? 12.455 -20.442 7.777   0.50 12.88 ?  13   THR   A HA   1 
ATOM   336  H  HA   B THR   A 1 13  ? 12.272 -20.096 7.963   0.50 12.91 ?  13   THR   A HA   1 
ATOM   337  H  HB   A THR   A 1 13  ? 14.433 -20.670 6.602   0.50 13.81 ?  13   THR   A HB   1 
ATOM   338  H  HB   B THR   A 1 13  ? 14.251 -20.334 6.777   0.50 13.39 ?  13   THR   A HB   1 
ATOM   339  H  HG1  A THR   A 1 13  ? 15.686 -18.873 6.277   0.50 14.21 ?  13   THR   A HG1  1 
ATOM   340  H  HG1  B THR   A 1 13  ? 15.496 -18.532 6.450   0.50 13.29 ?  13   THR   A HG1  1 
ATOM   341  H  HG21 A THR   A 1 13  ? 13.997 -19.568 4.638   0.50 14.66 ?  13   THR   A HG21 1 
ATOM   342  H  HG21 B THR   A 1 13  ? 13.796 -19.177 4.820   0.50 14.11 ?  13   THR   A HG21 1 
ATOM   343  H  HG22 A THR   A 1 13  ? 12.601 -19.967 5.259   0.50 14.66 ?  13   THR   A HG22 1 
ATOM   344  H  HG22 B THR   A 1 13  ? 12.419 -19.648 5.432   0.50 14.11 ?  13   THR   A HG22 1 
ATOM   345  H  HG23 A THR   A 1 13  ? 13.126 -18.484 5.387   0.50 14.66 ?  13   THR   A HG23 1 
ATOM   346  H  HG23 B THR   A 1 13  ? 12.887 -18.149 5.600   0.50 14.11 ?  13   THR   A HG23 1 
ATOM   347  N  N    A ASP   A 1 14  ? 14.724 -20.955 9.187   0.50 11.39 ?  14   ASP   A N    1 
ATOM   348  N  N    B ASP   A 1 14  ? 14.464 -20.751 9.347   0.50 11.91 ?  14   ASP   A N    1 
ATOM   349  C  CA   A ASP   A 1 14  ? 15.537 -21.213 10.368  0.50 12.29 ?  14   ASP   A CA   1 
ATOM   350  C  CA   B ASP   A 1 14  ? 15.361 -21.063 10.449  0.50 12.79 ?  14   ASP   A CA   1 
ATOM   351  C  C    A ASP   A 1 14  ? 16.370 -20.003 10.779  0.50 11.90 ?  14   ASP   A C    1 
ATOM   352  C  C    B ASP   A 1 14  ? 16.208 -19.855 10.823  0.50 12.35 ?  14   ASP   A C    1 
ATOM   353  O  O    A ASP   A 1 14  ? 16.681 -19.842 11.964  0.50 12.07 ?  14   ASP   A O    1 
ATOM   354  O  O    B ASP   A 1 14  ? 16.366 -19.545 12.010  0.50 13.04 ?  14   ASP   A O    1 
ATOM   355  C  CB   A ASP   A 1 14  ? 16.469 -22.399 10.121  0.50 14.64 ?  14   ASP   A CB   1 
ATOM   356  C  CB   B ASP   A 1 14  ? 16.262 -22.226 10.037  0.50 14.86 ?  14   ASP   A CB   1 
ATOM   357  C  CG   A ASP   A 1 14  ? 17.436 -22.602 11.258  0.50 18.08 ?  14   ASP   A CG   1 
ATOM   358  C  CG   B ASP   A 1 14  ? 17.114 -22.739 11.182  0.50 17.67 ?  14   ASP   A CG   1 
ATOM   359  O  OD1  A ASP   A 1 14  ? 16.971 -22.953 12.362  0.50 19.07 ?  14   ASP   A OD1  1 
ATOM   360  O  OD1  B ASP   A 1 14  ? 16.546 -23.216 12.188  0.50 18.33 ?  14   ASP   A OD1  1 
ATOM   361  O  OD2  A ASP   A 1 14  ? 18.650 -22.376 11.053  0.50 20.03 -1 14   ASP   A OD2  1 
ATOM   362  O  OD2  B ASP   A 1 14  ? 18.352 -22.673 11.071  0.50 19.71 -1 14   ASP   A OD2  1 
ATOM   363  H  H    A ASP   A 1 14  ? 14.835 -21.521 8.542   0.50 13.67 ?  14   ASP   A H    1 
ATOM   364  H  H    B ASP   A 1 14  ? 14.475 -21.318 8.713   0.50 14.29 ?  14   ASP   A H    1 
ATOM   365  H  HA   A ASP   A 1 14  ? 14.959 -21.445 11.110  0.50 14.74 ?  14   ASP   A HA   1 
ATOM   366  H  HA   B ASP   A 1 14  ? 14.842 -21.330 11.230  0.50 15.35 ?  14   ASP   A HA   1 
ATOM   367  H  HB2  A ASP   A 1 14  ? 15.931 -23.212 9.998   0.50 17.56 ?  14   ASP   A HB2  1 
ATOM   368  H  HB2  B ASP   A 1 14  ? 15.700 -22.951 9.710   0.50 17.83 ?  14   ASP   A HB2  1 
ATOM   369  H  HB3  A ASP   A 1 14  ? 17.002 -22.243 9.332   0.50 17.56 ?  14   ASP   A HB3  1 
ATOM   370  H  HB3  B ASP   A 1 14  ? 16.850 -21.925 9.324   0.50 17.83 ?  14   ASP   A HB3  1 
ATOM   371  N  N    . ASN   A 1 15  ? 16.748 -19.148 9.824   1.00 11.74 ?  15   ASN   A N    1 
ATOM   372  C  CA   . ASN   A 1 15  ? 17.734 -18.103 10.078  1.00 12.06 ?  15   ASN   A CA   1 
ATOM   373  C  C    . ASN   A 1 15  ? 17.367 -16.710 9.585   1.00 11.85 ?  15   ASN   A C    1 
ATOM   374  O  O    . ASN   A 1 15  ? 18.148 -15.783 9.823   1.00 13.60 ?  15   ASN   A O    1 
ATOM   375  C  CB   . ASN   A 1 15  ? 19.101 -18.507 9.491   1.00 11.80 ?  15   ASN   A CB   1 
ATOM   376  C  CG   . ASN   A 1 15  ? 19.086 -18.589 7.984   1.00 11.97 ?  15   ASN   A CG   1 
ATOM   377  O  OD1  . ASN   A 1 15  ? 18.367 -19.402 7.405   1.00 12.99 ?  15   ASN   A OD1  1 
ATOM   378  N  ND2  . ASN   A 1 15  ? 19.877 -17.741 7.335   1.00 12.16 ?  15   ASN   A ND2  1 
ATOM   379  H  H    A ASN   A 1 15  ? 16.441 -19.153 9.027   0.50 14.09 ?  15   ASN   A H    1 
ATOM   380  H  H    B ASN   A 1 15  ? 16.563 -19.265 8.997   0.50 14.09 ?  15   ASN   A H    1 
ATOM   381  H  HA   . ASN   A 1 15  ? 17.864 -18.030 11.036  1.00 14.47 ?  15   ASN   A HA   1 
ATOM   382  H  HB2  . ASN   A 1 15  ? 19.770 -17.846 9.752   1.00 14.16 ?  15   ASN   A HB2  1 
ATOM   383  H  HB3  . ASN   A 1 15  ? 19.357 -19.379 9.834   1.00 14.16 ?  15   ASN   A HB3  1 
ATOM   384  H  HD21 . ASN   A 1 15  ? 19.898 -17.742 6.473   1.00 14.59 ?  15   ASN   A HD21 1 
ATOM   385  H  HD22 . ASN   A 1 15  ? 20.370 -17.180 7.770   1.00 14.59 ?  15   ASN   A HD22 1 
ATOM   386  N  N    A VAL   A 1 16  ? 16.268 -16.561 8.842   0.50 10.97 ?  16   VAL   A N    1 
ATOM   387  N  N    B VAL   A 1 16  ? 16.187 -16.488 9.010   0.50 11.53 ?  16   VAL   A N    1 
ATOM   388  C  CA   A VAL   A 1 16  ? 15.861 -15.303 8.226   0.50 10.63 ?  16   VAL   A CA   1 
ATOM   389  C  CA   B VAL   A 1 16  ? 15.814 -15.172 8.498   0.50 11.00 ?  16   VAL   A CA   1 
ATOM   390  C  C    A VAL   A 1 16  ? 14.576 -14.819 8.889   0.50 9.91  ?  16   VAL   A C    1 
ATOM   391  C  C    B VAL   A 1 16  ? 14.563 -14.667 9.215   0.50 10.92 ?  16   VAL   A C    1 
ATOM   392  O  O    A VAL   A 1 16  ? 13.572 -15.542 8.941   0.50 9.48  ?  16   VAL   A O    1 
ATOM   393  O  O    B VAL   A 1 16  ? 13.578 -15.402 9.362   0.50 11.21 ?  16   VAL   A O    1 
ATOM   394  C  CB   A VAL   A 1 16  ? 15.680 -15.438 6.702   0.50 11.44 ?  16   VAL   A CB   1 
ATOM   395  C  CB   B VAL   A 1 16  ? 15.631 -15.181 6.969   0.50 11.17 ?  16   VAL   A CB   1 
ATOM   396  C  CG1  A VAL   A 1 16  ? 15.188 -14.119 6.106   0.50 11.72 ?  16   VAL   A CG1  1 
ATOM   397  C  CG1  B VAL   A 1 16  ? 15.283 -13.783 6.461   0.50 11.01 ?  16   VAL   A CG1  1 
ATOM   398  C  CG2  A VAL   A 1 16  ? 16.978 -15.870 6.031   0.50 12.27 ?  16   VAL   A CG2  1 
ATOM   399  C  CG2  B VAL   A 1 16  ? 16.886 -15.701 6.278   0.50 12.24 ?  16   VAL   A CG2  1 
ATOM   400  H  H    A VAL   A 1 16  ? 15.728 -17.214 8.677   0.50 13.16 ?  16   VAL   A H    1 
ATOM   401  H  H    B VAL   A 1 16  ? 15.576 -17.088 8.922   0.50 13.84 ?  16   VAL   A H    1 
ATOM   402  H  HA   A VAL   A 1 16  ? 16.555 -14.646 8.381   0.50 12.75 ?  16   VAL   A HA   1 
ATOM   403  H  HA   B VAL   A 1 16  ? 16.530 -14.548 8.698   0.50 13.20 ?  16   VAL   A HA   1 
ATOM   404  H  HB   A VAL   A 1 16  ? 15.014 -16.119 6.516   0.50 13.73 ?  16   VAL   A HB   1 
ATOM   405  H  HB   B VAL   A 1 16  ? 14.899 -15.773 6.745   0.50 13.40 ?  16   VAL   A HB   1 
ATOM   406  H  HG11 A VAL   A 1 16  ? 15.275 -14.155 5.140   0.50 14.06 ?  16   VAL   A HG11 1 
ATOM   407  H  HG11 B VAL   A 1 16  ? 15.328 -13.782 5.492   0.50 13.21 ?  16   VAL   A HG11 1 
ATOM   408  H  HG12 A VAL   A 1 16  ? 14.258 -13.990 6.347   0.50 14.06 ?  16   VAL   A HG12 1 
ATOM   409  H  HG12 B VAL   A 1 16  ? 14.384 -13.557 6.748   0.50 13.21 ?  16   VAL   A HG12 1 
ATOM   410  H  HG13 A VAL   A 1 16  ? 15.727 -13.394 6.457   0.50 14.06 ?  16   VAL   A HG13 1 
ATOM   411  H  HG13 B VAL   A 1 16  ? 15.918 -13.147 6.823   0.50 13.21 ?  16   VAL   A HG13 1 
ATOM   412  H  HG21 A VAL   A 1 16  ? 16.867 -15.825 5.067   0.50 14.72 ?  16   VAL   A HG21 1 
ATOM   413  H  HG21 B VAL   A 1 16  ? 16.819 -15.527 5.325   0.50 14.68 ?  16   VAL   A HG21 1 
ATOM   414  H  HG22 A VAL   A 1 16  ? 17.690 -15.271 6.307   0.50 14.72 ?  16   VAL   A HG22 1 
ATOM   415  H  HG22 B VAL   A 1 16  ? 17.662 -15.248 6.642   0.50 14.68 ?  16   VAL   A HG22 1 
ATOM   416  H  HG23 A VAL   A 1 16  ? 17.187 -16.777 6.298   0.50 14.72 ?  16   VAL   A HG23 1 
ATOM   417  H  HG23 B VAL   A 1 16  ? 16.961 -16.655 6.435   0.50 14.68 ?  16   VAL   A HG23 1 
ATOM   418  N  N    A TYR   A 1 17  ? 14.612 -13.575 9.351   0.50 9.80  ?  17   TYR   A N    1 
ATOM   419  N  N    B TYR   A 1 17  ? 14.609 -13.397 9.633   0.50 10.84 ?  17   TYR   A N    1 
ATOM   420  C  CA   A TYR   A 1 17  ? 13.531 -12.905 10.052  0.50 9.89  ?  17   TYR   A CA   1 
ATOM   421  C  CA   B TYR   A 1 17  ? 13.534 -12.714 10.339  0.50 10.67 ?  17   TYR   A CA   1 
ATOM   422  C  C    A TYR   A 1 17  ? 13.258 -11.575 9.351   0.50 9.89  ?  17   TYR   A C    1 
ATOM   423  C  C    B TYR   A 1 17  ? 13.261 -11.383 9.660   0.50 10.88 ?  17   TYR   A C    1 
ATOM   424  O  O    A TYR   A 1 17  ? 14.156 -11.014 8.723   0.50 9.93  ?  17   TYR   A O    1 
ATOM   425  O  O    B TYR   A 1 17  ? 14.166 -10.789 9.075   0.50 11.05 ?  17   TYR   A O    1 
ATOM   426  C  CB   A TYR   A 1 17  ? 13.966 -12.656 11.501  0.50 10.29 ?  17   TYR   A CB   1 
ATOM   427  C  CB   B TYR   A 1 17  ? 13.938 -12.441 11.782  0.50 11.16 ?  17   TYR   A CB   1 
ATOM   428  C  CG   A TYR   A 1 17  ? 14.231 -13.920 12.311  0.50 11.23 ?  17   TYR   A CG   1 
ATOM   429  C  CG   B TYR   A 1 17  ? 14.032 -13.697 12.587  0.50 11.54 ?  17   TYR   A CG   1 
ATOM   430  C  CD1  A TYR   A 1 17  ? 15.438 -14.611 12.222  0.50 11.78 ?  17   TYR   A CD1  1 
ATOM   431  C  CD1  B TYR   A 1 17  ? 15.153 -14.513 12.507  0.50 12.42 ?  17   TYR   A CD1  1 
ATOM   432  C  CD2  A TYR   A 1 17  ? 13.265 -14.420 13.173  0.50 11.62 ?  17   TYR   A CD2  1 
ATOM   433  C  CD2  B TYR   A 1 17  ? 12.988 -14.089 13.406  0.50 11.86 ?  17   TYR   A CD2  1 
ATOM   434  C  CE1  A TYR   A 1 17  ? 15.662 -15.774 12.970  0.50 12.07 ?  17   TYR   A CE1  1 
ATOM   435  C  CE1  B TYR   A 1 17  ? 15.237 -15.685 13.234  0.50 13.09 ?  17   TYR   A CE1  1 
ATOM   436  C  CE2  A TYR   A 1 17  ? 13.478 -15.573 13.921  0.50 11.82 ?  17   TYR   A CE2  1 
ATOM   437  C  CE2  B TYR   A 1 17  ? 13.057 -15.263 14.136  0.50 12.64 ?  17   TYR   A CE2  1 
ATOM   438  C  CZ   A TYR   A 1 17  ? 14.672 -16.245 13.818  0.50 11.70 ?  17   TYR   A CZ   1 
ATOM   439  C  CZ   B TYR   A 1 17  ? 14.188 -16.057 14.049  0.50 12.76 ?  17   TYR   A CZ   1 
ATOM   440  O  OH   A TYR   A 1 17  ? 14.865 -17.388 14.571  0.50 11.92 ?  17   TYR   A OH   1 
ATOM   441  O  OH   B TYR   A 1 17  ? 14.260 -17.224 14.778  0.50 13.33 ?  17   TYR   A OH   1 
ATOM   442  H  H    A TYR   A 1 17  ? 15.305 -13.081 9.251   0.50 11.75 ?  17   TYR   A H    1 
ATOM   443  H  H    B TYR   A 1 17  ? 15.293 -12.877 9.499   0.50 13.01 ?  17   TYR   A H    1 
ATOM   444  H  HA   A TYR   A 1 17  ? 12.739 -13.461 10.037  0.50 11.87 ?  17   TYR   A HA   1 
ATOM   445  H  HA   B TYR   A 1 17  ? 12.727 -13.241 10.325  0.50 12.80 ?  17   TYR   A HA   1 
ATOM   446  H  HB2  A TYR   A 1 17  ? 14.783 -12.136 11.491  0.50 12.35 ?  17   TYR   A HB2  1 
ATOM   447  H  HB2  B TYR   A 1 17  ? 14.808 -12.013 11.793  0.50 13.39 ?  17   TYR   A HB2  1 
ATOM   448  H  HB3  A TYR   A 1 17  ? 13.265 -12.166 11.944  0.50 12.35 ?  17   TYR   A HB3  1 
ATOM   449  H  HB3  B TYR   A 1 17  ? 13.281 -11.865 12.196  0.50 13.39 ?  17   TYR   A HB3  1 
ATOM   450  H  HD1  A TYR   A 1 17  ? 16.106 -14.308 11.654  0.50 14.13 ?  17   TYR   A HD1  1 
ATOM   451  H  HD1  B TYR   A 1 17  ? 15.859 -14.265 11.954  0.50 14.91 ?  17   TYR   A HD1  1 
ATOM   452  H  HD2  A TYR   A 1 17  ? 12.456 -13.981 13.249  0.50 13.95 ?  17   TYR   A HD2  1 
ATOM   453  H  HD2  B TYR   A 1 17  ? 12.226 -13.554 13.465  0.50 14.24 ?  17   TYR   A HD2  1 
ATOM   454  H  HE1  A TYR   A 1 17  ? 16.475 -16.232 12.904  0.50 14.48 ?  17   TYR   A HE1  1 
ATOM   455  H  HE1  B TYR   A 1 17  ? 15.994 -16.221 13.172  0.50 15.71 ?  17   TYR   A HE1  1 
ATOM   456  H  HE2  A TYR   A 1 17  ? 12.816 -15.894 14.495  0.50 14.18 ?  17   TYR   A HE2  1 
ATOM   457  H  HE2  B TYR   A 1 17  ? 12.351 -15.509 14.688  0.50 15.17 ?  17   TYR   A HE2  1 
ATOM   458  H  HH   A TYR   A 1 17  ? 15.630 -17.712 14.426  0.50 14.30 ?  17   TYR   A HH   1 
ATOM   459  H  HH   B TYR   A 1 17  ? 13.495 -17.420 15.069  0.50 16.00 ?  17   TYR   A HH   1 
ATOM   460  N  N    A ILE   A 1 18  ? 12.028 -11.058 9.452   0.50 10.11 ?  18   ILE   A N    1 
ATOM   461  N  N    B ILE   A 1 18  ? 12.025 -10.891 9.755   0.50 10.87 ?  18   ILE   A N    1 
ATOM   462  C  CA   A ILE   A 1 18  ? 11.638 -9.863  8.696   0.50 10.50 ?  18   ILE   A CA   1 
ATOM   463  C  CA   B ILE   A 1 18  ? 11.654 -9.646  9.089   0.50 10.50 ?  18   ILE   A CA   1 
ATOM   464  C  C    A ILE   A 1 18  ? 10.666 -9.004  9.506   0.50 10.71 ?  18   ILE   A C    1 
ATOM   465  C  C    B ILE   A 1 18  ? 10.764 -8.807  9.993   0.50 10.98 ?  18   ILE   A C    1 
ATOM   466  O  O    A ILE   A 1 18  ? 9.832  -9.519  10.254  0.50 10.90 ?  18   ILE   A O    1 
ATOM   467  O  O    B ILE   A 1 18  ? 9.905  -9.333  10.709  0.50 11.42 ?  18   ILE   A O    1 
ATOM   468  C  CB   A ILE   A 1 18  ? 11.084 -10.251 7.300   0.50 10.55 ?  18   ILE   A CB   1 
ATOM   469  C  CB   B ILE   A 1 18  ? 10.993 -9.912  7.723   0.50 9.83  ?  18   ILE   A CB   1 
ATOM   470  C  CG1  A ILE   A 1 18  ? 11.006 -9.026  6.385   0.50 10.67 ?  18   ILE   A CG1  1 
ATOM   471  C  CG1  B ILE   A 1 18  ? 10.883 -8.619  6.917   0.50 10.57 ?  18   ILE   A CG1  1 
ATOM   472  C  CG2  A ILE   A 1 18  ? 9.741  -10.979 7.418   0.50 10.09 ?  18   ILE   A CG2  1 
ATOM   473  C  CG2  B ILE   A 1 18  ? 9.632  -10.563 7.901   0.50 9.82  ?  18   ILE   A CG2  1 
ATOM   474  C  CD1  A ILE   A 1 18  ? 10.766 -9.380  4.937   0.50 11.76 ?  18   ILE   A CD1  1 
ATOM   475  C  CD1  B ILE   A 1 18  ? 10.543 -8.859  5.470   0.50 12.03 ?  18   ILE   A CD1  1 
ATOM   476  H  H    A ILE   A 1 18  ? 11.420 -11.387 9.953   0.50 12.14 ?  18   ILE   A H    1 
ATOM   477  H  H    B ILE   A 1 18  ? 11.388 -11.263 10.201  0.50 13.04 ?  18   ILE   A H    1 
ATOM   478  H  HA   A ILE   A 1 18  ? 12.434 -9.336  8.545   0.50 12.60 ?  18   ILE   A HA   1 
ATOM   479  H  HA   B ILE   A 1 18  ? 12.464 -9.135  8.930   0.50 12.60 ?  18   ILE   A HA   1 
ATOM   480  H  HB   A ILE   A 1 18  ? 11.712 -10.874 6.895   0.50 12.66 ?  18   ILE   A HB   1 
ATOM   481  H  HB   B ILE   A 1 18  ? 11.562 -10.522 7.236   0.50 11.80 ?  18   ILE   A HB   1 
ATOM   482  H  HG12 A ILE   A 1 18  ? 10.278 -8.462  6.675   0.50 12.80 ?  18   ILE   A HG12 1 
ATOM   483  H  HG12 B ILE   A 1 18  ? 10.182 -8.066  7.303   0.50 12.69 ?  18   ILE   A HG12 1 
ATOM   484  H  HG13 A ILE   A 1 18  ? 11.846 -8.546  6.433   0.50 12.80 ?  18   ILE   A HG13 1 
ATOM   485  H  HG13 B ILE   A 1 18  ? 11.730 -8.149  6.954   0.50 12.69 ?  18   ILE   A HG13 1 
ATOM   486  H  HG21 A ILE   A 1 18  ? 9.493  -11.337 6.546   0.50 12.11 ?  18   ILE   A HG21 1 
ATOM   487  H  HG21 B ILE   A 1 18  ? 9.322  -10.879 7.038   0.50 11.78 ?  18   ILE   A HG21 1 
ATOM   488  H  HG22 A ILE   A 1 18  ? 9.830  -11.710 8.052   0.50 12.11 ?  18   ILE   A HG22 1 
ATOM   489  H  HG22 B ILE   A 1 18  ? 9.714  -11.307 8.516   0.50 11.78 ?  18   ILE   A HG22 1 
ATOM   490  H  HG23 A ILE   A 1 18  ? 9.064  -10.358 7.721   0.50 12.11 ?  18   ILE   A HG23 1 
ATOM   491  H  HG23 B ILE   A 1 18  ? 9.008  -9.909  8.256   0.50 11.78 ?  18   ILE   A HG23 1 
ATOM   492  H  HD11 A ILE   A 1 18  ? 10.782 -8.565  4.408   0.50 14.11 ?  18   ILE   A HD11 1 
ATOM   493  H  HD11 B ILE   A 1 18  ? 10.546 -8.012  5.000   0.50 14.44 ?  18   ILE   A HD11 1 
ATOM   494  H  HD12 A ILE   A 1 18  ? 11.463 -9.982  4.636   0.50 14.11 ?  18   ILE   A HD12 1 
ATOM   495  H  HD12 B ILE   A 1 18  ? 11.207 -9.453  5.086   0.50 14.44 ?  18   ILE   A HD12 1 
ATOM   496  H  HD13 A ILE   A 1 18  ? 9.899  -9.808  4.855   0.50 14.11 ?  18   ILE   A HD13 1 
ATOM   497  H  HD13 B ILE   A 1 18  ? 9.664  -9.266  5.414   0.50 14.44 ?  18   ILE   A HD13 1 
ATOM   498  N  N    A LYS   A 1 19  ? 10.761 -7.680  9.328   0.50 10.88 ?  19   LYS   A N    1 
ATOM   499  N  N    B LYS   A 1 19  ? 10.971 -7.491  9.949   0.50 11.58 ?  19   LYS   A N    1 
ATOM   500  C  CA   A LYS   A 1 19  ? 9.947  -6.712  10.064  0.50 11.72 ?  19   LYS   A CA   1 
ATOM   501  C  CA   B LYS   A 1 19  ? 10.203 -6.558  10.757  0.50 12.25 ?  19   LYS   A CA   1 
ATOM   502  C  C    A LYS   A 1 19  ? 9.733  -5.463  9.212   0.50 12.00 ?  19   LYS   A C    1 
ATOM   503  C  C    B LYS   A 1 19  ? 9.878  -5.334  9.923   0.50 12.61 ?  19   LYS   A C    1 
ATOM   504  O  O    A LYS   A 1 19  ? 10.612 -5.066  8.442   0.50 12.12 ?  19   LYS   A O    1 
ATOM   505  O  O    B LYS   A 1 19  ? 10.686 -4.898  9.098   0.50 12.23 ?  19   LYS   A O    1 
ATOM   506  C  CB   A LYS   A 1 19  ? 10.646 -6.317  11.377  0.50 12.20 ?  19   LYS   A CB   1 
ATOM   507  C  CB   B LYS   A 1 19  ? 10.980 -6.141  12.011  0.50 12.89 ?  19   LYS   A CB   1 
ATOM   508  C  CG   A LYS   A 1 19  ? 9.886  -5.371  12.313  0.50 13.25 ?  19   LYS   A CG   1 
ATOM   509  C  CG   B LYS   A 1 19  ? 10.241 -5.240  12.983  0.50 13.62 ?  19   LYS   A CG   1 
ATOM   510  C  CD   A LYS   A 1 19  ? 10.758 -5.036  13.531  0.50 14.14 ?  19   LYS   A CD   1 
ATOM   511  C  CD   B LYS   A 1 19  ? 11.178 -4.868  14.125  0.50 14.42 ?  19   LYS   A CD   1 
ATOM   512  C  CE   A LYS   A 1 19  ? 10.039 -4.171  14.555  0.50 15.07 ?  19   LYS   A CE   1 
ATOM   513  C  CE   B LYS   A 1 19  ? 10.519 -3.988  15.170  0.50 15.05 ?  19   LYS   A CE   1 
ATOM   514  N  NZ   A LYS   A 1 19  ? 10.925 -3.827  15.706  0.50 15.34 ?  19   LYS   A NZ   1 
ATOM   515  N  NZ   B LYS   A 1 19  ? 11.417 -3.856  16.355  0.50 15.26 ?  19   LYS   A NZ   1 
ATOM   516  H  H    A LYS   A 1 19  ? 11.310 -7.320  8.776   0.50 13.06 ?  19   LYS   A H    1 
ATOM   517  H  H    B LYS   A 1 19  ? 11.570 -7.103  9.452   0.50 13.90 ?  19   LYS   A H    1 
ATOM   518  H  HA   A LYS   A 1 19  ? 9.082  -7.112  10.273  0.50 14.06 ?  19   LYS   A HA   1 
ATOM   519  H  HA   B LYS   A 1 19  ? 9.376  -6.967  11.032  0.50 14.70 ?  19   LYS   A HA   1 
ATOM   520  H  HB2  A LYS   A 1 19  ? 10.826 -7.125  11.875  0.50 14.64 ?  19   LYS   A HB2  1 
ATOM   521  H  HB2  B LYS   A 1 19  ? 11.223 -6.939  12.501  0.50 15.46 ?  19   LYS   A HB2  1 
ATOM   522  H  HB3  A LYS   A 1 19  ? 11.481 -5.883  11.147  0.50 14.64 ?  19   LYS   A HB3  1 
ATOM   523  H  HB3  B LYS   A 1 19  ? 11.785 -5.668  11.742  0.50 15.46 ?  19   LYS   A HB3  1 
ATOM   524  H  HG2  A LYS   A 1 19  ? 9.676  -4.546  11.848  0.50 15.90 ?  19   LYS   A HG2  1 
ATOM   525  H  HG2  B LYS   A 1 19  ? 9.961  -4.426  12.537  0.50 16.34 ?  19   LYS   A HG2  1 
ATOM   526  H  HG3  A LYS   A 1 19  ? 9.074  -5.803  12.624  0.50 15.90 ?  19   LYS   A HG3  1 
ATOM   527  H  HG3  B LYS   A 1 19  ? 9.477  -5.710  13.353  0.50 16.34 ?  19   LYS   A HG3  1 
ATOM   528  H  HD2  A LYS   A 1 19  ? 11.020 -5.863  13.970  0.50 16.97 ?  19   LYS   A HD2  1 
ATOM   529  H  HD2  B LYS   A 1 19  ? 11.475 -5.679  14.566  0.50 17.31 ?  19   LYS   A HD2  1 
ATOM   530  H  HD3  A LYS   A 1 19  ? 11.547 -4.556  13.234  0.50 16.97 ?  19   LYS   A HD3  1 
ATOM   531  H  HD3  B LYS   A 1 19  ? 11.941 -4.388  13.765  0.50 17.31 ?  19   LYS   A HD3  1 
ATOM   532  H  HE2  A LYS   A 1 19  ? 9.756  -3.344  14.134  0.50 18.08 ?  19   LYS   A HE2  1 
ATOM   533  H  HE2  B LYS   A 1 19  ? 10.363 -3.103  14.800  0.50 18.06 ?  19   LYS   A HE2  1 
ATOM   534  H  HE3  A LYS   A 1 19  ? 9.270  -4.652  14.900  0.50 18.08 ?  19   LYS   A HE3  1 
ATOM   535  H  HE3  B LYS   A 1 19  ? 9.684  -4.389  15.457  0.50 18.06 ?  19   LYS   A HE3  1 
ATOM   536  H  HZ1  A LYS   A 1 19  ? 10.482 -3.327  16.294  0.50 18.41 ?  19   LYS   A HZ1  1 
ATOM   537  H  HZ1  B LYS   A 1 19  ? 11.032 -3.347  16.975  0.50 18.31 ?  19   LYS   A HZ1  1 
ATOM   538  H  HZ2  A LYS   A 1 19  ? 11.202 -4.571  16.110  0.50 18.41 ?  19   LYS   A HZ2  1 
ATOM   539  H  HZ2  B LYS   A 1 19  ? 11.582 -4.659  16.702  0.50 18.31 ?  19   LYS   A HZ2  1 
ATOM   540  H  HZ3  A LYS   A 1 19  ? 11.636 -3.374  15.419  0.50 18.41 ?  19   LYS   A HZ3  1 
ATOM   541  H  HZ3  B LYS   A 1 19  ? 12.189 -3.483  16.114  0.50 18.31 ?  19   LYS   A HZ3  1 
ATOM   542  N  N    A ASN   A 1 20  ? 8.557  -4.843  9.356   0.50 12.74 ?  20   ASN   A N    1 
ATOM   543  N  N    B ASN   A 1 20  ? 8.686  -4.795  10.138  0.50 14.16 ?  20   ASN   A N    1 
ATOM   544  C  CA   A ASN   A 1 20  ? 8.309  -3.517  8.787   0.50 14.19 ?  20   ASN   A CA   1 
ATOM   545  C  CA   B ASN   A 1 20  ? 8.255  -3.570  9.481   0.50 16.01 ?  20   ASN   A CA   1 
ATOM   546  C  C    A ASN   A 1 20  ? 8.885  -2.512  9.772   0.50 15.27 ?  20   ASN   A C    1 
ATOM   547  C  C    B ASN   A 1 20  ? 8.861  -2.414  10.269  0.50 16.60 ?  20   ASN   A C    1 
ATOM   548  O  O    A ASN   A 1 20  ? 8.317  -2.276  10.839  0.50 16.35 ?  20   ASN   A O    1 
ATOM   549  O  O    B ASN   A 1 20  ? 8.334  -2.015  11.309  0.50 17.35 ?  20   ASN   A O    1 
ATOM   550  C  CB   A ASN   A 1 20  ? 6.815  -3.283  8.565   0.50 15.10 ?  20   ASN   A CB   1 
ATOM   551  C  CB   B ASN   A 1 20  ? 6.731  -3.517  9.485   0.50 17.49 ?  20   ASN   A CB   1 
ATOM   552  C  CG   A ASN   A 1 20  ? 6.477  -1.823  8.233   0.50 16.36 ?  20   ASN   A CG   1 
ATOM   553  C  CG   B ASN   A 1 20  ? 6.164  -2.411  8.608   0.50 18.96 ?  20   ASN   A CG   1 
ATOM   554  O  OD1  A ASN   A 1 20  ? 5.546  -1.243  8.805   0.50 18.21 ?  20   ASN   A OD1  1 
ATOM   555  O  OD1  B ASN   A 1 20  ? 4.979  -2.090  8.700   0.50 20.07 ?  20   ASN   A OD1  1 
ATOM   556  N  ND2  A ASN   A 1 20  ? 7.217  -1.237  7.300   0.50 16.82 ?  20   ASN   A ND2  1 
ATOM   557  N  ND2  B ASN   A 1 20  ? 6.992  -1.830  7.753   0.50 19.36 ?  20   ASN   A ND2  1 
ATOM   558  H  H    A ASN   A 1 20  ? 7.885  -5.167  9.787   0.50 15.29 ?  20   ASN   A H    1 
ATOM   559  H  H    B ASN   A 1 20  ? 8.102  -5.123  10.668  0.50 16.99 ?  20   ASN   A H    1 
ATOM   560  H  HA   A ASN   A 1 20  ? 8.767  -3.433  7.938   0.50 17.02 ?  20   ASN   A HA   1 
ATOM   561  H  HA   B ASN   A 1 20  ? 8.588  -3.566  8.569   0.50 19.21 ?  20   ASN   A HA   1 
ATOM   562  H  HB2  A ASN   A 1 20  ? 6.517  -3.830  7.824   0.50 18.12 ?  20   ASN   A HB2  1 
ATOM   563  H  HB2  B ASN   A 1 20  ? 6.388  -4.365  9.160   0.50 20.99 ?  20   ASN   A HB2  1 
ATOM   564  H  HB3  A ASN   A 1 20  ? 6.336  -3.529  9.372   0.50 18.12 ?  20   ASN   A HB3  1 
ATOM   565  H  HB3  B ASN   A 1 20  ? 6.426  -3.365  10.393  0.50 20.99 ?  20   ASN   A HB3  1 
ATOM   566  H  HD21 A ASN   A 1 20  ? 7.061  -0.419  7.083   0.50 20.18 ?  20   ASN   A HD21 1 
ATOM   567  H  HD21 B ASN   A 1 20  ? 6.699  -1.212  7.244   0.50 23.24 ?  20   ASN   A HD21 1 
ATOM   568  H  HD22 A ASN   A 1 20  ? 7.848  -1.673  6.917   0.50 20.18 ?  20   ASN   A HD22 1 
ATOM   569  H  HD22 B ASN   A 1 20  ? 7.816  -2.069  7.699   0.50 23.24 ?  20   ASN   A HD22 1 
ATOM   570  N  N    A ALA   A 1 21  ? 10.040 -1.942  9.439   0.50 15.58 ?  21   ALA   A N    1 
ATOM   571  N  N    B ALA   A 1 21  ? 9.990  -1.888  9.796   0.50 16.64 ?  21   ALA   A N    1 
ATOM   572  C  CA   A ALA   A 1 21  ? 10.725 -1.071  10.383  0.50 15.39 ?  21   ALA   A CA   1 
ATOM   573  C  CA   B ALA   A 1 21  ? 10.685 -0.831  10.523  0.50 16.57 ?  21   ALA   A CA   1 
ATOM   574  C  C    A ALA   A 1 21  ? 11.665 -0.140  9.639   0.50 15.20 ?  21   ALA   A C    1 
ATOM   575  C  C    B ALA   A 1 21  ? 11.721 -0.173  9.620   0.50 15.82 ?  21   ALA   A C    1 
ATOM   576  O  O    A ALA   A 1 21  ? 12.103 -0.429  8.522   0.50 15.42 ?  21   ALA   A O    1 
ATOM   577  O  O    B ALA   A 1 21  ? 12.166 -0.755  8.627   0.50 15.16 ?  21   ALA   A O    1 
ATOM   578  C  CB   A ALA   A 1 21  ? 11.506 -1.876  11.426  0.50 15.50 ?  21   ALA   A CB   1 
ATOM   579  C  CB   B ALA   A 1 21  ? 11.353 -1.375  11.792  0.50 17.28 ?  21   ALA   A CB   1 
ATOM   580  H  H    A ALA   A 1 21  ? 10.444 -2.041  8.682   0.50 18.70 ?  21   ALA   A H    1 
ATOM   581  H  H    B ALA   A 1 21  ? 10.373 -2.127  9.066   0.50 19.97 ?  21   ALA   A H    1 
ATOM   582  H  HA   A ALA   A 1 21  ? 10.068 -0.528  10.848  0.50 18.47 ?  21   ALA   A HA   1 
ATOM   583  H  HA   B ALA   A 1 21  ? 10.046 -0.155  10.788  0.50 19.88 ?  21   ALA   A HA   1 
ATOM   584  H  HB1  A ALA   A 1 21  ? 11.923 -1.262  12.046  0.50 18.59 ?  21   ALA   A HB1  1 
ATOM   585  H  HB1  B ALA   A 1 21  ? 11.824 -0.653  12.236  0.50 20.73 ?  21   ALA   A HB1  1 
ATOM   586  H  HB2  A ALA   A 1 21  ? 10.887 -2.456  11.899  0.50 18.59 ?  21   ALA   A HB2  1 
ATOM   587  H  HB2  B ALA   A 1 21  ? 10.667 -1.733  12.381  0.50 20.73 ?  21   ALA   A HB2  1 
ATOM   588  H  HB3  A ALA   A 1 21  ? 12.178 -2.407  10.974  0.50 18.59 ?  21   ALA   A HB3  1 
ATOM   589  H  HB3  B ALA   A 1 21  ? 11.977 -2.076  11.548  0.50 20.73 ?  21   ALA   A HB3  1 
ATOM   590  N  N    A ASP   A 1 22  ? 11.955 0.988   10.286  0.50 14.78 ?  22   ASP   A N    1 
ATOM   591  N  N    B ASP   A 1 22  ? 12.075 1.067   9.975   0.50 15.75 ?  22   ASP   A N    1 
ATOM   592  C  CA   A ASP   A 1 22  ? 12.963 1.929   9.819   0.50 13.63 ?  22   ASP   A CA   1 
ATOM   593  C  CA   B ASP   A 1 22  ? 13.219 1.760   9.392   0.50 15.46 ?  22   ASP   A CA   1 
ATOM   594  C  C    A ASP   A 1 22  ? 14.326 1.460   10.316  0.50 12.53 ?  22   ASP   A C    1 
ATOM   595  C  C    B ASP   A 1 22  ? 14.495 1.178   9.995   0.50 13.42 ?  22   ASP   A C    1 
ATOM   596  O  O    A ASP   A 1 22  ? 14.571 1.420   11.526  0.50 13.19 ?  22   ASP   A O    1 
ATOM   597  O  O    B ASP   A 1 22  ? 14.626 1.086   11.219  0.50 13.14 ?  22   ASP   A O    1 
ATOM   598  C  CB   A ASP   A 1 22  ? 12.647 3.312   10.383  0.50 14.47 ?  22   ASP   A CB   1 
ATOM   599  C  CB   B ASP   A 1 22  ? 13.118 3.259   9.710   0.50 17.26 ?  22   ASP   A CB   1 
ATOM   600  C  CG   A ASP   A 1 22  ? 13.596 4.381   9.885   0.50 15.13 ?  22   ASP   A CG   1 
ATOM   601  C  CG   B ASP   A 1 22  ? 14.221 4.105   9.054   0.50 18.43 ?  22   ASP   A CG   1 
ATOM   602  O  OD1  A ASP   A 1 22  ? 14.790 4.094   9.676   0.50 15.72 ?  22   ASP   A OD1  1 
ATOM   603  O  OD1  B ASP   A 1 22  ? 15.197 3.554   8.505   0.50 18.16 ?  22   ASP   A OD1  1 
ATOM   604  O  OD2  A ASP   A 1 22  ? 13.149 5.531   9.718   0.50 15.45 -1 22   ASP   A OD2  1 
ATOM   605  O  OD2  B ASP   A 1 22  ? 14.108 5.350   9.094   0.50 20.01 -1 22   ASP   A OD2  1 
ATOM   606  H  H    A ASP   A 1 22  ? 11.565 1.238   11.014  0.50 17.74 ?  22   ASP   A H    1 
ATOM   607  H  H    B ASP   A 1 22  ? 11.644 1.535   10.557  0.50 18.90 ?  22   ASP   A H    1 
ATOM   608  H  HA   A ASP   A 1 22  ? 12.967 1.968   8.850   0.50 16.36 ?  22   ASP   A HA   1 
ATOM   609  H  HA   B ASP   A 1 22  ? 13.222 1.634   8.430   0.50 18.55 ?  22   ASP   A HA   1 
ATOM   610  H  HB2  A ASP   A 1 22  ? 11.745 3.560   10.133  0.50 17.36 ?  22   ASP   A HB2  1 
ATOM   611  H  HB2  B ASP   A 1 22  ? 12.258 3.584   9.401   0.50 20.71 ?  22   ASP   A HB2  1 
ATOM   612  H  HB3  A ASP   A 1 22  ? 12.732 3.287   11.348  0.50 17.36 ?  22   ASP   A HB3  1 
ATOM   613  H  HB3  B ASP   A 1 22  ? 13.188 3.373   10.671  0.50 20.71 ?  22   ASP   A HB3  1 
ATOM   614  N  N    A ILE   A 1 23  ? 15.217 1.109   9.387   0.50 11.95 ?  23   ILE   A N    1 
ATOM   615  N  N    B ILE   A 1 23  ? 15.428 0.758   9.135   0.50 12.46 ?  23   ILE   A N    1 
ATOM   616  C  CA   A ILE   A 1 23  ? 16.484 0.496   9.780   0.50 11.47 ?  23   ILE   A CA   1 
ATOM   617  C  CA   B ILE   A 1 23  ? 16.660 0.132   9.609   0.50 11.75 ?  23   ILE   A CA   1 
ATOM   618  C  C    A ILE   A 1 23  ? 17.314 1.431   10.651  0.50 11.24 ?  23   ILE   A C    1 
ATOM   619  C  C    B ILE   A 1 23  ? 17.426 1.072   10.528  0.50 11.71 ?  23   ILE   A C    1 
ATOM   620  O  O    A ILE   A 1 23  ? 18.067 0.974   11.519  0.50 11.78 ?  23   ILE   A O    1 
ATOM   621  O  O    B ILE   A 1 23  ? 18.095 0.627   11.470  0.50 11.69 ?  23   ILE   A O    1 
ATOM   622  C  CB   A ILE   A 1 23  ? 17.254 -0.014  8.545   0.50 11.44 ?  23   ILE   A CB   1 
ATOM   623  C  CB   B ILE   A 1 23  ? 17.516 -0.373  8.423   0.50 11.22 ?  23   ILE   A CB   1 
ATOM   624  C  CG1  A ILE   A 1 23  ? 18.410 -0.916  8.980   0.50 11.43 ?  23   ILE   A CG1  1 
ATOM   625  C  CG1  B ILE   A 1 23  ? 18.608 -1.323  8.928   0.50 11.42 ?  23   ILE   A CG1  1 
ATOM   626  C  CG2  A ILE   A 1 23  ? 17.735 1.148   7.686   0.50 11.49 ?  23   ILE   A CG2  1 
ATOM   627  C  CG2  B ILE   A 1 23  ? 18.103 0.796   7.624   0.50 10.91 ?  23   ILE   A CG2  1 
ATOM   628  C  CD1  A ILE   A 1 23  ? 19.106 -1.604  7.829   0.50 12.18 ?  23   ILE   A CD1  1 
ATOM   629  C  CD1  B ILE   A 1 23  ? 19.443 -1.969  7.827   0.50 11.73 ?  23   ILE   A CD1  1 
ATOM   630  H  H    A ILE   A 1 23  ? 15.108 1.208   8.545   0.50 14.34 ?  23   ILE   A H    1 
ATOM   631  H  H    B ILE   A 1 23  ? 15.379 0.819   8.293   0.50 14.95 ?  23   ILE   A H    1 
ATOM   632  H  HA   A ILE   A 1 23  ? 16.282 -0.279  10.325  0.50 13.77 ?  23   ILE   A HA   1 
ATOM   633  H  HA   B ILE   A 1 23  ? 16.416 -0.646  10.130  0.50 14.11 ?  23   ILE   A HA   1 
ATOM   634  H  HB   A ILE   A 1 23  ? 16.644 -0.545  8.016   0.50 13.73 ?  23   ILE   A HB   1 
ATOM   635  H  HB   B ILE   A 1 23  ? 16.939 -0.878  7.829   0.50 13.47 ?  23   ILE   A HB   1 
ATOM   636  H  HG12 A ILE   A 1 23  ? 19.069 -0.381  9.448   0.50 13.72 ?  23   ILE   A HG12 1 
ATOM   637  H  HG12 B ILE   A 1 23  ? 19.213 -0.828  9.500   0.50 13.71 ?  23   ILE   A HG12 1 
ATOM   638  H  HG13 A ILE   A 1 23  ? 18.065 -1.604  9.571   0.50 13.72 ?  23   ILE   A HG13 1 
ATOM   639  H  HG13 B ILE   A 1 23  ? 18.190 -2.037  9.435   0.50 13.71 ?  23   ILE   A HG13 1 
ATOM   640  H  HG21 A ILE   A 1 23  ? 18.070 0.801   6.845   0.50 13.79 ?  23   ILE   A HG21 1 
ATOM   641  H  HG21 B ILE   A 1 23  ? 18.485 0.452   6.798   0.50 13.09 ?  23   ILE   A HG21 1 
ATOM   642  H  HG22 A ILE   A 1 23  ? 16.985 1.746   7.519   0.50 13.79 ?  23   ILE   A HG22 1 
ATOM   643  H  HG22 B ILE   A 1 23  ? 17.395 1.424   7.422   0.50 13.09 ?  23   ILE   A HG22 1 
ATOM   644  H  HG23 A ILE   A 1 23  ? 18.436 1.624   8.154   0.50 13.79 ?  23   ILE   A HG23 1 
ATOM   645  H  HG23 B ILE   A 1 23  ? 18.792 1.226   8.151   0.50 13.09 ?  23   ILE   A HG23 1 
ATOM   646  H  HD11 A ILE   A 1 23  ? 19.768 -2.219  8.183   0.50 14.61 ?  23   ILE   A HD11 1 
ATOM   647  H  HD11 B ILE   A 1 23  ? 20.054 -2.607  8.228   0.50 14.07 ?  23   ILE   A HD11 1 
ATOM   648  H  HD12 A ILE   A 1 23  ? 18.448 -2.090  7.308   0.50 14.61 ?  23   ILE   A HD12 1 
ATOM   649  H  HD12 B ILE   A 1 23  ? 18.849 -2.425  7.209   0.50 14.07 ?  23   ILE   A HD12 1 
ATOM   650  H  HD13 A ILE   A 1 23  ? 19.538 -0.935  7.276   0.50 14.61 ?  23   ILE   A HD13 1 
ATOM   651  H  HD13 B ILE   A 1 23  ? 19.940 -1.280  7.361   0.50 14.07 ?  23   ILE   A HD13 1 
ATOM   652  N  N    A VAL   A 1 24  ? 17.188 2.744   10.450  0.50 11.70 ?  24   VAL   A N    1 
ATOM   653  N  N    B VAL   A 1 24  ? 17.329 2.380   10.286  0.50 12.59 ?  24   VAL   A N    1 
ATOM   654  C  CA   A VAL   A 1 24  ? 17.899 3.694   11.303  0.50 12.94 ?  24   VAL   A CA   1 
ATOM   655  C  CA   B VAL   A 1 24  ? 18.001 3.353   11.142  0.50 13.78 ?  24   VAL   A CA   1 
ATOM   656  C  C    A VAL   A 1 24  ? 17.400 3.596   12.737  0.50 13.93 ?  24   VAL   A C    1 
ATOM   657  C  C    B VAL   A 1 24  ? 17.424 3.310   12.552  0.50 14.56 ?  24   VAL   A C    1 
ATOM   658  O  O    A VAL   A 1 24  ? 18.190 3.501   13.685  0.50 14.14 ?  24   VAL   A O    1 
ATOM   659  O  O    B VAL   A 1 24  ? 18.163 3.304   13.544  0.50 14.68 ?  24   VAL   A O    1 
ATOM   660  C  CB   A VAL   A 1 24  ? 17.759 5.124   10.752  0.50 13.56 ?  24   VAL   A CB   1 
ATOM   661  C  CB   B VAL   A 1 24  ? 17.905 4.757   10.521  0.50 14.72 ?  24   VAL   A CB   1 
ATOM   662  C  CG1  A VAL   A 1 24  ? 18.220 6.150   11.788  0.50 13.77 ?  24   VAL   A CG1  1 
ATOM   663  C  CG1  B VAL   A 1 24  ? 18.460 5.802   11.470  0.50 15.98 ?  24   VAL   A CG1  1 
ATOM   664  C  CG2  A VAL   A 1 24  ? 18.550 5.270   9.467   0.50 14.33 ?  24   VAL   A CG2  1 
ATOM   665  C  CG2  B VAL   A 1 24  ? 18.634 4.782   9.186   0.50 15.00 ?  24   VAL   A CG2  1 
ATOM   666  H  H    A VAL   A 1 24  ? 16.702 3.105   9.840   0.50 14.05 ?  24   VAL   A H    1 
ATOM   667  H  H    B VAL   A 1 24  ? 16.882 2.724   9.641   0.50 15.11 ?  24   VAL   A H    1 
ATOM   668  H  HA   A VAL   A 1 24  ? 18.839 3.472   11.305  0.50 15.53 ?  24   VAL   A HA   1 
ATOM   669  H  HA   B VAL   A 1 24  ? 18.938 3.117   11.206  0.50 16.54 ?  24   VAL   A HA   1 
ATOM   670  H  HB   A VAL   A 1 24  ? 16.825 5.303   10.551  0.50 16.27 ?  24   VAL   A HB   1 
ATOM   671  H  HB   B VAL   A 1 24  ? 16.972 4.962   10.352  0.50 17.67 ?  24   VAL   A HB   1 
ATOM   672  H  HG11 A VAL   A 1 24  ? 18.400 6.990   11.337  0.50 16.52 ?  24   VAL   A HG11 1 
ATOM   673  H  HG11 B VAL   A 1 24  ? 18.616 6.620   10.974  0.50 19.17 ?  24   VAL   A HG11 1 
ATOM   674  H  HG12 A VAL   A 1 24  ? 17.522 6.272   12.447  0.50 16.52 ?  24   VAL   A HG12 1 
ATOM   675  H  HG12 B VAL   A 1 24  ? 17.813 5.962   12.176  0.50 19.17 ?  24   VAL   A HG12 1 
ATOM   676  H  HG13 A VAL   A 1 24  ? 19.030 5.824   12.211  0.50 16.52 ?  24   VAL   A HG13 1 
ATOM   677  H  HG13 B VAL   A 1 24  ? 19.291 5.477   11.845  0.50 19.17 ?  24   VAL   A HG13 1 
ATOM   678  H  HG21 A VAL   A 1 24  ? 18.319 6.113   9.046   0.50 17.20 ?  24   VAL   A HG21 1 
ATOM   679  H  HG21 B VAL   A 1 24  ? 18.536 5.661   8.792   0.50 18.00 ?  24   VAL   A HG21 1 
ATOM   680  H  HG22 A VAL   A 1 24  ? 19.496 5.255   9.676   0.50 17.20 ?  24   VAL   A HG22 1 
ATOM   681  H  HG22 B VAL   A 1 24  ? 19.573 4.591   9.337   0.50 18.00 ?  24   VAL   A HG22 1 
ATOM   682  H  HG23 A VAL   A 1 24  ? 18.328 4.534   8.874   0.50 17.20 ?  24   VAL   A HG23 1 
ATOM   683  H  HG23 B VAL   A 1 24  ? 18.251 4.110   8.598   0.50 18.00 ?  24   VAL   A HG23 1 
ATOM   684  N  N    A GLU   A 1 25  ? 16.077 3.626   12.918  0.50 14.72 ?  25   GLU   A N    1 
ATOM   685  N  N    B GLU   A 1 25  ? 16.093 3.270   12.662  0.50 15.08 ?  25   GLU   A N    1 
ATOM   686  C  CA   A GLU   A 1 25  ? 15.515 3.548   14.262  0.50 15.94 ?  25   GLU   A CA   1 
ATOM   687  C  CA   B GLU   A 1 25  ? 15.461 3.205   13.977  0.50 16.39 ?  25   GLU   A CA   1 
ATOM   688  C  C    A GLU   A 1 25  ? 15.754 2.176   14.879  0.50 15.20 ?  25   GLU   A C    1 
ATOM   689  C  C    B GLU   A 1 25  ? 15.744 1.870   14.657  0.50 15.86 ?  25   GLU   A C    1 
ATOM   690  O  O    A GLU   A 1 25  ? 15.979 2.066   16.090  0.50 15.78 ?  25   GLU   A O    1 
ATOM   691  O  O    B GLU   A 1 25  ? 15.999 1.827   15.866  0.50 16.19 ?  25   GLU   A O    1 
ATOM   692  C  CB   A GLU   A 1 25  ? 14.025 3.887   14.227  0.50 18.27 ?  25   GLU   A CB   1 
ATOM   693  C  CB   B GLU   A 1 25  ? 13.957 3.468   13.857  0.50 18.26 ?  25   GLU   A CB   1 
ATOM   694  C  CG   A GLU   A 1 25  ? 13.749 5.329   13.825  0.50 20.69 ?  25   GLU   A CG   1 
ATOM   695  C  CG   B GLU   A 1 25  ? 13.618 4.864   13.350  0.50 20.80 ?  25   GLU   A CG   1 
ATOM   696  C  CD   A GLU   A 1 25  ? 14.534 6.332   14.655  0.50 22.93 ?  25   GLU   A CD   1 
ATOM   697  C  CD   B GLU   A 1 25  ? 14.181 5.950   14.237  0.50 22.99 ?  25   GLU   A CD   1 
ATOM   698  O  OE1  A GLU   A 1 25  ? 14.588 6.176   15.893  0.50 23.65 ?  25   GLU   A OE1  1 
ATOM   699  O  OE1  B GLU   A 1 25  ? 14.187 5.759   15.472  0.50 24.00 ?  25   GLU   A OE1  1 
ATOM   700  O  OE2  A GLU   A 1 25  ? 15.121 7.262   14.063  0.50 24.00 -1 25   GLU   A OE2  1 
ATOM   701  O  OE2  B GLU   A 1 25  ? 14.624 6.987   13.700  0.50 23.92 -1 25   GLU   A OE2  1 
ATOM   702  H  H    A GLU   A 1 25  ? 15.495 3.699   12.287  0.50 17.66 ?  25   GLU   A H    1 
ATOM   703  H  H    B GLU   A 1 25  ? 15.541 3.270   12.004  0.50 18.10 ?  25   GLU   A H    1 
ATOM   704  H  HA   A GLU   A 1 25  ? 15.955 4.203   14.824  0.50 19.12 ?  25   GLU   A HA   1 
ATOM   705  H  HA   B GLU   A 1 25  ? 15.836 3.896   14.540  0.50 19.67 ?  25   GLU   A HA   1 
ATOM   706  H  HB2  A GLU   A 1 25  ? 13.580 3.312   13.582  0.50 21.92 ?  25   GLU   A HB2  1 
ATOM   707  H  HB2  B GLU   A 1 25  ? 13.571 2.833   13.236  0.50 21.91 ?  25   GLU   A HB2  1 
ATOM   708  H  HB3  A GLU   A 1 25  ? 13.644 3.748   15.108  0.50 21.92 ?  25   GLU   A HB3  1 
ATOM   709  H  HB3  B GLU   A 1 25  ? 13.546 3.366   14.730  0.50 21.91 ?  25   GLU   A HB3  1 
ATOM   710  H  HG2  A GLU   A 1 25  ? 14.011 5.453   12.902  0.50 24.83 ?  25   GLU   A HG2  1 
ATOM   711  H  HG2  B GLU   A 1 25  ? 13.990 4.983   12.463  0.50 24.96 ?  25   GLU   A HG2  1 
ATOM   712  H  HG3  A GLU   A 1 25  ? 12.800 5.509   13.931  0.50 24.83 ?  25   GLU   A HG3  1 
ATOM   713  H  HG3  B GLU   A 1 25  ? 12.655 4.975   13.325  0.50 24.96 ?  25   GLU   A HG3  1 
ATOM   714  N  N    A GLU   A 1 26  ? 15.714 1.121   14.063  0.50 14.80 ?  26   GLU   A N    1 
ATOM   715  N  N    B GLU   A 1 26  ? 15.723 0.772   13.897  0.50 15.67 ?  26   GLU   A N    1 
ATOM   716  C  CA   A GLU   A 1 26  ? 16.027 -0.215  14.564  0.50 14.82 ?  26   GLU   A CA   1 
ATOM   717  C  CA   B GLU   A 1 26  ? 16.091 -0.522  14.464  0.50 15.72 ?  26   GLU   A CA   1 
ATOM   718  C  C    A GLU   A 1 26  ? 17.458 -0.275  15.085  0.50 13.95 ?  26   GLU   A C    1 
ATOM   719  C  C    B GLU   A 1 26  ? 17.517 -0.500  14.988  0.50 14.64 ?  26   GLU   A C    1 
ATOM   720  O  O    A GLU   A 1 26  ? 17.706 -0.722  16.211  0.50 13.73 ?  26   GLU   A O    1 
ATOM   721  O  O    B GLU   A 1 26  ? 17.814 -1.084  16.036  0.50 14.78 ?  26   GLU   A O    1 
ATOM   722  C  CB   A GLU   A 1 26  ? 15.830 -1.248  13.453  0.50 16.34 ?  26   GLU   A CB   1 
ATOM   723  C  CB   B GLU   A 1 26  ? 15.951 -1.617  13.406  0.50 17.37 ?  26   GLU   A CB   1 
ATOM   724  C  CG   A GLU   A 1 26  ? 14.440 -1.833  13.348  0.50 18.66 ?  26   GLU   A CG   1 
ATOM   725  C  CG   B GLU   A 1 26  ? 14.534 -2.053  13.162  0.50 18.98 ?  26   GLU   A CG   1 
ATOM   726  C  CD   A GLU   A 1 26  ? 14.091 -2.709  14.544  0.50 19.78 ?  26   GLU   A CD   1 
ATOM   727  C  CD   B GLU   A 1 26  ? 13.873 -2.575  14.412  0.50 19.82 ?  26   GLU   A CD   1 
ATOM   728  O  OE1  A GLU   A 1 26  ? 14.472 -3.902  14.589  0.50 20.14 ?  26   GLU   A OE1  1 
ATOM   729  O  OE1  B GLU   A 1 26  ? 14.478 -3.446  15.077  0.50 19.64 ?  26   GLU   A OE1  1 
ATOM   730  O  OE2  A GLU   A 1 26  ? 13.449 -2.190  15.463  0.50 19.40 -1 26   GLU   A OE2  1 
ATOM   731  O  OE2  B GLU   A 1 26  ? 12.769 -2.093  14.735  0.50 19.62 -1 26   GLU   A OE2  1 
ATOM   732  H  H    A GLU   A 1 26  ? 15.513 1.159   13.228  0.50 17.76 ?  26   GLU   A H    1 
ATOM   733  H  H    B GLU   A 1 26  ? 15.508 0.749   13.065  0.50 18.81 ?  26   GLU   A H    1 
ATOM   734  H  HA   A GLU   A 1 26  ? 15.428 -0.426  15.294  0.50 17.78 ?  26   GLU   A HA   1 
ATOM   735  H  HA   B GLU   A 1 26  ? 15.509 -0.728  15.208  0.50 18.86 ?  26   GLU   A HA   1 
ATOM   736  H  HB2  A GLU   A 1 26  ? 16.038 -0.829  12.603  0.50 19.61 ?  26   GLU   A HB2  1 
ATOM   737  H  HB2  B GLU   A 1 26  ? 16.309 -1.286  12.564  0.50 20.84 ?  26   GLU   A HB2  1 
ATOM   738  H  HB3  A GLU   A 1 26  ? 16.441 -1.983  13.611  0.50 19.61 ?  26   GLU   A HB3  1 
ATOM   739  H  HB3  B GLU   A 1 26  ? 16.461 -2.396  13.689  0.50 20.84 ?  26   GLU   A HB3  1 
ATOM   740  H  HG2  A GLU   A 1 26  ? 13.797 -1.101  13.276  0.50 22.39 ?  26   GLU   A HG2  1 
ATOM   741  H  HG2  B GLU   A 1 26  ? 14.023 -1.297  12.839  0.50 22.78 ?  26   GLU   A HG2  1 
ATOM   742  H  HG3  A GLU   A 1 26  ? 14.386 -2.388  12.555  0.50 22.39 ?  26   GLU   A HG3  1 
ATOM   743  H  HG3  B GLU   A 1 26  ? 14.527 -2.770  12.515  0.50 22.78 ?  26   GLU   A HG3  1 
ATOM   744  N  N    . ALA   A 1 27  ? 18.418 0.165   14.267  1.00 13.71 ?  27   ALA   A N    1 
ATOM   745  C  CA   . ALA   A 1 27  ? 19.812 0.178   14.695  1.00 13.50 ?  27   ALA   A CA   1 
ATOM   746  C  C    . ALA   A 1 27  ? 19.985 0.986   15.972  1.00 15.06 ?  27   ALA   A C    1 
ATOM   747  O  O    . ALA   A 1 27  ? 20.668 0.549   16.904  1.00 15.22 ?  27   ALA   A O    1 
ATOM   748  C  CB   . ALA   A 1 27  ? 20.706 0.717   13.577  1.00 12.84 ?  27   ALA   A CB   1 
ATOM   749  H  H    A ALA   A 1 27  ? 18.287 0.456   13.467  0.50 16.45 ?  27   ALA   A H    1 
ATOM   750  H  H    B ALA   A 1 27  ? 18.251 0.608   13.547  0.50 16.45 ?  27   ALA   A H    1 
ATOM   751  H  HA   . ALA   A 1 27  ? 20.089 -0.730  14.880  1.00 16.20 ?  27   ALA   A HA   1 
ATOM   752  H  HB1  . ALA   A 1 27  ? 21.628 0.717   13.883  1.00 15.41 ?  27   ALA   A HB1  1 
ATOM   753  H  HB2  . ALA   A 1 27  ? 20.618 0.145   12.798  1.00 15.41 ?  27   ALA   A HB2  1 
ATOM   754  H  HB3  . ALA   A 1 27  ? 20.432 1.620   13.356  1.00 15.41 ?  27   ALA   A HB3  1 
ATOM   755  N  N    A LYS   A 1 28  ? 19.371 2.169   16.045  0.50 16.85 ?  28   LYS   A N    1 
ATOM   756  N  N    B LYS   A 1 28  ? 19.351 2.163   16.038  0.50 16.73 ?  28   LYS   A N    1 
ATOM   757  C  CA   A LYS   A 1 28  ? 19.523 2.980   17.249  0.50 19.53 ?  28   LYS   A CA   1 
ATOM   758  C  CA   B LYS   A 1 28  ? 19.442 2.998   17.232  0.50 19.34 ?  28   LYS   A CA   1 
ATOM   759  C  C    A LYS   A 1 28  ? 18.991 2.254   18.481  0.50 20.35 ?  28   LYS   A C    1 
ATOM   760  C  C    B LYS   A 1 28  ? 18.887 2.288   18.461  0.50 20.49 ?  28   LYS   A C    1 
ATOM   761  O  O    A LYS   A 1 28  ? 19.571 2.362   19.568  0.50 21.30 ?  28   LYS   A O    1 
ATOM   762  O  O    B LYS   A 1 28  ? 19.371 2.513   19.576  0.50 21.58 ?  28   LYS   A O    1 
ATOM   763  C  CB   A LYS   A 1 28  ? 18.869 4.351   17.065  0.50 21.63 ?  28   LYS   A CB   1 
ATOM   764  C  CB   B LYS   A 1 28  ? 18.713 4.326   17.004  0.50 21.04 ?  28   LYS   A CB   1 
ATOM   765  C  CG   A LYS   A 1 28  ? 19.738 5.315   16.267  0.50 23.46 ?  28   LYS   A CG   1 
ATOM   766  C  CG   B LYS   A 1 28  ? 19.379 5.227   15.973  0.50 22.65 ?  28   LYS   A CG   1 
ATOM   767  C  CD   A LYS   A 1 28  ? 19.246 6.748   16.356  0.50 25.34 ?  28   LYS   A CD   1 
ATOM   768  C  CD   B LYS   A 1 28  ? 18.801 6.633   15.988  0.50 24.78 ?  28   LYS   A CD   1 
ATOM   769  C  CE   A LYS   A 1 28  ? 17.990 6.952   15.536  0.50 26.62 ?  28   LYS   A CE   1 
ATOM   770  C  CE   B LYS   A 1 28  ? 17.397 6.669   15.418  0.50 26.42 ?  28   LYS   A CE   1 
ATOM   771  N  NZ   A LYS   A 1 28  ? 17.598 8.387   15.488  0.50 27.41 ?  28   LYS   A NZ   1 
ATOM   772  N  NZ   B LYS   A 1 28  ? 16.854 8.056   15.390  0.50 27.13 ?  28   LYS   A NZ   1 
ATOM   773  H  H    A LYS   A 1 28  ? 18.879 2.516   15.431  0.50 20.22 ?  28   LYS   A H    1 
ATOM   774  H  H    B LYS   A 1 28  ? 18.867 2.495   15.411  0.50 20.08 ?  28   LYS   A H    1 
ATOM   775  H  HA   A LYS   A 1 28  ? 20.465 3.133   17.402  0.50 23.44 ?  28   LYS   A HA   1 
ATOM   776  H  HA   B LYS   A 1 28  ? 20.371 3.200   17.406  0.50 23.20 ?  28   LYS   A HA   1 
ATOM   777  H  HB2  A LYS   A 1 28  ? 18.031 4.244   16.591  0.50 25.95 ?  28   LYS   A HB2  1 
ATOM   778  H  HB2  B LYS   A 1 28  ? 17.813 4.144   16.694  0.50 25.25 ?  28   LYS   A HB2  1 
ATOM   779  H  HB3  A LYS   A 1 28  ? 18.709 4.748   17.937  0.50 25.95 ?  28   LYS   A HB3  1 
ATOM   780  H  HB3  B LYS   A 1 28  ? 18.680 4.816   17.841  0.50 25.25 ?  28   LYS   A HB3  1 
ATOM   781  H  HG2  A LYS   A 1 28  ? 20.645 5.288   16.611  0.50 28.16 ?  28   LYS   A HG2  1 
ATOM   782  H  HG2  B LYS   A 1 28  ? 20.327 5.288   16.167  0.50 27.18 ?  28   LYS   A HG2  1 
ATOM   783  H  HG3  A LYS   A 1 28  ? 19.730 5.052   15.333  0.50 28.16 ?  28   LYS   A HG3  1 
ATOM   784  H  HG3  B LYS   A 1 28  ? 19.243 4.856   15.087  0.50 27.18 ?  28   LYS   A HG3  1 
ATOM   785  H  HD2  A LYS   A 1 28  ? 19.044 6.962   17.281  0.50 30.41 ?  28   LYS   A HD2  1 
ATOM   786  H  HD2  B LYS   A 1 28  ? 18.766 6.954   16.904  0.50 29.74 ?  28   LYS   A HD2  1 
ATOM   787  H  HD3  A LYS   A 1 28  ? 19.931 7.346   16.016  0.50 30.41 ?  28   LYS   A HD3  1 
ATOM   788  H  HD3  B LYS   A 1 28  ? 19.362 7.216   15.452  0.50 29.74 ?  28   LYS   A HD3  1 
ATOM   789  H  HE2  A LYS   A 1 28  ? 18.148 6.648   14.628  0.50 31.95 ?  28   LYS   A HE2  1 
ATOM   790  H  HE2  B LYS   A 1 28  ? 17.413 6.329   14.509  0.50 31.70 ?  28   LYS   A HE2  1 
ATOM   791  H  HE3  A LYS   A 1 28  ? 17.262 6.450   15.936  0.50 31.95 ?  28   LYS   A HE3  1 
ATOM   792  H  HE3  B LYS   A 1 28  ? 16.814 6.125   15.970  0.50 31.70 ?  28   LYS   A HE3  1 
ATOM   793  H  HZ1  A LYS   A 1 28  ? 16.859 8.484   15.002  0.50 32.89 ?  28   LYS   A HZ1  1 
ATOM   794  H  HZ1  B LYS   A 1 28  ? 16.032 8.054   15.052  0.50 32.56 ?  28   LYS   A HZ1  1 
ATOM   795  H  HZ2  A LYS   A 1 28  ? 17.445 8.688   16.311  0.50 32.89 ?  28   LYS   A HZ2  1 
ATOM   796  H  HZ2  B LYS   A 1 28  ? 16.828 8.389   16.215  0.50 32.56 ?  28   LYS   A HZ2  1 
ATOM   797  H  HZ3  A LYS   A 1 28  ? 18.251 8.868   15.121  0.50 32.89 ?  28   LYS   A HZ3  1 
ATOM   798  H  HZ3  B LYS   A 1 28  ? 17.373 8.575   14.886  0.50 32.56 ?  28   LYS   A HZ3  1 
ATOM   799  N  N    A LYS   A 1 29  ? 17.912 1.484   18.327  0.50 20.78 ?  29   LYS   A N    1 
ATOM   800  N  N    B LYS   A 1 29  ? 17.881 1.430   18.282  0.50 21.02 ?  29   LYS   A N    1 
ATOM   801  C  CA   A LYS   A 1 29  ? 17.334 0.775   19.465  0.50 22.47 ?  29   LYS   A CA   1 
ATOM   802  C  CA   B LYS   A 1 29  ? 17.271 0.743   19.415  0.50 22.51 ?  29   LYS   A CA   1 
ATOM   803  C  C    A LYS   A 1 29  ? 18.168 -0.444  19.848  0.50 21.60 ?  29   LYS   A C    1 
ATOM   804  C  C    B LYS   A 1 29  ? 18.087 -0.474  19.837  0.50 21.51 ?  29   LYS   A C    1 
ATOM   805  O  O    A LYS   A 1 29  ? 18.494 -0.637  21.025  0.50 22.52 ?  29   LYS   A O    1 
ATOM   806  O  O    B LYS   A 1 29  ? 18.317 -0.695  21.032  0.50 22.03 ?  29   LYS   A O    1 
ATOM   807  C  CB   A LYS   A 1 29  ? 15.899 0.352   19.140  0.50 25.09 ?  29   LYS   A CB   1 
ATOM   808  C  CB   B LYS   A 1 29  ? 15.848 0.315   19.051  0.50 25.02 ?  29   LYS   A CB   1 
ATOM   809  C  CG   A LYS   A 1 29  ? 15.179 -0.356  20.281  0.50 27.85 ?  29   LYS   A CG   1 
ATOM   810  C  CG   B LYS   A 1 29  ? 15.086 -0.344  20.189  0.50 27.73 ?  29   LYS   A CG   1 
ATOM   811  C  CD   A LYS   A 1 29  ? 14.847 0.605   21.411  0.50 30.32 ?  29   LYS   A CD   1 
ATOM   812  C  CD   B LYS   A 1 29  ? 14.764 0.658   21.286  0.50 30.18 ?  29   LYS   A CD   1 
ATOM   813  C  CE   A LYS   A 1 29  ? 13.989 -0.064  22.472  0.50 32.05 ?  29   LYS   A CE   1 
ATOM   814  C  CE   B LYS   A 1 29  ? 13.963 0.017   22.406  0.50 31.89 ?  29   LYS   A CE   1 
ATOM   815  N  NZ   A LYS   A 1 29  ? 13.508 0.910   23.490  0.50 33.07 ?  29   LYS   A NZ   1 
ATOM   816  N  NZ   B LYS   A 1 29  ? 13.574 1.013   23.442  0.50 32.90 ?  29   LYS   A NZ   1 
ATOM   817  H  H    A LYS   A 1 29  ? 17.504 1.353   17.582  0.50 24.94 ?  29   LYS   A H    1 
ATOM   818  H  H    B LYS   A 1 29  ? 17.537 1.232   17.519  0.50 25.23 ?  29   LYS   A H    1 
ATOM   819  H  HA   A LYS   A 1 29  ? 17.305 1.368   20.229  0.50 26.96 ?  29   LYS   A HA   1 
ATOM   820  H  HA   B LYS   A 1 29  ? 17.223 1.352   20.167  0.50 27.02 ?  29   LYS   A HA   1 
ATOM   821  H  HB2  A LYS   A 1 29  ? 15.384 1.144   18.919  0.50 30.11 ?  29   LYS   A HB2  1 
ATOM   822  H  HB2  B LYS   A 1 29  ? 15.346 1.098   18.779  0.50 30.02 ?  29   LYS   A HB2  1 
ATOM   823  H  HB3  A LYS   A 1 29  ? 15.913 -0.252  18.383  0.50 30.11 ?  29   LYS   A HB3  1 
ATOM   824  H  HB3  B LYS   A 1 29  ? 15.890 -0.320  18.320  0.50 30.02 ?  29   LYS   A HB3  1 
ATOM   825  H  HG2  A LYS   A 1 29  ? 14.348 -0.730  19.950  0.50 33.42 ?  29   LYS   A HG2  1 
ATOM   826  H  HG2  B LYS   A 1 29  ? 14.250 -0.699  19.849  0.50 33.28 ?  29   LYS   A HG2  1 
ATOM   827  H  HG3  A LYS   A 1 29  ? 15.742 -1.062  20.638  0.50 33.42 ?  29   LYS   A HG3  1 
ATOM   828  H  HG3  B LYS   A 1 29  ? 15.620 -1.058  20.573  0.50 33.28 ?  29   LYS   A HG3  1 
ATOM   829  H  HD2  A LYS   A 1 29  ? 15.669 0.906   21.829  0.50 36.38 ?  29   LYS   A HD2  1 
ATOM   830  H  HD2  B LYS   A 1 29  ? 15.591 0.999   21.662  0.50 36.21 ?  29   LYS   A HD2  1 
ATOM   831  H  HD3  A LYS   A 1 29  ? 14.355 1.361   21.054  0.50 36.38 ?  29   LYS   A HD3  1 
ATOM   832  H  HD3  B LYS   A 1 29  ? 14.240 1.384   20.912  0.50 36.21 ?  29   LYS   A HD3  1 
ATOM   833  H  HE2  A LYS   A 1 29  ? 13.215 -0.467  22.049  0.50 38.46 ?  29   LYS   A HE2  1 
ATOM   834  H  HE2  B LYS   A 1 29  ? 13.154 -0.372  22.038  0.50 38.27 ?  29   LYS   A HE2  1 
ATOM   835  H  HE3  A LYS   A 1 29  ? 14.514 -0.742  22.926  0.50 38.46 ?  29   LYS   A HE3  1 
ATOM   836  H  HE3  B LYS   A 1 29  ? 14.501 -0.670  22.832  0.50 38.27 ?  29   LYS   A HE3  1 
ATOM   837  H  HZ1  A LYS   A 1 29  ? 13.009 0.493   24.098  0.50 39.68 ?  29   LYS   A HZ1  1 
ATOM   838  H  HZ1  B LYS   A 1 29  ? 13.106 0.615   24.086  0.50 39.48 ?  29   LYS   A HZ1  1 
ATOM   839  H  HZ2  A LYS   A 1 29  ? 14.201 1.292   23.897  0.50 39.68 ?  29   LYS   A HZ2  1 
ATOM   840  H  HZ2  B LYS   A 1 29  ? 14.301 1.382   23.798  0.50 39.48 ?  29   LYS   A HZ2  1 
ATOM   841  H  HZ3  A LYS   A 1 29  ? 13.019 1.542   23.099  0.50 39.68 ?  29   LYS   A HZ3  1 
ATOM   842  H  HZ3  B LYS   A 1 29  ? 13.074 1.653   23.076  0.50 39.48 ?  29   LYS   A HZ3  1 
ATOM   843  N  N    . VAL   A 1 30  ? 18.509 -1.282  18.869  1.00 20.57 ?  30   VAL   A N    1 
ATOM   844  C  CA   . VAL   A 1 30  ? 19.174 -2.546  19.168  1.00 19.52 ?  30   VAL   A CA   1 
ATOM   845  C  C    . VAL   A 1 30  ? 20.678 -2.385  19.382  1.00 18.12 ?  30   VAL   A C    1 
ATOM   846  O  O    . VAL   A 1 30  ? 21.270 -3.112  20.188  1.00 18.69 ?  30   VAL   A O    1 
ATOM   847  C  CB   . VAL   A 1 30  ? 18.872 -3.533  18.026  1.00 20.10 ?  30   VAL   A CB   1 
ATOM   848  C  CG1  . VAL   A 1 30  ? 19.637 -4.837  18.208  1.00 20.60 ?  30   VAL   A CG1  1 
ATOM   849  C  CG2  . VAL   A 1 30  ? 17.371 -3.797  17.935  1.00 20.94 ?  30   VAL   A CG2  1 
ATOM   850  H  H    A VAL   A 1 30  ? 18.362 -1.148  18.030  0.50 24.69 ?  30   VAL   A H    1 
ATOM   851  H  H    B VAL   A 1 30  ? 18.410 -1.130  18.027  0.50 24.69 ?  30   VAL   A H    1 
ATOM   852  H  HA   . VAL   A 1 30  ? 18.790 -2.915  19.978  1.00 23.43 ?  30   VAL   A HA   1 
ATOM   853  H  HB   . VAL   A 1 30  ? 19.151 -3.143  17.185  1.00 24.12 ?  30   VAL   A HB   1 
ATOM   854  H  HG11 . VAL   A 1 30  ? 19.264 -5.509  17.614  1.00 24.72 ?  30   VAL   A HG11 1 
ATOM   855  H  HG12 . VAL   A 1 30  ? 20.569 -4.690  17.994  1.00 24.72 ?  30   VAL   A HG12 1 
ATOM   856  H  HG13 . VAL   A 1 30  ? 19.546 -5.129  19.129  1.00 24.72 ?  30   VAL   A HG13 1 
ATOM   857  H  HG21 . VAL   A 1 30  ? 17.207 -4.472  17.256  1.00 25.13 ?  30   VAL   A HG21 1 
ATOM   858  H  HG22 . VAL   A 1 30  ? 17.052 -4.112  18.795  1.00 25.13 ?  30   VAL   A HG22 1 
ATOM   859  H  HG23 . VAL   A 1 30  ? 16.919 -2.973  17.695  1.00 25.13 ?  30   VAL   A HG23 1 
ATOM   860  N  N    . LYS   A 1 31  ? 21.312 -1.445  18.687  1.00 17.34 ?  31   LYS   A N    1 
ATOM   861  C  CA   . LYS   A 1 31  ? 22.766 -1.335  18.641  1.00 18.07 ?  31   LYS   A CA   1 
ATOM   862  C  C    . LYS   A 1 31  ? 23.383 -2.694  18.298  1.00 16.26 ?  31   LYS   A C    1 
ATOM   863  O  O    . LYS   A 1 31  ? 24.163 -3.247  19.080  1.00 17.50 ?  31   LYS   A O    1 
ATOM   864  C  CB   . LYS   A 1 31  ? 23.341 -0.779  19.934  1.00 22.62 ?  31   LYS   A CB   1 
ATOM   865  C  CG   . LYS   A 1 31  ? 22.638 0.479   20.419  1.00 28.42 ?  31   LYS   A CG   1 
ATOM   866  C  CD   . LYS   A 1 31  ? 23.629 1.543   20.871  1.00 32.91 ?  31   LYS   A CD   1 
ATOM   867  C  CE   . LYS   A 1 31  ? 22.973 2.554   21.800  1.00 36.04 ?  31   LYS   A CE   1 
ATOM   868  N  NZ   . LYS   A 1 31  ? 21.799 3.232   21.191  1.00 37.62 ?  31   LYS   A NZ   1 
ATOM   869  H  H    . LYS   A 1 31  ? 20.907 -0.839  18.230  1.00 20.81 ?  31   LYS   A H    1 
ATOM   870  H  HA   . LYS   A 1 31  ? 22.994 -0.721  17.930  1.00 21.69 ?  31   LYS   A HA   1 
ATOM   871  H  HB2  . LYS   A 1 31  ? 23.267 -1.454  20.620  1.00 27.14 ?  31   LYS   A HB2  1 
ATOM   872  H  HB3  . LYS   A 1 31  ? 24.276 -0.562  19.787  1.00 27.14 ?  31   LYS   A HB3  1 
ATOM   873  H  HG2  . LYS   A 1 31  ? 22.108 0.847   19.694  1.00 34.11 ?  31   LYS   A HG2  1 
ATOM   874  H  HG3  . LYS   A 1 31  ? 22.068 0.255   21.171  1.00 34.11 ?  31   LYS   A HG3  1 
ATOM   875  H  HD2  . LYS   A 1 31  ? 24.360 1.119   21.347  1.00 39.49 ?  31   LYS   A HD2  1 
ATOM   876  H  HD3  . LYS   A 1 31  ? 23.965 2.018   20.094  1.00 39.49 ?  31   LYS   A HD3  1 
ATOM   877  H  HE2  . LYS   A 1 31  ? 22.658 2.089   22.586  1.00 43.24 ?  31   LYS   A HE2  1 
ATOM   878  H  HE3  . LYS   A 1 31  ? 23.624 3.231   22.051  1.00 43.24 ?  31   LYS   A HE3  1 
ATOM   879  H  HZ1  . LYS   A 1 31  ? 21.454 3.818   21.766  1.00 45.15 ?  31   LYS   A HZ1  1 
ATOM   880  H  HZ2  . LYS   A 1 31  ? 22.046 3.662   20.453  1.00 45.15 ?  31   LYS   A HZ2  1 
ATOM   881  H  HZ3  . LYS   A 1 31  ? 21.176 2.631   20.983  1.00 45.15 ?  31   LYS   A HZ3  1 
ATOM   882  N  N    . PRO   A 1 32  ? 23.048 -3.249  17.140  1.00 14.21 ?  32   PRO   A N    1 
ATOM   883  C  CA   . PRO   A 1 32  ? 23.530 -4.584  16.786  1.00 14.46 ?  32   PRO   A CA   1 
ATOM   884  C  C    . PRO   A 1 32  ? 25.031 -4.590  16.575  1.00 14.35 ?  32   PRO   A C    1 
ATOM   885  O  O    . PRO   A 1 32  ? 25.664 -3.558  16.343  1.00 14.44 ?  32   PRO   A O    1 
ATOM   886  C  CB   . PRO   A 1 32  ? 22.801 -4.878  15.471  1.00 14.92 ?  32   PRO   A CB   1 
ATOM   887  C  CG   . PRO   A 1 32  ? 22.616 -3.515  14.861  1.00 13.90 ?  32   PRO   A CG   1 
ATOM   888  C  CD   . PRO   A 1 32  ? 22.308 -2.623  16.033  1.00 13.79 ?  32   PRO   A CD   1 
ATOM   889  H  HA   . PRO   A 1 32  ? 23.282 -5.237  17.453  1.00 17.36 ?  32   PRO   A HA   1 
ATOM   890  H  HB2  . PRO   A 1 32  ? 23.351 -5.443  14.898  1.00 17.91 ?  32   PRO   A HB2  1 
ATOM   891  H  HB3  . PRO   A 1 32  ? 21.945 -5.301  15.647  1.00 17.91 ?  32   PRO   A HB3  1 
ATOM   892  H  HG2  . PRO   A 1 32  ? 23.432 -3.243  14.416  1.00 16.68 ?  32   PRO   A HG2  1 
ATOM   893  H  HG3  . PRO   A 1 32  ? 21.873 -3.538  14.232  1.00 16.68 ?  32   PRO   A HG3  1 
ATOM   894  H  HD2  . PRO   A 1 32  ? 22.640 -1.729  15.852  1.00 16.55 ?  32   PRO   A HD2  1 
ATOM   895  H  HD3  . PRO   A 1 32  ? 21.356 -2.624  16.204  1.00 16.55 ?  32   PRO   A HD3  1 
ATOM   896  N  N    . THR   A 1 33  ? 25.597 -5.792  16.630  1.00 14.34 ?  33   THR   A N    1 
ATOM   897  C  CA   . THR   A 1 33  ? 27.006 -5.948  16.299  1.00 14.54 ?  33   THR   A CA   1 
ATOM   898  C  C    . THR   A 1 33  ? 27.287 -5.492  14.873  1.00 13.24 ?  33   THR   A C    1 
ATOM   899  O  O    . THR   A 1 33  ? 28.315 -4.851  14.613  1.00 13.62 ?  33   THR   A O    1 
ATOM   900  C  CB   . THR   A 1 33  ? 27.417 -7.403  16.503  1.00 16.26 ?  33   THR   A CB   1 
ATOM   901  O  OG1  . THR   A 1 33  ? 27.122 -7.782  17.850  1.00 18.02 ?  33   THR   A OG1  1 
ATOM   902  C  CG2  . THR   A 1 33  ? 28.908 -7.593  16.239  1.00 17.48 ?  33   THR   A CG2  1 
ATOM   903  H  H    . THR   A 1 33  ? 25.196 -6.518  16.854  1.00 17.21 ?  33   THR   A H    1 
ATOM   904  H  HA   . THR   A 1 33  ? 27.538 -5.404  16.900  1.00 17.45 ?  33   THR   A HA   1 
ATOM   905  H  HB   . THR   A 1 33  ? 26.925 -7.979  15.893  1.00 19.51 ?  33   THR   A HB   1 
ATOM   906  H  HG1  . THR   A 1 33  ? 27.562 -7.303  18.389  1.00 21.63 ?  33   THR   A HG1  1 
ATOM   907  H  HG21 . THR   A 1 33  ? 29.187 -8.480  16.519  1.00 20.97 ?  33   THR   A HG21 1 
ATOM   908  H  HG22 . THR   A 1 33  ? 29.095 -7.491  15.293  1.00 20.97 ?  33   THR   A HG22 1 
ATOM   909  H  HG23 . THR   A 1 33  ? 29.417 -6.934  16.736  1.00 20.97 ?  33   THR   A HG23 1 
ATOM   910  N  N    . VAL   A 1 34  ? 26.388 -5.812  13.939  1.00 11.92 ?  34   VAL   A N    1 
ATOM   911  C  CA   . VAL   A 1 34  ? 26.571 -5.479  12.529  1.00 11.36 ?  34   VAL   A CA   1 
ATOM   912  C  C    . VAL   A 1 34  ? 25.267 -4.925  11.969  1.00 10.59 ?  34   VAL   A C    1 
ATOM   913  O  O    . VAL   A 1 34  ? 24.231 -5.599  12.023  1.00 11.22 ?  34   VAL   A O    1 
ATOM   914  C  CB   . VAL   A 1 34  ? 27.017 -6.688  11.684  1.00 11.82 ?  34   VAL   A CB   1 
ATOM   915  C  CG1  . VAL   A 1 34  ? 27.180 -6.285  10.224  1.00 11.90 ?  34   VAL   A CG1  1 
ATOM   916  C  CG2  . VAL   A 1 34  ? 28.306 -7.289  12.224  1.00 12.98 ?  34   VAL   A CG2  1 
ATOM   917  H  H    . VAL   A 1 34  ? 25.658 -6.240  14.102  1.00 14.31 ?  34   VAL   A H    1 
ATOM   918  H  HA   . VAL   A 1 34  ? 27.245 -4.788  12.449  1.00 13.64 ?  34   VAL   A HA   1 
ATOM   919  H  HB   . VAL   A 1 34  ? 26.328 -7.369  11.727  1.00 14.18 ?  34   VAL   A HB   1 
ATOM   920  H  HG11 . VAL   A 1 34  ? 27.678 -6.977  9.763   1.00 14.28 ?  34   VAL   A HG11 1 
ATOM   921  H  HG12 . VAL   A 1 34  ? 26.305 -6.182  9.820   1.00 14.28 ?  34   VAL   A HG12 1 
ATOM   922  H  HG13 . VAL   A 1 34  ? 27.667 -5.446  10.182  1.00 14.28 ?  34   VAL   A HG13 1 
ATOM   923  H  HG21 . VAL   A 1 34  ? 28.574 -8.026  11.654  1.00 15.57 ?  34   VAL   A HG21 1 
ATOM   924  H  HG22 . VAL   A 1 34  ? 28.996 -6.606  12.229  1.00 15.57 ?  34   VAL   A HG22 1 
ATOM   925  H  HG23 . VAL   A 1 34  ? 28.153 -7.609  13.128  1.00 15.57 ?  34   VAL   A HG23 1 
ATOM   926  N  N    . VAL   A 1 35  ? 25.322 -3.719  11.407  1.00 9.82  ?  35   VAL   A N    1 
ATOM   927  C  CA   . VAL   A 1 35  ? 24.277 -3.210  10.528  1.00 9.57  ?  35   VAL   A CA   1 
ATOM   928  C  C    . VAL   A 1 35  ? 24.825 -3.212  9.111   1.00 8.90  ?  35   VAL   A C    1 
ATOM   929  O  O    . VAL   A 1 35  ? 25.970 -2.808  8.876   1.00 9.51  ?  35   VAL   A O    1 
ATOM   930  C  CB   . VAL   A 1 35  ? 23.748 -1.816  10.940  1.00 10.21 ?  35   VAL   A CB   1 
ATOM   931  C  CG1  . VAL   A 1 35  ? 24.813 -0.718  10.805  1.00 11.06 ?  35   VAL   A CG1  1 
ATOM   932  C  CG2  . VAL   A 1 35  ? 22.497 -1.463  10.130  1.00 11.14 ?  35   VAL   A CG2  1 
ATOM   933  H  H    . VAL   A 1 35  ? 25.967 -3.163  11.521  1.00 11.78 ?  35   VAL   A H    1 
ATOM   934  H  HA   . VAL   A 1 35  ? 23.518 -3.819  10.557  1.00 11.49 ?  35   VAL   A HA   1 
ATOM   935  H  HB   . VAL   A 1 35  ? 23.479 -1.843  11.869  1.00 12.25 ?  35   VAL   A HB   1 
ATOM   936  H  HG11 . VAL   A 1 35  ? 24.468 0.115   11.173  1.00 13.27 ?  35   VAL   A HG11 1 
ATOM   937  H  HG12 . VAL   A 1 35  ? 25.608 -0.986  11.293  1.00 13.27 ?  35   VAL   A HG12 1 
ATOM   938  H  HG13 . VAL   A 1 35  ? 25.032 -0.591  9.866   1.00 13.27 ?  35   VAL   A HG13 1 
ATOM   939  H  HG21 . VAL   A 1 35  ? 22.145 -0.610  10.435  1.00 13.36 ?  35   VAL   A HG21 1 
ATOM   940  H  HG22 . VAL   A 1 35  ? 22.733 -1.398  9.187   1.00 13.36 ?  35   VAL   A HG22 1 
ATOM   941  H  HG23 . VAL   A 1 35  ? 21.830 -2.156  10.253  1.00 13.36 ?  35   VAL   A HG23 1 
ATOM   942  N  N    . VAL   A 1 36  ? 24.006 -3.672  8.167   1.00 8.55  ?  36   VAL   A N    1 
ATOM   943  C  CA   . VAL   A 1 36  ? 24.378 -3.682  6.762   1.00 8.44  ?  36   VAL   A CA   1 
ATOM   944  C  C    . VAL   A 1 36  ? 23.913 -2.395  6.097   1.00 8.49  ?  36   VAL   A C    1 
ATOM   945  O  O    . VAL   A 1 36  ? 22.751 -1.986  6.243   1.00 9.14  ?  36   VAL   A O    1 
ATOM   946  C  CB   . VAL   A 1 36  ? 23.778 -4.901  6.044   1.00 8.78  ?  36   VAL   A CB   1 
ATOM   947  C  CG1  . VAL   A 1 36  ? 24.029 -4.829  4.555   1.00 8.91  ?  36   VAL   A CG1  1 
ATOM   948  C  CG2  . VAL   A 1 36  ? 24.337 -6.192  6.619   1.00 9.51  ?  36   VAL   A CG2  1 
ATOM   949  H  H    . VAL   A 1 36  ? 23.216 -3.993  8.324   1.00 10.27 ?  36   VAL   A H    1 
ATOM   950  H  HA   . VAL   A 1 36  ? 25.348 -3.736  6.693   1.00 10.13 ?  36   VAL   A HA   1 
ATOM   951  H  HB   . VAL   A 1 36  ? 22.821 -4.904  6.186   1.00 10.54 ?  36   VAL   A HB   1 
ATOM   952  H  HG11 . VAL   A 1 36  ? 23.890 -5.709  4.171   1.00 10.69 ?  36   VAL   A HG11 1 
ATOM   953  H  HG12 . VAL   A 1 36  ? 23.410 -4.196  4.160   1.00 10.69 ?  36   VAL   A HG12 1 
ATOM   954  H  HG13 . VAL   A 1 36  ? 24.943 -4.543  4.403   1.00 10.69 ?  36   VAL   A HG13 1 
ATOM   955  H  HG21 . VAL   A 1 36  ? 23.946 -6.948  6.146   1.00 11.41 ?  36   VAL   A HG21 1 
ATOM   956  H  HG22 . VAL   A 1 36  ? 25.302 -6.203  6.507   1.00 11.41 ?  36   VAL   A HG22 1 
ATOM   957  H  HG23 . VAL   A 1 36  ? 24.116 -6.249  7.563   1.00 11.41 ?  36   VAL   A HG23 1 
ATOM   958  N  N    A ASN   A 1 37  ? 24.821 -1.755  5.365   0.50 8.44  ?  37   ASN   A N    1 
ATOM   959  N  N    B ASN   A 1 37  ? 24.809 -1.777  5.332   0.50 8.08  ?  37   ASN   A N    1 
ATOM   960  C  CA   A ASN   A 1 37  ? 24.491 -0.611  4.532   0.50 8.46  ?  37   ASN   A CA   1 
ATOM   961  C  CA   B ASN   A 1 37  ? 24.457 -0.679  4.447   0.50 7.70  ?  37   ASN   A CA   1 
ATOM   962  C  C    A ASN   A 1 37  ? 24.309 -1.054  3.087   0.50 8.13  ?  37   ASN   A C    1 
ATOM   963  C  C    B ASN   A 1 37  ? 24.345 -1.174  3.012   0.50 7.74  ?  37   ASN   A C    1 
ATOM   964  O  O    A ASN   A 1 37  ? 25.026 -1.933  2.598   0.50 8.77  ?  37   ASN   A O    1 
ATOM   965  O  O    B ASN   A 1 37  ? 25.177 -1.957  2.541   0.50 8.37  ?  37   ASN   A O    1 
ATOM   966  C  CB   A ASN   A 1 37  ? 25.596 0.441   4.598   0.50 8.67  ?  37   ASN   A CB   1 
ATOM   967  C  CB   B ASN   A 1 37  ? 25.512 0.422   4.509   0.50 7.83  ?  37   ASN   A CB   1 
ATOM   968  C  CG   A ASN   A 1 37  ? 25.245 1.685   3.819   0.50 8.54  ?  37   ASN   A CG   1 
ATOM   969  C  CG   B ASN   A 1 37  ? 25.183 1.586   3.595   0.50 7.93  ?  37   ASN   A CG   1 
ATOM   970  O  OD1  A ASN   A 1 37  ? 24.067 2.022   3.683   0.50 8.63  ?  37   ASN   A OD1  1 
ATOM   971  O  OD1  B ASN   A 1 37  ? 24.011 1.901   3.368   0.50 8.14  ?  37   ASN   A OD1  1 
ATOM   972  N  ND2  A ASN   A 1 37  ? 26.258 2.377   3.305   0.50 8.22  ?  37   ASN   A ND2  1 
ATOM   973  N  ND2  B ASN   A 1 37  ? 26.212 2.226   3.064   0.50 8.35  ?  37   ASN   A ND2  1 
ATOM   974  H  H    A ASN   A 1 37  ? 25.657 -1.972  5.337   0.50 10.12 ?  37   ASN   A H    1 
ATOM   975  H  H    B ASN   A 1 37  ? 25.649 -1.984  5.315   0.50 9.70  ?  37   ASN   A H    1 
ATOM   976  H  HA   A ASN   A 1 37  ? 23.666 -0.212  4.841   0.50 10.15 ?  37   ASN   A HA   1 
ATOM   977  H  HA   B ASN   A 1 37  ? 23.606 -0.311  4.720   0.50 9.23  ?  37   ASN   A HA   1 
ATOM   978  H  HB2  A ASN   A 1 37  ? 25.731 0.700   5.524   0.50 10.41 ?  37   ASN   A HB2  1 
ATOM   979  H  HB2  B ASN   A 1 37  ? 25.568 0.754   5.421   0.50 9.40  ?  37   ASN   A HB2  1 
ATOM   980  H  HB3  A ASN   A 1 37  ? 26.418 0.071   4.234   0.50 10.41 ?  37   ASN   A HB3  1 
ATOM   981  H  HB3  B ASN   A 1 37  ? 26.370 0.054   4.239   0.50 9.40  ?  37   ASN   A HB3  1 
ATOM   982  H  HD21 A ASN   A 1 37  ? 26.108 3.091   2.847   0.50 9.87  ?  37   ASN   A HD21 1 
ATOM   983  H  HD21 B ASN   A 1 37  ? 26.076 2.887   2.538   0.50 10.02 ?  37   ASN   A HD21 1 
ATOM   984  H  HD22 A ASN   A 1 37  ? 27.065 2.117   3.421   0.50 9.87  ?  37   ASN   A HD22 1 
ATOM   985  H  HD22 B ASN   A 1 37  ? 27.012 1.975   3.242   0.50 10.02 ?  37   ASN   A HD22 1 
ATOM   986  N  N    A ALA   A 1 38  ? 23.326 -0.448  2.417   0.50 8.55  ?  38   ALA   A N    1 
ATOM   987  N  N    B ALA   A 1 38  ? 23.297 -0.715  2.325   0.50 7.94  ?  38   ALA   A N    1 
ATOM   988  C  CA   A ALA   A 1 38  ? 23.108 -0.615  0.979   0.50 7.98  ?  38   ALA   A CA   1 
ATOM   989  C  CA   B ALA   A 1 38  ? 23.114 -0.936  0.892   0.50 8.71  ?  38   ALA   A CA   1 
ATOM   990  C  C    A ALA   A 1 38  ? 24.034 0.357   0.244   0.50 7.64  ?  38   ALA   A C    1 
ATOM   991  C  C    B ALA   A 1 38  ? 23.938 0.117   0.153   0.50 8.73  ?  38   ALA   A C    1 
ATOM   992  O  O    A ALA   A 1 38  ? 23.647 1.452   -0.171  0.50 7.87  ?  38   ALA   A O    1 
ATOM   993  O  O    B ALA   A 1 38  ? 23.445 1.163   -0.275  0.50 8.86  ?  38   ALA   A O    1 
ATOM   994  C  CB   A ALA   A 1 38  ? 21.642 -0.369  0.639   0.50 7.90  ?  38   ALA   A CB   1 
ATOM   995  C  CB   B ALA   A 1 38  ? 21.637 -0.856  0.532   0.50 9.75  ?  38   ALA   A CB   1 
ATOM   996  H  H    A ALA   A 1 38  ? 22.763 0.081   2.789   0.50 10.26 ?  38   ALA   A H    1 
ATOM   997  H  H    B ALA   A 1 38  ? 22.676 -0.243  2.682   0.50 9.52  ?  38   ALA   A H    1 
ATOM   998  H  HA   A ALA   A 1 38  ? 23.341 -1.515  0.717   0.50 9.58  ?  38   ALA   A HA   1 
ATOM   999  H  HA   B ALA   A 1 38  ? 23.452 -1.813  0.655   0.50 10.45 ?  38   ALA   A HA   1 
ATOM   1000 H  HB1  A ALA   A 1 38  ? 21.510 -0.500  -0.311  0.50 9.48  ?  38   ALA   A HB1  1 
ATOM   1001 H  HB1  B ALA   A 1 38  ? 21.543 -0.985  -0.423  0.50 11.69 ?  38   ALA   A HB1  1 
ATOM   1002 H  HB2  A ALA   A 1 38  ? 21.093 -0.995  1.140   0.50 9.48  ?  38   ALA   A HB2  1 
ATOM   1003 H  HB2  B ALA   A 1 38  ? 21.160 -1.552  1.011   0.50 11.69 ?  38   ALA   A HB2  1 
ATOM   1004 H  HB3  A ALA   A 1 38  ? 21.407 0.541   0.885   0.50 9.48  ?  38   ALA   A HB3  1 
ATOM   1005 H  HB3  B ALA   A 1 38  ? 21.299 0.015   0.786   0.50 11.69 ?  38   ALA   A HB3  1 
ATOM   1006 N  N    A ALA   A 1 39  ? 25.288 -0.062  0.091   0.50 7.77  ?  39   ALA   A N    1 
ATOM   1007 N  N    B ALA   A 1 39  ? 25.227 -0.169  0.015   0.50 9.79  ?  39   ALA   A N    1 
ATOM   1008 C  CA   A ALA   A 1 39  ? 26.373 0.789   -0.373  0.50 7.94  ?  39   ALA   A CA   1 
ATOM   1009 C  CA   B ALA   A 1 39  ? 26.190 0.801   -0.478  0.50 9.84  ?  39   ALA   A CA   1 
ATOM   1010 C  C    A ALA   A 1 39  ? 26.510 0.752   -1.892  0.50 8.13  ?  39   ALA   A C    1 
ATOM   1011 C  C    B ALA   A 1 39  ? 26.324 0.724   -1.997  0.50 9.31  ?  39   ALA   A C    1 
ATOM   1012 O  O    A ALA   A 1 39  ? 26.019 -0.154  -2.569  0.50 8.25  ?  39   ALA   A O    1 
ATOM   1013 O  O    B ALA   A 1 39  ? 25.871 -0.222  -2.647  0.50 9.92  ?  39   ALA   A O    1 
ATOM   1014 C  CB   A ALA   A 1 39  ? 27.684 0.323   0.261   0.50 8.51  ?  39   ALA   A CB   1 
ATOM   1015 C  CB   B ALA   A 1 39  ? 27.547 0.556   0.182   0.50 10.29 ?  39   ALA   A CB   1 
ATOM   1016 H  H    A ALA   A 1 39  ? 25.541 -0.868  0.259   0.50 9.32  ?  39   ALA   A H    1 
ATOM   1017 H  H    B ALA   A 1 39  ? 25.570 -0.937  0.200   0.50 11.75 ?  39   ALA   A H    1 
ATOM   1018 H  HA   A ALA   A 1 39  ? 26.207 1.706   -0.105  0.50 9.53  ?  39   ALA   A HA   1 
ATOM   1019 H  HA   B ALA   A 1 39  ? 25.893 1.693   -0.237  0.50 11.80 ?  39   ALA   A HA   1 
ATOM   1020 H  HB1  A ALA   A 1 39  ? 28.404 0.891   -0.049  0.50 10.21 ?  39   ALA   A HB1  1 
ATOM   1021 H  HB1  B ALA   A 1 39  ? 28.179 1.210   -0.150  0.50 12.34 ?  39   ALA   A HB1  1 
ATOM   1022 H  HB2  A ALA   A 1 39  ? 27.603 0.389   1.228   0.50 10.21 ?  39   ALA   A HB2  1 
ATOM   1023 H  HB2  B ALA   A 1 39  ? 27.451 0.647   1.145   0.50 12.34 ?  39   ALA   A HB2  1 
ATOM   1024 H  HB3  A ALA   A 1 39  ? 27.849 -0.596  0.005   0.50 10.21 ?  39   ALA   A HB3  1 
ATOM   1025 H  HB3  B ALA   A 1 39  ? 27.845 -0.340  -0.036  0.50 12.34 ?  39   ALA   A HB3  1 
ATOM   1026 N  N    A ASN   A 1 40  ? 27.216 1.752   -2.423  0.50 8.55  ?  40   ASN   A N    1 
ATOM   1027 N  N    B ASN   A 1 40  ? 26.961 1.746   -2.565  0.50 8.92  ?  40   ASN   A N    1 
ATOM   1028 C  CA   A ASN   A 1 40  ? 27.751 1.715   -3.779  0.50 8.65  ?  40   ASN   A CA   1 
ATOM   1029 C  CA   B ASN   A 1 40  ? 27.444 1.705   -3.937  0.50 8.77  ?  40   ASN   A CA   1 
ATOM   1030 C  C    A ASN   A 1 40  ? 29.275 1.615   -3.724  0.50 7.79  ?  40   ASN   A C    1 
ATOM   1031 C  C    B ASN   A 1 40  ? 28.967 1.603   -3.935  0.50 8.31  ?  40   ASN   A C    1 
ATOM   1032 O  O    A ASN   A 1 40  ? 29.886 1.727   -2.657  0.50 8.10  ?  40   ASN   A O    1 
ATOM   1033 O  O    B ASN   A 1 40  ? 29.613 1.693   -2.889  0.50 8.54  ?  40   ASN   A O    1 
ATOM   1034 C  CB   A ASN   A 1 40  ? 27.258 2.902   -4.630  0.50 9.60  ?  40   ASN   A CB   1 
ATOM   1035 C  CB   B ASN   A 1 40  ? 26.934 2.905   -4.750  0.50 9.55  ?  40   ASN   A CB   1 
ATOM   1036 C  CG   A ASN   A 1 40  ? 27.664 4.255   -4.072  0.50 10.78 ?  40   ASN   A CG   1 
ATOM   1037 C  CG   B ASN   A 1 40  ? 27.317 4.241   -4.146  0.50 9.78  ?  40   ASN   A CG   1 
ATOM   1038 O  OD1  A ASN   A 1 40  ? 28.828 4.482   -3.728  0.50 11.05 ?  40   ASN   A OD1  1 
ATOM   1039 O  OD1  B ASN   A 1 40  ? 28.499 4.567   -4.018  0.50 10.64 ?  40   ASN   A OD1  1 
ATOM   1040 N  ND2  A ASN   A 1 40  ? 26.697 5.175   -4.002  0.50 11.88 ?  40   ASN   A ND2  1 
ATOM   1041 N  ND2  B ASN   A 1 40  ? 26.312 5.039   -3.808  0.50 10.05 ?  40   ASN   A ND2  1 
ATOM   1042 H  H    A ASN   A 1 40  ? 27.414 2.473   -2.003  0.50 10.26 ?  40   ASN   A H    1 
ATOM   1043 H  H    B ASN   A 1 40  ? 27.131 2.485   -2.163  0.50 10.70 ?  40   ASN   A H    1 
ATOM   1044 H  HA   A ASN   A 1 40  ? 27.436 0.908   -4.212  0.50 10.38 ?  40   ASN   A HA   1 
ATOM   1045 H  HA   B ASN   A 1 40  ? 27.102 0.897   -4.358  0.50 10.53 ?  40   ASN   A HA   1 
ATOM   1046 H  HB2  A ASN   A 1 40  ? 27.622 2.819   -5.530  0.50 11.52 ?  40   ASN   A HB2  1 
ATOM   1047 H  HB2  B ASN   A 1 40  ? 27.304 2.854   -5.640  0.50 11.46 ?  40   ASN   A HB2  1 
ATOM   1048 H  HB3  A ASN   A 1 40  ? 26.288 2.873   -4.671  0.50 11.52 ?  40   ASN   A HB3  1 
ATOM   1049 H  HB3  B ASN   A 1 40  ? 25.962 2.856   -4.789  0.50 11.46 ?  40   ASN   A HB3  1 
ATOM   1050 H  HD21 A ASN   A 1 40  ? 26.870 5.964   -3.706  0.50 14.26 ?  40   ASN   A HD21 1 
ATOM   1051 H  HD21 B ASN   A 1 40  ? 26.479 5.807   -3.463  0.50 12.05 ?  40   ASN   A HD21 1 
ATOM   1052 H  HD22 A ASN   A 1 40  ? 25.896 4.977   -4.250  0.50 14.26 ?  40   ASN   A HD22 1 
ATOM   1053 H  HD22 B ASN   A 1 40  ? 25.499 4.786   -3.927  0.50 12.05 ?  40   ASN   A HD22 1 
ATOM   1054 N  N    A VAL   A 1 41  ? 29.892 1.369   -4.885  0.50 7.68  ?  41   VAL   A N    1 
ATOM   1055 N  N    B VAL   A 1 41  ? 29.541 1.391   -5.122  0.50 9.15  ?  41   VAL   A N    1 
ATOM   1056 C  CA   A VAL   A 1 41  ? 31.320 1.060   -4.911  0.50 7.93  ?  41   VAL   A CA   1 
ATOM   1057 C  CA   B VAL   A 1 41  ? 30.967 1.076   -5.214  0.50 9.73  ?  41   VAL   A CA   1 
ATOM   1058 C  C    A VAL   A 1 41  ? 32.179 2.219   -4.436  0.50 8.30  ?  41   VAL   A C    1 
ATOM   1059 C  C    B VAL   A 1 41  ? 31.836 2.219   -4.711  0.50 9.10  ?  41   VAL   A C    1 
ATOM   1060 O  O    A VAL   A 1 41  ? 33.320 1.998   -4.009  0.50 8.66  ?  41   VAL   A O    1 
ATOM   1061 O  O    B VAL   A 1 41  ? 32.983 1.996   -4.304  0.50 9.40  ?  41   VAL   A O    1 
ATOM   1062 C  CB   A VAL   A 1 41  ? 31.798 0.551   -6.294  0.50 7.95  ?  41   VAL   A CB   1 
ATOM   1063 C  CB   B VAL   A 1 41  ? 31.362 0.663   -6.648  0.50 10.71 ?  41   VAL   A CB   1 
ATOM   1064 C  CG1  A VAL   A 1 41  ? 31.095 -0.751  -6.664  0.50 8.33  ?  41   VAL   A CG1  1 
ATOM   1065 C  CG1  B VAL   A 1 41  ? 30.668 -0.630  -7.040  0.50 11.30 ?  41   VAL   A CG1  1 
ATOM   1066 C  CG2  A VAL   A 1 41  ? 31.631 1.601   -7.390  0.50 7.95  ?  41   VAL   A CG2  1 
ATOM   1067 C  CG2  B VAL   A 1 41  ? 31.050 1.773   -7.643  0.50 11.65 ?  41   VAL   A CG2  1 
ATOM   1068 H  H    A VAL   A 1 41  ? 29.517 1.371   -5.658  0.50 9.22  ?  41   VAL   A H    1 
ATOM   1069 H  H    B VAL   A 1 41  ? 29.129 1.417   -5.874  0.50 10.98 ?  41   VAL   A H    1 
ATOM   1070 H  HA   A VAL   A 1 41  ? 31.478 0.338   -4.290  0.50 9.52  ?  41   VAL   A HA   1 
ATOM   1071 H  HA   B VAL   A 1 41  ? 31.145 0.315   -4.642  0.50 11.68 ?  41   VAL   A HA   1 
ATOM   1072 H  HB   A VAL   A 1 41  ? 32.749 0.355   -6.234  0.50 9.54  ?  41   VAL   A HB   1 
ATOM   1073 H  HB   B VAL   A 1 41  ? 32.318 0.501   -6.674  0.50 12.85 ?  41   VAL   A HB   1 
ATOM   1074 H  HG11 A VAL   A 1 41  ? 31.429 -1.068  -7.517  0.50 10.00 ?  41   VAL   A HG11 1 
ATOM   1075 H  HG11 B VAL   A 1 41  ? 30.867 -0.829  -7.968  0.50 13.56 ?  41   VAL   A HG11 1 
ATOM   1076 H  HG12 A VAL   A 1 41  ? 31.270 -1.415  -5.975  0.50 10.00 ?  41   VAL   A HG12 1 
ATOM   1077 H  HG12 B VAL   A 1 41  ? 30.994 -1.349  -6.473  0.50 13.56 ?  41   VAL   A HG12 1 
ATOM   1078 H  HG13 A VAL   A 1 41  ? 30.138 -0.589  -6.724  0.50 10.00 ?  41   VAL   A HG13 1 
ATOM   1079 H  HG13 B VAL   A 1 41  ? 29.712 -0.530  -6.921  0.50 13.56 ?  41   VAL   A HG13 1 
ATOM   1080 H  HG21 A VAL   A 1 41  ? 31.893 1.208   -8.241  0.50 9.54  ?  41   VAL   A HG21 1 
ATOM   1081 H  HG21 B VAL   A 1 41  ? 31.323 1.485   -8.528  0.50 13.98 ?  41   VAL   A HG21 1 
ATOM   1082 H  HG22 A VAL   A 1 41  ? 30.705 1.874   -7.423  0.50 9.54  ?  41   VAL   A HG22 1 
ATOM   1083 H  HG22 B VAL   A 1 41  ? 30.094 1.946   -7.635  0.50 13.98 ?  41   VAL   A HG22 1 
ATOM   1084 H  HG23 A VAL   A 1 41  ? 32.199 2.359   -7.190  0.50 9.54  ?  41   VAL   A HG23 1 
ATOM   1085 H  HG23 B VAL   A 1 41  ? 31.534 2.571   -7.390  0.50 13.98 ?  41   VAL   A HG23 1 
ATOM   1086 N  N    A TYR   A 1 42  ? 31.674 3.451   -4.513  0.50 8.46  ?  42   TYR   A N    1 
ATOM   1087 N  N    B TYR   A 1 42  ? 31.331 3.451   -4.756  0.50 8.86  ?  42   TYR   A N    1 
ATOM   1088 C  CA   A TYR   A 1 42  ? 32.414 4.630   -4.080  0.50 8.66  ?  42   TYR   A CA   1 
ATOM   1089 C  CA   B TYR   A 1 42  ? 32.089 4.628   -4.347  0.50 8.92  ?  42   TYR   A CA   1 
ATOM   1090 C  C    A TYR   A 1 42  ? 32.119 5.010   -2.638  0.50 8.79  ?  42   TYR   A C    1 
ATOM   1091 C  C    B TYR   A 1 42  ? 31.866 4.998   -2.889  0.50 8.85  ?  42   TYR   A C    1 
ATOM   1092 O  O    A TYR   A 1 42  ? 32.683 5.991   -2.138  0.50 9.40  ?  42   TYR   A O    1 
ATOM   1093 O  O    B TYR   A 1 42  ? 32.442 5.984   -2.419  0.50 9.71  ?  42   TYR   A O    1 
ATOM   1094 C  CB   A TYR   A 1 42  ? 32.124 5.821   -5.013  0.50 9.49  ?  42   TYR   A CB   1 
ATOM   1095 C  CB   B TYR   A 1 42  ? 31.728 5.826   -5.237  0.50 9.43  ?  42   TYR   A CB   1 
ATOM   1096 C  CG   A TYR   A 1 42  ? 32.300 5.490   -6.484  0.50 9.93  ?  42   TYR   A CG   1 
ATOM   1097 C  CG   B TYR   A 1 42  ? 31.891 5.533   -6.707  0.50 10.33 ?  42   TYR   A CG   1 
ATOM   1098 C  CD1  A TYR   A 1 42  ? 33.564 5.296   -7.024  0.50 10.63 ?  42   TYR   A CD1  1 
ATOM   1099 C  CD1  B TYR   A 1 42  ? 33.146 5.335   -7.256  0.50 10.55 ?  42   TYR   A CD1  1 
ATOM   1100 C  CD2  A TYR   A 1 42  ? 31.204 5.355   -7.329  0.50 10.80 ?  42   TYR   A CD2  1 
ATOM   1101 C  CD2  B TYR   A 1 42  ? 30.789 5.441   -7.544  0.50 11.81 ?  42   TYR   A CD2  1 
ATOM   1102 C  CE1  A TYR   A 1 42  ? 33.735 4.981   -8.362  0.50 10.91 ?  42   TYR   A CE1  1 
ATOM   1103 C  CE1  B TYR   A 1 42  ? 33.303 5.052   -8.598  0.50 11.24 ?  42   TYR   A CE1  1 
ATOM   1104 C  CE2  A TYR   A 1 42  ? 31.366 5.045   -8.672  0.50 11.58 ?  42   TYR   A CE2  1 
ATOM   1105 C  CE2  B TYR   A 1 42  ? 30.933 5.168   -8.891  0.50 12.54 ?  42   TYR   A CE2  1 
ATOM   1106 C  CZ   A TYR   A 1 42  ? 32.637 4.860   -9.183  0.50 11.49 ?  42   TYR   A CZ   1 
ATOM   1107 C  CZ   B TYR   A 1 42  ? 32.193 4.973   -9.414  0.50 11.91 ?  42   TYR   A CZ   1 
ATOM   1108 O  OH   A TYR   A 1 42  ? 32.813 4.547   -10.513 0.50 12.73 ?  42   TYR   A OH   1 
ATOM   1109 O  OH   B TYR   A 1 42  ? 32.339 4.704   -10.754 0.50 12.51 ?  42   TYR   A OH   1 
ATOM   1110 H  H    A TYR   A 1 42  ? 30.893 3.633   -4.819  0.50 10.15 ?  42   TYR   A H    1 
ATOM   1111 H  H    B TYR   A 1 42  ? 30.537 3.636   -5.033  0.50 10.63 ?  42   TYR   A H    1 
ATOM   1112 H  HA   A TYR   A 1 42  ? 33.364 4.444   -4.142  0.50 10.39 ?  42   TYR   A HA   1 
ATOM   1113 H  HA   B TYR   A 1 42  ? 33.033 4.454   -4.468  0.50 10.70 ?  42   TYR   A HA   1 
ATOM   1114 H  HB2  A TYR   A 1 42  ? 31.209 6.111   -4.881  0.50 11.39 ?  42   TYR   A HB2  1 
ATOM   1115 H  HB2  B TYR   A 1 42  ? 30.804 6.074   -5.085  0.50 11.31 ?  42   TYR   A HB2  1 
ATOM   1116 H  HB3  A TYR   A 1 42  ? 32.733 6.549   -4.795  0.50 11.39 ?  42   TYR   A HB3  1 
ATOM   1117 H  HB3  B TYR   A 1 42  ? 32.311 6.574   -5.018  0.50 11.31 ?  42   TYR   A HB3  1 
ATOM   1118 H  HD1  A TYR   A 1 42  ? 34.315 5.379   -6.480  0.50 12.76 ?  42   TYR   A HD1  1 
ATOM   1119 H  HD1  B TYR   A 1 42  ? 33.898 5.386   -6.709  0.50 12.66 ?  42   TYR   A HD1  1 
ATOM   1120 H  HD2  A TYR   A 1 42  ? 30.348 5.483   -6.990  0.50 12.96 ?  42   TYR   A HD2  1 
ATOM   1121 H  HD2  B TYR   A 1 42  ? 29.937 5.575   -7.195  0.50 14.18 ?  42   TYR   A HD2  1 
ATOM   1122 H  HE1  A TYR   A 1 42  ? 34.589 4.860   -8.713  0.50 13.09 ?  42   TYR   A HE1  1 
ATOM   1123 H  HE1  B TYR   A 1 42  ? 34.157 4.923   -8.948  0.50 13.49 ?  42   TYR   A HE1  1 
ATOM   1124 H  HE2  A TYR   A 1 42  ? 30.620 4.964   -9.226  0.50 13.90 ?  42   TYR   A HE2  1 
ATOM   1125 H  HE2  B TYR   A 1 42  ? 30.185 5.111   -9.442  0.50 15.05 ?  42   TYR   A HE2  1 
ATOM   1126 H  HH   A TYR   A 1 42  ? 33.625 4.414   -10.674 0.50 15.28 ?  42   TYR   A HH   1 
ATOM   1127 H  HH   B TYR   A 1 42  ? 31.590 4.683   -11.126 0.50 15.01 ?  42   TYR   A HH   1 
ATOM   1128 N  N    A LEU   A 1 43  ? 31.260 4.250   -1.961  0.50 8.86  ?  43   LEU   A N    1 
ATOM   1129 N  N    B LEU   A 1 43  ? 31.044 4.234   -2.173  0.50 8.92  ?  43   LEU   A N    1 
ATOM   1130 C  CA   A LEU   A 1 43  ? 30.805 4.580   -0.611  0.50 8.63  ?  43   LEU   A CA   1 
ATOM   1131 C  CA   B LEU   A 1 43  ? 30.628 4.571   -0.812  0.50 8.96  ?  43   LEU   A CA   1 
ATOM   1132 C  C    A LEU   A 1 43  ? 30.337 6.031   -0.517  0.50 8.74  ?  43   LEU   A C    1 
ATOM   1133 C  C    B LEU   A 1 43  ? 30.133 6.013   -0.707  0.50 8.87  ?  43   LEU   A C    1 
ATOM   1134 O  O    A LEU   A 1 43  ? 30.618 6.735   0.456   0.50 9.98  ?  43   LEU   A O    1 
ATOM   1135 O  O    B LEU   A 1 43  ? 30.378 6.706   0.281   0.50 9.43  ?  43   LEU   A O    1 
ATOM   1136 C  CB   A LEU   A 1 43  ? 31.858 4.265   0.451   0.50 9.12  ?  43   LEU   A CB   1 
ATOM   1137 C  CB   B LEU   A 1 43  ? 31.710 4.268   0.227   0.50 9.32  ?  43   LEU   A CB   1 
ATOM   1138 C  CG   A LEU   A 1 43  ? 32.398 2.831   0.495   0.50 9.50  ?  43   LEU   A CG   1 
ATOM   1139 C  CG   B LEU   A 1 43  ? 32.145 2.801   0.359   0.50 9.45  ?  43   LEU   A CG   1 
ATOM   1140 C  CD1  A LEU   A 1 43  ? 33.457 2.733   1.573   0.50 10.38 ?  43   LEU   A CD1  1 
ATOM   1141 C  CD1  B LEU   A 1 43  ? 33.206 2.662   1.442   0.50 9.99  ?  43   LEU   A CD1  1 
ATOM   1142 C  CD2  A LEU   A 1 43  ? 31.291 1.813   0.733   0.50 9.36  ?  43   LEU   A CD2  1 
ATOM   1143 C  CD2  B LEU   A 1 43  ? 30.961 1.882   0.642   0.50 9.29  ?  43   LEU   A CD2  1 
ATOM   1144 H  H    A LEU   A 1 43  ? 30.914 3.520   -2.268  0.50 10.63 ?  43   LEU   A H    1 
ATOM   1145 H  H    B LEU   A 1 43  ? 30.710 3.494   -2.458  0.50 10.71 ?  43   LEU   A H    1 
ATOM   1146 H  HA   A LEU   A 1 43  ? 30.037 4.016   -0.415  0.50 10.36 ?  43   LEU   A HA   1 
ATOM   1147 H  HA   B LEU   A 1 43  ? 29.868 4.008   -0.594  0.50 10.76 ?  43   LEU   A HA   1 
ATOM   1148 H  HB2  A LEU   A 1 43  ? 32.615 4.853   0.314   0.50 10.94 ?  43   LEU   A HB2  1 
ATOM   1149 H  HB2  B LEU   A 1 43  ? 32.498 4.783   0.005   0.50 11.18 ?  43   LEU   A HB2  1 
ATOM   1150 H  HB3  A LEU   A 1 43  ? 31.465 4.442   1.321   0.50 10.94 ?  43   LEU   A HB3  1 
ATOM   1151 H  HB3  B LEU   A 1 43  ? 31.378 4.545   1.097   0.50 11.18 ?  43   LEU   A HB3  1 
ATOM   1152 H  HG   A LEU   A 1 43  ? 32.816 2.624   -0.355  0.50 11.40 ?  43   LEU   A HG   1 
ATOM   1153 H  HG   B LEU   A 1 43  ? 32.544 2.519   -0.477  0.50 11.35 ?  43   LEU   A HG   1 
ATOM   1154 H  HD11 A LEU   A 1 43  ? 33.797 1.825   1.599   0.50 12.46 ?  43   LEU   A HD11 1 
ATOM   1155 H  HD11 B LEU   A 1 43  ? 33.472 1.731   1.509   0.50 11.98 ?  43   LEU   A HD11 1 
ATOM   1156 H  HD12 A LEU   A 1 43  ? 34.175 3.351   1.366   0.50 12.46 ?  43   LEU   A HD12 1 
ATOM   1157 H  HD12 B LEU   A 1 43  ? 33.974 3.208   1.206   0.50 11.98 ?  43   LEU   A HD12 1 
ATOM   1158 H  HD13 A LEU   A 1 43  ? 33.058 2.963   2.427   0.50 12.46 ?  43   LEU   A HD13 1 
ATOM   1159 H  HD13 B LEU   A 1 43  ? 32.838 2.961   2.289   0.50 11.98 ?  43   LEU   A HD13 1 
ATOM   1160 H  HD21 A LEU   A 1 43  ? 31.686 0.933   0.823   0.50 11.24 ?  43   LEU   A HD21 1 
ATOM   1161 H  HD21 B LEU   A 1 43  ? 31.292 0.999   0.865   0.50 11.14 ?  43   LEU   A HD21 1 
ATOM   1162 H  HD22 A LEU   A 1 43  ? 30.818 2.050   1.548   0.50 11.24 ?  43   LEU   A HD22 1 
ATOM   1163 H  HD22 B LEU   A 1 43  ? 30.452 2.243   1.385   0.50 11.14 ?  43   LEU   A HD22 1 
ATOM   1164 H  HD23 A LEU   A 1 43  ? 30.681 1.830   -0.020  0.50 11.24 ?  43   LEU   A HD23 1 
ATOM   1165 H  HD23 B LEU   A 1 43  ? 30.403 1.837   -0.150  0.50 11.14 ?  43   LEU   A HD23 1 
ATOM   1166 N  N    A LYS   A 1 44  ? 29.618 6.482   -1.547  0.50 8.71  ?  44   LYS   A N    1 
ATOM   1167 N  N    B LYS   A 1 44  ? 29.390 6.452   -1.723  0.50 8.86  ?  44   LYS   A N    1 
ATOM   1168 C  CA   A LYS   A 1 44  ? 28.976 7.794   -1.540  0.50 9.32  ?  44   LYS   A CA   1 
ATOM   1169 C  CA   B LYS   A 1 44  ? 28.724 7.756   -1.707  0.50 9.40  ?  44   LYS   A CA   1 
ATOM   1170 C  C    A LYS   A 1 44  ? 27.537 7.606   -1.071  0.50 8.67  ?  44   LYS   A C    1 
ATOM   1171 C  C    B LYS   A 1 44  ? 27.322 7.546   -1.150  0.50 9.12  ?  44   LYS   A C    1 
ATOM   1172 O  O    A LYS   A 1 44  ? 26.696 7.079   -1.806  0.50 9.97  ?  44   LYS   A O    1 
ATOM   1173 O  O    B LYS   A 1 44  ? 26.422 7.080   -1.852  0.50 9.51  ?  44   LYS   A O    1 
ATOM   1174 C  CB   A LYS   A 1 44  ? 29.039 8.438   -2.921  0.50 10.93 ?  44   LYS   A CB   1 
ATOM   1175 C  CB   B LYS   A 1 44  ? 28.690 8.365   -3.105  0.50 11.69 ?  44   LYS   A CB   1 
ATOM   1176 C  CG   A LYS   A 1 44  ? 30.438 8.861   -3.343  0.50 13.35 ?  44   LYS   A CG   1 
ATOM   1177 C  CG   B LYS   A 1 44  ? 30.030 8.905   -3.590  0.50 14.83 ?  44   LYS   A CG   1 
ATOM   1178 C  CD   A LYS   A 1 44  ? 31.110 9.767   -2.315  0.50 18.28 ?  44   LYS   A CD   1 
ATOM   1179 C  CD   B LYS   A 1 44  ? 30.688 9.808   -2.549  0.50 19.21 ?  44   LYS   A CD   1 
ATOM   1180 C  CE   A LYS   A 1 44  ? 32.373 10.394  -2.876  0.50 21.50 ?  44   LYS   A CE   1 
ATOM   1181 C  CE   B LYS   A 1 44  ? 32.063 10.261  -2.997  0.50 21.82 ?  44   LYS   A CE   1 
ATOM   1182 N  NZ   A LYS   A 1 44  ? 33.146 11.115  -1.834  0.50 23.27 ?  44   LYS   A NZ   1 
ATOM   1183 N  NZ   B LYS   A 1 44  ? 32.922 10.687  -1.853  0.50 22.58 ?  44   LYS   A NZ   1 
ATOM   1184 H  H    A LYS   A 1 44  ? 29.499 6.043   -2.280  0.50 10.46 ?  44   LYS   A H    1 
ATOM   1185 H  H    B LYS   A 1 44  ? 29.253 6.005   -2.444  0.50 10.64 ?  44   LYS   A H    1 
ATOM   1186 H  HA   A LYS   A 1 44  ? 29.425 8.369   -0.900  0.50 11.18 ?  44   LYS   A HA   1 
ATOM   1187 H  HA   B LYS   A 1 44  ? 29.184 8.350   -1.095  0.50 11.28 ?  44   LYS   A HA   1 
ATOM   1188 H  HB2  A LYS   A 1 44  ? 28.712 7.807   -3.578  0.50 13.12 ?  44   LYS   A HB2  1 
ATOM   1189 H  HB2  B LYS   A 1 44  ? 28.405 7.686   -3.736  0.50 14.03 ?  44   LYS   A HB2  1 
ATOM   1190 H  HB3  A LYS   A 1 44  ? 28.481 9.233   -2.921  0.50 13.12 ?  44   LYS   A HB3  1 
ATOM   1191 H  HB3  B LYS   A 1 44  ? 28.060 9.103   -3.111  0.50 14.03 ?  44   LYS   A HB3  1 
ATOM   1192 H  HG2  A LYS   A 1 44  ? 30.991 8.071   -3.452  0.50 16.02 ?  44   LYS   A HG2  1 
ATOM   1193 H  HG2  B LYS   A 1 44  ? 30.627 8.166   -3.777  0.50 17.80 ?  44   LYS   A HG2  1 
ATOM   1194 H  HG3  A LYS   A 1 44  ? 30.387 9.349   -4.181  0.50 16.02 ?  44   LYS   A HG3  1 
ATOM   1195 H  HG3  B LYS   A 1 44  ? 29.889 9.432   -4.399  0.50 17.80 ?  44   LYS   A HG3  1 
ATOM   1196 H  HD2  A LYS   A 1 44  ? 30.490 10.473  -2.065  0.50 21.94 ?  44   LYS   A HD2  1 
ATOM   1197 H  HD2  B LYS   A 1 44  ? 30.129 10.586  -2.397  0.50 23.05 ?  44   LYS   A HD2  1 
ATOM   1198 H  HD3  A LYS   A 1 44  ? 31.347 9.238   -1.536  0.50 21.94 ?  44   LYS   A HD3  1 
ATOM   1199 H  HD3  B LYS   A 1 44  ? 30.816 9.318   -1.722  0.50 23.05 ?  44   LYS   A HD3  1 
ATOM   1200 H  HE2  A LYS   A 1 44  ? 32.932 9.692   -3.245  0.50 25.80 ?  44   LYS   A HE2  1 
ATOM   1201 H  HE2  B LYS   A 1 44  ? 32.510 9.526   -3.445  0.50 26.19 ?  44   LYS   A HE2  1 
ATOM   1202 H  HE3  A LYS   A 1 44  ? 32.126 11.025  -3.570  0.50 25.80 ?  44   LYS   A HE3  1 
ATOM   1203 H  HE3  B LYS   A 1 44  ? 31.969 11.013  -3.598  0.50 26.19 ?  44   LYS   A HE3  1 
ATOM   1204 H  HZ1  A LYS   A 1 44  ? 33.909 11.411  -2.179  0.50 27.93 ?  44   LYS   A HZ1  1 
ATOM   1205 H  HZ1  B LYS   A 1 44  ? 33.720 10.949  -2.152  0.50 27.09 ?  44   LYS   A HZ1  1 
ATOM   1206 H  HZ2  A LYS   A 1 44  ? 32.675 11.807  -1.531  0.50 27.93 ?  44   LYS   A HZ2  1 
ATOM   1207 H  HZ2  B LYS   A 1 44  ? 32.540 11.369  -1.423  0.50 27.09 ?  44   LYS   A HZ2  1 
ATOM   1208 H  HZ3  A LYS   A 1 44  ? 33.326 10.567  -1.157  0.50 27.93 ?  44   LYS   A HZ3  1 
ATOM   1209 H  HZ3  B LYS   A 1 44  ? 33.033 10.014  -1.283  0.50 27.09 ?  44   LYS   A HZ3  1 
ATOM   1210 N  N    A HIS   A 1 45  ? 27.259 8.030   0.155   0.50 8.17  ?  45   HIS   A N    1 
ATOM   1211 N  N    B HIS   A 1 45  ? 27.141 7.881   0.127   0.50 9.31  ?  45   HIS   A N    1 
ATOM   1212 C  CA   A HIS   A 1 45  ? 26.034 7.642   0.849   0.50 8.20  ?  45   HIS   A CA   1 
ATOM   1213 C  CA   B HIS   A 1 45  ? 25.898 7.586   0.839   0.50 9.72  ?  45   HIS   A CA   1 
ATOM   1214 C  C    A HIS   A 1 45  ? 24.963 8.724   0.695   0.50 9.05  ?  45   HIS   A C    1 
ATOM   1215 C  C    B HIS   A 1 45  ? 24.931 8.753   0.665   0.50 10.20 ?  45   HIS   A C    1 
ATOM   1216 O  O    A HIS   A 1 45  ? 24.547 9.376   1.652   0.50 9.23  ?  45   HIS   A O    1 
ATOM   1217 O  O    B HIS   A 1 45  ? 24.795 9.628   1.523   0.50 11.00 ?  45   HIS   A O    1 
ATOM   1218 C  CB   A HIS   A 1 45  ? 26.345 7.367   2.311   0.50 7.94  ?  45   HIS   A CB   1 
ATOM   1219 C  CB   B HIS   A 1 45  ? 26.191 7.332   2.307   0.50 9.93  ?  45   HIS   A CB   1 
ATOM   1220 C  CG   A HIS   A 1 45  ? 27.451 6.381   2.517   0.50 8.22  ?  45   HIS   A CG   1 
ATOM   1221 C  CG   B HIS   A 1 45  ? 27.336 6.403   2.539   0.50 9.23  ?  45   HIS   A CG   1 
ATOM   1222 N  ND1  A HIS   A 1 45  ? 27.415 5.094   2.016   0.50 8.86  ?  45   HIS   A ND1  1 
ATOM   1223 N  ND1  B HIS   A 1 45  ? 27.362 5.112   2.050   0.50 9.40  ?  45   HIS   A ND1  1 
ATOM   1224 C  CD2  A HIS   A 1 45  ? 28.627 6.502   3.178   0.50 8.84  ?  45   HIS   A CD2  1 
ATOM   1225 C  CD2  B HIS   A 1 45  ? 28.497 6.584   3.211   0.50 8.89  ?  45   HIS   A CD2  1 
ATOM   1226 C  CE1  A HIS   A 1 45  ? 28.527 4.471   2.363   0.50 8.99  ?  45   HIS   A CE1  1 
ATOM   1227 C  CE1  B HIS   A 1 45  ? 28.497 4.543   2.416   0.50 8.77  ?  45   HIS   A CE1  1 
ATOM   1228 N  NE2  A HIS   A 1 45  ? 29.278 5.300   3.070   0.50 9.15  ?  45   HIS   A NE2  1 
ATOM   1229 N  NE2  B HIS   A 1 45  ? 29.202 5.411   3.124   0.50 8.64  ?  45   HIS   A NE2  1 
ATOM   1230 H  H    A HIS   A 1 45  ? 27.768 8.554   0.612   0.50 9.80  ?  45   HIS   A H    1 
ATOM   1231 H  H    B HIS   A 1 45  ? 27.730 8.288   0.608   0.50 11.17 ?  45   HIS   A H    1 
ATOM   1232 H  HA   A HIS   A 1 45  ? 25.692 6.829   0.455   0.50 9.84  ?  45   HIS   A HA   1 
ATOM   1233 H  HA   B HIS   A 1 45  ? 25.494 6.789   0.463   0.50 11.66 ?  45   HIS   A HA   1 
ATOM   1234 H  HB2  A HIS   A 1 45  ? 26.600 8.199   2.742   0.50 9.52  ?  45   HIS   A HB2  1 
ATOM   1235 H  HB2  B HIS   A 1 45  ? 26.402 8.177   2.734   0.50 11.92 ?  45   HIS   A HB2  1 
ATOM   1236 H  HB3  A HIS   A 1 45  ? 25.547 7.011   2.738   0.50 9.52  ?  45   HIS   A HB3  1 
ATOM   1237 H  HB3  B HIS   A 1 45  ? 25.405 6.942   2.718   0.50 11.92 ?  45   HIS   A HB3  1 
ATOM   1238 H  HD2  A HIS   A 1 45  ? 28.940 7.261   3.619   0.50 10.60 ?  45   HIS   A HD2  1 
ATOM   1239 H  HD2  B HIS   A 1 45  ? 28.770 7.360   3.649   0.50 10.66 ?  45   HIS   A HD2  1 
ATOM   1240 H  HE1  A HIS   A 1 45  ? 28.742 3.591   2.155   0.50 10.79 ?  45   HIS   A HE1  1 
ATOM   1241 H  HE1  B HIS   A 1 45  ? 28.753 3.672   2.217   0.50 10.53 ?  45   HIS   A HE1  1 
ATOM   1242 H  HE2  A HIS   A 1 45  ? 30.052 5.117   3.402   0.50 10.97 ?  45   HIS   A HE2  1 
ATOM   1243 H  HE2  B HIS   A 1 45  ? 29.977 5.265   3.465   0.50 10.37 ?  45   HIS   A HE2  1 
ATOM   1244 N  N    A GLY   A 1 46  ? 24.508 8.899   -0.546  0.50 9.66  ?  46   GLY   A N    1 
ATOM   1245 N  N    B GLY   A 1 46  ? 24.244 8.763   -0.473  0.50 9.82  ?  46   GLY   A N    1 
ATOM   1246 C  CA   A GLY   A 1 46  ? 23.696 10.055  -0.890  0.50 10.04 ?  46   GLY   A CA   1 
ATOM   1247 C  CA   B GLY   A 1 46  ? 23.412 9.901   -0.813  0.50 10.30 ?  46   GLY   A CA   1 
ATOM   1248 C  C    A GLY   A 1 46  ? 22.205 9.938   -0.640  0.50 9.72  ?  46   GLY   A C    1 
ATOM   1249 C  C    B GLY   A 1 46  ? 21.953 9.775   -0.423  0.50 9.89  ?  46   GLY   A C    1 
ATOM   1250 O  O    A GLY   A 1 46  ? 21.534 10.947  -0.399  0.50 10.02 ?  46   GLY   A O    1 
ATOM   1251 O  O    B GLY   A 1 46  ? 21.340 10.750  0.028   0.50 10.72 ?  46   GLY   A O    1 
ATOM   1252 H  H    A GLY   A 1 46  ? 24.657 8.363   -1.199  0.50 11.59 ?  46   GLY   A H    1 
ATOM   1253 H  H    B GLY   A 1 46  ? 24.253 8.133   -1.059  0.50 11.79 ?  46   GLY   A H    1 
ATOM   1254 H  HA2  A GLY   A 1 46  ? 24.020 10.822  -0.393  0.50 12.04 ?  46   GLY   A HA2  1 
ATOM   1255 H  HA2  B GLY   A 1 46  ? 23.762 10.691  -0.372  0.50 12.36 ?  46   GLY   A HA2  1 
ATOM   1256 H  HA3  A GLY   A 1 46  ? 23.810 10.244  -1.833  0.50 12.04 ?  46   GLY   A HA3  1 
ATOM   1257 H  HA3  B GLY   A 1 46  ? 23.460 10.048  -1.769  0.50 12.36 ?  46   GLY   A HA3  1 
ATOM   1258 N  N    A GLY   A 1 47  ? 21.669 8.725   -0.716  0.50 9.52  ?  47   GLY   A N    1 
ATOM   1259 N  N    B GLY   A 1 47  ? 21.379 8.586   -0.595  0.50 9.98  ?  47   GLY   A N    1 
ATOM   1260 C  CA   A GLY   A 1 47  ? 20.234 8.522   -0.654  0.50 10.02 ?  47   GLY   A CA   1 
ATOM   1261 C  CA   B GLY   A 1 47  ? 19.953 8.399   -0.419  0.50 10.01 ?  47   GLY   A CA   1 
ATOM   1262 C  C    A GLY   A 1 47  ? 19.928 7.075   -0.333  0.50 9.36  ?  47   GLY   A C    1 
ATOM   1263 C  C    B GLY   A 1 47  ? 19.635 6.967   -0.054  0.50 9.26  ?  47   GLY   A C    1 
ATOM   1264 O  O    A GLY   A 1 47  ? 20.827 6.256   -0.130  0.50 9.17  ?  47   GLY   A O    1 
ATOM   1265 O  O    B GLY   A 1 47  ? 20.526 6.129   0.097   0.50 9.46  ?  47   GLY   A O    1 
ATOM   1266 H  H    A GLY   A 1 47  ? 22.119 8.001   -0.792  0.50 11.42 ?  47   GLY   A H    1 
ATOM   1267 H  H    B GLY   A 1 47  ? 21.808 7.864   -0.799  0.50 11.97 ?  47   GLY   A H    1 
ATOM   1268 H  HA2  A GLY   A 1 47  ? 19.841 9.091   0.030   0.50 12.03 ?  47   GLY   A HA2  1 
ATOM   1269 H  HA2  B GLY   A 1 47  ? 19.629 8.974   0.290   0.50 12.02 ?  47   GLY   A HA2  1 
ATOM   1270 H  HA3  A GLY   A 1 47  ? 19.835 8.744   -1.511  0.50 12.03 ?  47   GLY   A HA3  1 
ATOM   1271 H  HA3  B GLY   A 1 47  ? 19.489 8.624   -1.241  0.50 12.02 ?  47   GLY   A HA3  1 
ATOM   1272 N  N    A GLY   A 1 48  ? 18.637 6.761   -0.309  0.50 9.56  ?  48   GLY   A N    1 
ATOM   1273 N  N    B GLY   A 1 48  ? 18.339 6.688   0.081   0.50 9.41  ?  48   GLY   A N    1 
ATOM   1274 C  CA   A GLY   A 1 48  ? 18.235 5.421   0.056   0.50 9.67  ?  48   GLY   A CA   1 
ATOM   1275 C  CA   B GLY   A 1 48  ? 17.928 5.360   0.487   0.50 8.94  ?  48   GLY   A CA   1 
ATOM   1276 C  C    A GLY   A 1 48  ? 18.652 5.089   1.475   0.50 9.34  ?  48   GLY   A C    1 
ATOM   1277 C  C    B GLY   A 1 48  ? 18.515 4.992   1.838   0.50 8.99  ?  48   GLY   A C    1 
ATOM   1278 O  O    A GLY   A 1 48  ? 18.824 5.970   2.326   0.50 9.68  ?  48   GLY   A O    1 
ATOM   1279 O  O    B GLY   A 1 48  ? 18.697 5.835   2.722   0.50 9.38  ?  48   GLY   A O    1 
ATOM   1280 H  H    A GLY   A 1 48  ? 17.993 7.294   -0.495  0.50 11.47 ?  48   GLY   A H    1 
ATOM   1281 H  H    B GLY   A 1 48  ? 17.685 7.244   -0.054  0.50 11.29 ?  48   GLY   A H    1 
ATOM   1282 H  HA2  A GLY   A 1 48  ? 17.274 5.334   -0.013  0.50 11.60 ?  48   GLY   A HA2  1 
ATOM   1283 H  HA2  B GLY   A 1 48  ? 16.959 5.313   0.543   0.50 10.72 ?  48   GLY   A HA2  1 
ATOM   1284 H  HA3  A GLY   A 1 48  ? 18.652 4.778   -0.540  0.50 11.60 ?  48   GLY   A HA3  1 
ATOM   1285 H  HA3  B GLY   A 1 48  ? 18.230 4.710   -0.167  0.50 10.72 ?  48   GLY   A HA3  1 
ATOM   1286 N  N    A VAL   A 1 49  ? 18.816 3.791   1.739   0.50 9.87  ?  49   VAL   A N    1 
ATOM   1287 N  N    B VAL   A 1 49  ? 18.805 3.701   2.005   0.50 8.86  ?  49   VAL   A N    1 
ATOM   1288 C  CA   A VAL   A 1 49  ? 19.277 3.345   3.052   0.50 9.57  ?  49   VAL   A CA   1 
ATOM   1289 C  CA   B VAL   A 1 49  ? 19.400 3.221   3.250   0.50 8.95  ?  49   VAL   A CA   1 
ATOM   1290 C  C    A VAL   A 1 49  ? 20.588 4.030   3.426   0.50 8.94  ?  49   VAL   A C    1 
ATOM   1291 C  C    B VAL   A 1 49  ? 20.708 3.949   3.542   0.50 8.43  ?  49   VAL   A C    1 
ATOM   1292 O  O    A VAL   A 1 49  ? 20.766 4.481   4.561   0.50 8.91  ?  49   VAL   A O    1 
ATOM   1293 O  O    B VAL   A 1 49  ? 20.971 4.347   4.682   0.50 8.28  ?  49   VAL   A O    1 
ATOM   1294 C  CB   A VAL   A 1 49  ? 19.404 1.809   3.084   0.50 10.58 ?  49   VAL   A CB   1 
ATOM   1295 C  CB   B VAL   A 1 49  ? 19.602 1.695   3.190   0.50 9.70  ?  49   VAL   A CB   1 
ATOM   1296 C  CG1  A VAL   A 1 49  ? 20.109 1.351   4.360   0.50 10.76 ?  49   VAL   A CG1  1 
ATOM   1297 C  CG1  B VAL   A 1 49  ? 20.529 1.238   4.308   0.50 9.05  ?  49   VAL   A CG1  1 
ATOM   1298 C  CG2  A VAL   A 1 49  ? 18.032 1.146   2.961   0.50 11.57 ?  49   VAL   A CG2  1 
ATOM   1299 C  CG2  B VAL   A 1 49  ? 18.258 0.967   3.270   0.50 10.92 ?  49   VAL   A CG2  1 
ATOM   1300 H  H    A VAL   A 1 49  ? 18.664 3.152   1.185   0.50 11.85 ?  49   VAL   A H    1 
ATOM   1301 H  H    B VAL   A 1 49  ? 18.668 3.088   1.417   0.50 10.64 ?  49   VAL   A H    1 
ATOM   1302 H  HA   A VAL   A 1 49  ? 18.619 3.591   3.720   0.50 11.48 ?  49   VAL   A HA   1 
ATOM   1303 H  HA   B VAL   A 1 49  ? 18.789 3.406   3.979   0.50 10.74 ?  49   VAL   A HA   1 
ATOM   1304 H  HB   A VAL   A 1 49  ? 19.941 1.515   2.333   0.50 12.70 ?  49   VAL   A HB   1 
ATOM   1305 H  HB   B VAL   A 1 49  ? 20.015 1.461   2.345   0.50 11.64 ?  49   VAL   A HB   1 
ATOM   1306 H  HG11 A VAL   A 1 49  ? 19.936 0.404   4.495   0.50 12.92 ?  49   VAL   A HG11 1 
ATOM   1307 H  HG11 B VAL   A 1 49  ? 20.415 0.283   4.442   0.50 10.86 ?  49   VAL   A HG11 1 
ATOM   1308 H  HG12 A VAL   A 1 49  ? 21.060 1.503   4.272   0.50 12.92 ?  49   VAL   A HG12 1 
ATOM   1309 H  HG12 B VAL   A 1 49  ? 21.448 1.424   4.058   0.50 10.86 ?  49   VAL   A HG12 1 
ATOM   1310 H  HG13 A VAL   A 1 49  ? 19.756 1.856   5.112   0.50 12.92 ?  49   VAL   A HG13 1 
ATOM   1311 H  HG13 B VAL   A 1 49  ? 20.302 1.712   5.123   0.50 10.86 ?  49   VAL   A HG13 1 
ATOM   1312 H  HG21 A VAL   A 1 49  ? 18.141 0.179   2.984   0.50 13.88 ?  49   VAL   A HG21 1 
ATOM   1313 H  HG21 B VAL   A 1 49  ? 18.410 0.009   3.224   0.50 13.11 ?  49   VAL   A HG21 1 
ATOM   1314 H  HG22 A VAL   A 1 49  ? 17.474 1.429   3.703   0.50 13.88 ?  49   VAL   A HG22 1 
ATOM   1315 H  HG22 B VAL   A 1 49  ? 17.824 1.190   4.110   0.50 13.11 ?  49   VAL   A HG22 1 
ATOM   1316 H  HG23 A VAL   A 1 49  ? 17.628 1.410   2.121   0.50 13.88 ?  49   VAL   A HG23 1 
ATOM   1317 H  HG23 B VAL   A 1 49  ? 17.700 1.247   2.528   0.50 13.11 ?  49   VAL   A HG23 1 
ATOM   1318 N  N    A ALA   A 1 50  ? 21.534 4.089   2.482   0.50 8.53  ?  50   ALA   A N    1 
ATOM   1319 N  N    B ALA   A 1 50  ? 21.567 4.088   2.529   0.50 8.37  ?  50   ALA   A N    1 
ATOM   1320 C  CA   A ALA   A 1 50  ? 22.847 4.658   2.788   0.50 8.34  ?  50   ALA   A CA   1 
ATOM   1321 C  CA   B ALA   A 1 50  ? 22.892 4.658   2.760   0.50 8.54  ?  50   ALA   A CA   1 
ATOM   1322 C  C    A ALA   A 1 50  ? 22.744 6.121   3.195   0.50 8.26  ?  50   ALA   A C    1 
ATOM   1323 C  C    B ALA   A 1 50  ? 22.797 6.103   3.233   0.50 8.25  ?  50   ALA   A C    1 
ATOM   1324 O  O    A ALA   A 1 50  ? 23.396 6.556   4.152   0.50 8.72  ?  50   ALA   A O    1 
ATOM   1325 O  O    B ALA   A 1 50  ? 23.425 6.488   4.228   0.50 8.68  ?  50   ALA   A O    1 
ATOM   1326 C  CB   A ALA   A 1 50  ? 23.771 4.520   1.582   0.50 8.38  ?  50   ALA   A CB   1 
ATOM   1327 C  CB   B ALA   A 1 50  ? 23.731 4.564   1.488   0.50 8.82  ?  50   ALA   A CB   1 
ATOM   1328 H  H    A ALA   A 1 50  ? 21.443 3.813   1.672   0.50 10.23 ?  50   ALA   A H    1 
ATOM   1329 H  H    B ALA   A 1 50  ? 21.406 3.870   1.711   0.50 10.04 ?  50   ALA   A H    1 
ATOM   1330 H  HA   A ALA   A 1 50  ? 23.241 4.173   3.527   0.50 10.01 ?  50   ALA   A HA   1 
ATOM   1331 H  HA   B ALA   A 1 50  ? 23.338 4.151   3.453   0.50 10.24 ?  50   ALA   A HA   1 
ATOM   1332 H  HB1  A ALA   A 1 50  ? 24.635 4.905   1.801   0.50 10.06 ?  50   ALA   A HB1  1 
ATOM   1333 H  HB1  B ALA   A 1 50  ? 24.608 4.943   1.659   0.50 10.59 ?  50   ALA   A HB1  1 
ATOM   1334 H  HB2  A ALA   A 1 50  ? 23.871 3.582   1.364   0.50 10.06 ?  50   ALA   A HB2  1 
ATOM   1335 H  HB2  B ALA   A 1 50  ? 23.819 3.630   1.236   0.50 10.59 ?  50   ALA   A HB2  1 
ATOM   1336 H  HB3  A ALA   A 1 50  ? 23.380 4.996   0.830   0.50 10.06 ?  50   ALA   A HB3  1 
ATOM   1337 H  HB3  B ALA   A 1 50  ? 23.290 5.057   0.779   0.50 10.59 ?  50   ALA   A HB3  1 
ATOM   1338 N  N    A GLY   A 1 51  ? 21.951 6.903   2.468   0.50 8.64  ?  51   GLY   A N    1 
ATOM   1339 N  N    B GLY   A 1 51  ? 22.029 6.926   2.521   0.50 8.56  ?  51   GLY   A N    1 
ATOM   1340 C  CA   A GLY   A 1 51  ? 21.811 8.306   2.819   0.50 8.98  ?  51   GLY   A CA   1 
ATOM   1341 C  CA   B GLY   A 1 51  ? 21.848 8.299   2.960   0.50 8.75  ?  51   GLY   A CA   1 
ATOM   1342 C  C    A GLY   A 1 51  ? 21.219 8.496   4.200   0.50 8.50  ?  51   GLY   A C    1 
ATOM   1343 C  C    B GLY   A 1 51  ? 21.229 8.378   4.341   0.50 9.21  ?  51   GLY   A C    1 
ATOM   1344 O  O    A GLY   A 1 51  ? 21.628 9.392   4.945   0.50 8.56  ?  51   GLY   A O    1 
ATOM   1345 O  O    B GLY   A 1 51  ? 21.584 9.245   5.145   0.50 9.90  ?  51   GLY   A O    1 
ATOM   1346 H  H    A GLY   A 1 51  ? 21.498 6.653   1.778   0.50 10.36 ?  51   GLY   A H    1 
ATOM   1347 H  H    B GLY   A 1 51  ? 21.614 6.718   1.792   0.50 10.27 ?  51   GLY   A H    1 
ATOM   1348 H  HA2  A GLY   A 1 51  ? 22.677 8.734   2.802   0.50 10.78 ?  51   GLY   A HA2  1 
ATOM   1349 H  HA2  B GLY   A 1 51  ? 22.705 8.751   2.978   0.50 10.49 ?  51   GLY   A HA2  1 
ATOM   1350 H  HA3  A GLY   A 1 51  ? 21.235 8.749   2.173   0.50 10.78 ?  51   GLY   A HA3  1 
ATOM   1351 H  HA3  B GLY   A 1 51  ? 21.269 8.766   2.331   0.50 10.49 ?  51   GLY   A HA3  1 
ATOM   1352 N  N    A ALA   A 1 52  ? 20.241 7.658   4.556   0.50 7.95  ?  52   ALA   A N    1 
ATOM   1353 N  N    B ALA   A 1 52  ? 20.295 7.470   4.635   0.50 9.47  ?  52   ALA   A N    1 
ATOM   1354 C  CA   A ALA   A 1 52  ? 19.599 7.754   5.861   0.50 8.64  ?  52   ALA   A CA   1 
ATOM   1355 C  CA   B ALA   A 1 52  ? 19.647 7.462   5.940   0.50 9.43  ?  52   ALA   A CA   1 
ATOM   1356 C  C    A ALA   A 1 52  ? 20.542 7.331   6.981   0.50 8.10  ?  52   ALA   A C    1 
ATOM   1357 C  C    B ALA   A 1 52  ? 20.628 7.078   7.043   0.50 9.12  ?  52   ALA   A C    1 
ATOM   1358 O  O    A ALA   A 1 52  ? 20.631 8.003   8.015   0.50 8.64  ?  52   ALA   A O    1 
ATOM   1359 O  O    B ALA   A 1 52  ? 20.693 7.738   8.087   0.50 9.54  ?  52   ALA   A O    1 
ATOM   1360 C  CB   A ALA   A 1 52  ? 18.319 6.915   5.873   0.50 9.29  ?  52   ALA   A CB   1 
ATOM   1361 C  CB   B ALA   A 1 52  ? 18.451 6.508   5.917   0.50 10.26 ?  52   ALA   A CB   1 
ATOM   1362 H  H    A ALA   A 1 52  ? 19.942 7.020   4.061   0.50 9.54  ?  52   ALA   A H    1 
ATOM   1363 H  H    B ALA   A 1 52  ? 20.030 6.846   4.101   0.50 11.36 ?  52   ALA   A H    1 
ATOM   1364 H  HA   A ALA   A 1 52  ? 19.350 8.675   6.018   0.50 10.36 ?  52   ALA   A HA   1 
ATOM   1365 H  HA   B ALA   A 1 52  ? 19.314 8.351   6.130   0.50 11.32 ?  52   ALA   A HA   1 
ATOM   1366 H  HB1  A ALA   A 1 52  ? 17.899 6.988   6.745   0.50 11.15 ?  52   ALA   A HB1  1 
ATOM   1367 H  HB1  B ALA   A 1 52  ? 18.004 6.540   6.778   0.50 12.31 ?  52   ALA   A HB1  1 
ATOM   1368 H  HB2  A ALA   A 1 52  ? 17.716 7.248   5.189   0.50 11.15 ?  52   ALA   A HB2  1 
ATOM   1369 H  HB2  B ALA   A 1 52  ? 17.836 6.790   5.219   0.50 12.31 ?  52   ALA   A HB2  1 
ATOM   1370 H  HB3  A ALA   A 1 52  ? 18.543 5.988   5.692   0.50 11.15 ?  52   ALA   A HB3  1 
ATOM   1371 H  HB3  B ALA   A 1 52  ? 18.763 5.609   5.737   0.50 12.31 ?  52   ALA   A HB3  1 
ATOM   1372 N  N    A LEU   A 1 53  ? 21.241 6.207   6.808   0.50 8.14  ?  53   LEU   A N    1 
ATOM   1373 N  N    B LEU   A 1 53  ? 21.389 6.001   6.843   0.50 8.78  ?  53   LEU   A N    1 
ATOM   1374 C  CA   A LEU   A 1 53  ? 22.193 5.778   7.827   0.50 8.71  ?  53   LEU   A CA   1 
ATOM   1375 C  CA   B LEU   A 1 53  ? 22.388 5.627   7.839   0.50 8.66  ?  53   LEU   A CA   1 
ATOM   1376 C  C    A LEU   A 1 53  ? 23.261 6.840   8.029   0.50 8.59  ?  53   LEU   A C    1 
ATOM   1377 C  C    B LEU   A 1 53  ? 23.410 6.738   8.026   0.50 8.36  ?  53   LEU   A C    1 
ATOM   1378 O  O    A LEU   A 1 53  ? 23.562 7.234   9.162   0.50 9.27  ?  53   LEU   A O    1 
ATOM   1379 O  O    B LEU   A 1 53  ? 23.784 7.067   9.157   0.50 9.16  ?  53   LEU   A O    1 
ATOM   1380 C  CB   A LEU   A 1 53  ? 22.829 4.439   7.434   0.50 9.45  ?  53   LEU   A CB   1 
ATOM   1381 C  CB   B LEU   A 1 53  ? 23.093 4.331   7.432   0.50 8.59  ?  53   LEU   A CB   1 
ATOM   1382 C  CG   A LEU   A 1 53  ? 21.952 3.182   7.487   0.50 9.76  ?  53   LEU   A CG   1 
ATOM   1383 C  CG   B LEU   A 1 53  ? 22.298 3.027   7.523   0.50 8.81  ?  53   LEU   A CG   1 
ATOM   1384 C  CD1  A LEU   A 1 53  ? 22.695 1.987   6.898   0.50 9.94  ?  53   LEU   A CD1  1 
ATOM   1385 C  CD1  B LEU   A 1 53  ? 23.100 1.888   6.906   0.50 9.47  ?  53   LEU   A CD1  1 
ATOM   1386 C  CD2  A LEU   A 1 53  ? 21.501 2.874   8.907   0.50 10.76 ?  53   LEU   A CD2  1 
ATOM   1387 C  CD2  B LEU   A 1 53  ? 21.935 2.699   8.962   0.50 9.46  ?  53   LEU   A CD2  1 
ATOM   1388 H  H    A LEU   A 1 53  ? 21.192 5.693   6.122   0.50 9.77  ?  53   LEU   A H    1 
ATOM   1389 H  H    B LEU   A 1 53  ? 21.340 5.479   6.158   0.50 10.53 ?  53   LEU   A H    1 
ATOM   1390 H  HA   A LEU   A 1 53  ? 21.732 5.655   8.668   0.50 10.46 ?  53   LEU   A HA   1 
ATOM   1391 H  HA   B LEU   A 1 53  ? 21.945 5.475   8.688   0.50 10.39 ?  53   LEU   A HA   1 
ATOM   1392 H  HB2  A LEU   A 1 53  ? 23.151 4.515   6.522   0.50 11.34 ?  53   LEU   A HB2  1 
ATOM   1393 H  HB2  B LEU   A 1 53  ? 23.379 4.422   6.509   0.50 10.31 ?  53   LEU   A HB2  1 
ATOM   1394 H  HB3  A LEU   A 1 53  ? 23.582 4.276   8.023   0.50 11.34 ?  53   LEU   A HB3  1 
ATOM   1395 H  HB3  B LEU   A 1 53  ? 23.873 4.225   7.997   0.50 10.31 ?  53   LEU   A HB3  1 
ATOM   1396 H  HG   A LEU   A 1 53  ? 21.157 3.326   6.947   0.50 11.71 ?  53   LEU   A HG   1 
ATOM   1397 H  HG   B LEU   A 1 53  ? 21.477 3.116   7.016   0.50 10.57 ?  53   LEU   A HG   1 
ATOM   1398 H  HD11 A LEU   A 1 53  ? 22.125 1.203   6.942   0.50 11.93 ?  53   LEU   A HD11 1 
ATOM   1399 H  HD11 B LEU   A 1 53  ? 22.586 1.067   6.973   0.50 11.36 ?  53   LEU   A HD11 1 
ATOM   1400 H  HD12 A LEU   A 1 53  ? 22.925 2.178   5.976   0.50 11.93 ?  53   LEU   A HD12 1 
ATOM   1401 H  HD12 B LEU   A 1 53  ? 23.275 2.093   5.975   0.50 11.36 ?  53   LEU   A HD12 1 
ATOM   1402 H  HD13 A LEU   A 1 53  ? 23.504 1.834   7.415   0.50 11.93 ?  53   LEU   A HD13 1 
ATOM   1403 H  HD13 B LEU   A 1 53  ? 23.937 1.794   7.388   0.50 11.36 ?  53   LEU   A HD13 1 
ATOM   1404 H  HD21 A LEU   A 1 53  ? 21.004 2.041   8.909   0.50 12.92 ?  53   LEU   A HD21 1 
ATOM   1405 H  HD21 B LEU   A 1 53  ? 21.402 1.890   8.979   0.50 11.36 ?  53   LEU   A HD21 1 
ATOM   1406 H  HD22 A LEU   A 1 53  ? 22.285 2.793   9.474   0.50 12.92 ?  53   LEU   A HD22 1 
ATOM   1407 H  HD22 B LEU   A 1 53  ? 22.748 2.574   9.474   0.50 11.36 ?  53   LEU   A HD22 1 
ATOM   1408 H  HD23 A LEU   A 1 53  ? 20.938 3.597   9.222   0.50 12.92 ?  53   LEU   A HD23 1 
ATOM   1409 H  HD23 B LEU   A 1 53  ? 21.423 3.437   9.334   0.50 11.36 ?  53   LEU   A HD23 1 
ATOM   1410 N  N    A ASN   A 1 54  ? 23.824 7.341   6.932   0.50 8.75  ?  54   ASN   A N    1 
ATOM   1411 N  N    B ASN   A 1 54  ? 23.884 7.323   6.927   0.50 8.44  ?  54   ASN   A N    1 
ATOM   1412 C  CA   A ASN   A 1 54  ? 24.892 8.322   7.058   0.50 8.93  ?  54   ASN   A CA   1 
ATOM   1413 C  CA   B ASN   A 1 54  ? 24.917 8.342   7.058   0.50 8.30  ?  54   ASN   A CA   1 
ATOM   1414 C  C    A ASN   A 1 54  ? 24.402 9.583   7.765   0.50 9.10  ?  54   ASN   A C    1 
ATOM   1415 C  C    B ASN   A 1 54  ? 24.390 9.571   7.795   0.50 8.50  ?  54   ASN   A C    1 
ATOM   1416 O  O    A ASN   A 1 54  ? 25.117 10.162  8.592   0.50 10.00 ?  54   ASN   A O    1 
ATOM   1417 O  O    B ASN   A 1 54  ? 25.060 10.104  8.689   0.50 8.98  ?  54   ASN   A O    1 
ATOM   1418 C  CB   A ASN   A 1 54  ? 25.455 8.666   5.688   0.50 9.06  ?  54   ASN   A CB   1 
ATOM   1419 C  CB   B ASN   A 1 54  ? 25.477 8.733   5.698   0.50 8.22  ?  54   ASN   A CB   1 
ATOM   1420 C  CG   A ASN   A 1 54  ? 26.506 9.733   5.779   0.50 9.40  ?  54   ASN   A CG   1 
ATOM   1421 C  CG   B ASN   A 1 54  ? 26.446 9.885   5.810   0.50 8.08  ?  54   ASN   A CG   1 
ATOM   1422 O  OD1  A ASN   A 1 54  ? 27.483 9.581   6.516   0.50 9.71  ?  54   ASN   A OD1  1 
ATOM   1423 O  OD1  B ASN   A 1 54  ? 27.489 9.759   6.456   0.50 8.34  ?  54   ASN   A OD1  1 
ATOM   1424 N  ND2  A ASN   A 1 54  ? 26.312 10.830  5.064   0.50 9.70  ?  54   ASN   A ND2  1 
ATOM   1425 N  ND2  B ASN   A 1 54  ? 26.102 11.022  5.218   0.50 8.35  ?  54   ASN   A ND2  1 
ATOM   1426 H  H    A ASN   A 1 54  ? 23.603 7.136   6.123   0.50 10.50 ?  54   ASN   A H    1 
ATOM   1427 H  H    B ASN   A 1 54  ? 23.629 7.150   6.123   0.50 10.13 ?  54   ASN   A H    1 
ATOM   1428 H  HA   A ASN   A 1 54  ? 25.602 7.938   7.589   0.50 10.71 ?  54   ASN   A HA   1 
ATOM   1429 H  HA   B ASN   A 1 54  ? 25.640 7.976   7.585   0.50 9.96  ?  54   ASN   A HA   1 
ATOM   1430 H  HB2  A ASN   A 1 54  ? 25.858 7.867   5.307   0.50 10.87 ?  54   ASN   A HB2  1 
ATOM   1431 H  HB2  B ASN   A 1 54  ? 25.952 7.966   5.324   0.50 9.87  ?  54   ASN   A HB2  1 
ATOM   1432 H  HB3  A ASN   A 1 54  ? 24.739 8.984   5.120   0.50 10.87 ?  54   ASN   A HB3  1 
ATOM   1433 H  HB3  B ASN   A 1 54  ? 24.752 8.992   5.114   0.50 9.87  ?  54   ASN   A HB3  1 
ATOM   1434 H  HD21 A ASN   A 1 54  ? 26.888 11.465  5.094   0.50 11.64 ?  54   ASN   A HD21 1 
ATOM   1435 H  HD21 B ASN   A 1 54  ? 26.622 11.706  5.264   0.50 10.02 ?  54   ASN   A HD21 1 
ATOM   1436 H  HD22 A ASN   A 1 54  ? 25.615 10.900  4.567   0.50 11.64 ?  54   ASN   A HD22 1 
ATOM   1437 H  HD22 B ASN   A 1 54  ? 25.360 11.074  4.789   0.50 10.02 ?  54   ASN   A HD22 1 
ATOM   1438 N  N    . LYS   A 1 55  ? 23.184 10.028  7.444   1.00 9.31  ?  55   LYS   A N    1 
ATOM   1439 C  CA   . LYS   A 1 55  ? 22.606 11.185  8.120   1.00 9.70  ?  55   LYS   A CA   1 
ATOM   1440 C  C    . LYS   A 1 55  ? 22.512 10.944  9.621   1.00 9.96  ?  55   LYS   A C    1 
ATOM   1441 O  O    . LYS   A 1 55  ? 22.791 11.843  10.425  1.00 10.58 ?  55   LYS   A O    1 
ATOM   1442 C  CB   . LYS   A 1 55  ? 21.236 11.497  7.509   1.00 10.64 ?  55   LYS   A CB   1 
ATOM   1443 C  CG   . LYS   A 1 55  ? 20.496 12.650  8.166   1.00 12.12 ?  55   LYS   A CG   1 
ATOM   1444 C  CD   . LYS   A 1 55  ? 19.182 12.941  7.434   1.00 13.11 ?  55   LYS   A CD   1 
ATOM   1445 C  CE   . LYS   A 1 55  ? 18.352 14.022  8.117   1.00 15.09 ?  55   LYS   A CE   1 
ATOM   1446 N  NZ   . LYS   A 1 55  ? 17.030 14.215  7.445   1.00 15.75 ?  55   LYS   A NZ   1 
ATOM   1447 H  H    A LYS   A 1 55  ? 22.673 9.676   6.843   0.50 11.17 ?  55   LYS   A H    1 
ATOM   1448 H  H    B LYS   A 1 55  ? 22.677 9.677   6.839   0.50 11.17 ?  55   LYS   A H    1 
ATOM   1449 H  HA   . LYS   A 1 55  ? 23.178 11.951  7.976   1.00 11.64 ?  55   LYS   A HA   1 
ATOM   1450 H  HB2  . LYS   A 1 55  ? 21.359 11.729  6.574   1.00 12.77 ?  55   LYS   A HB2  1 
ATOM   1451 H  HB3  . LYS   A 1 55  ? 20.674 10.711  7.578   1.00 12.77 ?  55   LYS   A HB3  1 
ATOM   1452 H  HG2  . LYS   A 1 55  ? 20.282 12.414  9.084   1.00 14.54 ?  55   LYS   A HG2  1 
ATOM   1453 H  HG3  . LYS   A 1 55  ? 21.044 13.446  8.140   1.00 14.54 ?  55   LYS   A HG3  1 
ATOM   1454 H  HD2  . LYS   A 1 55  ? 19.383 13.243  6.534   1.00 15.74 ?  55   LYS   A HD2  1 
ATOM   1455 H  HD3  . LYS   A 1 55  ? 18.650 12.130  7.401   1.00 15.74 ?  55   LYS   A HD3  1 
ATOM   1456 H  HE2  . LYS   A 1 55  ? 18.190 13.763  9.040   1.00 18.11 ?  55   LYS   A HE2  1 
ATOM   1457 H  HE3  . LYS   A 1 55  ? 18.835 14.862  8.087   1.00 18.11 ?  55   LYS   A HE3  1 
ATOM   1458 H  HZ1  . LYS   A 1 55  ? 16.491 14.692  7.969   1.00 18.90 ?  55   LYS   A HZ1  1 
ATOM   1459 H  HZ2  . LYS   A 1 55  ? 17.140 14.645  6.675   1.00 18.90 ?  55   LYS   A HZ2  1 
ATOM   1460 H  HZ3  . LYS   A 1 55  ? 16.651 13.424  7.287   1.00 18.90 ?  55   LYS   A HZ3  1 
ATOM   1461 N  N    . ALA   A 1 56  ? 22.135 9.728   10.022  1.00 10.14 ?  56   ALA   A N    1 
ATOM   1462 C  CA   . ALA   A 1 56  ? 22.016 9.401   11.436  1.00 10.85 ?  56   ALA   A CA   1 
ATOM   1463 C  C    . ALA   A 1 56  ? 23.359 9.425   12.156  1.00 10.54 ?  56   ALA   A C    1 
ATOM   1464 O  O    . ALA   A 1 56  ? 23.380 9.610   13.377  1.00 12.20 ?  56   ALA   A O    1 
ATOM   1465 C  CB   . ALA   A 1 56  ? 21.309 8.050   11.610  1.00 11.87 ?  56   ALA   A CB   1 
ATOM   1466 H  H    . ALA   A 1 56  ? 21.948 9.081   9.490   1.00 12.16 ?  56   ALA   A H    1 
ATOM   1467 H  HA   . ALA   A 1 56  ? 21.458 10.067  11.856  1.00 13.02 ?  56   ALA   A HA   1 
ATOM   1468 H  HB1  . ALA   A 1 56  ? 21.236 7.849   12.559  1.00 14.24 ?  56   ALA   A HB1  1 
ATOM   1469 H  HB2  . ALA   A 1 56  ? 20.421 8.104   11.219  1.00 14.24 ?  56   ALA   A HB2  1 
ATOM   1470 H  HB3  . ALA   A 1 56  ? 21.823 7.357   11.167  1.00 14.24 ?  56   ALA   A HB3  1 
ATOM   1471 N  N    . THR   A 1 57  ? 24.474 9.260   11.431  1.00 9.97  ?  57   THR   A N    1 
ATOM   1472 C  CA   . THR   A 1 57  ? 25.816 9.392   12.003  1.00 10.18 ?  57   THR   A CA   1 
ATOM   1473 C  C    . THR   A 1 57  ? 26.360 10.813  11.918  1.00 10.49 ?  57   THR   A C    1 
ATOM   1474 O  O    . THR   A 1 57  ? 27.542 11.033  12.210  1.00 11.01 ?  57   THR   A O    1 
ATOM   1475 C  CB   . THR   A 1 57  ? 26.828 8.448   11.331  1.00 9.90  ?  57   THR   A CB   1 
ATOM   1476 O  OG1  . THR   A 1 57  ? 27.202 8.944   10.033  1.00 9.79  ?  57   THR   A OG1  1 
ATOM   1477 C  CG2  . THR   A 1 57  ? 26.310 7.029   11.237  1.00 10.10 ?  57   THR   A CG2  1 
ATOM   1478 H  H    . THR   A 1 57  ? 24.476 9.054   10.592  1.00 11.96 ?  57   THR   A H    1 
ATOM   1479 H  HA   . THR   A 1 57  ? 25.773 9.142   12.942  1.00 12.22 ?  57   THR   A HA   1 
ATOM   1480 H  HB   . THR   A 1 57  ? 27.630 8.417   11.886  1.00 11.88 ?  57   THR   A HB   1 
ATOM   1481 H  HG1  . THR   A 1 57  ? 26.521 9.000   9.548   1.00 11.75 ?  57   THR   A HG1  1 
ATOM   1482 H  HG21 . THR   A 1 57  ? 26.987 6.450   10.845  1.00 12.12 ?  57   THR   A HG21 1 
ATOM   1483 H  HG22 . THR   A 1 57  ? 26.084 6.693   12.117  1.00 12.12 ?  57   THR   A HG22 1 
ATOM   1484 H  HG23 . THR   A 1 57  ? 25.519 7.000   10.678  1.00 12.12 ?  57   THR   A HG23 1 
ATOM   1485 N  N    . ASN   A 1 58  ? 25.540 11.782  11.518  1.00 10.77 ?  58   ASN   A N    1 
ATOM   1486 C  CA   . ASN   A 1 58  ? 25.995 13.166  11.416  1.00 11.98 ?  58   ASN   A CA   1 
ATOM   1487 C  C    . ASN   A 1 58  ? 27.137 13.297  10.407  1.00 10.52 ?  58   ASN   A C    1 
ATOM   1488 O  O    . ASN   A 1 58  ? 28.029 14.132  10.564  1.00 11.31 ?  58   ASN   A O    1 
ATOM   1489 C  CB   . ASN   A 1 58  ? 26.368 13.708  12.811  1.00 14.37 ?  58   ASN   A CB   1 
ATOM   1490 C  CG   . ASN   A 1 58  ? 26.794 15.159  12.805  1.00 17.95 ?  58   ASN   A CG   1 
ATOM   1491 O  OD1  . ASN   A 1 58  ? 26.172 15.989  12.158  1.00 19.31 ?  58   ASN   A OD1  1 
ATOM   1492 N  ND2  . ASN   A 1 58  ? 27.852 15.476  13.554  1.00 19.07 ?  58   ASN   A ND2  1 
ATOM   1493 H  H    . ASN   A 1 58  ? 24.719 11.656  11.289  1.00 12.92 ?  58   ASN   A H    1 
ATOM   1494 H  HA   . ASN   A 1 58  ? 25.257 13.699  11.083  1.00 14.38 ?  58   ASN   A HA   1 
ATOM   1495 H  HB2  . ASN   A 1 58  ? 25.589 13.623  13.392  1.00 17.25 ?  58   ASN   A HB2  1 
ATOM   1496 H  HB3  . ASN   A 1 58  ? 27.099 13.190  13.168  1.00 17.25 ?  58   ASN   A HB3  1 
ATOM   1497 H  HD21 . ASN   A 1 58  ? 28.123 16.290  13.587  1.00 22.88 ?  58   ASN   A HD21 1 
ATOM   1498 H  HD22 . ASN   A 1 58  ? 28.255 14.865  13.998  1.00 22.88 ?  58   ASN   A HD22 1 
ATOM   1499 N  N    . ASN   A 1 59  ? 27.121 12.475  9.358   1.00 9.81  ?  59   ASN   A N    1 
ATOM   1500 C  CA   . ASN   A 1 59  ? 28.094 12.462  8.260   1.00 9.37  ?  59   ASN   A CA   1 
ATOM   1501 C  C    . ASN   A 1 59  ? 29.412 11.781  8.642   1.00 9.36  ?  59   ASN   A C    1 
ATOM   1502 O  O    . ASN   A 1 59  ? 30.329 11.748  7.816   1.00 9.79  ?  59   ASN   A O    1 
ATOM   1503 C  CB   . ASN   A 1 59  ? 28.374 13.851  7.658   1.00 9.75  ?  59   ASN   A CB   1 
ATOM   1504 C  CG   . ASN   A 1 59  ? 28.726 13.788  6.188   1.00 9.94  ?  59   ASN   A CG   1 
ATOM   1505 O  OD1  . ASN   A 1 59  ? 28.020 13.157  5.397   1.00 10.35 ?  59   ASN   A OD1  1 
ATOM   1506 N  ND2  . ASN   A 1 59  ? 29.804 14.455  5.805   1.00 10.76 ?  59   ASN   A ND2  1 
ATOM   1507 H  H    . ASN   A 1 59  ? 26.519 11.870  9.252   1.00 11.78 ?  59   ASN   A H    1 
ATOM   1508 H  HA   . ASN   A 1 59  ? 27.713 11.932  7.547   1.00 11.24 ?  59   ASN   A HA   1 
ATOM   1509 H  HB2  . ASN   A 1 59  ? 27.586 14.408  7.747   1.00 11.71 ?  59   ASN   A HB2  1 
ATOM   1510 H  HB3  . ASN   A 1 59  ? 29.123 14.260  8.122   1.00 11.71 ?  59   ASN   A HB3  1 
ATOM   1511 H  HD21 . ASN   A 1 59  ? 30.045 14.459  4.977   1.00 12.91 ?  59   ASN   A HD21 1 
ATOM   1512 H  HD22 . ASN   A 1 59  ? 30.277 14.894  6.383   1.00 12.91 ?  59   ASN   A HD22 1 
ATOM   1513 N  N    . ALA   A 1 60  ? 29.542 11.236  9.852   1.00 9.29  ?  60   ALA   A N    1 
ATOM   1514 C  CA   . ALA   A 1 60  ? 30.783 10.555  10.209  1.00 9.65  ?  60   ALA   A CA   1 
ATOM   1515 C  C    . ALA   A 1 60  ? 31.008 9.326   9.335   1.00 9.61  ?  60   ALA   A C    1 
ATOM   1516 O  O    . ALA   A 1 60  ? 32.149 9.003   8.991   1.00 10.24 ?  60   ALA   A O    1 
ATOM   1517 C  CB   . ALA   A 1 60  ? 30.786 10.191  11.694  1.00 10.25 ?  60   ALA   A CB   1 
ATOM   1518 H  H    . ALA   A 1 60  ? 28.944 11.244  10.468  1.00 11.15 ?  60   ALA   A H    1 
ATOM   1519 H  HA   . ALA   A 1 60  ? 31.525 11.163  10.053  1.00 11.58 ?  60   ALA   A HA   1 
ATOM   1520 H  HB1  . ALA   A 1 60  ? 31.618 9.743   11.909  1.00 12.30 ?  60   ALA   A HB1  1 
ATOM   1521 H  HB2  . ALA   A 1 60  ? 30.705 11.006  12.218  1.00 12.30 ?  60   ALA   A HB2  1 
ATOM   1522 H  HB3  . ALA   A 1 60  ? 30.036 9.606   11.877  1.00 12.30 ?  60   ALA   A HB3  1 
ATOM   1523 N  N    . MET   A 1 61  ? 29.938 8.627   8.962   1.00 9.16  ?  61   MET   A N    1 
ATOM   1524 C  CA   . MET   A 1 61  ? 30.079 7.492   8.057   1.00 9.11  ?  61   MET   A CA   1 
ATOM   1525 C  C    . MET   A 1 61  ? 30.702 7.919   6.733   1.00 8.94  ?  61   MET   A C    1 
ATOM   1526 O  O    . MET   A 1 61  ? 31.590 7.239   6.207   1.00 9.37  ?  61   MET   A O    1 
ATOM   1527 C  CB   . MET   A 1 61  ? 28.719 6.825   7.850   1.00 8.95  ?  61   MET   A CB   1 
ATOM   1528 C  CG   . MET   A 1 61  ? 28.720 5.664   6.860   1.00 9.78  ?  61   MET   A CG   1 
ATOM   1529 S  SD   . MET   A 1 61  ? 27.099 4.905   6.678   1.00 10.41 ?  61   MET   A SD   1 
ATOM   1530 C  CE   . MET   A 1 61  ? 26.994 4.006   8.222   1.00 11.86 ?  61   MET   A CE   1 
ATOM   1531 H  H    . MET   A 1 61  ? 29.132 8.787   9.213   1.00 10.99 ?  61   MET   A H    1 
ATOM   1532 H  HA   . MET   A 1 61  ? 30.664 6.840   8.474   1.00 10.93 ?  61   MET   A HA   1 
ATOM   1533 H  HB2  . MET   A 1 61  ? 28.415 6.477   8.702   1.00 10.74 ?  61   MET   A HB2  1 
ATOM   1534 H  HB3  . MET   A 1 61  ? 28.094 7.486   7.525   1.00 10.74 ?  61   MET   A HB3  1 
ATOM   1535 H  HG2  . MET   A 1 61  ? 28.988 5.987   5.984   1.00 11.74 ?  61   MET   A HG2  1 
ATOM   1536 H  HG3  . MET   A 1 61  ? 29.333 4.980   7.163   1.00 11.74 ?  61   MET   A HG3  1 
ATOM   1537 H  HE1  . MET   A 1 61  ? 26.159 3.512   8.245   1.00 14.23 ?  61   MET   A HE1  1 
ATOM   1538 H  HE2  . MET   A 1 61  ? 27.743 3.391   8.279   1.00 14.23 ?  61   MET   A HE2  1 
ATOM   1539 H  HE3  . MET   A 1 61  ? 27.026 4.634   8.960   1.00 14.23 ?  61   MET   A HE3  1 
ATOM   1540 N  N    . GLN   A 1 62  ? 30.248 9.046   6.176   1.00 8.96  ?  62   GLN   A N    1 
ATOM   1541 C  CA   . GLN   A 1 62  ? 30.800 9.518   4.911   1.00 9.15  ?  62   GLN   A CA   1 
ATOM   1542 C  C    . GLN   A 1 62  ? 32.268 9.898   5.045   1.00 9.16  ?  62   GLN   A C    1 
ATOM   1543 O  O    . GLN   A 1 62  ? 33.071 9.587   4.160   1.00 9.79  ?  62   GLN   A O    1 
ATOM   1544 C  CB   . GLN   A 1 62  ? 29.991 10.702  4.380   1.00 9.30  ?  62   GLN   A CB   1 
ATOM   1545 C  CG   . GLN   A 1 62  ? 30.364 11.066  2.953   1.00 9.20  ?  62   GLN   A CG   1 
ATOM   1546 C  CD   . GLN   A 1 62  ? 30.025 9.935   2.007   1.00 9.42  ?  62   GLN   A CD   1 
ATOM   1547 O  OE1  . GLN   A 1 62  ? 28.844 9.631   1.811   1.00 10.10 ?  62   GLN   A OE1  1 
ATOM   1548 N  NE2  . GLN   A 1 62  ? 31.035 9.268   1.464   1.00 10.19 ?  62   GLN   A NE2  1 
ATOM   1549 H  H    . GLN   A 1 62  ? 29.626 9.541   6.506   1.00 10.75 ?  62   GLN   A H    1 
ATOM   1550 H  HA   . GLN   A 1 62  ? 30.743 8.801   4.264   1.00 10.98 ?  62   GLN   A HA   1 
ATOM   1551 H  HB2  . GLN   A 1 62  ? 29.049 10.478  4.397   1.00 11.16 ?  62   GLN   A HB2  1 
ATOM   1552 H  HB3  . GLN   A 1 62  ? 30.159 11.479  4.939   1.00 11.16 ?  62   GLN   A HB3  1 
ATOM   1553 H  HG2  . GLN   A 1 62  ? 29.863 11.847  2.681   1.00 11.04 ?  62   GLN   A HG2  1 
ATOM   1554 H  HG3  . GLN   A 1 62  ? 31.317 11.236  2.900   1.00 11.04 ?  62   GLN   A HG3  1 
ATOM   1555 H  HE21 . GLN   A 1 62  ? 31.846 9.494   1.638   1.00 12.23 ?  62   GLN   A HE21 1 
ATOM   1556 H  HE22 . GLN   A 1 62  ? 30.880 8.610   0.929   1.00 12.23 ?  62   GLN   A HE22 1 
ATOM   1557 N  N    . VAL   A 1 63  ? 32.634 10.590  6.130   1.00 9.53  ?  63   VAL   A N    1 
ATOM   1558 C  CA   . VAL   A 1 63  ? 34.026 10.984  6.337   1.00 10.77 ?  63   VAL   A CA   1 
ATOM   1559 C  C    . VAL   A 1 63  ? 34.924 9.753   6.388   1.00 10.08 ?  63   VAL   A C    1 
ATOM   1560 O  O    . VAL   A 1 63  ? 35.972 9.692   5.728   1.00 10.72 ?  63   VAL   A O    1 
ATOM   1561 C  CB   . VAL   A 1 63  ? 34.142 11.855  7.602   1.00 12.15 ?  63   VAL   A CB   1 
ATOM   1562 C  CG1  . VAL   A 1 63  ? 35.593 12.101  7.956   1.00 14.13 ?  63   VAL   A CG1  1 
ATOM   1563 C  CG2  . VAL   A 1 63  ? 33.403 13.176  7.396   1.00 12.73 ?  63   VAL   A CG2  1 
ATOM   1564 H  H    . VAL   A 1 63  ? 32.092 10.836  6.759   1.00 11.44 ?  63   VAL   A H    1 
ATOM   1565 H  HA   . VAL   A 1 63  ? 34.302 11.523  5.584   1.00 12.93 ?  63   VAL   A HA   1 
ATOM   1566 H  HB   . VAL   A 1 63  ? 33.725 11.393  8.346   1.00 14.59 ?  63   VAL   A HB   1 
ATOM   1567 H  HG11 . VAL   A 1 63  ? 35.639 12.829  8.593   1.00 16.96 ?  63   VAL   A HG11 1 
ATOM   1568 H  HG12 . VAL   A 1 63  ? 35.964 11.295  8.343   1.00 16.96 ?  63   VAL   A HG12 1 
ATOM   1569 H  HG13 . VAL   A 1 63  ? 36.074 12.338  7.148   1.00 16.96 ?  63   VAL   A HG13 1 
ATOM   1570 H  HG21 . VAL   A 1 63  ? 33.501 13.719  8.196   1.00 15.28 ?  63   VAL   A HG21 1 
ATOM   1571 H  HG22 . VAL   A 1 63  ? 33.787 13.638  6.635   1.00 15.28 ?  63   VAL   A HG22 1 
ATOM   1572 H  HG23 . VAL   A 1 63  ? 32.464 12.993  7.236   1.00 15.28 ?  63   VAL   A HG23 1 
ATOM   1573 N  N    . GLU   A 1 64  ? 34.514 8.745   7.161   1.00 10.07 ?  64   GLU   A N    1 
ATOM   1574 C  CA   . GLU   A 1 64  ? 35.285 7.513   7.257   1.00 9.87  ?  64   GLU   A CA   1 
ATOM   1575 C  C    . GLU   A 1 64  ? 35.363 6.820   5.904   1.00 9.64  ?  64   GLU   A C    1 
ATOM   1576 O  O    . GLU   A 1 64  ? 36.410 6.274   5.521   1.00 10.09 ?  64   GLU   A O    1 
ATOM   1577 C  CB   . GLU   A 1 64  ? 34.608 6.605   8.284   1.00 10.73 ?  64   GLU   A CB   1 
ATOM   1578 C  CG   . GLU   A 1 64  ? 35.259 5.253   8.444   1.00 11.30 ?  64   GLU   A CG   1 
ATOM   1579 C  CD   . GLU   A 1 64  ? 34.386 4.255   9.177   1.00 11.55 ?  64   GLU   A CD   1 
ATOM   1580 O  OE1  . GLU   A 1 64  ? 33.145 4.344   9.053   1.00 12.37 ?  64   GLU   A OE1  1 
ATOM   1581 O  OE2  . GLU   A 1 64  ? 34.939 3.366   9.870   1.00 11.92 -1 64   GLU   A OE2  1 
ATOM   1582 H  H    . GLU   A 1 64  ? 33.788 8.743   7.625   1.00 12.09 ?  64   GLU   A H    1 
ATOM   1583 H  HA   . GLU   A 1 64  ? 36.185 7.718   7.562   1.00 11.84 ?  64   GLU   A HA   1 
ATOM   1584 H  HB2  . GLU   A 1 64  ? 34.633 7.052   9.151   1.00 12.88 ?  64   GLU   A HB2  1 
ATOM   1585 H  HB3  . GLU   A 1 64  ? 33.690 6.470   8.016   1.00 12.88 ?  64   GLU   A HB3  1 
ATOM   1586 H  HG2  . GLU   A 1 64  ? 35.463 4.885   7.571   1.00 13.57 ?  64   GLU   A HG2  1 
ATOM   1587 H  HG3  . GLU   A 1 64  ? 36.080 5.361   8.952   1.00 13.57 ?  64   GLU   A HG3  1 
ATOM   1588 N  N    . SER   A 1 65  ? 34.242 6.809   5.176   1.00 9.47  ?  65   SER   A N    1 
ATOM   1589 C  CA   . SER   A 1 65  ? 34.187 6.142   3.882   1.00 9.44  ?  65   SER   A CA   1 
ATOM   1590 C  C    . SER   A 1 65  ? 35.099 6.814   2.865   1.00 9.60  ?  65   SER   A C    1 
ATOM   1591 O  O    . SER   A 1 65  ? 35.728 6.136   2.044   1.00 10.55 ?  65   SER   A O    1 
ATOM   1592 C  CB   . SER   A 1 65  ? 32.748 6.145   3.363   1.00 9.32  ?  65   SER   A CB   1 
ATOM   1593 O  OG   . SER   A 1 65  ? 31.902 5.338   4.163   1.00 9.73  ?  65   SER   A OG   1 
ATOM   1594 H  H    . SER   A 1 65  ? 33.510 7.188   5.412   1.00 11.36 ?  65   SER   A H    1 
ATOM   1595 H  HA   . SER   A 1 65  ? 34.475 5.224   3.982   1.00 11.33 ?  65   SER   A HA   1 
ATOM   1596 H  HB2  . SER   A 1 65  ? 32.415 7.055   3.375   1.00 11.18 ?  65   SER   A HB2  1 
ATOM   1597 H  HB3  . SER   A 1 65  ? 32.750 5.806   2.458   1.00 11.18 ?  65   SER   A HB3  1 
ATOM   1598 H  HG   . SER   A 1 65  ? 31.904 5.622   4.958   1.00 11.68 ?  65   SER   A HG   1 
ATOM   1599 N  N    . ASP   A 1 66  ? 35.170 8.148   2.887   1.00 9.84  ?  66   ASP   A N    1 
ATOM   1600 C  CA   . ASP   A 1 66  ? 36.022 8.846   1.930   1.00 10.46 ?  66   ASP   A CA   1 
ATOM   1601 C  C    . ASP   A 1 66  ? 37.490 8.493   2.156   1.00 10.64 ?  66   ASP   A C    1 
ATOM   1602 O  O    . ASP   A 1 66  ? 38.255 8.325   1.197   1.00 11.69 ?  66   ASP   A O    1 
ATOM   1603 C  CB   . ASP   A 1 66  ? 35.808 10.355  2.035   1.00 11.77 ?  66   ASP   A CB   1 
ATOM   1604 C  CG   . ASP   A 1 66  ? 34.465 10.819  1.442   1.00 13.33 ?  66   ASP   A CG   1 
ATOM   1605 O  OD1  . ASP   A 1 66  ? 33.741 10.018  0.812   1.00 13.48 ?  66   ASP   A OD1  1 
ATOM   1606 O  OD2  . ASP   A 1 66  ? 34.171 12.023  1.584   1.00 15.91 -1 66   ASP   A OD2  1 
ATOM   1607 H  H    . ASP   A 1 66  ? 34.738 8.664   3.431   1.00 11.80 ?  66   ASP   A H    1 
ATOM   1608 H  HA   . ASP   A 1 66  ? 35.776 8.570   1.033   1.00 12.56 ?  66   ASP   A HA   1 
ATOM   1609 H  HB2  . ASP   A 1 66  ? 35.825 10.612  2.969   1.00 14.12 ?  66   ASP   A HB2  1 
ATOM   1610 H  HB3  . ASP   A 1 66  ? 36.524 10.806  1.556   1.00 14.12 ?  66   ASP   A HB3  1 
ATOM   1611 N  N    . ASP   A 1 67  ? 37.897 8.358   3.419   1.00 10.77 ?  67   ASP   A N    1 
ATOM   1612 C  CA   . ASP   A 1 67  ? 39.251 7.907   3.712   1.00 11.78 ?  67   ASP   A CA   1 
ATOM   1613 C  C    . ASP   A 1 67  ? 39.463 6.474   3.237   1.00 11.61 ?  67   ASP   A C    1 
ATOM   1614 O  O    . ASP   A 1 67  ? 40.520 6.149   2.684   1.00 12.32 ?  67   ASP   A O    1 
ATOM   1615 C  CB   . ASP   A 1 67  ? 39.528 8.039   5.209   1.00 13.14 ?  67   ASP   A CB   1 
ATOM   1616 C  CG   . ASP   A 1 67  ? 40.828 7.380   5.623   1.00 14.20 ?  67   ASP   A CG   1 
ATOM   1617 O  OD1  . ASP   A 1 67  ? 41.898 8.019   5.482   1.00 17.00 ?  67   ASP   A OD1  1 
ATOM   1618 O  OD2  . ASP   A 1 67  ? 40.778 6.217   6.084   1.00 13.83 -1 67   ASP   A OD2  1 
ATOM   1619 H  H    . ASP   A 1 67  ? 37.414 8.516   4.106   1.00 12.93 ?  67   ASP   A H    1 
ATOM   1620 H  HA   . ASP   A 1 67  ? 39.880 8.471   3.235   1.00 14.13 ?  67   ASP   A HA   1 
ATOM   1621 H  HB2  . ASP   A 1 67  ? 39.578 8.977   5.431   1.00 15.76 ?  67   ASP   A HB2  1 
ATOM   1622 H  HB3  . ASP   A 1 67  ? 38.804 7.614   5.696   1.00 15.76 ?  67   ASP   A HB3  1 
ATOM   1623 N  N    A TYR   A 1 68  ? 38.466 5.608   3.424   0.50 10.96 ?  68   TYR   A N    1 
ATOM   1624 N  N    B TYR   A 1 68  ? 38.471 5.595   3.446   0.50 11.05 ?  68   TYR   A N    1 
ATOM   1625 C  CA   A TYR   A 1 68  ? 38.604 4.230   2.968   0.50 11.08 ?  68   TYR   A CA   1 
ATOM   1626 C  CA   B TYR   A 1 68  ? 38.581 4.219   2.959   0.50 11.15 ?  68   TYR   A CA   1 
ATOM   1627 C  C    A TYR   A 1 68  ? 38.817 4.166   1.457   0.50 11.09 ?  68   TYR   A C    1 
ATOM   1628 C  C    B TYR   A 1 68  ? 38.842 4.195   1.458   0.50 11.14 ?  68   TYR   A C    1 
ATOM   1629 O  O    A TYR   A 1 68  ? 39.670 3.409   0.975   0.50 11.45 ?  68   TYR   A O    1 
ATOM   1630 O  O    B TYR   A 1 68  ? 39.740 3.488   0.979   0.50 11.56 ?  68   TYR   A O    1 
ATOM   1631 C  CB   A TYR   A 1 68  ? 37.381 3.405   3.392   0.50 11.50 ?  68   TYR   A CB   1 
ATOM   1632 C  CB   B TYR   A 1 68  ? 37.317 3.399   3.292   0.50 11.50 ?  68   TYR   A CB   1 
ATOM   1633 C  CG   A TYR   A 1 68  ? 37.452 1.995   2.863   0.50 12.41 ?  68   TYR   A CG   1 
ATOM   1634 C  CG   B TYR   A 1 68  ? 37.329 2.038   2.602   0.50 12.11 ?  68   TYR   A CG   1 
ATOM   1635 C  CD1  A TYR   A 1 68  ? 36.988 1.696   1.591   0.50 13.67 ?  68   TYR   A CD1  1 
ATOM   1636 C  CD1  B TYR   A 1 68  ? 36.866 1.902   1.294   0.50 12.41 ?  68   TYR   A CD1  1 
ATOM   1637 C  CD2  A TYR   A 1 68  ? 38.036 0.980   3.604   0.50 13.90 ?  68   TYR   A CD2  1 
ATOM   1638 C  CD2  B TYR   A 1 68  ? 37.850 0.911   3.231   0.50 12.36 ?  68   TYR   A CD2  1 
ATOM   1639 C  CE1  A TYR   A 1 68  ? 37.089 0.430   1.073   0.50 14.96 ?  68   TYR   A CE1  1 
ATOM   1640 C  CE1  B TYR   A 1 68  ? 36.916 0.689   0.640   0.50 12.08 ?  68   TYR   A CE1  1 
ATOM   1641 C  CE2  A TYR   A 1 68  ? 38.132 -0.306  3.095   0.50 15.04 ?  68   TYR   A CE2  1 
ATOM   1642 C  CE2  B TYR   A 1 68  ? 37.893 -0.317  2.585   0.50 11.78 ?  68   TYR   A CE2  1 
ATOM   1643 C  CZ   A TYR   A 1 68  ? 37.661 -0.566  1.828   0.50 15.81 ?  68   TYR   A CZ   1 
ATOM   1644 C  CZ   B TYR   A 1 68  ? 37.435 -0.409  1.294   0.50 11.50 ?  68   TYR   A CZ   1 
ATOM   1645 O  OH   A TYR   A 1 68  ? 37.764 -1.829  1.304   0.50 17.88 ?  68   TYR   A OH   1 
ATOM   1646 O  OH   B TYR   A 1 68  ? 37.500 -1.619  0.658   0.50 11.79 ?  68   TYR   A OH   1 
ATOM   1647 H  H    A TYR   A 1 68  ? 37.713 5.792   3.801   0.50 13.16 ?  68   TYR   A H    1 
ATOM   1648 H  H    B TYR   A 1 68  ? 37.736 5.772   3.862   0.50 13.26 ?  68   TYR   A H    1 
ATOM   1649 H  HA   A TYR   A 1 68  ? 39.380 3.840   3.391   0.50 13.29 ?  68   TYR   A HA   1 
ATOM   1650 H  HA   B TYR   A 1 68  ? 39.328 3.792   3.398   0.50 13.38 ?  68   TYR   A HA   1 
ATOM   1651 H  HB2  A TYR   A 1 68  ? 37.346 3.363   4.360   0.50 13.79 ?  68   TYR   A HB2  1 
ATOM   1652 H  HB2  B TYR   A 1 68  ? 37.272 3.248   4.249   0.50 13.79 ?  68   TYR   A HB2  1 
ATOM   1653 H  HB3  A TYR   A 1 68  ? 36.577 3.819   3.044   0.50 13.79 ?  68   TYR   A HB3  1 
ATOM   1654 H  HB3  B TYR   A 1 68  ? 36.528 3.883   2.993   0.50 13.79 ?  68   TYR   A HB3  1 
ATOM   1655 H  HD1  A TYR   A 1 68  ? 36.610 2.373   1.074   0.50 16.41 ?  68   TYR   A HD1  1 
ATOM   1656 H  HD1  B TYR   A 1 68  ? 36.521 2.640   0.845   0.50 14.90 ?  68   TYR   A HD1  1 
ATOM   1657 H  HD2  A TYR   A 1 68  ? 38.369 1.164   4.453   0.50 16.68 ?  68   TYR   A HD2  1 
ATOM   1658 H  HD2  B TYR   A 1 68  ? 38.174 0.982   4.093   0.50 14.83 ?  68   TYR   A HD2  1 
ATOM   1659 H  HE1  A TYR   A 1 68  ? 36.766 0.251   0.217   0.50 17.95 ?  68   TYR   A HE1  1 
ATOM   1660 H  HE1  B TYR   A 1 68  ? 36.599 0.604   -0.237  0.50 14.50 ?  68   TYR   A HE1  1 
ATOM   1661 H  HE2  A TYR   A 1 68  ? 38.529 -0.983  3.593   0.50 18.04 ?  68   TYR   A HE2  1 
ATOM   1662 H  HE2  B TYR   A 1 68  ? 38.252 -1.067  3.007   0.50 14.14 ?  68   TYR   A HE2  1 
ATOM   1663 H  HH   A TYR   A 1 68  ? 38.125 -2.342  1.856   0.50 21.46 ?  68   TYR   A HH   1 
ATOM   1664 H  HH   B TYR   A 1 68  ? 37.839 -2.202  1.166   0.50 14.15 ?  68   TYR   A HH   1 
ATOM   1665 N  N    . ILE   A 1 69  ? 38.045 4.945   0.694   1.00 10.73 ?  69   ILE   A N    1 
ATOM   1666 C  CA   . ILE   A 1 69  ? 38.174 4.930   -0.761  1.00 10.97 ?  69   ILE   A CA   1 
ATOM   1667 C  C    . ILE   A 1 69  ? 39.503 5.535   -1.195  1.00 10.74 ?  69   ILE   A C    1 
ATOM   1668 O  O    . ILE   A 1 69  ? 40.145 5.045   -2.131  1.00 11.19 ?  69   ILE   A O    1 
ATOM   1669 C  CB   . ILE   A 1 69  ? 36.974 5.645   -1.417  1.00 11.67 ?  69   ILE   A CB   1 
ATOM   1670 C  CG1  . ILE   A 1 69  ? 35.658 4.909   -1.145  1.00 11.97 ?  69   ILE   A CG1  1 
ATOM   1671 C  CG2  . ILE   A 1 69  ? 37.215 5.856   -2.921  1.00 12.97 ?  69   ILE   A CG2  1 
ATOM   1672 C  CD1  . ILE   A 1 69  ? 35.500 3.612   -1.902  1.00 12.69 ?  69   ILE   A CD1  1 
ATOM   1673 H  H    A ILE   A 1 69  ? 37.446 5.487   0.993   0.50 12.88 ?  69   ILE   A H    1 
ATOM   1674 H  H    B ILE   A 1 69  ? 37.429 5.469   0.991   0.50 12.88 ?  69   ILE   A H    1 
ATOM   1675 H  HA   . ILE   A 1 69  ? 38.166 4.008   -1.060  1.00 13.17 ?  69   ILE   A HA   1 
ATOM   1676 H  HB   . ILE   A 1 69  ? 36.900 6.517   -1.012  1.00 14.01 ?  69   ILE   A HB   1 
ATOM   1677 H  HG12 . ILE   A 1 69  ? 35.609 4.703   -0.196  1.00 14.37 ?  69   ILE   A HG12 1 
ATOM   1678 H  HG13 . ILE   A 1 69  ? 34.923 5.488   -1.391  1.00 14.37 ?  69   ILE   A HG13 1 
ATOM   1679 H  HG21 . ILE   A 1 69  ? 36.367 6.063   -3.350  1.00 15.57 ?  69   ILE   A HG21 1 
ATOM   1680 H  HG22 . ILE   A 1 69  ? 37.829 6.601   -3.041  1.00 15.57 ?  69   ILE   A HG22 1 
ATOM   1681 H  HG23 . ILE   A 1 69  ? 37.590 5.051   -3.302  1.00 15.57 ?  69   ILE   A HG23 1 
ATOM   1682 H  HD11 . ILE   A 1 69  ? 34.684 3.177   -1.615  1.00 15.23 ?  69   ILE   A HD11 1 
ATOM   1683 H  HD12 . ILE   A 1 69  ? 35.456 3.803   -2.853  1.00 15.23 ?  69   ILE   A HD12 1 
ATOM   1684 H  HD13 . ILE   A 1 69  ? 36.262 3.040   -1.716  1.00 15.23 ?  69   ILE   A HD13 1 
ATOM   1685 N  N    . ALA   A 1 70  ? 39.925 6.616   -0.541  1.00 10.88 ?  70   ALA   A N    1 
ATOM   1686 C  CA   . ALA   A 1 70  ? 41.198 7.223   -0.901  1.00 12.07 ?  70   ALA   A CA   1 
ATOM   1687 C  C    . ALA   A 1 70  ? 42.346 6.238   -0.733  1.00 12.41 ?  70   ALA   A C    1 
ATOM   1688 O  O    . ALA   A 1 70  ? 43.309 6.271   -1.503  1.00 14.18 ?  70   ALA   A O    1 
ATOM   1689 C  CB   . ALA   A 1 70  ? 41.437 8.477   -0.061  1.00 12.59 ?  70   ALA   A CB   1 
ATOM   1690 H  H    . ALA   A 1 70  ? 39.501 7.008   0.093   1.00 13.05 ?  70   ALA   A H    1 
ATOM   1691 H  HA   . ALA   A 1 70  ? 41.169 7.492   -1.833  1.00 14.48 ?  70   ALA   A HA   1 
ATOM   1692 H  HB1  . ALA   A 1 70  ? 42.295 8.865   -0.313  1.00 15.11 ?  70   ALA   A HB1  1 
ATOM   1693 H  HB2  . ALA   A 1 70  ? 40.727 9.112   -0.226  1.00 15.11 ?  70   ALA   A HB2  1 
ATOM   1694 H  HB3  . ALA   A 1 70  ? 41.455 8.230   0.877   1.00 15.11 ?  70   ALA   A HB3  1 
ATOM   1695 N  N    . THR   A 1 71  ? 42.249 5.342   0.249   1.00 12.02 ?  71   THR   A N    1 
ATOM   1696 C  CA   . THR   A 1 71  ? 43.303 4.361   0.493   1.00 13.30 ?  71   THR   A CA   1 
ATOM   1697 C  C    . THR   A 1 71  ? 43.182 3.142   -0.411  1.00 13.58 ?  71   THR   A C    1 
ATOM   1698 O  O    . THR   A 1 71  ? 44.193 2.643   -0.924  1.00 15.28 ?  71   THR   A O    1 
ATOM   1699 C  CB   . THR   A 1 71  ? 43.240 3.906   1.946   1.00 15.10 ?  71   THR   A CB   1 
ATOM   1700 O  OG1  . THR   A 1 71  ? 43.504 5.026   2.796   1.00 16.41 ?  71   THR   A OG1  1 
ATOM   1701 C  CG2  . THR   A 1 71  ? 44.245 2.784   2.216   1.00 16.65 ?  71   THR   A CG2  1 
ATOM   1702 H  H    . THR   A 1 71  ? 41.578 5.278   0.787   1.00 14.42 ?  71   THR   A H    1 
ATOM   1703 H  HA   . THR   A 1 71  ? 44.165 4.771   0.331   1.00 15.95 ?  71   THR   A HA   1 
ATOM   1704 H  HB   . THR   A 1 71  ? 42.353 3.565   2.136   1.00 18.12 ?  71   THR   A HB   1 
ATOM   1705 H  HG1  . THR   A 1 71  ? 43.485 4.780   3.599   1.00 19.69 ?  71   THR   A HG1  1 
ATOM   1706 H  HG21 . THR   A 1 71  ? 44.401 2.703   3.169   1.00 19.99 ?  71   THR   A HG21 1 
ATOM   1707 H  HG22 . THR   A 1 71  ? 43.908 1.940   1.880   1.00 19.99 ?  71   THR   A HG22 1 
ATOM   1708 H  HG23 . THR   A 1 71  ? 45.091 2.983   1.778   1.00 19.99 ?  71   THR   A HG23 1 
ATOM   1709 N  N    . ASN   A 1 72  ? 41.957 2.633   -0.594  1.00 12.92 ?  72   ASN   A N    1 
ATOM   1710 C  CA   . ASN   A 1 72  ? 41.739 1.310   -1.160  1.00 12.88 ?  72   ASN   A CA   1 
ATOM   1711 C  C    . ASN   A 1 72  ? 41.108 1.301   -2.540  1.00 12.98 ?  72   ASN   A C    1 
ATOM   1712 O  O    . ASN   A 1 72  ? 41.120 0.250   -3.192  1.00 14.21 ?  72   ASN   A O    1 
ATOM   1713 C  CB   . ASN   A 1 72  ? 40.860 0.479   -0.216  1.00 13.58 ?  72   ASN   A CB   1 
ATOM   1714 C  CG   . ASN   A 1 72  ? 41.479 0.333   1.149   1.00 14.55 ?  72   ASN   A CG   1 
ATOM   1715 O  OD1  . ASN   A 1 72  ? 41.014 0.931   2.120   1.00 16.24 ?  72   ASN   A OD1  1 
ATOM   1716 N  ND2  . ASN   A 1 72  ? 42.544 -0.434  1.229   1.00 15.03 ?  72   ASN   A ND2  1 
ATOM   1717 H  H    . ASN   A 1 72  ? 41.221 3.046   -0.391  1.00 15.51 ?  72   ASN   A H    1 
ATOM   1718 H  HA   . ASN   A 1 72  ? 42.592 0.866   -1.231  1.00 15.46 ?  72   ASN   A HA   1 
ATOM   1719 H  HB2  . ASN   A 1 72  ? 39.996 0.909   -0.118  1.00 16.29 ?  72   ASN   A HB2  1 
ATOM   1720 H  HB3  . ASN   A 1 72  ? 40.748 -0.411  -0.588  1.00 16.29 ?  72   ASN   A HB3  1 
ATOM   1721 H  HD21 . ASN   A 1 72  ? 42.938 -0.534  1.987   1.00 18.03 ?  72   ASN   A HD21 1 
ATOM   1722 H  HD22 . ASN   A 1 72  ? 42.848 -0.817  0.528   1.00 18.03 ?  72   ASN   A HD22 1 
ATOM   1723 N  N    . GLY   A 1 73  ? 40.547 2.414   -2.995  1.00 12.54 ?  73   GLY   A N    1 
ATOM   1724 C  CA   . GLY   A 1 73  ? 39.811 2.437   -4.234  1.00 12.14 ?  73   GLY   A CA   1 
ATOM   1725 C  C    . GLY   A 1 73  ? 38.421 1.859   -4.059  1.00 11.38 ?  73   GLY   A C    1 
ATOM   1726 O  O    . GLY   A 1 73  ? 38.042 1.398   -2.975  1.00 12.11 ?  73   GLY   A O    1 
ATOM   1727 H  H    . GLY   A 1 73  ? 40.580 3.184   -2.601  1.00 15.04 ?  73   GLY   A H    1 
ATOM   1728 H  HA2  . GLY   A 1 73  ? 39.733 3.353   -4.552  1.00 14.57 ?  73   GLY   A HA2  1 
ATOM   1729 H  HA3  . GLY   A 1 73  ? 40.284 1.918   -4.905  1.00 14.57 ?  73   GLY   A HA3  1 
ATOM   1730 N  N    . PRO   A 1 74  ? 37.637 1.882   -5.135  1.00 12.03 ?  74   PRO   A N    1 
ATOM   1731 C  CA   . PRO   A 1 74  ? 36.243 1.445   -5.045  1.00 11.93 ?  74   PRO   A CA   1 
ATOM   1732 C  C    . PRO   A 1 74  ? 36.099 -0.038  -4.726  1.00 11.28 ?  74   PRO   A C    1 
ATOM   1733 O  O    . PRO   A 1 74  ? 36.963 -0.871  -5.019  1.00 12.28 ?  74   PRO   A O    1 
ATOM   1734 C  CB   . PRO   A 1 74  ? 35.680 1.750   -6.439  1.00 13.77 ?  74   PRO   A CB   1 
ATOM   1735 C  CG   . PRO   A 1 74  ? 36.625 2.737   -7.046  1.00 16.10 ?  74   PRO   A CG   1 
ATOM   1736 C  CD   . PRO   A 1 74  ? 37.969 2.396   -6.475  1.00 13.82 ?  74   PRO   A CD   1 
ATOM   1737 H  HA   . PRO   A 1 74  ? 35.764 1.966   -4.379  1.00 14.31 ?  74   PRO   A HA   1 
ATOM   1738 H  HB2  . PRO   A 1 74  ? 35.647 0.934   -6.961  1.00 16.52 ?  74   PRO   A HB2  1 
ATOM   1739 H  HB3  . PRO   A 1 74  ? 34.790 2.135   -6.352  1.00 16.52 ?  74   PRO   A HB3  1 
ATOM   1740 H  HG2  . PRO   A 1 74  ? 36.631 2.638   -8.010  1.00 19.32 ?  74   PRO   A HG2  1 
ATOM   1741 H  HG3  . PRO   A 1 74  ? 36.368 3.637   -6.794  1.00 19.32 ?  74   PRO   A HG3  1 
ATOM   1742 H  HD2  . PRO   A 1 74  ? 38.402 1.708   -7.005  1.00 16.58 ?  74   PRO   A HD2  1 
ATOM   1743 H  HD3  . PRO   A 1 74  ? 38.520 3.196   -6.417  1.00 16.58 ?  74   PRO   A HD3  1 
ATOM   1744 N  N    . LEU   A 1 75  ? 34.958 -0.359  -4.128  1.00 10.68 ?  75   LEU   A N    1 
ATOM   1745 C  CA   . LEU   A 1 75  ? 34.561 -1.747  -3.970  1.00 10.30 ?  75   LEU   A CA   1 
ATOM   1746 C  C    . LEU   A 1 75  ? 34.175 -2.338  -5.324  1.00 10.83 ?  75   LEU   A C    1 
ATOM   1747 O  O    . LEU   A 1 75  ? 34.030 -1.635  -6.327  1.00 12.73 ?  75   LEU   A O    1 
ATOM   1748 C  CB   . LEU   A 1 75  ? 33.378 -1.869  -3.007  1.00 10.46 ?  75   LEU   A CB   1 
ATOM   1749 C  CG   . LEU   A 1 75  ? 33.609 -1.465  -1.552  1.00 12.03 ?  75   LEU   A CG   1 
ATOM   1750 C  CD1  . LEU   A 1 75  ? 32.329 -1.645  -0.736  1.00 13.67 ?  75   LEU   A CD1  1 
ATOM   1751 C  CD2  . LEU   A 1 75  ? 34.740 -2.224  -0.926  1.00 15.01 ?  75   LEU   A CD2  1 
ATOM   1752 H  H    . LEU   A 1 75  ? 34.392 0.207   -3.814  1.00 12.81 ?  75   LEU   A H    1 
ATOM   1753 H  HA   . LEU   A 1 75  ? 35.304 -2.256  -3.614  1.00 12.36 ?  75   LEU   A HA   1 
ATOM   1754 H  HB2  . LEU   A 1 75  ? 32.656 -1.319  -3.341  1.00 12.55 ?  75   LEU   A HB2  1 
ATOM   1755 H  HB3  . LEU   A 1 75  ? 33.091 -2.799  -3.000  1.00 12.55 ?  75   LEU   A HB3  1 
ATOM   1756 H  HG   . LEU   A 1 75  ? 33.847 -0.527  -1.529  1.00 14.44 ?  75   LEU   A HG   1 
ATOM   1757 H  HD11 . LEU   A 1 75  ? 32.502 -1.378  0.181   1.00 16.40 ?  75   LEU   A HD11 1 
ATOM   1758 H  HD12 . LEU   A 1 75  ? 31.636 -1.085  -1.118  1.00 16.40 ?  75   LEU   A HD12 1 
ATOM   1759 H  HD13 . LEU   A 1 75  ? 32.062 -2.574  -0.767  1.00 16.40 ?  75   LEU   A HD13 1 
ATOM   1760 H  HD21 . LEU   A 1 75  ? 34.793 -1.995  0.015   1.00 18.01 ?  75   LEU   A HD21 1 
ATOM   1761 H  HD22 . LEU   A 1 75  ? 34.580 -3.176  -1.026  1.00 18.01 ?  75   LEU   A HD22 1 
ATOM   1762 H  HD23 . LEU   A 1 75  ? 35.572 -1.983  -1.369  1.00 18.01 ?  75   LEU   A HD23 1 
ATOM   1763 N  N    . LYS   A 1 76  ? 34.024 -3.659  -5.340  1.00 11.29 ?  76   LYS   A N    1 
ATOM   1764 C  CA   . LYS   A 1 76  ? 33.431 -4.378  -6.460  1.00 11.51 ?  76   LYS   A CA   1 
ATOM   1765 C  C    . LYS   A 1 76  ? 31.919 -4.460  -6.270  1.00 10.27 ?  76   LYS   A C    1 
ATOM   1766 O  O    . LYS   A 1 76  ? 31.435 -4.578  -5.148  1.00 10.14 ?  76   LYS   A O    1 
ATOM   1767 C  CB   . LYS   A 1 76  ? 33.974 -5.815  -6.505  1.00 13.20 ?  76   LYS   A CB   1 
ATOM   1768 C  CG   . LYS   A 1 76  ? 35.483 -5.922  -6.709  1.00 14.73 ?  76   LYS   A CG   1 
ATOM   1769 C  CD   . LYS   A 1 76  ? 36.008 -7.322  -6.475  1.00 15.99 ?  76   LYS   A CD   1 
ATOM   1770 C  CE   . LYS   A 1 76  ? 37.508 -7.380  -6.655  1.00 18.38 ?  76   LYS   A CE   1 
ATOM   1771 N  NZ   . LYS   A 1 76  ? 38.040 -8.742  -6.450  1.00 19.52 ?  76   LYS   A NZ   1 
ATOM   1772 H  H    . LYS   A 1 76  ? 34.261 -4.176  -4.689  1.00 13.55 ?  76   LYS   A H    1 
ATOM   1773 H  HA   . LYS   A 1 76  ? 33.629 -3.929  -7.293  1.00 13.81 ?  76   LYS   A HA   1 
ATOM   1774 H  HB2  . LYS   A 1 76  ? 33.759 -6.253  -5.669  1.00 15.84 ?  76   LYS   A HB2  1 
ATOM   1775 H  HB3  . LYS   A 1 76  ? 33.544 -6.281  -7.240  1.00 15.84 ?  76   LYS   A HB3  1 
ATOM   1776 H  HG2  . LYS   A 1 76  ? 35.694 -5.666  -7.622  1.00 17.68 ?  76   LYS   A HG2  1 
ATOM   1777 H  HG3  . LYS   A 1 76  ? 35.927 -5.323  -6.088  1.00 17.68 ?  76   LYS   A HG3  1 
ATOM   1778 H  HD2  . LYS   A 1 76  ? 35.793 -7.595  -5.569  1.00 19.19 ?  76   LYS   A HD2  1 
ATOM   1779 H  HD3  . LYS   A 1 76  ? 35.596 -7.927  -7.114  1.00 19.19 ?  76   LYS   A HD3  1 
ATOM   1780 H  HE2  . LYS   A 1 76  ? 37.729 -7.099  -7.555  1.00 22.05 ?  76   LYS   A HE2  1 
ATOM   1781 H  HE3  . LYS   A 1 76  ? 37.926 -6.791  -6.007  1.00 22.05 ?  76   LYS   A HE3  1 
ATOM   1782 H  HZ1  . LYS   A 1 76  ? 38.920 -8.749  -6.562  1.00 23.42 ?  76   LYS   A HZ1  1 
ATOM   1783 H  HZ2  . LYS   A 1 76  ? 37.849 -9.027  -5.626  1.00 23.42 ?  76   LYS   A HZ2  1 
ATOM   1784 H  HZ3  . LYS   A 1 76  ? 37.670 -9.307  -7.037  1.00 23.42 ?  76   LYS   A HZ3  1 
ATOM   1785 N  N    . VAL   A 1 77  ? 31.171 -4.443  -7.378  1.00 10.83 ?  77   VAL   A N    1 
ATOM   1786 C  CA   . VAL   A 1 77  ? 29.763 -4.828  -7.294  1.00 10.58 ?  77   VAL   A CA   1 
ATOM   1787 C  C    . VAL   A 1 77  ? 29.701 -6.281  -6.847  1.00 10.44 ?  77   VAL   A C    1 
ATOM   1788 O  O    . VAL   A 1 77  ? 30.363 -7.151  -7.426  1.00 10.62 ?  77   VAL   A O    1 
ATOM   1789 C  CB   . VAL   A 1 77  ? 29.038 -4.617  -8.632  1.00 11.85 ?  77   VAL   A CB   1 
ATOM   1790 C  CG1  . VAL   A 1 77  ? 27.582 -5.060  -8.514  1.00 12.53 ?  77   VAL   A CG1  1 
ATOM   1791 C  CG2  . VAL   A 1 77  ? 29.115 -3.165  -9.061  1.00 13.02 ?  77   VAL   A CG2  1 
ATOM   1792 H  H    . VAL   A 1 77  ? 31.453 -4.228  -8.159  1.00 13.00 ?  77   VAL   A H    1 
ATOM   1793 H  HA   . VAL   A 1 77  ? 29.325 -4.282  -6.622  1.00 12.69 ?  77   VAL   A HA   1 
ATOM   1794 H  HB   . VAL   A 1 77  ? 29.468 -5.155  -9.315  1.00 14.22 ?  77   VAL   A HB   1 
ATOM   1795 H  HG11 . VAL   A 1 77  ? 27.103 -4.763  -9.301  1.00 15.04 ?  77   VAL   A HG11 1 
ATOM   1796 H  HG12 . VAL   A 1 77  ? 27.550 -6.024  -8.447  1.00 15.04 ?  77   VAL   A HG12 1 
ATOM   1797 H  HG13 . VAL   A 1 77  ? 27.198 -4.655  -7.720  1.00 15.04 ?  77   VAL   A HG13 1 
ATOM   1798 H  HG21 . VAL   A 1 77  ? 28.617 -3.053  -9.886  1.00 15.63 ?  77   VAL   A HG21 1 
ATOM   1799 H  HG22 . VAL   A 1 77  ? 28.727 -2.610  -8.364  1.00 15.63 ?  77   VAL   A HG22 1 
ATOM   1800 H  HG23 . VAL   A 1 77  ? 30.043 -2.921  -9.198  1.00 15.63 ?  77   VAL   A HG23 1 
ATOM   1801 N  N    . GLY   A 1 78  ? 28.923 -6.546  -5.795  1.00 9.85  ?  78   GLY   A N    1 
ATOM   1802 C  CA   . GLY   A 1 78  ? 28.908 -7.832  -5.133  1.00 10.13 ?  78   GLY   A CA   1 
ATOM   1803 C  C    . GLY   A 1 78  ? 29.830 -7.922  -3.938  1.00 9.82  ?  78   GLY   A C    1 
ATOM   1804 O  O    . GLY   A 1 78  ? 29.774 -8.920  -3.204  1.00 10.33 ?  78   GLY   A O    1 
ATOM   1805 H  H    . GLY   A 1 78  ? 28.381 -5.971  -5.445  1.00 11.82 ?  78   GLY   A H    1 
ATOM   1806 H  HA2  . GLY   A 1 78  ? 28.005 -8.022  -4.837  1.00 12.16 ?  78   GLY   A HA2  1 
ATOM   1807 H  HA3  . GLY   A 1 78  ? 29.167 -8.515  -5.771  1.00 12.16 ?  78   GLY   A HA3  1 
ATOM   1808 N  N    . GLY   A 1 79  ? 30.682 -6.918  -3.721  1.00 9.69  ?  79   GLY   A N    1 
ATOM   1809 C  CA   . GLY   A 1 79  ? 31.646 -6.928  -2.646  1.00 10.17 ?  79   GLY   A CA   1 
ATOM   1810 C  C    . GLY   A 1 79  ? 31.200 -6.133  -1.433  1.00 9.33  ?  79   GLY   A C    1 
ATOM   1811 O  O    . GLY   A 1 79  ? 30.081 -5.621  -1.352  1.00 10.02 ?  79   GLY   A O    1 
ATOM   1812 H  H    . GLY   A 1 79  ? 30.722 -6.206  -4.203  1.00 11.63 ?  79   GLY   A H    1 
ATOM   1813 H  HA2  . GLY   A 1 79  ? 31.803 -7.854  -2.370  1.00 12.20 ?  79   GLY   A HA2  1 
ATOM   1814 H  HA3  . GLY   A 1 79  ? 32.485 -6.567  -2.961  1.00 12.20 ?  79   GLY   A HA3  1 
ATOM   1815 N  N    . SER   A 1 80  ? 32.109 -6.035  -0.469  1.00 10.16 ?  80   SER   A N    1 
ATOM   1816 C  CA   . SER   A 1 80  ? 31.798 -5.408  0.804   1.00 9.62  ?  80   SER   A CA   1 
ATOM   1817 C  C    . SER   A 1 80  ? 33.072 -4.952  1.494   1.00 9.65  ?  80   SER   A C    1 
ATOM   1818 O  O    . SER   A 1 80  ? 34.181 -5.380  1.162   1.00 11.04 ?  80   SER   A O    1 
ATOM   1819 C  CB   . SER   A 1 80  ? 31.053 -6.372  1.733   1.00 10.59 ?  80   SER   A CB   1 
ATOM   1820 O  OG   . SER   A 1 80  ? 31.891 -7.417  2.194   1.00 12.25 ?  80   SER   A OG   1 
ATOM   1821 H  H    . SER   A 1 80  ? 32.917 -6.310  -0.536  1.00 12.19 ?  80   SER   A H    1 
ATOM   1822 H  HA   . SER   A 1 80  ? 31.236 -4.631  0.636   1.00 11.54 ?  80   SER   A HA   1 
ATOM   1823 H  HB2  . SER   A 1 80  ? 30.722 -5.874  2.497   1.00 12.71 ?  80   SER   A HB2  1 
ATOM   1824 H  HB3  . SER   A 1 80  ? 30.306 -6.758  1.245   1.00 12.71 ?  80   SER   A HB3  1 
ATOM   1825 H  HG   . SER   A 1 80  ? 32.183 -7.853  1.534   1.00 14.70 ?  80   SER   A HG   1 
ATOM   1826 N  N    . CYS   A 1 81  ? 32.885 -4.104  2.501   1.00 9.62  ?  81   CYS   A N    1 
ATOM   1827 C  CA   . CYS   A 1 81  ? 33.936 -3.821  3.465   1.00 9.51  ?  81   CYS   A CA   1 
ATOM   1828 C  C    . CYS   A 1 81  ? 33.295 -3.590  4.826   1.00 9.43  ?  81   CYS   A C    1 
ATOM   1829 O  O    . CYS   A 1 81  ? 32.129 -3.191  4.919   1.00 10.53 ?  81   CYS   A O    1 
ATOM   1830 C  CB   . CYS   A 1 81  ? 34.803 -2.626  3.045   1.00 10.39 ?  81   CYS   A CB   1 
ATOM   1831 S  SG   . CYS   A 1 81  ? 33.898 -1.054  3.074   1.00 10.34 ?  81   CYS   A SG   1 
ATOM   1832 H  H    . CYS   A 1 81  ? 32.152 -3.669  2.647   1.00 11.54 ?  81   CYS   A H    1 
ATOM   1833 H  HA   . CYS   A 1 81  ? 34.513 -4.594  3.534   1.00 11.41 ?  81   CYS   A HA   1 
ATOM   1834 H  HB2  . CYS   A 1 81  ? 35.559 -2.555  3.650   1.00 12.47 ?  81   CYS   A HB2  1 
ATOM   1835 H  HB3  . CYS   A 1 81  ? 35.125 -2.776  2.138   1.00 12.47 ?  81   CYS   A HB3  1 
ATOM   1836 H  HG   . CYS   A 1 81  ? 34.639 -0.169  2.733   1.00 12.41 ?  81   CYS   A HG   1 
ATOM   1837 N  N    . VAL   A 1 82  ? 34.072 -3.844  5.878   1.00 9.71  ?  82   VAL   A N    1 
ATOM   1838 C  CA   . VAL   A 1 82  ? 33.657 -3.606  7.255   1.00 10.20 ?  82   VAL   A CA   1 
ATOM   1839 C  C    . VAL   A 1 82  ? 34.252 -2.287  7.725   1.00 10.12 ?  82   VAL   A C    1 
ATOM   1840 O  O    . VAL   A 1 82  ? 35.474 -2.105  7.707   1.00 11.16 ?  82   VAL   A O    1 
ATOM   1841 C  CB   . VAL   A 1 82  ? 34.084 -4.750  8.189   1.00 11.67 ?  82   VAL   A CB   1 
ATOM   1842 C  CG1  . VAL   A 1 82  ? 33.643 -4.456  9.617   1.00 13.01 ?  82   VAL   A CG1  1 
ATOM   1843 C  CG2  . VAL   A 1 82  ? 33.526 -6.081  7.714   1.00 12.60 ?  82   VAL   A CG2  1 
ATOM   1844 H  H    . VAL   A 1 82  ? 34.871 -4.173  5.817   1.00 11.65 ?  82   VAL   A H    1 
ATOM   1845 H  HA   . VAL   A 1 82  ? 32.689 -3.535  7.289   1.00 12.24 ?  82   VAL   A HA   1 
ATOM   1846 H  HB   . VAL   A 1 82  ? 35.051 -4.812  8.187   1.00 14.00 ?  82   VAL   A HB   1 
ATOM   1847 H  HG11 . VAL   A 1 82  ? 33.725 -5.265  10.148  1.00 15.61 ?  82   VAL   A HG11 1 
ATOM   1848 H  HG12 . VAL   A 1 82  ? 34.204 -3.759  9.993   1.00 15.61 ?  82   VAL   A HG12 1 
ATOM   1849 H  HG13 . VAL   A 1 82  ? 32.715 -4.164  9.611   1.00 15.61 ?  82   VAL   A HG13 1 
ATOM   1850 H  HG21 . VAL   A 1 82  ? 33.783 -6.773  8.344   1.00 15.12 ?  82   VAL   A HG21 1 
ATOM   1851 H  HG22 . VAL   A 1 82  ? 32.561 -6.019  7.663   1.00 15.12 ?  82   VAL   A HG22 1 
ATOM   1852 H  HG23 . VAL   A 1 82  ? 33.893 -6.281  6.838   1.00 15.12 ?  82   VAL   A HG23 1 
ATOM   1853 N  N    . LEU   A 1 83  ? 33.395 -1.368  8.146   1.00 9.85  ?  83   LEU   A N    1 
ATOM   1854 C  CA   . LEU   A 1 83  ? 33.808 -0.100  8.723   1.00 9.78  ?  83   LEU   A CA   1 
ATOM   1855 C  C    . LEU   A 1 83  ? 33.095 0.073   10.059  1.00 9.98  ?  83   LEU   A C    1 
ATOM   1856 O  O    . LEU   A 1 83  ? 32.383 -0.821  10.527  1.00 10.49 ?  83   LEU   A O    1 
ATOM   1857 C  CB   . LEU   A 1 83  ? 33.550 1.059   7.749   1.00 10.28 ?  83   LEU   A CB   1 
ATOM   1858 C  CG   . LEU   A 1 83  ? 34.441 1.060   6.500   1.00 11.19 ?  83   LEU   A CG   1 
ATOM   1859 C  CD1  . LEU   A 1 83  ? 33.991 2.104   5.492   1.00 11.62 ?  83   LEU   A CD1  1 
ATOM   1860 C  CD2  . LEU   A 1 83  ? 35.908 1.286   6.873   1.00 11.88 ?  83   LEU   A CD2  1 
ATOM   1861 H  H    . LEU   A 1 83  ? 32.539 -1.458  8.097   1.00 11.82 ?  83   LEU   A H    1 
ATOM   1862 H  HA   . LEU   A 1 83  ? 34.758 -0.126  8.899   1.00 11.74 ?  83   LEU   A HA   1 
ATOM   1863 H  HB2  . LEU   A 1 83  ? 32.626 1.019   7.448   1.00 12.34 ?  83   LEU   A HB2  1 
ATOM   1864 H  HB3  . LEU   A 1 83  ? 33.698 1.900   8.214   1.00 12.34 ?  83   LEU   A HB3  1 
ATOM   1865 H  HG   . LEU   A 1 83  ? 34.375 0.193   6.075   1.00 13.43 ?  83   LEU   A HG   1 
ATOM   1866 H  HD11 . LEU   A 1 83  ? 34.577 2.063   4.716   1.00 13.94 ?  83   LEU   A HD11 1 
ATOM   1867 H  HD12 . LEU   A 1 83  ? 33.079 1.910   5.223   1.00 13.94 ?  83   LEU   A HD12 1 
ATOM   1868 H  HD13 . LEU   A 1 83  ? 34.040 2.981   5.897   1.00 13.94 ?  83   LEU   A HD13 1 
ATOM   1869 H  HD21 . LEU   A 1 83  ? 36.421 1.438   6.062   1.00 14.26 ?  83   LEU   A HD21 1 
ATOM   1870 H  HD22 . LEU   A 1 83  ? 35.973 2.064   7.452   1.00 14.26 ?  83   LEU   A HD22 1 
ATOM   1871 H  HD23 . LEU   A 1 83  ? 36.244 0.503   7.334   1.00 14.26 ?  83   LEU   A HD23 1 
ATOM   1872 N  N    . SER   A 1 84  ? 33.308 1.221   10.693  1.00 10.54 ?  84   SER   A N    1 
ATOM   1873 C  CA   . SER   A 1 84  ? 32.662 1.472   11.971  1.00 10.76 ?  84   SER   A CA   1 
ATOM   1874 C  C    . SER   A 1 84  ? 31.145 1.555   11.824  1.00 10.50 ?  84   SER   A C    1 
ATOM   1875 O  O    . SER   A 1 84  ? 30.617 2.032   10.820  1.00 10.75 ?  84   SER   A O    1 
ATOM   1876 C  CB   . SER   A 1 84  ? 33.161 2.792   12.548  1.00 11.62 ?  84   SER   A CB   1 
ATOM   1877 O  OG   . SER   A 1 84  ? 32.534 3.063   13.787  1.00 12.47 ?  84   SER   A OG   1 
ATOM   1878 H  H    . SER   A 1 84  ? 33.806 1.863   10.399  1.00 12.65 ?  84   SER   A H    1 
ATOM   1879 H  HA   . SER   A 1 84  ? 32.881 0.758   12.583  1.00 12.91 ?  84   SER   A HA   1 
ATOM   1880 H  HB2  . SER   A 1 84  ? 34.122 2.737   12.675  1.00 13.94 ?  84   SER   A HB2  1 
ATOM   1881 H  HB3  . SER   A 1 84  ? 32.951 3.508   11.926  1.00 13.94 ?  84   SER   A HB3  1 
ATOM   1882 H  HG   . SER   A 1 84  ? 32.821 3.785   14.100  1.00 14.96 ?  84   SER   A HG   1 
ATOM   1883 N  N    . GLY   A 1 85  ? 30.438 1.138   12.872  1.00 11.31 ?  85   GLY   A N    1 
ATOM   1884 C  CA   . GLY   A 1 85  ? 29.015 1.381   12.956  1.00 12.10 ?  85   GLY   A CA   1 
ATOM   1885 C  C    . GLY   A 1 85  ? 28.652 2.687   13.617  1.00 11.46 ?  85   GLY   A C    1 
ATOM   1886 O  O    . GLY   A 1 85  ? 27.463 3.003   13.738  1.00 11.92 ?  85   GLY   A O    1 
ATOM   1887 H  H    . GLY   A 1 85  ? 30.771 0.717   13.545  1.00 13.57 ?  85   GLY   A H    1 
ATOM   1888 H  HA2  . GLY   A 1 85  ? 28.645 1.382   12.061  1.00 14.52 ?  85   GLY   A HA2  1 
ATOM   1889 H  HA3  . GLY   A 1 85  ? 28.605 0.670   13.459  1.00 14.52 ?  85   GLY   A HA3  1 
ATOM   1890 N  N    . HIS   A 1 86  ? 29.642 3.460   14.052  1.00 11.25 ?  86   HIS   A N    1 
ATOM   1891 C  CA   . HIS   A 1 86  ? 29.425 4.792   14.623  1.00 11.73 ?  86   HIS   A CA   1 
ATOM   1892 C  C    . HIS   A 1 86  ? 28.455 4.668   15.789  1.00 12.57 ?  86   HIS   A C    1 
ATOM   1893 O  O    . HIS   A 1 86  ? 28.651 3.793   16.649  1.00 13.63 ?  86   HIS   A O    1 
ATOM   1894 C  CB   . HIS   A 1 86  ? 29.033 5.772   13.527  1.00 11.76 ?  86   HIS   A CB   1 
ATOM   1895 C  CG   . HIS   A 1 86  ? 30.078 5.883   12.480  1.00 11.60 ?  86   HIS   A CG   1 
ATOM   1896 N  ND1  . HIS   A 1 86  ? 31.167 6.717   12.613  1.00 12.60 ?  86   HIS   A ND1  1 
ATOM   1897 C  CD2  . HIS   A 1 86  ? 30.262 5.192   11.333  1.00 11.33 ?  86   HIS   A CD2  1 
ATOM   1898 C  CE1  . HIS   A 1 86  ? 31.959 6.555   11.568  1.00 12.53 ?  86   HIS   A CE1  1 
ATOM   1899 N  NE2  . HIS   A 1 86  ? 31.436 5.632   10.782  1.00 12.10 ?  86   HIS   A NE2  1 
ATOM   1900 H  H    . HIS   A 1 86  ? 30.469 3.235   14.039  1.00 13.50 ?  86   HIS   A H    1 
ATOM   1901 H  HA   . HIS   A 1 86  ? 30.265 5.107   14.991  1.00 14.08 ?  86   HIS   A HA   1 
ATOM   1902 H  HB2  . HIS   A 1 86  ? 28.211 5.476   13.104  1.00 14.11 ?  86   HIS   A HB2  1 
ATOM   1903 H  HB3  . HIS   A 1 86  ? 28.903 6.658   13.913  1.00 14.11 ?  86   HIS   A HB3  1 
ATOM   1904 H  HD2  . HIS   A 1 86  ? 29.699 4.535   10.983  1.00 13.59 ?  86   HIS   A HD2  1 
ATOM   1905 H  HE1  . HIS   A 1 86  ? 32.749 7.019   11.400  1.00 15.03 ?  86   HIS   A HE1  1 
ATOM   1906 H  HE2  . HIS   A 1 86  ? 31.769 5.361   10.031  1.00 14.53 ?  86   HIS   A HE2  1 
ATOM   1907 N  N    . ASN   A 1 87  ? 27.446 5.523   15.874  1.00 13.24 ?  87   ASN   A N    1 
ATOM   1908 C  CA   . ASN   A 1 87  ? 26.462 5.508   16.938  1.00 14.35 ?  87   ASN   A CA   1 
ATOM   1909 C  C    . ASN   A 1 87  ? 25.348 4.499   16.707  1.00 15.32 ?  87   ASN   A C    1 
ATOM   1910 O  O    . ASN   A 1 87  ? 24.444 4.408   17.545  1.00 17.53 ?  87   ASN   A O    1 
ATOM   1911 C  CB   . ASN   A 1 87  ? 25.854 6.911   17.100  1.00 15.22 ?  87   ASN   A CB   1 
ATOM   1912 C  CG   . ASN   A 1 87  ? 25.333 7.490   15.789  1.00 16.08 ?  87   ASN   A CG   1 
ATOM   1913 O  OD1  . ASN   A 1 87  ? 25.982 7.395   14.750  1.00 16.30 ?  87   ASN   A OD1  1 
ATOM   1914 N  ND2  . ASN   A 1 87  ? 24.160 8.102   15.839  1.00 16.86 ?  87   ASN   A ND2  1 
ATOM   1915 H  H    . ASN   A 1 87  ? 27.306 6.145   15.302  1.00 15.89 ?  87   ASN   A H    1 
ATOM   1916 H  HA   . ASN   A 1 87  ? 26.895 5.274   17.773  1.00 17.23 ?  87   ASN   A HA   1 
ATOM   1917 H  HB2  . ASN   A 1 87  ? 25.107 6.861   17.727  1.00 18.27 ?  87   ASN   A HB2  1 
ATOM   1918 H  HB3  . ASN   A 1 87  ? 26.531 7.509   17.449  1.00 18.27 ?  87   ASN   A HB3  1 
ATOM   1919 H  HD21 . ASN   A 1 87  ? 23.826 8.447   15.127  1.00 20.24 ?  87   ASN   A HD21 1 
ATOM   1920 H  HD22 . ASN   A 1 87  ? 23.733 8.160   16.585  1.00 20.24 ?  87   ASN   A HD22 1 
ATOM   1921 N  N    . LEU   A 1 88  ? 25.394 3.736   15.618  1.00 14.07 ?  88   LEU   A N    1 
ATOM   1922 C  CA   . LEU   A 1 88  ? 24.282 2.872   15.232  1.00 14.10 ?  88   LEU   A CA   1 
ATOM   1923 C  C    . LEU   A 1 88  ? 24.505 1.394   15.531  1.00 13.71 ?  88   LEU   A C    1 
ATOM   1924 O  O    . LEU   A 1 88  ? 23.531 0.657   15.716  1.00 14.93 ?  88   LEU   A O    1 
ATOM   1925 C  CB   . LEU   A 1 88  ? 24.020 3.028   13.733  1.00 14.43 ?  88   LEU   A CB   1 
ATOM   1926 C  CG   . LEU   A 1 88  ? 23.701 4.449   13.267  1.00 15.96 ?  88   LEU   A CG   1 
ATOM   1927 C  CD1  . LEU   A 1 88  ? 23.495 4.467   11.764  1.00 16.29 ?  88   LEU   A CD1  1 
ATOM   1928 C  CD2  . LEU   A 1 88  ? 22.476 5.004   13.990  1.00 17.64 ?  88   LEU   A CD2  1 
ATOM   1929 H  H    . LEU   A 1 88  ? 26.069 3.697   15.086  1.00 16.88 ?  88   LEU   A H    1 
ATOM   1930 H  HA   . LEU   A 1 88  ? 23.487 3.154   15.706  1.00 16.92 ?  88   LEU   A HA   1 
ATOM   1931 H  HB2  . LEU   A 1 88  ? 24.806 2.737   13.246  1.00 17.32 ?  88   LEU   A HB2  1 
ATOM   1932 H  HB3  . LEU   A 1 88  ? 23.264 2.472   13.492  1.00 17.32 ?  88   LEU   A HB3  1 
ATOM   1933 H  HG   . LEU   A 1 88  ? 24.455 5.027   13.470  1.00 19.15 ?  88   LEU   A HG   1 
ATOM   1934 H  HD11 . LEU   A 1 88  ? 23.297 5.376   11.481  1.00 19.55 ?  88   LEU   A HD11 1 
ATOM   1935 H  HD12 . LEU   A 1 88  ? 24.305 4.158   11.329  1.00 19.55 ?  88   LEU   A HD12 1 
ATOM   1936 H  HD13 . LEU   A 1 88  ? 22.754 3.884   11.539  1.00 19.55 ?  88   LEU   A HD13 1 
ATOM   1937 H  HD21 . LEU   A 1 88  ? 22.221 5.845   13.576  1.00 21.16 ?  88   LEU   A HD21 1 
ATOM   1938 H  HD22 . LEU   A 1 88  ? 21.753 4.366   13.917  1.00 21.16 ?  88   LEU   A HD22 1 
ATOM   1939 H  HD23 . LEU   A 1 88  ? 22.701 5.151   14.922  1.00 21.16 ?  88   LEU   A HD23 1 
ATOM   1940 N  N    . ALA   A 1 89  ? 25.756 0.947   15.562  1.00 12.87 ?  89   ALA   A N    1 
ATOM   1941 C  CA   . ALA   A 1 89  ? 26.105 -0.463  15.654  1.00 12.54 ?  89   ALA   A CA   1 
ATOM   1942 C  C    . ALA   A 1 89  ? 27.590 -0.518  15.969  1.00 12.94 ?  89   ALA   A C    1 
ATOM   1943 O  O    . ALA   A 1 89  ? 28.296 0.483   15.851  1.00 13.72 ?  89   ALA   A O    1 
ATOM   1944 C  CB   . ALA   A 1 89  ? 25.837 -1.170  14.326  1.00 12.15 ?  89   ALA   A CB   1 
ATOM   1945 H  H    . ALA   A 1 89  ? 26.443 1.463   15.516  1.00 15.44 ?  89   ALA   A H    1 
ATOM   1946 H  HA   . ALA   A 1 89  ? 25.603 -0.891  16.364  1.00 15.04 ?  89   ALA   A HA   1 
ATOM   1947 H  HB1  . ALA   A 1 89  ? 26.093 -2.104  14.410  1.00 14.58 ?  89   ALA   A HB1  1 
ATOM   1948 H  HB2  . ALA   A 1 89  ? 24.891 -1.107  14.117  1.00 14.58 ?  89   ALA   A HB2  1 
ATOM   1949 H  HB3  . ALA   A 1 89  ? 26.360 -0.747  13.629  1.00 14.58 ?  89   ALA   A HB3  1 
ATOM   1950 N  N    . LYS   A 1 90  ? 28.077 -1.696  16.350  1.00 13.43 ?  90   LYS   A N    1 
ATOM   1951 C  CA   . LYS   A 1 90  ? 29.522 -1.831  16.495  1.00 13.88 ?  90   LYS   A CA   1 
ATOM   1952 C  C    . LYS   A 1 90  ? 30.214 -1.643  15.147  1.00 12.95 ?  90   LYS   A C    1 
ATOM   1953 O  O    . LYS   A 1 90  ? 31.143 -0.827  15.013  1.00 14.02 ?  90   LYS   A O    1 
ATOM   1954 C  CB   . LYS   A 1 90  ? 29.870 -3.179  17.125  1.00 16.57 ?  90   LYS   A CB   1 
ATOM   1955 C  CG   . LYS   A 1 90  ? 31.347 -3.320  17.445  1.00 20.65 ?  90   LYS   A CG   1 
ATOM   1956 C  CD   . LYS   A 1 90  ? 31.601 -4.546  18.303  1.00 25.23 ?  90   LYS   A CD   1 
ATOM   1957 C  CE   . LYS   A 1 90  ? 33.011 -4.555  18.870  1.00 28.79 ?  90   LYS   A CE   1 
ATOM   1958 N  NZ   . LYS   A 1 90  ? 34.025 -4.939  17.853  1.00 30.52 ?  90   LYS   A NZ   1 
ATOM   1959 H  H    . LYS   A 1 90  ? 27.615 -2.396  16.522  1.00 16.11 ?  90   LYS   A H    1 
ATOM   1960 H  HA   . LYS   A 1 90  ? 29.843 -1.134  17.087  1.00 16.66 ?  90   LYS   A HA   1 
ATOM   1961 H  HB2  . LYS   A 1 90  ? 29.372 -3.271  17.957  1.00 19.89 ?  90   LYS   A HB2  1 
ATOM   1962 H  HB3  . LYS   A 1 90  ? 29.623 -3.887  16.514  1.00 19.89 ?  90   LYS   A HB3  1 
ATOM   1963 H  HG2  . LYS   A 1 90  ? 31.846 -3.415  16.619  1.00 24.78 ?  90   LYS   A HG2  1 
ATOM   1964 H  HG3  . LYS   A 1 90  ? 31.648 -2.537  17.933  1.00 24.78 ?  90   LYS   A HG3  1 
ATOM   1965 H  HD2  . LYS   A 1 90  ? 30.976 -4.554  19.046  1.00 30.28 ?  90   LYS   A HD2  1 
ATOM   1966 H  HD3  . LYS   A 1 90  ? 31.486 -5.345  17.763  1.00 30.28 ?  90   LYS   A HD3  1 
ATOM   1967 H  HE2  . LYS   A 1 90  ? 33.229 -3.666  19.192  1.00 34.55 ?  90   LYS   A HE2  1 
ATOM   1968 H  HE3  . LYS   A 1 90  ? 33.057 -5.194  19.599  1.00 34.55 ?  90   LYS   A HE3  1 
ATOM   1969 H  HZ1  . LYS   A 1 90  ? 34.836 -4.948  18.221  1.00 36.62 ?  90   LYS   A HZ1  1 
ATOM   1970 H  HZ2  . LYS   A 1 90  ? 33.844 -5.751  17.536  1.00 36.62 ?  90   LYS   A HZ2  1 
ATOM   1971 H  HZ3  . LYS   A 1 90  ? 34.018 -4.357  17.182  1.00 36.62 ?  90   LYS   A HZ3  1 
ATOM   1972 N  N    . HIS   A 1 91  ? 29.741 -2.364  14.127  1.00 11.62 ?  91   HIS   A N    1 
ATOM   1973 C  CA   . HIS   A 1 91  ? 30.308 -2.347  12.792  1.00 11.27 ?  91   HIS   A CA   1 
ATOM   1974 C  C    . HIS   A 1 91  ? 29.215 -2.079  11.774  1.00 10.19 ?  91   HIS   A C    1 
ATOM   1975 O  O    . HIS   A 1 91  ? 28.048 -2.437  11.979  1.00 10.51 ?  91   HIS   A O    1 
ATOM   1976 C  CB   . HIS   A 1 91  ? 30.910 -3.711  12.425  1.00 13.43 ?  91   HIS   A CB   1 
ATOM   1977 C  CG   . HIS   A 1 91  ? 31.885 -4.238  13.427  1.00 17.34 ?  91   HIS   A CG   1 
ATOM   1978 N  ND1  . HIS   A 1 91  ? 33.171 -3.757  13.539  1.00 19.46 ?  91   HIS   A ND1  1 
ATOM   1979 C  CD2  . HIS   A 1 91  ? 31.770 -5.219  14.354  1.00 19.10 ?  91   HIS   A CD2  1 
ATOM   1980 C  CE1  . HIS   A 1 91  ? 33.804 -4.414  14.495  1.00 20.29 ?  91   HIS   A CE1  1 
ATOM   1981 N  NE2  . HIS   A 1 91  ? 32.975 -5.307  15.007  1.00 20.52 ?  91   HIS   A NE2  1 
ATOM   1982 H  H    . HIS   A 1 91  ? 29.065 -2.901  14.200  1.00 13.95 ?  91   HIS   A H    1 
ATOM   1983 H  HA   . HIS   A 1 91  ? 30.989 -1.664  12.723  1.00 13.52 ?  91   HIS   A HA   1 
ATOM   1984 H  HB2  . HIS   A 1 91  ? 30.192 -4.360  12.346  1.00 16.12 ?  91   HIS   A HB2  1 
ATOM   1985 H  HB3  . HIS   A 1 91  ? 31.371 -3.630  11.576  1.00 16.12 ?  91   HIS   A HB3  1 
ATOM   1986 H  HD1  . HIS   A 1 91  ? 33.509 -3.126  13.057  1.00 23.35 ?  91   HIS   A HD1  1 
ATOM   1987 H  HD2  . HIS   A 1 91  ? 31.017 -5.735  14.518  1.00 22.92 ?  91   HIS   A HD2  1 
ATOM   1988 H  HE1  . HIS   A 1 91  ? 34.686 -4.267  14.760  1.00 24.35 ?  91   HIS   A HE1  1 
ATOM   1989 N  N    . CYS   A 1 92  ? 29.612 -1.488  10.651  1.00 9.73  ?  92   CYS   A N    1 
ATOM   1990 C  CA   . CYS   A 1 92  ? 28.765 -1.411  9.471   1.00 9.76  ?  92   CYS   A CA   1 
ATOM   1991 C  C    . CYS   A 1 92  ? 29.413 -2.227  8.364   1.00 9.38  ?  92   CYS   A C    1 
ATOM   1992 O  O    . CYS   A 1 92  ? 30.566 -1.967  7.990   1.00 10.01 ?  92   CYS   A O    1 
ATOM   1993 C  CB   . CYS   A 1 92  ? 28.544 0.031   9.013   1.00 10.31 ?  92   CYS   A CB   1 
ATOM   1994 S  SG   . CYS   A 1 92  ? 27.521 0.131   7.516   1.00 9.65  ?  92   CYS   A SG   1 
ATOM   1995 H  H    . CYS   A 1 92  ? 30.383 -1.115  10.550  1.00 11.67 ?  92   CYS   A H    1 
ATOM   1996 H  HA   . CYS   A 1 92  ? 27.903 -1.801  9.672   1.00 11.72 ?  92   CYS   A HA   1 
ATOM   1997 H  HB2  . CYS   A 1 92  ? 28.095 0.522   9.720   1.00 12.37 ?  92   CYS   A HB2  1 
ATOM   1998 H  HB3  . CYS   A 1 92  ? 29.403 0.438   8.819   1.00 12.37 ?  92   CYS   A HB3  1 
ATOM   1999 H  HG   . CYS   A 1 92  ? 27.375 1.283   7.224   1.00 11.57 ?  92   CYS   A HG   1 
ATOM   2000 N  N    . LEU   A 1 93  ? 28.680 -3.221  7.866   1.00 9.11  ?  93   LEU   A N    1 
ATOM   2001 C  CA   . LEU   A 1 93  ? 29.077 -3.979  6.685   1.00 8.67  ?  93   LEU   A CA   1 
ATOM   2002 C  C    . LEU   A 1 93  ? 28.470 -3.286  5.472   1.00 8.33  ?  93   LEU   A C    1 
ATOM   2003 O  O    . LEU   A 1 93  ? 27.254 -3.353  5.254   1.00 8.53  ?  93   LEU   A O    1 
ATOM   2004 C  CB   . LEU   A 1 93  ? 28.597 -5.425  6.795   1.00 9.22  ?  93   LEU   A CB   1 
ATOM   2005 C  CG   . LEU   A 1 93  ? 28.982 -6.321  5.623   1.00 9.50  ?  93   LEU   A CG   1 
ATOM   2006 C  CD1  . LEU   A 1 93  ? 30.496 -6.562  5.598   1.00 10.59 ?  93   LEU   A CD1  1 
ATOM   2007 C  CD2  . LEU   A 1 93  ? 28.220 -7.647  5.666   1.00 10.74 ?  93   LEU   A CD2  1 
ATOM   2008 H  H    . LEU   A 1 93  ? 27.928 -3.473  8.207   1.00 10.94 ?  93   LEU   A H    1 
ATOM   2009 H  HA   . LEU   A 1 93  ? 30.041 -3.969  6.610   1.00 10.40 ?  93   LEU   A HA   1 
ATOM   2010 H  HB2  . LEU   A 1 93  ? 28.980 -5.814  7.604   1.00 11.07 ?  93   LEU   A HB2  1 
ATOM   2011 H  HB3  . LEU   A 1 93  ? 27.632 -5.428  6.865   1.00 11.07 ?  93   LEU   A HB3  1 
ATOM   2012 H  HG   . LEU   A 1 93  ? 28.749 -5.876  4.801   1.00 11.40 ?  93   LEU   A HG   1 
ATOM   2013 H  HD11 . LEU   A 1 93  ? 30.712 -7.180  4.881   1.00 12.71 ?  93   LEU   A HD11 1 
ATOM   2014 H  HD12 . LEU   A 1 93  ? 30.954 -5.717  5.451   1.00 12.71 ?  93   LEU   A HD12 1 
ATOM   2015 H  HD13 . LEU   A 1 93  ? 30.778 -6.941  6.450   1.00 12.71 ?  93   LEU   A HD13 1 
ATOM   2016 H  HD21 . LEU   A 1 93  ? 28.491 -8.195  4.907   1.00 12.89 ?  93   LEU   A HD21 1 
ATOM   2017 H  HD22 . LEU   A 1 93  ? 28.426 -8.113  6.492   1.00 12.89 ?  93   LEU   A HD22 1 
ATOM   2018 H  HD23 . LEU   A 1 93  ? 27.268 -7.470  5.615   1.00 12.89 ?  93   LEU   A HD23 1 
ATOM   2019 N  N    . HIS   A 1 94  ? 29.311 -2.588  4.712   1.00 8.49  ?  94   HIS   A N    1 
ATOM   2020 C  CA   . HIS   A 1 94  ? 28.886 -1.922  3.488   1.00 8.41  ?  94   HIS   A CA   1 
ATOM   2021 C  C    . HIS   A 1 94  ? 28.894 -2.955  2.376   1.00 8.40  ?  94   HIS   A C    1 
ATOM   2022 O  O    . HIS   A 1 94  ? 29.960 -3.468  2.027   1.00 9.63  ?  94   HIS   A O    1 
ATOM   2023 C  CB   . HIS   A 1 94  ? 29.835 -0.773  3.151   1.00 8.62  ?  94   HIS   A CB   1 
ATOM   2024 C  CG   . HIS   A 1 94  ? 29.822 0.322   4.160   1.00 8.62  ?  94   HIS   A CG   1 
ATOM   2025 N  ND1  . HIS   A 1 94  ? 28.940 1.381   4.106   1.00 8.76  ?  94   HIS   A ND1  1 
ATOM   2026 C  CD2  . HIS   A 1 94  ? 30.562 0.493   5.280   1.00 9.23  ?  94   HIS   A CD2  1 
ATOM   2027 C  CE1  . HIS   A 1 94  ? 29.154 2.162   5.150   1.00 8.82  ?  94   HIS   A CE1  1 
ATOM   2028 N  NE2  . HIS   A 1 94  ? 30.136 1.652   5.871   1.00 9.09  ?  94   HIS   A NE2  1 
ATOM   2029 H  H    . HIS   A 1 94  ? 30.150 -2.480  4.896   1.00 10.19 ?  94   HIS   A H    1 
ATOM   2030 H  HA   . HIS   A 1 94  ? 27.986 -1.580  3.596   1.00 10.09 ?  94   HIS   A HA   1 
ATOM   2031 H  HB2  . HIS   A 1 94  ? 30.735 -1.114  3.089   1.00 10.35 ?  94   HIS   A HB2  1 
ATOM   2032 H  HB3  . HIS   A 1 94  ? 29.563 -0.391  2.298   1.00 10.35 ?  94   HIS   A HB3  1 
ATOM   2033 H  HD2  . HIS   A 1 94  ? 31.242 -0.058  5.588   1.00 11.07 ?  94   HIS   A HD2  1 
ATOM   2034 H  HE1  . HIS   A 1 94  ? 28.688 2.948   5.340   1.00 10.59 ?  94   HIS   A HE1  1 
ATOM   2035 H  HE2  . HIS   A 1 94  ? 30.447 1.997   6.599   1.00 10.91 ?  94   HIS   A HE2  1 
ATOM   2036 N  N    . VAL   A 1 95  ? 27.722 -3.273  1.828   1.00 7.80  ?  95   VAL   A N    1 
ATOM   2037 C  CA   . VAL   A 1 95  ? 27.582 -4.309  0.806   1.00 8.36  ?  95   VAL   A CA   1 
ATOM   2038 C  C    . VAL   A 1 95  ? 27.029 -3.679  -0.458  1.00 7.84  ?  95   VAL   A C    1 
ATOM   2039 O  O    . VAL   A 1 95  ? 26.020 -2.968  -0.402  1.00 8.81  ?  95   VAL   A O    1 
ATOM   2040 C  CB   . VAL   A 1 95  ? 26.664 -5.458  1.264   1.00 9.01  ?  95   VAL   A CB   1 
ATOM   2041 C  CG1  . VAL   A 1 95  ? 26.559 -6.504  0.167   1.00 9.98  ?  95   VAL   A CG1  1 
ATOM   2042 C  CG2  . VAL   A 1 95  ? 27.173 -6.069  2.545   1.00 8.92  ?  95   VAL   A CG2  1 
ATOM   2043 H  H    . VAL   A 1 95  ? 26.975 -2.894  2.037   1.00 9.35  ?  95   VAL   A H    1 
ATOM   2044 H  HA   . VAL   A 1 95  ? 28.452 -4.677  0.604   1.00 10.03 ?  95   VAL   A HA   1 
ATOM   2045 H  HB   . VAL   A 1 95  ? 25.778 -5.111  1.429   1.00 10.81 ?  95   VAL   A HB   1 
ATOM   2046 H  HG11 . VAL   A 1 95  ? 26.181 -7.317  0.537   1.00 11.98 ?  95   VAL   A HG11 1 
ATOM   2047 H  HG12 . VAL   A 1 95  ? 25.993 -6.170  -0.544  1.00 11.98 ?  95   VAL   A HG12 1 
ATOM   2048 H  HG13 . VAL   A 1 95  ? 27.450 -6.691  -0.182  1.00 11.98 ?  95   VAL   A HG13 1 
ATOM   2049 H  HG21 . VAL   A 1 95  ? 26.619 -6.832  2.771   1.00 10.70 ?  95   VAL   A HG21 1 
ATOM   2050 H  HG22 . VAL   A 1 95  ? 28.092 -6.350  2.420   1.00 10.70 ?  95   VAL   A HG22 1 
ATOM   2051 H  HG23 . VAL   A 1 95  ? 27.122 -5.404  3.250   1.00 10.70 ?  95   VAL   A HG23 1 
ATOM   2052 N  N    . VAL   A 1 96  ? 27.653 -3.968  -1.596  1.00 8.10  ?  96   VAL   A N    1 
ATOM   2053 C  CA   . VAL   A 1 96  ? 27.233 -3.419  -2.878  1.00 8.77  ?  96   VAL   A CA   1 
ATOM   2054 C  C    . VAL   A 1 96  ? 26.433 -4.469  -3.640  1.00 9.17  ?  96   VAL   A C    1 
ATOM   2055 O  O    . VAL   A 1 96  ? 26.994 -5.415  -4.200  1.00 10.00 ?  96   VAL   A O    1 
ATOM   2056 C  CB   . VAL   A 1 96  ? 28.420 -2.930  -3.712  1.00 9.38  ?  96   VAL   A CB   1 
ATOM   2057 C  CG1  . VAL   A 1 96  ? 27.906 -2.298  -4.989  1.00 9.33  ?  96   VAL   A CG1  1 
ATOM   2058 C  CG2  . VAL   A 1 96  ? 29.273 -1.946  -2.921  1.00 10.07 ?  96   VAL   A CG2  1 
ATOM   2059 H  H    . VAL   A 1 96  ? 28.344 -4.487  -1.651  1.00 9.71  ?  96   VAL   A H    1 
ATOM   2060 H  HA   . VAL   A 1 96  ? 26.654 -2.662  -2.721  1.00 10.52 ?  96   VAL   A HA   1 
ATOM   2061 H  HB   . VAL   A 1 96  ? 28.974 -3.686  -3.954  1.00 11.25 ?  96   VAL   A HB   1 
ATOM   2062 H  HG11 . VAL   A 1 96  ? 28.638 -1.817  -5.412  1.00 11.19 ?  96   VAL   A HG11 1 
ATOM   2063 H  HG12 . VAL   A 1 96  ? 27.582 -2.989  -5.581  1.00 11.19 ?  96   VAL   A HG12 1 
ATOM   2064 H  HG13 . VAL   A 1 96  ? 27.193 -1.678  -4.770  1.00 11.19 ?  96   VAL   A HG13 1 
ATOM   2065 H  HG21 . VAL   A 1 96  ? 29.975 -1.600  -3.496  1.00 12.09 ?  96   VAL   A HG21 1 
ATOM   2066 H  HG22 . VAL   A 1 96  ? 28.712 -1.215  -2.612  1.00 12.09 ?  96   VAL   A HG22 1 
ATOM   2067 H  HG23 . VAL   A 1 96  ? 29.665 -2.403  -2.161  1.00 12.09 ?  96   VAL   A HG23 1 
ATOM   2068 N  N    A GLY   A 1 97  ? 25.114 -4.314  -3.643  0.50 9.33  ?  97   GLY   A N    1 
ATOM   2069 N  N    B GLY   A 1 97  ? 25.116 -4.306  -3.702  0.50 9.06  ?  97   GLY   A N    1 
ATOM   2070 C  CA   A GLY   A 1 97  ? 24.274 -5.053  -4.549  0.50 9.82  ?  97   GLY   A CA   1 
ATOM   2071 C  CA   B GLY   A 1 97  ? 24.319 -5.101  -4.604  0.50 9.38  ?  97   GLY   A CA   1 
ATOM   2072 C  C    A GLY   A 1 97  ? 24.238 -4.355  -5.892  0.50 9.37  ?  97   GLY   A C    1 
ATOM   2073 C  C    B GLY   A 1 97  ? 24.359 -4.513  -6.002  0.50 9.55  ?  97   GLY   A C    1 
ATOM   2074 O  O    A GLY   A 1 97  ? 24.508 -3.154  -5.994  0.50 9.94  ?  97   GLY   A O    1 
ATOM   2075 O  O    B GLY   A 1 97  ? 24.659 -3.327  -6.184  0.50 10.31 ?  97   GLY   A O    1 
ATOM   2076 H  H    A GLY   A 1 97  ? 24.685 -3.778  -3.120  0.50 11.20 ?  97   GLY   A H    1 
ATOM   2077 H  H    B GLY   A 1 97  ? 24.667 -3.742  -3.227  0.50 10.87 ?  97   GLY   A H    1 
ATOM   2078 H  HA2  A GLY   A 1 97  ? 24.622 -5.950  -4.654  0.50 11.79 ?  97   GLY   A HA2  1 
ATOM   2079 H  HA2  B GLY   A 1 97  ? 24.667 -6.007  -4.630  0.50 11.26 ?  97   GLY   A HA2  1 
ATOM   2080 H  HA3  A GLY   A 1 97  ? 23.370 -5.103  -4.196  0.50 11.79 ?  97   GLY   A HA3  1 
ATOM   2081 H  HA3  B GLY   A 1 97  ? 23.399 -5.133  -4.288  0.50 11.26 ?  97   GLY   A HA3  1 
ATOM   2082 N  N    A PRO   A 1 98  ? 23.899 -5.086  -6.951  0.50 8.64  ?  98   PRO   A N    1 
ATOM   2083 N  N    B PRO   A 1 98  ? 24.066 -5.321  -7.020  0.50 10.33 ?  98   PRO   A N    1 
ATOM   2084 C  CA   A PRO   A 1 98  ? 23.787 -4.454  -8.269  0.50 9.25  ?  98   PRO   A CA   1 
ATOM   2085 C  CA   B PRO   A 1 98  ? 24.003 -4.785  -8.384  0.50 11.23 ?  98   PRO   A CA   1 
ATOM   2086 C  C    A PRO   A 1 98  ? 22.679 -3.411  -8.293  0.50 9.27  ?  98   PRO   A C    1 
ATOM   2087 C  C    B PRO   A 1 98  ? 22.890 -3.755  -8.522  0.50 11.79 ?  98   PRO   A C    1 
ATOM   2088 O  O    A PRO   A 1 98  ? 21.607 -3.600  -7.714  0.50 9.16  ?  98   PRO   A O    1 
ATOM   2089 O  O    B PRO   A 1 98  ? 21.810 -3.889  -7.945  0.50 12.23 ?  98   PRO   A O    1 
ATOM   2090 C  CB   A PRO   A 1 98  ? 23.469 -5.630  -9.200  0.50 9.55  ?  98   PRO   A CB   1 
ATOM   2091 C  CB   B PRO   A 1 98  ? 23.730 -6.026  -9.242  0.50 11.09 ?  98   PRO   A CB   1 
ATOM   2092 C  CG   A PRO   A 1 98  ? 22.836 -6.664  -8.306  0.50 9.50  ?  98   PRO   A CG   1 
ATOM   2093 C  CG   B PRO   A 1 98  ? 23.095 -7.004  -8.301  0.50 11.46 ?  98   PRO   A CG   1 
ATOM   2094 C  CD   A PRO   A 1 98  ? 23.550 -6.519  -6.985  0.50 8.69  ?  98   PRO   A CD   1 
ATOM   2095 C  CD   B PRO   A 1 98  ? 23.781 -6.765  -6.984  0.50 10.62 ?  98   PRO   A CD   1 
ATOM   2096 H  HA   A PRO   A 1 98  ? 24.628 -4.052  -8.516  0.50 11.10 ?  98   PRO   A HA   1 
ATOM   2097 H  HA   B PRO   A 1 98  ? 24.853 -4.390  -8.635  0.50 13.48 ?  98   PRO   A HA   1 
ATOM   2098 H  HB2  A PRO   A 1 98  ? 22.844 -5.345  -9.884  0.50 11.45 ?  98   PRO   A HB2  1 
ATOM   2099 H  HB2  B PRO   A 1 98  ? 23.123 -5.795  -9.962  0.50 13.31 ?  98   PRO   A HB2  1 
ATOM   2100 H  HB3  A PRO   A 1 98  ? 24.285 -5.969  -9.592  0.50 11.45 ?  98   PRO   A HB3  1 
ATOM   2101 H  HB3  B PRO   A 1 98  ? 24.565 -6.373  -9.590  0.50 13.31 ?  98   PRO   A HB3  1 
ATOM   2102 H  HG2  A PRO   A 1 98  ? 21.889 -6.484  -8.208  0.50 11.40 ?  98   PRO   A HG2  1 
ATOM   2103 H  HG2  B PRO   A 1 98  ? 22.144 -6.823  -8.232  0.50 13.76 ?  98   PRO   A HG2  1 
ATOM   2104 H  HG3  A PRO   A 1 98  ? 22.980 -7.551  -8.677  0.50 11.40 ?  98   PRO   A HG3  1 
ATOM   2105 H  HG3  B PRO   A 1 98  ? 23.251 -7.908  -8.615  0.50 13.76 ?  98   PRO   A HG3  1 
ATOM   2106 H  HD2  A PRO   A 1 98  ? 22.954 -6.754  -6.249  0.50 10.43 ?  98   PRO   A HD2  1 
ATOM   2107 H  HD2  B PRO   A 1 98  ? 23.188 -6.979  -6.246  0.50 12.74 ?  98   PRO   A HD2  1 
ATOM   2108 H  HD3  A PRO   A 1 98  ? 24.357 -7.059  -6.967  0.50 10.43 ?  98   PRO   A HD3  1 
ATOM   2109 H  HD3  B PRO   A 1 98  ? 24.608 -7.276  -6.932  0.50 12.74 ?  98   PRO   A HD3  1 
ATOM   2110 N  N    A ASN   A 1 99  ? 22.953 -2.300  -8.970  0.50 10.30 ?  99   ASN   A N    1 
ATOM   2111 N  N    B ASN   A 1 99  ? 23.169 -2.718  -9.300  0.50 12.16 ?  99   ASN   A N    1 
ATOM   2112 C  CA   A ASN   A 1 99  ? 21.975 -1.240  -9.187  0.50 11.33 ?  99   ASN   A CA   1 
ATOM   2113 C  CA   B ASN   A 1 99  ? 22.208 -1.662  -9.588  0.50 13.25 ?  99   ASN   A CA   1 
ATOM   2114 C  C    A ASN   A 1 99  ? 21.421 -1.394  -10.600 0.50 12.32 ?  99   ASN   A C    1 
ATOM   2115 C  C    B ASN   A 1 99  ? 21.591 -1.961  -10.949 0.50 14.00 ?  99   ASN   A C    1 
ATOM   2116 O  O    A ASN   A 1 99  ? 22.105 -1.086  -11.586 0.50 13.52 ?  99   ASN   A O    1 
ATOM   2117 O  O    B ASN   A 1 99  ? 22.250 -1.819  -11.983 0.50 13.68 ?  99   ASN   A O    1 
ATOM   2118 C  CB   A ASN   A 1 99  ? 22.620 0.130   -8.993  0.50 11.46 ?  99   ASN   A CB   1 
ATOM   2119 C  CB   B ASN   A 1 99  ? 22.905 -0.305  -9.588  0.50 14.19 ?  99   ASN   A CB   1 
ATOM   2120 C  CG   A ASN   A 1 99  ? 21.606 1.264   -8.992  0.50 11.58 ?  99   ASN   A CG   1 
ATOM   2121 C  CG   B ASN   A 1 99  ? 21.951 0.843   -9.836  0.50 15.32 ?  99   ASN   A CG   1 
ATOM   2122 O  OD1  A ASN   A 1 99  ? 20.612 1.221   -9.715  0.50 12.22 ?  99   ASN   A OD1  1 
ATOM   2123 O  OD1  B ASN   A 1 99  ? 20.984 0.711   -10.583 0.50 15.41 ?  99   ASN   A OD1  1 
ATOM   2124 N  ND2  A ASN   A 1 99  ? 21.861 2.286   -8.183  0.50 12.09 ?  99   ASN   A ND2  1 
ATOM   2125 N  ND2  B ASN   A 1 99  ? 22.219 1.981   -9.206  0.50 16.36 ?  99   ASN   A ND2  1 
ATOM   2126 H  H    A ASN   A 1 99  ? 23.723 -2.132  -9.302  0.50 12.36 ?  99   ASN   A H    1 
ATOM   2127 H  H    B ASN   A 1 99  ? 23.934 -2.598  -9.672  0.50 14.59 ?  99   ASN   A H    1 
ATOM   2128 H  HA   A ASN   A 1 99  ? 21.246 -1.335  -8.542  0.50 13.60 ?  99   ASN   A HA   1 
ATOM   2129 H  HA   B ASN   A 1 99  ? 21.506 -1.663  -8.915  0.50 15.90 ?  99   ASN   A HA   1 
ATOM   2130 H  HB2  A ASN   A 1 99  ? 23.094 0.144   -8.149  0.50 13.75 ?  99   ASN   A HB2  1 
ATOM   2131 H  HB2  B ASN   A 1 99  ? 23.325 -0.169  -8.726  0.50 17.02 ?  99   ASN   A HB2  1 
ATOM   2132 H  HB3  A ASN   A 1 99  ? 23.239 0.283   -9.725  0.50 13.75 ?  99   ASN   A HB3  1 
ATOM   2133 H  HB3  B ASN   A 1 99  ? 23.572 -0.300  -10.290 0.50 17.02 ?  99   ASN   A HB3  1 
ATOM   2134 H  HD21 A ASN   A 1 99  ? 21.318 2.950   -8.144  0.50 14.51 ?  99   ASN   A HD21 1 
ATOM   2135 H  HD21 B ASN   A 1 99  ? 21.710 2.662   -9.314  0.50 19.63 ?  99   ASN   A HD21 1 
ATOM   2136 H  HD22 A ASN   A 1 99  ? 22.568 2.277   -7.693  0.50 14.51 ?  99   ASN   A HD22 1 
ATOM   2137 H  HD22 B ASN   A 1 99  ? 22.907 2.032   -8.690  0.50 19.63 ?  99   ASN   A HD22 1 
ATOM   2138 N  N    A VAL   A 1 100 ? 20.178 -1.884  -10.689 0.50 13.16 ?  100  VAL   A N    1 
ATOM   2139 N  N    B VAL   A 1 100 ? 20.326 -2.387  -10.936 0.50 15.97 ?  100  VAL   A N    1 
ATOM   2140 C  CA   A VAL   A 1 100 ? 19.548 -2.130  -11.984 0.50 15.15 ?  100  VAL   A CA   1 
ATOM   2141 C  CA   B VAL   A 1 100 ? 19.644 -2.786  -12.163 0.50 18.03 ?  100  VAL   A CA   1 
ATOM   2142 C  C    A VAL   A 1 100 ? 19.437 -0.840  -12.781 0.50 15.80 ?  100  VAL   A C    1 
ATOM   2143 C  C    B VAL   A 1 100 ? 19.490 -1.607  -13.113 0.50 18.52 ?  100  VAL   A C    1 
ATOM   2144 O  O    A VAL   A 1 100 ? 19.510 -0.853  -14.017 0.50 16.26 ?  100  VAL   A O    1 
ATOM   2145 O  O    B VAL   A 1 100 ? 19.467 -1.785  -14.337 0.50 18.54 ?  100  VAL   A O    1 
ATOM   2146 C  CB   A VAL   A 1 100 ? 18.176 -2.814  -11.789 0.50 16.86 ?  100  VAL   A CB   1 
ATOM   2147 C  CB   B VAL   A 1 100 ? 18.288 -3.430  -11.809 0.50 19.53 ?  100  VAL   A CB   1 
ATOM   2148 C  CG1  A VAL   A 1 100 ? 17.462 -2.988  -13.122 0.50 17.58 ?  100  VAL   A CG1  1 
ATOM   2149 C  CG1  B VAL   A 1 100 ? 17.472 -3.699  -13.062 0.50 20.14 ?  100  VAL   A CG1  1 
ATOM   2150 C  CG2  A VAL   A 1 100 ? 18.344 -4.165  -11.102 0.50 17.29 ?  100  VAL   A CG2  1 
ATOM   2151 C  CG2  B VAL   A 1 100 ? 18.508 -4.712  -11.024 0.50 20.00 ?  100  VAL   A CG2  1 
ATOM   2152 H  H    A VAL   A 1 100 ? 19.679 -2.091  -10.004 0.50 15.79 ?  100  VAL   A H    1 
ATOM   2153 H  H    B VAL   A 1 100 ? 19.847 -2.466  -10.224 0.50 19.17 ?  100  VAL   A H    1 
ATOM   2154 H  HA   A VAL   A 1 100 ? 20.105 -2.749  -12.481 0.50 18.19 ?  100  VAL   A HA   1 
ATOM   2155 H  HA   B VAL   A 1 100 ? 20.179 -3.461  -12.611 0.50 21.64 ?  100  VAL   A HA   1 
ATOM   2156 H  HB   A VAL   A 1 100 ? 17.618 -2.263  -11.221 0.50 20.23 ?  100  VAL   A HB   1 
ATOM   2157 H  HB   B VAL   A 1 100 ? 17.787 -2.815  -11.250 0.50 23.43 ?  100  VAL   A HB   1 
ATOM   2158 H  HG11 A VAL   A 1 100 ? 16.710 -3.592  -13.003 0.50 21.09 ?  100  VAL   A HG11 1 
ATOM   2159 H  HG11 B VAL   A 1 100 ? 16.732 -4.284  -12.833 0.50 24.16 ?  100  VAL   A HG11 1 
ATOM   2160 H  HG12 A VAL   A 1 100 ? 17.145 -2.125  -13.426 0.50 21.09 ?  100  VAL   A HG12 1 
ATOM   2161 H  HG12 B VAL   A 1 100 ? 17.131 -2.859  -13.409 0.50 24.16 ?  100  VAL   A HG12 1 
ATOM   2162 H  HG13 A VAL   A 1 100 ? 18.083 -3.363  -13.766 0.50 21.09 ?  100  VAL   A HG13 1 
ATOM   2163 H  HG13 B VAL   A 1 100 ? 18.038 -4.127  -13.723 0.50 24.16 ?  100  VAL   A HG13 1 
ATOM   2164 H  HG21 A VAL   A 1 100 ? 17.477 -4.599  -11.033 0.50 20.75 ?  100  VAL   A HG21 1 
ATOM   2165 H  HG21 B VAL   A 1 100 ? 17.649 -5.121  -10.846 0.50 23.99 ?  100  VAL   A HG21 1 
ATOM   2166 H  HG22 A VAL   A 1 100 ? 18.945 -4.717  -11.628 0.50 20.75 ?  100  VAL   A HG22 1 
ATOM   2167 H  HG22 B VAL   A 1 100 ? 19.060 -5.311  -11.551 0.50 23.99 ?  100  VAL   A HG22 1 
ATOM   2168 H  HG23 A VAL   A 1 100 ? 18.713 -4.027  -10.215 0.50 20.75 ?  100  VAL   A HG23 1 
ATOM   2169 H  HG23 B VAL   A 1 100 ? 18.954 -4.498  -10.190 0.50 23.99 ?  100  VAL   A HG23 1 
ATOM   2170 N  N    A ASN   A 1 101 ? 19.255 0.290   -12.102 0.50 16.53 ?  101  ASN   A N    1 
ATOM   2171 N  N    B ASN   A 1 101 ? 19.376 -0.389  -12.579 0.50 19.08 ?  101  ASN   A N    1 
ATOM   2172 C  CA   A ASN   A 1 101 ? 19.194 1.568   -12.798 0.50 17.71 ?  101  ASN   A CA   1 
ATOM   2173 C  CA   B ASN   A 1 101 ? 19.245 0.782   -13.437 0.50 20.02 ?  101  ASN   A CA   1 
ATOM   2174 C  C    A ASN   A 1 101 ? 20.552 2.008   -13.346 0.50 19.36 ?  101  ASN   A C    1 
ATOM   2175 C  C    B ASN   A 1 101 ? 20.515 1.056   -14.230 0.50 20.75 ?  101  ASN   A C    1 
ATOM   2176 O  O    A ASN   A 1 101 ? 20.625 3.054   -14.004 0.50 20.68 ?  101  ASN   A O    1 
ATOM   2177 O  O    B ASN   A 1 101 ? 20.449 1.723   -15.267 0.50 20.70 ?  101  ASN   A O    1 
ATOM   2178 C  CB   A ASN   A 1 101 ? 18.576 2.621   -11.876 0.50 17.17 ?  101  ASN   A CB   1 
ATOM   2179 C  CB   B ASN   A 1 101 ? 18.883 2.009   -12.601 0.50 20.08 ?  101  ASN   A CB   1 
ATOM   2180 C  CG   A ASN   A 1 101 ? 17.207 2.201   -11.349 0.50 16.80 ?  101  ASN   A CG   1 
ATOM   2181 C  CG   B ASN   A 1 101 ? 17.618 1.808   -11.787 0.50 20.77 ?  101  ASN   A CG   1 
ATOM   2182 O  OD1  A ASN   A 1 101 ? 16.366 1.693   -12.097 0.50 17.22 ?  101  ASN   A OD1  1 
ATOM   2183 O  OD1  B ASN   A 1 101 ? 16.633 1.246   -12.270 0.50 21.69 ?  101  ASN   A OD1  1 
ATOM   2184 N  ND2  A ASN   A 1 101 ? 16.985 2.397   -10.054 0.50 16.46 ?  101  ASN   A ND2  1 
ATOM   2185 N  ND2  B ASN   A 1 101 ? 17.643 2.256   -10.539 0.50 21.01 ?  101  ASN   A ND2  1 
ATOM   2186 H  H    A ASN   A 1 101 ? 19.155 0.335   -11.248 0.50 19.83 ?  101  ASN   A H    1 
ATOM   2187 H  H    B ASN   A 1 101 ? 19.374 -0.217  -11.736 0.50 22.89 ?  101  ASN   A H    1 
ATOM   2188 H  HA   A ASN   A 1 101 ? 18.600 1.461   -13.555 0.50 21.25 ?  101  ASN   A HA   1 
ATOM   2189 H  HA   B ASN   A 1 101 ? 18.523 0.628   -14.065 0.50 24.02 ?  101  ASN   A HA   1 
ATOM   2190 H  HB2  A ASN   A 1 101 ? 19.161 2.766   -11.120 0.50 20.61 ?  101  ASN   A HB2  1 
ATOM   2191 H  HB2  B ASN   A 1 101 ? 19.609 2.202   -11.988 0.50 24.10 ?  101  ASN   A HB2  1 
ATOM   2192 H  HB3  A ASN   A 1 101 ? 18.464 3.445   -12.377 0.50 20.61 ?  101  ASN   A HB3  1 
ATOM   2193 H  HB3  B ASN   A 1 101 ? 18.743 2.766   -13.195 0.50 24.10 ?  101  ASN   A HB3  1 
ATOM   2194 H  HD21 A ASN   A 1 101 ? 16.228 2.177   -9.709  0.50 19.75 ?  101  ASN   A HD21 1 
ATOM   2195 H  HD21 B ASN   A 1 101 ? 16.950 2.166   -10.040 0.50 25.21 ?  101  ASN   A HD21 1 
ATOM   2196 H  HD22 A ASN   A 1 101 ? 17.593 2.755   -9.563  0.50 19.75 ?  101  ASN   A HD22 1 
ATOM   2197 H  HD22 B ASN   A 1 101 ? 18.349 2.641   -10.234 0.50 25.21 ?  101  ASN   A HD22 1 
ATOM   2198 N  N    A LYS   A 1 102 ? 21.612 1.231   -13.101 0.50 20.71 ?  102  LYS   A N    1 
ATOM   2199 N  N    B LYS   A 1 102 ? 21.663 0.572   -13.761 0.50 22.16 ?  102  LYS   A N    1 
ATOM   2200 C  CA   A LYS   A 1 102 ? 22.904 1.407   -13.752 0.50 21.93 ?  102  LYS   A CA   1 
ATOM   2201 C  CA   B LYS   A 1 102 ? 22.926 0.694   -14.476 0.50 22.97 ?  102  LYS   A CA   1 
ATOM   2202 C  C    A LYS   A 1 102 ? 23.211 0.303   -14.754 0.50 22.17 ?  102  LYS   A C    1 
ATOM   2203 C  C    B LYS   A 1 102 ? 23.243 -0.532  -15.328 0.50 22.21 ?  102  LYS   A C    1 
ATOM   2204 O  O    A LYS   A 1 102 ? 24.304 0.298   -15.330 0.50 22.67 ?  102  LYS   A O    1 
ATOM   2205 O  O    B LYS   A 1 102 ? 24.367 -0.651  -15.825 0.50 22.25 ?  102  LYS   A O    1 
ATOM   2206 C  CB   A LYS   A 1 102 ? 24.029 1.455   -12.711 0.50 23.26 ?  102  LYS   A CB   1 
ATOM   2207 C  CB   B LYS   A 1 102 ? 24.079 0.925   -13.495 0.50 25.41 ?  102  LYS   A CB   1 
ATOM   2208 C  CG   A LYS   A 1 102 ? 23.928 2.599   -11.723 0.50 24.11 ?  102  LYS   A CG   1 
ATOM   2209 C  CG   B LYS   A 1 102 ? 23.985 2.197   -12.674 0.50 27.82 ?  102  LYS   A CG   1 
ATOM   2210 C  CD   A LYS   A 1 102 ? 25.077 2.555   -10.728 0.50 25.00 ?  102  LYS   A CD   1 
ATOM   2211 C  CD   B LYS   A 1 102 ? 25.377 2.668   -12.274 0.50 30.15 ?  102  LYS   A CD   1 
ATOM   2212 C  CE   A LYS   A 1 102 ? 25.045 3.742   -9.780  0.50 25.86 ?  102  LYS   A CE   1 
ATOM   2213 C  CE   B LYS   A 1 102 ? 25.366 3.402   -10.947 0.50 31.93 ?  102  LYS   A CE   1 
ATOM   2214 N  NZ   A LYS   A 1 102 ? 26.131 3.663   -8.761  0.50 26.21 ?  102  LYS   A NZ   1 
ATOM   2215 N  NZ   B LYS   A 1 102 ? 25.113 2.469   -9.814  0.50 32.98 ?  102  LYS   A NZ   1 
ATOM   2216 H  H    A LYS   A 1 102 ? 21.605 0.572   -12.542 0.50 24.86 ?  102  LYS   A H    1 
ATOM   2217 H  H    B LYS   A 1 102 ? 21.733 0.168   -13.009 0.50 26.59 ?  102  LYS   A H    1 
ATOM   2218 H  HA   A LYS   A 1 102 ? 22.903 2.244   -14.232 0.50 26.32 ?  102  LYS   A HA   1 
ATOM   2219 H  HA   B LYS   A 1 102 ? 22.882 1.471   -15.049 0.50 27.56 ?  102  LYS   A HA   1 
ATOM   2220 H  HB2  A LYS   A 1 102 ? 24.018 0.627   -12.204 0.50 27.91 ?  102  LYS   A HB2  1 
ATOM   2221 H  HB2  B LYS   A 1 102 ? 24.109 0.181   -12.876 0.50 30.49 ?  102  LYS   A HB2  1 
ATOM   2222 H  HB3  A LYS   A 1 102 ? 24.876 1.541   -13.176 0.50 27.91 ?  102  LYS   A HB3  1 
ATOM   2223 H  HB3  B LYS   A 1 102 ? 24.907 0.965   -13.998 0.50 30.49 ?  102  LYS   A HB3  1 
ATOM   2224 H  HG2  A LYS   A 1 102 ? 23.968 3.442   -12.202 0.50 28.93 ?  102  LYS   A HG2  1 
ATOM   2225 H  HG2  B LYS   A 1 102 ? 23.564 2.895   -13.201 0.50 33.38 ?  102  LYS   A HG2  1 
ATOM   2226 H  HG3  A LYS   A 1 102 ? 23.094 2.529   -11.233 0.50 28.93 ?  102  LYS   A HG3  1 
ATOM   2227 H  HG3  B LYS   A 1 102 ? 23.473 2.027   -11.868 0.50 33.38 ?  102  LYS   A HG3  1 
ATOM   2228 H  HD2  A LYS   A 1 102 ? 25.012 1.743   -10.201 0.50 30.00 ?  102  LYS   A HD2  1 
ATOM   2229 H  HD2  B LYS   A 1 102 ? 25.963 1.899   -12.190 0.50 36.18 ?  102  LYS   A HD2  1 
ATOM   2230 H  HD3  A LYS   A 1 102 ? 25.918 2.573   -11.212 0.50 30.00 ?  102  LYS   A HD3  1 
ATOM   2231 H  HD3  B LYS   A 1 102 ? 25.717 3.273   -12.953 0.50 36.18 ?  102  LYS   A HD3  1 
ATOM   2232 H  HE2  A LYS   A 1 102 ? 25.166 4.560   -10.289 0.50 31.03 ?  102  LYS   A HE2  1 
ATOM   2233 H  HE2  B LYS   A 1 102 ? 26.229 3.824   -10.808 0.50 38.32 ?  102  LYS   A HE2  1 
ATOM   2234 H  HE3  A LYS   A 1 102 ? 24.193 3.759   -9.317  0.50 31.03 ?  102  LYS   A HE3  1 
ATOM   2235 H  HE3  B LYS   A 1 102 ? 24.663 4.069   -10.956 0.50 38.32 ?  102  LYS   A HE3  1 
ATOM   2236 H  HZ1  A LYS   A 1 102 ? 26.091 4.368   -8.220  0.50 31.46 ?  102  LYS   A HZ1  1 
ATOM   2237 H  HZ1  B LYS   A 1 102 ? 24.877 2.926   -9.089  0.50 39.58 ?  102  LYS   A HZ1  1 
ATOM   2238 H  HZ2  A LYS   A 1 102 ? 26.039 2.921   -8.279  0.50 31.46 ?  102  LYS   A HZ2  1 
ATOM   2239 H  HZ2  B LYS   A 1 102 ? 24.459 1.904   -10.027 0.50 39.58 ?  102  LYS   A HZ2  1 
ATOM   2240 H  HZ3  A LYS   A 1 102 ? 26.924 3.651   -9.164  0.50 31.46 ?  102  LYS   A HZ3  1 
ATOM   2241 H  HZ3  B LYS   A 1 102 ? 25.849 2.000   -9.637  0.50 39.58 ?  102  LYS   A HZ3  1 
ATOM   2242 N  N    A GLY   A 1 103 ? 22.291 -0.634  -14.970 0.50 22.48 ?  103  GLY   A N    1 
ATOM   2243 N  N    B GLY   A 1 103 ? 22.291 -1.448  -15.494 0.50 21.60 ?  103  GLY   A N    1 
ATOM   2244 C  CA   A GLY   A 1 103 ? 22.536 -1.732  -15.883 0.50 22.92 ?  103  GLY   A CA   1 
ATOM   2245 C  CA   B GLY   A 1 103 ? 22.538 -2.647  -16.273 0.50 21.07 ?  103  GLY   A CA   1 
ATOM   2246 C  C    A GLY   A 1 103 ? 23.446 -2.808  -15.338 0.50 23.00 ?  103  GLY   A C    1 
ATOM   2247 C  C    B GLY   A 1 103 ? 23.420 -3.678  -15.602 0.50 19.67 ?  103  GLY   A C    1 
ATOM   2248 O  O    A GLY   A 1 103 ? 24.101 -3.504  -16.120 0.50 23.59 ?  103  GLY   A O    1 
ATOM   2249 O  O    B GLY   A 1 103 ? 23.906 -4.594  -16.270 0.50 20.30 ?  103  GLY   A O    1 
ATOM   2250 H  H    A GLY   A 1 103 ? 21.518 -0.660  -14.599 0.50 26.98 ?  103  GLY   A H    1 
ATOM   2251 H  H    B GLY   A 1 103 ? 21.494 -1.385  -15.178 0.50 25.92 ?  103  GLY   A H    1 
ATOM   2252 H  HA2  A GLY   A 1 103 ? 21.686 -2.134  -16.138 0.50 27.51 ?  103  GLY   A HA2  1 
ATOM   2253 H  HA2  B GLY   A 1 103 ? 21.691 -3.071  -16.471 0.50 25.29 ?  103  GLY   A HA2  1 
ATOM   2254 H  HA3  A GLY   A 1 103 ? 22.958 -1.396  -16.686 0.50 27.51 ?  103  GLY   A HA3  1 
ATOM   2255 H  HA3  B GLY   A 1 103 ? 22.943 -2.389  -17.120 0.50 25.29 ?  103  GLY   A HA3  1 
ATOM   2256 N  N    A GLU   A 1 104 ? 23.521 -2.957  -14.019 0.50 22.16 ?  104  GLU   A N    1 
ATOM   2257 N  N    B GLU   A 1 104 ? 23.634 -3.566  -14.296 0.50 18.03 ?  104  GLU   A N    1 
ATOM   2258 C  CA   A GLU   A 1 104 ? 24.401 -3.944  -13.413 0.50 21.27 ?  104  GLU   A CA   1 
ATOM   2259 C  CA   B GLU   A 1 104 ? 24.521 -4.487  -13.602 0.50 16.20 ?  104  GLU   A CA   1 
ATOM   2260 C  C    A GLU   A 1 104 ? 23.719 -5.305  -13.315 0.50 21.84 ?  104  GLU   A C    1 
ATOM   2261 C  C    B GLU   A 1 104 ? 23.847 -5.845  -13.419 0.50 15.62 ?  104  GLU   A C    1 
ATOM   2262 O  O    A GLU   A 1 104 ? 22.506 -5.407  -13.110 0.50 22.28 ?  104  GLU   A O    1 
ATOM   2263 O  O    B GLU   A 1 104 ? 22.625 -5.947  -13.282 0.50 16.52 ?  104  GLU   A O    1 
ATOM   2264 C  CB   A GLU   A 1 104 ? 24.888 -3.456  -12.046 0.50 20.19 ?  104  GLU   A CB   1 
ATOM   2265 C  CB   B GLU   A 1 104 ? 24.971 -3.888  -12.266 0.50 15.72 ?  104  GLU   A CB   1 
ATOM   2266 C  CG   A GLU   A 1 104 ? 25.877 -2.296  -12.188 0.50 19.65 ?  104  GLU   A CG   1 
ATOM   2267 C  CG   B GLU   A 1 104 ? 25.782 -2.602  -12.461 0.50 16.15 ?  104  GLU   A CG   1 
ATOM   2268 C  CD   A GLU   A 1 104 ? 26.215 -1.577  -10.893 0.50 19.08 ?  104  GLU   A CD   1 
ATOM   2269 C  CD   B GLU   A 1 104 ? 26.165 -1.874  -11.182 0.50 16.08 ?  104  GLU   A CD   1 
ATOM   2270 O  OE1  A GLU   A 1 104 ? 25.557 -1.821  -9.866  0.50 17.58 ?  104  GLU   A OE1  1 
ATOM   2271 O  OE1  B GLU   A 1 104 ? 25.704 -2.251  -10.090 0.50 16.06 ?  104  GLU   A OE1  1 
ATOM   2272 O  OE2  A GLU   A 1 104 ? 27.152 -0.748  -10.914 0.50 20.14 -1 104  GLU   A OE2  1 
ATOM   2273 O  OE2  B GLU   A 1 104 ? 26.932 -0.892  -11.285 0.50 16.29 -1 104  GLU   A OE2  1 
ATOM   2274 H  H    A GLU   A 1 104 ? 23.080 -2.487  -13.448 0.50 26.59 ?  104  GLU   A H    1 
ATOM   2275 H  H    B GLU   A 1 104 ? 23.272 -2.970  -13.801 0.50 21.63 ?  104  GLU   A H    1 
ATOM   2276 H  HA   A GLU   A 1 104 ? 25.176 -4.053  -13.981 0.50 25.52 ?  104  GLU   A HA   1 
ATOM   2277 H  HA   B GLU   A 1 104 ? 25.311 -4.623  -14.148 0.50 19.44 ?  104  GLU   A HA   1 
ATOM   2278 H  HB2  A GLU   A 1 104 ? 24.127 -3.152  -11.527 0.50 24.23 ?  104  GLU   A HB2  1 
ATOM   2279 H  HB2  B GLU   A 1 104 ? 24.189 -3.681  -11.735 0.50 18.87 ?  104  GLU   A HB2  1 
ATOM   2280 H  HB3  A GLU   A 1 104 ? 25.335 -4.186  -11.588 0.50 24.23 ?  104  GLU   A HB3  1 
ATOM   2281 H  HB3  B GLU   A 1 104 ? 25.529 -4.535  -11.809 0.50 18.87 ?  104  GLU   A HB3  1 
ATOM   2282 H  HG2  A GLU   A 1 104 ? 26.705 -2.642  -12.546 0.50 23.58 ?  104  GLU   A HG2  1 
ATOM   2283 H  HG2  B GLU   A 1 104 ? 26.602 -2.822  -12.926 0.50 19.38 ?  104  GLU   A HG2  1 
ATOM   2284 H  HG3  A GLU   A 1 104 ? 25.498 -1.646  -12.799 0.50 23.58 ?  104  GLU   A HG3  1 
ATOM   2285 H  HG3  B GLU   A 1 104 ? 25.257 -1.985  -12.994 0.50 19.38 ?  104  GLU   A HG3  1 
ATOM   2286 N  N    A ASP   A 1 105 ? 24.524 -6.354  -13.473 0.50 22.39 ?  105  ASP   A N    1 
ATOM   2287 N  N    B ASP   A 1 105 ? 24.672 -6.893  -13.415 0.50 15.50 ?  105  ASP   A N    1 
ATOM   2288 C  CA   A ASP   A 1 105 ? 24.019 -7.717  -13.569 0.50 23.00 ?  105  ASP   A CA   1 
ATOM   2289 C  CA   B ASP   A 1 105 ? 24.205 -8.274  -13.489 0.50 15.72 ?  105  ASP   A CA   1 
ATOM   2290 C  C    A ASP   A 1 105 ? 23.328 -8.124  -12.274 0.50 21.44 ?  105  ASP   A C    1 
ATOM   2291 C  C    B ASP   A 1 105 ? 23.480 -8.667  -12.206 0.50 14.07 ?  105  ASP   A C    1 
ATOM   2292 O  O    A ASP   A 1 105 ? 23.951 -8.135  -11.209 0.50 20.40 ?  105  ASP   A O    1 
ATOM   2293 O  O    B ASP   A 1 105 ? 24.079 -8.688  -11.130 0.50 12.58 ?  105  ASP   A O    1 
ATOM   2294 C  CB   A ASP   A 1 105 ? 25.192 -8.655  -13.855 0.50 25.15 ?  105  ASP   A CB   1 
ATOM   2295 C  CB   B ASP   A 1 105 ? 25.419 -9.176  -13.720 0.50 17.64 ?  105  ASP   A CB   1 
ATOM   2296 C  CG   A ASP   A 1 105 ? 24.743 -10.058 -14.198 0.50 27.11 ?  105  ASP   A CG   1 
ATOM   2297 C  CG   B ASP   A 1 105 ? 25.077 -10.649 -13.752 0.50 19.38 ?  105  ASP   A CG   1 
ATOM   2298 O  OD1  A ASP   A 1 105 ? 23.518 -10.280 -14.285 0.50 27.59 ?  105  ASP   A OD1  1 
ATOM   2299 O  OD1  B ASP   A 1 105 ? 23.880 -10.993 -13.834 0.50 19.47 ?  105  ASP   A OD1  1 
ATOM   2300 O  OD2  A ASP   A 1 105 ? 25.614 -10.933 -14.393 0.50 28.13 -1 105  ASP   A OD2  1 
ATOM   2301 O  OD2  B ASP   A 1 105 ? 26.027 -11.465 -13.693 0.50 20.87 -1 105  ASP   A OD2  1 
ATOM   2302 H  H    A ASP   A 1 105 ? 25.380 -6.302  -13.524 0.50 26.87 ?  105  ASP   A H    1 
ATOM   2303 H  H    B ASP   A 1 105 ? 25.527 -6.823  -13.359 0.50 18.60 ?  105  ASP   A H    1 
ATOM   2304 H  HA   A ASP   A 1 105 ? 23.386 -7.793  -14.300 0.50 27.59 ?  105  ASP   A HA   1 
ATOM   2305 H  HA   B ASP   A 1 105 ? 23.593 -8.375  -14.232 0.50 18.87 ?  105  ASP   A HA   1 
ATOM   2306 H  HB2  A ASP   A 1 105 ? 25.691 -8.323  -14.617 0.50 30.17 ?  105  ASP   A HB2  1 
ATOM   2307 H  HB2  B ASP   A 1 105 ? 25.829 -8.937  -14.568 0.50 21.17 ?  105  ASP   A HB2  1 
ATOM   2308 H  HB3  A ASP   A 1 105 ? 25.772 -8.687  -13.073 0.50 30.17 ?  105  ASP   A HB3  1 
ATOM   2309 H  HB3  B ASP   A 1 105 ? 26.050 -9.051  -12.999 0.50 21.17 ?  105  ASP   A HB3  1 
ATOM   2310 N  N    A ILE   A 1 106 ? 22.043 -8.477  -12.368 0.50 21.00 ?  106  ILE   A N    1 
ATOM   2311 N  N    B ILE   A 1 106 ? 22.191 -8.996  -12.320 0.50 14.52 ?  106  ILE   A N    1 
ATOM   2312 C  CA   A ILE   A 1 106 ? 21.289 -8.884  -11.187 0.50 20.41 ?  106  ILE   A CA   1 
ATOM   2313 C  CA   B ILE   A 1 106 ? 21.406 -9.374  -11.151 0.50 15.02 ?  106  ILE   A CA   1 
ATOM   2314 C  C    A ILE   A 1 106 ? 21.819 -10.186 -10.603 0.50 19.38 ?  106  ILE   A C    1 
ATOM   2315 C  C    B ILE   A 1 106 ? 21.959 -10.615 -10.468 0.50 14.95 ?  106  ILE   A C    1 
ATOM   2316 O  O    A ILE   A 1 106 ? 21.595 -10.464 -9.421  0.50 18.86 ?  106  ILE   A O    1 
ATOM   2317 O  O    B ILE   A 1 106 ? 21.747 -10.799 -9.264  0.50 15.08 ?  106  ILE   A O    1 
ATOM   2318 C  CB   A ILE   A 1 106 ? 19.781 -8.977  -11.503 0.50 21.29 ?  106  ILE   A CB   1 
ATOM   2319 C  CB   B ILE   A 1 106 ? 19.915 -9.525  -11.531 0.50 16.71 ?  106  ILE   A CB   1 
ATOM   2320 C  CG1  A ILE   A 1 106 ? 18.954 -9.055  -10.215 0.50 21.64 ?  106  ILE   A CG1  1 
ATOM   2321 C  CG1  B ILE   A 1 106 ? 19.036 -9.660  -10.282 0.50 17.18 ?  106  ILE   A CG1  1 
ATOM   2322 C  CG2  A ILE   A 1 106 ? 19.490 -10.199 -12.361 0.50 21.64 ?  106  ILE   A CG2  1 
ATOM   2323 C  CG2  B ILE   A 1 106 ? 19.709 -10.714 -12.460 0.50 17.42 ?  106  ILE   A CG2  1 
ATOM   2324 C  CD1  A ILE   A 1 106 ? 19.177 -7.893  -9.270  0.50 21.85 ?  106  ILE   A CD1  1 
ATOM   2325 C  CD1  B ILE   A 1 106 ? 18.997 -8.412  -9.420  0.50 17.47 ?  106  ILE   A CD1  1 
ATOM   2326 H  H    A ILE   A 1 106 ? 21.593 -8.492  -13.097 0.50 25.20 ?  106  ILE   A H    1 
ATOM   2327 H  H    B ILE   A 1 106 ? 21.756 -9.009  -13.055 0.50 17.42 ?  106  ILE   A H    1 
ATOM   2328 H  HA   A ILE   A 1 106 ? 21.407 -8.202  -10.515 0.50 24.50 ?  106  ILE   A HA   1 
ATOM   2329 H  HA   B ILE   A 1 106 ? 21.469 -8.665  -10.502 0.50 18.03 ?  106  ILE   A HA   1 
ATOM   2330 H  HB   A ILE   A 1 106 ? 19.514 -8.187  -11.997 0.50 25.55 ?  106  ILE   A HB   1 
ATOM   2331 H  HB   B ILE   A 1 106 ? 19.645 -8.721  -12.001 0.50 20.06 ?  106  ILE   A HB   1 
ATOM   2332 H  HG12 A ILE   A 1 106 ? 18.011 -9.068  -10.449 0.50 25.96 ?  106  ILE   A HG12 1 
ATOM   2333 H  HG12 B ILE   A 1 106 ? 18.127 -9.852  -10.559 0.50 20.62 ?  106  ILE   A HG12 1 
ATOM   2334 H  HG13 A ILE   A 1 106 ? 19.183 -9.871  -9.744  0.50 25.96 ?  106  ILE   A HG13 1 
ATOM   2335 H  HG13 B ILE   A 1 106 ? 19.370 -10.387 -9.734  0.50 20.62 ?  106  ILE   A HG13 1 
ATOM   2336 H  HG21 A ILE   A 1 106 ? 18.602 -10.114 -12.741 0.50 25.97 ?  106  ILE   A HG21 1 
ATOM   2337 H  HG21 B ILE   A 1 106 ? 18.797 -10.700 -12.791 0.50 20.90 ?  106  ILE   A HG21 1 
ATOM   2338 H  HG22 A ILE   A 1 106 ? 20.150 -10.249 -13.069 0.50 25.97 ?  106  ILE   A HG22 1 
ATOM   2339 H  HG22 B ILE   A 1 106 ? 20.330 -10.644 -13.202 0.50 20.90 ?  106  ILE   A HG22 1 
ATOM   2340 H  HG23 A ILE   A 1 106 ? 19.538 -10.994 -11.807 0.50 25.97 ?  106  ILE   A HG23 1 
ATOM   2341 H  HG23 B ILE   A 1 106 ? 19.871 -11.533 -11.969 0.50 20.90 ?  106  ILE   A HG23 1 
ATOM   2342 H  HD11 A ILE   A 1 106 ? 18.436 -7.849  -8.648  0.50 26.22 ?  106  ILE   A HD11 1 
ATOM   2343 H  HD11 B ILE   A 1 106 ? 18.301 -8.511  -8.752  0.50 20.96 ?  106  ILE   A HD11 1 
ATOM   2344 H  HD12 A ILE   A 1 106 ? 20.007 -8.035  -8.788  0.50 26.22 ?  106  ILE   A HD12 1 
ATOM   2345 H  HD12 B ILE   A 1 106 ? 19.857 -8.299  -8.984  0.50 20.96 ?  106  ILE   A HD12 1 
ATOM   2346 H  HD13 A ILE   A 1 106 ? 19.227 -7.074  -9.787  0.50 26.22 ?  106  ILE   A HD13 1 
ATOM   2347 H  HD13 B ILE   A 1 106 ? 18.808 -7.645  -9.983  0.50 20.96 ?  106  ILE   A HD13 1 
ATOM   2348 N  N    A GLN   A 1 107 ? 22.522 -10.992 -11.404 0.50 19.70 ?  107  GLN   A N    1 
ATOM   2349 N  N    B GLN   A 1 107 ? 22.679 -11.472 -11.201 0.50 15.58 ?  107  GLN   A N    1 
ATOM   2350 C  CA   A GLN   A 1 107 ? 23.125 -12.219 -10.894 0.50 20.84 ?  107  GLN   A CA   1 
ATOM   2351 C  CA   B GLN   A 1 107 ? 23.299 -12.633 -10.567 0.50 17.23 ?  107  GLN   A CA   1 
ATOM   2352 C  C    A GLN   A 1 107 ? 24.116 -11.944 -9.771  0.50 18.90 ?  107  GLN   A C    1 
ATOM   2353 C  C    B GLN   A 1 107 ? 24.280 -12.217 -9.478  0.50 15.59 ?  107  GLN   A C    1 
ATOM   2354 O  O    A GLN   A 1 107 ? 24.373 -12.834 -8.955  0.50 20.30 ?  107  GLN   A O    1 
ATOM   2355 O  O    B GLN   A 1 107 ? 24.510 -12.970 -8.523  0.50 15.74 ?  107  GLN   A O    1 
ATOM   2356 C  CB   A GLN   A 1 107 ? 23.835 -12.968 -12.028 0.50 24.17 ?  107  GLN   A CB   1 
ATOM   2357 C  CB   B GLN   A 1 107 ? 23.981 -13.509 -11.623 0.50 20.54 ?  107  GLN   A CB   1 
ATOM   2358 C  CG   A GLN   A 1 107 ? 22.972 -13.231 -13.255 0.50 27.47 ?  107  GLN   A CG   1 
ATOM   2359 C  CG   B GLN   A 1 107 ? 22.999 -14.145 -12.596 0.50 23.78 ?  107  GLN   A CG   1 
ATOM   2360 C  CD   A GLN   A 1 107 ? 21.738 -14.051 -12.940 0.50 30.13 ?  107  GLN   A CD   1 
ATOM   2361 C  CD   B GLN   A 1 107 ? 21.920 -14.941 -11.885 0.50 26.59 ?  107  GLN   A CD   1 
ATOM   2362 O  OE1  A GLN   A 1 107 ? 21.826 -15.124 -12.345 0.50 31.35 ?  107  GLN   A OE1  1 
ATOM   2363 O  OE1  B GLN   A 1 107 ? 22.206 -15.708 -10.965 0.50 27.46 ?  107  GLN   A OE1  1 
ATOM   2364 N  NE2  A GLN   A 1 107 ? 20.577 -13.545 -13.336 0.50 30.89 ?  107  GLN   A NE2  1 
ATOM   2365 N  NE2  B GLN   A 1 107 ? 20.670 -14.750 -12.296 0.50 27.50 ?  107  GLN   A NE2  1 
ATOM   2366 H  H    A GLN   A 1 107 ? 22.662 -10.849 -12.236 0.50 23.64 ?  107  GLN   A H    1 
ATOM   2367 H  H    B GLN   A 1 107 ? 22.819 -11.411 -12.050 0.50 18.70 ?  107  GLN   A H    1 
ATOM   2368 H  HA   A GLN   A 1 107 ? 22.430 -12.798 -10.546 0.50 25.01 ?  107  GLN   A HA   1 
ATOM   2369 H  HA   B GLN   A 1 107 ? 22.610 -13.165 -10.149 0.50 20.68 ?  107  GLN   A HA   1 
ATOM   2370 H  HB2  A GLN   A 1 107 ? 24.599 -12.444 -12.316 0.50 29.00 ?  107  GLN   A HB2  1 
ATOM   2371 H  HB2  B GLN   A 1 107 ? 24.600 -12.971 -12.142 0.50 24.64 ?  107  GLN   A HB2  1 
ATOM   2372 H  HB3  A GLN   A 1 107 ? 24.136 -13.828 -11.694 0.50 29.00 ?  107  GLN   A HB3  1 
ATOM   2373 H  HB3  B GLN   A 1 107 ? 24.464 -14.231 -11.183 0.50 24.64 ?  107  GLN   A HB3  1 
ATOM   2374 H  HG2  A GLN   A 1 107 ? 22.679 -12.386 -13.627 0.50 32.97 ?  107  GLN   A HG2  1 
ATOM   2375 H  HG2  B GLN   A 1 107 ? 22.570 -13.446 -13.112 0.50 28.53 ?  107  GLN   A HG2  1 
ATOM   2376 H  HG3  A GLN   A 1 107 ? 23.497 -13.717 -13.911 0.50 32.97 ?  107  GLN   A HG3  1 
ATOM   2377 H  HG3  B GLN   A 1 107 ? 23.477 -14.750 -13.184 0.50 28.53 ?  107  GLN   A HG3  1 
ATOM   2378 H  HE21 A GLN   A 1 107 ? 20.555 -12.792 -13.749 0.50 37.07 ?  107  GLN   A HE21 1 
ATOM   2379 H  HE21 B GLN   A 1 107 ? 20.508 -14.204 -12.939 0.50 33.01 ?  107  GLN   A HE21 1 
ATOM   2380 H  HE22 A GLN   A 1 107 ? 19.848 -13.973 -13.181 0.50 37.07 ?  107  GLN   A HE22 1 
ATOM   2381 H  HE22 B GLN   A 1 107 ? 20.022 -15.174 -11.919 0.50 33.01 ?  107  GLN   A HE22 1 
ATOM   2382 N  N    A LEU   A 1 108 ? 24.670 -10.731 -9.701  0.50 15.24 ?  108  LEU   A N    1 
ATOM   2383 N  N    B LEU   A 1 108 ? 24.850 -11.016 -9.589  0.50 14.31 ?  108  LEU   A N    1 
ATOM   2384 C  CA   A LEU   A 1 108 ? 25.629 -10.395 -8.654  0.50 13.48 ?  108  LEU   A CA   1 
ATOM   2385 C  CA   B LEU   A 1 108 ? 25.717 -10.492 -8.543  0.50 13.34 ?  108  LEU   A CA   1 
ATOM   2386 C  C    A LEU   A 1 108 ? 24.970 -10.249 -7.289  0.50 11.84 ?  108  LEU   A C    1 
ATOM   2387 C  C    B LEU   A 1 108 ? 24.975 -10.248 -7.237  0.50 11.74 ?  108  LEU   A C    1 
ATOM   2388 O  O    A LEU   A 1 108 ? 25.679 -10.116 -6.287  0.50 12.23 ?  108  LEU   A O    1 
ATOM   2389 O  O    B LEU   A 1 108 ? 25.631 -10.041 -6.209  0.50 12.12 ?  108  LEU   A O    1 
ATOM   2390 C  CB   A LEU   A 1 108 ? 26.385 -9.117  -9.028  0.50 13.23 ?  108  LEU   A CB   1 
ATOM   2391 C  CB   B LEU   A 1 108 ? 26.419 -9.214  -9.021  0.50 13.61 ?  108  LEU   A CB   1 
ATOM   2392 C  CG   A LEU   A 1 108 ? 27.325 -9.289  -10.224 0.50 14.35 ?  108  LEU   A CG   1 
ATOM   2393 C  CG   B LEU   A 1 108 ? 27.468 -9.438  -10.113 0.50 14.76 ?  108  LEU   A CG   1 
ATOM   2394 C  CD1  A LEU   A 1 108 ? 27.742 -7.943  -10.796 0.50 14.87 ?  108  LEU   A CD1  1 
ATOM   2395 C  CD1  B LEU   A 1 108 ? 28.016 -8.116  -10.625 0.50 15.18 ?  108  LEU   A CD1  1 
ATOM   2396 C  CD2  A LEU   A 1 108 ? 28.551 -10.100 -9.828  0.50 15.64 ?  108  LEU   A CD2  1 
ATOM   2397 C  CD2  B LEU   A 1 108 ? 28.600 -10.316 -9.600  0.50 16.11 ?  108  LEU   A CD2  1 
ATOM   2398 H  H    A LEU   A 1 108 ? 24.502 -10.096 -10.247 0.50 18.29 ?  108  LEU   A H    1 
ATOM   2399 H  H    B LEU   A 1 108 ? 24.759 -10.499 -10.264 0.50 17.17 ?  108  LEU   A H    1 
ATOM   2400 H  HA   A LEU   A 1 108 ? 26.274 -11.114 -8.586  0.50 16.18 ?  108  LEU   A HA   1 
ATOM   2401 H  HA   B LEU   A 1 108 ? 26.401 -11.149 -8.353  0.50 16.01 ?  108  LEU   A HA   1 
ATOM   2402 H  HB2  A LEU   A 1 108 ? 25.741 -8.430  -9.256  0.50 15.88 ?  108  LEU   A HB2  1 
ATOM   2403 H  HB2  B LEU   A 1 108 ? 25.754 -8.605  -9.373  0.50 16.33 ?  108  LEU   A HB2  1 
ATOM   2404 H  HB3  A LEU   A 1 108 ? 26.916 -8.837  -8.270  0.50 15.88 ?  108  LEU   A HB3  1 
ATOM   2405 H  HB3  B LEU   A 1 108 ? 26.868 -8.808  -8.265  0.50 16.33 ?  108  LEU   A HB3  1 
ATOM   2406 H  HG   A LEU   A 1 108 ? 26.862 -9.779  -10.922 0.50 17.23 ?  108  LEU   A HG   1 
ATOM   2407 H  HG   B LEU   A 1 108 ? 27.052 -9.896  -10.860 0.50 17.71 ?  108  LEU   A HG   1 
ATOM   2408 H  HD11 A LEU   A 1 108 ? 28.301 -8.091  -11.577 0.50 17.84 ?  108  LEU   A HD11 1 
ATOM   2409 H  HD11 B LEU   A 1 108 ? 28.658 -8.290  -11.331 0.50 18.22 ?  108  LEU   A HD11 1 
ATOM   2410 H  HD12 A LEU   A 1 108 ? 26.949 -7.447  -11.047 0.50 17.84 ?  108  LEU   A HD12 1 
ATOM   2411 H  HD12 B LEU   A 1 108 ? 27.282 -7.582  -10.971 0.50 18.22 ?  108  LEU   A HD12 1 
ATOM   2412 H  HD13 A LEU   A 1 108 ? 28.241 -7.454  -10.123 0.50 17.84 ?  108  LEU   A HD13 1 
ATOM   2413 H  HD13 B LEU   A 1 108 ? 28.448 -7.647  -9.894  0.50 18.22 ?  108  LEU   A HD13 1 
ATOM   2414 H  HD21 A LEU   A 1 108 ? 29.177 -10.110 -10.568 0.50 18.76 ?  108  LEU   A HD21 1 
ATOM   2415 H  HD21 B LEU   A 1 108 ? 29.348 -10.256 -10.214 0.50 19.33 ?  108  LEU   A HD21 1 
ATOM   2416 H  HD22 A LEU   A 1 108 ? 28.963 -9.690  -9.051  0.50 18.76 ?  108  LEU   A HD22 1 
ATOM   2417 H  HD22 B LEU   A 1 108 ? 28.866 -10.002 -8.722  0.50 19.33 ?  108  LEU   A HD22 1 
ATOM   2418 H  HD23 A LEU   A 1 108 ? 28.277 -11.007 -9.615  0.50 18.76 ?  108  LEU   A HD23 1 
ATOM   2419 H  HD23 B LEU   A 1 108 ? 28.289 -11.232 -9.544  0.50 19.33 ?  108  LEU   A HD23 1 
ATOM   2420 N  N    . LEU   A 1 109 ? 23.638 -10.295 -7.230  1.00 11.46 ?  109  LEU   A N    1 
ATOM   2421 C  CA   . LEU   A 1 109 ? 22.936 -10.166 -5.961  1.00 11.05 ?  109  LEU   A CA   1 
ATOM   2422 C  C    . LEU   A 1 109 ? 23.273 -11.323 -5.026  1.00 10.07 ?  109  LEU   A C    1 
ATOM   2423 O  O    . LEU   A 1 109 ? 23.401 -11.135 -3.811  1.00 10.62 ?  109  LEU   A O    1 
ATOM   2424 C  CB   . LEU   A 1 109 ? 21.430 -10.067 -6.213  1.00 11.71 ?  109  LEU   A CB   1 
ATOM   2425 C  CG   . LEU   A 1 109 ? 20.548 -9.789  -4.997  1.00 12.20 ?  109  LEU   A CG   1 
ATOM   2426 C  CD1  . LEU   A 1 109 ? 21.014 -8.543  -4.259  1.00 12.46 ?  109  LEU   A CD1  1 
ATOM   2427 C  CD2  . LEU   A 1 109 ? 19.085 -9.654  -5.414  1.00 13.43 ?  109  LEU   A CD2  1 
ATOM   2428 H  H    A LEU   A 1 109 ? 23.121 -10.400 -7.909  0.50 13.75 ?  109  LEU   A H    1 
ATOM   2429 H  H    B LEU   A 1 109 ? 23.137 -10.404 -7.920  0.50 13.75 ?  109  LEU   A H    1 
ATOM   2430 H  HA   . LEU   A 1 109 ? 23.221 -9.345  -5.533  1.00 13.26 ?  109  LEU   A HA   1 
ATOM   2431 H  HB2  . LEU   A 1 109 ? 21.274 -9.349  -6.848  1.00 14.05 ?  109  LEU   A HB2  1 
ATOM   2432 H  HB3  . LEU   A 1 109 ? 21.129 -10.905 -6.599  1.00 14.05 ?  109  LEU   A HB3  1 
ATOM   2433 H  HG   . LEU   A 1 109 ? 20.613 -10.538 -4.386  1.00 14.63 ?  109  LEU   A HG   1 
ATOM   2434 H  HD11 . LEU   A 1 109 ? 20.325 -8.261  -3.644  1.00 14.95 ?  109  LEU   A HD11 1 
ATOM   2435 H  HD12 . LEU   A 1 109 ? 21.832 -8.749  -3.776  1.00 14.95 ?  109  LEU   A HD12 1 
ATOM   2436 H  HD13 . LEU   A 1 109 ? 21.187 -7.838  -4.909  1.00 14.95 ?  109  LEU   A HD13 1 
ATOM   2437 H  HD21 . LEU   A 1 109 ? 18.566 -9.340  -4.654  1.00 16.12 ?  109  LEU   A HD21 1 
ATOM   2438 H  HD22 . LEU   A 1 109 ? 19.016 -9.021  -6.143  1.00 16.12 ?  109  LEU   A HD22 1 
ATOM   2439 H  HD23 . LEU   A 1 109 ? 18.753 -10.523 -5.699  1.00 16.12 ?  109  LEU   A HD23 1 
ATOM   2440 N  N    . LYS   A 1 110 ? 23.417 -12.535 -5.569  1.00 10.26 ?  110  LYS   A N    1 
ATOM   2441 C  CA   . LYS   A 1 110 ? 23.799 -13.659 -4.721  1.00 10.21 ?  110  LYS   A CA   1 
ATOM   2442 C  C    . LYS   A 1 110 ? 25.185 -13.439 -4.119  1.00 9.62  ?  110  LYS   A C    1 
ATOM   2443 O  O    . LYS   A 1 110 ? 25.389 -13.644 -2.920  1.00 9.87  ?  110  LYS   A O    1 
ATOM   2444 C  CB   . LYS   A 1 110 ? 23.718 -14.978 -5.494  1.00 10.75 ?  110  LYS   A CB   1 
ATOM   2445 C  CG   . LYS   A 1 110 ? 23.923 -16.189 -4.592  1.00 11.13 ?  110  LYS   A CG   1 
ATOM   2446 C  CD   . LYS   A 1 110 ? 23.681 -17.506 -5.303  1.00 11.95 ?  110  LYS   A CD   1 
ATOM   2447 C  CE   . LYS   A 1 110 ? 23.789 -18.685 -4.353  1.00 12.65 ?  110  LYS   A CE   1 
ATOM   2448 N  NZ   . LYS   A 1 110 ? 22.620 -18.816 -3.453  1.00 13.19 ?  110  LYS   A NZ   1 
ATOM   2449 H  H    . LYS   A 1 110 ? 23.308 -12.727 -6.398  1.00 12.31 ?  110  LYS   A H    1 
ATOM   2450 H  HA   . LYS   A 1 110 ? 23.161 -13.716 -3.985  1.00 12.26 ?  110  LYS   A HA   1 
ATOM   2451 H  HB2  . LYS   A 1 110 ? 22.843 -15.055 -5.904  1.00 12.90 ?  110  LYS   A HB2  1 
ATOM   2452 H  HB3  . LYS   A 1 110 ? 24.409 -14.990 -6.171  1.00 12.90 ?  110  LYS   A HB3  1 
ATOM   2453 H  HG2  . LYS   A 1 110 ? 24.834 -16.187 -4.259  1.00 13.35 ?  110  LYS   A HG2  1 
ATOM   2454 H  HG3  . LYS   A 1 110 ? 23.301 -16.134 -3.845  1.00 13.35 ?  110  LYS   A HG3  1 
ATOM   2455 H  HD2  . LYS   A 1 110 ? 22.794 -17.501 -5.685  1.00 14.34 ?  110  LYS   A HD2  1 
ATOM   2456 H  HD3  . LYS   A 1 110 ? 24.350 -17.613 -5.996  1.00 14.34 ?  110  LYS   A HD3  1 
ATOM   2457 H  HE2  . LYS   A 1 110 ? 23.861 -19.499 -4.869  1.00 15.19 ?  110  LYS   A HE2  1 
ATOM   2458 H  HE3  . LYS   A 1 110 ? 24.578 -18.572 -3.796  1.00 15.19 ?  110  LYS   A HE3  1 
ATOM   2459 H  HZ1  . LYS   A 1 110 ? 22.722 -19.517 -2.918  1.00 15.83 ?  110  LYS   A HZ1  1 
ATOM   2460 H  HZ2  . LYS   A 1 110 ? 22.530 -18.082 -2.957  1.00 15.83 ?  110  LYS   A HZ2  1 
ATOM   2461 H  HZ3  . LYS   A 1 110 ? 21.877 -18.927 -3.936  1.00 15.83 ?  110  LYS   A HZ3  1 
ATOM   2462 N  N    . SER   A 1 111 ? 26.142 -12.993 -4.938  1.00 10.00 ?  111  SER   A N    1 
ATOM   2463 C  CA   . SER   A 1 111 ? 27.475 -12.687 -4.427  1.00 10.10 ?  111  SER   A CA   1 
ATOM   2464 C  C    . SER   A 1 111 ? 27.413 -11.643 -3.316  1.00 9.45  ?  111  SER   A C    1 
ATOM   2465 O  O    . SER   A 1 111 ? 28.113 -11.750 -2.304  1.00 10.09 ?  111  SER   A O    1 
ATOM   2466 C  CB   . SER   A 1 111 ? 28.361 -12.194 -5.570  1.00 11.26 ?  111  SER   A CB   1 
ATOM   2467 O  OG   . SER   A 1 111 ? 28.422 -13.169 -6.597  1.00 13.51 ?  111  SER   A OG   1 
ATOM   2468 H  H    . SER   A 1 111 ? 26.034 -12.857 -5.777  1.00 12.00 ?  111  SER   A H    1 
ATOM   2469 H  HA   . SER   A 1 111 ? 27.867 -13.494 -4.062  1.00 12.12 ?  111  SER   A HA   1 
ATOM   2470 H  HB2  . SER   A 1 111 ? 27.981 -11.377 -5.933  1.00 13.51 ?  111  SER   A HB2  1 
ATOM   2471 H  HB3  . SER   A 1 111 ? 29.250 -12.022 -5.225  1.00 13.51 ?  111  SER   A HB3  1 
ATOM   2472 H  HG   . SER   A 1 111 ? 28.927 -12.886 -7.218  1.00 16.21 ?  111  SER   A HG   1 
ATOM   2473 N  N    . ALA   A 1 112 ? 26.564 -10.628 -3.486  1.00 9.63  ?  112  ALA   A N    1 
ATOM   2474 C  CA   . ALA   A 1 112 ? 26.419 -9.591  -2.467  1.00 9.52  ?  112  ALA   A CA   1 
ATOM   2475 C  C    . ALA   A 1 112 ? 25.947 -10.192 -1.145  1.00 9.41  ?  112  ALA   A C    1 
ATOM   2476 O  O    . ALA   A 1 112 ? 26.506 -9.905  -0.080  1.00 9.66  ?  112  ALA   A O    1 
ATOM   2477 C  CB   . ALA   A 1 112 ? 25.454 -8.509  -2.958  1.00 10.26 ?  112  ALA   A CB   1 
ATOM   2478 H  H    . ALA   A 1 112 ? 26.064 -10.514 -4.175  1.00 11.56 ?  112  ALA   A H    1 
ATOM   2479 H  HA   . ALA   A 1 112 ? 27.279 -9.169  -2.313  1.00 11.42 ?  112  ALA   A HA   1 
ATOM   2480 H  HB1  . ALA   A 1 112 ? 25.389 -7.807  -2.283  1.00 12.31 ?  112  ALA   A HB1  1 
ATOM   2481 H  HB2  . ALA   A 1 112 ? 25.786 -8.133  -3.786  1.00 12.31 ?  112  ALA   A HB2  1 
ATOM   2482 H  HB3  . ALA   A 1 112 ? 24.577 -8.901  -3.101  1.00 12.31 ?  112  ALA   A HB3  1 
ATOM   2483 N  N    . TYR   A 1 113 ? 24.910 -11.033 -1.196  1.00 9.40  ?  113  TYR   A N    1 
ATOM   2484 C  CA   . TYR   A 1 113 ? 24.399 -11.636 0.031   1.00 9.14  ?  113  TYR   A CA   1 
ATOM   2485 C  C    . TYR   A 1 113 ? 25.403 -12.594 0.673   1.00 9.01  ?  113  TYR   A C    1 
ATOM   2486 O  O    . TYR   A 1 113 ? 25.369 -12.781 1.894   1.00 9.58  ?  113  TYR   A O    1 
ATOM   2487 C  CB   . TYR   A 1 113 ? 23.075 -12.354 -0.235  1.00 9.85  ?  113  TYR   A CB   1 
ATOM   2488 C  CG   . TYR   A 1 113 ? 21.869 -11.448 -0.146  1.00 9.90  ?  113  TYR   A CG   1 
ATOM   2489 C  CD1  . TYR   A 1 113 ? 21.514 -10.843 1.057   1.00 10.20 ?  113  TYR   A CD1  1 
ATOM   2490 C  CD2  . TYR   A 1 113 ? 21.063 -11.217 -1.251  1.00 10.25 ?  113  TYR   A CD2  1 
ATOM   2491 C  CE1  . TYR   A 1 113 ? 20.395 -10.038 1.154   1.00 10.54 ?  113  TYR   A CE1  1 
ATOM   2492 C  CE2  . TYR   A 1 113 ? 19.918 -10.410 -1.159  1.00 10.50 ?  113  TYR   A CE2  1 
ATOM   2493 C  CZ   . TYR   A 1 113 ? 19.603 -9.826  0.047   1.00 10.56 ?  113  TYR   A CZ   1 
ATOM   2494 O  OH   . TYR   A 1 113 ? 18.485 -9.023  0.169   1.00 11.46 ?  113  TYR   A OH   1 
ATOM   2495 H  H    . TYR   A 1 113 ? 24.503 -11.267 -1.916  1.00 11.28 ?  113  TYR   A H    1 
ATOM   2496 H  HA   . TYR   A 1 113 ? 24.229 -10.929 0.668   1.00 10.97 ?  113  TYR   A HA   1 
ATOM   2497 H  HB2  . TYR   A 1 113 ? 23.097 -12.730 -1.129  1.00 11.82 ?  113  TYR   A HB2  1 
ATOM   2498 H  HB3  . TYR   A 1 113 ? 22.969 -13.062 0.417   1.00 11.82 ?  113  TYR   A HB3  1 
ATOM   2499 H  HD1  . TYR   A 1 113 ? 22.040 -10.991 1.810   1.00 12.24 ?  113  TYR   A HD1  1 
ATOM   2500 H  HD2  . TYR   A 1 113 ? 21.268 -11.623 -2.061  1.00 12.30 ?  113  TYR   A HD2  1 
ATOM   2501 H  HE1  . TYR   A 1 113 ? 20.178 -9.643  1.963   1.00 12.65 ?  113  TYR   A HE1  1 
ATOM   2502 H  HE2  . TYR   A 1 113 ? 19.382 -10.260 -1.910  1.00 12.60 ?  113  TYR   A HE2  1 
ATOM   2503 H  HH   . TYR   A 1 113 ? 18.088 -8.972  -0.576  1.00 13.75 ?  113  TYR   A HH   1 
ATOM   2504 N  N    . GLU   A 1 114 ? 26.302 -13.204 -0.115  1.00 9.49  ?  114  GLU   A N    1 
ATOM   2505 C  CA   . GLU   A 1 114 ? 27.294 -14.102 0.472   1.00 9.73  ?  114  GLU   A CA   1 
ATOM   2506 C  C    . GLU   A 1 114 ? 28.152 -13.400 1.518   1.00 9.58  ?  114  GLU   A C    1 
ATOM   2507 O  O    . GLU   A 1 114 ? 28.629 -14.041 2.464   1.00 9.78  ?  114  GLU   A O    1 
ATOM   2508 C  CB   . GLU   A 1 114 ? 28.158 -14.735 -0.624  1.00 9.86  ?  114  GLU   A CB   1 
ATOM   2509 C  CG   . GLU   A 1 114 ? 27.397 -15.799 -1.406  1.00 10.00 ?  114  GLU   A CG   1 
ATOM   2510 C  CD   . GLU   A 1 114 ? 28.106 -16.318 -2.653  1.00 10.57 ?  114  GLU   A CD   1 
ATOM   2511 O  OE1  . GLU   A 1 114 ? 29.059 -15.684 -3.151  1.00 10.83 ?  114  GLU   A OE1  1 
ATOM   2512 O  OE2  . GLU   A 1 114 ? 27.666 -17.380 -3.149  1.00 11.78 -1 114  GLU   A OE2  1 
ATOM   2513 H  H    . GLU   A 1 114 ? 26.354 -13.107 -0.975  1.00 11.39 ?  114  GLU   A H    1 
ATOM   2514 H  HA   . GLU   A 1 114 ? 26.822 -14.821 0.912   1.00 11.67 ?  114  GLU   A HA   1 
ATOM   2515 H  HB2  . GLU   A 1 114 ? 28.438 -14.046 -1.252  1.00 11.83 ?  114  GLU   A HB2  1 
ATOM   2516 H  HB3  . GLU   A 1 114 ? 28.931 -15.152 -0.221  1.00 11.83 ?  114  GLU   A HB3  1 
ATOM   2517 H  HG2  . GLU   A 1 114 ? 27.242 -16.558 -0.824  1.00 12.00 ?  114  GLU   A HG2  1 
ATOM   2518 H  HG3  . GLU   A 1 114 ? 26.545 -15.428 -1.689  1.00 12.00 ?  114  GLU   A HG3  1 
ATOM   2519 N  N    . ASN   A 1 115 ? 28.341 -12.081 1.387   1.00 9.29  ?  115  ASN   A N    1 
ATOM   2520 C  CA   . ASN   A 1 115 ? 29.110 -11.356 2.391   1.00 9.42  ?  115  ASN   A CA   1 
ATOM   2521 C  C    . ASN   A 1 115 ? 28.501 -11.492 3.779   1.00 9.13  ?  115  ASN   A C    1 
ATOM   2522 O  O    . ASN   A 1 115 ? 29.220 -11.426 4.783   1.00 9.82  ?  115  ASN   A O    1 
ATOM   2523 C  CB   . ASN   A 1 115 ? 29.219 -9.879  2.012   1.00 9.65  ?  115  ASN   A CB   1 
ATOM   2524 C  CG   . ASN   A 1 115 ? 30.005 -9.664  0.742   1.00 10.58 ?  115  ASN   A CG   1 
ATOM   2525 O  OD1  . ASN   A 1 115 ? 31.221 -9.779  0.741   1.00 13.85 ?  115  ASN   A OD1  1 
ATOM   2526 N  ND2  . ASN   A 1 115 ? 29.320 -9.347  -0.341  1.00 10.13 ?  115  ASN   A ND2  1 
ATOM   2527 H  H    . ASN   A 1 115 ? 28.035 -11.594 0.743   1.00 11.15 ?  115  ASN   A H    1 
ATOM   2528 H  HA   . ASN   A 1 115 ? 30.006 -11.723 2.422   1.00 11.31 ?  115  ASN   A HA   1 
ATOM   2529 H  HB2  . ASN   A 1 115 ? 28.328 -9.519  1.895   1.00 11.58 ?  115  ASN   A HB2  1 
ATOM   2530 H  HB3  . ASN   A 1 115 ? 29.672 -9.408  2.734   1.00 11.58 ?  115  ASN   A HB3  1 
ATOM   2531 H  HD21 . ASN   A 1 115 ? 29.728 -9.212  -1.083  1.00 12.16 ?  115  ASN   A HD21 1 
ATOM   2532 H  HD22 . ASN   A 1 115 ? 28.459 -9.288  -0.306  1.00 12.16 ?  115  ASN   A HD22 1 
ATOM   2533 N  N    . PHE   A 1 116 ? 27.176 -11.659 3.864   1.00 9.37  ?  116  PHE   A N    1 
ATOM   2534 C  CA   . PHE   A 1 116 ? 26.531 -11.757 5.171   1.00 9.31  ?  116  PHE   A CA   1 
ATOM   2535 C  C    . PHE   A 1 116 ? 27.008 -12.987 5.939   1.00 9.76  ?  116  PHE   A C    1 
ATOM   2536 O  O    . PHE   A 1 116 ? 26.943 -13.000 7.168   1.00 10.51 ?  116  PHE   A O    1 
ATOM   2537 C  CB   . PHE   A 1 116 ? 25.003 -11.884 5.042   1.00 9.47  ?  116  PHE   A CB   1 
ATOM   2538 C  CG   . PHE   A 1 116 ? 24.246 -10.636 4.585   1.00 9.56  ?  116  PHE   A CG   1 
ATOM   2539 C  CD1  . PHE   A 1 116 ? 24.811 -9.615  3.828   1.00 9.71  ?  116  PHE   A CD1  1 
ATOM   2540 C  CD2  . PHE   A 1 116 ? 22.892 -10.537 4.906   1.00 10.06 ?  116  PHE   A CD2  1 
ATOM   2541 C  CE1  . PHE   A 1 116 ? 24.038 -8.533  3.415   1.00 9.85  ?  116  PHE   A CE1  1 
ATOM   2542 C  CE2  . PHE   A 1 116 ? 22.125 -9.462  4.498   1.00 10.10 ?  116  PHE   A CE2  1 
ATOM   2543 C  CZ   . PHE   A 1 116 ? 22.685 -8.461  3.749   1.00 9.75  ?  116  PHE   A CZ   1 
ATOM   2544 H  H    . PHE   A 1 116 ? 26.639 -11.714 3.190   1.00 11.25 ?  116  PHE   A H    1 
ATOM   2545 H  HA   . PHE   A 1 116 ? 26.732 -10.962 5.692   1.00 11.17 ?  116  PHE   A HA   1 
ATOM   2546 H  HB2  . PHE   A 1 116 ? 24.812 -12.589 4.403   1.00 11.37 ?  116  PHE   A HB2  1 
ATOM   2547 H  HB3  . PHE   A 1 116 ? 24.648 -12.135 5.909   1.00 11.37 ?  116  PHE   A HB3  1 
ATOM   2548 H  HD1  . PHE   A 1 116 ? 25.705 -9.671  3.592   1.00 11.65 ?  116  PHE   A HD1  1 
ATOM   2549 H  HD2  . PHE   A 1 116 ? 22.489 -11.223 5.401   1.00 12.07 ?  116  PHE   A HD2  1 
ATOM   2550 H  HE1  . PHE   A 1 116 ? 24.427 -7.856  2.914   1.00 11.82 ?  116  PHE   A HE1  1 
ATOM   2551 H  HE2  . PHE   A 1 116 ? 21.223 -9.429  4.732   1.00 12.12 ?  116  PHE   A HE2  1 
ATOM   2552 H  HZ   . PHE   A 1 116 ? 22.172 -7.731  3.487   1.00 11.69 ?  116  PHE   A HZ   1 
ATOM   2553 N  N    . ASN   A 1 117 ? 27.450 -14.035 5.235   1.00 9.76  ?  117  ASN   A N    1 
ATOM   2554 C  CA   . ASN   A 1 117 ? 27.828 -15.286 5.895   1.00 9.87  ?  117  ASN   A CA   1 
ATOM   2555 C  C    . ASN   A 1 117 ? 29.095 -15.163 6.721   1.00 10.39 ?  117  ASN   A C    1 
ATOM   2556 O  O    . ASN   A 1 117 ? 29.397 -16.079 7.494   1.00 11.21 ?  117  ASN   A O    1 
ATOM   2557 C  CB   . ASN   A 1 117 ? 27.937 -16.401 4.863   1.00 10.04 ?  117  ASN   A CB   1 
ATOM   2558 C  CG   . ASN   A 1 117 ? 26.581 -16.787 4.331   1.00 10.11 ?  117  ASN   A CG   1 
ATOM   2559 O  OD1  . ASN   A 1 117 ? 25.611 -16.826 5.090   1.00 11.05 ?  117  ASN   A OD1  1 
ATOM   2560 N  ND2  . ASN   A 1 117 ? 26.485 -17.041 3.040   1.00 10.06 ?  117  ASN   A ND2  1 
ATOM   2561 H  H    . ASN   A 1 117 ? 27.528 -14.043 4.373   1.00 11.71 ?  117  ASN   A H    1 
ATOM   2562 H  HA   . ASN   A 1 117 ? 27.107 -15.522 6.499   1.00 11.84 ?  117  ASN   A HA   1 
ATOM   2563 H  HB2  . ASN   A 1 117 ? 28.486 -16.097 4.119   1.00 12.05 ?  117  ASN   A HB2  1 
ATOM   2564 H  HB3  . ASN   A 1 117 ? 28.331 -17.178 5.277   1.00 12.05 ?  117  ASN   A HB3  1 
ATOM   2565 H  HD21 . ASN   A 1 117 ? 25.727 -17.249 2.697   1.00 12.07 ?  117  ASN   A HD21 1 
ATOM   2566 H  HD22 . ASN   A 1 117 ? 27.183 -16.978 2.536   1.00 12.07 ?  117  ASN   A HD22 1 
ATOM   2567 N  N    . GLN   A 1 118 ? 29.821 -14.053 6.594   1.00 10.50 ?  118  GLN   A N    1 
ATOM   2568 C  CA   . GLN   A 1 118 ? 31.000 -13.811 7.413   1.00 11.09 ?  118  GLN   A CA   1 
ATOM   2569 C  C    . GLN   A 1 118 ? 30.660 -13.239 8.782   1.00 10.88 ?  118  GLN   A C    1 
ATOM   2570 O  O    . GLN   A 1 118 ? 31.576 -12.946 9.558   1.00 12.52 ?  118  GLN   A O    1 
ATOM   2571 C  CB   . GLN   A 1 118 ? 31.986 -12.906 6.671   1.00 11.10 ?  118  GLN   A CB   1 
ATOM   2572 C  CG   . GLN   A 1 118 ? 32.449 -13.488 5.346   1.00 11.12 ?  118  GLN   A CG   1 
ATOM   2573 C  CD   . GLN   A 1 118 ? 33.276 -14.752 5.519   1.00 11.38 ?  118  GLN   A CD   1 
ATOM   2574 O  OE1  . GLN   A 1 118 ? 34.134 -14.822 6.405   1.00 12.26 ?  118  GLN   A OE1  1 
ATOM   2575 N  NE2  . GLN   A 1 118 ? 33.025 -15.752 4.674   1.00 11.80 ?  118  GLN   A NE2  1 
ATOM   2576 H  H    . GLN   A 1 118 ? 29.638 -13.410 6.041   1.00 12.60 ?  118  GLN   A H    1 
ATOM   2577 H  HA   . GLN   A 1 118 ? 31.433 -14.665 7.557   1.00 13.31 ?  118  GLN   A HA   1 
ATOM   2578 H  HB2  . GLN   A 1 118 ? 31.561 -12.056 6.499   1.00 13.32 ?  118  GLN   A HB2  1 
ATOM   2579 H  HB3  . GLN   A 1 118 ? 32.768 -12.781 7.233   1.00 13.32 ?  118  GLN   A HB3  1 
ATOM   2580 H  HG2  . GLN   A 1 118 ? 31.673 -13.703 4.804   1.00 13.34 ?  118  GLN   A HG2  1 
ATOM   2581 H  HG3  . GLN   A 1 118 ? 32.997 -12.827 4.889   1.00 13.34 ?  118  GLN   A HG3  1 
ATOM   2582 H  HE21 . GLN   A 1 118 ? 32.417 -15.662 4.067   1.00 14.16 ?  118  GLN   A HE21 1 
ATOM   2583 H  HE22 . GLN   A 1 118 ? 33.467 -16.485 4.730   1.00 14.16 ?  118  GLN   A HE22 1 
ATOM   2584 N  N    . HIS   A 1 119 ? 29.371 -13.088 9.099   1.00 10.45 ?  119  HIS   A N    1 
ATOM   2585 C  CA   . HIS   A 1 119 ? 28.922 -12.479 10.348  1.00 10.94 ?  119  HIS   A CA   1 
ATOM   2586 C  C    . HIS   A 1 119 ? 27.792 -13.305 10.933  1.00 11.28 ?  119  HIS   A C    1 
ATOM   2587 O  O    . HIS   A 1 119 ? 26.841 -13.644 10.226  1.00 12.02 ?  119  HIS   A O    1 
ATOM   2588 C  CB   . HIS   A 1 119 ? 28.460 -11.047 10.084  1.00 11.56 ?  119  HIS   A CB   1 
ATOM   2589 C  CG   . HIS   A 1 119 ? 29.527 -10.236 9.453   1.00 12.72 ?  119  HIS   A CG   1 
ATOM   2590 N  ND1  . HIS   A 1 119 ? 30.511 -9.624  10.192  1.00 15.05 ?  119  HIS   A ND1  1 
ATOM   2591 C  CD2  . HIS   A 1 119 ? 29.848 -10.050 8.152   1.00 13.83 ?  119  HIS   A CD2  1 
ATOM   2592 C  CE1  . HIS   A 1 119 ? 31.368 -9.045  9.369   1.00 15.43 ?  119  HIS   A CE1  1 
ATOM   2593 N  NE2  . HIS   A 1 119 ? 30.995 -9.297  8.127   1.00 15.40 ?  119  HIS   A NE2  1 
ATOM   2594 H  H    . HIS   A 1 119 ? 28.717 -13.349 8.597   1.00 12.54 ?  119  HIS   A H    1 
ATOM   2595 H  HA   . HIS   A 1 119 ? 29.660 -12.464 10.982  1.00 13.13 ?  119  HIS   A HA   1 
ATOM   2596 H  HB2  . HIS   A 1 119 ? 27.695 -11.072 9.489   1.00 13.87 ?  119  HIS   A HB2  1 
ATOM   2597 H  HB3  . HIS   A 1 119 ? 28.221 -10.637 10.927  1.00 13.87 ?  119  HIS   A HB3  1 
ATOM   2598 H  HD2  . HIS   A 1 119 ? 29.374 -10.369 7.412   1.00 16.59 ?  119  HIS   A HD2  1 
ATOM   2599 H  HE1  . HIS   A 1 119 ? 32.106 -8.542  9.617   1.00 18.52 ?  119  HIS   A HE1  1 
ATOM   2600 H  HE2  . HIS   A 1 119 ? 31.385 -9.007  7.415   1.00 18.48 ?  119  HIS   A HE2  1 
ATOM   2601 N  N    . GLU   A 1 120 ? 27.897 -13.616 12.225  1.00 11.98 ?  120  GLU   A N    1 
ATOM   2602 C  CA   . GLU   A 1 120 ? 26.947 -14.546 12.834  1.00 13.88 ?  120  GLU   A CA   1 
ATOM   2603 C  C    . GLU   A 1 120 ? 25.528 -13.983 12.895  1.00 12.58 ?  120  GLU   A C    1 
ATOM   2604 O  O    . GLU   A 1 120 ? 24.554 -14.749 12.792  1.00 12.67 ?  120  GLU   A O    1 
ATOM   2605 C  CB   . GLU   A 1 120 ? 27.425 -14.931 14.237  1.00 18.82 ?  120  GLU   A CB   1 
ATOM   2606 C  CG   . GLU   A 1 120 ? 28.597 -15.896 14.243  1.00 26.71 ?  120  GLU   A CG   1 
ATOM   2607 C  CD   . GLU   A 1 120 ? 28.735 -16.639 15.555  1.00 33.37 ?  120  GLU   A CD   1 
ATOM   2608 O  OE1  . GLU   A 1 120 ? 28.182 -16.169 16.573  1.00 35.16 ?  120  GLU   A OE1  1 
ATOM   2609 O  OE2  . GLU   A 1 120 ? 29.392 -17.702 15.566  1.00 37.32 -1 120  GLU   A OE2  1 
ATOM   2610 H  H    . GLU   A 1 120 ? 28.494 -13.305 12.767  1.00 14.37 ?  120  GLU   A H    1 
ATOM   2611 H  HA   . GLU   A 1 120 ? 26.926 -15.357 12.307  1.00 16.66 ?  120  GLU   A HA   1 
ATOM   2612 H  HB2  . GLU   A 1 120 ? 27.706 -14.131 14.711  1.00 22.58 ?  120  GLU   A HB2  1 
ATOM   2613 H  HB3  . GLU   A 1 120 ? 26.695 -15.354 14.718  1.00 22.58 ?  120  GLU   A HB3  1 
ATOM   2614 H  HG2  . GLU   A 1 120 ? 28.474 -16.553 13.541  1.00 32.05 ?  120  GLU   A HG2  1 
ATOM   2615 H  HG3  . GLU   A 1 120 ? 29.419 -15.405 14.104  1.00 32.05 ?  120  GLU   A HG3  1 
ATOM   2616 N  N    . VAL   A 1 121 ? 25.393 -12.673 13.104  1.00 11.98 ?  121  VAL   A N    1 
ATOM   2617 C  CA   . VAL   A 1 121 ? 24.097 -12.009 13.238  1.00 12.02 ?  121  VAL   A CA   1 
ATOM   2618 C  C    . VAL   A 1 121 ? 24.200 -10.621 12.611  1.00 10.83 ?  121  VAL   A C    1 
ATOM   2619 O  O    . VAL   A 1 121 ? 25.167 -9.893  12.852  1.00 11.84 ?  121  VAL   A O    1 
ATOM   2620 C  CB   . VAL   A 1 121 ? 23.663 -11.883 14.716  1.00 15.10 ?  121  VAL   A CB   1 
ATOM   2621 C  CG1  . VAL   A 1 121 ? 22.275 -11.263 14.809  1.00 15.87 ?  121  VAL   A CG1  1 
ATOM   2622 C  CG2  . VAL   A 1 121 ? 23.694 -13.220 15.436  1.00 17.41 ?  121  VAL   A CG2  1 
ATOM   2623 H  H    . VAL   A 1 121 ? 26.058 -12.132 13.182  1.00 14.38 ?  121  VAL   A H    1 
ATOM   2624 H  HA   . VAL   A 1 121 ? 23.423 -12.518 12.764  1.00 14.42 ?  121  VAL   A HA   1 
ATOM   2625 H  HB   . VAL   A 1 121 ? 24.274 -11.289 15.173  1.00 18.12 ?  121  VAL   A HB   1 
ATOM   2626 H  HG11 . VAL   A 1 121 ? 21.955 -11.337 15.724  1.00 19.04 ?  121  VAL   A HG11 1 
ATOM   2627 H  HG12 . VAL   A 1 121 ? 22.324 -10.328 14.555  1.00 19.04 ?  121  VAL   A HG12 1 
ATOM   2628 H  HG13 . VAL   A 1 121 ? 21.673 -11.737 14.213  1.00 19.04 ?  121  VAL   A HG13 1 
ATOM   2629 H  HG21 . VAL   A 1 121 ? 23.337 -13.105 16.337  1.00 20.90 ?  121  VAL   A HG21 1 
ATOM   2630 H  HG22 . VAL   A 1 121 ? 23.142 -13.857 14.951  1.00 20.90 ?  121  VAL   A HG22 1 
ATOM   2631 H  HG23 . VAL   A 1 121 ? 24.605 -13.537 15.482  1.00 20.90 ?  121  VAL   A HG23 1 
ATOM   2632 N  N    . LEU   A 1 122 ? 23.184 -10.238 11.829  1.00 10.42 ?  122  LEU   A N    1 
ATOM   2633 C  CA   . LEU   A 1 122 ? 23.180 -8.939  11.160  1.00 10.41 ?  122  LEU   A CA   1 
ATOM   2634 C  C    . LEU   A 1 122 ? 21.778 -8.356  11.134  1.00 10.08 ?  122  LEU   A C    1 
ATOM   2635 O  O    . LEU   A 1 122 ? 20.796 -9.083  10.990  1.00 11.11 ?  122  LEU   A O    1 
ATOM   2636 C  CB   . LEU   A 1 122 ? 23.592 -9.031  9.685   1.00 11.80 ?  122  LEU   A CB   1 
ATOM   2637 C  CG   . LEU   A 1 122 ? 24.800 -9.881  9.321   1.00 11.72 ?  122  LEU   A CG   1 
ATOM   2638 C  CD1  . LEU   A 1 122 ? 24.405 -11.337 9.097   1.00 12.49 ?  122  LEU   A CD1  1 
ATOM   2639 C  CD2  . LEU   A 1 122 ? 25.476 -9.315  8.087   1.00 11.38 ?  122  LEU   A CD2  1 
ATOM   2640 H  H    . LEU   A 1 122 ? 22.484 -10.714 11.665  1.00 12.51 ?  122  LEU   A H    1 
ATOM   2641 H  HA   . LEU   A 1 122 ? 23.776 -8.322  11.619  1.00 12.50 ?  122  LEU   A HA   1 
ATOM   2642 H  HB2  . LEU   A 1 122 ? 22.848 -9.391  9.188   1.00 14.16 ?  122  LEU   A HB2  1 
ATOM   2643 H  HB3  . LEU   A 1 122 ? 23.785 -8.136  9.371   1.00 14.16 ?  122  LEU   A HB3  1 
ATOM   2644 H  HG   . LEU   A 1 122 ? 25.451 -9.857  10.042  1.00 14.06 ?  122  LEU   A HG   1 
ATOM   2645 H  HD11 . LEU   A 1 122 ? 25.180 -11.845 8.815   1.00 14.99 ?  122  LEU   A HD11 1 
ATOM   2646 H  HD12 . LEU   A 1 122 ? 24.057 -11.700 9.928   1.00 14.99 ?  122  LEU   A HD12 1 
ATOM   2647 H  HD13 . LEU   A 1 122 ? 23.718 -11.376 8.410   1.00 14.99 ?  122  LEU   A HD13 1 
ATOM   2648 H  HD21 . LEU   A 1 122 ? 26.218 -9.888  7.832   1.00 13.65 ?  122  LEU   A HD21 1 
ATOM   2649 H  HD22 . LEU   A 1 122 ? 24.830 -9.274  7.364   1.00 13.65 ?  122  LEU   A HD22 1 
ATOM   2650 H  HD23 . LEU   A 1 122 ? 25.804 -8.423  8.286   1.00 13.65 ?  122  LEU   A HD23 1 
ATOM   2651 N  N    . LEU   A 1 123 ? 21.707 -7.029  11.236  1.00 9.99  ?  123  LEU   A N    1 
ATOM   2652 C  CA   . LEU   A 1 123 ? 20.534 -6.241  10.868  1.00 9.77  ?  123  LEU   A CA   1 
ATOM   2653 C  C    . LEU   A 1 123 ? 20.769 -5.716  9.458   1.00 9.26  ?  123  LEU   A C    1 
ATOM   2654 O  O    . LEU   A 1 123 ? 21.823 -5.131  9.199   1.00 10.03 ?  123  LEU   A O    1 
ATOM   2655 C  CB   . LEU   A 1 123 ? 20.409 -5.061  11.830  1.00 10.49 ?  123  LEU   A CB   1 
ATOM   2656 C  CG   . LEU   A 1 123 ? 19.364 -4.002  11.484  1.00 11.15 ?  123  LEU   A CG   1 
ATOM   2657 C  CD1  . LEU   A 1 123 ? 17.960 -4.595  11.519  1.00 12.04 ?  123  LEU   A CD1  1 
ATOM   2658 C  CD2  . LEU   A 1 123 ? 19.472 -2.812  12.434  1.00 11.50 ?  123  LEU   A CD2  1 
ATOM   2659 H  H    . LEU   A 1 123 ? 22.353 -6.539  11.531  1.00 11.99 ?  123  LEU   A H    1 
ATOM   2660 H  HA   . LEU   A 1 123 ? 19.721 -6.782  10.901  1.00 11.72 ?  123  LEU   A HA   1 
ATOM   2661 H  HB2  . LEU   A 1 123 ? 20.179 -5.401  12.711  1.00 12.59 ?  123  LEU   A HB2  1 
ATOM   2662 H  HB3  . LEU   A 1 123 ? 21.263 -4.610  11.873  1.00 12.59 ?  123  LEU   A HB3  1 
ATOM   2663 H  HG   . LEU   A 1 123 ? 19.517 -3.668  10.582  1.00 13.38 ?  123  LEU   A HG   1 
ATOM   2664 H  HD11 . LEU   A 1 123 ? 17.311 -3.900  11.344  1.00 14.45 ?  123  LEU   A HD11 1 
ATOM   2665 H  HD12 . LEU   A 1 123 ? 17.896 -5.290  10.846  1.00 14.45 ?  123  LEU   A HD12 1 
ATOM   2666 H  HD13 . LEU   A 1 123 ? 17.807 -4.977  12.401  1.00 14.45 ?  123  LEU   A HD13 1 
ATOM   2667 H  HD21 . LEU   A 1 123 ? 18.803 -2.152  12.197  1.00 13.80 ?  123  LEU   A HD21 1 
ATOM   2668 H  HD22 . LEU   A 1 123 ? 19.325 -3.125  13.340  1.00 13.80 ?  123  LEU   A HD22 1 
ATOM   2669 H  HD23 . LEU   A 1 123 ? 20.359 -2.430  12.354  1.00 13.80 ?  123  LEU   A HD23 1 
ATOM   2670 N  N    A ALA   A 1 124 ? 19.781 -5.848  8.572   0.50 8.64  ?  124  ALA   A N    1 
ATOM   2671 N  N    B ALA   A 1 124 ? 19.832 -5.969  8.544   0.50 9.59  ?  124  ALA   A N    1 
ATOM   2672 C  CA   A ALA   A 1 124 ? 20.045 -5.542  7.173   0.50 8.06  ?  124  ALA   A CA   1 
ATOM   2673 C  CA   B ALA   A 1 124 ? 20.133 -5.754  7.136   0.50 10.15 ?  124  ALA   A CA   1 
ATOM   2674 C  C    A ALA   A 1 124 ? 18.786 -5.068  6.462   0.50 8.01  ?  124  ALA   A C    1 
ATOM   2675 C  C    B ALA   A 1 124 ? 18.921 -5.278  6.351   0.50 9.46  ?  124  ALA   A C    1 
ATOM   2676 O  O    A ALA   A 1 124 ? 17.663 -5.362  6.894   0.50 8.62  ?  124  ALA   A O    1 
ATOM   2677 O  O    B ALA   A 1 124 ? 17.777 -5.614  6.688   0.50 9.70  ?  124  ALA   A O    1 
ATOM   2678 C  CB   A ALA   A 1 124 ? 20.605 -6.763  6.440   0.50 8.36  ?  124  ALA   A CB   1 
ATOM   2679 C  CB   B ALA   A 1 124 ? 20.696 -7.029  6.490   0.50 11.02 ?  124  ALA   A CB   1 
ATOM   2680 H  H    A ALA   A 1 124 ? 18.974 -6.100  8.754   0.50 10.37 ?  124  ALA   A H    1 
ATOM   2681 H  H    B ALA   A 1 124 ? 19.046 -6.267  8.706   0.50 11.51 ?  124  ALA   A H    1 
ATOM   2682 H  HA   A ALA   A 1 124 ? 20.711 -4.837  7.140   0.50 9.68  ?  124  ALA   A HA   1 
ATOM   2683 H  HA   B ALA   A 1 124 ? 20.815 -5.070  7.077   0.50 12.18 ?  124  ALA   A HA   1 
ATOM   2684 H  HB1  A ALA   A 1 124 ? 20.773 -6.522  5.517   0.50 10.03 ?  124  ALA   A HB1  1 
ATOM   2685 H  HB1  B ALA   A 1 124 ? 20.888 -6.855  5.555   0.50 13.23 ?  124  ALA   A HB1  1 
ATOM   2686 H  HB2  A ALA   A 1 124 ? 21.434 -7.034  6.868   0.50 10.03 ?  124  ALA   A HB2  1 
ATOM   2687 H  HB2  B ALA   A 1 124 ? 21.516 -7.280  6.951   0.50 13.23 ?  124  ALA   A HB2  1 
ATOM   2688 H  HB3  A ALA   A 1 124 ? 19.957 -7.481  6.487   0.50 10.03 ?  124  ALA   A HB3  1 
ATOM   2689 H  HB3  B ALA   A 1 124 ? 20.044 -7.740  6.569   0.50 13.23 ?  124  ALA   A HB3  1 
ATOM   2690 N  N    A PRO   A 1 125 ? 18.946 -4.340  5.358   0.50 8.57  ?  125  PRO   A N    1 
ATOM   2691 N  N    B PRO   A 1 125 ? 19.149 -4.522  5.280   0.50 8.52  ?  125  PRO   A N    1 
ATOM   2692 C  CA   A PRO   A 1 125 ? 17.870 -4.143  4.387   0.50 9.71  ?  125  PRO   A CA   1 
ATOM   2693 C  CA   B PRO   A 1 125 ? 18.073 -4.140  4.370   0.50 8.98  ?  125  PRO   A CA   1 
ATOM   2694 C  C    A PRO   A 1 125 ? 17.966 -5.198  3.287   0.50 9.11  ?  125  PRO   A C    1 
ATOM   2695 C  C    B PRO   A 1 125 ? 17.978 -5.135  3.229   0.50 9.58  ?  125  PRO   A C    1 
ATOM   2696 O  O    A PRO   A 1 125 ? 18.953 -5.930  3.173   0.50 9.26  ?  125  PRO   A O    1 
ATOM   2697 O  O    B PRO   A 1 125 ? 18.817 -6.033  3.103   0.50 10.00 ?  125  PRO   A O    1 
ATOM   2698 C  CB   A PRO   A 1 125 ? 18.222 -2.766  3.804   0.50 10.00 ?  125  PRO   A CB   1 
ATOM   2699 C  CB   B PRO   A 1 125 ? 18.574 -2.796  3.839   0.50 8.48  ?  125  PRO   A CB   1 
ATOM   2700 C  CG   A PRO   A 1 125 ? 19.728 -2.811  3.739   0.50 10.20 ?  125  PRO   A CG   1 
ATOM   2701 C  CG   B PRO   A 1 125 ? 20.055 -3.053  3.670   0.50 7.82  ?  125  PRO   A CG   1 
ATOM   2702 C  CD   A PRO   A 1 125 ? 20.159 -3.587  4.979   0.50 9.71  ?  125  PRO   A CD   1 
ATOM   2703 C  CD   B PRO   A 1 125 ? 20.439 -3.961  4.836   0.50 7.80  ?  125  PRO   A CD   1 
ATOM   2704 H  HA   A PRO   A 1 125 ? 16.993 -4.129  4.804   0.50 11.65 ?  125  PRO   A HA   1 
ATOM   2705 H  HA   B PRO   A 1 125 ? 17.213 -4.050  4.827   0.50 10.77 ?  125  PRO   A HA   1 
ATOM   2706 H  HB2  A PRO   A 1 125 ? 17.839 -2.666  2.916   0.50 12.00 ?  125  PRO   A HB2  1 
ATOM   2707 H  HB2  B PRO   A 1 125 ? 18.154 -2.595  2.993   0.50 10.17 ?  125  PRO   A HB2  1 
ATOM   2708 H  HB3  A PRO   A 1 125 ? 17.921 -2.056  4.395   0.50 12.00 ?  125  PRO   A HB3  1 
ATOM   2709 H  HB3  B PRO   A 1 125 ? 18.416 -2.101  4.493   0.50 10.17 ?  125  PRO   A HB3  1 
ATOM   2710 H  HG2  A PRO   A 1 125 ? 20.008 -3.273  2.932   0.50 12.24 ?  125  PRO   A HG2  1 
ATOM   2711 H  HG2  B PRO   A 1 125 ? 20.211 -3.497  2.818   0.50 9.38  ?  125  PRO   A HG2  1 
ATOM   2712 H  HG3  A PRO   A 1 125 ? 20.086 -1.907  3.753   0.50 12.24 ?  125  PRO   A HG3  1 
ATOM   2713 H  HG3  B PRO   A 1 125 ? 20.535 -2.212  3.709   0.50 9.38  ?  125  PRO   A HG3  1 
ATOM   2714 H  HD2  A PRO   A 1 125 ? 20.888 -4.187  4.762   0.50 11.65 ?  125  PRO   A HD2  1 
ATOM   2715 H  HD2  B PRO   A 1 125 ? 21.040 -4.665  4.533   0.50 9.36  ?  125  PRO   A HD2  1 
ATOM   2716 H  HD3  A PRO   A 1 125 ? 20.414 -2.965  5.687   0.50 11.65 ?  125  PRO   A HD3  1 
ATOM   2717 H  HD3  B PRO   A 1 125 ? 20.842 -3.439  5.548   0.50 9.36  ?  125  PRO   A HD3  1 
ATOM   2718 N  N    A LEU   A 1 126 ? 16.932 -5.239  2.449   0.50 9.00  ?  126  LEU   A N    1 
ATOM   2719 N  N    B LEU   A 1 126 ? 16.983 -4.958  2.371   0.50 10.25 ?  126  LEU   A N    1 
ATOM   2720 C  CA   A LEU   A 1 126 ? 16.977 -6.076  1.258   0.50 9.84  ?  126  LEU   A CA   1 
ATOM   2721 C  CA   B LEU   A 1 126 ? 16.870 -5.751  1.150   0.50 9.96  ?  126  LEU   A CA   1 
ATOM   2722 C  C    A LEU   A 1 126 ? 17.912 -5.460  0.225   0.50 10.39 ?  126  LEU   A C    1 
ATOM   2723 C  C    B LEU   A 1 126 ? 17.817 -5.193  0.095   0.50 9.78  ?  126  LEU   A C    1 
ATOM   2724 O  O    A LEU   A 1 126 ? 17.749 -4.302  -0.169  0.50 11.26 ?  126  LEU   A O    1 
ATOM   2725 O  O    B LEU   A 1 126 ? 17.525 -4.182  -0.548  0.50 10.32 ?  126  LEU   A O    1 
ATOM   2726 C  CB   A LEU   A 1 126 ? 15.577 -6.233  0.668   0.50 10.34 ?  126  LEU   A CB   1 
ATOM   2727 C  CB   B LEU   A 1 126 ? 15.436 -5.728  0.646   0.50 10.95 ?  126  LEU   A CB   1 
ATOM   2728 C  CG   A LEU   A 1 126 ? 14.651 -7.212  1.395   0.50 11.02 ?  126  LEU   A CG   1 
ATOM   2729 C  CG   B LEU   A 1 126 ? 14.472 -6.584  1.456   0.50 11.88 ?  126  LEU   A CG   1 
ATOM   2730 C  CD1  A LEU   A 1 126 ? 13.228 -7.069  0.882   0.50 11.92 ?  126  LEU   A CD1  1 
ATOM   2731 C  CD1  B LEU   A 1 126 ? 13.090 -6.446  0.867   0.50 12.79 ?  126  LEU   A CD1  1 
ATOM   2732 C  CD2  A LEU   A 1 126 ? 15.143 -8.645  1.225   0.50 11.25 ?  126  LEU   A CD2  1 
ATOM   2733 C  CD2  B LEU   A 1 126 ? 14.897 -8.042  1.459   0.50 12.11 ?  126  LEU   A CD2  1 
ATOM   2734 H  H    A LEU   A 1 126 ? 16.207 -4.781  2.531   0.50 10.80 ?  126  LEU   A H    1 
ATOM   2735 H  H    B LEU   A 1 126 ? 16.351 -4.384  2.489   0.50 12.30 ?  126  LEU   A H    1 
ATOM   2736 H  HA   A LEU   A 1 126 ? 17.313 -6.953  1.486   0.50 11.81 ?  126  LEU   A HA   1 
ATOM   2737 H  HA   B LEU   A 1 126 ? 17.122 -6.669  1.345   0.50 11.96 ?  126  LEU   A HA   1 
ATOM   2738 H  HB2  A LEU   A 1 126 ? 15.139 -5.367  0.679   0.50 12.40 ?  126  LEU   A HB2  1 
ATOM   2739 H  HB2  B LEU   A 1 126 ? 15.109 -4.812  0.675   0.50 13.14 ?  126  LEU   A HB2  1 
ATOM   2740 H  HB3  A LEU   A 1 126 ? 15.655 -6.543  -0.247  0.50 12.40 ?  126  LEU   A HB3  1 
ATOM   2741 H  HB3  B LEU   A 1 126 ? 15.421 -6.052  -0.265  0.50 13.14 ?  126  LEU   A HB3  1 
ATOM   2742 H  HG   A LEU   A 1 126 ? 14.646 -7.006  2.343   0.50 13.22 ?  126  LEU   A HG   1 
ATOM   2743 H  HG   B LEU   A 1 126 ? 14.445 -6.266  2.374   0.50 14.26 ?  126  LEU   A HG   1 
ATOM   2744 H  HD11 A LEU   A 1 126 ? 12.657 -7.700  1.348   0.50 14.31 ?  126  LEU   A HD11 1 
ATOM   2745 H  HD11 B LEU   A 1 126 ? 12.471 -6.980  1.385   0.50 15.35 ?  126  LEU   A HD11 1 
ATOM   2746 H  HD12 A LEU   A 1 126 ? 12.923 -6.163  1.045   0.50 14.31 ?  126  LEU   A HD12 1 
ATOM   2747 H  HD12 B LEU   A 1 126 ? 12.828 -5.512  0.893   0.50 15.35 ?  126  LEU   A HD12 1 
ATOM   2748 H  HD13 A LEU   A 1 126 ? 13.216 -7.255  -0.071  0.50 14.31 ?  126  LEU   A HD13 1 
ATOM   2749 H  HD13 B LEU   A 1 126 ? 13.111 -6.757  -0.052  0.50 15.35 ?  126  LEU   A HD13 1 
ATOM   2750 H  HD21 A LEU   A 1 126 ? 14.478 -9.253  1.577   0.50 13.50 ?  126  LEU   A HD21 1 
ATOM   2751 H  HD21 B LEU   A 1 126 ? 14.147 -8.590  1.727   0.50 14.53 ?  126  LEU   A HD21 1 
ATOM   2752 H  HD22 A LEU   A 1 126 ? 15.284 -8.817  0.280   0.50 13.50 ?  126  LEU   A HD22 1 
ATOM   2753 H  HD22 B LEU   A 1 126 ? 15.183 -8.285  0.562   0.50 14.53 ?  126  LEU   A HD22 1 
ATOM   2754 H  HD23 A LEU   A 1 126 ? 15.978 -8.748  1.707   0.50 13.50 ?  126  LEU   A HD23 1 
ATOM   2755 H  HD23 B LEU   A 1 126 ? 15.633 -8.154  2.080   0.50 14.53 ?  126  LEU   A HD23 1 
ATOM   2756 N  N    A LEU   A 1 127 ? 18.890 -6.244  -0.219  0.50 10.64 ?  127  LEU   A N    1 
ATOM   2757 N  N    B LEU   A 1 127 ? 18.938 -5.877  -0.121  0.50 9.92  ?  127  LEU   A N    1 
ATOM   2758 C  CA   A LEU   A 1 127 ? 19.881 -5.741  -1.154  0.50 9.73  ?  127  LEU   A CA   1 
ATOM   2759 C  CA   B LEU   A 1 127 ? 19.921 -5.393  -1.078  0.50 9.80  ?  127  LEU   A CA   1 
ATOM   2760 C  C    A LEU   A 1 127 ? 19.260 -5.515  -2.522  0.50 9.14  ?  127  LEU   A C    1 
ATOM   2761 C  C    B LEU   A 1 127 ? 19.343 -5.347  -2.490  0.50 9.80  ?  127  LEU   A C    1 
ATOM   2762 O  O    A LEU   A 1 127 ? 18.440 -6.305  -2.997  0.50 9.73  ?  127  LEU   A O    1 
ATOM   2763 O  O    B LEU   A 1 127 ? 18.515 -6.174  -2.881  0.50 10.38 ?  127  LEU   A O    1 
ATOM   2764 C  CB   A LEU   A 1 127 ? 21.045 -6.722  -1.272  0.50 9.39  ?  127  LEU   A CB   1 
ATOM   2765 C  CB   B LEU   A 1 127 ? 21.159 -6.288  -1.060  0.50 10.23 ?  127  LEU   A CB   1 
ATOM   2766 C  CG   A LEU   A 1 127 ? 21.861 -6.951  0.000   0.50 9.37  ?  127  LEU   A CG   1 
ATOM   2767 C  CG   B LEU   A 1 127 ? 21.945 -6.323  0.252   0.50 11.03 ?  127  LEU   A CG   1 
ATOM   2768 C  CD1  A LEU   A 1 127 ? 22.982 -7.924  -0.288  0.50 9.39  ?  127  LEU   A CD1  1 
ATOM   2769 C  CD1  B LEU   A 1 127 ? 23.096 -7.296  0.153   0.50 11.66 ?  127  LEU   A CD1  1 
ATOM   2770 C  CD2  A LEU   A 1 127 ? 22.420 -5.648  0.541   0.50 10.01 ?  127  LEU   A CD2  1 
ATOM   2771 C  CD2  B LEU   A 1 127 ? 22.454 -4.931  0.603   0.50 11.82 ?  127  LEU   A CD2  1 
ATOM   2772 H  H    A LEU   A 1 127 ? 18.998 -7.069  0.004   0.50 12.76 ?  127  LEU   A H    1 
ATOM   2773 H  H    B LEU   A 1 127 ? 19.152 -6.615  0.285   0.50 11.90 ?  127  LEU   A H    1 
ATOM   2774 H  HA   A LEU   A 1 127 ? 20.223 -4.897  -0.838  0.50 11.67 ?  127  LEU   A HA   1 
ATOM   2775 H  HA   B LEU   A 1 127 ? 20.190 -4.495  -0.821  0.50 11.76 ?  127  LEU   A HA   1 
ATOM   2776 H  HB2  A LEU   A 1 127 ? 20.695 -7.585  -1.545  0.50 11.26 ?  127  LEU   A HB2  1 
ATOM   2777 H  HB2  B LEU   A 1 127 ? 20.884 -7.196  -1.256  0.50 12.28 ?  127  LEU   A HB2  1 
ATOM   2778 H  HB3  A LEU   A 1 127 ? 21.658 -6.395  -1.949  0.50 11.26 ?  127  LEU   A HB3  1 
ATOM   2779 H  HB3  B LEU   A 1 127 ? 21.767 -5.977  -1.749  0.50 12.28 ?  127  LEU   A HB3  1 
ATOM   2780 H  HG   A LEU   A 1 127 ? 21.288 -7.345  0.680   0.50 11.25 ?  127  LEU   A HG   1 
ATOM   2781 H  HG   B LEU   A 1 127 ? 21.358 -6.621  0.967   0.50 13.24 ?  127  LEU   A HG   1 
ATOM   2782 H  HD11 A LEU   A 1 127 ? 23.467 -8.106  0.535   0.50 11.27 ?  127  LEU   A HD11 1 
ATOM   2783 H  HD11 B LEU   A 1 127 ? 23.626 -7.240  0.965   0.50 13.99 ?  127  LEU   A HD11 1 
ATOM   2784 H  HD12 A LEU   A 1 127 ? 22.609 -8.751  -0.636  0.50 11.27 ?  127  LEU   A HD12 1 
ATOM   2785 H  HD12 B LEU   A 1 127 ? 22.745 -8.194  0.048   0.50 13.99 ?  127  LEU   A HD12 1 
ATOM   2786 H  HD13 A LEU   A 1 127 ? 23.581 -7.533  -0.943  0.50 11.27 ?  127  LEU   A HD13 1 
ATOM   2787 H  HD13 B LEU   A 1 127 ? 23.642 -7.061  -0.613  0.50 13.99 ?  127  LEU   A HD13 1 
ATOM   2788 H  HD21 A LEU   A 1 127 ? 23.051 -5.846  1.249   0.50 12.01 ?  127  LEU   A HD21 1 
ATOM   2789 H  HD21 B LEU   A 1 127 ? 23.077 -5.002  1.342   0.50 14.18 ?  127  LEU   A HD21 1 
ATOM   2790 H  HD22 A LEU   A 1 127 ? 22.868 -5.177  -0.181  0.50 12.01 ?  127  LEU   A HD22 1 
ATOM   2791 H  HD22 B LEU   A 1 127 ? 22.901 -4.558  -0.173  0.50 14.18 ?  127  LEU   A HD22 1 
ATOM   2792 H  HD23 A LEU   A 1 127 ? 21.691 -5.111  0.884   0.50 12.01 ?  127  LEU   A HD23 1 
ATOM   2793 H  HD23 B LEU   A 1 127 ? 21.702 -4.374  0.853   0.50 14.18 ?  127  LEU   A HD23 1 
ATOM   2794 N  N    A SER   A 1 128 ? 19.673 -4.423  -3.154  0.50 9.30  ?  128  SER   A N    1 
ATOM   2795 N  N    B SER   A 1 128 ? 19.812 -4.361  -3.255  0.50 10.15 ?  128  SER   A N    1 
ATOM   2796 C  CA   A SER   A 1 128 ? 19.251 -4.000  -4.482  0.50 9.52  ?  128  SER   A CA   1 
ATOM   2797 C  CA   B SER   A 1 128 ? 19.442 -4.125  -4.650  0.50 9.68  ?  128  SER   A CA   1 
ATOM   2798 C  C    A SER   A 1 128 ? 17.789 -3.569  -4.549  0.50 10.10 ?  128  SER   A C    1 
ATOM   2799 C  C    B SER   A 1 128 ? 18.011 -3.622  -4.844  0.50 9.28  ?  128  SER   A C    1 
ATOM   2800 O  O    A SER   A 1 128 ? 17.292 -3.289  -5.644  0.50 11.32 ?  128  SER   A O    1 
ATOM   2801 O  O    B SER   A 1 128 ? 17.643 -3.245  -5.959  0.50 9.59  ?  128  SER   A O    1 
ATOM   2802 C  CB   A SER   A 1 128 ? 19.598 -5.016  -5.578  0.50 9.31  ?  128  SER   A CB   1 
ATOM   2803 C  CB   B SER   A 1 128 ? 19.746 -5.335  -5.542  0.50 9.98  ?  128  SER   A CB   1 
ATOM   2804 O  OG   A SER   A 1 128 ? 21.003 -5.218  -5.644  0.50 10.12 ?  128  SER   A OG   1 
ATOM   2805 O  OG   B SER   A 1 128 ? 21.149 -5.489  -5.722  0.50 10.20 ?  128  SER   A OG   1 
ATOM   2806 H  H    A SER   A 1 128 ? 20.244 -3.877  -2.808  0.50 11.16 ?  128  SER   A H    1 
ATOM   2807 H  H    B SER   A 1 128 ? 20.396 -3.795  -2.974  0.50 12.18 ?  128  SER   A H    1 
ATOM   2808 H  HA   A SER   A 1 128 ? 19.770 -3.216  -4.685  0.50 11.42 ?  128  SER   A HA   1 
ATOM   2809 H  HA   B SER   A 1 128 ? 20.010 -3.415  -4.970  0.50 11.62 ?  128  SER   A HA   1 
ATOM   2810 H  HB2  A SER   A 1 128 ? 19.163 -5.862  -5.385  0.50 11.17 ?  128  SER   A HB2  1 
ATOM   2811 H  HB2  B SER   A 1 128 ? 19.394 -6.141  -5.135  0.50 11.98 ?  128  SER   A HB2  1 
ATOM   2812 H  HB3  A SER   A 1 128 ? 19.286 -4.674  -6.434  0.50 11.17 ?  128  SER   A HB3  1 
ATOM   2813 H  HB3  B SER   A 1 128 ? 19.332 -5.199  -6.413  0.50 11.98 ?  128  SER   A HB3  1 
ATOM   2814 H  HG   A SER   A 1 128 ? 21.389 -4.488  -5.809  0.50 12.14 ?  128  SER   A HG   1 
ATOM   2815 H  HG   B SER   A 1 128 ? 21.466 -4.792  -6.081  0.50 12.24 ?  128  SER   A HG   1 
ATOM   2816 N  N    A ALA   A 1 129 ? 17.095 -3.487  -3.412  0.50 10.64 ?  129  ALA   A N    1 
ATOM   2817 N  N    B ALA   A 1 129 ? 17.213 -3.587  -3.779  0.50 9.93  ?  129  ALA   A N    1 
ATOM   2818 C  CA   A ALA   A 1 129 ? 15.738 -2.966  -3.379  0.50 10.79 ?  129  ALA   A CA   1 
ATOM   2819 C  CA   B ALA   A 1 129 ? 15.840 -3.115  -3.857  0.50 10.29 ?  129  ALA   A CA   1 
ATOM   2820 C  C    A ALA   A 1 129 ? 15.773 -1.438  -3.368  0.50 10.76 ?  129  ALA   A C    1 
ATOM   2821 C  C    B ALA   A 1 129 ? 15.815 -1.590  -3.707  0.50 10.21 ?  129  ALA   A C    1 
ATOM   2822 O  O    A ALA   A 1 129 ? 16.831 -0.807  -3.476  0.50 10.85 ?  129  ALA   A O    1 
ATOM   2823 O  O    B ALA   A 1 129 ? 16.853 -0.920  -3.696  0.50 10.83 ?  129  ALA   A O    1 
ATOM   2824 C  CB   A ALA   A 1 129 ? 14.973 -3.536  -2.181  0.50 11.36 ?  129  ALA   A CB   1 
ATOM   2825 C  CB   B ALA   A 1 129 ? 14.974 -3.850  -2.831  0.50 10.90 ?  129  ALA   A CB   1 
ATOM   2826 H  H    A ALA   A 1 129 ? 17.391 -3.730  -2.637  0.50 12.77 ?  129  ALA   A H    1 
ATOM   2827 H  H    B ALA   A 1 129 ? 17.451 -3.836  -2.988  0.50 11.92 ?  129  ALA   A H    1 
ATOM   2828 H  HA   A ALA   A 1 129 ? 15.278 -3.245  -4.180  0.50 12.95 ?  129  ALA   A HA   1 
ATOM   2829 H  HA   B ALA   A 1 129 ? 15.494 -3.337  -4.735  0.50 12.35 ?  129  ALA   A HA   1 
ATOM   2830 H  HB1  A ALA   A 1 129 ? 14.067 -3.186  -2.185  0.50 13.64 ?  129  ALA   A HB1  1 
ATOM   2831 H  HB1  B ALA   A 1 129 ? 14.079 -3.482  -2.855  0.50 13.08 ?  129  ALA   A HB1  1 
ATOM   2832 H  HB2  A ALA   A 1 129 ? 14.950 -4.505  -2.253  0.50 13.64 ?  129  ALA   A HB2  1 
ATOM   2833 H  HB2  B ALA   A 1 129 ? 14.952 -4.794  -3.050  0.50 13.08 ?  129  ALA   A HB2  1 
ATOM   2834 H  HB3  A ALA   A 1 129 ? 15.423 -3.279  -1.361  0.50 13.64 ?  129  ALA   A HB3  1 
ATOM   2835 H  HB3  B ALA   A 1 129 ? 15.361 -3.726  -1.949  0.50 13.08 ?  129  ALA   A HB3  1 
ATOM   2836 N  N    A GLY   A 1 130 ? 14.599 -0.829  -3.244  0.50 11.65 ?  130  GLY   A N    1 
ATOM   2837 N  N    B GLY   A 1 130 ? 14.615 -1.025  -3.614  0.50 10.45 ?  130  GLY   A N    1 
ATOM   2838 C  CA   A GLY   A 1 130 ? 14.544 0.624   -3.211  0.50 12.39 ?  130  GLY   A CA   1 
ATOM   2839 C  CA   B GLY   A 1 130 ? 14.491 0.417   -3.507  0.50 11.02 ?  130  GLY   A CA   1 
ATOM   2840 C  C    A GLY   A 1 130 ? 15.121 1.221   -4.481  0.50 12.41 ?  130  GLY   A C    1 
ATOM   2841 C  C    B GLY   A 1 130 ? 15.132 1.112   -4.689  0.50 10.95 ?  130  GLY   A C    1 
ATOM   2842 O  O    A GLY   A 1 130 ? 14.807 0.789   -5.594  0.50 12.96 ?  130  GLY   A O    1 
ATOM   2843 O  O    B GLY   A 1 130 ? 14.996 0.690   -5.843  0.50 11.12 ?  130  GLY   A O    1 
ATOM   2844 H  H    A GLY   A 1 130 ? 13.832 -1.223  -3.180  0.50 13.98 ?  130  GLY   A H    1 
ATOM   2845 H  H    B GLY   A 1 130 ? 13.870 -1.454  -3.614  0.50 12.54 ?  130  GLY   A H    1 
ATOM   2846 H  HA2  A GLY   A 1 130 ? 13.621 0.917   -3.112  0.50 14.87 ?  130  GLY   A HA2  1 
ATOM   2847 H  HA2  B GLY   A 1 130 ? 13.552 0.660   -3.466  0.50 13.22 ?  130  GLY   A HA2  1 
ATOM   2848 H  HA3  A GLY   A 1 130 ? 15.054 0.954   -2.457  0.50 14.87 ?  130  GLY   A HA3  1 
ATOM   2849 H  HA3  B GLY   A 1 130 ? 14.927 0.726   -2.700  0.50 13.22 ?  130  GLY   A HA3  1 
ATOM   2850 N  N    A ILE   A 1 131 ? 15.990 2.225   -4.316  0.50 12.33 ?  131  ILE   A N    1 
ATOM   2851 N  N    B ILE   A 1 131 ? 15.857 2.195   -4.397  0.50 11.70 ?  131  ILE   A N    1 
ATOM   2852 C  CA   A ILE   A 1 131 ? 16.513 2.980   -5.454  0.50 12.02 ?  131  ILE   A CA   1 
ATOM   2853 C  CA   B ILE   A 1 131 ? 16.474 3.011   -5.437  0.50 11.90 ?  131  ILE   A CA   1 
ATOM   2854 C  C    A ILE   A 1 131 ? 17.520 2.202   -6.283  0.50 11.36 ?  131  ILE   A C    1 
ATOM   2855 C  C    B ILE   A 1 131 ? 17.485 2.247   -6.285  0.50 11.54 ?  131  ILE   A C    1 
ATOM   2856 O  O    A ILE   A 1 131 ? 17.929 2.690   -7.344  0.50 12.27 ?  131  ILE   A O    1 
ATOM   2857 O  O    B ILE   A 1 131 ? 17.900 2.759   -7.330  0.50 12.30 ?  131  ILE   A O    1 
ATOM   2858 C  CB   A ILE   A 1 131 ? 17.092 4.354   -5.047  0.50 12.62 ?  131  ILE   A CB   1 
ATOM   2859 C  CB   B ILE   A 1 131 ? 17.085 4.308   -4.852  0.50 12.88 ?  131  ILE   A CB   1 
ATOM   2860 C  CG1  A ILE   A 1 131 ? 18.351 4.193   -4.184  0.50 13.16 ?  131  ILE   A CG1  1 
ATOM   2861 C  CG1  B ILE   A 1 131 ? 18.258 3.996   -3.917  0.50 13.65 ?  131  ILE   A CG1  1 
ATOM   2862 C  CG2  A ILE   A 1 131 ? 16.035 5.183   -4.333  0.50 12.92 ?  131  ILE   A CG2  1 
ATOM   2863 C  CG2  B ILE   A 1 131 ? 16.019 5.121   -4.128  0.50 13.56 ?  131  ILE   A CG2  1 
ATOM   2864 C  CD1  A ILE   A 1 131 ? 19.021 5.518   -3.828  0.50 13.61 ?  131  ILE   A CD1  1 
ATOM   2865 C  CD1  B ILE   A 1 131 ? 18.911 5.237   -3.317  0.50 14.33 ?  131  ILE   A CD1  1 
ATOM   2866 H  H    A ILE   A 1 131 ? 16.284 2.483   -3.558  0.50 14.79 ?  131  ILE   A H    1 
ATOM   2867 H  H    B ILE   A 1 131 ? 15.983 2.489   -3.599  0.50 14.04 ?  131  ILE   A H    1 
ATOM   2868 H  HA   A ILE   A 1 131 ? 15.775 3.162   -6.048  0.50 14.42 ?  131  ILE   A HA   1 
ATOM   2869 H  HA   B ILE   A 1 131 ? 15.772 3.290   -6.038  0.50 14.28 ?  131  ILE   A HA   1 
ATOM   2870 H  HB   A ILE   A 1 131 ? 17.344 4.823   -5.857  0.50 15.14 ?  131  ILE   A HB   1 
ATOM   2871 H  HB   B ILE   A 1 131 ? 17.418 4.840   -5.590  0.50 15.46 ?  131  ILE   A HB   1 
ATOM   2872 H  HG12 A ILE   A 1 131 ? 18.110 3.750   -3.357  0.50 15.79 ?  131  ILE   A HG12 1 
ATOM   2873 H  HG12 B ILE   A 1 131 ? 17.938 3.448   -3.185  0.50 16.37 ?  131  ILE   A HG12 1 
ATOM   2874 H  HG13 A ILE   A 1 131 ? 19.003 3.659   -4.666  0.50 15.79 ?  131  ILE   A HG13 1 
ATOM   2875 H  HG13 B ILE   A 1 131 ? 18.939 3.520   -4.415  0.50 16.37 ?  131  ILE   A HG13 1 
ATOM   2876 H  HG21 A ILE   A 1 131 ? 16.363 6.086   -4.221  0.50 15.50 ?  131  ILE   A HG21 1 
ATOM   2877 H  HG21 B ILE   A 1 131 ? 16.368 6.006   -3.942  0.50 16.28 ?  131  ILE   A HG21 1 
ATOM   2878 H  HG22 A ILE   A 1 131 ? 15.227 5.186   -4.871  0.50 15.50 ?  131  ILE   A HG22 1 
ATOM   2879 H  HG22 B ILE   A 1 131 ? 15.235 5.186   -4.695  0.50 16.28 ?  131  ILE   A HG22 1 
ATOM   2880 H  HG23 A ILE   A 1 131 ? 15.853 4.782   -3.468  0.50 15.50 ?  131  ILE   A HG23 1 
ATOM   2881 H  HG23 B ILE   A 1 131 ? 15.791 4.672   -3.299  0.50 16.28 ?  131  ILE   A HG23 1 
ATOM   2882 H  HD11 A ILE   A 1 131 ? 19.867 5.338   -3.388  0.50 16.33 ?  131  ILE   A HD11 1 
ATOM   2883 H  HD11 B ILE   A 1 131 ? 19.724 4.977   -2.857  0.50 17.20 ?  131  ILE   A HD11 1 
ATOM   2884 H  HD12 A ILE   A 1 131 ? 19.175 6.025   -4.642  0.50 16.33 ?  131  ILE   A HD12 1 
ATOM   2885 H  HD12 B ILE   A 1 131 ? 19.120 5.863   -4.030  0.50 17.20 ?  131  ILE   A HD12 1 
ATOM   2886 H  HD13 A ILE   A 1 131 ? 18.440 6.019   -3.233  0.50 16.33 ?  131  ILE   A HD13 1 
ATOM   2887 H  HD13 B ILE   A 1 131 ? 18.295 5.650   -2.689  0.50 17.20 ?  131  ILE   A HD13 1 
ATOM   2888 N  N    A PHE   A 1 132 ? 17.937 1.012   -5.837  0.50 11.08 ?  132  PHE   A N    1 
ATOM   2889 N  N    B PHE   A 1 132 ? 17.891 1.035   -5.876  0.50 11.62 ?  132  PHE   A N    1 
ATOM   2890 C  CA   A PHE   A 1 132 ? 18.749 0.144   -6.683  0.50 10.92 ?  132  PHE   A CA   1 
ATOM   2891 C  CA   B PHE   A 1 132 ? 18.823 0.243   -6.678  0.50 11.93 ?  132  PHE   A CA   1 
ATOM   2892 C  C    A PHE   A 1 132 ? 17.918 -0.591  -7.735  0.50 10.51 ?  132  PHE   A C    1 
ATOM   2893 C  C    B PHE   A 1 132 ? 18.152 -0.505  -7.832  0.50 12.82 ?  132  PHE   A C    1 
ATOM   2894 O  O    A PHE   A 1 132 ? 18.495 -1.236  -8.616  0.50 10.71 ?  132  PHE   A O    1 
ATOM   2895 O  O    B PHE   A 1 132 ? 18.864 -1.052  -8.682  0.50 14.10 ?  132  PHE   A O    1 
ATOM   2896 C  CB   A PHE   A 1 132 ? 19.551 -0.854  -5.838  0.50 11.21 ?  132  PHE   A CB   1 
ATOM   2897 C  CB   B PHE   A 1 132 ? 19.623 -0.736  -5.805  0.50 11.27 ?  132  PHE   A CB   1 
ATOM   2898 C  CG   A PHE   A 1 132 ? 20.772 -0.266  -5.157  0.50 11.18 ?  132  PHE   A CG   1 
ATOM   2899 C  CG   B PHE   A 1 132 ? 20.828 -0.121  -5.122  0.50 10.95 ?  132  PHE   A CG   1 
ATOM   2900 C  CD1  A PHE   A 1 132 ? 20.652 0.757   -4.228  0.50 11.82 ?  132  PHE   A CD1  1 
ATOM   2901 C  CD1  B PHE   A 1 132 ? 20.671 0.844   -4.140  0.50 11.87 ?  132  PHE   A CD1  1 
ATOM   2902 C  CD2  A PHE   A 1 132 ? 22.034 -0.784  -5.410  0.50 11.78 ?  132  PHE   A CD2  1 
ATOM   2903 C  CD2  B PHE   A 1 132 ? 22.115 -0.536  -5.441  0.50 11.60 ?  132  PHE   A CD2  1 
ATOM   2904 C  CE1  A PHE   A 1 132 ? 21.774 1.277   -3.594  0.50 11.83 ?  132  PHE   A CE1  1 
ATOM   2905 C  CE1  B PHE   A 1 132 ? 21.770 1.400   -3.505  0.50 12.11 ?  132  PHE   A CE1  1 
ATOM   2906 C  CE2  A PHE   A 1 132 ? 23.155 -0.274  -4.776  0.50 11.82 ?  132  PHE   A CE2  1 
ATOM   2907 C  CE2  B PHE   A 1 132 ? 23.218 0.016   -4.804  0.50 12.21 ?  132  PHE   A CE2  1 
ATOM   2908 C  CZ   A PHE   A 1 132 ? 23.023 0.760   -3.867  0.50 11.51 ?  132  PHE   A CZ   1 
ATOM   2909 C  CZ   B PHE   A 1 132 ? 23.041 0.983   -3.834  0.50 12.07 ?  132  PHE   A CZ   1 
ATOM   2910 H  H    A PHE   A 1 132 ? 17.767 0.689   -5.054  0.50 13.29 ?  132  PHE   A H    1 
ATOM   2911 H  H    B PHE   A 1 132 ? 17.649 0.660   -5.137  0.50 13.95 ?  132  PHE   A H    1 
ATOM   2912 H  HA   A PHE   A 1 132 ? 19.390 0.696   -7.154  0.50 13.10 ?  132  PHE   A HA   1 
ATOM   2913 H  HA   B PHE   A 1 132 ? 19.461 0.852   -7.073  0.50 14.32 ?  132  PHE   A HA   1 
ATOM   2914 H  HB2  A PHE   A 1 132 ? 18.975 -1.204  -5.143  0.50 13.45 ?  132  PHE   A HB2  1 
ATOM   2915 H  HB2  B PHE   A 1 132 ? 19.045 -1.089  -5.113  0.50 13.53 ?  132  PHE   A HB2  1 
ATOM   2916 H  HB3  A PHE   A 1 132 ? 19.855 -1.579  -6.410  0.50 13.45 ?  132  PHE   A HB3  1 
ATOM   2917 H  HB3  B PHE   A 1 132 ? 19.944 -1.464  -6.365  0.50 13.53 ?  132  PHE   A HB3  1 
ATOM   2918 H  HD1  A PHE   A 1 132 ? 19.813 1.111   -4.038  0.50 14.19 ?  132  PHE   A HD1  1 
ATOM   2919 H  HD1  B PHE   A 1 132 ? 19.815 1.128   -3.913  0.50 14.25 ?  132  PHE   A HD1  1 
ATOM   2920 H  HD2  A PHE   A 1 132 ? 22.132 -1.478  -6.022  0.50 14.13 ?  132  PHE   A HD2  1 
ATOM   2921 H  HD2  B PHE   A 1 132 ? 22.242 -1.189  -6.094  0.50 13.92 ?  132  PHE   A HD2  1 
ATOM   2922 H  HE1  A PHE   A 1 132 ? 21.681 1.972   -2.979  0.50 14.19 ?  132  PHE   A HE1  1 
ATOM   2923 H  HE1  B PHE   A 1 132 ? 21.648 2.052   -2.852  0.50 14.53 ?  132  PHE   A HE1  1 
ATOM   2924 H  HE2  A PHE   A 1 132 ? 23.995 -0.620  -4.966  0.50 14.19 ?  132  PHE   A HE2  1 
ATOM   2925 H  HE2  B PHE   A 1 132 ? 24.076 -0.264  -5.031  0.50 14.65 ?  132  PHE   A HE2  1 
ATOM   2926 H  HZ   A PHE   A 1 132 ? 23.772 1.109   -3.442  0.50 13.81 ?  132  PHE   A HZ   1 
ATOM   2927 H  HZ   B PHE   A 1 132 ? 23.780 1.358   -3.410  0.50 14.49 ?  132  PHE   A HZ   1 
ATOM   2928 N  N    A GLY   A 1 133 ? 16.588 -0.530  -7.656  0.50 10.78 ?  133  GLY   A N    1 
ATOM   2929 N  N    B GLY   A 1 133 ? 16.817 -0.563  -7.887  0.50 12.57 ?  133  GLY   A N    1 
ATOM   2930 C  CA   A GLY   A 1 133 ? 15.732 -0.903  -8.769  0.50 11.47 ?  133  GLY   A CA   1 
ATOM   2931 C  CA   B GLY   A 1 133 ? 16.111 -0.957  -9.091  0.50 12.53 ?  133  GLY   A CA   1 
ATOM   2932 C  C    A GLY   A 1 133 ? 15.533 -2.381  -9.035  0.50 12.46 ?  133  GLY   A C    1 
ATOM   2933 C  C    B GLY   A 1 133 ? 15.528 -2.360  -9.107  0.50 12.64 ?  133  GLY   A C    1 
ATOM   2934 O  O    A GLY   A 1 133 ? 15.045 -2.725  -10.120 0.50 13.16 ?  133  GLY   A O    1 
ATOM   2935 O  O    B GLY   A 1 133 ? 14.605 -2.610  -9.893  0.50 13.08 ?  133  GLY   A O    1 
ATOM   2936 H  H    A GLY   A 1 133 ? 16.157 -0.270  -6.957  0.50 12.94 ?  133  GLY   A H    1 
ATOM   2937 H  H    B GLY   A 1 133 ? 16.299 -0.372  -7.227  0.50 15.08 ?  133  GLY   A H    1 
ATOM   2938 H  HA2  A GLY   A 1 133 ? 14.856 -0.516  -8.623  0.50 13.77 ?  133  GLY   A HA2  1 
ATOM   2939 H  HA2  B GLY   A 1 133 ? 15.378 -0.345  -9.235  0.50 15.03 ?  133  GLY   A HA2  1 
ATOM   2940 H  HA3  A GLY   A 1 133 ? 16.096 -0.516  -9.577  0.50 13.77 ?  133  GLY   A HA3  1 
ATOM   2941 H  HA3  B GLY   A 1 133 ? 16.717 -0.879  -9.845  0.50 15.03 ?  133  GLY   A HA3  1 
ATOM   2942 N  N    A ALA   A 1 134 ? 15.884 -3.266  -8.105  0.50 12.24 ?  134  ALA   A N    1 
ATOM   2943 N  N    B ALA   A 1 134 ? 16.036 -3.284  -8.292  0.50 11.85 ?  134  ALA   A N    1 
ATOM   2944 C  CA   A ALA   A 1 134 ? 15.604 -4.682  -8.297  0.50 12.94 ?  134  ALA   A CA   1 
ATOM   2945 C  CA   B ALA   A 1 134 ? 15.581 -4.663  -8.398  0.50 12.22 ?  134  ALA   A CA   1 
ATOM   2946 C  C    A ALA   A 1 134 ? 14.244 -5.045  -7.707  0.50 13.07 ?  134  ALA   A C    1 
ATOM   2947 C  C    B ALA   A 1 134 ? 14.274 -4.879  -7.629  0.50 11.85 ?  134  ALA   A C    1 
ATOM   2948 O  O    A ALA   A 1 134 ? 13.653 -4.292  -6.929  0.50 13.84 ?  134  ALA   A O    1 
ATOM   2949 O  O    B ALA   A 1 134 ? 13.857 -4.067  -6.798  0.50 12.45 ?  134  ALA   A O    1 
ATOM   2950 C  CB   A ALA   A 1 134 ? 16.694 -5.555  -7.672  0.50 13.57 ?  134  ALA   A CB   1 
ATOM   2951 C  CB   B ALA   A 1 134 ? 16.655 -5.632  -7.910  0.50 12.86 ?  134  ALA   A CB   1 
ATOM   2952 H  H    A ALA   A 1 134 ? 16.289 -3.073  -7.364  0.50 14.68 ?  134  ALA   A H    1 
ATOM   2953 H  H    B ALA   A 1 134 ? 16.639 -3.141  -7.689  0.50 14.22 ?  134  ALA   A H    1 
ATOM   2954 H  HA   A ALA   A 1 134 ? 15.581 -4.870  -9.248  0.50 15.53 ?  134  ALA   A HA   1 
ATOM   2955 H  HA   B ALA   A 1 134 ? 15.414 -4.857  -9.335  0.50 14.66 ?  134  ALA   A HA   1 
ATOM   2956 H  HB1  A ALA   A 1 134 ? 16.486 -6.486  -7.848  0.50 16.29 ?  134  ALA   A HB1  1 
ATOM   2957 H  HB1  B ALA   A 1 134 ? 16.321 -6.538  -7.999  0.50 15.43 ?  134  ALA   A HB1  1 
ATOM   2958 H  HB2  A ALA   A 1 134 ? 17.549 -5.327  -8.071  0.50 16.29 ?  134  ALA   A HB2  1 
ATOM   2959 H  HB2  B ALA   A 1 134 ? 17.452 -5.517  -8.452  0.50 15.43 ?  134  ALA   A HB2  1 
ATOM   2960 H  HB3  A ALA   A 1 134 ? 16.719 -5.395  -6.718  0.50 16.29 ?  134  ALA   A HB3  1 
ATOM   2961 H  HB3  B ALA   A 1 134 ? 16.854 -5.440  -6.982  0.50 15.43 ?  134  ALA   A HB3  1 
ATOM   2962 N  N    A ASP   A 1 135 ? 13.751 -6.215  -8.097  0.50 13.28 ?  135  ASP   A N    1 
ATOM   2963 N  N    B ASP   A 1 135 ? 13.638 -6.012  -7.916  0.50 12.40 ?  135  ASP   A N    1 
ATOM   2964 C  CA   A ASP   A 1 135 ? 12.503 -6.743  -7.550  0.50 13.99 ?  135  ASP   A CA   1 
ATOM   2965 C  CA   B ASP   A 1 135 ? 12.374 -6.385  -7.289  0.50 13.26 ?  135  ASP   A CA   1 
ATOM   2966 C  C    A ASP   A 1 135 ? 12.740 -7.183  -6.111  0.50 13.39 ?  135  ASP   A C    1 
ATOM   2967 C  C    B ASP   A 1 135 ? 12.625 -6.829  -5.853  0.50 12.81 ?  135  ASP   A C    1 
ATOM   2968 O  O    A ASP   A 1 135 ? 13.537 -8.100  -5.880  0.50 13.23 ?  135  ASP   A O    1 
ATOM   2969 O  O    B ASP   A 1 135 ? 13.384 -7.783  -5.635  0.50 12.86 ?  135  ASP   A O    1 
ATOM   2970 C  CB   A ASP   A 1 135 ? 12.057 -7.940  -8.385  0.50 15.66 ?  135  ASP   A CB   1 
ATOM   2971 C  CB   B ASP   A 1 135 ? 11.754 -7.528  -8.087  0.50 14.86 ?  135  ASP   A CB   1 
ATOM   2972 C  CG   A ASP   A 1 135 ? 10.822 -8.635  -7.829  0.50 17.22 ?  135  ASP   A CG   1 
ATOM   2973 C  CG   B ASP   A 1 135 ? 10.369 -7.918  -7.588  0.50 16.83 ?  135  ASP   A CG   1 
ATOM   2974 O  OD1  A ASP   A 1 135 ? 10.218 -8.146  -6.853  0.50 17.11 ?  135  ASP   A OD1  1 
ATOM   2975 O  OD1  B ASP   A 1 135 ? 9.965  -7.468  -6.492  0.50 17.22 ?  135  ASP   A OD1  1 
ATOM   2976 O  OD2  A ASP   A 1 135 ? 10.461 -9.693  -8.380  0.50 19.14 -1 135  ASP   A OD2  1 
ATOM   2977 O  OD2  B ASP   A 1 135 ? 9.681  -8.682  -8.298  0.50 18.47 -1 135  ASP   A OD2  1 
ATOM   2978 H  H    A ASP   A 1 135 ? 14.121 -6.723  -8.684  0.50 15.93 ?  135  ASP   A H    1 
ATOM   2979 H  H    B ASP   A 1 135 ? 13.917 -6.590  -8.480  0.50 14.88 ?  135  ASP   A H    1 
ATOM   2980 H  HA   A ASP   A 1 135 ? 11.818 -6.058  -7.583  0.50 16.78 ?  135  ASP   A HA   1 
ATOM   2981 H  HA   B ASP   A 1 135 ? 11.759 -5.633  -7.308  0.50 15.91 ?  135  ASP   A HA   1 
ATOM   2982 H  HB2  A ASP   A 1 135 ? 11.856 -7.640  -9.282  0.50 18.79 ?  135  ASP   A HB2  1 
ATOM   2983 H  HB2  B ASP   A 1 135 ? 11.696 -7.261  -9.021  0.50 17.83 ?  135  ASP   A HB2  1 
ATOM   2984 H  HB3  A ASP   A 1 135 ? 12.767 -8.596  -8.398  0.50 18.79 ?  135  ASP   A HB3  1 
ATOM   2985 H  HB3  B ASP   A 1 135 ? 12.318 -8.312  -8.005  0.50 17.83 ?  135  ASP   A HB3  1 
ATOM   2986 N  N    A PRO   A 1 136 ? 12.084 -6.571  -5.122  0.50 13.05 ?  136  PRO   A N    1 
ATOM   2987 N  N    B PRO   A 1 136 ? 12.028 -6.176  -4.852  0.50 12.47 ?  136  PRO   A N    1 
ATOM   2988 C  CA   A PRO   A 1 136 ? 12.341 -6.970  -3.729  0.50 13.03 ?  136  PRO   A CA   1 
ATOM   2989 C  CA   B PRO   A 1 136 ? 12.267 -6.586  -3.457  0.50 12.55 ?  136  PRO   A CA   1 
ATOM   2990 C  C    A PRO   A 1 136 ? 11.909 -8.391  -3.414  0.50 12.13 ?  136  PRO   A C    1 
ATOM   2991 C  C    B PRO   A 1 136 ? 11.855 -8.022  -3.151  0.50 12.11 ?  136  PRO   A C    1 
ATOM   2992 O  O    A PRO   A 1 136 ? 12.495 -9.015  -2.521  0.50 12.14 ?  136  PRO   A O    1 
ATOM   2993 O  O    B PRO   A 1 136 ? 12.477 -8.667  -2.297  0.50 11.66 ?  136  PRO   A O    1 
ATOM   2994 C  CB   A PRO   A 1 136 ? 11.552 -5.936  -2.915  0.50 14.00 ?  136  PRO   A CB   1 
ATOM   2995 C  CB   B PRO   A 1 136 ? 11.459 -5.556  -2.648  0.50 13.24 ?  136  PRO   A CB   1 
ATOM   2996 C  CG   A PRO   A 1 136 ? 10.484 -5.458  -3.845  0.50 14.58 ?  136  PRO   A CG   1 
ATOM   2997 C  CG   B PRO   A 1 136 ? 10.468 -4.980  -3.628  0.50 13.63 ?  136  PRO   A CG   1 
ATOM   2998 C  CD   A PRO   A 1 136 ? 11.084 -5.493  -5.216  0.50 13.87 ?  136  PRO   A CD   1 
ATOM   2999 C  CD   B PRO   A 1 136 ? 11.179 -4.977  -4.934  0.50 13.19 ?  136  PRO   A CD   1 
ATOM   3000 H  HA   A PRO   A 1 136 ? 13.287 -6.881  -3.523  0.50 15.64 ?  136  PRO   A HA   1 
ATOM   3001 H  HA   B PRO   A 1 136 ? 13.206 -6.472  -3.235  0.50 15.06 ?  136  PRO   A HA   1 
ATOM   3002 H  HB2  A PRO   A 1 136 ? 11.165 -6.364  -2.134  0.50 16.80 ?  136  PRO   A HB2  1 
ATOM   3003 H  HB2  B PRO   A 1 136 ? 10.999 -5.992  -1.916  0.50 15.89 ?  136  PRO   A HB2  1 
ATOM   3004 H  HB3  A PRO   A 1 136 ? 12.139 -5.211  -2.656  0.50 16.80 ?  136  PRO   A HB3  1 
ATOM   3005 H  HB3  B PRO   A 1 136 ? 12.048 -4.856  -2.314  0.50 15.89 ?  136  PRO   A HB3  1 
ATOM   3006 H  HG2  A PRO   A 1 136 ? 9.720  -6.052  -3.794  0.50 17.50 ?  136  PRO   A HG2  1 
ATOM   3007 H  HG2  B PRO   A 1 136 ? 9.686  -5.551  -3.675  0.50 16.35 ?  136  PRO   A HG2  1 
ATOM   3008 H  HG3  A PRO   A 1 136 ? 10.233 -4.553  -3.609  0.50 17.50 ?  136  PRO   A HG3  1 
ATOM   3009 H  HG3  B PRO   A 1 136 ? 10.225 -4.080  -3.367  0.50 16.35 ?  136  PRO   A HG3  1 
ATOM   3010 H  HD2  A PRO   A 1 136 ? 10.411 -5.723  -5.877  0.50 16.65 ?  136  PRO   A HD2  1 
ATOM   3011 H  HD2  B PRO   A 1 136 ? 10.539 -5.057  -5.661  0.50 15.83 ?  136  PRO   A HD2  1 
ATOM   3012 H  HD3  A PRO   A 1 136 ? 11.513 -4.648  -5.427  0.50 16.65 ?  136  PRO   A HD3  1 
ATOM   3013 H  HD3  B PRO   A 1 136 ? 11.724 -4.177  -5.028  0.50 15.83 ?  136  PRO   A HD3  1 
ATOM   3014 N  N    A ILE   A 1 137 ? 10.897 -8.921  -4.105  0.50 12.08 ?  137  ILE   A N    1 
ATOM   3015 N  N    B ILE   A 1 137 ? 10.817 -8.540  -3.811  0.50 12.29 ?  137  ILE   A N    1 
ATOM   3016 C  CA   A ILE   A 1 137 ? 10.524 -10.318 -3.896  0.50 12.38 ?  137  ILE   A CA   1 
ATOM   3017 C  CA   B ILE   A 1 137 ? 10.436 -9.938  -3.614  0.50 12.60 ?  137  ILE   A CA   1 
ATOM   3018 C  C    A ILE   A 1 137 ? 11.668 -11.241 -4.302  0.50 11.86 ?  137  ILE   A C    1 
ATOM   3019 C  C    B ILE   A 1 137 ? 11.596 -10.850 -3.988  0.50 11.93 ?  137  ILE   A C    1 
ATOM   3020 O  O    A ILE   A 1 137 ? 11.992 -12.204 -3.595  0.50 11.96 ?  137  ILE   A O    1 
ATOM   3021 O  O    B ILE   A 1 137 ? 11.888 -11.837 -3.300  0.50 12.12 ?  137  ILE   A O    1 
ATOM   3022 C  CB   A ILE   A 1 137 ? 9.209  -10.649 -4.627  0.50 14.07 ?  137  ILE   A CB   1 
ATOM   3023 C  CB   B ILE   A 1 137 ? 9.182  -10.271 -4.446  0.50 14.18 ?  137  ILE   A CB   1 
ATOM   3024 C  CG1  A ILE   A 1 137 ? 8.046  -9.860  -4.008  0.50 15.75 ?  137  ILE   A CG1  1 
ATOM   3025 C  CG1  B ILE   A 1 137 ? 8.021  -9.319  -4.138  0.50 16.11 ?  137  ILE   A CG1  1 
ATOM   3026 C  CG2  A ILE   A 1 137 ? 8.931  -12.148 -4.569  0.50 14.22 ?  137  ILE   A CG2  1 
ATOM   3027 C  CG2  B ILE   A 1 137 ? 8.777  -11.727 -4.230  0.50 14.59 ?  137  ILE   A CG2  1 
ATOM   3028 C  CD1  A ILE   A 1 137 ? 6.734  -9.981  -4.755  0.50 16.84 ?  137  ILE   A CD1  1 
ATOM   3029 C  CD1  B ILE   A 1 137 ? 6.827  -9.538  -5.049  0.50 17.53 ?  137  ILE   A CD1  1 
ATOM   3030 H  H    A ILE   A 1 137 ? 10.425 -8.504  -4.688  0.50 14.50 ?  137  ILE   A H    1 
ATOM   3031 H  H    B ILE   A 1 137 ? 10.333 -8.102  -4.370  0.50 14.74 ?  137  ILE   A H    1 
ATOM   3032 H  HA   A ILE   A 1 137 ? 10.376 -10.458 -2.954  0.50 14.86 ?  137  ILE   A HA   1 
ATOM   3033 H  HA   B ILE   A 1 137 ? 10.227 -10.073 -2.674  0.50 15.12 ?  137  ILE   A HA   1 
ATOM   3034 H  HB   A ILE   A 1 137 ? 9.296  -10.389 -5.556  0.50 16.88 ?  137  ILE   A HB   1 
ATOM   3035 H  HB   B ILE   A 1 137 ? 9.414  -10.157 -5.377  0.50 17.02 ?  137  ILE   A HB   1 
ATOM   3036 H  HG12 A ILE   A 1 137 ? 7.904  -10.178 -3.103  0.50 18.90 ?  137  ILE   A HG12 1 
ATOM   3037 H  HG12 B ILE   A 1 137 ? 7.732  -9.453  -3.223  0.50 19.33 ?  137  ILE   A HG12 1 
ATOM   3038 H  HG13 A ILE   A 1 137 ? 8.291  -8.919  -3.986  0.50 18.90 ?  137  ILE   A HG13 1 
ATOM   3039 H  HG13 B ILE   A 1 137 ? 8.315  -8.399  -4.259  0.50 19.33 ?  137  ILE   A HG13 1 
ATOM   3040 H  HG21 A ILE   A 1 137 ? 8.060  -12.329 -4.953  0.50 17.06 ?  137  ILE   A HG21 1 
ATOM   3041 H  HG21 B ILE   A 1 137 ? 7.963  -11.915 -4.720  0.50 17.51 ?  137  ILE   A HG21 1 
ATOM   3042 H  HG22 A ILE   A 1 137 ? 9.607  -12.618 -5.076  0.50 17.06 ?  137  ILE   A HG22 1 
ATOM   3043 H  HG22 B ILE   A 1 137 ? 9.487  -12.299 -4.552  0.50 17.51 ?  137  ILE   A HG22 1 
ATOM   3044 H  HG23 A ILE   A 1 137 ? 8.947  -12.433 -3.643  0.50 17.06 ?  137  ILE   A HG23 1 
ATOM   3045 H  HG23 B ILE   A 1 137 ? 8.634  -11.873 -3.285  0.50 17.51 ?  137  ILE   A HG23 1 
ATOM   3046 H  HD11 A ILE   A 1 137 ? 6.050  -9.555  -4.222  0.50 20.21 ?  137  ILE   A HD11 1 
ATOM   3047 H  HD11 B ILE   A 1 137 ? 6.043  -9.716  -4.506  0.50 21.03 ?  137  ILE   A HD11 1 
ATOM   3048 H  HD12 A ILE   A 1 137 ? 6.817  -9.533  -5.614  0.50 20.21 ?  137  ILE   A HD12 1 
ATOM   3049 H  HD12 B ILE   A 1 137 ? 6.691  -8.748  -5.587  0.50 21.03 ?  137  ILE   A HD12 1 
ATOM   3050 H  HD13 A ILE   A 1 137 ? 6.514  -10.913 -4.885  0.50 20.21 ?  137  ILE   A HD13 1 
ATOM   3051 H  HD13 B ILE   A 1 137 ? 7.000  -10.295 -5.634  0.50 21.03 ?  137  ILE   A HD13 1 
ATOM   3052 N  N    A HIS   A 1 138 ? 12.297 -10.963 -5.447  0.50 11.70 ?  138  HIS   A N    1 
ATOM   3053 N  N    B HIS   A 1 138 ? 12.257 -10.541 -5.103  0.50 11.66 ?  138  HIS   A N    1 
ATOM   3054 C  CA   A HIS   A 1 138 ? 13.453 -11.750 -5.863  0.50 11.94 ?  138  HIS   A CA   1 
ATOM   3055 C  CA   B HIS   A 1 138 ? 13.417 -11.312 -5.533  0.50 11.23 ?  138  HIS   A CA   1 
ATOM   3056 C  C    A HIS   A 1 138 ? 14.596 -11.609 -4.868  0.50 11.32 ?  138  HIS   A C    1 
ATOM   3057 C  C    B HIS   A 1 138 ? 14.573 -11.170 -4.550  0.50 10.38 ?  138  HIS   A C    1 
ATOM   3058 O  O    A HIS   A 1 138 ? 15.255 -12.598 -4.522  0.50 11.85 ?  138  HIS   A O    1 
ATOM   3059 O  O    B HIS   A 1 138 ? 15.251 -12.155 -4.232  0.50 10.82 ?  138  HIS   A O    1 
ATOM   3060 C  CB   A HIS   A 1 138 ? 13.900 -11.328 -7.261  0.50 12.83 ?  138  HIS   A CB   1 
ATOM   3061 C  CB   B HIS   A 1 138 ? 13.826 -10.870 -6.939  0.50 11.85 ?  138  HIS   A CB   1 
ATOM   3062 C  CG   A HIS   A 1 138 ? 15.177 -11.971 -7.702  0.50 13.51 ?  138  HIS   A CG   1 
ATOM   3063 C  CG   B HIS   A 1 138 ? 15.074 -11.525 -7.438  0.50 12.82 ?  138  HIS   A CG   1 
ATOM   3064 N  ND1  A HIS   A 1 138 ? 15.289 -13.326 -7.936  0.50 14.48 ?  138  HIS   A ND1  1 
ATOM   3065 N  ND1  B HIS   A 1 138 ? 15.149 -12.872 -7.716  0.50 14.14 ?  138  HIS   A ND1  1 
ATOM   3066 C  CD2  A HIS   A 1 138 ? 16.402 -11.447 -7.943  0.50 13.79 ?  138  HIS   A CD2  1 
ATOM   3067 C  CD2  B HIS   A 1 138 ? 16.301 -11.016 -7.702  0.50 13.18 ?  138  HIS   A CD2  1 
ATOM   3068 C  CE1  A HIS   A 1 138 ? 16.525 -13.606 -8.307  0.50 14.79 ?  138  HIS   A CE1  1 
ATOM   3069 C  CE1  B HIS   A 1 138 ? 16.368 -13.164 -8.134  0.50 14.27 ?  138  HIS   A CE1  1 
ATOM   3070 N  NE2  A HIS   A 1 138 ? 17.221 -12.484 -8.318  0.50 14.21 ?  138  HIS   A NE2  1 
ATOM   3071 N  NE2  B HIS   A 1 138 ? 17.087 -12.056 -8.134  0.50 13.94 ?  138  HIS   A NE2  1 
ATOM   3072 H  H    A HIS   A 1 138 ? 12.087 -10.327 -5.990  0.50 14.04 ?  138  HIS   A H    1 
ATOM   3073 H  H    B HIS   A 1 138 ? 12.050 -9.884  -5.623  0.50 13.99 ?  138  HIS   A H    1 
ATOM   3074 H  HA   A HIS   A 1 138 ? 13.206 -12.684 -5.902  0.50 14.33 ?  138  HIS   A HA   1 
ATOM   3075 H  HA   B HIS   A 1 138 ? 13.167 -12.243 -5.575  0.50 13.47 ?  138  HIS   A HA   1 
ATOM   3076 H  HB2  A HIS   A 1 138 ? 13.209 -11.574 -7.899  0.50 15.40 ?  138  HIS   A HB2  1 
ATOM   3077 H  HB2  B HIS   A 1 138 ? 13.109 -11.088 -7.557  0.50 14.22 ?  138  HIS   A HB2  1 
ATOM   3078 H  HB3  A HIS   A 1 138 ? 14.031 -10.367 -7.275  0.50 15.40 ?  138  HIS   A HB3  1 
ATOM   3079 H  HB3  B HIS   A 1 138 ? 13.973 -9.910  -6.938  0.50 14.22 ?  138  HIS   A HB3  1 
ATOM   3080 H  HD1  A HIS   A 1 138 ? 14.650 -13.897 -7.858  0.50 17.38 ?  138  HIS   A HD1  1 
ATOM   3081 H  HD1  B HIS   A 1 138 ? 14.501 -13.433 -7.631  0.50 16.97 ?  138  HIS   A HD1  1 
ATOM   3082 H  HD2  A HIS   A 1 138 ? 16.640 -10.550 -7.868  0.50 16.54 ?  138  HIS   A HD2  1 
ATOM   3083 H  HD2  B HIS   A 1 138 ? 16.561 -10.128 -7.609  0.50 15.81 ?  138  HIS   A HD2  1 
ATOM   3084 H  HE1  A HIS   A 1 138 ? 16.849 -14.448 -8.523  0.50 17.75 ?  138  HIS   A HE1  1 
ATOM   3085 H  HE1  B HIS   A 1 138 ? 16.666 -14.009 -8.383  0.50 17.12 ?  138  HIS   A HE1  1 
ATOM   3086 N  N    A SER   A 1 139 ? 14.851 -10.385 -4.402  0.50 10.65 ?  139  SER   A N    1 
ATOM   3087 N  N    B SER   A 1 139 ? 14.810 -9.953  -4.054  0.50 9.86  ?  139  SER   A N    1 
ATOM   3088 C  CA   A SER   A 1 139 ? 15.930 -10.179 -3.445  0.50 10.13 ?  139  SER   A CA   1 
ATOM   3089 C  CA   B SER   A 1 139 ? 15.882 -9.747  -3.087  0.50 9.61  ?  139  SER   A CA   1 
ATOM   3090 C  C    A SER   A 1 139 ? 15.713 -11.004 -2.182  0.50 9.96  ?  139  SER   A C    1 
ATOM   3091 C  C    B SER   A 1 139 ? 15.676 -10.604 -1.845  0.50 9.32  ?  139  SER   A C    1 
ATOM   3092 O  O    A SER   A 1 139 ? 16.661 -11.585 -1.643  0.50 9.80  ?  139  SER   A O    1 
ATOM   3093 O  O    B SER   A 1 139 ? 16.626 -11.206 -1.331  0.50 9.63  ?  139  SER   A O    1 
ATOM   3094 C  CB   A SER   A 1 139 ? 16.074 -8.693  -3.112  0.50 9.74  ?  139  SER   A CB   1 
ATOM   3095 C  CB   B SER   A 1 139 ? 15.977 -8.263  -2.719  0.50 9.92  ?  139  SER   A CB   1 
ATOM   3096 O  OG   A SER   A 1 139 ? 17.149 -8.498  -2.206  0.50 9.23  ?  139  SER   A OG   1 
ATOM   3097 O  OG   B SER   A 1 139 ? 17.023 -8.050  -1.785  0.50 10.34 ?  139  SER   A OG   1 
ATOM   3098 H  H    A SER   A 1 139 ? 14.425 -9.673  -4.626  0.50 12.78 ?  139  SER   A H    1 
ATOM   3099 H  H    B SER   A 1 139 ? 14.373 -9.241  -4.260  0.50 11.83 ?  139  SER   A H    1 
ATOM   3100 H  HA   A SER   A 1 139 ? 16.765 -10.466 -3.847  0.50 12.15 ?  139  SER   A HA   1 
ATOM   3101 H  HA   B SER   A 1 139 ? 16.725 -10.005 -3.489  0.50 11.53 ?  139  SER   A HA   1 
ATOM   3102 H  HB2  A SER   A 1 139 ? 16.249 -8.194  -3.932  0.50 11.68 ?  139  SER   A HB2  1 
ATOM   3103 H  HB2  B SER   A 1 139 ? 16.161 -7.747  -3.524  0.50 11.91 ?  139  SER   A HB2  1 
ATOM   3104 H  HB3  A SER   A 1 139 ? 15.256 -8.374  -2.702  0.50 11.68 ?  139  SER   A HB3  1 
ATOM   3105 H  HB3  B SER   A 1 139 ? 15.136 -7.976  -2.330  0.50 11.91 ?  139  SER   A HB3  1 
ATOM   3106 H  HG   A SER   A 1 139 ? 17.232 -7.679  -2.033  0.50 11.07 ?  139  SER   A HG   1 
ATOM   3107 H  HG   B SER   A 1 139 ? 17.066 -7.227  -1.589  0.50 12.41 ?  139  SER   A HG   1 
ATOM   3108 N  N    A LEU   A 1 140 ? 14.470 -11.080 -1.702  0.50 10.29 ?  140  LEU   A N    1 
ATOM   3109 N  N    B LEU   A 1 140 ? 14.443 -10.661 -1.338  0.50 9.05  ?  140  LEU   A N    1 
ATOM   3110 C  CA   A LEU   A 1 140 ? 14.200 -11.892 -0.521  0.50 9.97  ?  140  LEU   A CA   1 
ATOM   3111 C  CA   B LEU   A 1 140 ? 14.175 -11.487 -0.164  0.50 8.78  ?  140  LEU   A CA   1 
ATOM   3112 C  C    A LEU   A 1 140 ? 14.470 -13.365 -0.804  0.50 9.82  ?  140  LEU   A C    1 
ATOM   3113 C  C    B LEU   A 1 140 ? 14.437 -12.963 -0.453  0.50 9.11  ?  140  LEU   A C    1 
ATOM   3114 O  O    A LEU   A 1 140 ? 15.035 -14.074 0.037   0.50 10.01 ?  140  LEU   A O    1 
ATOM   3115 O  O    B LEU   A 1 140 ? 14.993 -13.681 0.390   0.50 9.71  ?  140  LEU   A O    1 
ATOM   3116 C  CB   A LEU   A 1 140 ? 12.759 -11.684 -0.052  0.50 10.30 ?  140  LEU   A CB   1 
ATOM   3117 C  CB   B LEU   A 1 140 ? 12.739 -11.259 0.314   0.50 8.88  ?  140  LEU   A CB   1 
ATOM   3118 C  CG   A LEU   A 1 140 ? 12.335 -12.555 1.134   0.50 10.66 ?  140  LEU   A CG   1 
ATOM   3119 C  CG   B LEU   A 1 140 ? 12.260 -12.127 1.475   0.50 9.41  ?  140  LEU   A CG   1 
ATOM   3120 C  CD1  A LEU   A 1 140 ? 13.237 -12.344 2.339   0.50 11.15 ?  140  LEU   A CD1  1 
ATOM   3121 C  CD1  B LEU   A 1 140 ? 13.143 -11.951 2.700   0.50 9.53  ?  140  LEU   A CD1  1 
ATOM   3122 C  CD2  A LEU   A 1 140 ? 10.877 -12.287 1.507   0.50 11.23 ?  140  LEU   A CD2  1 
ATOM   3123 C  CD2  B LEU   A 1 140 ? 10.816 -11.806 1.808   0.50 10.12 ?  140  LEU   A CD2  1 
ATOM   3124 H  H    A LEU   A 1 140 ? 13.786 -10.680 -2.037  0.50 12.35 ?  140  LEU   A H    1 
ATOM   3125 H  H    B LEU   A 1 140 ? 13.760 -10.235 -1.650  0.50 10.86 ?  140  LEU   A H    1 
ATOM   3126 H  HA   A LEU   A 1 140 ? 14.792 -11.610 0.190   0.50 11.97 ?  140  LEU   A HA   1 
ATOM   3127 H  HA   B LEU   A 1 140 ? 14.768 -11.206 0.551   0.50 10.54 ?  140  LEU   A HA   1 
ATOM   3128 H  HB2  A LEU   A 1 140 ? 12.651 -10.758 0.214   0.50 12.36 ?  140  LEU   A HB2  1 
ATOM   3129 H  HB2  B LEU   A 1 140 ? 12.654 -10.331 0.598   0.50 10.66 ?  140  LEU   A HB2  1 
ATOM   3130 H  HB3  A LEU   A 1 140 ? 12.161 -11.884 -0.788  0.50 12.36 ?  140  LEU   A HB3  1 
ATOM   3131 H  HB3  B LEU   A 1 140 ? 12.142 -11.419 -0.429  0.50 10.66 ?  140  LEU   A HB3  1 
ATOM   3132 H  HG   A LEU   A 1 140 ? 12.400 -13.488 0.879   0.50 12.79 ?  140  LEU   A HG   1 
ATOM   3133 H  HG   B LEU   A 1 140 ? 12.300 -13.056 1.210   0.50 11.29 ?  140  LEU   A HG   1 
ATOM   3134 H  HD11 A LEU   A 1 140 ? 12.869 -12.829 3.095   0.50 13.38 ?  140  LEU   A HD11 1 
ATOM   3135 H  HD11 B LEU   A 1 140 ? 12.762 -12.460 3.434   0.50 11.43 ?  140  LEU   A HD11 1 
ATOM   3136 H  HD12 A LEU   A 1 140 ? 14.123 -12.678 2.133   0.50 13.38 ?  140  LEU   A HD12 1 
ATOM   3137 H  HD12 B LEU   A 1 140 ? 14.031 -12.278 2.495   0.50 11.43 ?  140  LEU   A HD12 1 
ATOM   3138 H  HD13 A LEU   A 1 140 ? 13.276 -11.397 2.541   0.50 13.38 ?  140  LEU   A HD13 1 
ATOM   3139 H  HD13 B LEU   A 1 140 ? 13.176 -11.011 2.932   0.50 11.43 ?  140  LEU   A HD13 1 
ATOM   3140 H  HD21 A LEU   A 1 140 ? 10.631 -12.852 2.260   0.50 13.47 ?  140  LEU   A HD21 1 
ATOM   3141 H  HD21 B LEU   A 1 140 ? 10.526 -12.377 2.538   0.50 12.14 ?  140  LEU   A HD21 1 
ATOM   3142 H  HD22 A LEU   A 1 140 ? 10.776 -11.353 1.752   0.50 13.47 ?  140  LEU   A HD22 1 
ATOM   3143 H  HD22 B LEU   A 1 140 ? 10.748 -10.875 2.069   0.50 12.14 ?  140  LEU   A HD22 1 
ATOM   3144 H  HD23 A LEU   A 1 140 ? 10.310 -12.491 0.746   0.50 13.47 ?  140  LEU   A HD23 1 
ATOM   3145 H  HD23 B LEU   A 1 140 ? 10.267 -11.971 1.024   0.50 12.14 ?  140  LEU   A HD23 1 
ATOM   3146 N  N    A ARG   A 1 141 ? 14.072 -13.838 -1.987  0.50 10.33 ?  141  ARG   A N    1 
ATOM   3147 N  N    B ARG   A 1 141 ? 14.042 -13.440 -1.637  0.50 9.81  ?  141  ARG   A N    1 
ATOM   3148 C  CA   A ARG   A 1 141 ? 14.335 -15.219 -2.380  0.50 11.43 ?  141  ARG   A CA   1 
ATOM   3149 C  CA   B ARG   A 1 141 ? 14.266 -14.847 -1.955  0.50 10.47 ?  141  ARG   A CA   1 
ATOM   3150 C  C    A ARG   A 1 141 ? 15.829 -15.515 -2.359  0.50 10.82 ?  141  ARG   A C    1 
ATOM   3151 C  C    B ARG   A 1 141 ? 15.755 -15.160 -2.036  0.50 10.19 ?  141  ARG   A C    1 
ATOM   3152 O  O    A ARG   A 1 141 ? 16.270 -16.520 -1.790  0.50 11.45 ?  141  ARG   A O    1 
ATOM   3153 O  O    B ARG   A 1 141 ? 16.212 -16.180 -1.505  0.50 10.42 ?  141  ARG   A O    1 
ATOM   3154 C  CB   A ARG   A 1 141 ? 13.770 -15.445 -3.783  0.50 13.89 ?  141  ARG   A CB   1 
ATOM   3155 C  CB   B ARG   A 1 141 ? 13.545 -15.240 -3.244  0.50 11.33 ?  141  ARG   A CB   1 
ATOM   3156 C  CG   A ARG   A 1 141 ? 13.661 -16.892 -4.216  0.50 16.29 ?  141  ARG   A CG   1 
ATOM   3157 C  CG   B ARG   A 1 141 ? 13.716 -16.722 -3.615  0.50 13.18 ?  141  ARG   A CG   1 
ATOM   3158 C  CD   A ARG   A 1 141 ? 12.625 -17.600 -3.389  0.50 17.47 ?  141  ARG   A CD   1 
ATOM   3159 C  CD   B ARG   A 1 141 ? 13.136 -17.685 -2.565  0.50 14.46 ?  141  ARG   A CD   1 
ATOM   3160 N  NE   A ARG   A 1 141 ? 13.245 -18.389 -2.336  0.50 18.28 ?  141  ARG   A NE   1 
ATOM   3161 N  NE   B ARG   A 1 141 ? 11.702 -17.487 -2.399  0.50 15.26 ?  141  ARG   A NE   1 
ATOM   3162 C  CZ   A ARG   A 1 141 ? 12.579 -18.948 -1.336  0.50 18.83 ?  141  ARG   A CZ   1 
ATOM   3163 C  CZ   B ARG   A 1 141 ? 10.954 -18.093 -1.487  0.50 15.83 ?  141  ARG   A CZ   1 
ATOM   3164 N  NH1  A ARG   A 1 141 ? 11.282 -18.750 -1.174  0.50 19.44 ?  141  ARG   A NH1  1 
ATOM   3165 N  NH1  B ARG   A 1 141 ? 11.469 -18.964 -0.634  0.50 16.37 ?  141  ARG   A NH1  1 
ATOM   3166 N  NH2  A ARG   A 1 141 ? 13.232 -19.723 -0.476  0.50 18.94 ?  141  ARG   A NH2  1 
ATOM   3167 N  NH2  B ARG   A 1 141 ? 9.654  -17.815 -1.429  0.50 16.56 ?  141  ARG   A NH2  1 
ATOM   3168 H  H    A ARG   A 1 141 ? 13.650 -13.385 -2.579  0.50 12.39 ?  141  ARG   A H    1 
ATOM   3169 H  H    B ARG   A 1 141 ? 13.650 -12.972 -2.255  0.50 11.78 ?  141  ARG   A H    1 
ATOM   3170 H  HA   A ARG   A 1 141 ? 13.898 -15.829 -1.765  0.50 13.71 ?  141  ARG   A HA   1 
ATOM   3171 H  HA   B ARG   A 1 141 ? 13.897 -15.372 -1.238  0.50 12.56 ?  141  ARG   A HA   1 
ATOM   3172 H  HB2  A ARG   A 1 141 ? 12.882 -15.064 -3.822  0.50 16.67 ?  141  ARG   A HB2  1 
ATOM   3173 H  HB2  B ARG   A 1 141 ? 12.594 -15.064 -3.136  0.50 13.59 ?  141  ARG   A HB2  1 
ATOM   3174 H  HB3  A ARG   A 1 141 ? 14.345 -14.999 -4.422  0.50 16.67 ?  141  ARG   A HB3  1 
ATOM   3175 H  HB3  B ARG   A 1 141 ? 13.892 -14.702 -3.976  0.50 13.59 ?  141  ARG   A HB3  1 
ATOM   3176 H  HG2  A ARG   A 1 141 ? 13.395 -16.936 -5.150  0.50 19.55 ?  141  ARG   A HG2  1 
ATOM   3177 H  HG2  B ARG   A 1 141 ? 13.261 -16.887 -4.455  0.50 15.82 ?  141  ARG   A HG2  1 
ATOM   3178 H  HG3  A ARG   A 1 141 ? 14.516 -17.340 -4.090  0.50 19.55 ?  141  ARG   A HG3  1 
ATOM   3179 H  HG3  B ARG   A 1 141 ? 14.662 -16.917 -3.713  0.50 15.82 ?  141  ARG   A HG3  1 
ATOM   3180 H  HD2  A ARG   A 1 141 ? 12.045 -16.945 -2.972  0.50 20.96 ?  141  ARG   A HD2  1 
ATOM   3181 H  HD2  B ARG   A 1 141 ? 13.284 -18.598 -2.854  0.50 17.36 ?  141  ARG   A HD2  1 
ATOM   3182 H  HD3  A ARG   A 1 141 ? 12.107 -18.191 -3.960  0.50 20.96 ?  141  ARG   A HD3  1 
ATOM   3183 H  HD3  B ARG   A 1 141 ? 13.567 -17.530 -1.710  0.50 17.36 ?  141  ARG   A HD3  1 
ATOM   3184 H  HE   A ARG   A 1 141 ? 14.081 -18.574 -2.416  0.50 21.93 ?  141  ARG   A HE   1 
ATOM   3185 H  HE   B ARG   A 1 141 ? 11.311 -16.934 -2.931  0.50 18.31 ?  141  ARG   A HE   1 
ATOM   3186 H  HH11 A ARG   A 1 141 ? 10.846 -18.260 -1.729  0.50 23.33 ?  141  ARG   A HH11 1 
ATOM   3187 H  HH11 B ARG   A 1 141 ? 12.306 -19.155 -0.665  0.50 19.65 ?  141  ARG   A HH11 1 
ATOM   3188 H  HH12 A ARG   A 1 141 ? 10.871 -19.122 -0.515  0.50 23.33 ?  141  ARG   A HH12 1 
ATOM   3189 H  HH12 B ARG   A 1 141 ? 10.961 -19.349 -0.056  0.50 19.65 ?  141  ARG   A HH12 1 
ATOM   3190 H  HH21 A ARG   A 1 141 ? 14.078 -19.854 -0.574  0.50 22.72 ?  141  ARG   A HH21 1 
ATOM   3191 H  HH21 B ARG   A 1 141 ? 9.309  -17.250 -1.979  0.50 19.87 ?  141  ARG   A HH21 1 
ATOM   3192 H  HH22 A ARG   A 1 141 ? 12.815 -20.082 0.182   0.50 22.72 ?  141  ARG   A HH22 1 
ATOM   3193 H  HH22 B ARG   A 1 141 ? 9.156  -18.204 -0.845  0.50 19.87 ?  141  ARG   A HH22 1 
ATOM   3194 N  N    A VAL   A 1 142 ? 16.626 -14.652 -2.989  0.50 10.15 ?  142  VAL   A N    1 
ATOM   3195 N  N    B VAL   A 1 142 ? 16.536 -14.288 -2.683  0.50 10.03 ?  142  VAL   A N    1 
ATOM   3196 C  CA   A VAL   A 1 142 ? 18.071 -14.862 -3.010  0.50 10.23 ?  142  VAL   A CA   1 
ATOM   3197 C  CA   B VAL   A 1 142 ? 17.981 -14.499 -2.738  0.50 10.11 ?  142  VAL   A CA   1 
ATOM   3198 C  C    A VAL   A 1 142 ? 18.637 -14.823 -1.596  0.50 10.04 ?  142  VAL   A C    1 
ATOM   3199 C  C    B VAL   A 1 142 ? 18.570 -14.504 -1.335  0.50 9.69  ?  142  VAL   A C    1 
ATOM   3200 O  O    A VAL   A 1 142 ? 19.486 -15.644 -1.229  0.50 10.27 ?  142  VAL   A O    1 
ATOM   3201 O  O    B VAL   A 1 142 ? 19.453 -15.311 -1.019  0.50 10.14 ?  142  VAL   A O    1 
ATOM   3202 C  CB   A VAL   A 1 142 ? 18.755 -13.837 -3.932  0.50 9.99  ?  142  VAL   A CB   1 
ATOM   3203 C  CB   B VAL   A 1 142 ? 18.661 -13.460 -3.652  0.50 10.66 ?  142  VAL   A CB   1 
ATOM   3204 C  CG1  A VAL   A 1 142 ? 20.266 -14.020 -3.888  0.50 9.49  ?  142  VAL   A CG1  1 
ATOM   3205 C  CG1  B VAL   A 1 142 ? 20.173 -13.663 -3.649  0.50 11.07 ?  142  VAL   A CG1  1 
ATOM   3206 C  CG2  A VAL   A 1 142 ? 18.248 -13.974 -5.359  0.50 10.98 ?  142  VAL   A CG2  1 
ATOM   3207 C  CG2  B VAL   A 1 142 ? 18.138 -13.571 -5.072  0.50 11.26 ?  142  VAL   A CG2  1 
ATOM   3208 H  H    A VAL   A 1 142 ? 16.361 -13.952 -3.410  0.50 12.17 ?  142  VAL   A H    1 
ATOM   3209 H  H    B VAL   A 1 142 ? 16.261 -13.575 -3.095  0.50 12.04 ?  142  VAL   A H    1 
ATOM   3210 H  HA   A VAL   A 1 142 ? 18.253 -15.741 -3.379  0.50 12.28 ?  142  VAL   A HA   1 
ATOM   3211 H  HA   B VAL   A 1 142 ? 18.148 -15.365 -3.127  0.50 12.13 ?  142  VAL   A HA   1 
ATOM   3212 H  HB   A VAL   A 1 142 ? 18.554 -12.940 -3.625  0.50 11.99 ?  142  VAL   A HB   1 
ATOM   3213 H  HB   B VAL   A 1 142 ? 18.475 -12.560 -3.332  0.50 12.79 ?  142  VAL   A HB   1 
ATOM   3214 H  HG11 A VAL   A 1 142 ? 20.666 -13.539 -4.630  0.50 11.38 ?  142  VAL   A HG11 1 
ATOM   3215 H  HG11 B VAL   A 1 142 ? 20.574 -13.074 -4.311  0.50 13.28 ?  142  VAL   A HG11 1 
ATOM   3216 H  HG12 A VAL   A 1 142 ? 20.604 -13.667 -3.049  0.50 11.38 ?  142  VAL   A HG12 1 
ATOM   3217 H  HG12 B VAL   A 1 142 ? 20.524 -13.450 -2.770  0.50 13.28 ?  142  VAL   A HG12 1 
ATOM   3218 H  HG13 A VAL   A 1 142 ? 20.472 -14.965 -3.957  0.50 11.38 ?  142  VAL   A HG13 1 
ATOM   3219 H  HG13 B VAL   A 1 142 ? 20.366 -14.585 -3.869  0.50 13.28 ?  142  VAL   A HG13 1 
ATOM   3220 H  HG21 A VAL   A 1 142 ? 18.718 -13.339 -5.924  0.50 13.18 ?  142  VAL   A HG21 1 
ATOM   3221 H  HG21 B VAL   A 1 142 ? 18.596 -12.924 -5.633  0.50 13.51 ?  142  VAL   A HG21 1 
ATOM   3222 H  HG22 A VAL   A 1 142 ? 18.414 -14.877 -5.666  0.50 13.18 ?  142  VAL   A HG22 1 
ATOM   3223 H  HG22 B VAL   A 1 142 ? 18.311 -14.469 -5.399  0.50 13.51 ?  142  VAL   A HG22 1 
ATOM   3224 H  HG23 A VAL   A 1 142 ? 17.297 -13.786 -5.372  0.50 13.18 ?  142  VAL   A HG23 1 
ATOM   3225 H  HG23 B VAL   A 1 142 ? 17.186 -13.396 -5.073  0.50 13.51 ?  142  VAL   A HG23 1 
ATOM   3226 N  N    A CYS   A 1 143 ? 18.181 -13.871 -0.783  0.50 9.79  ?  143  CYS   A N    1 
ATOM   3227 N  N    B CYS   A 1 143 ? 18.097 -13.605 -0.469  0.50 9.64  ?  143  CYS   A N    1 
ATOM   3228 C  CA   A CYS   A 1 143 ? 18.642 -13.778 0.597   0.50 10.19 ?  143  CYS   A CA   1 
ATOM   3229 C  CA   B CYS   A 1 143 ? 18.569 -13.593 0.912   0.50 9.88  ?  143  CYS   A CA   1 
ATOM   3230 C  C    A CYS   A 1 143 ? 18.411 -15.090 1.334   0.50 10.19 ?  143  CYS   A C    1 
ATOM   3231 C  C    B CYS   A 1 143 ? 18.347 -14.953 1.572   0.50 10.24 ?  143  CYS   A C    1 
ATOM   3232 O  O    A CYS   A 1 143 ? 19.347 -15.706 1.853   0.50 9.28  ?  143  CYS   A O    1 
ATOM   3233 O  O    B CYS   A 1 143 ? 19.249 -15.507 2.211   0.50 10.00 ?  143  CYS   A O    1 
ATOM   3234 C  CB   A CYS   A 1 143 ? 17.896 -12.651 1.305   0.50 10.38 ?  143  CYS   A CB   1 
ATOM   3235 C  CB   B CYS   A 1 143 ? 17.864 -12.481 1.694   0.50 9.84  ?  143  CYS   A CB   1 
ATOM   3236 S  SG   A CYS   A 1 143 ? 18.299 -12.497 3.046   0.50 10.62 ?  143  CYS   A SG   1 
ATOM   3237 S  SG   B CYS   A 1 143 ? 18.448 -12.286 3.399   0.50 10.23 ?  143  CYS   A SG   1 
ATOM   3238 H  H    A CYS   A 1 143 ? 17.606 -13.276 -1.008  0.50 11.75 ?  143  CYS   A H    1 
ATOM   3239 H  H    B CYS   A 1 143 ? 17.511 -12.998 -0.657  0.50 11.57 ?  143  CYS   A H    1 
ATOM   3240 H  HA   A CYS   A 1 143 ? 19.590 -13.589 0.611   0.50 12.23 ?  143  CYS   A HA   1 
ATOM   3241 H  HA   B CYS   A 1 143 ? 19.517 -13.407 0.919   0.50 11.86 ?  143  CYS   A HA   1 
ATOM   3242 H  HB2  A CYS   A 1 143 ? 18.112 -11.816 0.876   0.50 12.46 ?  143  CYS   A HB2  1 
ATOM   3243 H  HB2  B CYS   A 1 143 ? 17.998 -11.636 1.230   0.50 11.81 ?  143  CYS   A HB2  1 
ATOM   3244 H  HB3  A CYS   A 1 143 ? 16.946 -12.820 1.243   0.50 12.46 ?  143  CYS   A HB3  1 
ATOM   3245 H  HB3  B CYS   A 1 143 ? 16.916 -12.677 1.734   0.50 11.81 ?  143  CYS   A HB3  1 
ATOM   3246 H  HG   A CYS   A 1 143 ? 17.738 -11.539 3.508   0.50 12.74 ?  143  CYS   A HG   1 
ATOM   3247 H  HG   B CYS   A 1 143 ? 17.842 -11.379 3.909   0.50 12.28 ?  143  CYS   A HG   1 
ATOM   3248 N  N    . VAL   A 1 144 ? 17.152 -15.521 1.401   1.00 11.11 ?  144  VAL   A N    1 
ATOM   3249 C  CA   . VAL   A 1 144 ? 16.813 -16.761 2.090   1.00 12.32 ?  144  VAL   A CA   1 
ATOM   3250 C  C    . VAL   A 1 144 ? 17.620 -17.931 1.550   1.00 11.97 ?  144  VAL   A C    1 
ATOM   3251 O  O    . VAL   A 1 144 ? 17.985 -18.845 2.301   1.00 12.59 ?  144  VAL   A O    1 
ATOM   3252 C  CB   . VAL   A 1 144 ? 15.294 -16.989 1.971   1.00 15.04 ?  144  VAL   A CB   1 
ATOM   3253 C  CG1  . VAL   A 1 144 ? 14.918 -18.419 2.279   1.00 16.77 ?  144  VAL   A CG1  1 
ATOM   3254 C  CG2  . VAL   A 1 144 ? 14.556 -16.000 2.873   1.00 14.94 ?  144  VAL   A CG2  1 
ATOM   3255 H  H    A VAL   A 1 144 ? 16.476 -15.109 1.055   0.50 13.33 ?  144  VAL   A H    1 
ATOM   3256 H  H    B VAL   A 1 144 ? 16.527 -15.213 0.890   0.50 13.33 ?  144  VAL   A H    1 
ATOM   3257 H  HA   . VAL   A 1 144 ? 17.018 -16.662 3.027   1.00 14.79 ?  144  VAL   A HA   1 
ATOM   3258 H  HB   . VAL   A 1 144 ? 15.017 -16.800 1.056   1.00 18.05 ?  144  VAL   A HB   1 
ATOM   3259 H  HG11 . VAL   A 1 144 ? 13.965 -18.462 2.468   1.00 20.13 ?  144  VAL   A HG11 1 
ATOM   3260 H  HG12 . VAL   A 1 144 ? 15.123 -18.974 1.512   1.00 20.13 ?  144  VAL   A HG12 1 
ATOM   3261 H  HG13 . VAL   A 1 144 ? 15.419 -18.715 3.053   1.00 20.13 ?  144  VAL   A HG13 1 
ATOM   3262 H  HG21 . VAL   A 1 144 ? 13.596 -16.146 2.797   1.00 17.93 ?  144  VAL   A HG21 1 
ATOM   3263 H  HG22 . VAL   A 1 144 ? 14.835 -16.134 3.792   1.00 17.93 ?  144  VAL   A HG22 1 
ATOM   3264 H  HG23 . VAL   A 1 144 ? 14.766 -15.090 2.596   1.00 17.93 ?  144  VAL   A HG23 1 
ATOM   3265 N  N    . ASP   A 1 145 ? 17.878 -17.952 0.247   1.00 12.23 ?  145  ASP   A N    1 
ATOM   3266 C  CA   . ASP   A 1 145 ? 18.586 -19.055 -0.393  1.00 12.70 ?  145  ASP   A CA   1 
ATOM   3267 C  C    . ASP   A 1 145 ? 20.108 -18.911 -0.353  1.00 12.55 ?  145  ASP   A C    1 
ATOM   3268 O  O    . ASP   A 1 145 ? 20.809 -19.810 -0.831  1.00 14.88 ?  145  ASP   A O    1 
ATOM   3269 C  CB   . ASP   A 1 145 ? 18.133 -19.185 -1.848  1.00 14.26 ?  145  ASP   A CB   1 
ATOM   3270 C  CG   . ASP   A 1 145 ? 16.693 -19.643 -1.975  1.00 16.37 ?  145  ASP   A CG   1 
ATOM   3271 O  OD1  . ASP   A 1 145 ? 16.141 -20.191 -0.997  1.00 17.23 ?  145  ASP   A OD1  1 
ATOM   3272 O  OD2  . ASP   A 1 145 ? 16.120 -19.457 -3.065  1.00 17.96 -1 145  ASP   A OD2  1 
ATOM   3273 H  H    . ASP   A 1 145 ? 17.637 -17.328 -0.299  1.00 14.67 ?  145  ASP   A H    1 
ATOM   3274 H  HA   . ASP   A 1 145 ? 18.352 -19.875 0.064   1.00 15.24 ?  145  ASP   A HA   1 
ATOM   3275 H  HB2  . ASP   A 1 145 ? 18.215 -18.323 -2.287  1.00 17.11 ?  145  ASP   A HB2  1 
ATOM   3276 H  HB3  . ASP   A 1 145 ? 18.689 -19.840 -2.294  1.00 17.11 ?  145  ASP   A HB3  1 
ATOM   3277 N  N    . THR   A 1 146 ? 20.634 -17.826 0.204   1.00 11.14 ?  146  THR   A N    1 
ATOM   3278 C  CA   . THR   A 1 146 ? 22.072 -17.572 0.218   1.00 10.57 ?  146  THR   A CA   1 
ATOM   3279 C  C    . THR   A 1 146 ? 22.635 -17.390 1.615   1.00 10.29 ?  146  THR   A C    1 
ATOM   3280 O  O    . THR   A 1 146 ? 23.711 -17.915 1.919   1.00 11.38 ?  146  THR   A O    1 
ATOM   3281 C  CB   . THR   A 1 146 ? 22.391 -16.318 -0.618  1.00 10.67 ?  146  THR   A CB   1 
ATOM   3282 O  OG1  . THR   A 1 146 ? 21.859 -16.474 -1.932  1.00 11.22 ?  146  THR   A OG1  1 
ATOM   3283 C  CG2  . THR   A 1 146 ? 23.889 -16.095 -0.716  1.00 11.22 ?  146  THR   A CG2  1 
ATOM   3284 H  H    . THR   A 1 146 ? 20.171 -17.206 0.586   1.00 13.37 ?  146  THR   A H    1 
ATOM   3285 H  HA   . THR   A 1 146 ? 22.529 -18.318 -0.189  1.00 12.68 ?  146  THR   A HA   1 
ATOM   3286 H  HB   . THR   A 1 146 ? 21.997 -15.536 -0.204  1.00 12.81 ?  146  THR   A HB   1 
ATOM   3287 H  HG1  . THR   A 1 146 ? 21.023 -16.554 -1.898  1.00 13.47 ?  146  THR   A HG1  1 
ATOM   3288 H  HG21 . THR   A 1 146 ? 24.079 -15.431 -1.399  1.00 13.46 ?  146  THR   A HG21 1 
ATOM   3289 H  HG22 . THR   A 1 146 ? 24.233 -15.777 0.133   1.00 13.46 ?  146  THR   A HG22 1 
ATOM   3290 H  HG23 . THR   A 1 146 ? 24.331 -16.923 -0.950  1.00 13.46 ?  146  THR   A HG23 1 
ATOM   3291 N  N    . VAL   A 1 147 ? 21.963 -16.619 2.458   1.00 10.35 ?  147  VAL   A N    1 
ATOM   3292 C  CA   . VAL   A 1 147 ? 22.460 -16.327 3.793   1.00 10.38 ?  147  VAL   A CA   1 
ATOM   3293 C  C    . VAL   A 1 147 ? 22.144 -17.502 4.707   1.00 10.94 ?  147  VAL   A C    1 
ATOM   3294 O  O    . VAL   A 1 147 ? 21.004 -17.982 4.752   1.00 11.54 ?  147  VAL   A O    1 
ATOM   3295 C  CB   . VAL   A 1 147 ? 21.846 -15.023 4.320   1.00 10.83 ?  147  VAL   A CB   1 
ATOM   3296 C  CG1  . VAL   A 1 147 ? 22.389 -14.721 5.686   1.00 11.93 ?  147  VAL   A CG1  1 
ATOM   3297 C  CG2  . VAL   A 1 147 ? 22.101 -13.871 3.353   1.00 10.94 ?  147  VAL   A CG2  1 
ATOM   3298 H  H    . VAL   A 1 147 ? 21.202 -16.257 2.282   1.00 12.42 ?  147  VAL   A H    1 
ATOM   3299 H  HA   . VAL   A 1 147 ? 23.423 -16.213 3.757   1.00 12.46 ?  147  VAL   A HA   1 
ATOM   3300 H  HB   . VAL   A 1 147 ? 20.888 -15.134 4.407   1.00 12.99 ?  147  VAL   A HB   1 
ATOM   3301 H  HG11 . VAL   A 1 147 ? 22.162 -13.812 5.926   1.00 14.32 ?  147  VAL   A HG11 1 
ATOM   3302 H  HG12 . VAL   A 1 147 ? 21.997 -15.338 6.327   1.00 14.32 ?  147  VAL   A HG12 1 
ATOM   3303 H  HG13 . VAL   A 1 147 ? 23.354 -14.830 5.674   1.00 14.32 ?  147  VAL   A HG13 1 
ATOM   3304 H  HG21 . VAL   A 1 147 ? 21.774 -13.046 3.751   1.00 13.13 ?  147  VAL   A HG21 1 
ATOM   3305 H  HG22 . VAL   A 1 147 ? 23.052 -13.803 3.186   1.00 13.13 ?  147  VAL   A HG22 1 
ATOM   3306 H  HG23 . VAL   A 1 147 ? 21.628 -14.047 2.526   1.00 13.13 ?  147  VAL   A HG23 1 
ATOM   3307 N  N    . ARG   A 1 148 ? 23.166 -17.971 5.424   1.00 11.12 ?  148  ARG   A N    1 
ATOM   3308 C  CA   . ARG   A 1 148 ? 23.037 -19.052 6.389   1.00 11.23 ?  148  ARG   A CA   1 
ATOM   3309 C  C    . ARG   A 1 148 ? 23.176 -18.581 7.825   1.00 11.70 ?  148  ARG   A C    1 
ATOM   3310 O  O    . ARG   A 1 148 ? 22.775 -19.307 8.745   1.00 13.12 ?  148  ARG   A O    1 
ATOM   3311 C  CB   . ARG   A 1 148 ? 24.070 -20.151 6.101   1.00 12.08 ?  148  ARG   A CB   1 
ATOM   3312 C  CG   . ARG   A 1 148 ? 23.893 -20.790 4.735   1.00 13.21 ?  148  ARG   A CG   1 
ATOM   3313 C  CD   . ARG   A 1 148 ? 24.972 -21.822 4.417   1.00 14.27 ?  148  ARG   A CD   1 
ATOM   3314 N  NE   . ARG   A 1 148 ? 26.307 -21.237 4.432   1.00 14.24 ?  148  ARG   A NE   1 
ATOM   3315 C  CZ   . ARG   A 1 148 ? 26.813 -20.502 3.451   1.00 13.54 ?  148  ARG   A CZ   1 
ATOM   3316 N  NH1  . ARG   A 1 148 ? 26.127 -20.255 2.346   1.00 13.78 ?  148  ARG   A NH1  1 
ATOM   3317 N  NH2  . ARG   A 1 148 ? 28.034 -19.986 3.588   1.00 13.84 ?  148  ARG   A NH2  1 
ATOM   3318 H  H    . ARG   A 1 148 ? 23.974 -17.665 5.354   1.00 13.34 ?  148  ARG   A H    1 
ATOM   3319 H  HA   . ARG   A 1 148 ? 22.161 -19.439 6.296   1.00 13.47 ?  148  ARG   A HA   1 
ATOM   3320 H  HB2  . ARG   A 1 148 ? 24.960 -19.777 6.144   1.00 14.49 ?  148  ARG   A HB2  1 
ATOM   3321 H  HB3  . ARG   A 1 148 ? 23.972 -20.853 6.769   1.00 14.49 ?  148  ARG   A HB3  1 
ATOM   3322 H  HG2  . ARG   A 1 148 ? 23.030 -21.231 4.706   1.00 15.85 ?  148  ARG   A HG2  1 
ATOM   3323 H  HG3  . ARG   A 1 148 ? 23.931 -20.092 4.061   1.00 15.85 ?  148  ARG   A HG3  1 
ATOM   3324 H  HD2  . ARG   A 1 148 ? 24.946 -22.529 5.082   1.00 17.13 ?  148  ARG   A HD2  1 
ATOM   3325 H  HD3  . ARG   A 1 148 ? 24.807 -22.195 3.534   1.00 17.13 ?  148  ARG   A HD3  1 
ATOM   3326 H  HE   . ARG   A 1 148 ? 26.810 -21.400 5.105   1.00 17.09 ?  148  ARG   A HE   1 
ATOM   3327 H  HH11 . ARG   A 1 148 ? 25.337 -20.576 2.244   1.00 16.54 ?  148  ARG   A HH11 1 
ATOM   3328 H  HH12 . ARG   A 1 148 ? 26.472 -19.765 1.726   1.00 16.54 ?  148  ARG   A HH12 1 
ATOM   3329 H  HH21 . ARG   A 1 148 ? 28.486 -20.138 4.298   1.00 16.61 ?  148  ARG   A HH21 1 
ATOM   3330 H  HH22 . ARG   A 1 148 ? 28.368 -19.499 2.958   1.00 16.61 ?  148  ARG   A HH22 1 
ATOM   3331 N  N    . THR   A 1 149 ? 23.729 -17.390 8.033   1.00 11.57 ?  149  THR   A N    1 
ATOM   3332 C  CA   . THR   A 1 149 ? 23.815 -16.801 9.352   1.00 11.73 ?  149  THR   A CA   1 
ATOM   3333 C  C    . THR   A 1 149 ? 22.489 -16.108 9.667   1.00 11.41 ?  149  THR   A C    1 
ATOM   3334 O  O    . THR   A 1 149 ? 21.547 -16.110 8.865   1.00 12.15 ?  149  THR   A O    1 
ATOM   3335 C  CB   . THR   A 1 149 ? 25.013 -15.860 9.402   1.00 12.05 ?  149  THR   A CB   1 
ATOM   3336 O  OG1  . THR   A 1 149 ? 24.878 -14.931 8.328   1.00 12.03 ?  149  THR   A OG1  1 
ATOM   3337 C  CG2  . THR   A 1 149 ? 26.321 -16.646 9.266   1.00 12.66 ?  149  THR   A CG2  1 
ATOM   3338 H  H    . THR   A 1 149 ? 24.067 -16.894 7.410   1.00 13.88 ?  149  THR   A H    1 
ATOM   3339 H  HA   . THR   A 1 149 ? 23.950 -17.503 10.003  1.00 14.08 ?  149  THR   A HA   1 
ATOM   3340 H  HB   . THR   A 1 149 ? 25.015 -15.387 10.246  1.00 14.47 ?  149  THR   A HB   1 
ATOM   3341 H  HG1  . THR   A 1 149 ? 25.526 -14.394 8.324   1.00 14.44 ?  149  THR   A HG1  1 
ATOM   3342 H  HG21 . THR   A 1 149 ? 27.079 -16.044 9.318   1.00 15.20 ?  149  THR   A HG21 1 
ATOM   3343 H  HG22 . THR   A 1 149 ? 26.392 -17.303 9.979   1.00 15.20 ?  149  THR   A HG22 1 
ATOM   3344 H  HG23 . THR   A 1 149 ? 26.347 -17.111 8.412   1.00 15.20 ?  149  THR   A HG23 1 
ATOM   3345 N  N    . ASN   A 1 150 ? 22.376 -15.553 10.867  1.00 11.59 ?  150  ASN   A N    1 
ATOM   3346 C  CA   . ASN   A 1 150 ? 21.092 -15.048 11.356  1.00 11.90 ?  150  ASN   A CA   1 
ATOM   3347 C  C    . ASN   A 1 150 ? 20.902 -13.609 10.899  1.00 11.23 ?  150  ASN   A C    1 
ATOM   3348 O  O    . ASN   A 1 150 ? 21.642 -12.710 11.318  1.00 12.75 ?  150  ASN   A O    1 
ATOM   3349 C  CB   . ASN   A 1 150 ? 21.035 -15.157 12.872  1.00 14.65 ?  150  ASN   A CB   1 
ATOM   3350 C  CG   . ASN   A 1 150 ? 20.933 -16.583 13.334  1.00 18.60 ?  150  ASN   A CG   1 
ATOM   3351 O  OD1  . ASN   A 1 150 ? 20.341 -17.420 12.654  1.00 19.89 ?  150  ASN   A OD1  1 
ATOM   3352 N  ND2  . ASN   A 1 150 ? 21.526 -16.881 14.483  1.00 20.75 ?  150  ASN   A ND2  1 
ATOM   3353 H  H    . ASN   A 1 150 ? 23.026 -15.458 11.420  1.00 13.91 ?  150  ASN   A H    1 
ATOM   3354 H  HA   . ASN   A 1 150 ? 20.372 -15.584 10.986  1.00 14.28 ?  150  ASN   A HA   1 
ATOM   3355 H  HB2  . ASN   A 1 150 ? 21.841 -14.776 13.253  1.00 17.58 ?  150  ASN   A HB2  1 
ATOM   3356 H  HB3  . ASN   A 1 150 ? 20.254 -14.683 13.200  1.00 17.58 ?  150  ASN   A HB3  1 
ATOM   3357 H  HD21 . ASN   A 1 150 ? 21.501 -17.688 14.791  1.00 24.90 ?  150  ASN   A HD21 1 
ATOM   3358 H  HD22 . ASN   A 1 150 ? 21.934 -16.270 14.933  1.00 24.90 ?  150  ASN   A HD22 1 
ATOM   3359 N  N    . VAL   A 1 151 ? 19.909 -13.384 10.048  1.00 11.13 ?  151  VAL   A N    1 
ATOM   3360 C  CA   . VAL   A 1 151 ? 19.691 -12.077 9.449   1.00 11.24 ?  151  VAL   A CA   1 
ATOM   3361 C  C    . VAL   A 1 151 ? 18.308 -11.561 9.822   1.00 10.70 ?  151  VAL   A C    1 
ATOM   3362 O  O    . VAL   A 1 151 ? 17.298 -12.268 9.676   1.00 12.12 ?  151  VAL   A O    1 
ATOM   3363 C  CB   . VAL   A 1 151 ? 19.971 -12.072 7.931   1.00 12.54 ?  151  VAL   A CB   1 
ATOM   3364 C  CG1  . VAL   A 1 151 ? 19.148 -13.097 7.186   1.00 13.33 ?  151  VAL   A CG1  1 
ATOM   3365 C  CG2  . VAL   A 1 151 ? 19.784 -10.669 7.351   1.00 12.82 ?  151  VAL   A CG2  1 
ATOM   3366 H  H    . VAL   A 1 151 ? 19.344 -13.981 9.799   1.00 13.35 ?  151  VAL   A H    1 
ATOM   3367 H  HA   . VAL   A 1 151 ? 20.333 -11.461 9.841   1.00 13.49 ?  151  VAL   A HA   1 
ATOM   3368 H  HB   . VAL   A 1 151 ? 20.906 -12.306 7.795   1.00 15.05 ?  151  VAL   A HB   1 
ATOM   3369 H  HG11 . VAL   A 1 151 ? 19.335 -13.034 6.236   1.00 15.99 ?  151  VAL   A HG11 1 
ATOM   3370 H  HG12 . VAL   A 1 151 ? 19.382 -13.986 7.507   1.00 15.99 ?  151  VAL   A HG12 1 
ATOM   3371 H  HG13 . VAL   A 1 151 ? 18.206 -12.929 7.348   1.00 15.99 ?  151  VAL   A HG13 1 
ATOM   3372 H  HG21 . VAL   A 1 151 ? 20.094 -10.665 6.429   1.00 15.39 ?  151  VAL   A HG21 1 
ATOM   3373 H  HG22 . VAL   A 1 151 ? 18.845 -10.434 7.383   1.00 15.39 ?  151  VAL   A HG22 1 
ATOM   3374 H  HG23 . VAL   A 1 151 ? 20.304 -10.037 7.873   1.00 15.39 ?  151  VAL   A HG23 1 
ATOM   3375 N  N    . TYR   A 1 152 ? 18.296 -10.323 10.310  1.00 10.88 ?  152  TYR   A N    1 
ATOM   3376 C  CA   . TYR   A 1 152 ? 17.107 -9.589  10.708  1.00 10.55 ?  152  TYR   A CA   1 
ATOM   3377 C  C    . TYR   A 1 152 ? 16.907 -8.484  9.683   1.00 10.40 ?  152  TYR   A C    1 
ATOM   3378 O  O    . TYR   A 1 152 ? 17.674 -7.513  9.645   1.00 10.95 ?  152  TYR   A O    1 
ATOM   3379 C  CB   . TYR   A 1 152 ? 17.306 -9.051  12.122  1.00 11.21 ?  152  TYR   A CB   1 
ATOM   3380 C  CG   . TYR   A 1 152 ? 17.272 -10.180 13.123  1.00 12.32 ?  152  TYR   A CG   1 
ATOM   3381 C  CD1  . TYR   A 1 152 ? 18.404 -10.940 13.393  1.00 13.67 ?  152  TYR   A CD1  1 
ATOM   3382 C  CD2  . TYR   A 1 152 ? 16.092 -10.532 13.752  1.00 12.61 ?  152  TYR   A CD2  1 
ATOM   3383 C  CE1  . TYR   A 1 152 ? 18.368 -11.998 14.278  1.00 15.08 ?  152  TYR   A CE1  1 
ATOM   3384 C  CE2  . TYR   A 1 152 ? 16.045 -11.594 14.642  1.00 14.15 ?  152  TYR   A CE2  1 
ATOM   3385 C  CZ   . TYR   A 1 152 ? 17.187 -12.321 14.898  1.00 15.37 ?  152  TYR   A CZ   1 
ATOM   3386 O  OH   . TYR   A 1 152 ? 17.149 -13.383 15.778  1.00 17.51 ?  152  TYR   A OH   1 
ATOM   3387 H  H    . TYR   A 1 152 ? 19.015 -9.855  10.412  1.00 13.05 ?  152  TYR   A H    1 
ATOM   3388 H  HA   . TYR   A 1 152 ? 16.336 -10.183 10.699  1.00 12.66 ?  152  TYR   A HA   1 
ATOM   3389 H  HB2  . TYR   A 1 152 ? 18.171 -8.622  12.184  1.00 13.45 ?  152  TYR   A HB2  1 
ATOM   3390 H  HB3  . TYR   A 1 152 ? 16.600 -8.427  12.338  1.00 13.45 ?  152  TYR   A HB3  1 
ATOM   3391 H  HD1  . TYR   A 1 152 ? 19.202 -10.723 12.969  1.00 16.40 ?  152  TYR   A HD1  1 
ATOM   3392 H  HD2  . TYR   A 1 152 ? 15.312 -10.050 13.580  1.00 15.13 ?  152  TYR   A HD2  1 
ATOM   3393 H  HE1  . TYR   A 1 152 ? 19.140 -12.487 14.452  1.00 18.10 ?  152  TYR   A HE1  1 
ATOM   3394 H  HE2  . TYR   A 1 152 ? 15.244 -11.814 15.065  1.00 16.98 ?  152  TYR   A HE2  1 
ATOM   3395 H  HH   . TYR   A 1 152 ? 16.369 -13.466 16.090  1.00 21.01 ?  152  TYR   A HH   1 
ATOM   3396 N  N    A LEU   A 1 153 ? 15.910 -8.677  8.813   0.50 10.23 ?  153  LEU   A N    1 
ATOM   3397 N  N    B LEU   A 1 153 ? 15.874 -8.612  8.869   0.50 10.53 ?  153  LEU   A N    1 
ATOM   3398 C  CA   A LEU   A 1 153 ? 15.644 -7.808  7.671   0.50 10.07 ?  153  LEU   A CA   1 
ATOM   3399 C  CA   B LEU   A 1 153 ? 15.593 -7.627  7.841   0.50 10.46 ?  153  LEU   A CA   1 
ATOM   3400 C  C    A LEU   A 1 153 ? 14.616 -6.746  8.038   0.50 10.32 ?  153  LEU   A C    1 
ATOM   3401 C  C    B LEU   A 1 153 ? 14.613 -6.587  8.367   0.50 10.73 ?  153  LEU   A C    1 
ATOM   3402 O  O    A LEU   A 1 153 ? 13.526 -7.069  8.523   0.50 11.41 ?  153  LEU   A O    1 
ATOM   3403 O  O    B LEU   A 1 153 ? 13.563 -6.935  8.919   0.50 11.60 ?  153  LEU   A O    1 
ATOM   3404 C  CB   A LEU   A 1 153 ? 15.100 -8.628  6.496   0.50 10.13 ?  153  LEU   A CB   1 
ATOM   3405 C  CB   B LEU   A 1 153 ? 15.001 -8.322  6.622   0.50 10.49 ?  153  LEU   A CB   1 
ATOM   3406 C  CG   A LEU   A 1 153 ? 16.031 -9.621  5.797   0.50 10.61 ?  153  LEU   A CG   1 
ATOM   3407 C  CG   B LEU   A 1 153 ? 15.926 -9.342  5.963   0.50 10.36 ?  153  LEU   A CG   1 
ATOM   3408 C  CD1  A LEU   A 1 153 ? 15.229 -10.502 4.849   0.50 10.81 ?  153  LEU   A CD1  1 
ATOM   3409 C  CD1  B LEU   A 1 153 ? 15.132 -10.189 4.988   0.50 10.63 ?  153  LEU   A CD1  1 
ATOM   3410 C  CD2  A LEU   A 1 153 ? 17.128 -8.896  5.035   0.50 11.07 ?  153  LEU   A CD2  1 
ATOM   3411 C  CD2  B LEU   A 1 153 ? 17.081 -8.642  5.264   0.50 10.87 ?  153  LEU   A CD2  1 
ATOM   3412 H  H    A LEU   A 1 153 ? 15.345 -9.332  8.876   0.50 12.27 ?  153  LEU   A H    1 
ATOM   3413 H  H    B LEU   A 1 153 ? 15.307 -9.263  8.897   0.50 12.63 ?  153  LEU   A H    1 
ATOM   3414 H  HA   A LEU   A 1 153 ? 16.462 -7.376  7.394   0.50 12.08 ?  153  LEU   A HA   1 
ATOM   3415 H  HA   B LEU   A 1 153 ? 16.418 -7.187  7.593   0.50 12.55 ?  153  LEU   A HA   1 
ATOM   3416 H  HB2  A LEU   A 1 153 ? 14.339 -9.138  6.809   0.50 12.16 ?  153  LEU   A HB2  1 
ATOM   3417 H  HB2  B LEU   A 1 153 ? 14.195 -8.781  6.897   0.50 12.59 ?  153  LEU   A HB2  1 
ATOM   3418 H  HB3  A LEU   A 1 153 ? 14.802 -8.007  5.811   0.50 12.16 ?  153  LEU   A HB3  1 
ATOM   3419 H  HB3  B LEU   A 1 153 ? 14.786 -7.642  5.965   0.50 12.59 ?  153  LEU   A HB3  1 
ATOM   3420 H  HG   A LEU   A 1 153 ? 16.450 -10.195 6.459   0.50 12.73 ?  153  LEU   A HG   1 
ATOM   3421 H  HG   B LEU   A 1 153 ? 16.297 -9.924  6.645   0.50 12.44 ?  153  LEU   A HG   1 
ATOM   3422 H  HD11 A LEU   A 1 153 ? 15.797 -11.217 4.520   0.50 12.97 ?  153  LEU   A HD11 1 
ATOM   3423 H  HD11 B LEU   A 1 153 ? 15.723 -10.842 4.586   0.50 12.75 ?  153  LEU   A HD11 1 
ATOM   3424 H  HD12 A LEU   A 1 153 ? 14.474 -10.875 5.327   0.50 12.97 ?  153  LEU   A HD12 1 
ATOM   3425 H  HD12 B LEU   A 1 153 ? 14.419 -10.634 5.469   0.50 12.75 ?  153  LEU   A HD12 1 
ATOM   3426 H  HD13 A LEU   A 1 153 ? 14.916 -9.961  4.106   0.50 12.97 ?  153  LEU   A HD13 1 
ATOM   3427 H  HD13 B LEU   A 1 153 ? 14.760 -9.610  4.303   0.50 12.75 ?  153  LEU   A HD13 1 
ATOM   3428 H  HD21 A LEU   A 1 153 ? 17.710 -9.550  4.618   0.50 13.29 ?  153  LEU   A HD21 1 
ATOM   3429 H  HD21 B LEU   A 1 153 ? 17.623 -9.307  4.812   0.50 13.05 ?  153  LEU   A HD21 1 
ATOM   3430 H  HD22 A LEU   A 1 153 ? 16.720 -8.336  4.355   0.50 13.29 ?  153  LEU   A HD22 1 
ATOM   3431 H  HD22 B LEU   A 1 153 ? 16.723 -8.012  4.620   0.50 13.05 ?  153  LEU   A HD22 1 
ATOM   3432 H  HD23 A LEU   A 1 153 ? 17.633 -8.351  5.655   0.50 13.29 ?  153  LEU   A HD23 1 
ATOM   3433 H  HD23 B LEU   A 1 153 ? 17.616 -8.173  5.924   0.50 13.05 ?  153  LEU   A HD23 1 
ATOM   3434 N  N    A ALA   A 1 154 ? 14.954 -5.487  7.772   0.50 10.04 ?  154  ALA   A N    1 
ATOM   3435 N  N    B ALA   A 1 154 ? 14.967 -5.313  8.202   0.50 10.17 ?  154  ALA   A N    1 
ATOM   3436 C  CA   A ALA   A 1 154 ? 14.070 -4.351  8.008   0.50 10.48 ?  154  ALA   A CA   1 
ATOM   3437 C  CA   B ALA   A 1 154 ? 14.086 -4.193  8.511   0.50 11.10 ?  154  ALA   A CA   1 
ATOM   3438 C  C    A ALA   A 1 154 ? 13.575 -3.818  6.670   0.50 10.30 ?  154  ALA   A C    1 
ATOM   3439 C  C    B ALA   A 1 154 ? 13.598 -3.606  7.193   0.50 11.34 ?  154  ALA   A C    1 
ATOM   3440 O  O    A ALA   A 1 154 ? 14.382 -3.457  5.807   0.50 10.80 ?  154  ALA   A O    1 
ATOM   3441 O  O    B ALA   A 1 154 ? 14.409 -3.200  6.354   0.50 11.53 ?  154  ALA   A O    1 
ATOM   3442 C  CB   A ALA   A 1 154 ? 14.809 -3.246  8.761   0.50 10.95 ?  154  ALA   A CB   1 
ATOM   3443 C  CB   B ALA   A 1 154 ? 14.810 -3.131  9.339   0.50 11.62 ?  154  ALA   A CB   1 
ATOM   3444 H  H    A ALA   A 1 154 ? 15.718 -5.265  7.447   0.50 12.05 ?  154  ALA   A H    1 
ATOM   3445 H  H    B ALA   A 1 154 ? 15.737 -5.061  7.901   0.50 12.21 ?  154  ALA   A H    1 
ATOM   3446 H  HA   A ALA   A 1 154 ? 13.308 -4.633  8.535   0.50 12.57 ?  154  ALA   A HA   1 
ATOM   3447 H  HA   B ALA   A 1 154 ? 13.320 -4.503  9.015   0.50 13.32 ?  154  ALA   A HA   1 
ATOM   3448 H  HB1  A ALA   A 1 154 ? 14.203 -2.505  8.905   0.50 13.14 ?  154  ALA   A HB1  1 
ATOM   3449 H  HB1  B ALA   A 1 154 ? 14.199 -2.399  9.527   0.50 13.95 ?  154  ALA   A HB1  1 
ATOM   3450 H  HB2  A ALA   A 1 154 ? 15.118 -3.595  9.612   0.50 13.14 ?  154  ALA   A HB2  1 
ATOM   3451 H  HB2  B ALA   A 1 154 ? 15.112 -3.528  10.173  0.50 13.95 ?  154  ALA   A HB2  1 
ATOM   3452 H  HB3  A ALA   A 1 154 ? 15.568 -2.956  8.229   0.50 13.14 ?  154  ALA   A HB3  1 
ATOM   3453 H  HB3  B ALA   A 1 154 ? 15.574 -2.800  8.839   0.50 13.95 ?  154  ALA   A HB3  1 
ATOM   3454 N  N    A VAL   A 1 155 ? 12.254 -3.757  6.513   0.50 10.61 ?  155  VAL   A N    1 
ATOM   3455 N  N    B VAL   A 1 155 ? 12.280 -3.567  7.017   0.50 11.98 ?  155  VAL   A N    1 
ATOM   3456 C  CA   A VAL   A 1 155 ? 11.604 -3.265  5.302   0.50 11.89 ?  155  VAL   A CA   1 
ATOM   3457 C  CA   B VAL   A 1 155 ? 11.642 -3.029  5.820   0.50 12.50 ?  155  VAL   A CA   1 
ATOM   3458 C  C    A VAL   A 1 155 ? 10.848 -1.984  5.658   0.50 13.20 ?  155  VAL   A C    1 
ATOM   3459 C  C    B VAL   A 1 155 ? 10.615 -2.008  6.279   0.50 13.87 ?  155  VAL   A C    1 
ATOM   3460 O  O    A VAL   A 1 155 ? 9.902  -2.013  6.452   0.50 13.55 ?  155  VAL   A O    1 
ATOM   3461 O  O    B VAL   A 1 155 ? 9.665  -2.360  6.989   0.50 14.27 ?  155  VAL   A O    1 
ATOM   3462 C  CB   A VAL   A 1 155 ? 10.668 -4.330  4.705   0.50 12.55 ?  155  VAL   A CB   1 
ATOM   3463 C  CB   B VAL   A 1 155 ? 10.957 -4.124  4.986   0.50 12.56 ?  155  VAL   A CB   1 
ATOM   3464 C  CG1  A VAL   A 1 155 ? 9.958  -3.798  3.472   0.50 13.24 ?  155  VAL   A CG1  1 
ATOM   3465 C  CG1  B VAL   A 1 155 ? 10.171 -3.496  3.841   0.50 13.33 ?  155  VAL   A CG1  1 
ATOM   3466 C  CG2  A VAL   A 1 155 ? 11.447 -5.599  4.363   0.50 13.07 ?  155  VAL   A CG2  1 
ATOM   3467 C  CG2  B VAL   A 1 155 ? 11.981 -5.125  4.466   0.50 12.01 ?  155  VAL   A CG2  1 
ATOM   3468 H  H    A VAL   A 1 155 ? 11.701 -4.024  7.115   0.50 12.73 ?  155  VAL   A H    1 
ATOM   3469 H  H    B VAL   A 1 155 ? 11.719 -3.843  7.605   0.50 14.38 ?  155  VAL   A H    1 
ATOM   3470 H  HA   A VAL   A 1 155 ? 12.280 -3.054  4.641   0.50 14.27 ?  155  VAL   A HA   1 
ATOM   3471 H  HA   B VAL   A 1 155 ? 12.300 -2.576  5.268   0.50 15.00 ?  155  VAL   A HA   1 
ATOM   3472 H  HB   A VAL   A 1 155 ? 9.993  -4.567  5.364   0.50 15.06 ?  155  VAL   A HB   1 
ATOM   3473 H  HB   B VAL   A 1 155 ? 10.329 -4.597  5.555   0.50 15.08 ?  155  VAL   A HB   1 
ATOM   3474 H  HG11 A VAL   A 1 155 ? 9.503  -4.530  3.029   0.50 15.89 ?  155  VAL   A HG11 1 
ATOM   3475 H  HG11 B VAL   A 1 155 ? 9.917  -4.192  3.217   0.50 15.99 ?  155  VAL   A HG11 1 
ATOM   3476 H  HG12 A VAL   A 1 155 ? 9.314  -3.125  3.744   0.50 15.89 ?  155  VAL   A HG12 1 
ATOM   3477 H  HG12 B VAL   A 1 155 ? 9.372  -3.062  4.190   0.50 15.99 ?  155  VAL   A HG12 1 
ATOM   3478 H  HG13 A VAL   A 1 155 ? 10.616 -3.408  2.876   0.50 15.89 ?  155  VAL   A HG13 1 
ATOM   3479 H  HG13 B VAL   A 1 155 ? 10.734 -2.845  3.397   0.50 15.99 ?  155  VAL   A HG13 1 
ATOM   3480 H  HG21 A VAL   A 1 155 ? 10.846 -6.235  3.940   0.50 15.68 ?  155  VAL   A HG21 1 
ATOM   3481 H  HG21 B VAL   A 1 155 ? 11.524 -5.798  3.942   0.50 14.41 ?  155  VAL   A HG21 1 
ATOM   3482 H  HG22 A VAL   A 1 155 ? 12.167 -5.371  3.754   0.50 15.68 ?  155  VAL   A HG22 1 
ATOM   3483 H  HG22 B VAL   A 1 155 ? 12.629 -4.657  3.917   0.50 14.41 ?  155  VAL   A HG22 1 
ATOM   3484 H  HG23 A VAL   A 1 155 ? 11.809 -5.980  5.177   0.50 15.68 ?  155  VAL   A HG23 1 
ATOM   3485 H  HG23 B VAL   A 1 155 ? 12.428 -5.539  5.222   0.50 14.41 ?  155  VAL   A HG23 1 
ATOM   3486 N  N    A PHE   A 1 156 ? 11.254 -0.859  5.063   0.50 14.24 ?  156  PHE   A N    1 
ATOM   3487 N  N    B PHE   A 1 156 ? 10.793 -0.750  5.865   0.50 14.85 ?  156  PHE   A N    1 
ATOM   3488 C  CA   A PHE   A 1 156 ? 10.718 0.441   5.479   0.50 15.54 ?  156  PHE   A CA   1 
ATOM   3489 C  CA   B PHE   A 1 156 ? 9.920  0.303   6.370   0.50 15.88 ?  156  PHE   A CA   1 
ATOM   3490 C  C    A PHE   A 1 156 ? 9.252  0.614   5.087   0.50 16.14 ?  156  PHE   A C    1 
ATOM   3491 C  C    B PHE   A 1 156 ? 8.588  0.362   5.626   0.50 16.53 ?  156  PHE   A C    1 
ATOM   3492 O  O    A PHE   A 1 156 ? 8.452  1.151   5.865   0.50 16.79 ?  156  PHE   A O    1 
ATOM   3493 O  O    B PHE   A 1 156 ? 7.530  0.510   6.252   0.50 17.17 ?  156  PHE   A O    1 
ATOM   3494 C  CB   A PHE   A 1 156 ? 11.563 1.563   4.875   0.50 16.69 ?  156  PHE   A CB   1 
ATOM   3495 C  CB   B PHE   A 1 156 ? 10.625 1.658   6.307   0.50 16.92 ?  156  PHE   A CB   1 
ATOM   3496 C  CG   A PHE   A 1 156 ? 11.067 2.949   5.206   0.50 18.16 ?  156  PHE   A CG   1 
ATOM   3497 C  CG   B PHE   A 1 156 ? 9.765  2.793   6.763   0.50 17.91 ?  156  PHE   A CG   1 
ATOM   3498 C  CD1  A PHE   A 1 156 ? 11.018 3.380   6.521   0.50 18.99 ?  156  PHE   A CD1  1 
ATOM   3499 C  CD1  B PHE   A 1 156 ? 9.638  3.083   8.111   0.50 18.60 ?  156  PHE   A CD1  1 
ATOM   3500 C  CD2  A PHE   A 1 156 ? 10.672 3.819   4.202   0.50 19.06 ?  156  PHE   A CD2  1 
ATOM   3501 C  CD2  B PHE   A 1 156 ? 9.065  3.560   5.847   0.50 18.25 ?  156  PHE   A CD2  1 
ATOM   3502 C  CE1  A PHE   A 1 156 ? 10.575 4.653   6.831   0.50 19.96 ?  156  PHE   A CE1  1 
ATOM   3503 C  CE1  B PHE   A 1 156 ? 8.838  4.126   8.537   0.50 19.00 ?  156  PHE   A CE1  1 
ATOM   3504 C  CE2  A PHE   A 1 156 ? 10.228 5.094   4.505   0.50 19.87 ?  156  PHE   A CE2  1 
ATOM   3505 C  CE2  B PHE   A 1 156 ? 8.266  4.606   6.264   0.50 18.70 ?  156  PHE   A CE2  1 
ATOM   3506 C  CZ   A PHE   A 1 156 ? 10.181 5.511   5.821   0.50 20.22 ?  156  PHE   A CZ   1 
ATOM   3507 C  CZ   B PHE   A 1 156 ? 8.149  4.888   7.612   0.50 18.97 ?  156  PHE   A CZ   1 
ATOM   3508 H  H    A PHE   A 1 156 ? 11.829 -0.833  4.429   0.50 17.08 ?  156  PHE   A H    1 
ATOM   3509 H  H    B PHE   A 1 156 ? 11.399 -0.480  5.309   0.50 17.82 ?  156  PHE   A H    1 
ATOM   3510 H  HA   A PHE   A 1 156 ? 10.785 0.507   6.446   0.50 18.64 ?  156  PHE   A HA   1 
ATOM   3511 H  HA   B PHE   A 1 156 ? 9.727  0.126   7.298   0.50 19.06 ?  156  PHE   A HA   1 
ATOM   3512 H  HB2  A PHE   A 1 156 ? 12.474 1.481   5.206   0.50 20.03 ?  156  PHE   A HB2  1 
ATOM   3513 H  HB2  B PHE   A 1 156 ? 11.409 1.633   6.881   0.50 20.30 ?  156  PHE   A HB2  1 
ATOM   3514 H  HB3  A PHE   A 1 156 ? 11.560 1.466   3.909   0.50 20.03 ?  156  PHE   A HB3  1 
ATOM   3515 H  HB3  B PHE   A 1 156 ? 10.894 1.838   5.392   0.50 20.30 ?  156  PHE   A HB3  1 
ATOM   3516 H  HD1  A PHE   A 1 156 ? 11.289 2.803   7.205   0.50 22.78 ?  156  PHE   A HD1  1 
ATOM   3517 H  HD1  B PHE   A 1 156 ? 10.101 2.576   8.736   0.50 22.32 ?  156  PHE   A HD1  1 
ATOM   3518 H  HD2  A PHE   A 1 156 ? 10.707 3.535   3.317   0.50 22.87 ?  156  PHE   A HD2  1 
ATOM   3519 H  HD2  B PHE   A 1 156 ? 9.142  3.379   4.937   0.50 21.90 ?  156  PHE   A HD2  1 
ATOM   3520 H  HE1  A PHE   A 1 156 ? 10.547 4.930   7.719   0.50 23.95 ?  156  PHE   A HE1  1 
ATOM   3521 H  HE1  B PHE   A 1 156 ? 8.764  4.321   9.443   0.50 22.80 ?  156  PHE   A HE1  1 
ATOM   3522 H  HE2  A PHE   A 1 156 ? 9.964  5.664   3.826   0.50 23.85 ?  156  PHE   A HE2  1 
ATOM   3523 H  HE2  B PHE   A 1 156 ? 7.806  5.122   5.637   0.50 22.44 ?  156  PHE   A HE2  1 
ATOM   3524 H  HZ   A PHE   A 1 156 ? 9.883  6.364   6.028   0.50 24.26 ?  156  PHE   A HZ   1 
ATOM   3525 H  HZ   B PHE   A 1 156 ? 7.614  5.597   7.892   0.50 22.76 ?  156  PHE   A HZ   1 
ATOM   3526 N  N    A ASP   A 1 157 ? 8.881  0.175   3.890   0.50 17.03 ?  157  ASP   A N    1 
ATOM   3527 N  N    B ASP   A 1 157 ? 8.623  0.272   4.297   0.50 16.70 ?  157  ASP   A N    1 
ATOM   3528 C  CA   A ASP   A 1 157 ? 7.544  0.425   3.361   0.50 17.98 ?  157  ASP   A CA   1 
ATOM   3529 C  CA   B ASP   A 1 157 ? 7.416  0.393   3.484   0.50 17.42 ?  157  ASP   A CA   1 
ATOM   3530 C  C    A ASP   A 1 157 ? 6.572  -0.620  3.899   0.50 18.22 ?  157  ASP   A C    1 
ATOM   3531 C  C    B ASP   A 1 157 ? 6.419  -0.707  3.834   0.50 17.65 ?  157  ASP   A C    1 
ATOM   3532 O  O    A ASP   A 1 157 ? 6.737  -1.816  3.635   0.50 17.56 ?  157  ASP   A O    1 
ATOM   3533 O  O    B ASP   A 1 157 ? 6.708  -1.896  3.666   0.50 17.36 ?  157  ASP   A O    1 
ATOM   3534 C  CB   A ASP   A 1 157 ? 7.602  0.359   1.838   0.50 19.05 ?  157  ASP   A CB   1 
ATOM   3535 C  CB   B ASP   A 1 157 ? 7.796  0.327   2.004   0.50 18.14 ?  157  ASP   A CB   1 
ATOM   3536 C  CG   A ASP   A 1 157 ? 6.324  0.847   1.176   0.50 20.59 ?  157  ASP   A CG   1 
ATOM   3537 C  CG   B ASP   A 1 157 ? 6.643  0.713   1.095   0.50 18.94 ?  157  ASP   A CG   1 
ATOM   3538 O  OD1  A ASP   A 1 157 ? 5.998  2.049   1.289   0.50 21.72 ?  157  ASP   A OD1  1 
ATOM   3539 O  OD1  B ASP   A 1 157 ? 5.553  0.116   1.247   0.50 19.40 ?  157  ASP   A OD1  1 
ATOM   3540 O  OD2  A ASP   A 1 157 ? 5.643  0.016   0.534   0.50 21.03 -1 157  ASP   A OD2  1 
ATOM   3541 O  OD2  B ASP   A 1 157 ? 6.816  1.627   0.255   0.50 19.08 -1 157  ASP   A OD2  1 
ATOM   3542 H  H    A ASP   A 1 157 ? 9.394  -0.276  3.364   0.50 20.44 ?  157  ASP   A H    1 
ATOM   3543 H  H    B ASP   A 1 157 ? 9.338  0.150   3.840   0.50 20.04 ?  157  ASP   A H    1 
ATOM   3544 H  HA   A ASP   A 1 157 ? 7.249  1.306   3.635   0.50 21.57 ?  157  ASP   A HA   1 
ATOM   3545 H  HA   B ASP   A 1 157 ? 6.992  1.248   3.643   0.50 20.90 ?  157  ASP   A HA   1 
ATOM   3546 H  HB2  A ASP   A 1 157 ? 8.371  0.874   1.537   0.50 22.86 ?  157  ASP   A HB2  1 
ATOM   3547 H  HB2  B ASP   A 1 157 ? 8.534  0.941   1.837   0.50 21.76 ?  157  ASP   A HB2  1 
ATOM   3548 H  HB3  A ASP   A 1 157 ? 7.707  -0.566  1.575   0.50 22.86 ?  157  ASP   A HB3  1 
ATOM   3549 H  HB3  B ASP   A 1 157 ? 8.081  -0.580  1.785   0.50 21.76 ?  157  ASP   A HB3  1 
ATOM   3550 N  N    A LYS   A 1 158 ? 5.558  -0.174  4.652   0.50 19.05 ?  158  LYS   A N    1 
ATOM   3551 N  N    B LYS   A 1 158 ? 5.238  -0.299  4.307   0.50 18.25 ?  158  LYS   A N    1 
ATOM   3552 C  CA   A LYS   A 1 158 ? 4.603  -1.114  5.236   0.50 19.59 ?  158  LYS   A CA   1 
ATOM   3553 C  CA   B LYS   A 1 158 ? 4.254  -1.242  4.835   0.50 19.17 ?  158  LYS   A CA   1 
ATOM   3554 C  C    A LYS   A 1 158 ? 3.858  -1.886  4.155   0.50 19.58 ?  158  LYS   A C    1 
ATOM   3555 C  C    B LYS   A 1 158 ? 3.666  -2.121  3.733   0.50 18.53 ?  158  LYS   A C    1 
ATOM   3556 O  O    A LYS   A 1 158 ? 3.613  -3.090  4.298   0.50 19.92 ?  158  LYS   A O    1 
ATOM   3557 O  O    B LYS   A 1 158 ? 3.581  -3.348  3.879   0.50 18.18 ?  158  LYS   A O    1 
ATOM   3558 C  CB   A LYS   A 1 158 ? 3.621  -0.379  6.154   0.50 20.00 ?  158  LYS   A CB   1 
ATOM   3559 C  CB   B LYS   A 1 158 ? 3.160  -0.455  5.560   0.50 21.04 ?  158  LYS   A CB   1 
ATOM   3560 C  CG   A LYS   A 1 158 ? 2.420  -1.215  6.616   0.50 20.63 ?  158  LYS   A CG   1 
ATOM   3561 C  CG   B LYS   A 1 158 ? 1.873  -1.211  5.839   0.50 22.85 ?  158  LYS   A CG   1 
ATOM   3562 C  CD   A LYS   A 1 158 ? 2.831  -2.451  7.413   0.50 21.31 ?  158  LYS   A CD   1 
ATOM   3563 C  CD   B LYS   A 1 158 ? 2.090  -2.345  6.812   0.50 24.20 ?  158  LYS   A CD   1 
ATOM   3564 C  CE   A LYS   A 1 158 ? 1.606  -3.144  8.000   0.50 21.89 ?  158  LYS   A CE   1 
ATOM   3565 C  CE   B LYS   A 1 158 ? 0.773  -2.984  7.203   0.50 25.08 ?  158  LYS   A CE   1 
ATOM   3566 N  NZ   A LYS   A 1 158 ? 1.909  -4.495  8.549   0.50 22.12 ?  158  LYS   A NZ   1 
ATOM   3567 N  NZ   B LYS   A 1 158 ? 0.975  -4.280  7.904   0.50 25.81 ?  158  LYS   A NZ   1 
ATOM   3568 H  H    A LYS   A 1 158 ? 5.409  0.652   4.832   0.50 22.86 ?  158  LYS   A H    1 
ATOM   3569 H  H    B LYS   A 1 158 ? 4.985  0.521   4.339   0.50 21.90 ?  158  LYS   A H    1 
ATOM   3570 H  HA   A LYS   A 1 158 ? 5.087  -1.753  5.782   0.50 23.50 ?  158  LYS   A HA   1 
ATOM   3571 H  HA   B LYS   A 1 158 ? 4.684  -1.821  5.484   0.50 23.00 ?  158  LYS   A HA   1 
ATOM   3572 H  HB2  A LYS   A 1 158 ? 4.097  -0.087  6.950   0.50 24.00 ?  158  LYS   A HB2  1 
ATOM   3573 H  HB2  B LYS   A 1 158 ? 3.512  -0.161  6.417   0.50 25.25 ?  158  LYS   A HB2  1 
ATOM   3574 H  HB3  A LYS   A 1 158 ? 3.276  0.396   5.683   0.50 24.00 ?  158  LYS   A HB3  1 
ATOM   3575 H  HB3  B LYS   A 1 158 ? 2.932  0.319   5.024   0.50 25.25 ?  158  LYS   A HB3  1 
ATOM   3576 H  HG2  A LYS   A 1 158 ? 1.862  -0.666  7.187   0.50 24.75 ?  158  LYS   A HG2  1 
ATOM   3577 H  HG2  B LYS   A 1 158 ? 1.233  -0.599  6.233   0.50 27.42 ?  158  LYS   A HG2  1 
ATOM   3578 H  HG3  A LYS   A 1 158 ? 1.910  -1.505  5.843   0.50 24.75 ?  158  LYS   A HG3  1 
ATOM   3579 H  HG3  B LYS   A 1 158 ? 1.514  -1.574  5.014   0.50 27.42 ?  158  LYS   A HG3  1 
ATOM   3580 H  HD2  A LYS   A 1 158 ? 3.286  -3.075  6.827   0.50 25.57 ?  158  LYS   A HD2  1 
ATOM   3581 H  HD2  B LYS   A 1 158 ? 2.650  -3.020  6.399   0.50 29.04 ?  158  LYS   A HD2  1 
ATOM   3582 H  HD3  A LYS   A 1 158 ? 3.413  -2.183  8.141   0.50 25.57 ?  158  LYS   A HD3  1 
ATOM   3583 H  HD3  B LYS   A 1 158 ? 2.514  -2.000  7.615   0.50 29.04 ?  158  LYS   A HD3  1 
ATOM   3584 H  HE2  A LYS   A 1 158 ? 1.241  -2.600  8.715   0.50 26.26 ?  158  LYS   A HE2  1 
ATOM   3585 H  HE2  B LYS   A 1 158 ? 0.300  -2.385  7.801   0.50 30.10 ?  158  LYS   A HE2  1 
ATOM   3586 H  HE3  A LYS   A 1 158 ? 0.945  -3.250  7.303   0.50 26.26 ?  158  LYS   A HE3  1 
ATOM   3587 H  HE3  B LYS   A 1 158 ? 0.244  -3.138  6.405   0.50 30.10 ?  158  LYS   A HE3  1 
ATOM   3588 H  HZ1  A LYS   A 1 158 ? 1.170  -4.863  8.878   0.50 26.55 ?  158  LYS   A HZ1  1 
ATOM   3589 H  HZ1  B LYS   A 1 158 ? 0.187  -4.633  8.119   0.50 30.97 ?  158  LYS   A HZ1  1 
ATOM   3590 H  HZ2  A LYS   A 1 158 ? 2.230  -5.018  7.903   0.50 26.55 ?  158  LYS   A HZ2  1 
ATOM   3591 H  HZ2  B LYS   A 1 158 ? 1.412  -4.846  7.374   0.50 30.97 ?  158  LYS   A HZ2  1 
ATOM   3592 H  HZ3  A LYS   A 1 158 ? 2.516  -4.433  9.197   0.50 26.55 ?  158  LYS   A HZ3  1 
ATOM   3593 H  HZ3  B LYS   A 1 158 ? 1.449  -4.152  8.646   0.50 30.97 ?  158  LYS   A HZ3  1 
ATOM   3594 N  N    A ASN   A 1 159 ? 3.488  -1.213  3.065   0.50 19.65 ?  159  ASN   A N    1 
ATOM   3595 N  N    B ASN   A 1 159 ? 3.230  -1.512  2.630   0.50 19.44 ?  159  ASN   A N    1 
ATOM   3596 C  CA   A ASN   A 1 159 ? 2.823  -1.916  1.974   0.50 19.95 ?  159  ASN   A CA   1 
ATOM   3597 C  CA   B ASN   A 1 159 ? 2.647  -2.290  1.542   0.50 20.28 ?  159  ASN   A CA   1 
ATOM   3598 C  C    A ASN   A 1 159 ? 3.731  -2.986  1.372   0.50 19.10 ?  159  ASN   A C    1 
ATOM   3599 C  C    B ASN   A 1 159 ? 3.640  -3.325  1.024   0.50 18.81 ?  159  ASN   A C    1 
ATOM   3600 O  O    A ASN   A 1 159 ? 3.285  -4.107  1.106   0.50 19.03 ?  159  ASN   A O    1 
ATOM   3601 O  O    B ASN   A 1 159 ? 3.275  -4.477  0.755   0.50 18.95 ?  159  ASN   A O    1 
ATOM   3602 C  CB   A ASN   A 1 159 ? 2.345  -0.915  0.922   0.50 21.28 ?  159  ASN   A CB   1 
ATOM   3603 C  CB   B ASN   A 1 159 ? 2.182  -1.341  0.433   0.50 22.81 ?  159  ASN   A CB   1 
ATOM   3604 C  CG   A ASN   A 1 159 ? 1.170  -0.084  1.406   0.50 23.01 ?  159  ASN   A CG   1 
ATOM   3605 C  CG   B ASN   A 1 159 ? 1.094  -0.386  0.904   0.50 25.23 ?  159  ASN   A CG   1 
ATOM   3606 O  OD1  A ASN   A 1 159 ? 0.312  -0.578  2.134   0.50 23.67 ?  159  ASN   A OD1  1 
ATOM   3607 O  OD1  B ASN   A 1 159 ? 0.077  -0.814  1.448   0.50 26.03 ?  159  ASN   A OD1  1 
ATOM   3608 N  ND2  A ASN   A 1 159 ? 1.129  1.183   1.009   0.50 23.90 ?  159  ASN   A ND2  1 
ATOM   3609 N  ND2  B ASN   A 1 159 ? 1.313  0.913   0.710   0.50 26.40 ?  159  ASN   A ND2  1 
ATOM   3610 H  H    A ASN   A 1 159 ? 3.607  -0.372  2.941   0.50 23.58 ?  159  ASN   A H    1 
ATOM   3611 H  H    B ASN   A 1 159 ? 3.264  -0.668  2.492   0.50 23.33 ?  159  ASN   A H    1 
ATOM   3612 H  HA   A ASN   A 1 159 ? 2.039  -2.363  2.331   0.50 23.95 ?  159  ASN   A HA   1 
ATOM   3613 H  HA   B ASN   A 1 159 ? 1.866  -2.763  1.870   0.50 24.34 ?  159  ASN   A HA   1 
ATOM   3614 H  HB2  A ASN   A 1 159 ? 3.068  -0.311  0.706   0.50 25.53 ?  159  ASN   A HB2  1 
ATOM   3615 H  HB2  B ASN   A 1 159 ? 2.934  -0.807  0.132   0.50 27.37 ?  159  ASN   A HB2  1 
ATOM   3616 H  HB3  A ASN   A 1 159 ? 2.064  -1.401  0.130   0.50 25.53 ?  159  ASN   A HB3  1 
ATOM   3617 H  HB3  B ASN   A 1 159 ? 1.821  -1.855  -0.303  0.50 27.37 ?  159  ASN   A HB3  1 
ATOM   3618 H  HD21 A ASN   A 1 159 ? 0.485  1.691   1.257   0.50 28.68 ?  159  ASN   A HD21 1 
ATOM   3619 H  HD21 B ASN   A 1 159 ? 0.730  1.495   0.966   0.50 31.68 ?  159  ASN   A HD21 1 
ATOM   3620 H  HD22 A ASN   A 1 159 ? 1.753  1.494   0.508   0.50 28.68 ?  159  ASN   A HD22 1 
ATOM   3621 H  HD22 B ASN   A 1 159 ? 2.038  1.177   0.330   0.50 31.68 ?  159  ASN   A HD22 1 
ATOM   3622 N  N    A LEU   A 1 160 ? 5.013  -2.673  1.177   0.50 18.42 ?  160  LEU   A N    1 
ATOM   3623 N  N    B LEU   A 1 160 ? 4.911  -2.941  0.913   0.50 17.70 ?  160  LEU   A N    1 
ATOM   3624 C  CA   A LEU   A 1 160 ? 5.921  -3.667  0.609   0.50 17.92 ?  160  LEU   A CA   1 
ATOM   3625 C  CA   B LEU   A 1 160 ? 5.935  -3.886  0.487   0.50 17.34 ?  160  LEU   A CA   1 
ATOM   3626 C  C    A LEU   A 1 160 ? 6.121  -4.838  1.559   0.50 17.13 ?  160  LEU   A C    1 
ATOM   3627 C  C    B LEU   A 1 160 ? 6.163  -4.963  1.543   0.50 16.55 ?  160  LEU   A C    1 
ATOM   3628 O  O    A LEU   A 1 160 ? 6.159  -5.997  1.127   0.50 17.69 ?  160  LEU   A O    1 
ATOM   3629 O  O    B LEU   A 1 160 ? 6.234  -6.156  1.222   0.50 16.92 ?  160  LEU   A O    1 
ATOM   3630 C  CB   A LEU   A 1 160 ? 7.266  -3.035  0.258   0.50 17.93 ?  160  LEU   A CB   1 
ATOM   3631 C  CB   B LEU   A 1 160 ? 7.232  -3.137  0.194   0.50 17.67 ?  160  LEU   A CB   1 
ATOM   3632 C  CG   A LEU   A 1 160 ? 8.338  -4.049  -0.154  0.50 18.03 ?  160  LEU   A CG   1 
ATOM   3633 C  CG   B LEU   A 1 160 ? 8.381  -4.042  -0.227  0.50 18.32 ?  160  LEU   A CG   1 
ATOM   3634 C  CD1  A LEU   A 1 160 ? 7.913  -4.795  -1.410  0.50 18.61 ?  160  LEU   A CD1  1 
ATOM   3635 C  CD1  B LEU   A 1 160 ? 7.928  -4.915  -1.380  0.50 18.95 ?  160  LEU   A CD1  1 
ATOM   3636 C  CD2  A LEU   A 1 160 ? 9.688  -3.384  -0.349  0.50 17.70 ?  160  LEU   A CD2  1 
ATOM   3637 C  CD2  B LEU   A 1 160 ? 9.589  -3.210  -0.607  0.50 18.47 ?  160  LEU   A CD2  1 
ATOM   3638 H  H    A LEU   A 1 160 ? 5.372  -1.919  1.374   0.50 22.10 ?  160  LEU   A H    1 
ATOM   3639 H  H    B LEU   A 1 160 ? 5.197  -2.149  1.077   0.50 21.24 ?  160  LEU   A H    1 
ATOM   3640 H  HA   A LEU   A 1 160 ? 5.529  -4.013  -0.203  0.50 21.51 ?  160  LEU   A HA   1 
ATOM   3641 H  HA   B LEU   A 1 160 ? 5.634  -4.311  -0.332  0.50 20.81 ?  160  LEU   A HA   1 
ATOM   3642 H  HB2  A LEU   A 1 160 ? 7.137  -2.409  -0.476  0.50 21.51 ?  160  LEU   A HB2  1 
ATOM   3643 H  HB2  B LEU   A 1 160 ? 7.075  -2.502  -0.526  0.50 21.20 ?  160  LEU   A HB2  1 
ATOM   3644 H  HB3  A LEU   A 1 160 ? 7.596  -2.567  1.037   0.50 21.51 ?  160  LEU   A HB3  1 
ATOM   3645 H  HB3  B LEU   A 1 160 ? 7.506  -2.661  0.994   0.50 21.20 ?  160  LEU   A HB3  1 
ATOM   3646 H  HG   A LEU   A 1 160 ? 8.446  -4.702  0.553   0.50 21.63 ?  160  LEU   A HG   1 
ATOM   3647 H  HG   B LEU   A 1 160 ? 8.627  -4.617  0.514   0.50 21.98 ?  160  LEU   A HG   1 
ATOM   3648 H  HD11 A LEU   A 1 160 ? 8.646  -5.356  -1.703  0.50 22.33 ?  160  LEU   A HD11 1 
ATOM   3649 H  HD11 B LEU   A 1 160 ? 8.691  -5.383  -1.730  0.50 22.73 ?  160  LEU   A HD11 1 
ATOM   3650 H  HD12 A LEU   A 1 160 ? 7.138  -5.346  -1.205  0.50 22.33 ?  160  LEU   A HD12 1 
ATOM   3651 H  HD12 B LEU   A 1 160 ? 7.271  -5.555  -1.060  0.50 22.73 ?  160  LEU   A HD12 1 
ATOM   3652 H  HD13 A LEU   A 1 160 ? 7.688  -4.152  -2.099  0.50 22.33 ?  160  LEU   A HD13 1 
ATOM   3653 H  HD13 B LEU   A 1 160 ? 7.533  -4.350  -2.066  0.50 22.73 ?  160  LEU   A HD13 1 
ATOM   3654 H  HD21 A LEU   A 1 160 ? 10.335 -4.059  -0.605  0.50 21.24 ?  160  LEU   A HD21 1 
ATOM   3655 H  HD21 B LEU   A 1 160 ? 10.347 -3.798  -0.743  0.50 22.17 ?  160  LEU   A HD21 1 
ATOM   3656 H  HD22 A LEU   A 1 160 ? 9.612  -2.715  -1.047  0.50 21.24 ?  160  LEU   A HD22 1 
ATOM   3657 H  HD22 B LEU   A 1 160 ? 9.394  -2.725  -1.424  0.50 22.17 ?  160  LEU   A HD22 1 
ATOM   3658 H  HD23 A LEU   A 1 160 ? 9.956  -2.965  0.484   0.50 21.24 ?  160  LEU   A HD23 1 
ATOM   3659 H  HD23 B LEU   A 1 160 ? 9.779  -2.585  0.111   0.50 22.17 ?  160  LEU   A HD23 1 
ATOM   3660 N  N    A TYR   A 1 161 ? 6.270  -4.555  2.853   0.50 16.39 ?  161  TYR   A N    1 
ATOM   3661 N  N    B TYR   A 1 161 ? 6.295  -4.559  2.809   0.50 16.09 ?  161  TYR   A N    1 
ATOM   3662 C  CA   A TYR   A 1 161 ? 6.427  -5.620  3.833   0.50 15.74 ?  161  TYR   A CA   1 
ATOM   3663 C  CA   B TYR   A 1 161 ? 6.395  -5.539  3.888   0.50 15.84 ?  161  TYR   A CA   1 
ATOM   3664 C  C    A TYR   A 1 161 ? 5.291  -6.631  3.732   0.50 15.50 ?  161  TYR   A C    1 
ATOM   3665 C  C    B TYR   A 1 161 ? 5.246  -6.540  3.829   0.50 16.26 ?  161  TYR   A C    1 
ATOM   3666 O  O    A TYR   A 1 161 ? 5.527  -7.838  3.612   0.50 14.82 ?  161  TYR   A O    1 
ATOM   3667 O  O    B TYR   A 1 161 ? 5.455  -7.744  4.014   0.50 15.78 ?  161  TYR   A O    1 
ATOM   3668 C  CB   A TYR   A 1 161 ? 6.489  -5.020  5.234   0.50 15.69 ?  161  TYR   A CB   1 
ATOM   3669 C  CB   B TYR   A 1 161 ? 6.451  -4.837  5.252   0.50 15.59 ?  161  TYR   A CB   1 
ATOM   3670 C  CG   A TYR   A 1 161 ? 6.406  -6.065  6.307   0.50 15.22 ?  161  TYR   A CG   1 
ATOM   3671 C  CG   B TYR   A 1 161 ? 6.355  -5.779  6.445   0.50 15.09 ?  161  TYR   A CG   1 
ATOM   3672 C  CD1  A TYR   A 1 161 ? 7.532  -6.767  6.694   0.50 15.16 ?  161  TYR   A CD1  1 
ATOM   3673 C  CD1  B TYR   A 1 161 ? 7.484  -6.414  6.957   0.50 14.94 ?  161  TYR   A CD1  1 
ATOM   3674 C  CD2  A TYR   A 1 161 ? 5.196  -6.368  6.922   0.50 15.13 ?  161  TYR   A CD2  1 
ATOM   3675 C  CD2  B TYR   A 1 161 ? 5.135  -6.024  7.065   0.50 15.33 ?  161  TYR   A CD2  1 
ATOM   3676 C  CE1  A TYR   A 1 161 ? 7.465  -7.731  7.663   0.50 15.35 ?  161  TYR   A CE1  1 
ATOM   3677 C  CE1  B TYR   A 1 161 ? 7.394  -7.275  8.046   0.50 15.51 ?  161  TYR   A CE1  1 
ATOM   3678 C  CE2  A TYR   A 1 161 ? 5.120  -7.333  7.895   0.50 15.18 ?  161  TYR   A CE2  1 
ATOM   3679 C  CE2  B TYR   A 1 161 ? 5.036  -6.879  8.151   0.50 15.60 ?  161  TYR   A CE2  1 
ATOM   3680 C  CZ   A TYR   A 1 161 ? 6.259  -8.011  8.261   0.50 15.38 ?  161  TYR   A CZ   1 
ATOM   3681 C  CZ   B TYR   A 1 161 ? 6.164  -7.501  8.637   0.50 16.00 ?  161  TYR   A CZ   1 
ATOM   3682 O  OH   A TYR   A 1 161 ? 6.201  -8.977  9.231   0.50 15.60 ?  161  TYR   A OH   1 
ATOM   3683 O  OH   B TYR   A 1 161 ? 6.058  -8.352  9.719   0.50 17.28 ?  161  TYR   A OH   1 
ATOM   3684 H  H    A TYR   A 1 161 ? 6.270  -3.765  3.187   0.50 19.66 ?  161  TYR   A H    1 
ATOM   3685 H  H    B TYR   A 1 161 ? 6.327  -3.738  3.059   0.50 19.31 ?  161  TYR   A H    1 
ATOM   3686 H  HA   A TYR   A 1 161 ? 7.256  -6.090  3.670   0.50 18.88 ?  161  TYR   A HA   1 
ATOM   3687 H  HA   B TYR   A 1 161 ? 7.217  -6.030  3.780   0.50 19.00 ?  161  TYR   A HA   1 
ATOM   3688 H  HB2  A TYR   A 1 161 ? 7.331  -4.550  5.339   0.50 18.82 ?  161  TYR   A HB2  1 
ATOM   3689 H  HB2  B TYR   A 1 161 ? 7.292  -4.359  5.320   0.50 18.70 ?  161  TYR   A HB2  1 
ATOM   3690 H  HB3  A TYR   A 1 161 ? 5.747  -4.407  5.353   0.50 18.82 ?  161  TYR   A HB3  1 
ATOM   3691 H  HB3  B TYR   A 1 161 ? 5.713  -4.209  5.312   0.50 18.70 ?  161  TYR   A HB3  1 
ATOM   3692 H  HD1  A TYR   A 1 161 ? 8.347  -6.582  6.289   0.50 18.19 ?  161  TYR   A HD1  1 
ATOM   3693 H  HD1  B TYR   A 1 161 ? 8.312  -6.262  6.563   0.50 17.93 ?  161  TYR   A HD1  1 
ATOM   3694 H  HD2  A TYR   A 1 161 ? 4.426  -5.909  6.673   0.50 18.16 ?  161  TYR   A HD2  1 
ATOM   3695 H  HD2  B TYR   A 1 161 ? 4.367  -5.611  6.745   0.50 18.39 ?  161  TYR   A HD2  1 
ATOM   3696 H  HE1  A TYR   A 1 161 ? 8.230  -8.198  7.913   0.50 18.42 ?  161  TYR   A HE1  1 
ATOM   3697 H  HE1  B TYR   A 1 161 ? 8.159  -7.694  8.379   0.50 18.61 ?  161  TYR   A HE1  1 
ATOM   3698 H  HE2  A TYR   A 1 161 ? 4.303  -7.527  8.302   0.50 18.22 ?  161  TYR   A HE2  1 
ATOM   3699 H  HE2  B TYR   A 1 161 ? 4.209  -7.036  8.553   0.50 18.72 ?  161  TYR   A HE2  1 
ATOM   3700 H  HH   A TYR   A 1 161 ? 5.406  -9.054  9.510   0.50 18.73 ?  161  TYR   A HH   1 
ATOM   3701 H  HH   B TYR   A 1 161 ? 5.256  -8.399  9.978   0.50 20.73 ?  161  TYR   A HH   1 
ATOM   3702 N  N    A ASP   A 1 162 ? 4.044  -6.152  3.781   0.50 16.09 ?  162  ASP   A N    1 
ATOM   3703 N  N    B ASP   A 1 162 ? 4.025  -6.065  3.555   0.50 17.16 ?  162  ASP   A N    1 
ATOM   3704 C  CA   A ASP   A 1 162 ? 2.896  -7.054  3.721   0.50 16.74 ?  162  ASP   A CA   1 
ATOM   3705 C  CA   B ASP   A 1 162 ? 2.876  -6.967  3.485   0.50 18.28 ?  162  ASP   A CA   1 
ATOM   3706 C  C    A ASP   A 1 162 ? 2.936  -7.915  2.463   0.50 17.43 ?  162  ASP   A C    1 
ATOM   3707 C  C    B ASP   A 1 162 ? 2.967  -7.893  2.277   0.50 18.80 ?  162  ASP   A C    1 
ATOM   3708 O  O    A ASP   A 1 162 ? 2.555  -9.092  2.495   0.50 17.74 ?  162  ASP   A O    1 
ATOM   3709 O  O    B ASP   A 1 162 ? 2.638  -9.082  2.372   0.50 19.08 ?  162  ASP   A O    1 
ATOM   3710 C  CB   A ASP   A 1 162 ? 1.587  -6.257  3.776   0.50 17.21 ?  162  ASP   A CB   1 
ATOM   3711 C  CB   B ASP   A 1 162 ? 1.566  -6.173  3.428   0.50 19.57 ?  162  ASP   A CB   1 
ATOM   3712 C  CG   A ASP   A 1 162 ? 1.266  -5.718  5.165   0.50 18.09 ?  162  ASP   A CG   1 
ATOM   3713 C  CG   B ASP   A 1 162 ? 1.253  -5.430  4.716   0.50 20.85 ?  162  ASP   A CG   1 
ATOM   3714 O  OD1  A ASP   A 1 162 ? 1.988  -6.048  6.129   0.50 19.10 ?  162  ASP   A OD1  1 
ATOM   3715 O  OD1  B ASP   A 1 162 ? 1.745  -5.826  5.790   0.50 21.33 ?  162  ASP   A OD1  1 
ATOM   3716 O  OD2  A ASP   A 1 162 ? 0.271  -4.964  5.284   0.50 18.62 -1 162  ASP   A OD2  1 
ATOM   3717 O  OD2  B ASP   A 1 162 ? 0.480  -4.450  4.646   0.50 21.42 -1 162  ASP   A OD2  1 
ATOM   3718 H  H    A ASP   A 1 162 ? 3.838  -5.324  3.844   0.50 19.31 ?  162  ASP   A H    1 
ATOM   3719 H  H    B ASP   A 1 162 ? 3.837  -5.242  3.407   0.50 20.60 ?  162  ASP   A H    1 
ATOM   3720 H  HA   A ASP   A 1 162 ? 2.912  -7.652  4.482   0.50 20.09 ?  162  ASP   A HA   1 
ATOM   3721 H  HA   B ASP   A 1 162 ? 2.855  -7.523  4.278   0.50 21.94 ?  162  ASP   A HA   1 
ATOM   3722 H  HB2  A ASP   A 1 162 ? 1.647  -5.507  3.168   0.50 20.66 ?  162  ASP   A HB2  1 
ATOM   3723 H  HB2  B ASP   A 1 162 ? 1.622  -5.518  2.721   0.50 23.49 ?  162  ASP   A HB2  1 
ATOM   3724 H  HB3  A ASP   A 1 162 ? 0.850  -6.834  3.526   0.50 20.66 ?  162  ASP   A HB3  1 
ATOM   3725 H  HB3  B ASP   A 1 162 ? 0.830  -6.784  3.265   0.50 23.49 ?  162  ASP   A HB3  1 
ATOM   3726 N  N    A LYS   A 1 163 ? 3.396  -7.349  1.344   0.50 18.32 ?  163  LYS   A N    1 
ATOM   3727 N  N    B LYS   A 1 163 ? 3.397  -7.366  1.127   0.50 19.61 ?  163  LYS   A N    1 
ATOM   3728 C  CA   A LYS   A 1 163 ? 3.465  -8.118  0.104   0.50 19.02 ?  163  LYS   A CA   1 
ATOM   3729 C  CA   B LYS   A 1 163 ? 3.536  -8.197  -0.065  0.50 20.28 ?  163  LYS   A CA   1 
ATOM   3730 C  C    A LYS   A 1 163 ? 4.552  -9.185  0.166   0.50 18.40 ?  163  LYS   A C    1 
ATOM   3731 C  C    B LYS   A 1 163 ? 4.648  -9.224  0.114   0.50 19.06 ?  163  LYS   A C    1 
ATOM   3732 O  O    A LYS   A 1 163 ? 4.368  -10.293 -0.349  0.50 19.24 ?  163  LYS   A O    1 
ATOM   3733 O  O    B LYS   A 1 163 ? 4.512  -10.380 -0.303  0.50 19.78 ?  163  LYS   A O    1 
ATOM   3734 C  CB   A LYS   A 1 163 ? 3.688  -7.181  -1.083  0.50 21.06 ?  163  LYS   A CB   1 
ATOM   3735 C  CB   B LYS   A 1 163 ? 3.807  -7.305  -1.279  0.50 22.80 ?  163  LYS   A CB   1 
ATOM   3736 C  CG   A LYS   A 1 163 ? 3.655  -7.876  -2.435  0.50 23.21 ?  163  LYS   A CG   1 
ATOM   3737 C  CG   B LYS   A 1 163 ? 3.869  -8.044  -2.605  0.50 25.24 ?  163  LYS   A CG   1 
ATOM   3738 C  CD   A LYS   A 1 163 ? 4.068  -6.935  -3.556  0.50 25.03 ?  163  LYS   A CD   1 
ATOM   3739 C  CD   B LYS   A 1 163 ? 3.666  -7.102  -3.791  0.50 27.57 ?  163  LYS   A CD   1 
ATOM   3740 C  CE   A LYS   A 1 163 ? 3.960  -7.614  -4.914  0.50 26.46 ?  163  LYS   A CE   1 
ATOM   3741 C  CE   B LYS   A 1 163 ? 4.984  -6.598  -4.362  0.50 29.18 ?  163  LYS   A CE   1 
ATOM   3742 N  NZ   A LYS   A 1 163 ? 4.579  -6.806  -5.998  0.50 27.20 ?  163  LYS   A NZ   1 
ATOM   3743 N  NZ   B LYS   A 1 163 ? 4.811  -6.016  -5.725  0.50 30.02 ?  163  LYS   A NZ   1 
ATOM   3744 H  H    A LYS   A 1 163 ? 3.669  -6.536  1.278   0.50 21.99 ?  163  LYS   A H    1 
ATOM   3745 H  H    B LYS   A 1 163 ? 3.622  -6.544  1.016   0.50 23.54 ?  163  LYS   A H    1 
ATOM   3746 H  HA   A LYS   A 1 163 ? 2.619  -8.569  -0.032  0.50 22.83 ?  163  LYS   A HA   1 
ATOM   3747 H  HA   B LYS   A 1 163 ? 2.705  -8.672  -0.224  0.50 24.33 ?  163  LYS   A HA   1 
ATOM   3748 H  HB2  A LYS   A 1 163 ? 2.990  -6.505  -1.083  0.50 25.27 ?  163  LYS   A HB2  1 
ATOM   3749 H  HB2  B LYS   A 1 163 ? 3.098  -6.645  -1.341  0.50 27.36 ?  163  LYS   A HB2  1 
ATOM   3750 H  HB3  A LYS   A 1 163 ? 4.555  -6.756  -0.992  0.50 25.27 ?  163  LYS   A HB3  1 
ATOM   3751 H  HB3  B LYS   A 1 163 ? 4.658  -6.857  -1.154  0.50 27.36 ?  163  LYS   A HB3  1 
ATOM   3752 H  HG2  A LYS   A 1 163 ? 4.270  -8.625  -2.430  0.50 27.85 ?  163  LYS   A HG2  1 
ATOM   3753 H  HG2  B LYS   A 1 163 ? 4.739  -8.465  -2.696  0.50 30.28 ?  163  LYS   A HG2  1 
ATOM   3754 H  HG3  A LYS   A 1 163 ? 2.752  -8.185  -2.614  0.50 27.85 ?  163  LYS   A HG3  1 
ATOM   3755 H  HG3  B LYS   A 1 163 ? 3.169  -8.713  -2.631  0.50 30.28 ?  163  LYS   A HG3  1 
ATOM   3756 H  HD2  A LYS   A 1 163 ? 3.481  -6.160  -3.557  0.50 30.04 ?  163  LYS   A HD2  1 
ATOM   3757 H  HD2  B LYS   A 1 163 ? 3.196  -7.572  -4.495  0.50 33.09 ?  163  LYS   A HD2  1 
ATOM   3758 H  HD3  A LYS   A 1 163 ? 4.987  -6.660  -3.423  0.50 30.04 ?  163  LYS   A HD3  1 
ATOM   3759 H  HD3  B LYS   A 1 163 ? 3.152  -6.328  -3.507  0.50 33.09 ?  163  LYS   A HD3  1 
ATOM   3760 H  HE2  A LYS   A 1 163 ? 4.403  -8.474  -4.883  0.50 31.76 ?  163  LYS   A HE2  1 
ATOM   3761 H  HE2  B LYS   A 1 163 ? 5.340  -5.906  -3.786  0.50 35.02 ?  163  LYS   A HE2  1 
ATOM   3762 H  HE3  A LYS   A 1 163 ? 3.023  -7.736  -5.130  0.50 31.76 ?  163  LYS   A HE3  1 
ATOM   3763 H  HE3  B LYS   A 1 163 ? 5.613  -7.332  -4.421  0.50 35.02 ?  163  LYS   A HE3  1 
ATOM   3764 H  HZ1  A LYS   A 1 163 ? 4.501  -7.230  -6.776  0.50 32.64 ?  163  LYS   A HZ1  1 
ATOM   3765 H  HZ1  B LYS   A 1 163 ? 5.594  -5.732  -6.039  0.50 36.02 ?  163  LYS   A HZ1  1 
ATOM   3766 H  HZ2  A LYS   A 1 163 ? 4.172  -6.016  -6.057  0.50 32.64 ?  163  LYS   A HZ2  1 
ATOM   3767 H  HZ2  B LYS   A 1 163 ? 4.485  -6.631  -6.281  0.50 36.02 ?  163  LYS   A HZ2  1 
ATOM   3768 H  HZ3  A LYS   A 1 163 ? 5.442  -6.674  -5.825  0.50 32.64 ?  163  LYS   A HZ3  1 
ATOM   3769 H  HZ3  B LYS   A 1 163 ? 4.246  -5.329  -5.693  0.50 36.02 ?  163  LYS   A HZ3  1 
ATOM   3770 N  N    A LEU   A 1 164 ? 5.695  -8.870  0.783   0.50 16.87 ?  164  LEU   A N    1 
ATOM   3771 N  N    B LEU   A 1 164 ? 5.754  -8.813  0.737   0.50 17.21 ?  164  LEU   A N    1 
ATOM   3772 C  CA   A LEU   A 1 164 ? 6.777  -9.848  0.880   0.50 16.18 ?  164  LEU   A CA   1 
ATOM   3773 C  CA   B LEU   A 1 164 ? 6.862  -9.727  1.001   0.50 16.05 ?  164  LEU   A CA   1 
ATOM   3774 C  C    A LEU   A 1 164 ? 6.353  -11.041 1.723   0.50 16.19 ?  164  LEU   A C    1 
ATOM   3775 C  C    B LEU   A 1 164 ? 6.422  -10.887 1.879   0.50 15.95 ?  164  LEU   A C    1 
ATOM   3776 O  O    A LEU   A 1 164 ? 6.615  -12.194 1.363   0.50 16.73 ?  164  LEU   A O    1 
ATOM   3777 O  O    B LEU   A 1 164 ? 6.792  -12.041 1.632   0.50 16.34 ?  164  LEU   A O    1 
ATOM   3778 C  CB   A LEU   A 1 164 ? 8.022  -9.189  1.476   0.50 15.76 ?  164  LEU   A CB   1 
ATOM   3779 C  CB   B LEU   A 1 164 ? 7.993  -8.966  1.692   0.50 15.54 ?  164  LEU   A CB   1 
ATOM   3780 C  CG   A LEU   A 1 164 ? 8.714  -8.152  0.590   0.50 15.64 ?  164  LEU   A CG   1 
ATOM   3781 C  CG   B LEU   A 1 164 ? 8.799  -7.980  0.844   0.50 15.75 ?  164  LEU   A CG   1 
ATOM   3782 C  CD1  A LEU   A 1 164 ? 9.674  -7.297  1.403   0.50 15.25 ?  164  LEU   A CD1  1 
ATOM   3783 C  CD1  B LEU   A 1 164 ? 9.619  -7.051  1.731   0.50 15.77 ?  164  LEU   A CD1  1 
ATOM   3784 C  CD2  A LEU   A 1 164 ? 9.442  -8.835  -0.554  0.50 15.79 ?  164  LEU   A CD2  1 
ATOM   3785 C  CD2  B LEU   A 1 164 ? 9.698  -8.719  -0.134  0.50 15.83 ?  164  LEU   A CD2  1 
ATOM   3786 H  H    A LEU   A 1 164 ? 5.866  -8.116  1.156   0.50 20.24 ?  164  LEU   A H    1 
ATOM   3787 H  H    B LEU   A 1 164 ? 5.884  -8.013  1.011   0.50 20.65 ?  164  LEU   A H    1 
ATOM   3788 H  HA   A LEU   A 1 164 ? 7.001  -10.173 -0.004  0.50 19.42 ?  164  LEU   A HA   1 
ATOM   3789 H  HA   B LEU   A 1 164 ? 7.195  -10.087 0.164   0.50 19.26 ?  164  LEU   A HA   1 
ATOM   3790 H  HB2  A LEU   A 1 164 ? 7.771  -8.744  2.298   0.50 18.92 ?  164  LEU   A HB2  1 
ATOM   3791 H  HB2  B LEU   A 1 164 ? 7.609  -8.463  2.427   0.50 18.65 ?  164  LEU   A HB2  1 
ATOM   3792 H  HB3  A LEU   A 1 164 ? 8.676  -9.881  1.669   0.50 18.92 ?  164  LEU   A HB3  1 
ATOM   3793 H  HB3  B LEU   A 1 164 ? 8.619  -9.616  2.045   0.50 18.65 ?  164  LEU   A HB3  1 
ATOM   3794 H  HG   A LEU   A 1 164 ? 8.042  -7.566  0.209   0.50 18.77 ?  164  LEU   A HG   1 
ATOM   3795 H  HG   B LEU   A 1 164 ? 8.185  -7.432  0.332   0.50 18.90 ?  164  LEU   A HG   1 
ATOM   3796 H  HD11 A LEU   A 1 164 ? 10.103 -6.658  0.815   0.50 18.30 ?  164  LEU   A HD11 1 
ATOM   3797 H  HD11 B LEU   A 1 164 ? 10.122 -6.441  1.170   0.50 18.92 ?  164  LEU   A HD11 1 
ATOM   3798 H  HD12 A LEU   A 1 164 ? 9.173  -6.830  2.091   0.50 18.30 ?  164  LEU   A HD12 1 
ATOM   3799 H  HD12 B LEU   A 1 164 ? 9.018  -6.550  2.307   0.50 18.92 ?  164  LEU   A HD12 1 
ATOM   3800 H  HD13 A LEU   A 1 164 ? 10.339 -7.872  1.812   0.50 18.30 ?  164  LEU   A HD13 1 
ATOM   3801 H  HD13 B LEU   A 1 164 ? 10.226 -7.582  2.271   0.50 18.92 ?  164  LEU   A HD13 1 
ATOM   3802 H  HD21 A LEU   A 1 164 ? 9.912  -8.164  -1.075  0.50 18.95 ?  164  LEU   A HD21 1 
ATOM   3803 H  HD21 B LEU   A 1 164 ? 10.215 -8.070  -0.638  0.50 18.99 ?  164  LEU   A HD21 1 
ATOM   3804 H  HD22 A LEU   A 1 164 ? 10.076 -9.473  -0.190  0.50 18.95 ?  164  LEU   A HD22 1 
ATOM   3805 H  HD22 B LEU   A 1 164 ? 10.292 -9.303  0.360   0.50 18.99 ?  164  LEU   A HD22 1 
ATOM   3806 H  HD23 A LEU   A 1 164 ? 8.795  -9.293  -1.113  0.50 18.95 ?  164  LEU   A HD23 1 
ATOM   3807 H  HD23 B LEU   A 1 164 ? 9.146  -9.240  -0.738  0.50 18.99 ?  164  LEU   A HD23 1 
ATOM   3808 N  N    A VAL   A 1 165 ? 5.688  -10.779 2.847   0.50 15.97 ?  165  VAL   A N    1 
ATOM   3809 N  N    B VAL   A 1 165 ? 5.653  -10.596 2.928   0.50 15.67 ?  165  VAL   A N    1 
ATOM   3810 C  CA   A VAL   A 1 165 ? 5.200  -11.855 3.702   0.50 15.82 ?  165  VAL   A CA   1 
ATOM   3811 C  CA   B VAL   A 1 165 ? 5.194  -11.648 3.826   0.50 15.73 ?  165  VAL   A CA   1 
ATOM   3812 C  C    A VAL   A 1 165 ? 4.139  -12.666 2.969   0.50 16.00 ?  165  VAL   A C    1 
ATOM   3813 C  C    B VAL   A 1 165 ? 4.186  -12.551 3.123   0.50 15.77 ?  165  VAL   A C    1 
ATOM   3814 O  O    A VAL   A 1 165 ? 4.246  -13.890 2.833   0.50 15.72 ?  165  VAL   A O    1 
ATOM   3815 O  O    B VAL   A 1 165 ? 4.277  -13.782 3.195   0.50 15.69 ?  165  VAL   A O    1 
ATOM   3816 C  CB   A VAL   A 1 165 ? 4.653  -11.264 5.013   0.50 16.13 ?  165  VAL   A CB   1 
ATOM   3817 C  CB   B VAL   A 1 165 ? 4.626  -11.036 5.121   0.50 16.24 ?  165  VAL   A CB   1 
ATOM   3818 C  CG1  A VAL   A 1 165 ? 3.891  -12.318 5.803   0.50 16.26 ?  165  VAL   A CG1  1 
ATOM   3819 C  CG1  B VAL   A 1 165 ? 3.946  -12.102 5.969   0.50 16.57 ?  165  VAL   A CG1  1 
ATOM   3820 C  CG2  A VAL   A 1 165 ? 5.779  -10.656 5.837   0.50 16.43 ?  165  VAL   A CG2  1 
ATOM   3821 C  CG2  B VAL   A 1 165 ? 5.730  -10.349 5.911   0.50 16.46 ?  165  VAL   A CG2  1 
ATOM   3822 H  H    A VAL   A 1 165 ? 5.494  -9.995  3.129   0.50 19.16 ?  165  VAL   A H    1 
ATOM   3823 H  H    B VAL   A 1 165 ? 5.395  -9.803  3.144   0.50 18.80 ?  165  VAL   A H    1 
ATOM   3824 H  HA   A VAL   A 1 165 ? 5.936  -12.451 3.926   0.50 18.98 ?  165  VAL   A HA   1 
ATOM   3825 H  HA   B VAL   A 1 165 ? 5.953  -12.195 4.077   0.50 18.88 ?  165  VAL   A HA   1 
ATOM   3826 H  HB   A VAL   A 1 165 ? 4.033  -10.553 4.796   0.50 19.36 ?  165  VAL   A HB   1 
ATOM   3827 H  HB   B VAL   A 1 165 ? 3.963  -10.364 4.896   0.50 19.48 ?  165  VAL   A HB   1 
ATOM   3828 H  HG11 A VAL   A 1 165 ? 3.806  -12.020 6.722   0.50 19.51 ?  165  VAL   A HG11 1 
ATOM   3829 H  HG11 B VAL   A 1 165 ? 3.833  -11.762 6.872   0.50 19.88 ?  165  VAL   A HG11 1 
ATOM   3830 H  HG12 A VAL   A 1 165 ? 3.008  -12.428 5.412   0.50 19.51 ?  165  VAL   A HG12 1 
ATOM   3831 H  HG12 B VAL   A 1 165 ? 3.079  -12.306 5.586   0.50 19.88 ?  165  VAL   A HG12 1 
ATOM   3832 H  HG13 A VAL   A 1 165 ? 4.378  -13.153 5.769   0.50 19.51 ?  165  VAL   A HG13 1 
ATOM   3833 H  HG13 B VAL   A 1 165 ? 4.501  -12.895 5.983   0.50 19.88 ?  165  VAL   A HG13 1 
ATOM   3834 H  HG21 A VAL   A 1 165 ? 5.413  -10.297 6.660   0.50 19.72 ?  165  VAL   A HG21 1 
ATOM   3835 H  HG21 B VAL   A 1 165 ? 5.349  -9.932  6.701   0.50 19.75 ?  165  VAL   A HG21 1 
ATOM   3836 H  HG22 A VAL   A 1 165 ? 6.433  -11.344 6.038   0.50 19.72 ?  165  VAL   A HG22 1 
ATOM   3837 H  HG22 B VAL   A 1 165 ? 6.390  -11.010 6.175   0.50 19.75 ?  165  VAL   A HG22 1 
ATOM   3838 H  HG23 A VAL   A 1 165 ? 6.197  -9.945  5.324   0.50 19.72 ?  165  VAL   A HG23 1 
ATOM   3839 H  HG23 B VAL   A 1 165 ? 6.148  -9.673  5.353   0.50 19.75 ?  165  VAL   A HG23 1 
ATOM   3840 N  N    A SER   A 1 166 ? 3.100  -11.986 2.478   0.50 16.93 ?  166  SER   A N    1 
ATOM   3841 N  N    B SER   A 1 166 ? 3.220  -11.955 2.417   0.50 16.06 ?  166  SER   A N    1 
ATOM   3842 C  CA   A SER   A 1 166 ? 1.976  -12.673 1.854   0.50 17.70 ?  166  SER   A CA   1 
ATOM   3843 C  CA   B SER   A 1 166 ? 2.092  -12.741 1.924   0.50 16.70 ?  166  SER   A CA   1 
ATOM   3844 C  C    A SER   A 1 166 ? 2.380  -13.403 0.588   0.50 17.66 ?  166  SER   A C    1 
ATOM   3845 C  C    B SER   A 1 166 ? 2.507  -13.751 0.854   0.50 16.91 ?  166  SER   A C    1 
ATOM   3846 O  O    A SER   A 1 166 ? 1.689  -14.346 0.185   0.50 18.23 ?  166  SER   A O    1 
ATOM   3847 O  O    B SER   A 1 166 ? 1.906  -14.827 0.762   0.50 17.13 ?  166  SER   A O    1 
ATOM   3848 C  CB   A SER   A 1 166 ? 0.878  -11.677 1.489   0.50 18.81 ?  166  SER   A CB   1 
ATOM   3849 C  CB   B SER   A 1 166 ? 0.949  -11.827 1.458   0.50 17.71 ?  166  SER   A CB   1 
ATOM   3850 O  OG   A SER   A 1 166 ? 0.334  -11.059 2.638   0.50 19.51 ?  166  SER   A OG   1 
ATOM   3851 O  OG   B SER   A 1 166 ? 1.303  -10.997 0.372   0.50 18.48 ?  166  SER   A OG   1 
ATOM   3852 H  H    A SER   A 1 166 ? 3.033  -11.134 2.486   0.50 20.31 ?  166  SER   A H    1 
ATOM   3853 H  H    B SER   A 1 166 ? 3.196  -11.120 2.219   0.50 19.27 ?  166  SER   A H    1 
ATOM   3854 H  HA   A SER   A 1 166 ? 1.609  -13.320 2.481   0.50 21.24 ?  166  SER   A HA   1 
ATOM   3855 H  HA   B SER   A 1 166 ? 1.742  -13.255 2.663   0.50 20.04 ?  166  SER   A HA   1 
ATOM   3856 H  HB2  A SER   A 1 166 ? 1.256  -11.003 0.905   0.50 22.57 ?  166  SER   A HB2  1 
ATOM   3857 H  HB2  B SER   A 1 166 ? 0.203  -12.375 1.175   0.50 21.25 ?  166  SER   A HB2  1 
ATOM   3858 H  HB3  A SER   A 1 166 ? 0.169  -12.154 1.027   0.50 22.57 ?  166  SER   A HB3  1 
ATOM   3859 H  HB3  B SER   A 1 166 ? 0.676  -11.265 2.204   0.50 21.25 ?  166  SER   A HB3  1 
ATOM   3860 H  HG   A SER   A 1 166 ? -0.255 -10.511 2.411   0.50 23.41 ?  166  SER   A HG   1 
ATOM   3861 H  HG   B SER   A 1 166 ? 0.661  -10.498 0.158   0.50 22.17 ?  166  SER   A HG   1 
ATOM   3862 N  N    A SER   A 1 167 ? 3.453  -12.971 -0.069  0.50 16.81 ?  167  SER   A N    1 
ATOM   3863 N  N    B SER   A 1 167 ? 3.548  -13.457 0.076   0.50 16.76 ?  167  SER   A N    1 
ATOM   3864 C  CA   A SER   A 1 167 ? 3.948  -13.646 -1.257  0.50 16.70 ?  167  SER   A CA   1 
ATOM   3865 C  CA   B SER   A 1 167 ? 3.919  -14.280 -1.069  0.50 16.74 ?  167  SER   A CA   1 
ATOM   3866 C  C    A SER   A 1 167 ? 5.125  -14.567 -0.973  0.50 16.74 ?  167  SER   A C    1 
ATOM   3867 C  C    B SER   A 1 167 ? 5.042  -15.269 -0.764  0.50 16.33 ?  167  SER   A C    1 
ATOM   3868 O  O    A SER   A 1 167 ? 5.663  -15.159 -1.914  0.50 17.31 ?  167  SER   A O    1 
ATOM   3869 O  O    B SER   A 1 167 ? 5.596  -15.859 -1.695  0.50 16.96 ?  167  SER   A O    1 
ATOM   3870 C  CB   A SER   A 1 167 ? 4.350  -12.625 -2.329  0.50 16.86 ?  167  SER   A CB   1 
ATOM   3871 C  CB   B SER   A 1 167 ? 4.313  -13.390 -2.252  0.50 17.41 ?  167  SER   A CB   1 
ATOM   3872 O  OG   A SER   A 1 167 ? 5.416  -11.805 -1.881  0.50 16.85 ?  167  SER   A OG   1 
ATOM   3873 O  OG   B SER   A 1 167 ? 5.525  -12.694 -2.002  0.50 17.71 ?  167  SER   A OG   1 
ATOM   3874 H  H    A SER   A 1 167 ? 3.900  -12.268 0.150   0.50 20.17 ?  167  SER   A H    1 
ATOM   3875 H  H    B SER   A 1 167 ? 4.070  -12.787 0.202   0.50 20.11 ?  167  SER   A H    1 
ATOM   3876 H  HA   A SER   A 1 167 ? 3.230  -14.185 -1.622  0.50 20.04 ?  167  SER   A HA   1 
ATOM   3877 H  HA   B SER   A 1 167 ? 3.152  -14.800 -1.342  0.50 20.09 ?  167  SER   A HA   1 
ATOM   3878 H  HB2  A SER   A 1 167 ? 4.631  -13.107 -3.125  0.50 20.24 ?  167  SER   A HB2  1 
ATOM   3879 H  HB2  B SER   A 1 167 ? 4.425  -13.944 -3.042  0.50 20.89 ?  167  SER   A HB2  1 
ATOM   3880 H  HB3  A SER   A 1 167 ? 3.582  -12.070 -2.535  0.50 20.24 ?  167  SER   A HB3  1 
ATOM   3881 H  HB3  B SER   A 1 167 ? 3.607  -12.741 -2.404  0.50 20.89 ?  167  SER   A HB3  1 
ATOM   3882 H  HG   A SER   A 1 167 ? 5.220  -11.473 -1.134  0.50 20.23 ?  167  SER   A HG   1 
ATOM   3883 H  HG   B SER   A 1 167 ? 5.446  -12.211 -1.322  0.50 21.25 ?  167  SER   A HG   1 
ATOM   3884 N  N    A PHE   A 1 168 ? 5.545  -14.707 0.284   0.50 16.33 ?  168  PHE   A N    1 
ATOM   3885 N  N    B PHE   A 1 168 ? 5.355  -15.504 0.510   0.50 15.47 ?  168  PHE   A N    1 
ATOM   3886 C  CA   A PHE   A 1 168 ? 6.718  -15.525 0.566   0.50 17.04 ?  168  PHE   A CA   1 
ATOM   3887 C  CA   B PHE   A 1 168 ? 6.617  -16.160 0.847   0.50 15.42 ?  168  PHE   A CA   1 
ATOM   3888 C  C    A PHE   A 1 168 ? 6.378  -17.002 0.447   0.50 18.89 ?  168  PHE   A C    1 
ATOM   3889 C  C    B PHE   A 1 168 ? 6.552  -17.682 0.741   0.50 16.67 ?  168  PHE   A C    1 
ATOM   3890 O  O    A PHE   A 1 168 ? 5.367  -17.465 0.984   0.50 19.71 ?  168  PHE   A O    1 
ATOM   3891 O  O    B PHE   A 1 168 ? 7.434  -18.299 0.130   0.50 16.91 ?  168  PHE   A O    1 
ATOM   3892 C  CB   A PHE   A 1 168 ? 7.284  -15.248 1.956   0.50 15.83 ?  168  PHE   A CB   1 
ATOM   3893 C  CB   B PHE   A 1 168 ? 7.087  -15.743 2.239   0.50 15.48 ?  168  PHE   A CB   1 
ATOM   3894 C  CG   A PHE   A 1 168 ? 8.514  -16.061 2.263   0.50 15.03 ?  168  PHE   A CG   1 
ATOM   3895 C  CG   B PHE   A 1 168 ? 8.439  -16.280 2.588   0.50 16.01 ?  168  PHE   A CG   1 
ATOM   3896 C  CD1  A PHE   A 1 168 ? 9.710  -15.784 1.625   0.50 14.89 ?  168  PHE   A CD1  1 
ATOM   3897 C  CD1  B PHE   A 1 168 ? 9.568  -15.775 1.973   0.50 16.52 ?  168  PHE   A CD1  1 
ATOM   3898 C  CD2  A PHE   A 1 168 ? 8.470  -17.123 3.154   0.50 14.51 ?  168  PHE   A CD2  1 
ATOM   3899 C  CD2  B PHE   A 1 168 ? 8.583  -17.305 3.505   0.50 15.98 ?  168  PHE   A CD2  1 
ATOM   3900 C  CE1  A PHE   A 1 168 ? 10.843 -16.533 1.883   0.50 14.17 ?  168  PHE   A CE1  1 
ATOM   3901 C  CE1  B PHE   A 1 168 ? 10.818 -16.270 2.275   0.50 16.56 ?  168  PHE   A CE1  1 
ATOM   3902 C  CE2  A PHE   A 1 168 ? 9.605  -17.874 3.417   0.50 14.20 ?  168  PHE   A CE2  1 
ATOM   3903 C  CE2  B PHE   A 1 168 ? 9.834  -17.803 3.812   0.50 16.24 ?  168  PHE   A CE2  1 
ATOM   3904 C  CZ   A PHE   A 1 168 ? 10.793 -17.573 2.780   0.50 14.13 ?  168  PHE   A CZ   1 
ATOM   3905 C  CZ   B PHE   A 1 168 ? 10.951 -17.285 3.195   0.50 16.46 ?  168  PHE   A CZ   1 
ATOM   3906 H  H    A PHE   A 1 168 ? 5.178  -14.347 0.976   0.50 19.60 ?  168  PHE   A H    1 
ATOM   3907 H  H    B PHE   A 1 168 ? 4.862  -15.304 1.183   0.50 18.57 ?  168  PHE   A H    1 
ATOM   3908 H  HA   A PHE   A 1 168 ? 7.404  -15.324 -0.084  0.50 20.44 ?  168  PHE   A HA   1 
ATOM   3909 H  HA   B PHE   A 1 168 ? 7.291  -15.863 0.218   0.50 18.50 ?  168  PHE   A HA   1 
ATOM   3910 H  HB2  A PHE   A 1 168 ? 7.523  -14.310 2.016   0.50 19.00 ?  168  PHE   A HB2  1 
ATOM   3911 H  HB2  B PHE   A 1 168 ? 7.134  -14.775 2.277   0.50 18.58 ?  168  PHE   A HB2  1 
ATOM   3912 H  HB3  A PHE   A 1 168 ? 6.607  -15.458 2.621   0.50 19.00 ?  168  PHE   A HB3  1 
ATOM   3913 H  HB3  B PHE   A 1 168 ? 6.458  -16.072 2.898   0.50 18.58 ?  168  PHE   A HB3  1 
ATOM   3914 H  HD1  A PHE   A 1 168 ? 9.754  -15.079 1.020   0.50 17.87 ?  168  PHE   A HD1  1 
ATOM   3915 H  HD1  B PHE   A 1 168 ? 9.485  -15.090 1.349   0.50 19.82 ?  168  PHE   A HD1  1 
ATOM   3916 H  HD2  A PHE   A 1 168 ? 7.671  -17.327 3.587   0.50 17.41 ?  168  PHE   A HD2  1 
ATOM   3917 H  HD2  B PHE   A 1 168 ? 7.830  -17.657 3.923   0.50 19.18 ?  168  PHE   A HD2  1 
ATOM   3918 H  HE1  A PHE   A 1 168 ? 11.642 -16.332 1.453   0.50 17.01 ?  168  PHE   A HE1  1 
ATOM   3919 H  HE1  B PHE   A 1 168 ? 11.571 -15.919 1.858   0.50 19.88 ?  168  PHE   A HE1  1 
ATOM   3920 H  HE2  A PHE   A 1 168 ? 9.564  -18.582 4.021   0.50 17.04 ?  168  PHE   A HE2  1 
ATOM   3921 H  HE2  B PHE   A 1 168 ? 9.918  -18.489 4.435   0.50 19.49 ?  168  PHE   A HE2  1 
ATOM   3922 H  HZ   A PHE   A 1 168 ? 11.554 -18.081 2.952   0.50 16.95 ?  168  PHE   A HZ   1 
ATOM   3923 H  HZ   B PHE   A 1 168 ? 11.793 -17.619 3.402   0.50 19.75 ?  168  PHE   A HZ   1 
ATOM   3924 N  N    A LEU   A 1 169 ? 7.241  -17.744 -0.240  0.50 20.13 ?  169  LEU   A N    1 
ATOM   3925 N  N    B LEU   A 1 169 ? 5.562  -18.314 1.363   0.50 18.02 ?  169  LEU   A N    1 
ATOM   3926 C  CA   A LEU   A 1 169 ? 7.061  -19.182 -0.383  0.50 21.33 ?  169  LEU   A CA   1 
ATOM   3927 C  CA   B LEU   A 1 169 ? 5.555  -19.778 1.435   0.50 19.91 ?  169  LEU   A CA   1 
ATOM   3928 C  C    A LEU   A 1 169 ? 7.920  -19.929 0.633   0.50 21.43 ?  169  LEU   A C    1 
ATOM   3929 C  C    B LEU   A 1 169 ? 4.972  -20.444 0.191   0.50 21.25 ?  169  LEU   A C    1 
ATOM   3930 O  O    A LEU   A 1 169 ? 7.406  -20.375 1.659   0.50 21.88 ?  169  LEU   A O    1 
ATOM   3931 O  O    B LEU   A 1 169 ? 5.431  -21.517 -0.210  0.50 22.33 ?  169  LEU   A O    1 
ATOM   3932 C  CB   A LEU   A 1 169 ? 7.385  -19.628 -1.814  0.50 22.12 ?  169  LEU   A CB   1 
ATOM   3933 C  CB   B LEU   A 1 169 ? 4.809  -20.264 2.681   0.50 20.28 ?  169  LEU   A CB   1 
ATOM   3934 C  CG   A LEU   A 1 169 ? 7.076  -21.086 -2.168  0.50 22.64 ?  169  LEU   A CG   1 
ATOM   3935 C  CG   B LEU   A 1 169 ? 4.957  -21.763 2.959   0.50 20.55 ?  169  LEU   A CG   1 
ATOM   3936 C  CD1  A LEU   A 1 169 ? 5.650  -21.451 -1.789  0.50 22.91 ?  169  LEU   A CD1  1 
ATOM   3937 C  CD1  B LEU   A 1 169 ? 6.426  -22.127 3.119   0.50 21.17 ?  169  LEU   A CD1  1 
ATOM   3938 C  CD2  A LEU   A 1 169 ? 7.312  -21.343 -3.652  0.50 22.64 ?  169  LEU   A CD2  1 
ATOM   3939 C  CD2  B LEU   A 1 169 ? 4.161  -22.173 4.187   0.50 20.70 ?  169  LEU   A CD2  1 
ATOM   3940 O  OXT  A LEU   A 1 169 ? 9.131  -20.099 0.475   0.50 21.03 -1 169  LEU   A OXT  1 
ATOM   3941 O  OXT  B LEU   A 1 169 ? 4.038  -19.941 -0.433  0.50 21.56 -1 169  LEU   A OXT  1 
ATOM   3942 H  H    A LEU   A 1 169 ? 7.945  -17.440 -0.630  0.50 24.15 ?  169  LEU   A H    1 
ATOM   3943 H  H    B LEU   A 1 169 ? 4.901  -17.930 1.754   0.50 21.62 ?  169  LEU   A H    1 
ATOM   3944 H  HA   A LEU   A 1 169 ? 6.141  -19.404 -0.199  0.50 25.59 ?  169  LEU   A HA   1 
ATOM   3945 H  HA   B LEU   A 1 169 ? 6.474  -20.072 1.507   0.50 23.89 ?  169  LEU   A HA   1 
ATOM   3946 H  HB2  A LEU   A 1 169 ? 6.872  -19.075 -2.422  0.50 26.55 ?  169  LEU   A HB2  1 
ATOM   3947 H  HB2  B LEU   A 1 169 ? 5.148  -19.787 3.455   0.50 24.34 ?  169  LEU   A HB2  1 
ATOM   3948 H  HB3  A LEU   A 1 169 ? 8.330  -19.492 -1.972  0.50 26.55 ?  169  LEU   A HB3  1 
ATOM   3949 H  HB3  B LEU   A 1 169 ? 3.863  -20.080 2.571   0.50 24.34 ?  169  LEU   A HB3  1 
ATOM   3950 H  HG   A LEU   A 1 169 ? 7.674  -21.667 -1.672  0.50 27.17 ?  169  LEU   A HG   1 
ATOM   3951 H  HG   B LEU   A 1 169 ? 4.612  -22.259 2.201   0.50 24.65 ?  169  LEU   A HG   1 
ATOM   3952 H  HD11 A LEU   A 1 169 ? 5.424  -22.306 -2.190  0.50 27.49 ?  169  LEU   A HD11 1 
ATOM   3953 H  HD11 B LEU   A 1 169 ? 6.491  -22.995 3.541   0.50 25.40 ?  169  LEU   A HD11 1 
ATOM   3954 H  HD12 A LEU   A 1 169 ? 5.585  -21.514 -0.823  0.50 27.49 ?  169  LEU   A HD12 1 
ATOM   3955 H  HD12 B LEU   A 1 169 ? 6.844  -22.154 2.242   0.50 25.40 ?  169  LEU   A HD12 1 
ATOM   3956 H  HD13 A LEU   A 1 169 ? 5.049  -20.764 -2.119  0.50 27.49 ?  169  LEU   A HD13 1 
ATOM   3957 H  HD13 B LEU   A 1 169 ? 6.859  -21.456 3.670   0.50 25.40 ?  169  LEU   A HD13 1 
ATOM   3958 H  HD21 A LEU   A 1 169 ? 7.115  -22.273 -3.849  0.50 27.16 ?  169  LEU   A HD21 1 
ATOM   3959 H  HD21 B LEU   A 1 169 ? 4.272  -23.125 4.329   0.50 24.84 ?  169  LEU   A HD21 1 
ATOM   3960 H  HD22 A LEU   A 1 169 ? 6.726  -20.766 -4.168  0.50 27.16 ?  169  LEU   A HD22 1 
ATOM   3961 H  HD22 B LEU   A 1 169 ? 4.496  -21.682 4.955   0.50 24.84 ?  169  LEU   A HD22 1 
ATOM   3962 H  HD23 A LEU   A 1 169 ? 8.238  -21.149 -3.863  0.50 27.16 ?  169  LEU   A HD23 1 
ATOM   3963 H  HD23 B LEU   A 1 169 ? 3.228  -21.963 4.039   0.50 24.84 ?  169  LEU   A HD23 1 
ATOM   3964 N  N    A SER   B 1 1   ? 50.729 -9.192  -23.727 0.50 28.61 ?  1    SER   B N    1 
ATOM   3965 N  N    B SER   B 1 1   ? 50.840 -9.305  -23.854 0.50 23.75 ?  1    SER   B N    1 
ATOM   3966 C  CA   A SER   B 1 1   ? 51.251 -10.262 -22.852 0.50 28.24 ?  1    SER   B CA   1 
ATOM   3967 C  CA   B SER   B 1 1   ? 51.242 -10.246 -22.789 0.50 23.72 ?  1    SER   B CA   1 
ATOM   3968 C  C    A SER   B 1 1   ? 50.194 -11.329 -22.609 0.50 26.97 ?  1    SER   B C    1 
ATOM   3969 C  C    B SER   B 1 1   ? 50.141 -11.257 -22.503 0.50 22.94 ?  1    SER   B C    1 
ATOM   3970 O  O    A SER   B 1 1   ? 49.000 -11.130 -22.868 0.50 26.52 ?  1    SER   B O    1 
ATOM   3971 O  O    B SER   B 1 1   ? 48.971 -11.079 -22.876 0.50 22.31 ?  1    SER   B O    1 
ATOM   3972 C  CB   A SER   B 1 1   ? 51.718 -9.688  -21.518 0.50 28.97 ?  1    SER   B CB   1 
ATOM   3973 C  CB   B SER   B 1 1   ? 51.606 -9.499  -21.509 0.50 24.34 ?  1    SER   B CB   1 
ATOM   3974 O  OG   A SER   B 1 1   ? 50.613 -9.283  -20.733 0.50 30.24 ?  1    SER   B OG   1 
ATOM   3975 O  OG   B SER   B 1 1   ? 50.565 -9.600  -20.555 0.50 25.70 ?  1    SER   B OG   1 
ATOM   3976 H  H1   A SER   B 1 1   ? 50.522 -9.540  -24.517 0.50 34.33 ?  1    SER   B H1   1 
ATOM   3977 H  H1   B SER   B 1 1   ? 51.501 -8.729  -23.992 0.50 28.50 ?  1    SER   B H1   1 
ATOM   3978 H  H2   A SER   B 1 1   ? 50.008 -8.838  -23.353 0.50 34.33 ?  1    SER   B H2   1 
ATOM   3979 H  H2   B SER   B 1 1   ? 50.677 -9.763  -24.597 0.50 28.50 ?  1    SER   B H2   1 
ATOM   3980 H  H3   A SER   B 1 1   ? 51.356 -8.571  -23.826 0.50 34.33 ?  1    SER   B H3   1 
ATOM   3981 H  H3   B SER   B 1 1   ? 50.110 -8.874  -23.597 0.50 28.50 ?  1    SER   B H3   1 
ATOM   3982 H  HA   A SER   B 1 1   ? 52.006 -10.673 -23.292 0.50 33.88 ?  1    SER   B HA   1 
ATOM   3983 H  HA   B SER   B 1 1   ? 52.025 -10.726 -23.092 0.50 28.46 ?  1    SER   B HA   1 
ATOM   3984 H  HB2  A SER   B 1 1   ? 52.218 -10.372 -21.047 0.50 34.77 ?  1    SER   B HB2  1 
ATOM   3985 H  HB2  B SER   B 1 1   ? 52.414 -9.887  -21.142 0.50 29.20 ?  1    SER   B HB2  1 
ATOM   3986 H  HB3  A SER   B 1 1   ? 52.281 -8.917  -21.684 0.50 34.77 ?  1    SER   B HB3  1 
ATOM   3987 H  HB3  B SER   B 1 1   ? 51.754 -8.563  -21.720 0.50 29.20 ?  1    SER   B HB3  1 
ATOM   3988 H  HG   A SER   B 1 1   ? 50.878 -8.806  -20.096 0.50 36.28 ?  1    SER   B HG   1 
ATOM   3989 H  HG   B SER   B 1 1   ? 50.588 -8.936  -20.041 0.50 30.84 ?  1    SER   B HG   1 
ATOM   3990 N  N    A MET   B 1 2   ? 50.653 -12.463 -22.098 0.50 26.16 ?  2    MET   B N    1 
ATOM   3991 N  N    B MET   B 1 2   ? 50.541 -12.320 -21.818 0.50 22.88 ?  2    MET   B N    1 
ATOM   3992 C  CA   A MET   B 1 2   ? 49.833 -13.654 -21.925 0.50 25.82 ?  2    MET   B CA   1 
ATOM   3993 C  CA   B MET   B 1 2   ? 49.724 -13.510 -21.625 0.50 23.19 ?  2    MET   B CA   1 
ATOM   3994 C  C    A MET   B 1 2   ? 49.607 -13.874 -20.436 0.50 22.99 ?  2    MET   B C    1 
ATOM   3995 C  C    B MET   B 1 2   ? 49.460 -13.656 -20.133 0.50 20.84 ?  2    MET   B C    1 
ATOM   3996 O  O    A MET   B 1 2   ? 50.551 -14.159 -19.695 0.50 22.85 ?  2    MET   B O    1 
ATOM   3997 O  O    B MET   B 1 2   ? 50.373 -13.987 -19.368 0.50 20.99 ?  2    MET   B O    1 
ATOM   3998 C  CB   A MET   B 1 2   ? 50.540 -14.849 -22.548 0.50 29.01 ?  2    MET   B CB   1 
ATOM   3999 C  CB   B MET   B 1 2   ? 50.486 -14.717 -22.166 0.50 26.64 ?  2    MET   B CB   1 
ATOM   4000 C  CG   A MET   B 1 2   ? 49.682 -16.097 -22.650 0.50 31.97 ?  2    MET   B CG   1 
ATOM   4001 C  CG   B MET   B 1 2   ? 49.633 -15.871 -22.661 0.50 29.52 ?  2    MET   B CG   1 
ATOM   4002 S  SD   A MET   B 1 2   ? 50.492 -17.389 -23.610 0.50 34.59 ?  2    MET   B SD   1 
ATOM   4003 S  SD   B MET   B 1 2   ? 50.581 -16.967 -23.728 0.50 31.98 ?  2    MET   B SD   1 
ATOM   4004 C  CE   A MET   B 1 2   ? 51.082 -16.403 -24.984 0.50 34.87 ?  2    MET   B CE   1 
ATOM   4005 C  CE   B MET   B 1 2   ? 51.419 -15.775 -24.754 0.50 32.29 ?  2    MET   B CE   1 
ATOM   4006 H  H    A MET   B 1 2   ? 51.467 -12.570 -21.839 0.50 31.39 ?  2    MET   B H    1 
ATOM   4007 H  H    B MET   B 1 2   ? 51.314 -12.387 -21.440 0.50 27.45 ?  2    MET   B H    1 
ATOM   4008 H  HA   A MET   B 1 2   ? 48.983 -13.535 -22.373 0.50 30.98 ?  2    MET   B HA   1 
ATOM   4009 H  HA   B MET   B 1 2   ? 48.891 -13.433 -22.111 0.50 27.83 ?  2    MET   B HA   1 
ATOM   4010 H  HB2  A MET   B 1 2   ? 50.815 -14.575 -23.432 0.50 34.81 ?  2    MET   B HB2  1 
ATOM   4011 H  HB2  B MET   B 1 2   ? 51.036 -14.388 -22.889 0.50 31.97 ?  2    MET   B HB2  1 
ATOM   4012 H  HB3  A MET   B 1 2   ? 51.319 -15.077 -22.018 0.50 34.81 ?  2    MET   B HB3  1 
ATOM   4013 H  HB3  B MET   B 1 2   ? 51.055 -15.081 -21.478 0.50 31.97 ?  2    MET   B HB3  1 
ATOM   4014 H  HG2  A MET   B 1 2   ? 49.510 -16.435 -21.755 0.50 38.37 ?  2    MET   B HG2  1 
ATOM   4015 H  HG2  B MET   B 1 2   ? 49.317 -16.385 -21.898 0.50 35.42 ?  2    MET   B HG2  1 
ATOM   4016 H  HG3  A MET   B 1 2   ? 48.849 -15.878 -23.094 0.50 38.37 ?  2    MET   B HG3  1 
ATOM   4017 H  HG3  B MET   B 1 2   ? 48.886 -15.542 -23.174 0.50 35.42 ?  2    MET   B HG3  1 
ATOM   4018 H  HE1  A MET   B 1 2   ? 51.262 -16.987 -25.723 0.50 41.84 ?  2    MET   B HE1  1 
ATOM   4019 H  HE1  B MET   B 1 2   ? 51.639 -16.201 -25.580 0.50 38.75 ?  2    MET   B HE1  1 
ATOM   4020 H  HE2  A MET   B 1 2   ? 50.389 -15.762 -25.222 0.50 41.84 ?  2    MET   B HE2  1 
ATOM   4021 H  HE2  B MET   B 1 2   ? 50.821 -15.025 -24.912 0.50 38.75 ?  2    MET   B HE2  1 
ATOM   4022 H  HE3  A MET   B 1 2   ? 51.892 -15.926 -24.727 0.50 41.84 ?  2    MET   B HE3  1 
ATOM   4023 H  HE3  B MET   B 1 2   ? 52.227 -15.469 -24.302 0.50 38.75 ?  2    MET   B HE3  1 
ATOM   4024 N  N    A VAL   B 1 3   ? 48.355 -13.737 -20.005 0.50 20.53 ?  3    VAL   B N    1 
ATOM   4025 N  N    B VAL   B 1 3   ? 48.226 -13.382 -19.716 0.50 18.78 ?  3    VAL   B N    1 
ATOM   4026 C  CA   A VAL   B 1 3   ? 47.961 -13.976 -18.625 0.50 18.96 ?  3    VAL   B CA   1 
ATOM   4027 C  CA   B VAL   B 1 3   ? 47.776 -13.649 -18.355 0.50 17.92 ?  3    VAL   B CA   1 
ATOM   4028 C  C    A VAL   B 1 3   ? 46.721 -14.860 -18.636 0.50 16.90 ?  3    VAL   B C    1 
ATOM   4029 C  C    B VAL   B 1 3   ? 46.533 -14.523 -18.420 0.50 16.60 ?  3    VAL   B C    1 
ATOM   4030 O  O    A VAL   B 1 3   ? 46.032 -14.992 -19.652 0.50 16.41 ?  3    VAL   B O    1 
ATOM   4031 O  O    B VAL   B 1 3   ? 45.707 -14.383 -19.326 0.50 16.76 ?  3    VAL   B O    1 
ATOM   4032 C  CB   A VAL   B 1 3   ? 47.667 -12.665 -17.866 0.50 20.22 ?  3    VAL   B CB   1 
ATOM   4033 C  CB   B VAL   B 1 3   ? 47.528 -12.365 -17.527 0.50 18.83 ?  3    VAL   B CB   1 
ATOM   4034 C  CG1  A VAL   B 1 3   ? 48.916 -11.797 -17.785 0.50 20.76 ?  3    VAL   B CG1  1 
ATOM   4035 C  CG1  B VAL   B 1 3   ? 48.815 -11.551 -17.412 0.50 19.41 ?  3    VAL   B CG1  1 
ATOM   4036 C  CG2  A VAL   B 1 3   ? 46.522 -11.916 -18.536 0.50 20.75 ?  3    VAL   B CG2  1 
ATOM   4037 C  CG2  B VAL   B 1 3   ? 46.404 -11.526 -18.121 0.50 18.84 ?  3    VAL   B CG2  1 
ATOM   4038 H  H    A VAL   B 1 3   ? 47.705 -13.497 -20.512 0.50 24.63 ?  3    VAL   B H    1 
ATOM   4039 H  H    B VAL   B 1 3   ? 47.620 -13.034 -20.220 0.50 22.54 ?  3    VAL   B H    1 
ATOM   4040 H  HA   A VAL   B 1 3   ? 48.682 -14.443 -18.165 0.50 22.76 ?  3    VAL   B HA   1 
ATOM   4041 H  HA   B VAL   B 1 3   ? 48.454 -14.154 -17.898 0.50 21.50 ?  3    VAL   B HA   1 
ATOM   4042 H  HB   A VAL   B 1 3   ? 47.395 -12.887 -16.961 0.50 24.27 ?  3    VAL   B HB   1 
ATOM   4043 H  HB   B VAL   B 1 3   ? 47.262 -12.617 -16.628 0.50 22.60 ?  3    VAL   B HB   1 
ATOM   4044 H  HG11 A VAL   B 1 3   ? 48.704 -10.991 -17.289 0.50 24.91 ?  3    VAL   B HG11 1 
ATOM   4045 H  HG11 B VAL   B 1 3   ? 48.648 -10.766 -16.866 0.50 23.30 ?  3    VAL   B HG11 1 
ATOM   4046 H  HG12 A VAL   B 1 3   ? 49.615 -12.292 -17.329 0.50 24.91 ?  3    VAL   B HG12 1 
ATOM   4047 H  HG12 B VAL   B 1 3   ? 49.500 -12.101 -17.000 0.50 23.30 ?  3    VAL   B HG12 1 
ATOM   4048 H  HG13 A VAL   B 1 3   ? 49.201 -11.570 -18.683 0.50 24.91 ?  3    VAL   B HG13 1 
ATOM   4049 H  HG13 B VAL   B 1 3   ? 49.099 -11.281 -18.300 0.50 23.30 ?  3    VAL   B HG13 1 
ATOM   4050 H  HG21 A VAL   B 1 3   ? 46.450 -11.036 -18.139 0.50 24.90 ?  3    VAL   B HG21 1 
ATOM   4051 H  HG21 B VAL   B 1 3   ? 46.368 -10.672 -17.659 0.50 22.61 ?  3    VAL   B HG21 1 
ATOM   4052 H  HG22 A VAL   B 1 3   ? 46.708 -11.837 -19.485 0.50 24.90 ?  3    VAL   B HG22 1 
ATOM   4053 H  HG22 B VAL   B 1 3   ? 46.579 -11.385 -19.063 0.50 22.61 ?  3    VAL   B HG22 1 
ATOM   4054 H  HG23 A VAL   B 1 3   ? 45.696 -12.409 -18.402 0.50 24.90 ?  3    VAL   B HG23 1 
ATOM   4055 H  HG23 B VAL   B 1 3   ? 45.563 -11.997 -18.006 0.50 22.61 ?  3    VAL   B HG23 1 
ATOM   4056 N  N    . ASN   B 1 4   ? 46.433 -15.455 -17.477 1.00 15.69 ?  4    ASN   B N    1 
ATOM   4057 C  CA   . ASN   B 1 4   ? 45.296 -16.370 -17.363 1.00 14.71 ?  4    ASN   B CA   1 
ATOM   4058 C  C    . ASN   B 1 4   ? 45.249 -17.338 -18.542 1.00 14.70 ?  4    ASN   B C    1 
ATOM   4059 O  O    . ASN   B 1 4   ? 44.185 -17.600 -19.099 1.00 15.59 ?  4    ASN   B O    1 
ATOM   4060 C  CB   . ASN   B 1 4   ? 43.968 -15.621 -17.197 1.00 13.85 ?  4    ASN   B CB   1 
ATOM   4061 C  CG   . ASN   B 1 4   ? 43.913 -14.806 -15.917 1.00 13.07 ?  4    ASN   B CG   1 
ATOM   4062 O  OD1  . ASN   B 1 4   ? 44.198 -15.314 -14.837 1.00 12.96 ?  4    ASN   B OD1  1 
ATOM   4063 N  ND2  . ASN   B 1 4   ? 43.555 -13.532 -16.035 1.00 14.30 ?  4    ASN   B ND2  1 
ATOM   4064 H  H    A ASN   B 1 4   ? 46.874 -15.341 -16.750 0.50 18.82 ?  4    ASN   B H    1 
ATOM   4065 H  H    B ASN   B 1 4   ? 47.044 -15.592 -16.889 0.50 18.82 ?  4    ASN   B H    1 
ATOM   4066 H  HA   . ASN   B 1 4   ? 45.426 -16.900 -16.560 1.00 17.65 ?  4    ASN   B HA   1 
ATOM   4067 H  HB2  . ASN   B 1 4   ? 43.839 -15.021 -17.942 1.00 16.63 ?  4    ASN   B HB2  1 
ATOM   4068 H  HB3  . ASN   B 1 4   ? 43.245 -16.274 -17.169 1.00 16.63 ?  4    ASN   B HB3  1 
ATOM   4069 H  HD21 . ASN   B 1 4   ? 43.510 -13.031 -15.336 1.00 17.15 ?  4    ASN   B HD21 1 
ATOM   4070 H  HD22 . ASN   B 1 4   ? 43.362 -13.210 -16.808 1.00 17.15 ?  4    ASN   B HD22 1 
ATOM   4071 N  N    . SER   B 1 5   ? 46.409 -17.866 -18.931 1.00 15.80 ?  5    SER   B N    1 
ATOM   4072 C  CA   . SER   B 1 5   ? 46.504 -18.777 -20.071 1.00 18.01 ?  5    SER   B CA   1 
ATOM   4073 C  C    . SER   B 1 5   ? 46.481 -20.216 -19.565 1.00 19.38 ?  5    SER   B C    1 
ATOM   4074 O  O    . SER   B 1 5   ? 47.474 -20.937 -19.579 1.00 21.80 ?  5    SER   B O    1 
ATOM   4075 C  CB   . SER   B 1 5   ? 47.763 -18.484 -20.883 1.00 19.54 ?  5    SER   B CB   1 
ATOM   4076 O  OG   . SER   B 1 5   ? 48.933 -18.668 -20.103 1.00 21.75 ?  5    SER   B OG   1 
ATOM   4077 H  H    . SER   B 1 5   ? 47.165 -17.705 -18.549 1.00 18.96 ?  5    SER   B H    1 
ATOM   4078 H  HA   . SER   B 1 5   ? 45.735 -18.651 -20.644 1.00 21.61 ?  5    SER   B HA   1 
ATOM   4079 H  HB2  . SER   B 1 5   ? 47.789 -19.083 -21.647 1.00 23.45 ?  5    SER   B HB2  1 
ATOM   4080 H  HB3  . SER   B 1 5   ? 47.714 -17.566 -21.186 1.00 23.45 ?  5    SER   B HB3  1 
ATOM   4081 H  HG   . SER   B 1 5   ? 48.984 -19.467 -19.853 1.00 26.10 ?  5    SER   B HG   1 
ATOM   4082 N  N    . PHE   B 1 6   ? 45.305 -20.610 -19.091 1.00 19.26 ?  6    PHE   B N    1 
ATOM   4083 C  CA   . PHE   B 1 6   ? 45.101 -21.963 -18.596 1.00 18.84 ?  6    PHE   B CA   1 
ATOM   4084 C  C    . PHE   B 1 6   ? 45.014 -22.929 -19.767 1.00 21.92 ?  6    PHE   B C    1 
ATOM   4085 O  O    . PHE   B 1 6   ? 44.360 -22.645 -20.773 1.00 23.82 ?  6    PHE   B O    1 
ATOM   4086 C  CB   . PHE   B 1 6   ? 43.810 -22.018 -17.779 1.00 17.23 ?  6    PHE   B CB   1 
ATOM   4087 C  CG   . PHE   B 1 6   ? 43.834 -21.157 -16.547 1.00 15.25 ?  6    PHE   B CG   1 
ATOM   4088 C  CD1  . PHE   B 1 6   ? 44.338 -21.649 -15.362 1.00 14.07 ?  6    PHE   B CD1  1 
ATOM   4089 C  CD2  . PHE   B 1 6   ? 43.349 -19.856 -16.575 1.00 14.72 ?  6    PHE   B CD2  1 
ATOM   4090 C  CE1  . PHE   B 1 6   ? 44.354 -20.868 -14.217 1.00 13.67 ?  6    PHE   B CE1  1 
ATOM   4091 C  CE2  . PHE   B 1 6   ? 43.373 -19.061 -15.436 1.00 14.93 ?  6    PHE   B CE2  1 
ATOM   4092 C  CZ   . PHE   B 1 6   ? 43.881 -19.561 -14.259 1.00 14.00 ?  6    PHE   B CZ   1 
ATOM   4093 H  H    . PHE   B 1 6   ? 44.607 -20.117 -19.053 1.00 23.11 ?  6    PHE   B H    1 
ATOM   4094 H  HA   . PHE   B 1 6   ? 45.840 -22.225 -18.025 1.00 22.61 ?  6    PHE   B HA   1 
ATOM   4095 H  HB2  . PHE   B 1 6   ? 43.073 -21.717 -18.334 1.00 20.68 ?  6    PHE   B HB2  1 
ATOM   4096 H  HB3  . PHE   B 1 6   ? 43.653 -22.933 -17.495 1.00 20.68 ?  6    PHE   B HB3  1 
ATOM   4097 H  HD1  . PHE   B 1 6   ? 44.669 -22.518 -15.323 1.00 16.88 ?  6    PHE   B HD1  1 
ATOM   4098 H  HD2  . PHE   B 1 6   ? 43.005 -19.513 -17.366 1.00 17.66 ?  6    PHE   B HD2  1 
ATOM   4099 H  HE1  . PHE   B 1 6   ? 44.709 -21.205 -13.421 1.00 16.40 ?  6    PHE   B HE1  1 
ATOM   4100 H  HE2  . PHE   B 1 6   ? 43.042 -18.191 -15.467 1.00 17.92 ?  6    PHE   B HE2  1 
ATOM   4101 H  HZ   . PHE   B 1 6   ? 43.893 -19.036 -13.491 1.00 16.80 ?  6    PHE   B HZ   1 
ATOM   4102 N  N    . SER   B 1 7   ? 45.695 -24.070 -19.639 1.00 22.70 ?  7    SER   B N    1 
ATOM   4103 C  CA   . SER   B 1 7   ? 45.778 -25.047 -20.714 1.00 25.25 ?  7    SER   B CA   1 
ATOM   4104 C  C    . SER   B 1 7   ? 45.714 -26.456 -20.147 1.00 25.06 ?  7    SER   B C    1 
ATOM   4105 O  O    . SER   B 1 7   ? 46.308 -26.746 -19.104 1.00 26.08 ?  7    SER   B O    1 
ATOM   4106 C  CB   . SER   B 1 7   ? 47.079 -24.878 -21.512 1.00 27.62 ?  7    SER   B CB   1 
ATOM   4107 O  OG   . SER   B 1 7   ? 47.125 -25.770 -22.610 1.00 29.57 ?  7    SER   B OG   1 
ATOM   4108 H  H    . SER   B 1 7   ? 46.129 -24.299 -18.928 1.00 27.24 ?  7    SER   B H    1 
ATOM   4109 H  HA   . SER   B 1 7   ? 45.031 -24.930 -21.317 1.00 30.30 ?  7    SER   B HA   1 
ATOM   4110 H  HB2  . SER   B 1 7   ? 47.128 -23.967 -21.844 1.00 33.14 ?  7    SER   B HB2  1 
ATOM   4111 H  HB3  . SER   B 1 7   ? 47.834 -25.058 -20.930 1.00 33.14 ?  7    SER   B HB3  1 
ATOM   4112 H  HG   . SER   B 1 7   ? 47.842 -25.663 -23.038 1.00 35.49 ?  7    SER   B HG   1 
ATOM   4113 N  N    . GLY   B 1 8   ? 44.994 -27.332 -20.847 1.00 25.06 ?  8    GLY   B N    1 
ATOM   4114 C  CA   . GLY   B 1 8   ? 44.953 -28.731 -20.483 1.00 24.49 ?  8    GLY   B CA   1 
ATOM   4115 C  C    . GLY   B 1 8   ? 44.027 -29.066 -19.341 1.00 23.04 ?  8    GLY   B C    1 
ATOM   4116 O  O    . GLY   B 1 8   ? 44.175 -30.133 -18.732 1.00 24.17 ?  8    GLY   B O    1 
ATOM   4117 H  H    . GLY   B 1 8   ? 44.524 -27.132 -21.538 1.00 30.07 ?  8    GLY   B H    1 
ATOM   4118 H  HA2  . GLY   B 1 8   ? 44.676 -29.249 -21.256 1.00 29.39 ?  8    GLY   B HA2  1 
ATOM   4119 H  HA3  . GLY   B 1 8   ? 45.842 -29.019 -20.231 1.00 29.39 ?  8    GLY   B HA3  1 
ATOM   4120 N  N    . TYR   B 1 9   ? 43.057 -28.207 -19.041 1.00 20.74 ?  9    TYR   B N    1 
ATOM   4121 C  CA   . TYR   B 1 9   ? 42.110 -28.490 -17.977 1.00 18.59 ?  9    TYR   B CA   1 
ATOM   4122 C  C    . TYR   B 1 9   ? 40.922 -29.278 -18.498 1.00 17.82 ?  9    TYR   B C    1 
ATOM   4123 O  O    . TYR   B 1 9   ? 40.495 -29.128 -19.647 1.00 19.87 ?  9    TYR   B O    1 
ATOM   4124 C  CB   . TYR   B 1 9   ? 41.605 -27.206 -17.326 1.00 17.93 ?  9    TYR   B CB   1 
ATOM   4125 C  CG   . TYR   B 1 9   ? 42.629 -26.579 -16.418 1.00 17.56 ?  9    TYR   B CG   1 
ATOM   4126 C  CD1  . TYR   B 1 9   ? 43.712 -25.895 -16.942 1.00 18.01 ?  9    TYR   B CD1  1 
ATOM   4127 C  CD2  . TYR   B 1 9   ? 42.529 -26.691 -15.041 1.00 16.76 ?  9    TYR   B CD2  1 
ATOM   4128 C  CE1  . TYR   B 1 9   ? 44.668 -25.333 -16.120 1.00 18.18 ?  9    TYR   B CE1  1 
ATOM   4129 C  CE2  . TYR   B 1 9   ? 43.477 -26.133 -14.209 1.00 17.08 ?  9    TYR   B CE2  1 
ATOM   4130 C  CZ   . TYR   B 1 9   ? 44.545 -25.452 -14.755 1.00 17.75 ?  9    TYR   B CZ   1 
ATOM   4131 O  OH   . TYR   B 1 9   ? 45.494 -24.900 -13.933 1.00 18.54 ?  9    TYR   B OH   1 
ATOM   4132 H  H    . TYR   B 1 9   ? 42.914 -27.466 -19.453 1.00 24.89 ?  9    TYR   B H    1 
ATOM   4133 H  HA   . TYR   B 1 9   ? 42.545 -29.022 -17.295 1.00 22.31 ?  9    TYR   B HA   1 
ATOM   4134 H  HB2  . TYR   B 1 9   ? 41.370 -26.564 -18.014 1.00 21.52 ?  9    TYR   B HB2  1 
ATOM   4135 H  HB3  . TYR   B 1 9   ? 40.828 -27.426 -16.793 1.00 21.52 ?  9    TYR   B HB3  1 
ATOM   4136 H  HD1  . TYR   B 1 9   ? 43.796 -25.817 -17.866 1.00 21.62 ?  9    TYR   B HD1  1 
ATOM   4137 H  HD2  . TYR   B 1 9   ? 41.806 -27.157 -14.673 1.00 20.11 ?  9    TYR   B HD2  1 
ATOM   4138 H  HE1  . TYR   B 1 9   ? 45.384 -24.877 -16.486 1.00 21.82 ?  9    TYR   B HE1  1 
ATOM   4139 H  HE2  . TYR   B 1 9   ? 43.386 -26.221 -13.287 1.00 20.50 ?  9    TYR   B HE2  1 
ATOM   4140 H  HH   . TYR   B 1 9   ? 46.075 -24.519 -14.397 1.00 22.25 ?  9    TYR   B HH   1 
ATOM   4141 N  N    . LEU   B 1 10  ? 40.400 -30.134 -17.629 1.00 16.07 ?  10   LEU   B N    1 
ATOM   4142 C  CA   . LEU   B 1 10  ? 39.200 -30.901 -17.901 1.00 15.89 ?  10   LEU   B CA   1 
ATOM   4143 C  C    . LEU   B 1 10  ? 38.011 -30.140 -17.331 1.00 15.32 ?  10   LEU   B C    1 
ATOM   4144 O  O    . LEU   B 1 10  ? 38.029 -29.723 -16.169 1.00 14.93 ?  10   LEU   B O    1 
ATOM   4145 C  CB   . LEU   B 1 10  ? 39.321 -32.272 -17.240 1.00 17.11 ?  10   LEU   B CB   1 
ATOM   4146 C  CG   . LEU   B 1 10  ? 38.172 -33.227 -17.545 1.00 18.80 ?  10   LEU   B CG   1 
ATOM   4147 C  CD1  . LEU   B 1 10  ? 38.263 -33.739 -18.976 1.00 20.26 ?  10   LEU   B CD1  1 
ATOM   4148 C  CD2  . LEU   B 1 10  ? 38.139 -34.374 -16.551 1.00 19.90 ?  10   LEU   B CD2  1 
ATOM   4149 H  H    . LEU   B 1 10  ? 40.731 -30.287 -16.846 1.00 19.29 ?  10   LEU   B H    1 
ATOM   4150 H  HA   . LEU   B 1 10  ? 39.081 -31.019 -18.853 1.00 19.06 ?  10   LEU   B HA   1 
ATOM   4151 H  HB2  . LEU   B 1 10  ? 40.143 -32.697 -17.543 1.00 20.53 ?  10   LEU   B HB2  1 
ATOM   4152 H  HB3  . LEU   B 1 10  ? 39.358 -32.158 -16.275 1.00 20.53 ?  10   LEU   B HB3  1 
ATOM   4153 H  HG   . LEU   B 1 10  ? 37.337 -32.746 -17.460 1.00 22.56 ?  10   LEU   B HG   1 
ATOM   4154 H  HD11 . LEU   B 1 10  ? 37.550 -34.379 -19.126 1.00 24.31 ?  10   LEU   B HD11 1 
ATOM   4155 H  HD12 . LEU   B 1 10  ? 38.167 -32.989 -19.583 1.00 24.31 ?  10   LEU   B HD12 1 
ATOM   4156 H  HD13 . LEU   B 1 10  ? 39.123 -34.164 -19.105 1.00 24.31 ?  10   LEU   B HD13 1 
ATOM   4157 H  HD21 . LEU   B 1 10  ? 37.401 -34.961 -16.775 1.00 23.88 ?  10   LEU   B HD21 1 
ATOM   4158 H  HD22 . LEU   B 1 10  ? 38.976 -34.856 -16.597 1.00 23.88 ?  10   LEU   B HD22 1 
ATOM   4159 H  HD23 . LEU   B 1 10  ? 38.012 -34.009 -15.660 1.00 23.88 ?  10   LEU   B HD23 1 
ATOM   4160 N  N    . LYS   B 1 11  ? 36.982 -29.965 -18.147 1.00 16.63 ?  11   LYS   B N    1 
ATOM   4161 C  CA   . LYS   B 1 11  ? 35.791 -29.242 -17.730 1.00 18.68 ?  11   LYS   B CA   1 
ATOM   4162 C  C    . LYS   B 1 11  ? 34.907 -30.161 -16.894 1.00 17.69 ?  11   LYS   B C    1 
ATOM   4163 O  O    . LYS   B 1 11  ? 34.506 -31.235 -17.355 1.00 19.57 ?  11   LYS   B O    1 
ATOM   4164 C  CB   . LYS   B 1 11  ? 35.050 -28.758 -18.974 1.00 22.29 ?  11   LYS   B CB   1 
ATOM   4165 C  CG   . LYS   B 1 11  ? 33.915 -27.785 -18.716 1.00 25.58 ?  11   LYS   B CG   1 
ATOM   4166 C  CD   . LYS   B 1 11  ? 33.197 -27.449 -20.019 1.00 28.36 ?  11   LYS   B CD   1 
ATOM   4167 C  CE   . LYS   B 1 11  ? 32.164 -26.351 -19.836 1.00 30.44 ?  11   LYS   B CE   1 
ATOM   4168 N  NZ   . LYS   B 1 11  ? 32.799 -25.025 -19.610 1.00 31.59 ?  11   LYS   B NZ   1 
ATOM   4169 H  H    . LYS   B 1 11  ? 36.945 -30.272 -18.950 1.00 19.96 ?  11   LYS   B H    1 
ATOM   4170 H  HA   . LYS   B 1 11  ? 36.046 -28.475 -17.195 1.00 22.41 ?  11   LYS   B HA   1 
ATOM   4171 H  HB2  . LYS   B 1 11  ? 35.687 -28.313 -19.557 1.00 26.75 ?  11   LYS   B HB2  1 
ATOM   4172 H  HB3  . LYS   B 1 11  ? 34.678 -29.528 -19.431 1.00 26.75 ?  11   LYS   B HB3  1 
ATOM   4173 H  HG2  . LYS   B 1 11  ? 33.275 -28.188 -18.109 1.00 30.70 ?  11   LYS   B HG2  1 
ATOM   4174 H  HG3  . LYS   B 1 11  ? 34.269 -26.964 -18.341 1.00 30.70 ?  11   LYS   B HG3  1 
ATOM   4175 H  HD2  . LYS   B 1 11  ? 33.848 -27.147 -20.672 1.00 34.04 ?  11   LYS   B HD2  1 
ATOM   4176 H  HD3  . LYS   B 1 11  ? 32.742 -28.242 -20.345 1.00 34.04 ?  11   LYS   B HD3  1 
ATOM   4177 H  HE2  . LYS   B 1 11  ? 31.615 -26.292 -20.634 1.00 36.53 ?  11   LYS   B HE2  1 
ATOM   4178 H  HE3  . LYS   B 1 11  ? 31.613 -26.562 -19.067 1.00 36.53 ?  11   LYS   B HE3  1 
ATOM   4179 H  HZ1  . LYS   B 1 11  ? 32.173 -24.400 -19.515 1.00 37.91 ?  11   LYS   B HZ1  1 
ATOM   4180 H  HZ2  . LYS   B 1 11  ? 33.299 -25.049 -18.875 1.00 37.91 ?  11   LYS   B HZ2  1 
ATOM   4181 H  HZ3  . LYS   B 1 11  ? 33.315 -24.814 -20.305 1.00 37.91 ?  11   LYS   B HZ3  1 
ATOM   4182 N  N    . LEU   B 1 12  ? 34.598 -29.744 -15.667 1.00 15.98 ?  12   LEU   B N    1 
ATOM   4183 C  CA   . LEU   B 1 12  ? 33.637 -30.446 -14.821 1.00 15.57 ?  12   LEU   B CA   1 
ATOM   4184 C  C    . LEU   B 1 12  ? 32.244 -29.838 -14.909 1.00 15.56 ?  12   LEU   B C    1 
ATOM   4185 O  O    . LEU   B 1 12  ? 31.254 -30.552 -15.078 1.00 16.37 ?  12   LEU   B O    1 
ATOM   4186 C  CB   . LEU   B 1 12  ? 34.112 -30.451 -13.364 1.00 15.12 ?  12   LEU   B CB   1 
ATOM   4187 C  CG   . LEU   B 1 12  ? 35.443 -31.149 -13.091 1.00 15.49 ?  12   LEU   B CG   1 
ATOM   4188 C  CD1  . LEU   B 1 12  ? 35.785 -31.110 -11.610 1.00 15.76 ?  12   LEU   B CD1  1 
ATOM   4189 C  CD2  . LEU   B 1 12  ? 35.423 -32.584 -13.603 1.00 16.30 ?  12   LEU   B CD2  1 
ATOM   4190 H  H    . LEU   B 1 12  ? 34.941 -29.044 -15.299 1.00 19.18 ?  12   LEU   B H    1 
ATOM   4191 H  HA   . LEU   B 1 12  ? 33.575 -31.364 -15.118 1.00 18.68 ?  12   LEU   B HA   1 
ATOM   4192 H  HB2  . LEU   B 1 12  ? 34.203 -29.529 -13.070 1.00 18.14 ?  12   LEU   B HB2  1 
ATOM   4193 H  HB3  . LEU   B 1 12  ? 33.438 -30.894 -12.827 1.00 18.14 ?  12   LEU   B HB3  1 
ATOM   4194 H  HG   . LEU   B 1 12  ? 36.145 -30.674 -13.566 1.00 18.59 ?  12   LEU   B HG   1 
ATOM   4195 H  HD11 . LEU   B 1 12  ? 36.637 -31.558 -11.470 1.00 18.91 ?  12   LEU   B HD11 1 
ATOM   4196 H  HD12 . LEU   B 1 12  ? 35.848 -30.188 -11.320 1.00 18.91 ?  12   LEU   B HD12 1 
ATOM   4197 H  HD13 . LEU   B 1 12  ? 35.089 -31.568 -11.112 1.00 18.91 ?  12   LEU   B HD13 1 
ATOM   4198 H  HD21 . LEU   B 1 12  ? 36.209 -33.046 -13.277 1.00 19.56 ?  12   LEU   B HD21 1 
ATOM   4199 H  HD22 . LEU   B 1 12  ? 34.621 -33.021 -13.281 1.00 19.56 ?  12   LEU   B HD22 1 
ATOM   4200 H  HD23 . LEU   B 1 12  ? 35.426 -32.571 -14.575 1.00 19.56 ?  12   LEU   B HD23 1 
ATOM   4201 N  N    . THR   B 1 13  ? 32.157 -28.520 -14.794 1.00 15.54 ?  13   THR   B N    1 
ATOM   4202 C  CA   . THR   B 1 13  ? 30.932 -27.766 -14.993 1.00 15.59 ?  13   THR   B CA   1 
ATOM   4203 C  C    . THR   B 1 13  ? 31.267 -26.565 -15.871 1.00 17.53 ?  13   THR   B C    1 
ATOM   4204 O  O    . THR   B 1 13  ? 32.413 -26.369 -16.291 1.00 18.26 ?  13   THR   B O    1 
ATOM   4205 C  CB   . THR   B 1 13  ? 30.339 -27.291 -13.661 1.00 15.49 ?  13   THR   B CB   1 
ATOM   4206 O  OG1  . THR   B 1 13  ? 31.185 -26.269 -13.115 1.00 15.25 ?  13   THR   B OG1  1 
ATOM   4207 C  CG2  . THR   B 1 13  ? 30.219 -28.445 -12.666 1.00 16.32 ?  13   THR   B CG2  1 
ATOM   4208 H  H    . THR   B 1 13  ? 32.826 -28.017 -14.594 1.00 18.65 ?  13   THR   B H    1 
ATOM   4209 H  HA   . THR   B 1 13  ? 30.276 -28.321 -15.445 1.00 18.71 ?  13   THR   B HA   1 
ATOM   4210 H  HB   . THR   B 1 13  ? 29.446 -26.931 -13.817 1.00 18.59 ?  13   THR   B HB   1 
ATOM   4211 H  HG1  . THR   B 1 13  ? 30.864 -25.510 -13.299 1.00 18.30 ?  13   THR   B HG1  1 
ATOM   4212 H  HG21 . THR   B 1 13  ? 29.715 -28.162 -11.887 1.00 19.58 ?  13   THR   B HG21 1 
ATOM   4213 H  HG22 . THR   B 1 13  ? 29.764 -29.196 -13.078 1.00 19.58 ?  13   THR   B HG22 1 
ATOM   4214 H  HG23 . THR   B 1 13  ? 31.103 -28.730 -12.383 1.00 19.58 ?  13   THR   B HG23 1 
ATOM   4215 N  N    A ASP   B 1 14  ? 30.251 -25.745 -16.141 0.50 18.45 ?  14   ASP   B N    1 
ATOM   4216 N  N    B ASP   B 1 14  ? 30.256 -25.736 -16.138 0.50 18.38 ?  14   ASP   B N    1 
ATOM   4217 C  CA   A ASP   B 1 14  ? 30.467 -24.580 -16.989 0.50 19.78 ?  14   ASP   B CA   1 
ATOM   4218 C  CA   B ASP   B 1 14  ? 30.465 -24.576 -17.000 0.50 19.61 ?  14   ASP   B CA   1 
ATOM   4219 C  C    A ASP   B 1 14  ? 31.583 -23.690 -16.453 0.50 17.98 ?  14   ASP   B C    1 
ATOM   4220 C  C    B ASP   B 1 14  ? 31.466 -23.580 -16.429 0.50 17.93 ?  14   ASP   B C    1 
ATOM   4221 O  O    A ASP   B 1 14  ? 32.295 -23.053 -17.239 0.50 18.48 ?  14   ASP   B O    1 
ATOM   4222 O  O    B ASP   B 1 14  ? 31.933 -22.707 -17.168 0.50 18.49 ?  14   ASP   B O    1 
ATOM   4223 C  CB   A ASP   B 1 14  ? 29.165 -23.793 -17.147 0.50 22.78 ?  14   ASP   B CB   1 
ATOM   4224 C  CB   B ASP   B 1 14  ? 29.146 -23.851 -17.257 0.50 22.46 ?  14   ASP   B CB   1 
ATOM   4225 C  CG   A ASP   B 1 14  ? 28.165 -24.490 -18.043 0.50 25.49 ?  14   ASP   B CG   1 
ATOM   4226 C  CG   B ASP   B 1 14  ? 28.273 -24.577 -18.261 0.50 25.04 ?  14   ASP   B CG   1 
ATOM   4227 O  OD1  A ASP   B 1 14  ? 28.478 -25.576 -18.578 0.50 26.30 ?  14   ASP   B OD1  1 
ATOM   4228 O  OD1  B ASP   B 1 14  ? 28.833 -25.255 -19.149 0.50 25.81 ?  14   ASP   B OD1  1 
ATOM   4229 O  OD2  A ASP   B 1 14  ? 27.054 -23.944 -18.206 0.50 26.60 -1 14   ASP   B OD2  1 
ATOM   4230 O  OD2  B ASP   B 1 14  ? 27.033 -24.479 -18.164 0.50 26.04 -1 14   ASP   B OD2  1 
ATOM   4231 H  H    A ASP   B 1 14  ? 29.449 -25.833 -15.843 0.50 22.14 ?  14   ASP   B H    1 
ATOM   4232 H  H    B ASP   B 1 14  ? 29.454 -25.823 -15.841 0.50 22.05 ?  14   ASP   B H    1 
ATOM   4233 H  HA   A ASP   B 1 14  ? 30.739 -24.874 -17.868 0.50 23.74 ?  14   ASP   B HA   1 
ATOM   4234 H  HA   B ASP   B 1 14  ? 30.803 -24.884 -17.856 0.50 23.54 ?  14   ASP   B HA   1 
ATOM   4235 H  HB2  A ASP   B 1 14  ? 28.737 -23.694 -16.287 0.50 27.34 ?  14   ASP   B HB2  1 
ATOM   4236 H  HB2  B ASP   B 1 14  ? 28.658 -23.778 -16.421 0.50 26.95 ?  14   ASP   B HB2  1 
ATOM   4237 H  HB3  A ASP   B 1 14  ? 29.355 -22.925 -17.533 0.50 27.34 ?  14   ASP   B HB3  1 
ATOM   4238 H  HB3  B ASP   B 1 14  ? 29.341 -22.960 -17.601 0.50 26.95 ?  14   ASP   B HB3  1 
ATOM   4239 N  N    . ASN   B 1 15  ? 31.779 -23.660 -15.132 1.00 15.85 ?  15   ASN   B N    1 
ATOM   4240 C  CA   . ASN   B 1 15  ? 32.736 -22.742 -14.523 1.00 13.77 ?  15   ASN   B CA   1 
ATOM   4241 C  C    . ASN   B 1 15  ? 33.832 -23.400 -13.691 1.00 12.60 ?  15   ASN   B C    1 
ATOM   4242 O  O    . ASN   B 1 15  ? 34.681 -22.675 -13.158 1.00 12.94 ?  15   ASN   B O    1 
ATOM   4243 C  CB   . ASN   B 1 15  ? 32.020 -21.693 -13.655 1.00 13.95 ?  15   ASN   B CB   1 
ATOM   4244 C  CG   . ASN   B 1 15  ? 31.399 -22.298 -12.418 1.00 13.73 ?  15   ASN   B CG   1 
ATOM   4245 O  OD1  . ASN   B 1 15  ? 30.458 -23.095 -12.507 1.00 15.14 ?  15   ASN   B OD1  1 
ATOM   4246 N  ND2  . ASN   B 1 15  ? 31.925 -21.947 -11.256 1.00 13.18 ?  15   ASN   B ND2  1 
ATOM   4247 H  H    A ASN   B 1 15  ? 31.374 -24.174 -14.569 0.50 19.02 ?  15   ASN   B H    1 
ATOM   4248 H  H    B ASN   B 1 15  ? 31.420 -24.215 -14.578 0.50 19.02 ?  15   ASN   B H    1 
ATOM   4249 H  HA   . ASN   B 1 15  ? 33.181 -22.254 -15.227 1.00 16.52 ?  15   ASN   B HA   1 
ATOM   4250 H  HB2  . ASN   B 1 15  ? 32.668 -21.018 -13.373 1.00 16.73 ?  15   ASN   B HB2  1 
ATOM   4251 H  HB3  . ASN   B 1 15  ? 31.315 -21.270 -14.170 1.00 16.73 ?  15   ASN   B HB3  1 
ATOM   4252 H  HD21 . ASN   B 1 15  ? 31.606 -22.265 -10.522 1.00 15.82 ?  15   ASN   B HD21 1 
ATOM   4253 H  HD22 . ASN   B 1 15  ? 32.585 -21.389 -11.225 1.00 15.82 ?  15   ASN   B HD22 1 
ATOM   4254 N  N    . VAL   B 1 16  ? 33.843 -24.725 -13.551 1.00 12.54 ?  16   VAL   B N    1 
ATOM   4255 C  CA   . VAL   B 1 16  ? 34.843 -25.421 -12.742 1.00 12.27 ?  16   VAL   B CA   1 
ATOM   4256 C  C    . VAL   B 1 16  ? 35.636 -26.359 -13.640 1.00 12.24 ?  16   VAL   B C    1 
ATOM   4257 O  O    . VAL   B 1 16  ? 35.057 -27.235 -14.303 1.00 13.23 ?  16   VAL   B O    1 
ATOM   4258 C  CB   . VAL   B 1 16  ? 34.218 -26.186 -11.566 1.00 12.41 ?  16   VAL   B CB   1 
ATOM   4259 C  CG1  . VAL   B 1 16  ? 35.302 -26.918 -10.776 1.00 12.59 ?  16   VAL   B CG1  1 
ATOM   4260 C  CG2  . VAL   B 1 16  ? 33.427 -25.243 -10.668 1.00 13.26 ?  16   VAL   B CG2  1 
ATOM   4261 H  H    . VAL   B 1 16  ? 33.269 -25.252 -13.918 1.00 15.05 ?  16   VAL   B H    1 
ATOM   4262 H  HA   . VAL   B 1 16  ? 35.460 -24.768 -12.376 1.00 14.72 ?  16   VAL   B HA   1 
ATOM   4263 H  HB   . VAL   B 1 16  ? 33.604 -26.853 -11.912 1.00 14.89 ?  16   VAL   B HB   1 
ATOM   4264 H  HG11 . VAL   B 1 16  ? 34.927 -27.216 -9.931  1.00 15.11 ?  16   VAL   B HG11 1 
ATOM   4265 H  HG12 . VAL   B 1 16  ? 35.608 -27.682 -11.287 1.00 15.11 ?  16   VAL   B HG12 1 
ATOM   4266 H  HG13 . VAL   B 1 16  ? 36.038 -26.308 -10.613 1.00 15.11 ?  16   VAL   B HG13 1 
ATOM   4267 H  HG21 . VAL   B 1 16  ? 33.086 -25.739 -9.907  1.00 15.92 ?  16   VAL   B HG21 1 
ATOM   4268 H  HG22 . VAL   B 1 16  ? 34.009 -24.530 -10.365 1.00 15.92 ?  16   VAL   B HG22 1 
ATOM   4269 H  HG23 . VAL   B 1 16  ? 32.687 -24.870 -11.176 1.00 15.92 ?  16   VAL   B HG23 1 
ATOM   4270 N  N    . TYR   B 1 17  ? 36.962 -26.196 -13.618 1.00 12.73 ?  17   TYR   B N    1 
ATOM   4271 C  CA   . TYR   B 1 17  ? 37.907 -26.943 -14.434 1.00 13.21 ?  17   TYR   B CA   1 
ATOM   4272 C  C    . TYR   B 1 17  ? 38.957 -27.556 -13.519 1.00 12.10 ?  17   TYR   B C    1 
ATOM   4273 O  O    . TYR   B 1 17  ? 39.242 -27.024 -12.442 1.00 12.64 ?  17   TYR   B O    1 
ATOM   4274 C  CB   . TYR   B 1 17  ? 38.616 -26.010 -15.425 1.00 15.55 ?  17   TYR   B CB   1 
ATOM   4275 C  CG   . TYR   B 1 17  ? 37.688 -25.241 -16.332 1.00 18.30 ?  17   TYR   B CG   1 
ATOM   4276 C  CD1  . TYR   B 1 17  ? 37.097 -24.052 -15.918 1.00 19.82 ?  17   TYR   B CD1  1 
ATOM   4277 C  CD2  . TYR   B 1 17  ? 37.400 -25.707 -17.607 1.00 20.32 ?  17   TYR   B CD2  1 
ATOM   4278 C  CE1  . TYR   B 1 17  ? 36.246 -23.348 -16.750 1.00 21.35 ?  17   TYR   B CE1  1 
ATOM   4279 C  CE2  . TYR   B 1 17  ? 36.554 -25.009 -18.448 1.00 22.07 ?  17   TYR   B CE2  1 
ATOM   4280 C  CZ   . TYR   B 1 17  ? 35.978 -23.834 -18.013 1.00 22.64 ?  17   TYR   B CZ   1 
ATOM   4281 O  OH   . TYR   B 1 17  ? 35.134 -23.138 -18.846 1.00 24.08 ?  17   TYR   B OH   1 
ATOM   4282 H  H    . TYR   B 1 17  ? 37.358 -25.624 -13.105 1.00 15.27 ?  17   TYR   B H    1 
ATOM   4283 H  HA   . TYR   B 1 17  ? 37.448 -27.649 -14.922 1.00 15.86 ?  17   TYR   B HA   1 
ATOM   4284 H  HB2  . TYR   B 1 17  ? 39.149 -25.371 -14.930 1.00 18.66 ?  17   TYR   B HB2  1 
ATOM   4285 H  HB3  . TYR   B 1 17  ? 39.187 -26.546 -15.992 1.00 18.66 ?  17   TYR   B HB3  1 
ATOM   4286 H  HD1  . TYR   B 1 17  ? 37.281 -23.724 -15.069 1.00 23.79 ?  17   TYR   B HD1  1 
ATOM   4287 H  HD2  . TYR   B 1 17  ? 37.781 -26.501 -17.904 1.00 24.38 ?  17   TYR   B HD2  1 
ATOM   4288 H  HE1  . TYR   B 1 17  ? 35.859 -22.551 -16.462 1.00 25.62 ?  17   TYR   B HE1  1 
ATOM   4289 H  HE2  . TYR   B 1 17  ? 36.363 -25.335 -19.301 1.00 26.48 ?  17   TYR   B HE2  1 
ATOM   4290 H  HH   . TYR   B 1 17  ? 35.050 -23.535 -19.582 1.00 28.90 ?  17   TYR   B HH   1 
ATOM   4291 N  N    . ILE   B 1 18  ? 39.566 -28.658 -13.958 1.00 12.19 ?  18   ILE   B N    1 
ATOM   4292 C  CA   . ILE   B 1 18  ? 40.500 -29.383 -13.101 1.00 12.23 ?  18   ILE   B CA   1 
ATOM   4293 C  C    . ILE   B 1 18  ? 41.661 -29.929 -13.926 1.00 12.64 ?  18   ILE   B C    1 
ATOM   4294 O  O    . ILE   B 1 18  ? 41.496 -30.333 -15.082 1.00 13.78 ?  18   ILE   B O    1 
ATOM   4295 C  CB   . ILE   B 1 18  ? 39.748 -30.486 -12.307 1.00 12.84 ?  18   ILE   B CB   1 
ATOM   4296 C  CG1  . ILE   B 1 18  ? 40.594 -31.028 -11.152 1.00 13.26 ?  18   ILE   B CG1  1 
ATOM   4297 C  CG2  . ILE   B 1 18  ? 39.259 -31.600 -13.235 1.00 13.42 ?  18   ILE   B CG2  1 
ATOM   4298 C  CD1  . ILE   B 1 18  ? 39.763 -31.817 -10.139 1.00 14.83 ?  18   ILE   B CD1  1 
ATOM   4299 H  H    . ILE   B 1 18  ? 39.464 -29.003 -14.740 1.00 14.63 ?  18   ILE   B H    1 
ATOM   4300 H  HA   . ILE   B 1 18  ? 40.864 -28.770 -12.449 1.00 14.67 ?  18   ILE   B HA   1 
ATOM   4301 H  HB   . ILE   B 1 18  ? 38.958 -30.081 -11.912 1.00 15.41 ?  18   ILE   B HB   1 
ATOM   4302 H  HG12 . ILE   B 1 18  ? 41.273 -31.618 -11.502 1.00 15.91 ?  18   ILE   B HG12 1 
ATOM   4303 H  HG13 . ILE   B 1 18  ? 41.002 -30.283 -10.684 1.00 15.91 ?  18   ILE   B HG13 1 
ATOM   4304 H  HG21 . ILE   B 1 18  ? 38.662 -32.188 -12.740 1.00 16.11 ?  18   ILE   B HG21 1 
ATOM   4305 H  HG22 . ILE   B 1 18  ? 38.783 -31.200 -13.978 1.00 16.11 ?  18   ILE   B HG22 1 
ATOM   4306 H  HG23 . ILE   B 1 18  ? 40.021 -32.101 -13.558 1.00 16.11 ?  18   ILE   B HG23 1 
ATOM   4307 H  HD11 . ILE   B 1 18  ? 40.335 -32.096 -9.407  1.00 17.80 ?  18   ILE   B HD11 1 
ATOM   4308 H  HD12 . ILE   B 1 18  ? 39.050 -31.247 -9.800  1.00 17.80 ?  18   ILE   B HD12 1 
ATOM   4309 H  HD13 . ILE   B 1 18  ? 39.381 -32.593 -10.577 1.00 17.80 ?  18   ILE   B HD13 1 
ATOM   4310 N  N    . LYS   B 1 19  ? 42.842 -29.962 -13.306 1.00 12.97 ?  19   LYS   B N    1 
ATOM   4311 C  CA   . LYS   B 1 19  ? 44.052 -30.438 -13.962 1.00 13.87 ?  19   LYS   B CA   1 
ATOM   4312 C  C    . LYS   B 1 19  ? 44.950 -31.119 -12.940 1.00 13.49 ?  19   LYS   B C    1 
ATOM   4313 O  O    . LYS   B 1 19  ? 45.036 -30.683 -11.789 1.00 13.14 ?  19   LYS   B O    1 
ATOM   4314 C  CB   . LYS   B 1 19  ? 44.823 -29.272 -14.594 1.00 15.41 ?  19   LYS   B CB   1 
ATOM   4315 C  CG   . LYS   B 1 19  ? 46.025 -29.680 -15.427 1.00 17.47 ?  19   LYS   B CG   1 
ATOM   4316 C  CD   . LYS   B 1 19  ? 46.748 -28.451 -15.967 1.00 19.25 ?  19   LYS   B CD   1 
ATOM   4317 C  CE   . LYS   B 1 19  ? 47.919 -28.828 -16.850 1.00 21.21 ?  19   LYS   B CE   1 
ATOM   4318 N  NZ   . LYS   B 1 19  ? 48.664 -27.636 -17.326 1.00 22.19 ?  19   LYS   B NZ   1 
ATOM   4319 H  H    . LYS   B 1 19  ? 42.959 -29.709 -12.487 1.00 15.56 ?  19   LYS   B H    1 
ATOM   4320 H  HA   . LYS   B 1 19  ? 43.815 -31.078 -14.651 1.00 16.64 ?  19   LYS   B HA   1 
ATOM   4321 H  HB2  . LYS   B 1 19  ? 44.215 -28.785 -15.170 1.00 18.49 ?  19   LYS   B HB2  1 
ATOM   4322 H  HB3  . LYS   B 1 19  ? 45.133 -28.689 -13.880 1.00 18.49 ?  19   LYS   B HB3  1 
ATOM   4323 H  HG2  . LYS   B 1 19  ? 46.642 -30.184 -14.876 1.00 20.97 ?  19   LYS   B HG2  1 
ATOM   4324 H  HG3  . LYS   B 1 19  ? 45.724 -30.217 -16.177 1.00 20.97 ?  19   LYS   B HG3  1 
ATOM   4325 H  HD2  . LYS   B 1 19  ? 46.126 -27.922 -16.492 1.00 23.10 ?  19   LYS   B HD2  1 
ATOM   4326 H  HD3  . LYS   B 1 19  ? 47.084 -27.928 -15.222 1.00 23.10 ?  19   LYS   B HD3  1 
ATOM   4327 H  HE2  . LYS   B 1 19  ? 48.527 -29.390 -16.345 1.00 25.46 ?  19   LYS   B HE2  1 
ATOM   4328 H  HE3  . LYS   B 1 19  ? 47.585 -29.311 -17.625 1.00 25.46 ?  19   LYS   B HE3  1 
ATOM   4329 H  HZ1  . LYS   B 1 19  ? 49.298 -27.884 -17.899 1.00 26.63 ?  19   LYS   B HZ1  1 
ATOM   4330 H  HZ2  . LYS   B 1 19  ? 48.109 -27.073 -17.735 1.00 26.63 ?  19   LYS   B HZ2  1 
ATOM   4331 H  HZ3  . LYS   B 1 19  ? 49.043 -27.220 -16.637 1.00 26.63 ?  19   LYS   B HZ3  1 
ATOM   4332 N  N    . ASN   B 1 20  ? 45.637 -32.172 -13.378 1.00 14.60 ?  20   ASN   B N    1 
ATOM   4333 C  CA   . ASN   B 1 20  ? 46.675 -32.799 -12.571 1.00 15.75 ?  20   ASN   B CA   1 
ATOM   4334 C  C    . ASN   B 1 20  ? 47.942 -31.974 -12.756 1.00 16.22 ?  20   ASN   B C    1 
ATOM   4335 O  O    . ASN   B 1 20  ? 48.578 -32.036 -13.815 1.00 17.94 ?  20   ASN   B O    1 
ATOM   4336 C  CB   . ASN   B 1 20  ? 46.860 -34.245 -13.026 1.00 17.46 ?  20   ASN   B CB   1 
ATOM   4337 C  CG   . ASN   B 1 20  ? 48.013 -34.952 -12.336 1.00 18.89 ?  20   ASN   B CG   1 
ATOM   4338 O  OD1  . ASN   B 1 20  ? 48.681 -35.795 -12.941 1.00 21.10 ?  20   ASN   B OD1  1 
ATOM   4339 N  ND2  . ASN   B 1 20  ? 48.248 -34.631 -11.074 1.00 18.60 ?  20   ASN   B ND2  1 
ATOM   4340 H  H    . ASN   B 1 20  ? 45.521 -32.537 -14.147 1.00 17.52 ?  20   ASN   B H    1 
ATOM   4341 H  HA   . ASN   B 1 20  ? 46.409 -32.788 -11.637 1.00 18.90 ?  20   ASN   B HA   1 
ATOM   4342 H  HB2  . ASN   B 1 20  ? 46.045 -34.738 -12.833 1.00 20.95 ?  20   ASN   B HB2  1 
ATOM   4343 H  HB3  . ASN   B 1 20  ? 47.028 -34.249 -13.980 1.00 20.95 ?  20   ASN   B HB3  1 
ATOM   4344 H  HD21 . ASN   B 1 20  ? 48.895 -35.003 -10.651 1.00 22.32 ?  20   ASN   B HD21 1 
ATOM   4345 H  HD22 . ASN   B 1 20  ? 47.761 -34.039 -10.676 1.00 22.32 ?  20   ASN   B HD22 1 
ATOM   4346 N  N    . ALA   B 1 21  ? 48.299 -31.183 -11.744 1.00 15.54 ?  21   ALA   B N    1 
ATOM   4347 C  CA   . ALA   B 1 21  ? 49.399 -30.246 -11.898 1.00 16.30 ?  21   ALA   B CA   1 
ATOM   4348 C  C    . ALA   B 1 21  ? 49.862 -29.754 -10.535 1.00 15.33 ?  21   ALA   B C    1 
ATOM   4349 O  O    . ALA   B 1 21  ? 49.120 -29.787 -9.549  1.00 15.25 ?  21   ALA   B O    1 
ATOM   4350 C  CB   . ALA   B 1 21  ? 48.983 -29.072 -12.780 1.00 17.69 ?  21   ALA   B CB   1 
ATOM   4351 H  H    . ALA   B 1 21  ? 47.923 -31.180 -10.962 1.00 18.65 ?  21   ALA   B H    1 
ATOM   4352 H  HA   . ALA   B 1 21  ? 50.141 -30.706 -12.319 1.00 19.56 ?  21   ALA   B HA   1 
ATOM   4353 H  HB1  . ALA   B 1 21  ? 49.764 -28.545 -12.966 1.00 21.23 ?  21   ALA   B HB1  1 
ATOM   4354 H  HB2  . ALA   B 1 21  ? 48.611 -29.428 -13.603 1.00 21.23 ?  21   ALA   B HB2  1 
ATOM   4355 H  HB3  . ALA   B 1 21  ? 48.313 -28.554 -12.311 1.00 21.23 ?  21   ALA   B HB3  1 
ATOM   4356 N  N    . ASP   B 1 22  ? 51.120 -29.312 -10.510 1.00 14.68 ?  22   ASP   B N    1 
ATOM   4357 C  CA   . ASP   B 1 22  ? 51.736 -28.631 -9.378  1.00 14.22 ?  22   ASP   B CA   1 
ATOM   4358 C  C    . ASP   B 1 22  ? 51.332 -27.159 -9.450  1.00 12.74 ?  22   ASP   B C    1 
ATOM   4359 O  O    . ASP   B 1 22  ? 51.639 -26.481 -10.435 1.00 13.05 ?  22   ASP   B O    1 
ATOM   4360 C  CB   . ASP   B 1 22  ? 53.252 -28.806 -9.540  1.00 15.86 ?  22   ASP   B CB   1 
ATOM   4361 C  CG   . ASP   B 1 22  ? 54.080 -28.048 -8.512  1.00 17.46 ?  22   ASP   B CG   1 
ATOM   4362 O  OD1  . ASP   B 1 22  ? 53.706 -26.938 -8.098  1.00 17.37 ?  22   ASP   B OD1  1 
ATOM   4363 O  OD2  . ASP   B 1 22  ? 55.161 -28.560 -8.144  1.00 19.89 -1 22   ASP   B OD2  1 
ATOM   4364 H  H    . ASP   B 1 22  ? 51.660 -29.409 -11.176 1.00 17.62 ?  22   ASP   B H    1 
ATOM   4365 H  HA   . ASP   B 1 22  ? 51.445 -29.024 -8.536  1.00 17.06 ?  22   ASP   B HA   1 
ATOM   4366 H  HB2  . ASP   B 1 22  ? 53.473 -29.744 -9.463  1.00 19.03 ?  22   ASP   B HB2  1 
ATOM   4367 H  HB3  . ASP   B 1 22  ? 53.509 -28.476 -10.417 1.00 19.03 ?  22   ASP   B HB3  1 
ATOM   4368 N  N    . ILE   B 1 23  ? 50.618 -26.673 -8.427  1.00 12.24 ?  23   ILE   B N    1 
ATOM   4369 C  CA   . ILE   B 1 23  ? 50.028 -25.332 -8.488  1.00 11.65 ?  23   ILE   B CA   1 
ATOM   4370 C  C    . ILE   B 1 23  ? 51.084 -24.243 -8.621  1.00 11.36 ?  23   ILE   B C    1 
ATOM   4371 O  O    . ILE   B 1 23  ? 50.818 -23.195 -9.216  1.00 11.20 ?  23   ILE   B O    1 
ATOM   4372 C  CB   . ILE   B 1 23  ? 49.087 -25.093 -7.292  1.00 11.74 ?  23   ILE   B CB   1 
ATOM   4373 C  CG1  . ILE   B 1 23  ? 48.254 -23.826 -7.497  1.00 12.42 ?  23   ILE   B CG1  1 
ATOM   4374 C  CG2  . ILE   B 1 23  ? 49.849 -25.053 -5.985  1.00 12.63 ?  23   ILE   B CG2  1 
ATOM   4375 C  CD1  . ILE   B 1 23  ? 47.142 -23.663 -6.469  1.00 13.38 ?  23   ILE   B CD1  1 
ATOM   4376 H  H    . ILE   B 1 23  ? 50.464 -27.100 -7.693  1.00 14.68 ?  23   ILE   B H    1 
ATOM   4377 H  HA   . ILE   B 1 23  ? 49.479 -25.292 -9.285  1.00 13.98 ?  23   ILE   B HA   1 
ATOM   4378 H  HB   . ILE   B 1 23  ? 48.471 -25.842 -7.250  1.00 14.09 ?  23   ILE   B HB   1 
ATOM   4379 H  HG12 . ILE   B 1 23  ? 48.836 -23.051 -7.433  1.00 14.90 ?  23   ILE   B HG12 1 
ATOM   4380 H  HG13 . ILE   B 1 23  ? 47.844 -23.855 -8.379  1.00 14.90 ?  23   ILE   B HG13 1 
ATOM   4381 H  HG21 . ILE   B 1 23  ? 49.217 -25.064 -5.250  1.00 15.16 ?  23   ILE   B HG21 1 
ATOM   4382 H  HG22 . ILE   B 1 23  ? 50.428 -25.829 -5.935  1.00 15.16 ?  23   ILE   B HG22 1 
ATOM   4383 H  HG23 . ILE   B 1 23  ? 50.380 -24.242 -5.954  1.00 15.16 ?  23   ILE   B HG23 1 
ATOM   4384 H  HD11 . ILE   B 1 23  ? 46.600 -22.897 -6.709  1.00 16.06 ?  23   ILE   B HD11 1 
ATOM   4385 H  HD12 . ILE   B 1 23  ? 46.599 -24.467 -6.467  1.00 16.06 ?  23   ILE   B HD12 1 
ATOM   4386 H  HD13 . ILE   B 1 23  ? 47.539 -23.529 -5.595  1.00 16.06 ?  23   ILE   B HD13 1 
ATOM   4387 N  N    . VAL   B 1 24  ? 52.279 -24.452 -8.065  1.00 11.80 ?  24   VAL   B N    1 
ATOM   4388 C  CA   . VAL   B 1 24  ? 53.354 -23.468 -8.224  1.00 12.23 ?  24   VAL   B CA   1 
ATOM   4389 C  C    . VAL   B 1 24  ? 53.805 -23.411 -9.676  1.00 12.50 ?  24   VAL   B C    1 
ATOM   4390 O  O    . VAL   B 1 24  ? 53.941 -22.330 -10.265 1.00 12.87 ?  24   VAL   B O    1 
ATOM   4391 C  CB   . VAL   B 1 24  ? 54.535 -23.790 -7.287  1.00 13.03 ?  24   VAL   B CB   1 
ATOM   4392 C  CG1  . VAL   B 1 24  ? 55.754 -22.916 -7.624  1.00 13.64 ?  24   VAL   B CG1  1 
ATOM   4393 C  CG2  . VAL   B 1 24  ? 54.127 -23.620 -5.841  1.00 14.05 ?  24   VAL   B CG2  1 
ATOM   4394 H  H    . VAL   B 1 24  ? 52.489 -25.142 -7.598  1.00 14.16 ?  24   VAL   B H    1 
ATOM   4395 H  HA   . VAL   B 1 24  ? 53.013 -22.593 -7.985  1.00 14.68 ?  24   VAL   B HA   1 
ATOM   4396 H  HB   . VAL   B 1 24  ? 54.789 -24.718 -7.411  1.00 15.63 ?  24   VAL   B HB   1 
ATOM   4397 H  HG11 . VAL   B 1 24  ? 56.347 -22.903 -6.858  1.00 16.37 ?  24   VAL   B HG11 1 
ATOM   4398 H  HG12 . VAL   B 1 24  ? 56.208 -23.300 -8.389  1.00 16.37 ?  24   VAL   B HG12 1 
ATOM   4399 H  HG13 . VAL   B 1 24  ? 55.450 -22.019 -7.826  1.00 16.37 ?  24   VAL   B HG13 1 
ATOM   4400 H  HG21 . VAL   B 1 24  ? 54.850 -23.921 -5.270  1.00 16.86 ?  24   VAL   B HG21 1 
ATOM   4401 H  HG22 . VAL   B 1 24  ? 53.942 -22.682 -5.674  1.00 16.86 ?  24   VAL   B HG22 1 
ATOM   4402 H  HG23 . VAL   B 1 24  ? 53.330 -24.149 -5.671  1.00 16.86 ?  24   VAL   B HG23 1 
ATOM   4403 N  N    . GLU   B 1 25  ? 54.075 -24.579 -10.267 1.00 13.22 ?  25   GLU   B N    1 
ATOM   4404 C  CA   . GLU   B 1 25  ? 54.467 -24.615 -11.670 1.00 14.66 ?  25   GLU   B CA   1 
ATOM   4405 C  C    . GLU   B 1 25  ? 53.360 -24.068 -12.557 1.00 13.52 ?  25   GLU   B C    1 
ATOM   4406 O  O    . GLU   B 1 25  ? 53.627 -23.348 -13.529 1.00 14.40 ?  25   GLU   B O    1 
ATOM   4407 C  CB   . GLU   B 1 25  ? 54.872 -26.034 -12.068 1.00 18.49 ?  25   GLU   B CB   1 
ATOM   4408 C  CG   . GLU   B 1 25  ? 56.170 -26.476 -11.412 1.00 24.13 ?  25   GLU   B CG   1 
ATOM   4409 C  CD   . GLU   B 1 25  ? 57.278 -25.439 -11.521 1.00 28.71 ?  25   GLU   B CD   1 
ATOM   4410 O  OE1  . GLU   B 1 25  ? 57.646 -25.071 -12.658 1.00 30.31 ?  25   GLU   B OE1  1 
ATOM   4411 O  OE2  . GLU   B 1 25  ? 57.774 -24.974 -10.468 1.00 30.26 -1 25   GLU   B OE2  1 
ATOM   4412 H  H    . GLU   B 1 25  ? 54.035 -25.350 -9.882  1.00 15.86 ?  25   GLU   B H    1 
ATOM   4413 H  HA   . GLU   B 1 25  ? 55.224 -24.030 -11.792 1.00 17.59 ?  25   GLU   B HA   1 
ATOM   4414 H  HB2  . GLU   B 1 25  ? 54.176 -26.655 -11.795 1.00 22.19 ?  25   GLU   B HB2  1 
ATOM   4415 H  HB3  . GLU   B 1 25  ? 54.991 -26.074 -13.030 1.00 22.19 ?  25   GLU   B HB3  1 
ATOM   4416 H  HG2  . GLU   B 1 25  ? 56.015 -26.633 -10.472 1.00 28.96 ?  25   GLU   B HG2  1 
ATOM   4417 H  HG3  . GLU   B 1 25  ? 56.485 -27.284 -11.845 1.00 28.96 ?  25   GLU   B HG3  1 
ATOM   4418 N  N    A GLU   B 1 26  ? 52.106 -24.382 -12.229 0.50 12.68 ?  26   GLU   B N    1 
ATOM   4419 N  N    B GLU   B 1 26  ? 52.105 -24.391 -12.231 0.50 13.10 ?  26   GLU   B N    1 
ATOM   4420 C  CA   A GLU   B 1 26  ? 50.986 -23.852 -12.997 0.50 13.07 ?  26   GLU   B CA   1 
ATOM   4421 C  CA   B GLU   B 1 26  ? 50.974 -23.862 -12.988 0.50 13.78 ?  26   GLU   B CA   1 
ATOM   4422 C  C    A GLU   B 1 26  ? 50.931 -22.336 -12.910 0.50 12.52 ?  26   GLU   B C    1 
ATOM   4423 C  C    B GLU   B 1 26  ? 50.923 -22.344 -12.908 0.50 12.82 ?  26   GLU   B C    1 
ATOM   4424 O  O    A GLU   B 1 26  ? 50.737 -21.653 -13.921 0.50 13.58 ?  26   GLU   B O    1 
ATOM   4425 O  O    B GLU   B 1 26  ? 50.723 -21.666 -13.921 0.50 13.77 ?  26   GLU   B O    1 
ATOM   4426 C  CB   A GLU   B 1 26  ? 49.675 -24.439 -12.482 0.50 14.20 ?  26   GLU   B CB   1 
ATOM   4427 C  CB   B GLU   B 1 26  ? 49.661 -24.442 -12.455 0.50 15.44 ?  26   GLU   B CB   1 
ATOM   4428 C  CG   A GLU   B 1 26  ? 49.366 -25.809 -13.019 0.50 16.05 ?  26   GLU   B CG   1 
ATOM   4429 C  CG   B GLU   B 1 26  ? 49.105 -25.631 -13.223 0.50 17.54 ?  26   GLU   B CG   1 
ATOM   4430 C  CD   A GLU   B 1 26  ? 49.167 -25.820 -14.523 0.50 16.71 ?  26   GLU   B CD   1 
ATOM   4431 C  CD   B GLU   B 1 26  ? 48.798 -25.310 -14.682 0.50 18.19 ?  26   GLU   B CD   1 
ATOM   4432 O  OE1  A GLU   B 1 26  ? 48.324 -25.045 -15.022 0.50 16.07 ?  26   GLU   B OE1  1 
ATOM   4433 O  OE1  B GLU   B 1 26  ? 47.738 -24.712 -14.983 0.50 19.04 ?  26   GLU   B OE1  1 
ATOM   4434 O  OE2  A GLU   B 1 26  ? 49.861 -26.595 -15.205 0.50 17.86 -1 26   GLU   B OE2  1 
ATOM   4435 O  OE2  B GLU   B 1 26  ? 49.632 -25.672 -15.530 0.50 17.84 -1 26   GLU   B OE2  1 
ATOM   4436 H  H    A GLU   B 1 26  ? 51.879 -24.895 -11.572 0.50 15.21 ?  26   GLU   B H    1 
ATOM   4437 H  H    B GLU   B 1 26  ? 51.883 -24.911 -11.578 0.50 15.72 ?  26   GLU   B H    1 
ATOM   4438 H  HA   A GLU   B 1 26  ? 51.090 -24.100 -13.928 0.50 15.68 ?  26   GLU   B HA   1 
ATOM   4439 H  HA   B GLU   B 1 26  ? 51.067 -24.115 -13.919 0.50 16.54 ?  26   GLU   B HA   1 
ATOM   4440 H  HB2  A GLU   B 1 26  ? 49.719 -24.502 -11.513 0.50 17.04 ?  26   GLU   B HB2  1 
ATOM   4441 H  HB2  B GLU   B 1 26  ? 49.798 -24.726 -11.538 0.50 18.52 ?  26   GLU   B HB2  1 
ATOM   4442 H  HB3  A GLU   B 1 26  ? 48.947 -23.846 -12.735 0.50 17.04 ?  26   GLU   B HB3  1 
ATOM   4443 H  HB3  B GLU   B 1 26  ? 48.987 -23.744 -12.478 0.50 18.52 ?  26   GLU   B HB3  1 
ATOM   4444 H  HG2  A GLU   B 1 26  ? 50.108 -26.386 -12.814 0.50 19.26 ?  26   GLU   B HG2  1 
ATOM   4445 H  HG2  B GLU   B 1 26  ? 49.755 -26.350 -13.190 0.50 21.04 ?  26   GLU   B HG2  1 
ATOM   4446 H  HG3  A GLU   B 1 26  ? 48.554 -26.127 -12.595 0.50 19.26 ?  26   GLU   B HG3  1 
ATOM   4447 H  HG3  B GLU   B 1 26  ? 48.277 -25.915 -12.806 0.50 21.04 ?  26   GLU   B HG3  1 
ATOM   4448 N  N    . ALA   B 1 27  ? 51.071 -21.792 -11.700 1.00 11.96 ?  27   ALA   B N    1 
ATOM   4449 C  CA   . ALA   B 1 27  ? 51.029 -20.342 -11.546 1.00 12.29 ?  27   ALA   B CA   1 
ATOM   4450 C  C    . ALA   B 1 27  ? 52.100 -19.673 -12.394 1.00 13.27 ?  27   ALA   B C    1 
ATOM   4451 O  O    . ALA   B 1 27  ? 51.841 -18.664 -13.066 1.00 13.85 ?  27   ALA   B O    1 
ATOM   4452 C  CB   . ALA   B 1 27  ? 51.175 -19.961 -10.074 1.00 12.37 ?  27   ALA   B CB   1 
ATOM   4453 H  H    A ALA   B 1 27  ? 51.187 -22.231 -10.970 0.50 14.35 ?  27   ALA   B H    1 
ATOM   4454 H  H    B ALA   B 1 27  ? 51.191 -22.229 -10.969 0.50 14.35 ?  27   ALA   B H    1 
ATOM   4455 H  HA   . ALA   B 1 27  ? 50.171 -20.017 -11.851 1.00 14.75 ?  27   ALA   B HA   1 
ATOM   4456 H  HB1  . ALA   B 1 27  ? 51.135 -18.995 -9.990  1.00 14.84 ?  27   ALA   B HB1  1 
ATOM   4457 H  HB2  . ALA   B 1 27  ? 50.445 -20.363 -9.572  1.00 14.84 ?  27   ALA   B HB2  1 
ATOM   4458 H  HB3  . ALA   B 1 27  ? 52.023 -20.288 -9.741  1.00 14.84 ?  27   ALA   B HB3  1 
ATOM   4459 N  N    . LYS   B 1 28  ? 53.312 -20.226 -12.387 1.00 14.69 ?  28   LYS   B N    1 
ATOM   4460 C  CA   . LYS   B 1 28  ? 54.391 -19.605 -13.145 1.00 17.01 ?  28   LYS   B CA   1 
ATOM   4461 C  C    . LYS   B 1 28  ? 54.139 -19.672 -14.646 1.00 18.04 ?  28   LYS   B C    1 
ATOM   4462 O  O    . LYS   B 1 28  ? 54.565 -18.773 -15.382 1.00 19.11 ?  28   LYS   B O    1 
ATOM   4463 C  CB   . LYS   B 1 28  ? 55.742 -20.215 -12.751 1.00 19.71 ?  28   LYS   B CB   1 
ATOM   4464 C  CG   . LYS   B 1 28  ? 56.141 -19.885 -11.314 1.00 22.39 ?  28   LYS   B CG   1 
ATOM   4465 C  CD   . LYS   B 1 28  ? 57.576 -20.266 -10.985 1.00 26.37 ?  28   LYS   B CD   1 
ATOM   4466 C  CE   . LYS   B 1 28  ? 57.702 -21.730 -10.641 1.00 29.33 ?  28   LYS   B CE   1 
ATOM   4467 N  NZ   . LYS   B 1 28  ? 59.050 -22.042 -10.090 1.00 30.14 ?  28   LYS   B NZ   1 
ATOM   4468 H  H    . LYS   B 1 28  ? 53.535 -20.938 -11.958 1.00 17.62 ?  28   LYS   B H    1 
ATOM   4469 H  HA   . LYS   B 1 28  ? 54.430 -18.667 -12.910 1.00 20.41 ?  28   LYS   B HA   1 
ATOM   4470 H  HB2  . LYS   B 1 28  ? 55.699 -21.178 -12.831 1.00 23.65 ?  28   LYS   B HB2  1 
ATOM   4471 H  HB3  . LYS   B 1 28  ? 56.436 -19.863 -13.335 1.00 23.65 ?  28   LYS   B HB3  1 
ATOM   4472 H  HG2  . LYS   B 1 28  ? 56.044 -18.928 -11.174 1.00 26.87 ?  28   LYS   B HG2  1 
ATOM   4473 H  HG3  . LYS   B 1 28  ? 55.554 -20.366 -10.709 1.00 26.87 ?  28   LYS   B HG3  1 
ATOM   4474 H  HD2  . LYS   B 1 28  ? 58.136 -20.083 -11.754 1.00 31.65 ?  28   LYS   B HD2  1 
ATOM   4475 H  HD3  . LYS   B 1 28  ? 57.873 -19.745 -10.222 1.00 31.65 ?  28   LYS   B HD3  1 
ATOM   4476 H  HE2  . LYS   B 1 28  ? 57.038 -21.961 -9.971  1.00 35.20 ?  28   LYS   B HE2  1 
ATOM   4477 H  HE3  . LYS   B 1 28  ? 57.568 -22.262 -11.441 1.00 35.20 ?  28   LYS   B HE3  1 
ATOM   4478 H  HZ1  . LYS   B 1 28  ? 59.107 -22.908 -9.892  1.00 36.17 ?  28   LYS   B HZ1  1 
ATOM   4479 H  HZ2  . LYS   B 1 28  ? 59.677 -21.840 -10.688 1.00 36.17 ?  28   LYS   B HZ2  1 
ATOM   4480 H  HZ3  . LYS   B 1 28  ? 59.194 -21.568 -9.350  1.00 36.17 ?  28   LYS   B HZ3  1 
ATOM   4481 N  N    A LYS   B 1 29  ? 53.434 -20.703 -15.117 0.50 18.85 ?  29   LYS   B N    1 
ATOM   4482 N  N    B LYS   B 1 29  ? 53.439 -20.703 -15.115 0.50 18.78 ?  29   LYS   B N    1 
ATOM   4483 C  CA   A LYS   B 1 29  ? 53.150 -20.853 -16.542 0.50 20.93 ?  29   LYS   B CA   1 
ATOM   4484 C  CA   B LYS   B 1 29  ? 53.154 -20.826 -16.539 0.50 20.81 ?  29   LYS   B CA   1 
ATOM   4485 C  C    A LYS   B 1 29  ? 51.889 -20.115 -16.983 0.50 20.15 ?  29   LYS   B C    1 
ATOM   4486 C  C    B LYS   B 1 29  ? 51.909 -20.048 -16.952 0.50 20.02 ?  29   LYS   B C    1 
ATOM   4487 O  O    A LYS   B 1 29  ? 51.866 -19.538 -18.076 0.50 21.02 ?  29   LYS   B O    1 
ATOM   4488 O  O    B LYS   B 1 29  ? 51.928 -19.354 -17.975 0.50 20.87 ?  29   LYS   B O    1 
ATOM   4489 C  CB   A LYS   B 1 29  ? 53.023 -22.336 -16.907 0.50 24.35 ?  29   LYS   B CB   1 
ATOM   4490 C  CB   B LYS   B 1 29  ? 53.009 -22.304 -16.917 0.50 24.20 ?  29   LYS   B CB   1 
ATOM   4491 C  CG   A LYS   B 1 29  ? 52.766 -22.584 -18.388 0.50 27.45 ?  29   LYS   B CG   1 
ATOM   4492 C  CG   B LYS   B 1 29  ? 52.873 -22.557 -18.409 0.50 27.28 ?  29   LYS   B CG   1 
ATOM   4493 C  CD   A LYS   B 1 29  ? 52.982 -24.043 -18.764 0.50 29.84 ?  29   LYS   B CD   1 
ATOM   4494 C  CD   B LYS   B 1 29  ? 53.133 -24.018 -18.755 0.50 29.64 ?  29   LYS   B CD   1 
ATOM   4495 C  CE   A LYS   B 1 29  ? 51.912 -24.945 -18.173 0.50 31.47 ?  29   LYS   B CE   1 
ATOM   4496 C  CE   B LYS   B 1 29  ? 52.090 -24.943 -18.144 0.50 31.24 ?  29   LYS   B CE   1 
ATOM   4497 N  NZ   A LYS   B 1 29  ? 52.126 -26.370 -18.555 0.50 32.49 ?  29   LYS   B NZ   1 
ATOM   4498 N  NZ   B LYS   B 1 29  ? 52.333 -26.368 -18.511 0.50 32.24 ?  29   LYS   B NZ   1 
ATOM   4499 H  H    A LYS   B 1 29  ? 53.113 -21.334 -14.625 0.50 22.62 ?  29   LYS   B H    1 
ATOM   4500 H  H    B LYS   B 1 29  ? 53.116 -21.339 -14.629 0.50 22.53 ?  29   LYS   B H    1 
ATOM   4501 H  HA   A LYS   B 1 29  ? 53.893 -20.490 -17.043 0.50 25.12 ?  29   LYS   B HA   1 
ATOM   4502 H  HA   B LYS   B 1 29  ? 53.900 -20.466 -17.036 0.50 24.97 ?  29   LYS   B HA   1 
ATOM   4503 H  HB2  A LYS   B 1 29  ? 53.849 -22.789 -16.672 0.50 29.22 ?  29   LYS   B HB2  1 
ATOM   4504 H  HB2  B LYS   B 1 29  ? 53.798 -22.780 -16.610 0.50 29.05 ?  29   LYS   B HB2  1 
ATOM   4505 H  HB3  A LYS   B 1 29  ? 52.285 -22.722 -16.411 0.50 29.22 ?  29   LYS   B HB3  1 
ATOM   4506 H  HB3  B LYS   B 1 29  ? 52.221 -22.663 -16.484 0.50 29.05 ?  29   LYS   B HB3  1 
ATOM   4507 H  HG2  A LYS   B 1 29  ? 51.847 -22.352 -18.597 0.50 32.94 ?  29   LYS   B HG2  1 
ATOM   4508 H  HG2  B LYS   B 1 29  ? 51.972 -22.334 -18.689 0.50 32.74 ?  29   LYS   B HG2  1 
ATOM   4509 H  HG3  A LYS   B 1 29  ? 53.376 -22.042 -18.914 0.50 32.94 ?  29   LYS   B HG3  1 
ATOM   4510 H  HG3  B LYS   B 1 29  ? 53.518 -22.012 -18.887 0.50 32.74 ?  29   LYS   B HG3  1 
ATOM   4511 H  HD2  A LYS   B 1 29  ? 52.954 -24.133 -19.730 0.50 35.81 ?  29   LYS   B HD2  1 
ATOM   4512 H  HD2  B LYS   B 1 29  ? 53.107 -24.127 -19.718 0.50 35.57 ?  29   LYS   B HD2  1 
ATOM   4513 H  HD3  A LYS   B 1 29  ? 53.844 -24.336 -18.427 0.50 35.81 ?  29   LYS   B HD3  1 
ATOM   4514 H  HD3  B LYS   B 1 29  ? 54.003 -24.276 -18.412 0.50 35.57 ?  29   LYS   B HD3  1 
ATOM   4515 H  HE2  A LYS   B 1 29  ? 51.938 -24.883 -17.205 0.50 37.77 ?  29   LYS   B HE2  1 
ATOM   4516 H  HE2  B LYS   B 1 29  ? 52.122 -24.872 -17.177 0.50 37.49 ?  29   LYS   B HE2  1 
ATOM   4517 H  HE3  A LYS   B 1 29  ? 51.043 -24.669 -18.504 0.50 37.77 ?  29   LYS   B HE3  1 
ATOM   4518 H  HE3  B LYS   B 1 29  ? 51.210 -24.692 -18.469 0.50 37.49 ?  29   LYS   B HE3  1 
ATOM   4519 H  HZ1  A LYS   B 1 29  ? 51.489 -26.880 -18.199 0.50 38.99 ?  29   LYS   B HZ1  1 
ATOM   4520 H  HZ1  B LYS   B 1 29  ? 51.711 -26.889 -18.144 0.50 38.69 ?  29   LYS   B HZ1  1 
ATOM   4521 H  HZ2  A LYS   B 1 29  ? 52.102 -26.455 -19.441 0.50 38.99 ?  29   LYS   B HZ2  1 
ATOM   4522 H  HZ2  B LYS   B 1 29  ? 52.303 -26.464 -19.396 0.50 38.69 ?  29   LYS   B HZ2  1 
ATOM   4523 H  HZ3  A LYS   B 1 29  ? 52.918 -26.649 -18.259 0.50 38.99 ?  29   LYS   B HZ3  1 
ATOM   4524 H  HZ3  B LYS   B 1 29  ? 53.134 -26.625 -18.220 0.50 38.69 ?  29   LYS   B HZ3  1 
ATOM   4525 N  N    . VAL   B 1 30  ? 50.834 -20.142 -16.165 1.00 18.90 ?  30   VAL   B N    1 
ATOM   4526 C  CA   . VAL   B 1 30  ? 49.553 -19.533 -16.543 1.00 18.93 ?  30   VAL   B CA   1 
ATOM   4527 C  C    . VAL   B 1 30  ? 49.557 -18.020 -16.368 1.00 17.99 ?  30   VAL   B C    1 
ATOM   4528 O  O    . VAL   B 1 30  ? 48.812 -17.302 -17.052 1.00 18.79 ?  30   VAL   B O    1 
ATOM   4529 C  CB   . VAL   B 1 30  ? 48.441 -20.163 -15.679 1.00 20.11 ?  30   VAL   B CB   1 
ATOM   4530 C  CG1  . VAL   B 1 30  ? 47.146 -19.356 -15.752 1.00 20.32 ?  30   VAL   B CG1  1 
ATOM   4531 C  CG2  . VAL   B 1 30  ? 48.207 -21.612 -16.080 1.00 20.93 ?  30   VAL   B CG2  1 
ATOM   4532 H  H    A VAL   B 1 30  ? 50.828 -20.519 -15.385 0.50 22.68 ?  30   VAL   B H    1 
ATOM   4533 H  H    B VAL   B 1 30  ? 50.815 -20.566 -15.409 0.50 22.68 ?  30   VAL   B H    1 
ATOM   4534 H  HA   . VAL   B 1 30  ? 49.362 -19.751 -17.472 1.00 22.71 ?  30   VAL   B HA   1 
ATOM   4535 H  HB   . VAL   B 1 30  ? 48.727 -20.170 -14.753 1.00 24.13 ?  30   VAL   B HB   1 
ATOM   4536 H  HG11 . VAL   B 1 30  ? 46.404 -19.939 -15.525 1.00 24.38 ?  30   VAL   B HG11 1 
ATOM   4537 H  HG12 . VAL   B 1 30  ? 47.191 -18.625 -15.119 1.00 24.38 ?  30   VAL   B HG12 1 
ATOM   4538 H  HG13 . VAL   B 1 30  ? 47.029 -19.023 -16.651 1.00 24.38 ?  30   VAL   B HG13 1 
ATOM   4539 H  HG21 . VAL   B 1 30  ? 47.508 -21.990 -15.519 1.00 25.11 ?  30   VAL   B HG21 1 
ATOM   4540 H  HG22 . VAL   B 1 30  ? 47.931 -21.641 -17.010 1.00 25.11 ?  30   VAL   B HG22 1 
ATOM   4541 H  HG23 . VAL   B 1 30  ? 49.029 -22.109 -15.962 1.00 25.11 ?  30   VAL   B HG23 1 
ATOM   4542 N  N    . LYS   B 1 31  ? 50.340 -17.527 -15.423 1.00 17.73 ?  31   LYS   B N    1 
ATOM   4543 C  CA   . LYS   B 1 31  ? 50.356 -16.121 -15.055 1.00 18.37 ?  31   LYS   B CA   1 
ATOM   4544 C  C    . LYS   B 1 31  ? 48.951 -15.656 -14.669 1.00 15.91 ?  31   LYS   B C    1 
ATOM   4545 O  O    . LYS   B 1 31  ? 48.406 -14.734 -15.290 1.00 17.18 ?  31   LYS   B O    1 
ATOM   4546 C  CB   . LYS   B 1 31  ? 50.982 -15.299 -16.188 1.00 21.82 ?  31   LYS   B CB   1 
ATOM   4547 C  CG   . LYS   B 1 31  ? 52.409 -15.746 -16.519 1.00 25.33 ?  31   LYS   B CG   1 
ATOM   4548 C  CD   . LYS   B 1 31  ? 52.996 -14.988 -17.695 1.00 28.51 ?  31   LYS   B CD   1 
ATOM   4549 C  CE   . LYS   B 1 31  ? 54.486 -15.232 -17.817 1.00 30.72 ?  31   LYS   B CE   1 
ATOM   4550 N  NZ   . LYS   B 1 31  ? 55.189 -14.815 -16.574 1.00 32.22 ?  31   LYS   B NZ   1 
ATOM   4551 H  H    . LYS   B 1 31  ? 50.888 -18.017 -14.976 1.00 21.27 ?  31   LYS   B H    1 
ATOM   4552 H  HA   . LYS   B 1 31  ? 50.910 -16.035 -14.279 1.00 22.04 ?  31   LYS   B HA   1 
ATOM   4553 H  HB2  . LYS   B 1 31  ? 50.443 -15.395 -16.991 1.00 26.19 ?  31   LYS   B HB2  1 
ATOM   4554 H  HB3  . LYS   B 1 31  ? 51.011 -14.373 -15.914 1.00 26.19 ?  31   LYS   B HB3  1 
ATOM   4555 H  HG2  . LYS   B 1 31  ? 52.963 -15.599 -15.738 1.00 30.40 ?  31   LYS   B HG2  1 
ATOM   4556 H  HG3  . LYS   B 1 31  ? 52.396 -16.694 -16.741 1.00 30.40 ?  31   LYS   B HG3  1 
ATOM   4557 H  HD2  . LYS   B 1 31  ? 52.566 -15.289 -18.510 1.00 34.21 ?  31   LYS   B HD2  1 
ATOM   4558 H  HD3  . LYS   B 1 31  ? 52.847 -14.041 -17.563 1.00 34.21 ?  31   LYS   B HD3  1 
ATOM   4559 H  HE2  . LYS   B 1 31  ? 54.654 -16.179 -17.960 1.00 36.86 ?  31   LYS   B HE2  1 
ATOM   4560 H  HE3  . LYS   B 1 31  ? 54.841 -14.713 -18.557 1.00 36.86 ?  31   LYS   B HE3  1 
ATOM   4561 H  HZ1  . LYS   B 1 31  ? 56.067 -14.794 -16.712 1.00 38.67 ?  31   LYS   B HZ1  1 
ATOM   4562 H  HZ2  . LYS   B 1 31  ? 54.913 -14.005 -16.329 1.00 38.67 ?  31   LYS   B HZ2  1 
ATOM   4563 H  HZ3  . LYS   B 1 31  ? 55.013 -15.391 -15.918 1.00 38.67 ?  31   LYS   B HZ3  1 
ATOM   4564 N  N    . PRO   B 1 32  ? 48.339 -16.262 -13.644 1.00 13.29 ?  32   PRO   B N    1 
ATOM   4565 C  CA   . PRO   B 1 32  ? 46.957 -15.905 -13.296 1.00 12.21 ?  32   PRO   B CA   1 
ATOM   4566 C  C    . PRO   B 1 32  ? 46.875 -14.559 -12.594 1.00 12.19 ?  32   PRO   B C    1 
ATOM   4567 O  O    . PRO   B 1 32  ? 47.793 -14.143 -11.882 1.00 13.78 ?  32   PRO   B O    1 
ATOM   4568 C  CB   . PRO   B 1 32  ? 46.549 -17.022 -12.331 1.00 12.46 ?  32   PRO   B CB   1 
ATOM   4569 C  CG   . PRO   B 1 32  ? 47.845 -17.360 -11.643 1.00 12.79 ?  32   PRO   B CG   1 
ATOM   4570 C  CD   . PRO   B 1 32  ? 48.902 -17.253 -12.705 1.00 13.11 ?  32   PRO   B CD   1 
ATOM   4571 H  HA   . PRO   B 1 32  ? 46.379 -15.917 -14.080 1.00 14.65 ?  32   PRO   B HA   1 
ATOM   4572 H  HB2  . PRO   B 1 32  ? 45.893 -16.694 -11.694 1.00 14.95 ?  32   PRO   B HB2  1 
ATOM   4573 H  HB3  . PRO   B 1 32  ? 46.208 -17.785 -12.822 1.00 14.95 ?  32   PRO   B HB3  1 
ATOM   4574 H  HG2  . PRO   B 1 32  ? 48.016 -16.721 -10.930 1.00 15.35 ?  32   PRO   B HG2  1 
ATOM   4575 H  HG3  . PRO   B 1 32  ? 47.810 -18.261 -11.291 1.00 15.35 ?  32   PRO   B HG3  1 
ATOM   4576 H  HD2  . PRO   B 1 32  ? 49.730 -16.920 -12.324 1.00 15.73 ?  32   PRO   B HD2  1 
ATOM   4577 H  HD3  . PRO   B 1 32  ? 49.024 -18.105 -13.144 1.00 15.73 ?  32   PRO   B HD3  1 
ATOM   4578 N  N    . THR   B 1 33  ? 45.723 -13.904 -12.763 1.00 11.72 ?  33   THR   B N    1 
ATOM   4579 C  CA   . THR   B 1 33  ? 45.426 -12.731 -11.951 1.00 12.14 ?  33   THR   B CA   1 
ATOM   4580 C  C    . THR   B 1 33  ? 45.381 -13.085 -10.470 1.00 11.55 ?  33   THR   B C    1 
ATOM   4581 O  O    . THR   B 1 33  ? 45.855 -12.309 -9.628  1.00 12.86 ?  33   THR   B O    1 
ATOM   4582 C  CB   . THR   B 1 33  ? 44.104 -12.104 -12.394 1.00 12.76 ?  33   THR   B CB   1 
ATOM   4583 O  OG1  . THR   B 1 33  ? 44.145 -11.846 -13.799 1.00 12.97 ?  33   THR   B OG1  1 
ATOM   4584 C  CG2  . THR   B 1 33  ? 43.848 -10.807 -11.645 1.00 14.09 ?  33   THR   B CG2  1 
ATOM   4585 H  H    . THR   B 1 33  ? 45.100 -14.125 -13.323 1.00 14.06 ?  33   THR   B H    1 
ATOM   4586 H  HA   . THR   B 1 33  ? 46.124 -12.076 -12.080 1.00 14.57 ?  33   THR   B HA   1 
ATOM   4587 H  HB   . THR   B 1 33  ? 43.373 -12.717 -12.201 1.00 15.31 ?  33   THR   B HB   1 
ATOM   4588 H  HG1  . THR   B 1 33  ? 43.420 -11.488 -14.050 1.00 15.56 ?  33   THR   B HG1  1 
ATOM   4589 H  HG21 . THR   B 1 33  ? 43.095 -10.342 -12.035 1.00 16.91 ?  33   THR   B HG21 1 
ATOM   4590 H  HG22 . THR   B 1 33  ? 43.656 -10.995 -10.712 1.00 16.91 ?  33   THR   B HG22 1 
ATOM   4591 H  HG23 . THR   B 1 33  ? 44.633 -10.239 -11.697 1.00 16.91 ?  33   THR   B HG23 1 
ATOM   4592 N  N    . VAL   B 1 34  ? 44.832 -14.257 -10.133 1.00 11.05 ?  34   VAL   B N    1 
ATOM   4593 C  CA   . VAL   B 1 34  ? 44.646 -14.660 -8.743  1.00 10.42 ?  34   VAL   B CA   1 
ATOM   4594 C  C    . VAL   B 1 34  ? 45.077 -16.108 -8.580  1.00 9.67  ?  34   VAL   B C    1 
ATOM   4595 O  O    . VAL   B 1 34  ? 44.554 -16.997 -9.261  1.00 10.41 ?  34   VAL   B O    1 
ATOM   4596 C  CB   . VAL   B 1 34  ? 43.178 -14.519 -8.285  1.00 11.38 ?  34   VAL   B CB   1 
ATOM   4597 C  CG1  . VAL   B 1 34  ? 43.021 -14.988 -6.838  1.00 11.92 ?  34   VAL   B CG1  1 
ATOM   4598 C  CG2  . VAL   B 1 34  ? 42.675 -13.095 -8.462  1.00 12.50 ?  34   VAL   B CG2  1 
ATOM   4599 H  H    . VAL   B 1 34  ? 44.567 -14.850 -10.702 1.00 13.26 ?  34   VAL   B H    1 
ATOM   4600 H  HA   . VAL   B 1 34  ? 45.202 -14.110 -8.167  1.00 12.51 ?  34   VAL   B HA   1 
ATOM   4601 H  HB   . VAL   B 1 34  ? 42.626 -15.096 -8.839  1.00 13.65 ?  34   VAL   B HB   1 
ATOM   4602 H  HG11 . VAL   B 1 34  ? 42.168 -14.676 -6.495  1.00 14.30 ?  34   VAL   B HG11 1 
ATOM   4603 H  HG12 . VAL   B 1 34  ? 43.048 -15.959 -6.809  1.00 14.30 ?  34   VAL   B HG12 1 
ATOM   4604 H  HG13 . VAL   B 1 34  ? 43.743 -14.621 -6.306  1.00 14.30 ?  34   VAL   B HG13 1 
ATOM   4605 H  HG21 . VAL   B 1 34  ? 41.759 -13.044 -8.146  1.00 15.00 ?  34   VAL   B HG21 1 
ATOM   4606 H  HG22 . VAL   B 1 34  ? 43.239 -12.498 -7.952  1.00 15.00 ?  34   VAL   B HG22 1 
ATOM   4607 H  HG23 . VAL   B 1 34  ? 42.711 -12.866 -9.405  1.00 15.00 ?  34   VAL   B HG23 1 
ATOM   4608 N  N    . VAL   B 1 35  ? 45.988 -16.358 -7.644  1.00 9.17  ?  35   VAL   B N    1 
ATOM   4609 C  CA   . VAL   B 1 35  ? 46.228 -17.702 -7.132  1.00 9.08  ?  35   VAL   B CA   1 
ATOM   4610 C  C    . VAL   B 1 35  ? 45.688 -17.760 -5.711  1.00 8.82  ?  35   VAL   B C    1 
ATOM   4611 O  O    . VAL   B 1 35  ? 45.913 -16.839 -4.915  1.00 9.29  ?  35   VAL   B O    1 
ATOM   4612 C  CB   . VAL   B 1 35  ? 47.711 -18.126 -7.220  1.00 9.54  ?  35   VAL   B CB   1 
ATOM   4613 C  CG1  . VAL   B 1 35  ? 48.612 -17.288 -6.301  1.00 10.23 ?  35   VAL   B CG1  1 
ATOM   4614 C  CG2  . VAL   B 1 35  ? 47.859 -19.620 -6.914  1.00 10.33 ?  35   VAL   B CG2  1 
ATOM   4615 H  H    . VAL   B 1 35  ? 46.490 -15.757 -7.286  1.00 11.00 ?  35   VAL   B H    1 
ATOM   4616 H  HA   . VAL   B 1 35  ? 45.715 -18.331 -7.662  1.00 10.90 ?  35   VAL   B HA   1 
ATOM   4617 H  HB   . VAL   B 1 35  ? 48.013 -17.988 -8.136  1.00 11.45 ?  35   VAL   B HB   1 
ATOM   4618 H  HG11 . VAL   B 1 35  ? 49.537 -17.516 -6.478  1.00 12.28 ?  35   VAL   B HG11 1 
ATOM   4619 H  HG12 . VAL   B 1 35  ? 48.456 -16.352 -6.474  1.00 12.28 ?  35   VAL   B HG12 1 
ATOM   4620 H  HG13 . VAL   B 1 35  ? 48.393 -17.499 -5.376  1.00 12.28 ?  35   VAL   B HG13 1 
ATOM   4621 H  HG21 . VAL   B 1 35  ? 48.785 -19.881 -7.021  1.00 12.39 ?  35   VAL   B HG21 1 
ATOM   4622 H  HG22 . VAL   B 1 35  ? 47.572 -19.789 -5.999  1.00 12.39 ?  35   VAL   B HG22 1 
ATOM   4623 H  HG23 . VAL   B 1 35  ? 47.300 -20.133 -7.527  1.00 12.39 ?  35   VAL   B HG23 1 
ATOM   4624 N  N    . VAL   B 1 36  ? 44.968 -18.842 -5.394  1.00 8.83  ?  36   VAL   B N    1 
ATOM   4625 C  CA   . VAL   B 1 36  ? 44.427 -19.051 -4.061  1.00 8.36  ?  36   VAL   B CA   1 
ATOM   4626 C  C    . VAL   B 1 36  ? 45.437 -19.813 -3.213  1.00 8.29  ?  36   VAL   B C    1 
ATOM   4627 O  O    . VAL   B 1 36  ? 45.984 -20.843 -3.637  1.00 9.40  ?  36   VAL   B O    1 
ATOM   4628 C  CB   . VAL   B 1 36  ? 43.092 -19.808 -4.130  1.00 8.96  ?  36   VAL   B CB   1 
ATOM   4629 C  CG1  . VAL   B 1 36  ? 42.592 -20.162 -2.738  1.00 9.72  ?  36   VAL   B CG1  1 
ATOM   4630 C  CG2  . VAL   B 1 36  ? 42.060 -18.976 -4.883  1.00 9.67  ?  36   VAL   B CG2  1 
ATOM   4631 H  H    . VAL   B 1 36  ? 44.784 -19.478 -5.948  1.00 10.59 ?  36   VAL   B H    1 
ATOM   4632 H  HA   . VAL   B 1 36  ? 44.268 -18.192 -3.644  1.00 10.03 ?  36   VAL   B HA   1 
ATOM   4633 H  HB   . VAL   B 1 36  ? 43.222 -20.635 -4.616  1.00 10.75 ?  36   VAL   B HB   1 
ATOM   4634 H  HG11 . VAL   B 1 36  ? 41.653 -20.394 -2.790  1.00 11.66 ?  36   VAL   B HG11 1 
ATOM   4635 H  HG12 . VAL   B 1 36  ? 43.102 -20.904 -2.392  1.00 11.66 ?  36   VAL   B HG12 1 
ATOM   4636 H  HG13 . VAL   B 1 36  ? 42.701 -19.383 -2.159  1.00 11.66 ?  36   VAL   B HG13 1 
ATOM   4637 H  HG21 . VAL   B 1 36  ? 41.216 -19.454 -4.896  1.00 11.61 ?  36   VAL   B HG21 1 
ATOM   4638 H  HG22 . VAL   B 1 36  ? 41.954 -18.122 -4.442  1.00 11.61 ?  36   VAL   B HG22 1 
ATOM   4639 H  HG23 . VAL   B 1 36  ? 42.372 -18.840 -5.796  1.00 11.61 ?  36   VAL   B HG23 1 
ATOM   4640 N  N    . ASN   B 1 37  ? 45.661 -19.317 -1.999  1.00 8.49  ?  37   ASN   B N    1 
ATOM   4641 C  CA   . ASN   B 1 37  ? 46.412 -20.044 -0.990  1.00 8.75  ?  37   ASN   B CA   1 
ATOM   4642 C  C    . ASN   B 1 37  ? 45.464 -20.715 -0.004  1.00 8.75  ?  37   ASN   B C    1 
ATOM   4643 O  O    . ASN   B 1 37  ? 44.458 -20.136 0.412   1.00 9.35  ?  37   ASN   B O    1 
ATOM   4644 C  CB   . ASN   B 1 37  ? 47.344 -19.101 -0.232  1.00 8.98  ?  37   ASN   B CB   1 
ATOM   4645 C  CG   . ASN   B 1 37  ? 48.197 -19.818 0.780   1.00 9.13  ?  37   ASN   B CG   1 
ATOM   4646 O  OD1  . ASN   B 1 37  ? 48.544 -20.989 0.602   1.00 9.87  ?  37   ASN   B OD1  1 
ATOM   4647 N  ND2  . ASN   B 1 37  ? 48.551 -19.119 1.849   1.00 9.50  ?  37   ASN   B ND2  1 
ATOM   4648 H  H    . ASN   B 1 37  ? 45.391 -18.544 -1.730  1.00 10.18 ?  37   ASN   B H    1 
ATOM   4649 H  HA   . ASN   B 1 37  ? 46.948 -20.736 -1.410  1.00 10.50 ?  37   ASN   B HA   1 
ATOM   4650 H  HB2  . ASN   B 1 37  ? 47.935 -18.671 -0.864  1.00 10.77 ?  37   ASN   B HB2  1 
ATOM   4651 H  HB3  . ASN   B 1 37  ? 46.817 -18.445 0.243   1.00 10.77 ?  37   ASN   B HB3  1 
ATOM   4652 H  HD21 . ASN   B 1 37  ? 49.041 -19.482 2.458   1.00 11.40 ?  37   ASN   B HD21 1 
ATOM   4653 H  HD22 . ASN   B 1 37  ? 48.291 -18.311 1.939   1.00 11.40 ?  37   ASN   B HD22 1 
ATOM   4654 N  N    . ALA   B 1 38  ? 45.814 -21.947 0.374   1.00 8.98  ?  38   ALA   B N    1 
ATOM   4655 C  CA   . ALA   B 1 38  ? 45.171 -22.694 1.456   1.00 9.35  ?  38   ALA   B CA   1 
ATOM   4656 C  C    . ALA   B 1 38  ? 45.761 -22.211 2.779   1.00 9.15  ?  38   ALA   B C    1 
ATOM   4657 O  O    . ALA   B 1 38  ? 46.665 -22.818 3.361   1.00 10.14 ?  38   ALA   B O    1 
ATOM   4658 C  CB   . ALA   B 1 38  ? 45.396 -24.187 1.263   1.00 10.56 ?  38   ALA   B CB   1 
ATOM   4659 H  H    . ALA   B 1 38  ? 46.455 -22.388 0.010   1.00 10.78 ?  38   ALA   B H    1 
ATOM   4660 H  HA   . ALA   B 1 38  ? 44.216 -22.518 1.459   1.00 11.22 ?  38   ALA   B HA   1 
ATOM   4661 H  HB1  . ALA   B 1 38  ? 44.958 -24.669 1.993   1.00 12.68 ?  38   ALA   B HB1  1 
ATOM   4662 H  HB2  . ALA   B 1 38  ? 45.006 -24.459 0.419   1.00 12.68 ?  38   ALA   B HB2  1 
ATOM   4663 H  HB3  . ALA   B 1 38  ? 46.343 -24.373 1.273   1.00 12.68 ?  38   ALA   B HB3  1 
ATOM   4664 N  N    . ALA   B 1 39  ? 45.248 -21.067 3.238   1.00 9.15  ?  39   ALA   B N    1 
ATOM   4665 C  CA   . ALA   B 1 39  ? 45.797 -20.330 4.364   1.00 9.49  ?  39   ALA   B CA   1 
ATOM   4666 C  C    . ALA   B 1 39  ? 45.184 -20.779 5.690   1.00 9.56  ?  39   ALA   B C    1 
ATOM   4667 O  O    . ALA   B 1 39  ? 44.156 -21.457 5.742   1.00 10.34 ?  39   ALA   B O    1 
ATOM   4668 C  CB   . ALA   B 1 39  ? 45.544 -18.831 4.168   1.00 10.44 ?  39   ALA   B CB   1 
ATOM   4669 H  H    . ALA   B 1 39  ? 44.548 -20.694 2.900   1.00 10.98 ?  39   ALA   B H    1 
ATOM   4670 H  HA   . ALA   B 1 39  ? 46.753 -20.472 4.402   1.00 11.39 ?  39   ALA   B HA   1 
ATOM   4671 H  HB1  . ALA   B 1 39  ? 45.916 -18.345 4.921   1.00 12.53 ?  39   ALA   B HB1  1 
ATOM   4672 H  HB2  . ALA   B 1 39  ? 45.971 -18.541 3.345   1.00 12.53 ?  39   ALA   B HB2  1 
ATOM   4673 H  HB3  . ALA   B 1 39  ? 44.587 -18.673 4.115   1.00 12.53 ?  39   ALA   B HB3  1 
ATOM   4674 N  N    . ASN   B 1 40  ? 45.825 -20.354 6.775   1.00 10.39 ?  40   ASN   B N    1 
ATOM   4675 C  CA   . ASN   B 1 40  ? 45.263 -20.410 8.113   1.00 11.12 ?  40   ASN   B CA   1 
ATOM   4676 C  C    . ASN   B 1 40  ? 45.084 -18.984 8.641   1.00 10.64 ?  40   ASN   B C    1 
ATOM   4677 O  O    . ASN   B 1 40  ? 45.502 -18.006 8.011   1.00 10.72 ?  40   ASN   B O    1 
ATOM   4678 C  CB   . ASN   B 1 40  ? 46.115 -21.287 9.047   1.00 12.00 ?  40   ASN   B CB   1 
ATOM   4679 C  CG   . ASN   B 1 40  ? 47.574 -20.884 9.066   1.00 12.76 ?  40   ASN   B CG   1 
ATOM   4680 O  OD1  . ASN   B 1 40  ? 47.898 -19.703 9.132   1.00 14.92 ?  40   ASN   B OD1  1 
ATOM   4681 N  ND2  . ASN   B 1 40  ? 48.463 -21.862 9.015   1.00 13.09 ?  40   ASN   B ND2  1 
ATOM   4682 H  H    . ASN   B 1 40  ? 46.619 -20.015 6.754   1.00 12.47 ?  40   ASN   B H    1 
ATOM   4683 H  HA   . ASN   B 1 40  ? 44.384 -20.809 8.067   1.00 13.35 ?  40   ASN   B HA   1 
ATOM   4684 H  HB2  . ASN   B 1 40  ? 45.771 -21.214 9.953   1.00 14.39 ?  40   ASN   B HB2  1 
ATOM   4685 H  HB3  . ASN   B 1 40  ? 46.063 -22.209 8.748   1.00 14.39 ?  40   ASN   B HB3  1 
ATOM   4686 H  HD21 . ASN   B 1 40  ? 49.303 -21.681 9.026   1.00 15.71 ?  40   ASN   B HD21 1 
ATOM   4687 H  HD22 . ASN   B 1 40  ? 48.201 -22.681 8.967   1.00 15.71 ?  40   ASN   B HD22 1 
ATOM   4688 N  N    . VAL   B 1 41  ? 44.434 -18.859 9.801   1.00 11.02 ?  41   VAL   B N    1 
ATOM   4689 C  CA   . VAL   B 1 41  ? 43.979 -17.540 10.249  1.00 11.86 ?  41   VAL   B CA   1 
ATOM   4690 C  C    . VAL   B 1 41  ? 45.134 -16.591 10.548  1.00 11.62 ?  41   VAL   B C    1 
ATOM   4691 O  O    . VAL   B 1 41  ? 44.957 -15.370 10.468  1.00 11.89 ?  41   VAL   B O    1 
ATOM   4692 C  CB   . VAL   B 1 41  ? 43.003 -17.614 11.440  1.00 13.10 ?  41   VAL   B CB   1 
ATOM   4693 C  CG1  . VAL   B 1 41  ? 41.697 -18.285 11.030  1.00 13.65 ?  41   VAL   B CG1  1 
ATOM   4694 C  CG2  . VAL   B 1 41  ? 43.644 -18.304 12.629  1.00 14.06 ?  41   VAL   B CG2  1 
ATOM   4695 H  H    . VAL   B 1 41  ? 44.249 -19.502 10.334  1.00 13.22 ?  41   VAL   B H    1 
ATOM   4696 H  HA   . VAL   B 1 41  ? 43.482 -17.141 9.519   1.00 14.23 ?  41   VAL   B HA   1 
ATOM   4697 H  HB   . VAL   B 1 41  ? 42.786 -16.708 11.714  1.00 15.72 ?  41   VAL   B HB   1 
ATOM   4698 H  HG11 . VAL   B 1 41  ? 41.092 -18.290 11.791  1.00 16.38 ?  41   VAL   B HG11 1 
ATOM   4699 H  HG12 . VAL   B 1 41  ? 41.299 -17.786 10.299  1.00 16.38 ?  41   VAL   B HG12 1 
ATOM   4700 H  HG13 . VAL   B 1 41  ? 41.881 -19.193 10.750  1.00 16.38 ?  41   VAL   B HG13 1 
ATOM   4701 H  HG21 . VAL   B 1 41  ? 43.004 -18.330 13.358  1.00 16.88 ?  41   VAL   B HG21 1 
ATOM   4702 H  HG22 . VAL   B 1 41  ? 43.889 -19.208 12.374  1.00 16.88 ?  41   VAL   B HG22 1 
ATOM   4703 H  HG23 . VAL   B 1 41  ? 44.431 -17.809 12.896  1.00 16.88 ?  41   VAL   B HG23 1 
ATOM   4704 N  N    . TYR   B 1 42  ? 46.303 -17.106 10.930  1.00 12.00 ?  42   TYR   B N    1 
ATOM   4705 C  CA   . TYR   B 1 42  ? 47.459 -16.259 11.189  1.00 12.54 ?  42   TYR   B CA   1 
ATOM   4706 C  C    . TYR   B 1 42  ? 48.416 -16.186 10.004  1.00 11.74 ?  42   TYR   B C    1 
ATOM   4707 O  O    . TYR   B 1 42  ? 49.508 -15.619 10.132  1.00 12.56 ?  42   TYR   B O    1 
ATOM   4708 C  CB   . TYR   B 1 42  ? 48.169 -16.661 12.488  1.00 14.39 ?  42   TYR   B CB   1 
ATOM   4709 C  CG   . TYR   B 1 42  ? 47.563 -15.988 13.714  1.00 14.70 ?  42   TYR   B CG   1 
ATOM   4710 C  CD1  . TYR   B 1 42  ? 47.781 -14.635 13.961  1.00 13.79 ?  42   TYR   B CD1  1 
ATOM   4711 C  CD2  . TYR   B 1 42  ? 46.765 -16.690 14.604  1.00 16.41 ?  42   TYR   B CD2  1 
ATOM   4712 C  CE1  . TYR   B 1 42  ? 47.230 -14.005 15.059  1.00 14.84 ?  42   TYR   B CE1  1 
ATOM   4713 C  CE2  . TYR   B 1 42  ? 46.209 -16.066 15.710  1.00 16.69 ?  42   TYR   B CE2  1 
ATOM   4714 C  CZ   . TYR   B 1 42  ? 46.446 -14.721 15.933  1.00 16.57 ?  42   TYR   B CZ   1 
ATOM   4715 O  OH   . TYR   B 1 42  ? 45.904 -14.094 17.034  1.00 19.50 ?  42   TYR   B OH   1 
ATOM   4716 H  H    . TYR   B 1 42  ? 46.446 -17.952 11.038  1.00 14.40 ?  42   TYR   B H    1 
ATOM   4717 H  HA   . TYR   B 1 42  ? 47.133 -15.361 11.327  1.00 15.05 ?  42   TYR   B HA   1 
ATOM   4718 H  HB2  . TYR   B 1 42  ? 48.097 -17.621 12.606  1.00 17.27 ?  42   TYR   B HB2  1 
ATOM   4719 H  HB3  . TYR   B 1 42  ? 49.102 -16.402 12.430  1.00 17.27 ?  42   TYR   B HB3  1 
ATOM   4720 H  HD1  . TYR   B 1 42  ? 48.316 -14.147 13.368  1.00 16.55 ?  42   TYR   B HD1  1 
ATOM   4721 H  HD2  . TYR   B 1 42  ? 46.600 -17.593 14.453  1.00 19.69 ?  42   TYR   B HD2  1 
ATOM   4722 H  HE1  . TYR   B 1 42  ? 47.395 -13.102 15.208  1.00 17.81 ?  42   TYR   B HE1  1 
ATOM   4723 H  HE2  . TYR   B 1 42  ? 45.675 -16.550 16.297  1.00 20.02 ?  42   TYR   B HE2  1 
ATOM   4724 H  HH   . TYR   B 1 42  ? 46.128 -13.288 17.038  1.00 23.41 ?  42   TYR   B HH   1 
ATOM   4725 N  N    . LEU   B 1 43  ? 48.014 -16.703 8.845   1.00 10.38 ?  43   LEU   B N    1 
ATOM   4726 C  CA   . LEU   B 1 43  ? 48.828 -16.629 7.636   1.00 10.35 ?  43   LEU   B CA   1 
ATOM   4727 C  C    . LEU   B 1 43  ? 50.243 -17.137 7.892   1.00 10.88 ?  43   LEU   B C    1 
ATOM   4728 O  O    . LEU   B 1 43  ? 51.222 -16.540 7.444   1.00 11.57 ?  43   LEU   B O    1 
ATOM   4729 C  CB   . LEU   B 1 43  ? 48.851 -15.219 7.039   1.00 10.53 ?  43   LEU   B CB   1 
ATOM   4730 C  CG   . LEU   B 1 43  ? 47.493 -14.612 6.671   1.00 10.83 ?  43   LEU   B CG   1 
ATOM   4731 C  CD1  . LEU   B 1 43  ? 47.704 -13.219 6.092   1.00 12.17 ?  43   LEU   B CD1  1 
ATOM   4732 C  CD2  . LEU   B 1 43  ? 46.720 -15.491 5.699   1.00 10.94 ?  43   LEU   B CD2  1 
ATOM   4733 H  H    . LEU   B 1 43  ? 47.273 -17.128 8.738   1.00 12.45 ?  43   LEU   B H    1 
ATOM   4734 H  HA   . LEU   B 1 43  ? 48.433 -17.215 6.969   1.00 12.41 ?  43   LEU   B HA   1 
ATOM   4735 H  HB2  . LEU   B 1 43  ? 49.268 -14.626 7.681   1.00 12.64 ?  43   LEU   B HB2  1 
ATOM   4736 H  HB3  . LEU   B 1 43  ? 49.381 -15.245 6.228   1.00 12.64 ?  43   LEU   B HB3  1 
ATOM   4737 H  HG   . LEU   B 1 43  ? 46.960 -14.518 7.475   1.00 13.00 ?  43   LEU   B HG   1 
ATOM   4738 H  HD11 . LEU   B 1 43  ? 46.843 -12.833 5.862   1.00 14.61 ?  43   LEU   B HD11 1 
ATOM   4739 H  HD12 . LEU   B 1 43  ? 48.143 -12.661 6.759   1.00 14.61 ?  43   LEU   B HD12 1 
ATOM   4740 H  HD13 . LEU   B 1 43  ? 48.261 -13.281 5.301   1.00 14.61 ?  43   LEU   B HD13 1 
ATOM   4741 H  HD21 . LEU   B 1 43  ? 45.914 -15.022 5.420   1.00 13.13 ?  43   LEU   B HD21 1 
ATOM   4742 H  HD22 . LEU   B 1 43  ? 47.275 -15.676 4.927   1.00 13.13 ?  43   LEU   B HD22 1 
ATOM   4743 H  HD23 . LEU   B 1 43  ? 46.480 -16.319 6.143   1.00 13.13 ?  43   LEU   B HD23 1 
ATOM   4744 N  N    . LYS   B 1 44  ? 50.346 -18.258 8.609   1.00 10.76 ?  44   LYS   B N    1 
ATOM   4745 C  CA   . LYS   B 1 44  ? 51.616 -18.937 8.838   1.00 11.43 ?  44   LYS   B CA   1 
ATOM   4746 C  C    . LYS   B 1 44  ? 51.725 -20.049 7.804   1.00 10.92 ?  44   LYS   B C    1 
ATOM   4747 O  O    . LYS   B 1 44  ? 51.023 -21.061 7.888   1.00 12.11 ?  44   LYS   B O    1 
ATOM   4748 C  CB   . LYS   B 1 44  ? 51.682 -19.459 10.271  1.00 13.19 ?  44   LYS   B CB   1 
ATOM   4749 C  CG   . LYS   B 1 44  ? 51.834 -18.349 11.302  1.00 15.57 ?  44   LYS   B CG   1 
ATOM   4750 C  CD   . LYS   B 1 44  ? 53.037 -17.471 10.945  1.00 18.56 ?  44   LYS   B CD   1 
ATOM   4751 C  CE   . LYS   B 1 44  ? 53.481 -16.568 12.067  1.00 21.13 ?  44   LYS   B CE   1 
ATOM   4752 N  NZ   . LYS   B 1 44  ? 54.665 -15.755 11.687  1.00 22.49 ?  44   LYS   B NZ   1 
ATOM   4753 H  H    . LYS   B 1 44  ? 49.674 -18.645 8.984   1.00 12.91 ?  44   LYS   B H    1 
ATOM   4754 H  HA   . LYS   B 1 44  ? 52.344 -18.319 8.678   1.00 13.71 ?  44   LYS   B HA   1 
ATOM   4755 H  HB2  . LYS   B 1 44  ? 50.858 -19.937 10.470  1.00 15.83 ?  44   LYS   B HB2  1 
ATOM   4756 H  HB3  . LYS   B 1 44  ? 52.439 -20.054 10.355  1.00 15.83 ?  44   LYS   B HB3  1 
ATOM   4757 H  HG2  . LYS   B 1 44  ? 51.039 -17.798 11.312  1.00 18.69 ?  44   LYS   B HG2  1 
ATOM   4758 H  HG3  . LYS   B 1 44  ? 51.990 -18.741 12.179  1.00 18.69 ?  44   LYS   B HG3  1 
ATOM   4759 H  HD2  . LYS   B 1 44  ? 53.779 -18.050 10.694  1.00 22.27 ?  44   LYS   B HD2  1 
ATOM   4760 H  HD3  . LYS   B 1 44  ? 52.794 -16.907 10.194  1.00 22.27 ?  44   LYS   B HD3  1 
ATOM   4761 H  HE2  . LYS   B 1 44  ? 52.763 -15.956 12.264  1.00 25.35 ?  44   LYS   B HE2  1 
ATOM   4762 H  HE3  . LYS   B 1 44  ? 53.706 -17.104 12.844  1.00 25.35 ?  44   LYS   B HE3  1 
ATOM   4763 H  HZ1  . LYS   B 1 44  ? 54.902 -15.230 12.365  1.00 26.98 ?  44   LYS   B HZ1  1 
ATOM   4764 H  HZ2  . LYS   B 1 44  ? 55.347 -16.284 11.475  1.00 26.98 ?  44   LYS   B HZ2  1 
ATOM   4765 H  HZ3  . LYS   B 1 44  ? 54.468 -15.243 10.983  1.00 26.98 ?  44   LYS   B HZ3  1 
ATOM   4766 N  N    . HIS   B 1 45  ? 52.572 -19.829 6.801   1.00 10.84 ?  45   HIS   B N    1 
ATOM   4767 C  CA   . HIS   B 1 45  ? 52.586 -20.658 5.597   1.00 11.08 ?  45   HIS   B CA   1 
ATOM   4768 C  C    . HIS   B 1 45  ? 53.605 -21.781 5.748   1.00 13.15 ?  45   HIS   B C    1 
ATOM   4769 O  O    . HIS   B 1 45  ? 54.666 -21.787 5.135   1.00 15.26 ?  45   HIS   B O    1 
ATOM   4770 C  CB   . HIS   B 1 45  ? 52.899 -19.802 4.383   1.00 10.89 ?  45   HIS   B CB   1 
ATOM   4771 C  CG   . HIS   B 1 45  ? 52.032 -18.597 4.278   1.00 10.75 ?  45   HIS   B CG   1 
ATOM   4772 N  ND1  . HIS   B 1 45  ? 50.654 -18.670 4.255   1.00 10.84 ?  45   HIS   B ND1  1 
ATOM   4773 C  CD2  . HIS   B 1 45  ? 52.352 -17.284 4.202   1.00 11.36 ?  45   HIS   B CD2  1 
ATOM   4774 C  CE1  . HIS   B 1 45  ? 50.171 -17.445 4.149   1.00 10.43 ?  45   HIS   B CE1  1 
ATOM   4775 N  NE2  . HIS   B 1 45  ? 51.176 -16.588 4.119   1.00 10.96 ?  45   HIS   B NE2  1 
ATOM   4776 H  H    . HIS   B 1 45  ? 53.142 -19.186 6.784   1.00 13.01 ?  45   HIS   B H    1 
ATOM   4777 H  HA   . HIS   B 1 45  ? 51.708 -21.054 5.467   1.00 13.30 ?  45   HIS   B HA   1 
ATOM   4778 H  HB2  . HIS   B 1 45  ? 53.821 -19.512 4.429   1.00 13.07 ?  45   HIS   B HB2  1 
ATOM   4779 H  HB3  . HIS   B 1 45  ? 52.766 -20.341 3.578   1.00 13.07 ?  45   HIS   B HB3  1 
ATOM   4780 H  HD2  . HIS   B 1 45  ? 53.212 -16.921 4.198   1.00 13.63 ?  45   HIS   B HD2  1 
ATOM   4781 H  HE1  . HIS   B 1 45  ? 49.271 -17.226 4.105   1.00 12.52 ?  45   HIS   B HE1  1 
ATOM   4782 H  HE2  . HIS   B 1 45  ? 51.101 -15.732 4.061   1.00 13.15 ?  45   HIS   B HE2  1 
ATOM   4783 N  N    A GLY   B 1 46  ? 53.241 -22.762 6.570   0.50 13.93 ?  46   GLY   B N    1 
ATOM   4784 N  N    B GLY   B 1 46  ? 53.254 -22.746 6.588   0.50 13.78 ?  46   GLY   B N    1 
ATOM   4785 C  CA   A GLY   B 1 46  ? 54.170 -23.813 6.944   0.50 15.48 ?  46   GLY   B CA   1 
ATOM   4786 C  CA   B GLY   B 1 46  ? 54.181 -23.812 6.912   0.50 15.15 ?  46   GLY   B CA   1 
ATOM   4787 C  C    A GLY   B 1 46  ? 54.204 -25.046 6.062   0.50 16.91 ?  46   GLY   B C    1 
ATOM   4788 C  C    B GLY   B 1 46  ? 54.190 -24.970 5.936   0.50 16.57 ?  46   GLY   B C    1 
ATOM   4789 O  O    A GLY   B 1 46  ? 55.281 -25.501 5.666   0.50 18.71 ?  46   GLY   B O    1 
ATOM   4790 O  O    B GLY   B 1 46  ? 55.218 -25.275 5.324   0.50 17.67 ?  46   GLY   B O    1 
ATOM   4791 H  H    A GLY   B 1 46  ? 52.464 -22.822 6.943   0.50 16.72 ?  46   GLY   B H    1 
ATOM   4792 H  H    B GLY   B 1 46  ? 52.493 -22.793 6.995   0.50 16.53 ?  46   GLY   B H    1 
ATOM   4793 H  HA2  A GLY   B 1 46  ? 55.063 -23.437 6.968   0.50 18.57 ?  46   GLY   B HA2  1 
ATOM   4794 H  HA2  B GLY   B 1 46  ? 55.077 -23.442 6.951   0.50 18.18 ?  46   GLY   B HA2  1 
ATOM   4795 H  HA3  A GLY   B 1 46  ? 53.949 -24.113 7.838   0.50 18.57 ?  46   GLY   B HA3  1 
ATOM   4796 H  HA3  B GLY   B 1 46  ? 53.962 -24.158 7.791   0.50 18.18 ?  46   GLY   B HA3  1 
ATOM   4797 N  N    . GLY   B 1 47  ? 53.040 -25.619 5.765   1.00 16.70 ?  47   GLY   B N    1 
ATOM   4798 C  CA   . GLY   B 1 47  ? 52.967 -26.894 5.083   1.00 14.65 ?  47   GLY   B CA   1 
ATOM   4799 C  C    . GLY   B 1 47  ? 52.065 -26.866 3.865   1.00 12.65 ?  47   GLY   B C    1 
ATOM   4800 O  O    . GLY   B 1 47  ? 51.418 -25.862 3.567   1.00 12.68 ?  47   GLY   B O    1 
ATOM   4801 H  H    A GLY   B 1 47  ? 52.273 -25.292 5.976   0.50 20.04 ?  47   GLY   B H    1 
ATOM   4802 H  H    B GLY   B 1 47  ? 52.280 -25.332 6.047   0.50 20.04 ?  47   GLY   B H    1 
ATOM   4803 H  HA2  . GLY   B 1 47  ? 53.854 -27.163 4.795   1.00 17.58 ?  47   GLY   B HA2  1 
ATOM   4804 H  HA3  . GLY   B 1 47  ? 52.634 -27.565 5.700   1.00 17.58 ?  47   GLY   B HA3  1 
ATOM   4805 N  N    . GLY   B 1 48  ? 52.023 -28.005 3.175   1.00 11.65 ?  48   GLY   B N    1 
ATOM   4806 C  CA   . GLY   B 1 48  ? 51.093 -28.146 2.072   1.00 11.36 ?  48   GLY   B CA   1 
ATOM   4807 C  C    . GLY   B 1 48  ? 51.235 -27.034 1.056   1.00 10.73 ?  48   GLY   B C    1 
ATOM   4808 O  O    . GLY   B 1 48  ? 52.341 -26.571 0.744   1.00 11.37 ?  48   GLY   B O    1 
ATOM   4809 H  H    . GLY   B 1 48  ? 52.518 -28.689 3.321   1.00 13.98 ?  48   GLY   B H    1 
ATOM   4810 H  HA2  . GLY   B 1 48  ? 51.245 -28.992 1.626   1.00 13.63 ?  48   GLY   B HA2  1 
ATOM   4811 H  HA3  . GLY   B 1 48  ? 50.183 -28.136 2.412   1.00 13.63 ?  48   GLY   B HA3  1 
ATOM   4812 N  N    . VAL   B 1 49  ? 50.089 -26.603 0.524   1.00 10.79 ?  49   VAL   B N    1 
ATOM   4813 C  CA   . VAL   B 1 49  ? 50.076 -25.574 -0.513  1.00 10.85 ?  49   VAL   B CA   1 
ATOM   4814 C  C    . VAL   B 1 49  ? 50.737 -24.290 -0.019  1.00 10.01 ?  49   VAL   B C    1 
ATOM   4815 O  O    . VAL   B 1 49  ? 51.520 -23.667 -0.744  1.00 10.66 ?  49   VAL   B O    1 
ATOM   4816 C  CB   . VAL   B 1 49  ? 48.635 -25.318 -0.999  1.00 11.94 ?  49   VAL   B CB   1 
ATOM   4817 C  CG1  . VAL   B 1 49  ? 48.572 -24.062 -1.864  1.00 11.73 ?  49   VAL   B CG1  1 
ATOM   4818 C  CG2  . VAL   B 1 49  ? 48.098 -26.525 -1.758  1.00 13.60 ?  49   VAL   B CG2  1 
ATOM   4819 H  H    . VAL   B 1 49  ? 49.305 -26.885 0.746   1.00 12.95 ?  49   VAL   B H    1 
ATOM   4820 H  HA   . VAL   B 1 49  ? 50.586 -25.894 -1.273  1.00 13.02 ?  49   VAL   B HA   1 
ATOM   4821 H  HB   . VAL   B 1 49  ? 48.066 -25.175 -0.231  1.00 14.33 ?  49   VAL   B HB   1 
ATOM   4822 H  HG11 . VAL   B 1 49  ? 47.747 -24.071 -2.375  1.00 14.07 ?  49   VAL   B HG11 1 
ATOM   4823 H  HG12 . VAL   B 1 49  ? 48.592 -23.278 -1.290  1.00 14.07 ?  49   VAL   B HG12 1 
ATOM   4824 H  HG13 . VAL   B 1 49  ? 49.332 -24.050 -2.467  1.00 14.07 ?  49   VAL   B HG13 1 
ATOM   4825 H  HG21 . VAL   B 1 49  ? 47.193 -26.336 -2.051  1.00 16.32 ?  49   VAL   B HG21 1 
ATOM   4826 H  HG22 . VAL   B 1 49  ? 48.667 -26.689 -2.531  1.00 16.32 ?  49   VAL   B HG22 1 
ATOM   4827 H  HG23 . VAL   B 1 49  ? 48.107 -27.294 -1.172  1.00 16.32 ?  49   VAL   B HG23 1 
ATOM   4828 N  N    . ALA   B 1 50  ? 50.397 -23.849 1.197   1.00 9.87  ?  50   ALA   B N    1 
ATOM   4829 C  CA   . ALA   B 1 50  ? 50.914 -22.570 1.677   1.00 9.68  ?  50   ALA   B CA   1 
ATOM   4830 C  C    . ALA   B 1 50  ? 52.432 -22.601 1.782   1.00 10.05 ?  50   ALA   B C    1 
ATOM   4831 O  O    . ALA   B 1 50  ? 53.110 -21.631 1.424   1.00 10.13 ?  50   ALA   B O    1 
ATOM   4832 C  CB   . ALA   B 1 50  ? 50.287 -22.212 3.021   1.00 9.92  ?  50   ALA   B CB   1 
ATOM   4833 H  H    . ALA   B 1 50  ? 49.893 -24.267 1.749   1.00 11.84 ?  50   ALA   B H    1 
ATOM   4834 H  HA   . ALA   B 1 50  ? 50.685 -21.880 1.046   1.00 11.61 ?  50   ALA   B HA   1 
ATOM   4835 H  HB1  . ALA   B 1 50  ? 50.642 -21.361 3.320   1.00 11.90 ?  50   ALA   B HB1  1 
ATOM   4836 H  HB2  . ALA   B 1 50  ? 49.325 -22.149 2.909   1.00 11.90 ?  50   ALA   B HB2  1 
ATOM   4837 H  HB3  . ALA   B 1 50  ? 50.499 -22.905 3.667   1.00 11.90 ?  50   ALA   B HB3  1 
ATOM   4838 N  N    . GLY   B 1 51  ? 52.985 -23.698 2.291   1.00 10.28 ?  51   GLY   B N    1 
ATOM   4839 C  CA   . GLY   B 1 51  ? 54.431 -23.797 2.365   1.00 11.27 ?  51   GLY   B CA   1 
ATOM   4840 C  C    . GLY   B 1 51  ? 55.076 -23.746 0.995   1.00 10.90 ?  51   GLY   B C    1 
ATOM   4841 O  O    . GLY   B 1 51  ? 56.116 -23.108 0.810   1.00 11.79 ?  51   GLY   B O    1 
ATOM   4842 H  H    . GLY   B 1 51  ? 52.562 -24.384 2.595   1.00 12.34 ?  51   GLY   B H    1 
ATOM   4843 H  HA2  . GLY   B 1 51  ? 54.782 -23.062 2.898   1.00 13.52 ?  51   GLY   B HA2  1 
ATOM   4844 H  HA3  . GLY   B 1 51  ? 54.684 -24.631 2.793   1.00 13.52 ?  51   GLY   B HA3  1 
ATOM   4845 N  N    . ALA   B 1 52  ? 54.468 -24.412 0.015   1.00 10.70 ?  52   ALA   B N    1 
ATOM   4846 C  CA   . ALA   B 1 52  ? 55.026 -24.418 -1.331  1.00 10.93 ?  52   ALA   B CA   1 
ATOM   4847 C  C    . ALA   B 1 52  ? 54.944 -23.040 -1.981  1.00 10.36 ?  52   ALA   B C    1 
ATOM   4848 O  O    . ALA   B 1 52  ? 55.916 -22.587 -2.608  1.00 11.12 ?  52   ALA   B O    1 
ATOM   4849 C  CB   . ALA   B 1 52  ? 54.314 -25.457 -2.187  1.00 11.73 ?  52   ALA   B CB   1 
ATOM   4850 H  H    . ALA   B 1 52  ? 53.731 -24.851 0.103   1.00 12.84 ?  52   ALA   B H    1 
ATOM   4851 H  HA   . ALA   B 1 52  ? 55.960 -24.664 -1.276  1.00 13.12 ?  52   ALA   B HA   1 
ATOM   4852 H  HB1  . ALA   B 1 52  ? 54.703 -25.450 -3.077  1.00 14.07 ?  52   ALA   B HB1  1 
ATOM   4853 H  HB2  . ALA   B 1 52  ? 54.434 -26.333 -1.784  1.00 14.07 ?  52   ALA   B HB2  1 
ATOM   4854 H  HB3  . ALA   B 1 52  ? 53.372 -25.241 -2.235  1.00 14.07 ?  52   ALA   B HB3  1 
ATOM   4855 N  N    . LEU   B 1 53  ? 53.799 -22.362 -1.860  1.00 10.26 ?  53   LEU   B N    1 
ATOM   4856 C  CA   . LEU   B 1 53  ? 53.689 -21.024 -2.433  1.00 10.34 ?  53   LEU   B CA   1 
ATOM   4857 C  C    . LEU   B 1 53  ? 54.697 -20.084 -1.787  1.00 10.32 ?  53   LEU   B C    1 
ATOM   4858 O  O    . LEU   B 1 53  ? 55.396 -19.331 -2.475  1.00 11.03 ?  53   LEU   B O    1 
ATOM   4859 C  CB   . LEU   B 1 53  ? 52.267 -20.483 -2.260  1.00 10.57 ?  53   LEU   B CB   1 
ATOM   4860 C  CG   . LEU   B 1 53  ? 51.137 -21.211 -3.000  1.00 11.02 ?  53   LEU   B CG   1 
ATOM   4861 C  CD1  . LEU   B 1 53  ? 49.792 -20.596 -2.658  1.00 12.65 ?  53   LEU   B CD1  1 
ATOM   4862 C  CD2  . LEU   B 1 53  ? 51.352 -21.206 -4.505  1.00 12.93 ?  53   LEU   B CD2  1 
ATOM   4863 H  H    . LEU   B 1 53  ? 53.091 -22.648 -1.460  1.00 12.31 ?  53   LEU   B H    1 
ATOM   4864 H  HA   . LEU   B 1 53  ? 53.884 -21.071 -3.384  1.00 12.41 ?  53   LEU   B HA   1 
ATOM   4865 H  HB2  . LEU   B 1 53  ? 52.050 -20.515 -1.316  1.00 12.69 ?  53   LEU   B HB2  1 
ATOM   4866 H  HB3  . LEU   B 1 53  ? 52.256 -19.567 -2.564  1.00 12.69 ?  53   LEU   B HB3  1 
ATOM   4867 H  HG   . LEU   B 1 53  ? 51.111 -22.135 -2.707  1.00 13.22 ?  53   LEU   B HG   1 
ATOM   4868 H  HD11 . LEU   B 1 53  ? 49.091 -21.075 -3.134  1.00 15.18 ?  53   LEU   B HD11 1 
ATOM   4869 H  HD12 . LEU   B 1 53  ? 49.642 -20.672 -1.699  1.00 15.18 ?  53   LEU   B HD12 1 
ATOM   4870 H  HD13 . LEU   B 1 53  ? 49.790 -19.664 -2.918  1.00 15.18 ?  53   LEU   B HD13 1 
ATOM   4871 H  HD21 . LEU   B 1 53  ? 50.612 -21.659 -4.937  1.00 15.52 ?  53   LEU   B HD21 1 
ATOM   4872 H  HD22 . LEU   B 1 53  ? 51.405 -20.290 -4.816  1.00 15.52 ?  53   LEU   B HD22 1 
ATOM   4873 H  HD23 . LEU   B 1 53  ? 52.183 -21.671 -4.705  1.00 15.52 ?  53   LEU   B HD23 1 
ATOM   4874 N  N    . ASN   B 1 54  ? 54.790 -20.114 -0.460  1.00 9.93  ?  54   ASN   B N    1 
ATOM   4875 C  CA   . ASN   B 1 54  ? 55.704 -19.201 0.210   1.00 10.79 ?  54   ASN   B CA   1 
ATOM   4876 C  C    . ASN   B 1 54  ? 57.148 -19.478 -0.190  1.00 11.03 ?  54   ASN   B C    1 
ATOM   4877 O  O    . ASN   B 1 54  ? 57.923 -18.540 -0.420  1.00 11.47 ?  54   ASN   B O    1 
ATOM   4878 C  CB   . ASN   B 1 54  ? 55.542 -19.276 1.720   1.00 11.15 ?  54   ASN   B CB   1 
ATOM   4879 C  CG   . ASN   B 1 54  ? 56.525 -18.373 2.428   1.00 11.35 ?  54   ASN   B CG   1 
ATOM   4880 O  OD1  . ASN   B 1 54  ? 56.538 -17.163 2.194   1.00 11.64 ?  54   ASN   B OD1  1 
ATOM   4881 N  ND2  . ASN   B 1 54  ? 57.377 -18.955 3.267   1.00 13.06 ?  54   ASN   B ND2  1 
ATOM   4882 H  H    . ASN   B 1 54  ? 54.347 -20.640 0.061   1.00 11.91 ?  54   ASN   B H    1 
ATOM   4883 H  HA   . ASN   B 1 54  ? 55.490 -18.299 -0.066  1.00 12.95 ?  54   ASN   B HA   1 
ATOM   4884 H  HB2  . ASN   B 1 54  ? 54.642 -18.990 1.957   1.00 13.38 ?  54   ASN   B HB2  1 
ATOM   4885 H  HB3  . ASN   B 1 54  ? 55.691 -20.184 2.016   1.00 13.38 ?  54   ASN   B HB3  1 
ATOM   4886 H  HD21 . ASN   B 1 54  ? 57.962 -18.483 3.684   1.00 15.67 ?  54   ASN   B HD21 1 
ATOM   4887 H  HD22 . ASN   B 1 54  ? 57.347 -19.807 3.389   1.00 15.67 ?  54   ASN   B HD22 1 
ATOM   4888 N  N    . LYS   B 1 55  ? 57.534 -20.754 -0.259  1.00 11.71 ?  55   LYS   B N    1 
ATOM   4889 C  CA   . LYS   B 1 55  ? 58.888 -21.094 -0.682  1.00 12.52 ?  55   LYS   B CA   1 
ATOM   4890 C  C    . LYS   B 1 55  ? 59.180 -20.553 -2.076  1.00 11.98 ?  55   LYS   B C    1 
ATOM   4891 O  O    . LYS   B 1 55  ? 60.278 -20.051 -2.335  1.00 13.04 ?  55   LYS   B O    1 
ATOM   4892 C  CB   . LYS   B 1 55  ? 59.082 -22.609 -0.635  1.00 13.93 ?  55   LYS   B CB   1 
ATOM   4893 C  CG   . LYS   B 1 55  ? 60.468 -23.070 -1.035  1.00 18.12 ?  55   LYS   B CG   1 
ATOM   4894 C  CD   . LYS   B 1 55  ? 60.630 -24.573 -0.875  1.00 21.86 ?  55   LYS   B CD   1 
ATOM   4895 C  CE   . LYS   B 1 55  ? 60.549 -25.004 0.588   1.00 24.78 ?  55   LYS   B CE   1 
ATOM   4896 N  NZ   . LYS   B 1 55  ? 61.003 -26.399 0.786   1.00 26.19 ?  55   LYS   B NZ   1 
ATOM   4897 H  H    . LYS   B 1 55  ? 57.038 -21.428 -0.064  1.00 14.05 ?  55   LYS   B H    1 
ATOM   4898 H  HA   . LYS   B 1 55  ? 59.522 -20.688 -0.068  1.00 15.02 ?  55   LYS   B HA   1 
ATOM   4899 H  HB2  . LYS   B 1 55  ? 58.918 -22.904 0.273   1.00 16.72 ?  55   LYS   B HB2  1 
ATOM   4900 H  HB3  . LYS   B 1 55  ? 58.448 -23.020 -1.237  1.00 16.72 ?  55   LYS   B HB3  1 
ATOM   4901 H  HG2  . LYS   B 1 55  ? 60.625 -22.846 -1.966  1.00 21.74 ?  55   LYS   B HG2  1 
ATOM   4902 H  HG3  . LYS   B 1 55  ? 61.127 -22.631 -0.472  1.00 21.74 ?  55   LYS   B HG3  1 
ATOM   4903 H  HD2  . LYS   B 1 55  ? 59.923 -25.025 -1.363  1.00 26.23 ?  55   LYS   B HD2  1 
ATOM   4904 H  HD3  . LYS   B 1 55  ? 61.497 -24.841 -1.217  1.00 26.23 ?  55   LYS   B HD3  1 
ATOM   4905 H  HE2  . LYS   B 1 55  ? 61.107 -24.413 1.121   1.00 29.74 ?  55   LYS   B HE2  1 
ATOM   4906 H  HE3  . LYS   B 1 55  ? 59.623 -24.935 0.884   1.00 29.74 ?  55   LYS   B HE3  1 
ATOM   4907 H  HZ1  . LYS   B 1 55  ? 60.912 -26.626 1.641   1.00 31.43 ?  55   LYS   B HZ1  1 
ATOM   4908 H  HZ2  . LYS   B 1 55  ? 60.514 -26.948 0.286   1.00 31.43 ?  55   LYS   B HZ2  1 
ATOM   4909 H  HZ3  . LYS   B 1 55  ? 61.856 -26.473 0.552   1.00 31.43 ?  55   LYS   B HZ3  1 
ATOM   4910 N  N    . ALA   B 1 56  ? 58.208 -20.635 -2.987  1.00 11.66 ?  56   ALA   B N    1 
ATOM   4911 C  CA   . ALA   B 1 56  ? 58.427 -20.131 -4.339  1.00 12.44 ?  56   ALA   B CA   1 
ATOM   4912 C  C    . ALA   B 1 56  ? 58.703 -18.635 -4.339  1.00 12.37 ?  56   ALA   B C    1 
ATOM   4913 O  O    . ALA   B 1 56  ? 59.427 -18.135 -5.210  1.00 13.63 ?  56   ALA   B O    1 
ATOM   4914 C  CB   . ALA   B 1 56  ? 57.227 -20.457 -5.225  1.00 13.60 ?  56   ALA   B CB   1 
ATOM   4915 H  H    . ALA   B 1 56  ? 57.421 -20.957 -2.846  1.00 13.99 ?  56   ALA   B H    1 
ATOM   4916 H  HA   . ALA   B 1 56  ? 59.205 -20.568 -4.709  1.00 14.92 ?  56   ALA   B HA   1 
ATOM   4917 H  HB1  . ALA   B 1 56  ? 57.399 -20.122 -6.121  1.00 16.32 ?  56   ALA   B HB1  1 
ATOM   4918 H  HB2  . ALA   B 1 56  ? 57.112 -21.419 -5.251  1.00 16.32 ?  56   ALA   B HB2  1 
ATOM   4919 H  HB3  . ALA   B 1 56  ? 56.436 -20.036 -4.860  1.00 16.32 ?  56   ALA   B HB3  1 
ATOM   4920 N  N    . THR   B 1 57  ? 58.140 -17.905 -3.374  1.00 12.14 ?  57   THR   B N    1 
ATOM   4921 C  CA   . THR   B 1 57  ? 58.377 -16.472 -3.242  1.00 12.29 ?  57   THR   B CA   1 
ATOM   4922 C  C    . THR   B 1 57  ? 59.628 -16.148 -2.433  1.00 13.12 ?  57   THR   B C    1 
ATOM   4923 O  O    . THR   B 1 57  ? 59.864 -14.972 -2.127  1.00 13.49 ?  57   THR   B O    1 
ATOM   4924 C  CB   . THR   B 1 57  ? 57.179 -15.747 -2.600  1.00 11.73 ?  57   THR   B CB   1 
ATOM   4925 O  OG1  . THR   B 1 57  ? 57.158 -15.965 -1.182  1.00 11.78 ?  57   THR   B OG1  1 
ATOM   4926 C  CG2  . THR   B 1 57  ? 55.856 -16.156 -3.237  1.00 11.78 ?  57   THR   B CG2  1 
ATOM   4927 H  H    . THR   B 1 57  ? 57.594 -18.217 -2.782  1.00 14.57 ?  57   THR   B H    1 
ATOM   4928 H  HA   . THR   B 1 57  ? 58.496 -16.097 -4.129  1.00 14.75 ?  57   THR   B HA   1 
ATOM   4929 H  HB   . THR   B 1 57  ? 57.284 -14.791 -2.759  1.00 14.08 ?  57   THR   B HB   1 
ATOM   4930 H  HG1  . THR   B 1 57  ? 57.087 -16.787 -1.023  1.00 14.13 ?  57   THR   B HG1  1 
ATOM   4931 H  HG21 . THR   B 1 57  ? 55.134 -15.625 -2.876  1.00 14.13 ?  57   THR   B HG21 1 
ATOM   4932 H  HG22 . THR   B 1 57  ? 55.897 -16.024 -4.199  1.00 14.13 ?  57   THR   B HG22 1 
ATOM   4933 H  HG23 . THR   B 1 57  ? 55.681 -17.093 -3.059  1.00 14.13 ?  57   THR   B HG23 1 
ATOM   4934 N  N    . ASN   B 1 58  ? 60.425 -17.153 -2.073  1.00 13.50 ?  58   ASN   B N    1 
ATOM   4935 C  CA   . ASN   B 1 58  ? 61.626 -16.935 -1.274  1.00 16.31 ?  58   ASN   B CA   1 
ATOM   4936 C  C    . ASN   B 1 58  ? 61.293 -16.229 0.039   1.00 14.18 ?  58   ASN   B C    1 
ATOM   4937 O  O    . ASN   B 1 58  ? 62.027 -15.354 0.504   1.00 14.90 ?  58   ASN   B O    1 
ATOM   4938 C  CB   . ASN   B 1 58  ? 62.693 -16.166 -2.056  1.00 23.45 ?  58   ASN   B CB   1 
ATOM   4939 C  CG   . ASN   B 1 58  ? 64.067 -16.274 -1.424  1.00 31.18 ?  58   ASN   B CG   1 
ATOM   4940 O  OD1  . ASN   B 1 58  ? 64.380 -17.260 -0.757  1.00 33.63 ?  58   ASN   B OD1  1 
ATOM   4941 N  ND2  . ASN   B 1 58  ? 64.892 -15.255 -1.627  1.00 35.11 ?  58   ASN   B ND2  1 
ATOM   4942 H  H    . ASN   B 1 58  ? 60.285 -17.981 -2.271  1.00 16.19 ?  58   ASN   B H    1 
ATOM   4943 H  HA   . ASN   B 1 58  ? 62.002 -17.802 -1.054  1.00 19.57 ?  58   ASN   B HA   1 
ATOM   4944 H  HB2  . ASN   B 1 58  ? 62.745 -16.525 -2.956  1.00 28.14 ?  58   ASN   B HB2  1 
ATOM   4945 H  HB3  . ASN   B 1 58  ? 62.450 -15.228 -2.085  1.00 28.14 ?  58   ASN   B HB3  1 
ATOM   4946 H  HD21 . ASN   B 1 58  ? 65.683 -15.270 -1.289  1.00 42.14 ?  58   ASN   B HD21 1 
ATOM   4947 H  HD22 . ASN   B 1 58  ? 64.637 -14.583 -2.096  1.00 42.14 ?  58   ASN   B HD22 1 
ATOM   4948 N  N    . ASN   B 1 59  ? 60.172 -16.613 0.645   1.00 13.24 ?  59   ASN   B N    1 
ATOM   4949 C  CA   . ASN   B 1 59  ? 59.702 -16.137 1.945   1.00 13.29 ?  59   ASN   B CA   1 
ATOM   4950 C  C    . ASN   B 1 59  ? 59.103 -14.733 1.888   1.00 12.44 ?  59   ASN   B C    1 
ATOM   4951 O  O    . ASN   B 1 59  ? 58.671 -14.231 2.933   1.00 12.71 ?  59   ASN   B O    1 
ATOM   4952 C  CB   . ASN   B 1 59  ? 60.775 -16.190 3.048   1.00 14.34 ?  59   ASN   B CB   1 
ATOM   4953 C  CG   . ASN   B 1 59  ? 60.190 -16.388 4.430   1.00 15.23 ?  59   ASN   B CG   1 
ATOM   4954 O  OD1  . ASN   B 1 59  ? 59.359 -17.272 4.649   1.00 15.60 ?  59   ASN   B OD1  1 
ATOM   4955 N  ND2  . ASN   B 1 59  ? 60.619 -15.562 5.374   1.00 15.79 ?  59   ASN   B ND2  1 
ATOM   4956 H  H    . ASN   B 1 59  ? 59.630 -17.192 0.304   1.00 15.88 ?  59   ASN   B H    1 
ATOM   4957 H  HA   . ASN   B 1 59  ? 58.995 -16.731 2.234   1.00 15.95 ?  59   ASN   B HA   1 
ATOM   4958 H  HB2  . ASN   B 1 59  ? 61.377 -16.931 2.880   1.00 17.21 ?  59   ASN   B HB2  1 
ATOM   4959 H  HB3  . ASN   B 1 59  ? 61.270 -15.356 3.058   1.00 17.21 ?  59   ASN   B HB3  1 
ATOM   4960 H  HD21 . ASN   B 1 59  ? 60.321 -15.631 6.179   1.00 18.94 ?  59   ASN   B HD21 1 
ATOM   4961 H  HD22 . ASN   B 1 59  ? 61.204 -14.958 5.187   1.00 18.94 ?  59   ASN   B HD22 1 
ATOM   4962 N  N    . ALA   B 1 60  ? 59.036 -14.089 0.718   1.00 12.34 ?  60   ALA   B N    1 
ATOM   4963 C  CA   . ALA   B 1 60  ? 58.441 -12.754 0.654   1.00 12.32 ?  60   ALA   B CA   1 
ATOM   4964 C  C    . ALA   B 1 60  ? 56.971 -12.777 1.054   1.00 11.52 ?  60   ALA   B C    1 
ATOM   4965 O  O    . ALA   B 1 60  ? 56.473 -11.829 1.677   1.00 12.12 ?  60   ALA   B O    1 
ATOM   4966 C  CB   . ALA   B 1 60  ? 58.609 -12.161 -0.744  1.00 13.17 ?  60   ALA   B CB   1 
ATOM   4967 H  H    . ALA   B 1 60  ? 59.317 -14.400 -0.030  1.00 14.81 ?  60   ALA   B H    1 
ATOM   4968 H  HA   . ALA   B 1 60  ? 58.906 -12.178 1.282   1.00 14.78 ?  60   ALA   B HA   1 
ATOM   4969 H  HB1  . ALA   B 1 60  ? 58.214 -11.276 -0.761  1.00 15.80 ?  60   ALA   B HB1  1 
ATOM   4970 H  HB2  . ALA   B 1 60  ? 59.559 -12.100 -0.948  1.00 15.80 ?  60   ALA   B HB2  1 
ATOM   4971 H  HB3  . ALA   B 1 60  ? 58.171 -12.736 -1.388  1.00 15.80 ?  60   ALA   B HB3  1 
ATOM   4972 N  N    . MET   B 1 61  ? 56.260 -13.852 0.709   1.00 11.18 ?  61   MET   B N    1 
ATOM   4973 C  CA   . MET   B 1 61  ? 54.866 -13.976 1.110   1.00 11.06 ?  61   MET   B CA   1 
ATOM   4974 C  C    . MET   B 1 61  ? 54.733 -13.993 2.632   1.00 11.00 ?  61   MET   B C    1 
ATOM   4975 O  O    . MET   B 1 61  ? 53.836 -13.349 3.189   1.00 10.99 ?  61   MET   B O    1 
ATOM   4976 C  CB   . MET   B 1 61  ? 54.284 -15.243 0.480   1.00 10.63 ?  61   MET   B CB   1 
ATOM   4977 C  CG   . MET   B 1 61  ? 52.842 -15.538 0.892   1.00 10.55 ?  61   MET   B CG   1 
ATOM   4978 S  SD   . MET   B 1 61  ? 52.201 -17.040 0.132   1.00 11.16 ?  61   MET   B SD   1 
ATOM   4979 C  CE   . MET   B 1 61  ? 51.943 -16.454 -1.538  1.00 12.40 ?  61   MET   B CE   1 
ATOM   4980 H  H    . MET   B 1 61  ? 56.559 -14.515 0.245   1.00 13.41 ?  61   MET   B H    1 
ATOM   4981 H  HA   . MET   B 1 61  ? 54.369 -13.219 0.757   1.00 13.27 ?  61   MET   B HA   1 
ATOM   4982 H  HB2  . MET   B 1 61  ? 54.302 -15.148 -0.488  1.00 12.76 ?  61   MET   B HB2  1 
ATOM   4983 H  HB3  . MET   B 1 61  ? 54.831 -16.000 0.742   1.00 12.76 ?  61   MET   B HB3  1 
ATOM   4984 H  HG2  . MET   B 1 61  ? 52.802 -15.654 1.853   1.00 12.66 ?  61   MET   B HG2  1 
ATOM   4985 H  HG3  . MET   B 1 61  ? 52.277 -14.801 0.620   1.00 12.66 ?  61   MET   B HG3  1 
ATOM   4986 H  HE1  . MET   B 1 61  ? 51.560 -17.168 -2.068  1.00 14.88 ?  61   MET   B HE1  1 
ATOM   4987 H  HE2  . MET   B 1 61  ? 51.340 -15.695 -1.515  1.00 14.88 ?  61   MET   B HE2  1 
ATOM   4988 H  HE3  . MET   B 1 61  ? 52.799 -16.185 -1.912  1.00 14.88 ?  61   MET   B HE3  1 
ATOM   4989 N  N    . GLN   B 1 62  ? 55.615 -14.716 3.328   1.00 10.78 ?  62   GLN   B N    1 
ATOM   4990 C  CA   . GLN   B 1 62  ? 55.517 -14.771 4.785   1.00 11.11 ?  62   GLN   B CA   1 
ATOM   4991 C  C    . GLN   B 1 62  ? 55.802 -13.414 5.414   1.00 11.41 ?  62   GLN   B C    1 
ATOM   4992 O  O    . GLN   B 1 62  ? 55.120 -13.008 6.362   1.00 11.79 ?  62   GLN   B O    1 
ATOM   4993 C  CB   . GLN   B 1 62  ? 56.469 -15.826 5.347   1.00 11.37 ?  62   GLN   B CB   1 
ATOM   4994 C  CG   . GLN   B 1 62  ? 56.252 -16.108 6.829   1.00 11.56 ?  62   GLN   B CG   1 
ATOM   4995 C  CD   . GLN   B 1 62  ? 54.880 -16.694 7.072   1.00 11.08 ?  62   GLN   B CD   1 
ATOM   4996 O  OE1  . GLN   B 1 62  ? 54.622 -17.838 6.713   1.00 11.83 ?  62   GLN   B OE1  1 
ATOM   4997 N  NE2  . GLN   B 1 62  ? 53.972 -15.901 7.632   1.00 11.97 ?  62   GLN   B NE2  1 
ATOM   4998 H  H    . GLN   B 1 62  ? 56.257 -15.174 2.981   1.00 12.94 ?  62   GLN   B H    1 
ATOM   4999 H  HA   . GLN   B 1 62  ? 54.612 -15.024 5.020   1.00 13.33 ?  62   GLN   B HA   1 
ATOM   5000 H  HB2  . GLN   B 1 62  ? 56.341 -16.654 4.859   1.00 13.65 ?  62   GLN   B HB2  1 
ATOM   5001 H  HB3  . GLN   B 1 62  ? 57.381 -15.514 5.230   1.00 13.65 ?  62   GLN   B HB3  1 
ATOM   5002 H  HG2  . GLN   B 1 62  ? 56.917 -16.752 7.126   1.00 13.87 ?  62   GLN   B HG2  1 
ATOM   5003 H  HG3  . GLN   B 1 62  ? 56.332 -15.286 7.330   1.00 13.87 ?  62   GLN   B HG3  1 
ATOM   5004 H  HE21 . GLN   B 1 62  ? 54.182 -15.099 7.857   1.00 14.37 ?  62   GLN   B HE21 1 
ATOM   5005 H  HE22 . GLN   B 1 62  ? 53.179 -16.198 7.784   1.00 14.37 ?  62   GLN   B HE22 1 
ATOM   5006 N  N    . VAL   B 1 63  ? 56.816 -12.700 4.917   1.00 12.05 ?  63   VAL   B N    1 
ATOM   5007 C  CA   . VAL   B 1 63  ? 57.127 -11.385 5.470   1.00 12.79 ?  63   VAL   B CA   1 
ATOM   5008 C  C    . VAL   B 1 63  ? 55.935 -10.451 5.295   1.00 12.11 ?  63   VAL   B C    1 
ATOM   5009 O  O    . VAL   B 1 63  ? 55.528 -9.747  6.230   1.00 12.66 ?  63   VAL   B O    1 
ATOM   5010 C  CB   . VAL   B 1 63  ? 58.416 -10.827 4.842   1.00 14.20 ?  63   VAL   B CB   1 
ATOM   5011 C  CG1  . VAL   B 1 63  ? 58.643 -9.388  5.286   1.00 14.90 ?  63   VAL   B CG1  1 
ATOM   5012 C  CG2  . VAL   B 1 63  ? 59.602 -11.696 5.235   1.00 15.16 ?  63   VAL   B CG2  1 
ATOM   5013 H  H    . VAL   B 1 63  ? 57.324 -12.949 4.264   1.00 14.46 ?  63   VAL   B H    1 
ATOM   5014 H  HA   . VAL   B 1 63  ? 57.287 -11.485 6.417   1.00 15.35 ?  63   VAL   B HA   1 
ATOM   5015 H  HB   . VAL   B 1 63  ? 58.344 -10.841 3.875   1.00 17.04 ?  63   VAL   B HB   1 
ATOM   5016 H  HG11 . VAL   B 1 63  ? 59.560 -9.139  5.100   1.00 17.88 ?  63   VAL   B HG11 1 
ATOM   5017 H  HG12 . VAL   B 1 63  ? 58.036 -8.808  4.801   1.00 17.88 ?  63   VAL   B HG12 1 
ATOM   5018 H  HG13 . VAL   B 1 63  ? 58.472 -9.324  6.241   1.00 17.88 ?  63   VAL   B HG13 1 
ATOM   5019 H  HG21 . VAL   B 1 63  ? 60.413 -11.323 4.851   1.00 18.19 ?  63   VAL   B HG21 1 
ATOM   5020 H  HG22 . VAL   B 1 63  ? 59.678 -11.706 6.206   1.00 18.19 ?  63   VAL   B HG22 1 
ATOM   5021 H  HG23 . VAL   B 1 63  ? 59.464 -12.595 4.907   1.00 18.19 ?  63   VAL   B HG23 1 
ATOM   5022 N  N    . GLU   B 1 64  ? 55.360 -10.438 4.091   1.00 11.82 ?  64   GLU   B N    1 
ATOM   5023 C  CA   . GLU   B 1 64  ? 54.190 -9.604  3.822   1.00 11.27 ?  64   GLU   B CA   1 
ATOM   5024 C  C    . GLU   B 1 64  ? 53.014 -10.005 4.705   1.00 10.99 ?  64   GLU   B C    1 
ATOM   5025 O  O    . GLU   B 1 64  ? 52.270 -9.145  5.206   1.00 11.71 ?  64   GLU   B O    1 
ATOM   5026 C  CB   . GLU   B 1 64  ? 53.814 -9.760  2.347   1.00 11.51 ?  64   GLU   B CB   1 
ATOM   5027 C  CG   . GLU   B 1 64  ? 52.551 -9.021  1.920   1.00 11.70 ?  64   GLU   B CG   1 
ATOM   5028 C  CD   . GLU   B 1 64  ? 52.015 -9.514  0.589   1.00 12.20 ?  64   GLU   B CD   1 
ATOM   5029 O  OE1  . GLU   B 1 64  ? 52.196 -10.721 0.271   1.00 13.25 ?  64   GLU   B OE1  1 
ATOM   5030 O  OE2  . GLU   B 1 64  ? 51.393 -8.698  -0.135  1.00 13.24 -1 64   GLU   B OE2  1 
ATOM   5031 H  H    . GLU   B 1 64  ? 55.633 -10.898 3.413   1.00 14.18 ?  64   GLU   B H    1 
ATOM   5032 H  HA   . GLU   B 1 64  ? 54.406 -8.675  3.988   1.00 13.52 ?  64   GLU   B HA   1 
ATOM   5033 H  HB2  . GLU   B 1 64  ? 54.544 -9.421  1.800   1.00 13.81 ?  64   GLU   B HB2  1 
ATOM   5034 H  HB3  . GLU   B 1 64  ? 53.680 -10.701 2.159   1.00 13.81 ?  64   GLU   B HB3  1 
ATOM   5035 H  HG2  . GLU   B 1 64  ? 51.855 -9.147  2.586   1.00 14.04 ?  64   GLU   B HG2  1 
ATOM   5036 H  HG3  . GLU   B 1 64  ? 52.752 -8.075  1.833   1.00 14.04 ?  64   GLU   B HG3  1 
ATOM   5037 N  N    . SER   B 1 65  ? 52.827 -11.312 4.890   1.00 10.90 ?  65   SER   B N    1 
ATOM   5038 C  CA   . SER   B 1 65  ? 51.722 -11.819 5.693   1.00 10.94 ?  65   SER   B CA   1 
ATOM   5039 C  C    . SER   B 1 65  ? 51.860 -11.420 7.155   1.00 10.83 ?  65   SER   B C    1 
ATOM   5040 O  O    . SER   B 1 65  ? 50.866 -11.052 7.796   1.00 11.35 ?  65   SER   B O    1 
ATOM   5041 C  CB   . SER   B 1 65  ? 51.648 -13.341 5.561   1.00 11.15 ?  65   SER   B CB   1 
ATOM   5042 O  OG   . SER   B 1 65  ? 51.286 -13.727 4.245   1.00 11.23 ?  65   SER   B OG   1 
ATOM   5043 H  H    . SER   B 1 65  ? 53.328 -11.933 4.555   1.00 13.08 ?  65   SER   B H    1 
ATOM   5044 H  HA   . SER   B 1 65  ? 50.889 -11.455 5.356   1.00 13.13 ?  65   SER   B HA   1 
ATOM   5045 H  HB2  . SER   B 1 65  ? 52.516 -13.721 5.771   1.00 13.38 ?  65   SER   B HB2  1 
ATOM   5046 H  HB3  . SER   B 1 65  ? 50.982 -13.681 6.180   1.00 13.38 ?  65   SER   B HB3  1 
ATOM   5047 H  HG   . SER   B 1 65  ? 51.857 -13.437 3.693   1.00 13.47 ?  65   SER   B HG   1 
ATOM   5048 N  N    . ASP   B 1 66  ? 53.069 -11.526 7.717   1.00 11.33 ?  66   ASP   B N    1 
ATOM   5049 C  CA   . ASP   B 1 66  ? 53.262 -11.139 9.114   1.00 11.66 ?  66   ASP   B CA   1 
ATOM   5050 C  C    . ASP   B 1 66  ? 52.944 -9.661  9.319   1.00 11.87 ?  66   ASP   B C    1 
ATOM   5051 O  O    . ASP   B 1 66  ? 52.366 -9.273  10.343  1.00 12.37 ?  66   ASP   B O    1 
ATOM   5052 C  CB   . ASP   B 1 66  ? 54.696 -11.442 9.554   1.00 13.11 ?  66   ASP   B CB   1 
ATOM   5053 C  CG   . ASP   B 1 66  ? 54.973 -12.933 9.710   1.00 14.82 ?  66   ASP   B CG   1 
ATOM   5054 O  OD1  . ASP   B 1 66  ? 54.022 -13.743 9.644   1.00 15.27 ?  66   ASP   B OD1  1 
ATOM   5055 O  OD2  . ASP   B 1 66  ? 56.155 -13.301 9.911   1.00 17.26 -1 66   ASP   B OD2  1 
ATOM   5056 H  H    . ASP   B 1 66  ? 53.770 -11.821 7.324   1.00 13.60 ?  66   ASP   B H    1 
ATOM   5057 H  HA   . ASP   B 1 66  ? 52.658 -11.649 9.676   1.00 14.00 ?  66   ASP   B HA   1 
ATOM   5058 H  HB2  . ASP   B 1 66  ? 55.308 -11.096 8.886   1.00 15.73 ?  66   ASP   B HB2  1 
ATOM   5059 H  HB3  . ASP   B 1 66  ? 54.860 -11.011 10.409  1.00 15.73 ?  66   ASP   B HB3  1 
ATOM   5060 N  N    . ASP   B 1 67  ? 53.317 -8.817  8.358   1.00 11.73 ?  67   ASP   B N    1 
ATOM   5061 C  CA   . ASP   B 1 67  ? 52.972 -7.405  8.446   1.00 12.25 ?  67   ASP   B CA   1 
ATOM   5062 C  C    . ASP   B 1 67  ? 51.461 -7.197  8.366   1.00 12.35 ?  67   ASP   B C    1 
ATOM   5063 O  O    . ASP   B 1 67  ? 50.898 -6.396  9.122   1.00 12.93 ?  67   ASP   B O    1 
ATOM   5064 C  CB   . ASP   B 1 67  ? 53.688 -6.635  7.343   1.00 13.39 ?  67   ASP   B CB   1 
ATOM   5065 C  CG   . ASP   B 1 67  ? 53.276 -5.190  7.306   1.00 14.85 ?  67   ASP   B CG   1 
ATOM   5066 O  OD1  . ASP   B 1 67  ? 53.785 -4.389  8.124   1.00 15.98 ?  67   ASP   B OD1  1 
ATOM   5067 O  OD2  . ASP   B 1 67  ? 52.405 -4.876  6.477   1.00 16.01 -1 67   ASP   B OD2  1 
ATOM   5068 H  H    . ASP   B 1 67  ? 53.777 -9.033  7.662   1.00 14.08 ?  67   ASP   B H    1 
ATOM   5069 H  HA   . ASP   B 1 67  ? 53.277 -7.053  9.296   1.00 14.70 ?  67   ASP   B HA   1 
ATOM   5070 H  HB2  . ASP   B 1 67  ? 54.648 -6.674  7.496   1.00 16.07 ?  67   ASP   B HB2  1 
ATOM   5071 H  HB3  . ASP   B 1 67  ? 53.477 -7.040  6.483   1.00 16.07 ?  67   ASP   B HB3  1 
ATOM   5072 N  N    . TYR   B 1 68  ? 50.783 -7.924  7.469   1.00 11.91 ?  68   TYR   B N    1 
ATOM   5073 C  CA   . TYR   B 1 68  ? 49.324 -7.856  7.399   1.00 12.50 ?  68   TYR   B CA   1 
ATOM   5074 C  C    . TYR   B 1 68  ? 48.690 -8.196  8.746   1.00 12.11 ?  68   TYR   B C    1 
ATOM   5075 O  O    . TYR   B 1 68  ? 47.760 -7.516  9.200   1.00 12.69 ?  68   TYR   B O    1 
ATOM   5076 C  CB   . TYR   B 1 68  ? 48.793 -8.792  6.302   1.00 13.35 ?  68   TYR   B CB   1 
ATOM   5077 C  CG   . TYR   B 1 68  ? 47.285 -8.942  6.361   1.00 14.23 ?  68   TYR   B CG   1 
ATOM   5078 C  CD1  . TYR   B 1 68  ? 46.696 -9.894  7.189   1.00 15.06 ?  68   TYR   B CD1  1 
ATOM   5079 C  CD2  . TYR   B 1 68  ? 46.455 -8.108  5.631   1.00 15.10 ?  68   TYR   B CD2  1 
ATOM   5080 C  CE1  . TYR   B 1 68  ? 45.331 -10.011 7.286   1.00 16.09 ?  68   TYR   B CE1  1 
ATOM   5081 C  CE2  . TYR   B 1 68  ? 45.074 -8.228  5.714   1.00 15.58 ?  68   TYR   B CE2  1 
ATOM   5082 C  CZ   . TYR   B 1 68  ? 44.532 -9.181  6.545   1.00 16.03 ?  68   TYR   B CZ   1 
ATOM   5083 O  OH   . TYR   B 1 68  ? 43.164 -9.295  6.644   1.00 16.77 ?  68   TYR   B OH   1 
ATOM   5084 H  H    . TYR   B 1 68  ? 51.145 -8.464  6.895   1.00 14.29 ?  68   TYR   B H    1 
ATOM   5085 H  HA   . TYR   B 1 68  ? 49.068 -6.954  7.169   1.00 15.00 ?  68   TYR   B HA   1 
ATOM   5086 H  HB2  . TYR   B 1 68  ? 49.022 -8.428  5.435   1.00 16.02 ?  68   TYR   B HB2  1 
ATOM   5087 H  HB3  . TYR   B 1 68  ? 49.188 -9.672  6.413   1.00 16.02 ?  68   TYR   B HB3  1 
ATOM   5088 H  HD1  . TYR   B 1 68  ? 47.237 -10.458 7.698   1.00 18.07 ?  68   TYR   B HD1  1 
ATOM   5089 H  HD2  . TYR   B 1 68  ? 46.831 -7.461  5.086   1.00 18.12 ?  68   TYR   B HD2  1 
ATOM   5090 H  HE1  . TYR   B 1 68  ? 44.952 -10.661 7.837   1.00 19.30 ?  68   TYR   B HE1  1 
ATOM   5091 H  HE2  . TYR   B 1 68  ? 44.523 -7.665  5.224   1.00 18.69 ?  68   TYR   B HE2  1 
ATOM   5092 H  HH   . TYR   B 1 68  ? 42.780 -8.738  6.136   1.00 20.13 ?  68   TYR   B HH   1 
ATOM   5093 N  N    . ILE   B 1 69  ? 49.174 -9.265  9.392   1.00 12.12 ?  69   ILE   B N    1 
ATOM   5094 C  CA   . ILE   B 1 69  ? 48.615 -9.691  10.674  1.00 12.70 ?  69   ILE   B CA   1 
ATOM   5095 C  C    . ILE   B 1 69  ? 48.870 -8.644  11.751  1.00 12.07 ?  69   ILE   B C    1 
ATOM   5096 O  O    . ILE   B 1 69  ? 48.002 -8.371  12.585  1.00 12.63 ?  69   ILE   B O    1 
ATOM   5097 C  CB   . ILE   B 1 69  ? 49.183 -11.069 11.068  1.00 13.57 ?  69   ILE   B CB   1 
ATOM   5098 C  CG1  . ILE   B 1 69  ? 48.656 -12.167 10.137  1.00 13.91 ?  69   ILE   B CG1  1 
ATOM   5099 C  CG2  . ILE   B 1 69  ? 48.894 -11.389 12.532  1.00 14.69 ?  69   ILE   B CG2  1 
ATOM   5100 C  CD1  . ILE   B 1 69  ? 47.180 -12.472 10.290  1.00 14.03 ?  69   ILE   B CD1  1 
ATOM   5101 H  H    . ILE   B 1 69  ? 49.825 -9.752  9.115   1.00 14.54 ?  69   ILE   B H    1 
ATOM   5102 H  HA   . ILE   B 1 69  ? 47.658 -9.781  10.579  1.00 15.24 ?  69   ILE   B HA   1 
ATOM   5103 H  HB   . ILE   B 1 69  ? 50.147 -11.032 10.962  1.00 16.28 ?  69   ILE   B HB   1 
ATOM   5104 H  HG12 . ILE   B 1 69  ? 48.806 -11.890 9.219   1.00 16.69 ?  69   ILE   B HG12 1 
ATOM   5105 H  HG13 . ILE   B 1 69  ? 49.147 -12.984 10.315  1.00 16.69 ?  69   ILE   B HG13 1 
ATOM   5106 H  HG21 . ILE   B 1 69  ? 49.042 -12.339 12.677  1.00 17.63 ?  69   ILE   B HG21 1 
ATOM   5107 H  HG22 . ILE   B 1 69  ? 49.494 -10.877 13.096  1.00 17.63 ?  69   ILE   B HG22 1 
ATOM   5108 H  HG23 . ILE   B 1 69  ? 47.974 -11.166 12.730  1.00 17.63 ?  69   ILE   B HG23 1 
ATOM   5109 H  HD11 . ILE   B 1 69  ? 46.942 -13.182 9.676   1.00 16.83 ?  69   ILE   B HD11 1 
ATOM   5110 H  HD12 . ILE   B 1 69  ? 47.006 -12.756 11.203  1.00 16.83 ?  69   ILE   B HD12 1 
ATOM   5111 H  HD13 . ILE   B 1 69  ? 46.666 -11.676 10.089  1.00 16.83 ?  69   ILE   B HD13 1 
ATOM   5112 N  N    . ALA   B 1 70  ? 50.066 -8.060  11.773  1.00 12.17 ?  70   ALA   B N    1 
ATOM   5113 C  CA   . ALA   B 1 70  ? 50.349 -7.019  12.757  1.00 12.16 ?  70   ALA   B CA   1 
ATOM   5114 C  C    . ALA   B 1 70  ? 49.350 -5.877  12.645  1.00 12.33 ?  70   ALA   B C    1 
ATOM   5115 O  O    . ALA   B 1 70  ? 48.913 -5.325  13.660  1.00 12.87 ?  70   ALA   B O    1 
ATOM   5116 C  CB   . ALA   B 1 70  ? 51.775 -6.502  12.579  1.00 12.93 ?  70   ALA   B CB   1 
ATOM   5117 H  H    . ALA   B 1 70  ? 50.716 -8.249  11.250  1.00 14.60 ?  70   ALA   B H    1 
ATOM   5118 H  HA   . ALA   B 1 70  ? 50.283 -7.393  13.651  1.00 14.60 ?  70   ALA   B HA   1 
ATOM   5119 H  HB1  . ALA   B 1 70  ? 51.962 -5.838  13.263  1.00 15.51 ?  70   ALA   B HB1  1 
ATOM   5120 H  HB2  . ALA   B 1 70  ? 52.397 -7.243  12.664  1.00 15.51 ?  70   ALA   B HB2  1 
ATOM   5121 H  HB3  . ALA   B 1 70  ? 51.861 -6.101  11.699  1.00 15.51 ?  70   ALA   B HB3  1 
ATOM   5122 N  N    . THR   B 1 71  ? 48.978 -5.511  11.421  1.00 12.86 ?  71   THR   B N    1 
ATOM   5123 C  CA   . THR   B 1 71  ? 48.091 -4.374  11.209  1.00 13.96 ?  71   THR   B CA   1 
ATOM   5124 C  C    . THR   B 1 71  ? 46.622 -4.734  11.417  1.00 14.29 ?  71   THR   B C    1 
ATOM   5125 O  O    . THR   B 1 71  ? 45.845 -3.915  11.927  1.00 16.06 ?  71   THR   B O    1 
ATOM   5126 C  CB   . THR   B 1 71  ? 48.315 -3.818  9.801   1.00 16.03 ?  71   THR   B CB   1 
ATOM   5127 O  OG1  . THR   B 1 71  ? 49.642 -3.287  9.708   1.00 17.87 ?  71   THR   B OG1  1 
ATOM   5128 C  CG2  . THR   B 1 71  ? 47.299 -2.732  9.468   1.00 17.13 ?  71   THR   B CG2  1 
ATOM   5129 H  H    . THR   B 1 71  ? 49.228 -5.906  10.701  1.00 15.44 ?  71   THR   B H    1 
ATOM   5130 H  HA   . THR   B 1 71  ? 48.318 -3.675  11.842  1.00 16.76 ?  71   THR   B HA   1 
ATOM   5131 H  HB   . THR   B 1 71  ? 48.219 -4.532  9.152   1.00 19.24 ?  71   THR   B HB   1 
ATOM   5132 H  HG1  . THR   B 1 71  ? 49.773 -2.964  8.939   1.00 21.44 ?  71   THR   B HG1  1 
ATOM   5133 H  HG21 . THR   B 1 71  ? 47.608 -2.213  8.707   1.00 20.55 ?  71   THR   B HG21 1 
ATOM   5134 H  HG22 . THR   B 1 71  ? 46.444 -3.129  9.251   1.00 20.55 ?  71   THR   B HG22 1 
ATOM   5135 H  HG23 . THR   B 1 71  ? 47.192 -2.136  10.227  1.00 20.55 ?  71   THR   B HG23 1 
ATOM   5136 N  N    . ASN   B 1 72  ? 46.224 -5.948  11.028  1.00 14.09 ?  72   ASN   B N    1 
ATOM   5137 C  CA   . ASN   B 1 72  ? 44.819 -6.303  10.895  1.00 14.66 ?  72   ASN   B CA   1 
ATOM   5138 C  C    . ASN   B 1 72  ? 44.344 -7.404  11.829  1.00 15.23 ?  72   ASN   B C    1 
ATOM   5139 O  O    . ASN   B 1 72  ? 43.126 -7.561  11.992  1.00 16.40 ?  72   ASN   B O    1 
ATOM   5140 C  CB   . ASN   B 1 72  ? 44.515 -6.726  9.449   1.00 15.59 ?  72   ASN   B CB   1 
ATOM   5141 C  CG   . ASN   B 1 72  ? 44.792 -5.621  8.462   1.00 16.57 ?  72   ASN   B CG   1 
ATOM   5142 O  OD1  . ASN   B 1 72  ? 45.799 -5.629  7.753   1.00 17.92 ?  72   ASN   B OD1  1 
ATOM   5143 N  ND2  . ASN   B 1 72  ? 43.918 -4.637  8.438   1.00 18.17 ?  72   ASN   B ND2  1 
ATOM   5144 H  H    . ASN   B 1 72  ? 46.766 -6.593  10.824  1.00 16.91 ?  72   ASN   B H    1 
ATOM   5145 H  HA   . ASN   B 1 72  ? 44.291 -5.515  11.079  1.00 17.59 ?  72   ASN   B HA   1 
ATOM   5146 H  HB2  . ASN   B 1 72  ? 45.074 -7.485  9.212   1.00 18.71 ?  72   ASN   B HB2  1 
ATOM   5147 H  HB3  . ASN   B 1 72  ? 43.580 -6.966  9.377   1.00 18.71 ?  72   ASN   B HB3  1 
ATOM   5148 H  HD21 . ASN   B 1 72  ? 44.021 -3.977  7.894   1.00 21.81 ?  72   ASN   B HD21 1 
ATOM   5149 H  HD22 . ASN   B 1 72  ? 43.225 -4.661  8.951   1.00 21.81 ?  72   ASN   B HD22 1 
ATOM   5150 N  N    . GLY   B 1 73  ? 45.246 -8.162  12.445  1.00 14.61 ?  73   GLY   B N    1 
ATOM   5151 C  CA   . GLY   B 1 73  ? 44.848 -9.296  13.239  1.00 13.79 ?  73   GLY   B CA   1 
ATOM   5152 C  C    . GLY   B 1 73  ? 44.489 -10.482 12.372  1.00 12.73 ?  73   GLY   B C    1 
ATOM   5153 O  O    . GLY   B 1 73  ? 44.476 -10.400 11.142  1.00 12.68 ?  73   GLY   B O    1 
ATOM   5154 H  H    . GLY   B 1 73  ? 46.098 -8.032  12.415  1.00 17.53 ?  73   GLY   B H    1 
ATOM   5155 H  HA2  . GLY   B 1 73  ? 45.574 -9.550  13.828  1.00 16.55 ?  73   GLY   B HA2  1 
ATOM   5156 H  HA3  . GLY   B 1 73  ? 44.077 -9.060  13.778  1.00 16.55 ?  73   GLY   B HA3  1 
ATOM   5157 N  N    . PRO   B 1 74  ? 44.185 -11.607 13.011  1.00 13.10 ?  74   PRO   B N    1 
ATOM   5158 C  CA   . PRO   B 1 74  ? 43.938 -12.840 12.264  1.00 12.64 ?  74   PRO   B CA   1 
ATOM   5159 C  C    . PRO   B 1 74  ? 42.632 -12.785 11.484  1.00 12.13 ?  74   PRO   B C    1 
ATOM   5160 O  O    . PRO   B 1 74  ? 41.692 -12.051 11.809  1.00 13.33 ?  74   PRO   B O    1 
ATOM   5161 C  CB   . PRO   B 1 74  ? 43.871 -13.905 13.364  1.00 13.75 ?  74   PRO   B CB   1 
ATOM   5162 C  CG   . PRO   B 1 74  ? 43.430 -13.159 14.579  1.00 15.46 ?  74   PRO   B CG   1 
ATOM   5163 C  CD   . PRO   B 1 74  ? 44.101 -11.819 14.465  1.00 14.68 ?  74   PRO   B CD   1 
ATOM   5164 H  HA   . PRO   B 1 74  ? 44.676 -13.029 11.659  1.00 15.17 ?  74   PRO   B HA   1 
ATOM   5165 H  HB2  . PRO   B 1 74  ? 43.225 -14.585 13.119  1.00 16.50 ?  74   PRO   B HB2  1 
ATOM   5166 H  HB3  . PRO   B 1 74  ? 44.750 -14.293 13.495  1.00 16.50 ?  74   PRO   B HB3  1 
ATOM   5167 H  HG2  . PRO   B 1 74  ? 42.464 -13.062 14.570  1.00 18.55 ?  74   PRO   B HG2  1 
ATOM   5168 H  HG3  . PRO   B 1 74  ? 43.724 -13.625 15.374  1.00 18.55 ?  74   PRO   B HG3  1 
ATOM   5169 H  HD2  . PRO   B 1 74  ? 43.556 -11.129 14.880  1.00 17.61 ?  74   PRO   B HD2  1 
ATOM   5170 H  HD3  . PRO   B 1 74  ? 44.990 -11.849 14.851  1.00 17.61 ?  74   PRO   B HD3  1 
ATOM   5171 N  N    . LEU   B 1 75  ? 42.595 -13.597 10.432  1.00 11.63 ?  75   LEU   B N    1 
ATOM   5172 C  CA   . LEU   B 1 75  ? 41.377 -13.819 9.671   1.00 11.43 ?  75   LEU   B CA   1 
ATOM   5173 C  C    . LEU   B 1 75  ? 40.414 -14.690 10.475  1.00 11.87 ?  75   LEU   B C    1 
ATOM   5174 O  O    . LEU   B 1 75  ? 40.764 -15.255 11.513  1.00 12.91 ?  75   LEU   B O    1 
ATOM   5175 C  CB   . LEU   B 1 75  ? 41.703 -14.539 8.363   1.00 11.46 ?  75   LEU   B CB   1 
ATOM   5176 C  CG   . LEU   B 1 75  ? 42.561 -13.800 7.331   1.00 13.45 ?  75   LEU   B CG   1 
ATOM   5177 C  CD1  . LEU   B 1 75  ? 42.762 -14.652 6.081   1.00 14.86 ?  75   LEU   B CD1  1 
ATOM   5178 C  CD2  . LEU   B 1 75  ? 41.970 -12.472 6.963   1.00 16.48 ?  75   LEU   B CD2  1 
ATOM   5179 H  H    . LEU   B 1 75  ? 43.271 -14.033 10.128  1.00 13.96 ?  75   LEU   B H    1 
ATOM   5180 H  HA   . LEU   B 1 75  ? 40.947 -12.971 9.467   1.00 13.71 ?  75   LEU   B HA   1 
ATOM   5181 H  HB2  . LEU   B 1 75  ? 42.168 -15.361 8.580   1.00 13.75 ?  75   LEU   B HB2  1 
ATOM   5182 H  HB3  . LEU   B 1 75  ? 40.864 -14.758 7.922   1.00 13.75 ?  75   LEU   B HB3  1 
ATOM   5183 H  HG   . LEU   B 1 75  ? 43.436 -13.640 7.715   1.00 16.14 ?  75   LEU   B HG   1 
ATOM   5184 H  HD11 . LEU   B 1 75  ? 43.314 -14.163 5.447   1.00 17.83 ?  75   LEU   B HD11 1 
ATOM   5185 H  HD12 . LEU   B 1 75  ? 43.204 -15.482 6.326   1.00 17.83 ?  75   LEU   B HD12 1 
ATOM   5186 H  HD13 . LEU   B 1 75  ? 41.899 -14.845 5.682   1.00 17.83 ?  75   LEU   B HD13 1 
ATOM   5187 H  HD21 . LEU   B 1 75  ? 42.495 -12.080 6.251   1.00 19.77 ?  75   LEU   B HD21 1 
ATOM   5188 H  HD22 . LEU   B 1 75  ? 41.056 -12.605 6.670   1.00 19.77 ?  75   LEU   B HD22 1 
ATOM   5189 H  HD23 . LEU   B 1 75  ? 41.987 -11.896 7.744   1.00 19.77 ?  75   LEU   B HD23 1 
ATOM   5190 N  N    . LYS   B 1 76  ? 39.179 -14.783 9.979   1.00 13.17 ?  76   LYS   B N    1 
ATOM   5191 C  CA   . LYS   B 1 76  ? 38.203 -15.754 10.454  1.00 14.04 ?  76   LYS   B CA   1 
ATOM   5192 C  C    . LYS   B 1 76  ? 38.294 -17.025 9.614   1.00 12.88 ?  76   LYS   B C    1 
ATOM   5193 O  O    . LYS   B 1 76  ? 38.568 -16.968 8.417   1.00 12.41 ?  76   LYS   B O    1 
ATOM   5194 C  CB   . LYS   B 1 76  ? 36.781 -15.192 10.288  1.00 17.02 ?  76   LYS   B CB   1 
ATOM   5195 C  CG   . LYS   B 1 76  ? 36.519 -13.784 10.862  1.00 19.53 ?  76   LYS   B CG   1 
ATOM   5196 C  CD   . LYS   B 1 76  ? 35.109 -13.265 10.518  1.00 21.32 ?  76   LYS   B CD   1 
ATOM   5197 C  CE   . LYS   B 1 76  ? 34.841 -11.898 11.130  1.00 23.48 ?  76   LYS   B CE   1 
ATOM   5198 N  NZ   . LYS   B 1 76  ? 33.537 -11.323 10.703  1.00 24.30 ?  76   LYS   B NZ   1 
ATOM   5199 H  H    . LYS   B 1 76  ? 38.880 -14.281 9.351   1.00 15.80 ?  76   LYS   B H    1 
ATOM   5200 H  HA   . LYS   B 1 76  ? 38.358 -15.972 11.388  1.00 16.84 ?  76   LYS   B HA   1 
ATOM   5201 H  HB2  . LYS   B 1 76  ? 36.578 -15.154 9.340   1.00 20.42 ?  76   LYS   B HB2  1 
ATOM   5202 H  HB3  . LYS   B 1 76  ? 36.160 -15.796 10.724  1.00 20.42 ?  76   LYS   B HB3  1 
ATOM   5203 H  HG2  . LYS   B 1 76  ? 36.604 -13.813 11.828  1.00 23.44 ?  76   LYS   B HG2  1 
ATOM   5204 H  HG3  . LYS   B 1 76  ? 37.169 -13.164 10.491  1.00 23.44 ?  76   LYS   B HG3  1 
ATOM   5205 H  HD2  . LYS   B 1 76  ? 35.026 -13.186 9.554   1.00 25.59 ?  76   LYS   B HD2  1 
ATOM   5206 H  HD3  . LYS   B 1 76  ? 34.449 -13.886 10.861  1.00 25.59 ?  76   LYS   B HD3  1 
ATOM   5207 H  HE2  . LYS   B 1 76  ? 34.833 -11.982 12.096  1.00 28.18 ?  76   LYS   B HE2  1 
ATOM   5208 H  HE3  . LYS   B 1 76  ? 35.544 -11.287 10.857  1.00 28.18 ?  76   LYS   B HE3  1 
ATOM   5209 H  HZ1  . LYS   B 1 76  ? 33.417 -10.526 11.081  1.00 29.16 ?  76   LYS   B HZ1  1 
ATOM   5210 H  HZ2  . LYS   B 1 76  ? 33.520 -11.228 9.818   1.00 29.16 ?  76   LYS   B HZ2  1 
ATOM   5211 H  HZ3  . LYS   B 1 76  ? 32.872 -11.862 10.948  1.00 29.16 ?  76   LYS   B HZ3  1 
ATOM   5212 N  N    . VAL   B 1 77  ? 38.040 -18.179 10.239  1.00 13.38 ?  77   VAL   B N    1 
ATOM   5213 C  CA   . VAL   B 1 77  ? 37.832 -19.391 9.451   1.00 13.43 ?  77   VAL   B CA   1 
ATOM   5214 C  C    . VAL   B 1 77  ? 36.639 -19.157 8.536   1.00 12.21 ?  77   VAL   B C    1 
ATOM   5215 O  O    . VAL   B 1 77  ? 35.578 -18.702 8.982   1.00 12.46 ?  77   VAL   B O    1 
ATOM   5216 C  CB   . VAL   B 1 77  ? 37.633 -20.617 10.355  1.00 14.56 ?  77   VAL   B CB   1 
ATOM   5217 C  CG1  . VAL   B 1 77  ? 37.369 -21.852 9.500   1.00 15.41 ?  77   VAL   B CG1  1 
ATOM   5218 C  CG2  . VAL   B 1 77  ? 38.859 -20.836 11.243  1.00 16.10 ?  77   VAL   B CG2  1 
ATOM   5219 H  H    . VAL   B 1 77  ? 37.998 -18.283 11.086  1.00 16.05 ?  77   VAL   B H    1 
ATOM   5220 H  HA   . VAL   B 1 77  ? 38.609 -19.550 8.892   1.00 16.12 ?  77   VAL   B HA   1 
ATOM   5221 H  HB   . VAL   B 1 77  ? 36.859 -20.468 10.925  1.00 17.47 ?  77   VAL   B HB   1 
ATOM   5222 H  HG11 . VAL   B 1 77  ? 37.417 -22.639 10.065  1.00 18.50 ?  77   VAL   B HG11 1 
ATOM   5223 H  HG12 . VAL   B 1 77  ? 36.482 -21.786 9.106   1.00 18.50 ?  77   VAL   B HG12 1 
ATOM   5224 H  HG13 . VAL   B 1 77  ? 38.038 -21.903 8.803   1.00 18.50 ?  77   VAL   B HG13 1 
ATOM   5225 H  HG21 . VAL   B 1 77  ? 38.720 -21.639 11.769  1.00 19.33 ?  77   VAL   B HG21 1 
ATOM   5226 H  HG22 . VAL   B 1 77  ? 39.638 -20.934 10.679  1.00 19.33 ?  77   VAL   B HG22 1 
ATOM   5227 H  HG23 . VAL   B 1 77  ? 38.962 -20.070 11.828  1.00 19.33 ?  77   VAL   B HG23 1 
ATOM   5228 N  N    . GLY   B 1 78  ? 36.822 -19.431 7.247   1.00 11.74 ?  78   GLY   B N    1 
ATOM   5229 C  CA   . GLY   B 1 78  ? 35.846 -19.107 6.234   1.00 11.46 ?  78   GLY   B CA   1 
ATOM   5230 C  C    . GLY   B 1 78  ? 36.085 -17.785 5.541   1.00 10.95 ?  78   GLY   B C    1 
ATOM   5231 O  O    . GLY   B 1 78  ? 35.407 -17.498 4.550   1.00 11.32 ?  78   GLY   B O    1 
ATOM   5232 H  H    . GLY   B 1 78  ? 37.529 -19.811 6.930   1.00 14.09 ?  78   GLY   B H    1 
ATOM   5233 H  HA2  . GLY   B 1 78  ? 35.847 -19.800 5.557   1.00 13.75 ?  78   GLY   B HA2  1 
ATOM   5234 H  HA3  . GLY   B 1 78  ? 34.968 -19.072 6.635   1.00 13.75 ?  78   GLY   B HA3  1 
ATOM   5235 N  N    . GLY   B 1 79  ? 37.035 -16.979 6.028   1.00 11.09 ?  79   GLY   B N    1 
ATOM   5236 C  CA   . GLY   B 1 79  ? 37.335 -15.684 5.454   1.00 10.69 ?  79   GLY   B CA   1 
ATOM   5237 C  C    . GLY   B 1 79  ? 38.571 -15.697 4.562   1.00 9.98  ?  79   GLY   B C    1 
ATOM   5238 O  O    . GLY   B 1 79  ? 39.185 -16.729 4.302   1.00 10.78 ?  79   GLY   B O    1 
ATOM   5239 H  H    . GLY   B 1 79  ? 37.535 -17.177 6.696   1.00 13.31 ?  79   GLY   B H    1 
ATOM   5240 H  HA2  . GLY   B 1 79  ? 36.582 -15.377 4.927   1.00 12.82 ?  79   GLY   B HA2  1 
ATOM   5241 H  HA3  . GLY   B 1 79  ? 37.487 -15.044 6.169   1.00 12.82 ?  79   GLY   B HA3  1 
ATOM   5242 N  N    . SER   B 1 80  ? 38.932 -14.501 4.092   1.00 10.29 ?  80   SER   B N    1 
ATOM   5243 C  CA   . SER   B 1 80  ? 40.040 -14.367 3.156   1.00 10.17 ?  80   SER   B CA   1 
ATOM   5244 C  C    . SER   B 1 80  ? 40.618 -12.960 3.215   1.00 10.00 ?  80   SER   B C    1 
ATOM   5245 O  O    . SER   B 1 80  ? 39.999 -12.026 3.729   1.00 11.25 ?  80   SER   B O    1 
ATOM   5246 C  CB   . SER   B 1 80  ? 39.590 -14.657 1.719   1.00 10.70 ?  80   SER   B CB   1 
ATOM   5247 O  OG   . SER   B 1 80  ? 38.758 -13.627 1.207   1.00 11.72 ?  80   SER   B OG   1 
ATOM   5248 H  H    . SER   B 1 80  ? 38.555 -13.756 4.300   1.00 12.35 ?  80   SER   B H    1 
ATOM   5249 H  HA   . SER   B 1 80  ? 40.732 -14.999 3.400   1.00 12.21 ?  80   SER   B HA   1 
ATOM   5250 H  HB2  . SER   B 1 80  ? 40.371 -14.729 1.150   1.00 12.84 ?  80   SER   B HB2  1 
ATOM   5251 H  HB3  . SER   B 1 80  ? 39.093 -15.490 1.705   1.00 12.84 ?  80   SER   B HB3  1 
ATOM   5252 H  HG   . SER   B 1 80  ? 38.067 -13.549 1.687   1.00 14.06 ?  80   SER   B HG   1 
ATOM   5253 N  N    . CYS   B 1 81  ? 41.807 -12.814 2.632   1.00 9.82  ?  81   CYS   B N    1 
ATOM   5254 C  CA   . CYS   B 1 81  ? 42.345 -11.498 2.323   1.00 10.08 ?  81   CYS   B CA   1 
ATOM   5255 C  C    . CYS   B 1 81  ? 43.112 -11.577 1.012   1.00 9.49  ?  81   CYS   B C    1 
ATOM   5256 O  O    . CYS   B 1 81  ? 43.622 -12.636 0.633   1.00 10.52 ?  81   CYS   B O    1 
ATOM   5257 C  CB   . CYS   B 1 81  ? 43.239 -10.951 3.445   1.00 10.83 ?  81   CYS   B CB   1 
ATOM   5258 S  SG   . CYS   B 1 81  ? 44.764 -11.884 3.678   1.00 11.08 ?  81   CYS   B SG   1 
ATOM   5259 H  H    . CYS   B 1 81  ? 42.322 -13.464 2.400   1.00 11.78 ?  81   CYS   B H    1 
ATOM   5260 H  HA   . CYS   B 1 81  ? 41.609 -10.876 2.202   1.00 12.10 ?  81   CYS   B HA   1 
ATOM   5261 H  HB2  . CYS   B 1 81  ? 43.479 -10.034 3.241   1.00 13.00 ?  81   CYS   B HB2  1 
ATOM   5262 H  HB3  . CYS   B 1 81  ? 42.742 -10.977 4.283   1.00 13.00 ?  81   CYS   B HB3  1 
ATOM   5263 H  HG   . CYS   B 1 81  ? 45.396 -11.392 4.576   1.00 13.30 ?  81   CYS   B HG   1 
ATOM   5264 N  N    . VAL   B 1 82  ? 43.213 -10.435 0.337   1.00 10.04 ?  82   VAL   B N    1 
ATOM   5265 C  CA   . VAL   B 1 82  ? 43.973 -10.304 -0.904  1.00 10.37 ?  82   VAL   B CA   1 
ATOM   5266 C  C    . VAL   B 1 82  ? 45.314 -9.664  -0.589  1.00 10.26 ?  82   VAL   B C    1 
ATOM   5267 O  O    . VAL   B 1 82  ? 45.368 -8.549  -0.053  1.00 11.47 ?  82   VAL   B O    1 
ATOM   5268 C  CB   . VAL   B 1 82  ? 43.221 -9.460  -1.945  1.00 11.15 ?  82   VAL   B CB   1 
ATOM   5269 C  CG1  . VAL   B 1 82  ? 44.059 -9.309  -3.208  1.00 12.72 ?  82   VAL   B CG1  1 
ATOM   5270 C  CG2  . VAL   B 1 82  ? 41.864 -10.062 -2.255  1.00 12.33 ?  82   VAL   B CG2  1 
ATOM   5271 H  H    . VAL   B 1 82  ? 42.837 -9.694  0.584   1.00 12.04 ?  82   VAL   B H    1 
ATOM   5272 H  HA   . VAL   B 1 82  ? 44.128 -11.183 -1.280  1.00 12.45 ?  82   VAL   B HA   1 
ATOM   5273 H  HB   . VAL   B 1 82  ? 43.070 -8.574  -1.583  1.00 13.38 ?  82   VAL   B HB   1 
ATOM   5274 H  HG11 . VAL   B 1 82  ? 43.490 -8.993  -3.928  1.00 15.26 ?  82   VAL   B HG11 1 
ATOM   5275 H  HG12 . VAL   B 1 82  ? 44.767 -8.665  -3.043  1.00 15.26 ?  82   VAL   B HG12 1 
ATOM   5276 H  HG13 . VAL   B 1 82  ? 44.439 -10.169 -3.440  1.00 15.26 ?  82   VAL   B HG13 1 
ATOM   5277 H  HG21 . VAL   B 1 82  ? 41.427 -9.532  -2.942  1.00 14.80 ?  82   VAL   B HG21 1 
ATOM   5278 H  HG22 . VAL   B 1 82  ? 41.984 -10.973 -2.570  1.00 14.80 ?  82   VAL   B HG22 1 
ATOM   5279 H  HG23 . VAL   B 1 82  ? 41.323 -10.063 -1.448  1.00 14.80 ?  82   VAL   B HG23 1 
ATOM   5280 N  N    . LEU   B 1 83  ? 46.392 -10.348 -0.958  1.00 9.93  ?  83   LEU   B N    1 
ATOM   5281 C  CA   . LEU   B 1 83  ? 47.745 -9.837  -0.840  1.00 9.97  ?  83   LEU   B CA   1 
ATOM   5282 C  C    . LEU   B 1 83  ? 48.442 -9.981  -2.190  1.00 9.77  ?  83   LEU   B C    1 
ATOM   5283 O  O    . LEU   B 1 83  ? 47.840 -10.392 -3.184  1.00 9.87  ?  83   LEU   B O    1 
ATOM   5284 C  CB   . LEU   B 1 83  ? 48.496 -10.517 0.312   1.00 10.33 ?  83   LEU   B CB   1 
ATOM   5285 C  CG   . LEU   B 1 83  ? 47.995 -10.146 1.714   1.00 11.76 ?  83   LEU   B CG   1 
ATOM   5286 C  CD1  . LEU   B 1 83  ? 48.629 -11.004 2.790   1.00 12.05 ?  83   LEU   B CD1  1 
ATOM   5287 C  CD2  . LEU   B 1 83  ? 48.217 -8.663  2.015   1.00 13.04 ?  83   LEU   B CD2  1 
ATOM   5288 H  H    . LEU   B 1 83  ? 46.355 -11.144 -1.294  1.00 11.91 ?  83   LEU   B H    1 
ATOM   5289 H  HA   . LEU   B 1 83  ? 47.694 -8.893  -0.640  1.00 11.96 ?  83   LEU   B HA   1 
ATOM   5290 H  HB2  . LEU   B 1 83  ? 48.415 -11.476 0.217   1.00 12.40 ?  83   LEU   B HB2  1 
ATOM   5291 H  HB3  . LEU   B 1 83  ? 49.433 -10.262 0.260   1.00 12.40 ?  83   LEU   B HB3  1 
ATOM   5292 H  HG   . LEU   B 1 83  ? 47.042 -10.301 1.744   1.00 14.11 ?  83   LEU   B HG   1 
ATOM   5293 H  HD11 . LEU   B 1 83  ? 48.273 -10.739 3.654   1.00 14.46 ?  83   LEU   B HD11 1 
ATOM   5294 H  HD12 . LEU   B 1 83  ? 48.412 -11.934 2.616   1.00 14.46 ?  83   LEU   B HD12 1 
ATOM   5295 H  HD13 . LEU   B 1 83  ? 49.589 -10.878 2.774   1.00 14.46 ?  83   LEU   B HD13 1 
ATOM   5296 H  HD21 . LEU   B 1 83  ? 48.041 -8.500  2.955   1.00 15.64 ?  83   LEU   B HD21 1 
ATOM   5297 H  HD22 . LEU   B 1 83  ? 49.135 -8.429  1.806   1.00 15.64 ?  83   LEU   B HD22 1 
ATOM   5298 H  HD23 . LEU   B 1 83  ? 47.611 -8.133  1.471   1.00 15.64 ?  83   LEU   B HD23 1 
ATOM   5299 N  N    . SER   B 1 84  ? 49.714 -9.602  -2.245  1.00 10.89 ?  84   SER   B N    1 
ATOM   5300 C  CA   . SER   B 1 84  ? 50.452 -9.707  -3.496  1.00 11.39 ?  84   SER   B CA   1 
ATOM   5301 C  C    . SER   B 1 84  ? 50.608 -11.166 -3.918  1.00 10.26 ?  84   SER   B C    1 
ATOM   5302 O  O    . SER   B 1 84  ? 50.729 -12.068 -3.090  1.00 10.12 ?  84   SER   B O    1 
ATOM   5303 C  CB   . SER   B 1 84  ? 51.846 -9.103  -3.346  1.00 13.02 ?  84   SER   B CB   1 
ATOM   5304 O  OG   . SER   B 1 84  ? 52.582 -9.312  -4.533  1.00 14.68 ?  84   SER   B OG   1 
ATOM   5305 H  H    . SER   B 1 84  ? 50.156 -9.270  -1.585  1.00 13.07 ?  84   SER   B H    1 
ATOM   5306 H  HA   . SER   B 1 84  ? 49.980 -9.231  -4.196  1.00 13.66 ?  84   SER   B HA   1 
ATOM   5307 H  HB2  . SER   B 1 84  ? 51.763 -8.146  -3.179  1.00 15.62 ?  84   SER   B HB2  1 
ATOM   5308 H  HB3  . SER   B 1 84  ? 52.304 -9.529  -2.607  1.00 15.62 ?  84   SER   B HB3  1 
ATOM   5309 H  HG   . SER   B 1 84  ? 53.352 -8.971  -4.462  1.00 17.62 ?  84   SER   B HG   1 
ATOM   5310 N  N    . GLY   B 1 85  ? 50.668 -11.385 -5.227  1.00 11.39 ?  85   GLY   B N    1 
ATOM   5311 C  CA   . GLY   B 1 85  ? 51.020 -12.679 -5.761  1.00 12.15 ?  85   GLY   B CA   1 
ATOM   5312 C  C    . GLY   B 1 85  ? 52.490 -12.869 -6.065  1.00 11.42 ?  85   GLY   B C    1 
ATOM   5313 O  O    . GLY   B 1 85  ? 52.862 -13.947 -6.530  1.00 11.62 ?  85   GLY   B O    1 
ATOM   5314 H  H    . GLY   B 1 85  ? 50.517 -10.793 -5.823  1.00 13.67 ?  85   GLY   B H    1 
ATOM   5315 H  HA2  . GLY   B 1 85  ? 50.758 -13.367 -5.127  1.00 14.58 ?  85   GLY   B HA2  1 
ATOM   5316 H  HA3  . GLY   B 1 85  ? 50.531 -12.826 -6.580  1.00 14.58 ?  85   GLY   B HA3  1 
ATOM   5317 N  N    . HIS   B 1 86  ? 53.342 -11.871 -5.833  1.00 11.32 ?  86   HIS   B N    1 
ATOM   5318 C  CA   . HIS   B 1 86  ? 54.801 -12.042 -5.928  1.00 11.35 ?  86   HIS   B CA   1 
ATOM   5319 C  C    . HIS   B 1 86  ? 55.166 -12.550 -7.321  1.00 11.40 ?  86   HIS   B C    1 
ATOM   5320 O  O    . HIS   B 1 86  ? 54.781 -11.926 -8.324  1.00 12.15 ?  86   HIS   B O    1 
ATOM   5321 C  CB   . HIS   B 1 86  ? 55.301 -12.891 -4.758  1.00 11.47 ?  86   HIS   B CB   1 
ATOM   5322 C  CG   . HIS   B 1 86  ? 54.990 -12.290 -3.431  1.00 11.57 ?  86   HIS   B CG   1 
ATOM   5323 N  ND1  . HIS   B 1 86  ? 55.809 -11.364 -2.821  1.00 12.99 ?  86   HIS   B ND1  1 
ATOM   5324 C  CD2  . HIS   B 1 86  ? 53.916 -12.443 -2.623  1.00 11.73 ?  86   HIS   B CD2  1 
ATOM   5325 C  CE1  . HIS   B 1 86  ? 55.251 -10.981 -1.687  1.00 12.81 ?  86   HIS   B CE1  1 
ATOM   5326 N  NE2  . HIS   B 1 86  ? 54.103 -11.621 -1.542  1.00 12.14 ?  86   HIS   B NE2  1 
ATOM   5327 H  H    . HIS   B 1 86  ? 53.104 -11.080 -5.624  1.00 13.59 ?  86   HIS   B H    1 
ATOM   5328 H  HA   . HIS   B 1 86  ? 55.211 -11.170 -5.835  1.00 13.62 ?  86   HIS   B HA   1 
ATOM   5329 H  HB2  . HIS   B 1 86  ? 54.890 -13.766 -4.800  1.00 13.77 ?  86   HIS   B HB2  1 
ATOM   5330 H  HB3  . HIS   B 1 86  ? 56.271 -12.980 -4.825  1.00 13.77 ?  86   HIS   B HB3  1 
ATOM   5331 H  HD2  . HIS   B 1 86  ? 53.188 -13.004 -2.776  1.00 14.07 ?  86   HIS   B HD2  1 
ATOM   5332 H  HE1  . HIS   B 1 86  ? 55.613 -10.377 -1.081  1.00 15.37 ?  86   HIS   B HE1  1 
ATOM   5333 H  HE2  . HIS   B 1 86  ? 53.567 -11.550 -0.874  1.00 14.57 ?  86   HIS   B HE2  1 
ATOM   5334 N  N    . ASN   B 1 87  ? 55.927 -13.637 -7.435  1.00 11.51 ?  87   ASN   B N    1 
ATOM   5335 C  CA   . ASN   B 1 87  ? 56.320 -14.208 -8.713  1.00 12.49 ?  87   ASN   B CA   1 
ATOM   5336 C  C    . ASN   B 1 87  ? 55.340 -15.253 -9.216  1.00 12.02 ?  87   ASN   B C    1 
ATOM   5337 O  O    . ASN   B 1 87  ? 55.652 -15.965 -10.177 1.00 13.64 ?  87   ASN   B O    1 
ATOM   5338 C  CB   . ASN   B 1 87  ? 57.716 -14.830 -8.602  1.00 14.18 ?  87   ASN   B CB   1 
ATOM   5339 C  CG   . ASN   B 1 87  ? 57.782 -15.950 -7.567  1.00 15.13 ?  87   ASN   B CG   1 
ATOM   5340 O  OD1  . ASN   B 1 87  ? 57.148 -15.880 -6.509  1.00 14.27 ?  87   ASN   B OD1  1 
ATOM   5341 N  ND2  . ASN   B 1 87  ? 58.532 -17.006 -7.885  1.00 17.45 ?  87   ASN   B ND2  1 
ATOM   5342 H  H    . ASN   B 1 87  ? 56.235 -14.077 -6.763  1.00 13.82 ?  87   ASN   B H    1 
ATOM   5343 H  HA   . ASN   B 1 87  ? 56.360 -13.500 -9.373  1.00 14.99 ?  87   ASN   B HA   1 
ATOM   5344 H  HB2  . ASN   B 1 87  ? 57.966 -15.200 -9.466  1.00 17.01 ?  87   ASN   B HB2  1 
ATOM   5345 H  HB3  . ASN   B 1 87  ? 58.347 -14.142 -8.343  1.00 17.01 ?  87   ASN   B HB3  1 
ATOM   5346 H  HD21 . ASN   B 1 87  ? 58.605 -17.660 -7.338  1.00 20.94 ?  87   ASN   B HD21 1 
ATOM   5347 H  HD22 . ASN   B 1 87  ? 58.958 -17.021 -8.636  1.00 20.94 ?  87   ASN   B HD22 1 
ATOM   5348 N  N    . LEU   B 1 88  ? 54.164 -15.355 -8.595  1.00 11.09 ?  88   LEU   B N    1 
ATOM   5349 C  CA   . LEU   B 1 88  ? 53.184 -16.384 -8.917  1.00 11.25 ?  88   LEU   B CA   1 
ATOM   5350 C  C    . LEU   B 1 88  ? 51.952 -15.864 -9.634  1.00 10.97 ?  88   LEU   B C    1 
ATOM   5351 O  O    . LEU   B 1 88  ? 51.343 -16.611 -10.409 1.00 12.57 ?  88   LEU   B O    1 
ATOM   5352 C  CB   . LEU   B 1 88  ? 52.717 -17.062 -7.626  1.00 12.20 ?  88   LEU   B CB   1 
ATOM   5353 C  CG   . LEU   B 1 88  ? 53.836 -17.723 -6.834  1.00 14.43 ?  88   LEU   B CG   1 
ATOM   5354 C  CD1  . LEU   B 1 88  ? 53.346 -18.070 -5.440  1.00 15.95 ?  88   LEU   B CD1  1 
ATOM   5355 C  CD2  . LEU   B 1 88  ? 54.299 -18.958 -7.569  1.00 17.49 ?  88   LEU   B CD2  1 
ATOM   5356 H  H    . LEU   B 1 88  ? 53.905 -14.827 -7.958  1.00 13.31 ?  88   LEU   B H    1 
ATOM   5357 H  HA   . LEU   B 1 88  ? 53.596 -17.052 -9.476  1.00 13.50 ?  88   LEU   B HA   1 
ATOM   5358 H  HB2  . LEU   B 1 88  ? 52.302 -16.398 -7.052  1.00 14.64 ?  88   LEU   B HB2  1 
ATOM   5359 H  HB3  . LEU   B 1 88  ? 52.070 -17.750 -7.850  1.00 14.64 ?  88   LEU   B HB3  1 
ATOM   5360 H  HG   . LEU   B 1 88  ? 54.586 -17.109 -6.756  1.00 17.31 ?  88   LEU   B HG   1 
ATOM   5361 H  HD11 . LEU   B 1 88  ? 53.985 -18.669 -5.023  1.00 19.14 ?  88   LEU   B HD11 1 
ATOM   5362 H  HD12 . LEU   B 1 88  ? 53.268 -17.254 -4.921  1.00 19.14 ?  88   LEU   B HD12 1 
ATOM   5363 H  HD13 . LEU   B 1 88  ? 52.483 -18.502 -5.513  1.00 19.14 ?  88   LEU   B HD13 1 
ATOM   5364 H  HD21 . LEU   B 1 88  ? 54.947 -19.426 -7.020  1.00 20.99 ?  88   LEU   B HD21 1 
ATOM   5365 H  HD22 . LEU   B 1 88  ? 53.534 -19.530 -7.737  1.00 20.99 ?  88   LEU   B HD22 1 
ATOM   5366 H  HD23 . LEU   B 1 88  ? 54.707 -18.695 -8.409  1.00 20.99 ?  88   LEU   B HD23 1 
ATOM   5367 N  N    . ALA   B 1 89  ? 51.552 -14.626 -9.371  1.00 10.58 ?  89   ALA   B N    1 
ATOM   5368 C  CA   . ALA   B 1 89  ? 50.255 -14.132 -9.807  1.00 10.22 ?  89   ALA   B CA   1 
ATOM   5369 C  C    . ALA   B 1 89  ? 50.229 -12.641 -9.533  1.00 10.39 ?  89   ALA   B C    1 
ATOM   5370 O  O    . ALA   B 1 89  ? 51.066 -12.121 -8.796  1.00 11.12 ?  89   ALA   B O    1 
ATOM   5371 C  CB   . ALA   B 1 89  ? 49.124 -14.809 -9.035  1.00 10.28 ?  89   ALA   B CB   1 
ATOM   5372 H  H    . ALA   B 1 89  ? 52.009 -14.047 -8.933  1.00 12.70 ?  89   ALA   B H    1 
ATOM   5373 H  HA   . ALA   B 1 89  ? 50.130 -14.290 -10.759 1.00 12.26 ?  89   ALA   B HA   1 
ATOM   5374 H  HB1  . ALA   B 1 89  ? 48.271 -14.475 -9.362  1.00 12.34 ?  89   ALA   B HB1  1 
ATOM   5375 H  HB2  . ALA   B 1 89  ? 49.173 -15.770 -9.179  1.00 12.34 ?  89   ALA   B HB2  1 
ATOM   5376 H  HB3  . ALA   B 1 89  ? 49.220 -14.610 -8.094  1.00 12.34 ?  89   ALA   B HB3  1 
ATOM   5377 N  N    . LYS   B 1 90  ? 49.232 -11.955 -10.085 1.00 11.36 ?  90   LYS   B N    1 
ATOM   5378 C  CA   . LYS   B 1 90  ? 49.046 -10.566 -9.681  1.00 11.56 ?  90   LYS   B CA   1 
ATOM   5379 C  C    . LYS   B 1 90  ? 48.735 -10.489 -8.191  1.00 11.13 ?  90   LYS   B C    1 
ATOM   5380 O  O    . LYS   B 1 90  ? 49.373 -9.736  -7.441  1.00 12.38 ?  90   LYS   B O    1 
ATOM   5381 C  CB   . LYS   B 1 90  ? 47.964 -9.906  -10.538 1.00 13.07 ?  90   LYS   B CB   1 
ATOM   5382 C  CG   . LYS   B 1 90  ? 47.663 -8.464  -10.163 1.00 13.62 ?  90   LYS   B CG   1 
ATOM   5383 C  CD   . LYS   B 1 90  ? 48.867 -7.559  -10.262 1.00 16.64 ?  90   LYS   B CD   1 
ATOM   5384 C  CE   . LYS   B 1 90  ? 48.427 -6.132  -10.037 1.00 18.60 ?  90   LYS   B CE   1 
ATOM   5385 N  NZ   . LYS   B 1 90  ? 49.576 -5.213  -9.885  1.00 18.76 ?  90   LYS   B NZ   1 
ATOM   5386 H  H    . LYS   B 1 90  ? 48.673 -12.257 -10.668 1.00 13.63 ?  90   LYS   B H    1 
ATOM   5387 H  HA   . LYS   B 1 90  ? 49.874 -10.089 -9.839  1.00 13.88 ?  90   LYS   B HA   1 
ATOM   5388 H  HB2  . LYS   B 1 90  ? 48.255 -9.911  -11.467 1.00 15.68 ?  90   LYS   B HB2  1 
ATOM   5389 H  HB3  . LYS   B 1 90  ? 47.144 -10.414 -10.455 1.00 15.68 ?  90   LYS   B HB3  1 
ATOM   5390 H  HG2  . LYS   B 1 90  ? 46.980 -8.119  -10.761 1.00 16.34 ?  90   LYS   B HG2  1 
ATOM   5391 H  HG3  . LYS   B 1 90  ? 47.336 -8.436  -9.247  1.00 16.34 ?  90   LYS   B HG3  1 
ATOM   5392 H  HD2  . LYS   B 1 90  ? 49.512 -7.797  -9.576  1.00 19.96 ?  90   LYS   B HD2  1 
ATOM   5393 H  HD3  . LYS   B 1 90  ? 49.260 -7.633  -11.144 1.00 19.96 ?  90   LYS   B HD3  1 
ATOM   5394 H  HE2  . LYS   B 1 90  ? 47.905 -5.833  -10.800 1.00 22.32 ?  90   LYS   B HE2  1 
ATOM   5395 H  HE3  . LYS   B 1 90  ? 47.895 -6.079  -9.229  1.00 22.32 ?  90   LYS   B HE3  1 
ATOM   5396 H  HZ1  . LYS   B 1 90  ? 49.290 -4.377  -9.757  1.00 22.51 ?  90   LYS   B HZ1  1 
ATOM   5397 H  HZ2  . LYS   B 1 90  ? 50.073 -5.454  -9.188  1.00 22.51 ?  90   LYS   B HZ2  1 
ATOM   5398 H  HZ3  . LYS   B 1 90  ? 50.083 -5.230  -10.619 1.00 22.51 ?  90   LYS   B HZ3  1 
ATOM   5399 N  N    . HIS   B 1 91  ? 47.782 -11.310 -7.742  1.00 9.81  ?  91   HIS   B N    1 
ATOM   5400 C  CA   . HIS   B 1 91  ? 47.312 -11.336 -6.372  1.00 9.96  ?  91   HIS   B CA   1 
ATOM   5401 C  C    . HIS   B 1 91  ? 47.311 -12.763 -5.851  1.00 9.28  ?  91   HIS   B C    1 
ATOM   5402 O  O    . HIS   B 1 91  ? 47.076 -13.715 -6.603  1.00 10.06 ?  91   HIS   B O    1 
ATOM   5403 C  CB   . HIS   B 1 91  ? 45.864 -10.856 -6.260  1.00 11.61 ?  91   HIS   B CB   1 
ATOM   5404 C  CG   . HIS   B 1 91  ? 45.651 -9.449  -6.694  1.00 15.05 ?  91   HIS   B CG   1 
ATOM   5405 N  ND1  . HIS   B 1 91  ? 46.235 -8.374  -6.059  1.00 17.75 ?  91   HIS   B ND1  1 
ATOM   5406 C  CD2  . HIS   B 1 91  ? 44.883 -8.934  -7.679  1.00 17.44 ?  91   HIS   B CD2  1 
ATOM   5407 C  CE1  . HIS   B 1 91  ? 45.852 -7.255  -6.650  1.00 18.67 ?  91   HIS   B CE1  1 
ATOM   5408 N  NE2  . HIS   B 1 91  ? 45.025 -7.568  -7.632  1.00 18.76 ?  91   HIS   B NE2  1 
ATOM   5409 H  H    . HIS   B 1 91  ? 47.381 -11.883 -8.243  1.00 11.77 ?  91   HIS   B H    1 
ATOM   5410 H  HA   . HIS   B 1 91  ? 47.879 -10.779 -5.808  1.00 11.96 ?  91   HIS   B HA   1 
ATOM   5411 H  HB2  . HIS   B 1 91  ? 45.304 -11.421 -6.816  1.00 13.93 ?  91   HIS   B HB2  1 
ATOM   5412 H  HB3  . HIS   B 1 91  ? 45.580 -10.925 -5.334  1.00 13.93 ?  91   HIS   B HB3  1 
ATOM   5413 H  HD1  . HIS   B 1 91  ? 46.769 -8.423  -5.386  1.00 21.31 ?  91   HIS   B HD1  1 
ATOM   5414 H  HD2  . HIS   B 1 91  ? 44.360 -9.405  -8.284  1.00 20.93 ?  91   HIS   B HD2  1 
ATOM   5415 H  HE1  . HIS   B 1 91  ? 46.115 -6.394  -6.406  1.00 22.40 ?  91   HIS   B HE1  1 
ATOM   5416 N  N    . CYS   B 1 92  ? 47.506 -12.895 -4.549  1.00 9.24  ?  92   CYS   B N    1 
ATOM   5417 C  CA   . CYS   B 1 92  ? 47.217 -14.132 -3.839  1.00 9.10  ?  92   CYS   B CA   1 
ATOM   5418 C  C    . CYS   B 1 92  ? 45.998 -13.898 -2.953  1.00 8.75  ?  92   CYS   B C    1 
ATOM   5419 O  O    . CYS   B 1 92  ? 45.999 -12.996 -2.105  1.00 9.76  ?  92   CYS   B O    1 
ATOM   5420 C  CB   . CYS   B 1 92  ? 48.404 -14.593 -2.998  1.00 9.50  ?  92   CYS   B CB   1 
ATOM   5421 S  SG   . CYS   B 1 92  ? 48.039 -16.130 -2.095  1.00 9.66  ?  92   CYS   B SG   1 
ATOM   5422 H  H    . CYS   B 1 92  ? 47.826 -12.272 -4.041  1.00 11.09 ?  92   CYS   B H    1 
ATOM   5423 H  HA   . CYS   B 1 92  ? 47.015 -14.829 -4.482  1.00 10.92 ?  92   CYS   B HA   1 
ATOM   5424 H  HB2  . CYS   B 1 92  ? 49.163 -14.753 -3.574  1.00 11.40 ?  92   CYS   B HB2  1 
ATOM   5425 H  HB3  . CYS   B 1 92  ? 48.614 -13.905 -2.346  1.00 11.40 ?  92   CYS   B HB3  1 
ATOM   5426 H  HG   . CYS   B 1 92  ? 49.014 -16.448 -1.471  1.00 11.60 ?  92   CYS   B HG   1 
ATOM   5427 N  N    . LEU   B 1 93  ? 44.959 -14.701 -3.170  1.00 8.82  ?  93   LEU   B N    1 
ATOM   5428 C  CA   . LEU   B 1 93  ? 43.787 -14.723 -2.305  1.00 8.96  ?  93   LEU   B CA   1 
ATOM   5429 C  C    . LEU   B 1 93  ? 44.016 -15.788 -1.240  1.00 8.52  ?  93   LEU   B C    1 
ATOM   5430 O  O    . LEU   B 1 93  ? 43.973 -16.987 -1.533  1.00 9.08  ?  93   LEU   B O    1 
ATOM   5431 C  CB   . LEU   B 1 93  ? 42.525 -15.011 -3.111  1.00 9.34  ?  93   LEU   B CB   1 
ATOM   5432 C  CG   . LEU   B 1 93  ? 41.230 -15.035 -2.295  1.00 10.12 ?  93   LEU   B CG   1 
ATOM   5433 C  CD1  . LEU   B 1 93  ? 40.870 -13.650 -1.790  1.00 10.44 ?  93   LEU   B CD1  1 
ATOM   5434 C  CD2  . LEU   B 1 93  ? 40.097 -15.614 -3.126  1.00 10.30 ?  93   LEU   B CD2  1 
ATOM   5435 H  H    . LEU   B 1 93  ? 44.915 -15.266 -3.830  1.00 10.58 ?  93   LEU   B H    1 
ATOM   5436 H  HA   . LEU   B 1 93  ? 43.695 -13.863 -1.874  1.00 10.75 ?  93   LEU   B HA   1 
ATOM   5437 H  HB2  . LEU   B 1 93  ? 42.430 -14.322 -3.788  1.00 11.20 ?  93   LEU   B HB2  1 
ATOM   5438 H  HB3  . LEU   B 1 93  ? 42.616 -15.875 -3.534  1.00 11.20 ?  93   LEU   B HB3  1 
ATOM   5439 H  HG   . LEU   B 1 93  ? 41.354 -15.603 -1.523  1.00 12.14 ?  93   LEU   B HG   1 
ATOM   5440 H  HD11 . LEU   B 1 93  ? 40.020 -13.695 -1.322  1.00 12.53 ?  93   LEU   B HD11 1 
ATOM   5441 H  HD12 . LEU   B 1 93  ? 41.562 -13.340 -1.184  1.00 12.53 ?  93   LEU   B HD12 1 
ATOM   5442 H  HD13 . LEU   B 1 93  ? 40.797 -13.043 -2.545  1.00 12.53 ?  93   LEU   B HD13 1 
ATOM   5443 H  HD21 . LEU   B 1 93  ? 39.283 -15.610 -2.600  1.00 12.36 ?  93   LEU   B HD21 1 
ATOM   5444 H  HD22 . LEU   B 1 93  ? 39.978 -15.071 -3.923  1.00 12.36 ?  93   LEU   B HD22 1 
ATOM   5445 H  HD23 . LEU   B 1 93  ? 40.325 -16.523 -3.378  1.00 12.36 ?  93   LEU   B HD23 1 
ATOM   5446 N  N    . HIS   B 1 94  ? 44.296 -15.350 -0.019  1.00 8.49  ?  94   HIS   B N    1 
ATOM   5447 C  CA   . HIS   B 1 94  ? 44.519 -16.258 1.100   1.00 8.65  ?  94   HIS   B CA   1 
ATOM   5448 C  C    . HIS   B 1 94  ? 43.161 -16.619 1.682   1.00 9.05  ?  94   HIS   B C    1 
ATOM   5449 O  O    . HIS   B 1 94  ? 42.488 -15.749 2.235   1.00 10.32 ?  94   HIS   B O    1 
ATOM   5450 C  CB   . HIS   B 1 94  ? 45.391 -15.587 2.158   1.00 9.13  ?  94   HIS   B CB   1 
ATOM   5451 C  CG   . HIS   B 1 94  ? 46.772 -15.283 1.684   1.00 9.00  ?  94   HIS   B CG   1 
ATOM   5452 N  ND1  . HIS   B 1 94  ? 47.801 -16.196 1.765   1.00 9.25  ?  94   HIS   B ND1  1 
ATOM   5453 C  CD2  . HIS   B 1 94  ? 47.274 -14.176 1.082   1.00 9.53  ?  94   HIS   B CD2  1 
ATOM   5454 C  CE1  . HIS   B 1 94  ? 48.887 -15.644 1.254   1.00 9.12  ?  94   HIS   B CE1  1 
ATOM   5455 N  NE2  . HIS   B 1 94  ? 48.598 -14.421 0.836   1.00 9.57  ?  94   HIS   B NE2  1 
ATOM   5456 H  H    . HIS   B 1 94  ? 44.371 -14.513 0.192   1.00 10.19 ?  94   HIS   B H    1 
ATOM   5457 H  HA   . HIS   B 1 94  ? 44.958 -17.064 0.789   1.00 10.38 ?  94   HIS   B HA   1 
ATOM   5458 H  HB2  . HIS   B 1 94  ? 44.975 -14.753 2.425   1.00 10.95 ?  94   HIS   B HB2  1 
ATOM   5459 H  HB3  . HIS   B 1 94  ? 45.463 -16.179 2.925   1.00 10.95 ?  94   HIS   B HB3  1 
ATOM   5460 H  HD2  . HIS   B 1 94  ? 46.817 -13.393 0.888   1.00 11.43 ?  94   HIS   B HD2  1 
ATOM   5461 H  HE1  . HIS   B 1 94  ? 49.720 -16.059 1.205   1.00 10.94 ?  94   HIS   B HE1  1 
ATOM   5462 H  HE2  . HIS   B 1 94  ? 49.154 -13.884 0.468   1.00 11.48 ?  94   HIS   B HE2  1 
ATOM   5463 N  N    . VAL   B 1 95  ? 42.727 -17.870 1.523   1.00 8.93  ?  95   VAL   B N    1 
ATOM   5464 C  CA   . VAL   B 1 95  ? 41.402 -18.311 1.960   1.00 9.00  ?  95   VAL   B CA   1 
ATOM   5465 C  C    . VAL   B 1 95  ? 41.568 -19.351 3.054   1.00 8.97  ?  95   VAL   B C    1 
ATOM   5466 O  O    . VAL   B 1 95  ? 42.341 -20.300 2.893   1.00 9.68  ?  95   VAL   B O    1 
ATOM   5467 C  CB   . VAL   B 1 95  ? 40.584 -18.911 0.802   1.00 9.41  ?  95   VAL   B CB   1 
ATOM   5468 C  CG1  . VAL   B 1 95  ? 39.208 -19.364 1.291   1.00 10.55 ?  95   VAL   B CG1  1 
ATOM   5469 C  CG2  . VAL   B 1 95  ? 40.454 -17.930 -0.331  1.00 9.57  ?  95   VAL   B CG2  1 
ATOM   5470 H  H    . VAL   B 1 95  ? 43.187 -18.497 1.157   1.00 10.71 ?  95   VAL   B H    1 
ATOM   5471 H  HA   . VAL   B 1 95  ? 40.905 -17.560 2.325   1.00 10.80 ?  95   VAL   B HA   1 
ATOM   5472 H  HB   . VAL   B 1 95  ? 41.044 -19.692 0.463   1.00 11.29 ?  95   VAL   B HB   1 
ATOM   5473 H  HG11 . VAL   B 1 95  ? 38.639 -19.549 0.521   1.00 12.66 ?  95   VAL   B HG11 1 
ATOM   5474 H  HG12 . VAL   B 1 95  ? 39.302 -20.173 1.821   1.00 12.66 ?  95   VAL   B HG12 1 
ATOM   5475 H  HG13 . VAL   B 1 95  ? 38.807 -18.663 1.827   1.00 12.66 ?  95   VAL   B HG13 1 
ATOM   5476 H  HG21 . VAL   B 1 95  ? 39.876 -18.311 -1.013  1.00 11.48 ?  95   VAL   B HG21 1 
ATOM   5477 H  HG22 . VAL   B 1 95  ? 40.066 -17.108 0.008   1.00 11.48 ?  95   VAL   B HG22 1 
ATOM   5478 H  HG23 . VAL   B 1 95  ? 41.332 -17.759 -0.698  1.00 11.48 ?  95   VAL   B HG23 1 
ATOM   5479 N  N    . VAL   B 1 96  ? 40.842 -19.183 4.153   1.00 9.54  ?  96   VAL   B N    1 
ATOM   5480 C  CA   . VAL   B 1 96  ? 40.923 -20.102 5.287   1.00 9.95  ?  96   VAL   B CA   1 
ATOM   5481 C  C    . VAL   B 1 96  ? 39.733 -21.061 5.241   1.00 10.55 ?  96   VAL   B C    1 
ATOM   5482 O  O    . VAL   B 1 96  ? 38.613 -20.705 5.625   1.00 11.18 ?  96   VAL   B O    1 
ATOM   5483 C  CB   . VAL   B 1 96  ? 40.977 -19.357 6.622   1.00 10.94 ?  96   VAL   B CB   1 
ATOM   5484 C  CG1  . VAL   B 1 96  ? 41.158 -20.354 7.758   1.00 11.51 ?  96   VAL   B CG1  1 
ATOM   5485 C  CG2  . VAL   B 1 96  ? 42.093 -18.324 6.630   1.00 11.66 ?  96   VAL   B CG2  1 
ATOM   5486 H  H    . VAL   B 1 96  ? 40.287 -18.537 4.273   1.00 11.45 ?  96   VAL   B H    1 
ATOM   5487 H  HA   . VAL   B 1 96  ? 41.738 -20.628 5.209   1.00 11.94 ?  96   VAL   B HA   1 
ATOM   5488 H  HB   . VAL   B 1 96  ? 40.137 -18.896 6.765   1.00 13.13 ?  96   VAL   B HB   1 
ATOM   5489 H  HG11 . VAL   B 1 96  ? 41.356 -19.870 8.580   1.00 13.81 ?  96   VAL   B HG11 1 
ATOM   5490 H  HG12 . VAL   B 1 96  ? 40.346 -20.869 7.871   1.00 13.81 ?  96   VAL   B HG12 1 
ATOM   5491 H  HG13 . VAL   B 1 96  ? 41.901 -20.947 7.548   1.00 13.81 ?  96   VAL   B HG13 1 
ATOM   5492 H  HG21 . VAL   B 1 96  ? 42.149 -17.919 7.512   1.00 13.99 ?  96   VAL   B HG21 1 
ATOM   5493 H  HG22 . VAL   B 1 96  ? 42.932 -18.756 6.411   1.00 13.99 ?  96   VAL   B HG22 1 
ATOM   5494 H  HG23 . VAL   B 1 96  ? 41.894 -17.638 5.969   1.00 13.99 ?  96   VAL   B HG23 1 
ATOM   5495 N  N    . GLY   B 1 97  ? 39.972 -22.297 4.802   1.00 10.59 ?  97   GLY   B N    1 
ATOM   5496 C  CA   . GLY   B 1 97  ? 39.005 -23.357 4.968   1.00 11.17 ?  97   GLY   B CA   1 
ATOM   5497 C  C    . GLY   B 1 97  ? 39.126 -23.957 6.350   1.00 11.77 ?  97   GLY   B C    1 
ATOM   5498 O  O    . GLY   B 1 97  ? 40.168 -23.834 7.005   1.00 12.36 ?  97   GLY   B O    1 
ATOM   5499 H  H    . GLY   B 1 97  ? 40.695 -22.541 4.399   1.00 12.71 ?  97   GLY   B H    1 
ATOM   5500 H  HA2  . GLY   B 1 97  ? 38.110 -22.995 4.847   1.00 13.40 ?  97   GLY   B HA2  1 
ATOM   5501 H  HA3  . GLY   B 1 97  ? 39.153 -24.047 4.302   1.00 13.40 ?  97   GLY   B HA3  1 
ATOM   5502 N  N    . PRO   B 1 98  ? 38.072 -24.627 6.820   1.00 12.71 ?  98   PRO   B N    1 
ATOM   5503 C  CA   . PRO   B 1 98  ? 38.158 -25.325 8.107   1.00 13.39 ?  98   PRO   B CA   1 
ATOM   5504 C  C    . PRO   B 1 98  ? 39.183 -26.448 8.059   1.00 13.12 ?  98   PRO   B C    1 
ATOM   5505 O  O    . PRO   B 1 98  ? 39.283 -27.185 7.079   1.00 13.49 ?  98   PRO   B O    1 
ATOM   5506 C  CB   . PRO   B 1 98  ? 36.737 -25.866 8.305   1.00 14.05 ?  98   PRO   B CB   1 
ATOM   5507 C  CG   . PRO   B 1 98  ? 36.193 -26.003 6.925   1.00 13.76 ?  98   PRO   B CG   1 
ATOM   5508 C  CD   . PRO   B 1 98  ? 36.762 -24.828 6.174   1.00 12.56 ?  98   PRO   B CD   1 
ATOM   5509 H  HA   . PRO   B 1 98  ? 38.377 -24.706 8.817   1.00 16.07 ?  98   PRO   B HA   1 
ATOM   5510 H  HB2  . PRO   B 1 98  ? 36.771 -26.729 8.744   1.00 16.86 ?  98   PRO   B HB2  1 
ATOM   5511 H  HB3  . PRO   B 1 98  ? 36.212 -25.234 8.817   1.00 16.86 ?  98   PRO   B HB3  1 
ATOM   5512 H  HG2  . PRO   B 1 98  ? 36.494 -26.839 6.534   1.00 16.51 ?  98   PRO   B HG2  1 
ATOM   5513 H  HG3  . PRO   B 1 98  ? 35.226 -25.959 6.945   1.00 16.51 ?  98   PRO   B HG3  1 
ATOM   5514 H  HD2  . PRO   B 1 98  ? 36.875 -25.049 5.229   1.00 15.07 ?  98   PRO   B HD2  1 
ATOM   5515 H  HD3  . PRO   B 1 98  ? 36.209 -24.042 6.287   1.00 15.07 ?  98   PRO   B HD3  1 
ATOM   5516 N  N    . ASN   B 1 99  ? 39.938 -26.577 9.140   1.00 13.91 ?  99   ASN   B N    1 
ATOM   5517 C  CA   . ASN   B 1 99  ? 40.917 -27.647 9.299   1.00 14.82 ?  99   ASN   B CA   1 
ATOM   5518 C  C    . ASN   B 1 99  ? 40.287 -28.734 10.171  1.00 17.13 ?  99   ASN   B C    1 
ATOM   5519 O  O    . ASN   B 1 99  ? 40.205 -28.596 11.394  1.00 17.83 ?  99   ASN   B O    1 
ATOM   5520 C  CB   . ASN   B 1 99  ? 42.194 -27.090 9.914   1.00 15.16 ?  99   ASN   B CB   1 
ATOM   5521 C  CG   . ASN   B 1 99  ? 43.325 -28.098 9.917   1.00 16.19 ?  99   ASN   B CG   1 
ATOM   5522 O  OD1  . ASN   B 1 99  ? 43.096 -29.291 10.077  1.00 17.10 ?  99   ASN   B OD1  1 
ATOM   5523 N  ND2  . ASN   B 1 99  ? 44.548 -27.625 9.734   1.00 16.62 ?  99   ASN   B ND2  1 
ATOM   5524 H  H    . ASN   B 1 99  ? 39.897 -26.044 9.814   1.00 16.69 ?  99   ASN   B H    1 
ATOM   5525 H  HA   . ASN   B 1 99  ? 41.128 -28.032 8.435   1.00 17.79 ?  99   ASN   B HA   1 
ATOM   5526 H  HB2  . ASN   B 1 99  ? 42.477 -26.319 9.409   1.00 18.19 ?  99   ASN   B HB2  1 
ATOM   5527 H  HB3  . ASN   B 1 99  ? 42.010 -26.837 10.838  1.00 18.19 ?  99   ASN   B HB3  1 
ATOM   5528 H  HD21 . ASN   B 1 99  ? 45.219 -28.161 9.732   1.00 19.95 ?  99   ASN   B HD21 1 
ATOM   5529 H  HD22 . ASN   B 1 99  ? 44.665 -26.782 9.628   1.00 19.95 ?  99   ASN   B HD22 1 
ATOM   5530 N  N    A VAL   B 1 100 ? 39.830 -29.814 9.532   0.50 19.20 ?  100  VAL   B N    1 
ATOM   5531 N  N    B VAL   B 1 100 ? 39.833 -29.813 9.527   0.50 19.15 ?  100  VAL   B N    1 
ATOM   5532 C  CA   A VAL   B 1 100 ? 39.206 -30.908 10.273  0.50 21.60 ?  100  VAL   B CA   1 
ATOM   5533 C  CA   B VAL   B 1 100 ? 39.206 -30.919 10.249  0.50 21.48 ?  100  VAL   B CA   1 
ATOM   5534 C  C    A VAL   B 1 100 ? 40.208 -31.566 11.212  0.50 21.97 ?  100  VAL   B C    1 
ATOM   5535 C  C    B VAL   B 1 100 ? 40.199 -31.596 11.187  0.50 21.84 ?  100  VAL   B C    1 
ATOM   5536 O  O    A VAL   B 1 100 ? 39.839 -32.046 12.291  0.50 22.51 ?  100  VAL   B O    1 
ATOM   5537 O  O    B VAL   B 1 100 ? 39.814 -32.124 12.237  0.50 22.21 ?  100  VAL   B O    1 
ATOM   5538 C  CB   A VAL   B 1 100 ? 38.567 -31.920 9.302   0.50 23.86 ?  100  VAL   B CB   1 
ATOM   5539 C  CB   B VAL   B 1 100 ? 38.579 -31.912 9.247   0.50 23.68 ?  100  VAL   B CB   1 
ATOM   5540 C  CG1  A VAL   B 1 100 ? 38.085 -33.154 10.053  0.50 24.79 ?  100  VAL   B CG1  1 
ATOM   5541 C  CG1  B VAL   B 1 100 ? 38.088 -33.163 9.959   0.50 24.59 ?  100  VAL   B CG1  1 
ATOM   5542 C  CG2  A VAL   B 1 100 ? 37.416 -31.273 8.548   0.50 24.47 ?  100  VAL   B CG2  1 
ATOM   5543 C  CG2  B VAL   B 1 100 ? 37.438 -31.247 8.490   0.50 24.28 ?  100  VAL   B CG2  1 
ATOM   5544 H  H    A VAL   B 1 100 ? 39.869 -29.934 8.680   0.50 23.05 ?  100  VAL   B H    1 
ATOM   5545 H  H    B VAL   B 1 100 ? 39.870 -29.923 8.674   0.50 22.98 ?  100  VAL   B H    1 
ATOM   5546 H  HA   A VAL   B 1 100 ? 38.490 -30.542 10.815  0.50 25.92 ?  100  VAL   B HA   1 
ATOM   5547 H  HA   B VAL   B 1 100 ? 38.485 -30.565 10.790  0.50 25.77 ?  100  VAL   B HA   1 
ATOM   5548 H  HB   A VAL   B 1 100 ? 39.231 -32.205 8.655   0.50 28.63 ?  100  VAL   B HB   1 
ATOM   5549 H  HB   B VAL   B 1 100 ? 39.252 -32.181 8.602   0.50 28.42 ?  100  VAL   B HB   1 
ATOM   5550 H  HG11 A VAL   B 1 100 ? 37.489 -33.661 9.478   0.50 29.75 ?  100  VAL   B HG11 1 
ATOM   5551 H  HG11 B VAL   B 1 100 ? 37.508 -33.660 9.359   0.50 29.51 ?  100  VAL   B HG11 1 
ATOM   5552 H  HG12 A VAL   B 1 100 ? 38.849 -33.701 10.296  0.50 29.75 ?  100  VAL   B HG12 1 
ATOM   5553 H  HG12 B VAL   B 1 100 ? 38.849 -33.711 10.206  0.50 29.51 ?  100  VAL   B HG12 1 
ATOM   5554 H  HG13 A VAL   B 1 100 ? 37.610 -32.874 10.852  0.50 29.75 ?  100  VAL   B HG13 1 
ATOM   5555 H  HG13 B VAL   B 1 100 ? 37.593 -32.903 10.752  0.50 29.51 ?  100  VAL   B HG13 1 
ATOM   5556 H  HG21 A VAL   B 1 100 ? 37.033 -31.923 7.938   0.50 29.36 ?  100  VAL   B HG21 1 
ATOM   5557 H  HG21 B VAL   B 1 100 ? 37.053 -31.889 7.872   0.50 29.14 ?  100  VAL   B HG21 1 
ATOM   5558 H  HG22 A VAL   B 1 100 ? 36.745 -30.984 9.187   0.50 29.36 ?  100  VAL   B HG22 1 
ATOM   5559 H  HG22 B VAL   B 1 100 ? 36.766 -30.956 9.126   0.50 29.14 ?  100  VAL   B HG22 1 
ATOM   5560 H  HG23 A VAL   B 1 100 ? 37.753 -30.512 8.053   0.50 29.36 ?  100  VAL   B HG23 1 
ATOM   5561 H  HG23 B VAL   B 1 100 ? 37.785 -30.485 8.002   0.50 29.14 ?  100  VAL   B HG23 1 
ATOM   5562 N  N    . ASN   B 1 101 ? 41.484 -31.616 10.819  1.00 22.34 ?  101  ASN   B N    1 
ATOM   5563 C  CA   . ASN   B 1 101 ? 42.516 -32.156 11.704  1.00 24.50 ?  101  ASN   B CA   1 
ATOM   5564 C  C    . ASN   B 1 101 ? 42.699 -31.324 12.969  1.00 26.51 ?  101  ASN   B C    1 
ATOM   5565 O  O    . ASN   B 1 101 ? 43.324 -31.802 13.925  1.00 27.66 ?  101  ASN   B O    1 
ATOM   5566 C  CB   . ASN   B 1 101 ? 43.845 -32.278 10.954  1.00 24.50 ?  101  ASN   B CB   1 
ATOM   5567 C  CG   . ASN   B 1 101 ? 43.840 -33.411 9.946   1.00 24.17 ?  101  ASN   B CG   1 
ATOM   5568 O  OD1  . ASN   B 1 101 ? 43.160 -34.415 10.134  1.00 25.00 ?  101  ASN   B OD1  1 
ATOM   5569 N  ND2  . ASN   B 1 101 ? 44.594 -33.248 8.865   1.00 23.75 ?  101  ASN   B ND2  1 
ATOM   5570 H  H    A ASN   B 1 101 ? 41.764 -31.361 10.048  0.50 26.81 ?  101  ASN   B H    1 
ATOM   5571 H  H    B ASN   B 1 101 ? 41.773 -31.338 10.059  0.50 26.81 ?  101  ASN   B H    1 
ATOM   5572 H  HA   . ASN   B 1 101 ? 42.253 -33.039 11.983  1.00 29.40 ?  101  ASN   B HA   1 
ATOM   5573 H  HB2  . ASN   B 1 101 ? 44.025 -31.454 10.475  1.00 29.39 ?  101  ASN   B HB2  1 
ATOM   5574 H  HB3  . ASN   B 1 101 ? 44.553 -32.450 11.593  1.00 29.39 ?  101  ASN   B HB3  1 
ATOM   5575 H  HD21 . ASN   B 1 101 ? 44.625 -33.866 8.267   1.00 28.50 ?  101  ASN   B HD21 1 
ATOM   5576 H  HD22 . ASN   B 1 101 ? 45.057 -32.531 8.768   1.00 28.50 ?  101  ASN   B HD22 1 
ATOM   5577 N  N    . LYS   B 1 102 ? 42.177 -30.095 12.990  1.00 28.47 ?  102  LYS   B N    1 
ATOM   5578 C  CA   . LYS   B 1 102 ? 42.161 -29.251 14.178  1.00 31.26 ?  102  LYS   B CA   1 
ATOM   5579 C  C    . LYS   B 1 102 ? 40.783 -29.188 14.825  1.00 30.56 ?  102  LYS   B C    1 
ATOM   5580 O  O    . LYS   B 1 102 ? 40.570 -28.372 15.726  1.00 31.14 ?  102  LYS   B O    1 
ATOM   5581 C  CB   . LYS   B 1 102 ? 42.606 -27.828 13.833  1.00 35.02 ?  102  LYS   B CB   1 
ATOM   5582 C  CG   . LYS   B 1 102 ? 44.068 -27.667 13.459  1.00 38.36 ?  102  LYS   B CG   1 
ATOM   5583 C  CD   . LYS   B 1 102 ? 44.305 -26.259 12.930  1.00 41.41 ?  102  LYS   B CD   1 
ATOM   5584 C  CE   . LYS   B 1 102 ? 45.780 -25.916 12.827  1.00 43.80 ?  102  LYS   B CE   1 
ATOM   5585 N  NZ   . LYS   B 1 102 ? 45.970 -24.516 12.341  1.00 44.93 ?  102  LYS   B NZ   1 
ATOM   5586 H  H    . LYS   B 1 102 ? 41.805 -29.717 12.308  1.00 34.16 ?  102  LYS   B H    1 
ATOM   5587 H  HA   . LYS   B 1 102 ? 42.788 -29.606 14.826  1.00 37.51 ?  102  LYS   B HA   1 
ATOM   5588 H  HB2  . LYS   B 1 102 ? 42.079 -27.511 13.085  1.00 42.03 ?  102  LYS   B HB2  1 
ATOM   5589 H  HB3  . LYS   B 1 102 ? 42.444 -27.258 14.605  1.00 42.03 ?  102  LYS   B HB3  1 
ATOM   5590 H  HG2  . LYS   B 1 102 ? 44.624 -27.802 14.243  1.00 46.03 ?  102  LYS   B HG2  1 
ATOM   5591 H  HG3  . LYS   B 1 102 ? 44.297 -28.303 12.763  1.00 46.03 ?  102  LYS   B HG3  1 
ATOM   5592 H  HD2  . LYS   B 1 102 ? 43.917 -26.184 12.044  1.00 49.69 ?  102  LYS   B HD2  1 
ATOM   5593 H  HD3  . LYS   B 1 102 ? 43.889 -25.621 13.531  1.00 49.69 ?  102  LYS   B HD3  1 
ATOM   5594 H  HE2  . LYS   B 1 102 ? 46.191 -25.994 13.702  1.00 52.56 ?  102  LYS   B HE2  1 
ATOM   5595 H  HE3  . LYS   B 1 102 ? 46.207 -26.518 12.198  1.00 52.56 ?  102  LYS   B HE3  1 
ATOM   5596 H  HZ1  . LYS   B 1 102 ? 46.838 -24.328 12.285  1.00 53.92 ?  102  LYS   B HZ1  1 
ATOM   5597 H  HZ2  . LYS   B 1 102 ? 45.601 -24.420 11.537  1.00 53.92 ?  102  LYS   B HZ2  1 
ATOM   5598 H  HZ3  . LYS   B 1 102 ? 45.586 -23.943 12.905  1.00 53.92 ?  102  LYS   B HZ3  1 
ATOM   5599 N  N    . GLY   B 1 103 ? 39.838 -30.009 14.372  1.00 29.60 ?  103  GLY   B N    1 
ATOM   5600 C  CA   . GLY   B 1 103 ? 38.511 -30.040 14.952  1.00 29.06 ?  103  GLY   B CA   1 
ATOM   5601 C  C    . GLY   B 1 103 ? 37.568 -28.959 14.475  1.00 27.82 ?  103  GLY   B C    1 
ATOM   5602 O  O    . GLY   B 1 103 ? 36.473 -28.825 15.034  1.00 28.54 ?  103  GLY   B O    1 
ATOM   5603 H  H    . GLY   B 1 103 ? 39.947 -30.558 13.722  1.00 35.52 ?  103  GLY   B H    1 
ATOM   5604 H  HA2  . GLY   B 1 103 ? 38.102 -30.894 14.751  1.00 34.87 ?  103  GLY   B HA2  1 
ATOM   5605 H  HA3  . GLY   B 1 103 ? 38.589 -29.965 15.917  1.00 34.87 ?  103  GLY   B HA3  1 
ATOM   5606 N  N    A GLU   B 1 104 ? 37.965 -28.171 13.479  0.50 26.86 ?  104  GLU   B N    1 
ATOM   5607 N  N    B GLU   B 1 104 ? 37.934 -28.203 13.445  0.50 26.52 ?  104  GLU   B N    1 
ATOM   5608 C  CA   A GLU   B 1 104 ? 37.138 -27.066 13.020  0.50 25.73 ?  104  GLU   B CA   1 
ATOM   5609 C  CA   B GLU   B 1 104 ? 37.082 -27.124 12.970  0.50 25.06 ?  104  GLU   B CA   1 
ATOM   5610 C  C    A GLU   B 1 104 ? 35.958 -27.583 12.203  0.50 26.35 ?  104  GLU   B C    1 
ATOM   5611 C  C    B GLU   B 1 104 ? 35.925 -27.668 12.137  0.50 25.46 ?  104  GLU   B C    1 
ATOM   5612 O  O    A GLU   B 1 104 ? 36.006 -28.665 11.609  0.50 27.11 ?  104  GLU   B O    1 
ATOM   5613 O  O    B GLU   B 1 104 ? 36.006 -28.748 11.544  0.50 26.26 ?  104  GLU   B O    1 
ATOM   5614 C  CB   A GLU   B 1 104 ? 37.984 -26.083 12.210  0.50 24.54 ?  104  GLU   B CB   1 
ATOM   5615 C  CB   B GLU   B 1 104 ? 37.910 -26.110 12.181  0.50 23.73 ?  104  GLU   B CB   1 
ATOM   5616 C  CG   A GLU   B 1 104 ? 39.098 -25.455 13.039  0.50 23.48 ?  104  GLU   B CG   1 
ATOM   5617 C  CG   B GLU   B 1 104 ? 38.989 -25.475 13.042  0.50 22.51 ?  104  GLU   B CG   1 
ATOM   5618 C  CD   A GLU   B 1 104 ? 40.024 -24.564 12.239  0.50 22.34 ?  104  GLU   B CD   1 
ATOM   5619 C  CD   B GLU   B 1 104 ? 39.957 -24.605 12.272  0.50 21.15 ?  104  GLU   B CD   1 
ATOM   5620 O  OE1  A GLU   B 1 104 ? 40.008 -24.626 10.992  0.50 20.71 ?  104  GLU   B OE1  1 
ATOM   5621 O  OE1  B GLU   B 1 104 ? 39.947 -24.626 11.022  0.50 19.78 ?  104  GLU   B OE1  1 
ATOM   5622 O  OE2  A GLU   B 1 104 ? 40.772 -23.791 12.872  0.50 22.89 -1 104  GLU   B OE2  1 
ATOM   5623 O  OE2  B GLU   B 1 104 ? 40.736 -23.892 12.936  0.50 21.19 -1 104  GLU   B OE2  1 
ATOM   5624 H  H    A GLU   B 1 104 ? 38.711 -28.254 13.060  0.50 32.23 ?  104  GLU   B H    1 
ATOM   5625 H  H    B GLU   B 1 104 ? 38.671 -28.292 13.010  0.50 31.82 ?  104  GLU   B H    1 
ATOM   5626 H  HA   A GLU   B 1 104 ? 36.789 -26.590 13.792  0.50 30.88 ?  104  GLU   B HA   1 
ATOM   5627 H  HA   B GLU   B 1 104 ? 36.708 -26.664 13.737  0.50 30.07 ?  104  GLU   B HA   1 
ATOM   5628 H  HB2  A GLU   B 1 104 ? 38.393 -26.551 11.466  0.50 29.44 ?  104  GLU   B HB2  1 
ATOM   5629 H  HB2  B GLU   B 1 104 ? 38.339 -26.557 11.436  0.50 28.47 ?  104  GLU   B HB2  1 
ATOM   5630 H  HB3  A GLU   B 1 104 ? 37.417 -25.367 11.882  0.50 29.44 ?  104  GLU   B HB3  1 
ATOM   5631 H  HB3  B GLU   B 1 104 ? 37.326 -25.405 11.858  0.50 28.47 ?  104  GLU   B HB3  1 
ATOM   5632 H  HG2  A GLU   B 1 104 ? 38.705 -24.909 13.738  0.50 28.17 ?  104  GLU   B HG2  1 
ATOM   5633 H  HG2  B GLU   B 1 104 ? 38.566 -24.919 13.716  0.50 27.01 ?  104  GLU   B HG2  1 
ATOM   5634 H  HG3  A GLU   B 1 104 ? 39.636 -26.158 13.435  0.50 28.17 ?  104  GLU   B HG3  1 
ATOM   5635 H  HG3  B GLU   B 1 104 ? 39.503 -26.176 13.472  0.50 27.01 ?  104  GLU   B HG3  1 
ATOM   5636 N  N    A ASP   B 1 105 ? 34.886 -26.796 12.186  0.50 26.36 ?  105  ASP   B N    1 
ATOM   5637 N  N    B ASP   B 1 105 ? 34.835 -26.902 12.107  0.50 25.11 ?  105  ASP   B N    1 
ATOM   5638 C  CA   A ASP   B 1 105 ? 33.614 -27.251 11.638  0.50 26.96 ?  105  ASP   B CA   1 
ATOM   5639 C  CA   B ASP   B 1 105 ? 33.567 -27.373 11.562  0.50 25.42 ?  105  ASP   B CA   1 
ATOM   5640 C  C    A ASP   B 1 105 ? 33.675 -27.306 10.116  0.50 25.43 ?  105  ASP   B C    1 
ATOM   5641 C  C    B ASP   B 1 105 ? 33.619 -27.390 10.038  0.50 24.06 ?  105  ASP   B C    1 
ATOM   5642 O  O    A ASP   B 1 105 ? 33.848 -26.277 9.454   0.50 24.85 ?  105  ASP   B O    1 
ATOM   5643 O  O    B ASP   B 1 105 ? 33.787 -26.343 9.403   0.50 23.41 ?  105  ASP   B O    1 
ATOM   5644 C  CB   A ASP   B 1 105 ? 32.501 -26.308 12.089  0.50 29.39 ?  105  ASP   B CB   1 
ATOM   5645 C  CB   B ASP   B 1 105 ? 32.431 -26.474 12.048  0.50 27.42 ?  105  ASP   B CB   1 
ATOM   5646 C  CG   A ASP   B 1 105 ? 31.128 -26.771 11.646  0.50 31.41 ?  105  ASP   B CG   1 
ATOM   5647 C  CG   B ASP   B 1 105 ? 31.059 -27.049 11.738  0.50 28.89 ?  105  ASP   B CG   1 
ATOM   5648 O  OD1  A ASP   B 1 105 ? 31.007 -27.915 11.160  0.50 31.80 ?  105  ASP   B OD1  1 
ATOM   5649 O  OD1  B ASP   B 1 105 ? 30.976 -28.004 10.938  0.50 29.27 ?  105  ASP   B OD1  1 
ATOM   5650 O  OD2  A ASP   B 1 105 ? 30.169 -25.979 11.772  0.50 32.63 -1 105  ASP   B OD2  1 
ATOM   5651 O  OD2  B ASP   B 1 105 ? 30.062 -26.556 12.309  0.50 29.15 -1 105  ASP   B OD2  1 
ATOM   5652 H  H    A ASP   B 1 105 ? 34.873 -25.990 12.488  0.50 31.63 ?  105  ASP   B H    1 
ATOM   5653 H  H    B ASP   B 1 105 ? 34.808 -26.095 12.399  0.50 30.13 ?  105  ASP   B H    1 
ATOM   5654 H  HA   A ASP   B 1 105 ? 33.422 -28.142 11.972  0.50 32.35 ?  105  ASP   B HA   1 
ATOM   5655 H  HA   B ASP   B 1 105 ? 33.393 -28.275 11.873  0.50 30.50 ?  105  ASP   B HA   1 
ATOM   5656 H  HB2  A ASP   B 1 105 ? 32.526 -26.234 13.060  0.50 35.26 ?  105  ASP   B HB2  1 
ATOM   5657 H  HB2  B ASP   B 1 105 ? 32.504 -26.363 13.010  0.50 32.91 ?  105  ASP   B HB2  1 
ATOM   5658 H  HB3  A ASP   B 1 105 ? 32.638 -25.440 11.687  0.50 35.26 ?  105  ASP   B HB3  1 
ATOM   5659 H  HB3  B ASP   B 1 105 ? 32.506 -25.607 11.613  0.50 32.91 ?  105  ASP   B HB3  1 
ATOM   5660 N  N    A ILE   B 1 106 ? 33.506 -28.511 9.563   0.50 24.95 ?  106  ILE   B N    1 
ATOM   5661 N  N    B ILE   B 1 106 ? 33.450 -28.581 9.456   0.50 23.73 ?  106  ILE   B N    1 
ATOM   5662 C  CA   A ILE   B 1 106 ? 33.507 -28.697 8.117   0.50 24.30 ?  106  ILE   B CA   1 
ATOM   5663 C  CA   B ILE   B 1 106 ? 33.450 -28.734 8.006   0.50 23.41 ?  106  ILE   B CA   1 
ATOM   5664 C  C    A ILE   B 1 106 ? 32.408 -27.885 7.441   0.50 23.34 ?  106  ILE   B C    1 
ATOM   5665 C  C    B ILE   B 1 106 ? 32.359 -27.898 7.351   0.50 22.69 ?  106  ILE   B C    1 
ATOM   5666 O  O    A ILE   B 1 106 ? 32.510 -27.578 6.249   0.50 22.71 ?  106  ILE   B O    1 
ATOM   5667 O  O    B ILE   B 1 106 ? 32.460 -27.568 6.164   0.50 21.98 ?  106  ILE   B O    1 
ATOM   5668 C  CB   A ILE   B 1 106 ? 33.403 -30.205 7.791   0.50 24.92 ?  106  ILE   B CB   1 
ATOM   5669 C  CB   B ILE   B 1 106 ? 33.339 -30.233 7.641   0.50 24.14 ?  106  ILE   B CB   1 
ATOM   5670 C  CG1  A ILE   B 1 106 ? 33.642 -30.463 6.301   0.50 25.18 ?  106  ILE   B CG1  1 
ATOM   5671 C  CG1  B ILE   B 1 106 ? 33.640 -30.459 6.158   0.50 24.57 ?  106  ILE   B CG1  1 
ATOM   5672 C  CG2  A ILE   B 1 106 ? 32.047 -30.757 8.220   0.50 25.28 ?  106  ILE   B CG2  1 
ATOM   5673 C  CG2  B ILE   B 1 106 ? 31.956 -30.773 7.991   0.50 24.55 ?  106  ILE   B CG2  1 
ATOM   5674 C  CD1  A ILE   B 1 106 ? 34.999 -30.006 5.819   0.50 25.27 ?  106  ILE   B CD1  1 
ATOM   5675 C  CD1  B ILE   B 1 106 ? 35.018 -29.997 5.745   0.50 24.76 ?  106  ILE   B CD1  1 
ATOM   5676 H  H    A ILE   B 1 106 ? 33.392 -29.234 10.010  0.50 29.94 ?  106  ILE   B H    1 
ATOM   5677 H  H    B ILE   B 1 106 ? 33.336 -29.315 9.885   0.50 28.48 ?  106  ILE   B H    1 
ATOM   5678 H  HA   A ILE   B 1 106 ? 34.353 -28.377 7.774   0.50 29.16 ?  106  ILE   B HA   1 
ATOM   5679 H  HA   B ILE   B 1 106 ? 34.296 -28.409 7.671   0.50 28.09 ?  106  ILE   B HA   1 
ATOM   5680 H  HB   A ILE   B 1 106 ? 34.090 -30.671 8.291   0.50 29.90 ?  106  ILE   B HB   1 
ATOM   5681 H  HB   B ILE   B 1 106 ? 33.996 -30.722 8.162   0.50 28.97 ?  106  ILE   B HB   1 
ATOM   5682 H  HG12 A ILE   B 1 106 ? 33.579 -31.418 6.135   0.50 30.22 ?  106  ILE   B HG12 1 
ATOM   5683 H  HG12 B ILE   B 1 106 ? 33.581 -31.410 5.968   0.50 29.48 ?  106  ILE   B HG12 1 
ATOM   5684 H  HG13 A ILE   B 1 106 ? 32.970 -29.995 5.785   0.50 30.22 ?  106  ILE   B HG13 1 
ATOM   5685 H  HG13 B ILE   B 1 106 ? 32.992 -29.976 5.626   0.50 29.48 ?  106  ILE   B HG13 1 
ATOM   5686 H  HG21 A ILE   B 1 106 ? 32.058 -31.722 8.127   0.50 30.33 ?  106  ILE   B HG21 1 
ATOM   5687 H  HG21 B ILE   B 1 106 ? 31.970 -31.741 7.923   0.50 29.46 ?  106  ILE   B HG21 1 
ATOM   5688 H  HG22 A ILE   B 1 106 ? 31.888 -30.516 9.146   0.50 30.33 ?  106  ILE   B HG22 1 
ATOM   5689 H  HG22 B ILE   B 1 106 ? 31.736 -30.509 8.898   0.50 29.46 ?  106  ILE   B HG22 1 
ATOM   5690 H  HG23 A ILE   B 1 106 ? 31.356 -30.378 7.656   0.50 30.33 ?  106  ILE   B HG23 1 
ATOM   5691 H  HG23 B ILE   B 1 106 ? 31.306 -30.407 7.372   0.50 29.46 ?  106  ILE   B HG23 1 
ATOM   5692 H  HD11 A ILE   B 1 106 ? 35.181 -30.411 4.958   0.50 30.32 ?  106  ILE   B HD11 1 
ATOM   5693 H  HD11 B ILE   B 1 106 ? 35.249 -30.410 4.900   0.50 29.71 ?  106  ILE   B HD11 1 
ATOM   5694 H  HD12 A ILE   B 1 106 ? 34.997 -29.039 5.735   0.50 30.32 ?  106  ILE   B HD12 1 
ATOM   5695 H  HD12 B ILE   B 1 106 ? 35.012 -29.031 5.651   0.50 29.71 ?  106  ILE   B HD12 1 
ATOM   5696 H  HD13 A ILE   B 1 106 ? 35.673 -30.281 6.462   0.50 30.32 ?  106  ILE   B HD13 1 
ATOM   5697 H  HD13 B ILE   B 1 106 ? 35.657 -30.260 6.428   0.50 29.71 ?  106  ILE   B HD13 1 
ATOM   5698 N  N    A GLN   B 1 107 ? 31.361 -27.511 8.181   0.50 23.61 ?  107  GLN   B N    1 
ATOM   5699 N  N    B GLN   B 1 107 ? 31.319 -27.528 8.101   0.50 23.25 ?  107  GLN   B N    1 
ATOM   5700 C  CA   A GLN   B 1 107 ? 30.277 -26.728 7.598   0.50 23.79 ?  107  GLN   B CA   1 
ATOM   5701 C  CA   B GLN   B 1 107 ? 30.247 -26.711 7.543   0.50 23.70 ?  107  GLN   B CA   1 
ATOM   5702 C  C    A GLN   B 1 107 ? 30.759 -25.383 7.071   0.50 21.74 ?  107  GLN   B C    1 
ATOM   5703 C  C    B GLN   B 1 107 ? 30.739 -25.346 7.077   0.50 21.76 ?  107  GLN   B C    1 
ATOM   5704 O  O    A GLN   B 1 107 ? 30.117 -24.814 6.183   0.50 22.36 ?  107  GLN   B O    1 
ATOM   5705 O  O    B GLN   B 1 107 ? 30.082 -24.723 6.239   0.50 22.53 ?  107  GLN   B O    1 
ATOM   5706 C  CB   A GLN   B 1 107 ? 29.175 -26.518 8.641   0.50 26.73 ?  107  GLN   B CB   1 
ATOM   5707 C  CB   B GLN   B 1 107 ? 29.129 -26.547 8.577   0.50 26.70 ?  107  GLN   B CB   1 
ATOM   5708 C  CG   A GLN   B 1 107 ? 27.848 -26.009 8.084   0.50 29.68 ?  107  GLN   B CG   1 
ATOM   5709 C  CG   B GLN   B 1 107 ? 27.793 -26.079 8.007   0.50 29.70 ?  107  GLN   B CG   1 
ATOM   5710 C  CD   A GLN   B 1 107 ? 27.799 -24.497 7.950   0.50 31.90 ?  107  GLN   B CD   1 
ATOM   5711 C  CD   B GLN   B 1 107 ? 27.671 -24.567 7.946   0.50 31.99 ?  107  GLN   B CD   1 
ATOM   5712 O  OE1  A GLN   B 1 107 ? 28.633 -23.783 8.510   0.50 32.69 ?  107  GLN   B OE1  1 
ATOM   5713 O  OE1  B GLN   B 1 107 ? 28.491 -23.841 8.510   0.50 32.81 ?  107  GLN   B OE1  1 
ATOM   5714 N  NE2  A GLN   B 1 107 ? 26.813 -24.000 7.205   0.50 32.67 ?  107  GLN   B NE2  1 
ATOM   5715 N  NE2  B GLN   B 1 107 ? 26.637 -24.084 7.261   0.50 32.79 ?  107  GLN   B NE2  1 
ATOM   5716 H  H    A GLN   B 1 107 ? 31.263 -27.684 9.013   0.50 28.33 ?  107  GLN   B H    1 
ATOM   5717 H  H    B GLN   B 1 107 ? 31.213 -27.733 8.926   0.50 27.90 ?  107  GLN   B H    1 
ATOM   5718 H  HA   A GLN   B 1 107 ? 29.895 -27.222 6.856   0.50 28.54 ?  107  GLN   B HA   1 
ATOM   5719 H  HA   B GLN   B 1 107 ? 29.871 -27.170 6.774   0.50 28.44 ?  107  GLN   B HA   1 
ATOM   5720 H  HB2  A GLN   B 1 107 ? 29.001 -27.364 9.075   0.50 32.07 ?  107  GLN   B HB2  1 
ATOM   5721 H  HB2  B GLN   B 1 107 ? 28.978 -27.401 9.004   0.50 32.04 ?  107  GLN   B HB2  1 
ATOM   5722 H  HB3  A GLN   B 1 107 ? 29.487 -25.873 9.294   0.50 32.07 ?  107  GLN   B HB3  1 
ATOM   5723 H  HB3  B GLN   B 1 107 ? 29.411 -25.897 9.240   0.50 32.04 ?  107  GLN   B HB3  1 
ATOM   5724 H  HG2  A GLN   B 1 107 ? 27.705 -26.388 7.204   0.50 35.61 ?  107  GLN   B HG2  1 
ATOM   5725 H  HG2  B GLN   B 1 107 ? 27.694 -26.421 7.105   0.50 35.64 ?  107  GLN   B HG2  1 
ATOM   5726 H  HG3  A GLN   B 1 107 ? 27.131 -26.283 8.681   0.50 35.61 ?  107  GLN   B HG3  1 
ATOM   5727 H  HG3  B GLN   B 1 107 ? 27.075 -26.418 8.568   0.50 35.64 ?  107  GLN   B HG3  1 
ATOM   5728 H  HE21 A GLN   B 1 107 ? 26.249 -24.530 6.827   0.50 39.21 ?  107  GLN   B HE21 1 
ATOM   5729 H  HE21 B GLN   B 1 107 ? 26.085 -24.622 6.878   0.50 39.34 ?  107  GLN   B HE21 1 
ATOM   5730 H  HE22 A GLN   B 1 107 ? 26.736 -23.150 7.101   0.50 39.21 ?  107  GLN   B HE22 1 
ATOM   5731 H  HE22 B GLN   B 1 107 ? 26.520 -23.234 7.200   0.50 39.34 ?  107  GLN   B HE22 1 
ATOM   5732 N  N    . LEU   B 1 108 ? 31.880 -24.872 7.584   1.00 19.49 ?  108  LEU   B N    1 
ATOM   5733 C  CA   . LEU   B 1 108 ? 32.430 -23.579 7.174   1.00 17.00 ?  108  LEU   B CA   1 
ATOM   5734 C  C    . LEU   B 1 108 ? 33.073 -23.606 5.795   1.00 14.52 ?  108  LEU   B C    1 
ATOM   5735 O  O    . LEU   B 1 108 ? 33.500 -22.551 5.306   1.00 14.14 ?  108  LEU   B O    1 
ATOM   5736 C  CB   . LEU   B 1 108 ? 33.446 -23.098 8.208   1.00 17.61 ?  108  LEU   B CB   1 
ATOM   5737 C  CG   . LEU   B 1 108 ? 32.831 -22.599 9.514   1.00 18.73 ?  108  LEU   B CG   1 
ATOM   5738 C  CD1  . LEU   B 1 108 ? 33.853 -22.595 10.635  1.00 18.95 ?  108  LEU   B CD1  1 
ATOM   5739 C  CD2  . LEU   B 1 108 ? 32.260 -21.205 9.308   1.00 19.59 ?  108  LEU   B CD2  1 
ATOM   5740 H  H    A LEU   B 1 108 ? 32.343 -25.264 8.192   0.50 23.39 ?  108  LEU   B H    1 
ATOM   5741 H  H    B LEU   B 1 108 ? 32.350 -25.282 8.175   0.50 23.39 ?  108  LEU   B H    1 
ATOM   5742 H  HA   . LEU   B 1 108 ? 31.709 -22.937 7.143   1.00 20.40 ?  108  LEU   B HA   1 
ATOM   5743 H  HB2  . LEU   B 1 108 ? 34.038 -23.834 8.426   1.00 21.13 ?  108  LEU   B HB2  1 
ATOM   5744 H  HB3  . LEU   B 1 108 ? 33.954 -22.369 7.825   1.00 21.13 ?  108  LEU   B HB3  1 
ATOM   5745 H  HG   . LEU   B 1 108 ? 32.101 -23.186 9.771   1.00 22.47 ?  108  LEU   B HG   1 
ATOM   5746 H  HD11 . LEU   B 1 108 ? 33.423 -22.295 11.454  1.00 22.74 ?  108  LEU   B HD11 1 
ATOM   5747 H  HD12 . LEU   B 1 108 ? 34.196 -23.493 10.754  1.00 22.74 ?  108  LEU   B HD12 1 
ATOM   5748 H  HD13 . LEU   B 1 108 ? 34.574 -21.991 10.402  1.00 22.74 ?  108  LEU   B HD13 1 
ATOM   5749 H  HD21 . LEU   B 1 108 ? 31.907 -20.880 10.151  1.00 23.50 ?  108  LEU   B HD21 1 
ATOM   5750 H  HD22 . LEU   B 1 108 ? 32.968 -20.619 8.998   1.00 23.50 ?  108  LEU   B HD22 1 
ATOM   5751 H  HD23 . LEU   B 1 108 ? 31.551 -21.247 8.647   1.00 23.50 ?  108  LEU   B HD23 1 
ATOM   5752 N  N    . LEU   B 1 109 ? 33.139 -24.774 5.161   1.00 13.30 ?  109  LEU   B N    1 
ATOM   5753 C  CA   . LEU   B 1 109 ? 33.767 -24.882 3.853   1.00 12.62 ?  109  LEU   B CA   1 
ATOM   5754 C  C    . LEU   B 1 109 ? 33.000 -24.095 2.800   1.00 12.04 ?  109  LEU   B C    1 
ATOM   5755 O  O    . LEU   B 1 109 ? 33.610 -23.503 1.903   1.00 12.03 ?  109  LEU   B O    1 
ATOM   5756 C  CB   . LEU   B 1 109 ? 33.876 -26.356 3.467   1.00 12.51 ?  109  LEU   B CB   1 
ATOM   5757 C  CG   . LEU   B 1 109 ? 34.657 -26.691 2.197   1.00 12.50 ?  109  LEU   B CG   1 
ATOM   5758 C  CD1  . LEU   B 1 109 ? 36.039 -26.041 2.204   1.00 12.66 ?  109  LEU   B CD1  1 
ATOM   5759 C  CD2  . LEU   B 1 109 ? 34.783 -28.203 2.042   1.00 13.22 ?  109  LEU   B CD2  1 
ATOM   5760 H  H    . LEU   B 1 109 ? 32.834 -25.518 5.461   1.00 15.97 ?  109  LEU   B H    1 
ATOM   5761 H  HA   . LEU   B 1 109 ? 34.664 -24.521 3.897   1.00 15.15 ?  109  LEU   B HA   1 
ATOM   5762 H  HB2  . LEU   B 1 109 ? 34.310 -26.829 4.194   1.00 15.01 ?  109  LEU   B HB2  1 
ATOM   5763 H  HB3  . LEU   B 1 109 ? 32.980 -26.709 3.347   1.00 15.01 ?  109  LEU   B HB3  1 
ATOM   5764 H  HG   . LEU   B 1 109 ? 34.170 -26.363 1.423   1.00 15.00 ?  109  LEU   B HG   1 
ATOM   5765 H  HD11 . LEU   B 1 109 ? 36.565 -26.402 1.472   1.00 15.19 ?  109  LEU   B HD11 1 
ATOM   5766 H  HD12 . LEU   B 1 109 ? 35.935 -25.084 2.094   1.00 15.19 ?  109  LEU   B HD12 1 
ATOM   5767 H  HD13 . LEU   B 1 109 ? 36.473 -26.235 3.049   1.00 15.19 ?  109  LEU   B HD13 1 
ATOM   5768 H  HD21 . LEU   B 1 109 ? 35.359 -28.401 1.282   1.00 15.86 ?  109  LEU   B HD21 1 
ATOM   5769 H  HD22 . LEU   B 1 109 ? 35.170 -28.576 2.850   1.00 15.86 ?  109  LEU   B HD22 1 
ATOM   5770 H  HD23 . LEU   B 1 109 ? 33.903 -28.587 1.892   1.00 15.86 ?  109  LEU   B HD23 1 
ATOM   5771 N  N    . LYS   B 1 110 ? 31.667 -24.061 2.887   1.00 11.53 ?  110  LYS   B N    1 
ATOM   5772 C  CA   . LYS   B 1 110 ? 30.905 -23.299 1.903   1.00 11.60 ?  110  LYS   B CA   1 
ATOM   5773 C  C    . LYS   B 1 110 ? 31.242 -21.811 1.991   1.00 11.10 ?  110  LYS   B C    1 
ATOM   5774 O  O    . LYS   B 1 110 ? 31.502 -21.160 0.973   1.00 11.19 ?  110  LYS   B O    1 
ATOM   5775 C  CB   . LYS   B 1 110 ? 29.400 -23.541 2.060   1.00 12.15 ?  110  LYS   B CB   1 
ATOM   5776 C  CG   . LYS   B 1 110 ? 28.598 -22.922 0.920   1.00 12.47 ?  110  LYS   B CG   1 
ATOM   5777 C  CD   . LYS   B 1 110 ? 27.133 -23.350 0.934   1.00 12.64 ?  110  LYS   B CD   1 
ATOM   5778 C  CE   . LYS   B 1 110 ? 26.367 -22.797 -0.269  1.00 13.62 ?  110  LYS   B CE   1 
ATOM   5779 N  NZ   . LYS   B 1 110 ? 26.685 -23.517 -1.535  1.00 14.01 ?  110  LYS   B NZ   1 
ATOM   5780 H  H    . LYS   B 1 110 ? 31.199 -24.467 3.485   1.00 13.84 ?  110  LYS   B H    1 
ATOM   5781 H  HA   . LYS   B 1 110 ? 31.157 -23.603 1.017   1.00 13.93 ?  110  LYS   B HA   1 
ATOM   5782 H  HB2  . LYS   B 1 110 ? 29.232 -24.498 2.065   1.00 14.58 ?  110  LYS   B HB2  1 
ATOM   5783 H  HB3  . LYS   B 1 110 ? 29.100 -23.147 2.893   1.00 14.58 ?  110  LYS   B HB3  1 
ATOM   5784 H  HG2  . LYS   B 1 110 ? 28.623 -21.957 0.998   1.00 14.96 ?  110  LYS   B HG2  1 
ATOM   5785 H  HG3  . LYS   B 1 110 ? 28.978 -23.199 0.073   1.00 14.96 ?  110  LYS   B HG3  1 
ATOM   5786 H  HD2  . LYS   B 1 110 ? 27.079 -24.321 0.906   1.00 15.17 ?  110  LYS   B HD2  1 
ATOM   5787 H  HD3  . LYS   B 1 110 ? 26.707 -23.019 1.743   1.00 15.17 ?  110  LYS   B HD3  1 
ATOM   5788 H  HE2  . LYS   B 1 110 ? 25.415 -22.879 -0.108  1.00 16.34 ?  110  LYS   B HE2  1 
ATOM   5789 H  HE3  . LYS   B 1 110 ? 26.605 -21.863 -0.390  1.00 16.34 ?  110  LYS   B HE3  1 
ATOM   5790 H  HZ1  . LYS   B 1 110 ? 26.223 -23.163 -2.207  1.00 16.81 ?  110  LYS   B HZ1  1 
ATOM   5791 H  HZ2  . LYS   B 1 110 ? 27.554 -23.450 -1.710  1.00 16.81 ?  110  LYS   B HZ2  1 
ATOM   5792 H  HZ3  . LYS   B 1 110 ? 26.469 -24.376 -1.453  1.00 16.81 ?  110  LYS   B HZ3  1 
ATOM   5793 N  N    . SER   B 1 111 ? 31.262 -21.257 3.207   1.00 11.53 ?  111  SER   B N    1 
ATOM   5794 C  CA   . SER   B 1 111 ? 31.659 -19.858 3.383   1.00 11.60 ?  111  SER   B CA   1 
ATOM   5795 C  C    . SER   B 1 111 ? 33.041 -19.600 2.793   1.00 11.00 ?  111  SER   B C    1 
ATOM   5796 O  O    . SER   B 1 111 ? 33.269 -18.569 2.143   1.00 11.17 ?  111  SER   B O    1 
ATOM   5797 C  CB   . SER   B 1 111 ? 31.659 -19.503 4.871   1.00 12.57 ?  111  SER   B CB   1 
ATOM   5798 O  OG   . SER   B 1 111 ? 30.352 -19.500 5.405   1.00 14.47 ?  111  SER   B OG   1 
ATOM   5799 H  H    . SER   B 1 111 ? 31.058 -21.667 3.936   1.00 13.84 ?  111  SER   B H    1 
ATOM   5800 H  HA   . SER   B 1 111 ? 31.026 -19.286 2.933   1.00 13.92 ?  111  SER   B HA   1 
ATOM   5801 H  HB2  . SER   B 1 111 ? 32.183 -20.160 5.356   1.00 15.08 ?  111  SER   B HB2  1 
ATOM   5802 H  HB3  . SER   B 1 111 ? 32.043 -18.623 4.988   1.00 15.08 ?  111  SER   B HB3  1 
ATOM   5803 H  HG   . SER   B 1 111 ? 30.371 -19.297 6.228   1.00 17.36 ?  111  SER   B HG   1 
ATOM   5804 N  N    . ALA   B 1 112 ? 33.980 -20.521 3.017   1.00 11.18 ?  112  ALA   B N    1 
ATOM   5805 C  CA   . ALA   B 1 112 ? 35.323 -20.347 2.470   1.00 10.91 ?  112  ALA   B CA   1 
ATOM   5806 C  C    . ALA   B 1 112 ? 35.287 -20.245 0.947   1.00 10.30 ?  112  ALA   B C    1 
ATOM   5807 O  O    . ALA   B 1 112 ? 35.913 -19.355 0.356   1.00 10.70 ?  112  ALA   B O    1 
ATOM   5808 C  CB   . ALA   B 1 112 ? 36.222 -21.499 2.928   1.00 11.41 ?  112  ALA   B CB   1 
ATOM   5809 H  H    . ALA   B 1 112 ? 33.870 -21.240 3.480   1.00 13.41 ?  112  ALA   B H    1 
ATOM   5810 H  HA   . ALA   B 1 112 ? 35.699 -19.525 2.817   1.00 13.10 ?  112  ALA   B HA   1 
ATOM   5811 H  HB1  . ALA   B 1 112 ? 37.111 -21.367 2.564   1.00 13.69 ?  112  ALA   B HB1  1 
ATOM   5812 H  HB2  . ALA   B 1 112 ? 36.262 -21.500 3.900   1.00 13.69 ?  112  ALA   B HB2  1 
ATOM   5813 H  HB3  . ALA   B 1 112 ? 35.853 -22.336 2.612   1.00 13.69 ?  112  ALA   B HB3  1 
ATOM   5814 N  N    . TYR   B 1 113 ? 34.551 -21.147 0.290   1.00 10.38 ?  113  TYR   B N    1 
ATOM   5815 C  CA   . TYR   B 1 113 ? 34.476 -21.098 -1.166  1.00 9.97  ?  113  TYR   B CA   1 
ATOM   5816 C  C    . TYR   B 1 113 ? 33.769 -19.848 -1.681  1.00 9.58  ?  113  TYR   B C    1 
ATOM   5817 O  O    . TYR   B 1 113 ? 34.037 -19.416 -2.807  1.00 9.77  ?  113  TYR   B O    1 
ATOM   5818 C  CB   . TYR   B 1 113 ? 33.809 -22.357 -1.718  1.00 10.51 ?  113  TYR   B CB   1 
ATOM   5819 C  CG   . TYR   B 1 113 ? 34.766 -23.503 -1.981  1.00 10.71 ?  113  TYR   B CG   1 
ATOM   5820 C  CD1  . TYR   B 1 113 ? 35.749 -23.401 -2.959  1.00 11.06 ?  113  TYR   B CD1  1 
ATOM   5821 C  CD2  . TYR   B 1 113 ? 34.673 -24.691 -1.274  1.00 10.79 ?  113  TYR   B CD2  1 
ATOM   5822 C  CE1  . TYR   B 1 113 ? 36.627 -24.429 -3.211  1.00 11.35 ?  113  TYR   B CE1  1 
ATOM   5823 C  CE2  . TYR   B 1 113 ? 35.543 -25.739 -1.525  1.00 11.04 ?  113  TYR   B CE2  1 
ATOM   5824 C  CZ   . TYR   B 1 113 ? 36.514 -25.604 -2.501  1.00 11.32 ?  113  TYR   B CZ   1 
ATOM   5825 O  OH   . TYR   B 1 113 ? 37.395 -26.623 -2.777  1.00 11.84 ?  113  TYR   B OH   1 
ATOM   5826 H  H    . TYR   B 1 113 ? 34.092 -21.776 0.662   1.00 12.45 ?  113  TYR   B H    1 
ATOM   5827 H  HA   . TYR   B 1 113 ? 35.378 -21.080 -1.505  1.00 11.96 ?  113  TYR   B HA   1 
ATOM   5828 H  HB2  . TYR   B 1 113 ? 33.148 -22.676 -1.080  1.00 12.61 ?  113  TYR   B HB2  1 
ATOM   5829 H  HB3  . TYR   B 1 113 ? 33.373 -22.140 -2.556  1.00 12.61 ?  113  TYR   B HB3  1 
ATOM   5830 H  HD1  . TYR   B 1 113 ? 35.830 -22.606 -3.446  1.00 13.27 ?  113  TYR   B HD1  1 
ATOM   5831 H  HD2  . TYR   B 1 113 ? 34.016 -24.785 -0.627  1.00 12.94 ?  113  TYR   B HD2  1 
ATOM   5832 H  HE1  . TYR   B 1 113 ? 37.282 -24.339 -3.874  1.00 13.62 ?  113  TYR   B HE1  1 
ATOM   5833 H  HE2  . TYR   B 1 113 ? 35.467 -26.531 -1.048  1.00 13.25 ?  113  TYR   B HE2  1 
ATOM   5834 H  HH   . TYR   B 1 113 ? 37.221 -27.290 -2.292  1.00 14.20 ?  113  TYR   B HH   1 
ATOM   5835 N  N    . GLU   B 1 114 ? 32.846 -19.272 -0.902  1.00 10.04 ?  114  GLU   B N    1 
ATOM   5836 C  CA   . GLU   B 1 114 ? 32.158 -18.065 -1.355  1.00 9.74  ?  114  GLU   B CA   1 
ATOM   5837 C  C    . GLU   B 1 114 ? 33.141 -16.941 -1.650  1.00 9.67  ?  114  GLU   B C    1 
ATOM   5838 O  O    . GLU   B 1 114 ? 32.865 -16.082 -2.491  1.00 10.14 ?  114  GLU   B O    1 
ATOM   5839 C  CB   . GLU   B 1 114 ? 31.107 -17.642 -0.330  1.00 10.11 ?  114  GLU   B CB   1 
ATOM   5840 C  CG   . GLU   B 1 114 ? 29.885 -18.554 -0.402  1.00 10.31 ?  114  GLU   B CG   1 
ATOM   5841 C  CD   . GLU   B 1 114 ? 28.873 -18.376 0.713   1.00 10.60 ?  114  GLU   B CD   1 
ATOM   5842 O  OE1  . GLU   B 1 114 ? 29.172 -17.762 1.757   1.00 11.10 ?  114  GLU   B OE1  1 
ATOM   5843 O  OE2  . GLU   B 1 114 ? 27.746 -18.911 0.548   1.00 11.56 -1 114  GLU   B OE2  1 
ATOM   5844 H  H    . GLU   B 1 114 ? 32.596 -19.567 -0.127  1.00 12.05 ?  114  GLU   B H    1 
ATOM   5845 H  HA   . GLU   B 1 114 ? 31.696 -18.269 -2.176  1.00 11.69 ?  114  GLU   B HA   1 
ATOM   5846 H  HB2  . GLU   B 1 114 ? 31.480 -17.704 0.565   1.00 12.13 ?  114  GLU   B HB2  1 
ATOM   5847 H  HB3  . GLU   B 1 114 ? 30.822 -16.737 -0.516  1.00 12.13 ?  114  GLU   B HB3  1 
ATOM   5848 H  HG2  . GLU   B 1 114 ? 29.427 -18.387 -1.237  1.00 12.37 ?  114  GLU   B HG2  1 
ATOM   5849 H  HG3  . GLU   B 1 114 ? 30.189 -19.476 -0.376  1.00 12.37 ?  114  GLU   B HG3  1 
ATOM   5850 N  N    . ASN   B 1 115 ? 34.307 -16.938 -0.999  1.00 9.60  ?  115  ASN   B N    1 
ATOM   5851 C  CA   . ASN   B 1 115 ? 35.300 -15.907 -1.294  1.00 9.68  ?  115  ASN   B CA   1 
ATOM   5852 C  C    . ASN   B 1 115 ? 35.710 -15.922 -2.761  1.00 9.37  ?  115  ASN   B C    1 
ATOM   5853 O  O    . ASN   B 1 115 ? 36.099 -14.881 -3.311  1.00 9.96  ?  115  ASN   B O    1 
ATOM   5854 C  CB   . ASN   B 1 115 ? 36.542 -16.089 -0.415  1.00 10.44 ?  115  ASN   B CB   1 
ATOM   5855 C  CG   . ASN   B 1 115 ? 36.279 -15.820 1.047   1.00 10.78 ?  115  ASN   B CG   1 
ATOM   5856 O  OD1  . ASN   B 1 115 ? 36.280 -14.673 1.483   1.00 12.60 ?  115  ASN   B OD1  1 
ATOM   5857 N  ND2  . ASN   B 1 115 ? 36.114 -16.882 1.829   1.00 10.74 ?  115  ASN   B ND2  1 
ATOM   5858 H  H    . ASN   B 1 115 ? 34.545 -17.504 -0.390  1.00 11.53 ?  115  ASN   B H    1 
ATOM   5859 H  HA   . ASN   B 1 115 ? 34.922 -15.037 -1.098  1.00 11.61 ?  115  ASN   B HA   1 
ATOM   5860 H  HB2  . ASN   B 1 115 ? 36.862 -16.999 -0.504  1.00 12.52 ?  115  ASN   B HB2  1 
ATOM   5861 H  HB3  . ASN   B 1 115 ? 37.230 -15.468 -0.713  1.00 12.52 ?  115  ASN   B HB3  1 
ATOM   5862 H  HD21 . ASN   B 1 115 ? 35.974 -16.775 2.674   1.00 12.89 ?  115  ASN   B HD21 1 
ATOM   5863 H  HD22 . ASN   B 1 115 ? 36.134 -17.671 1.495   1.00 12.89 ?  115  ASN   B HD22 1 
ATOM   5864 N  N    . PHE   B 1 116 ? 35.686 -17.098 -3.399  1.00 9.31  ?  116  PHE   B N    1 
ATOM   5865 C  CA   . PHE   B 1 116 ? 36.116 -17.188 -4.791  1.00 9.56  ?  116  PHE   B CA   1 
ATOM   5866 C  C    . PHE   B 1 116 ? 35.209 -16.360 -5.698  1.00 9.36  ?  116  PHE   B C    1 
ATOM   5867 O  O    . PHE   B 1 116 ? 35.637 -15.932 -6.773  1.00 9.91  ?  116  PHE   B O    1 
ATOM   5868 C  CB   . PHE   B 1 116 ? 36.079 -18.638 -5.317  1.00 9.44  ?  116  PHE   B CB   1 
ATOM   5869 C  CG   . PHE   B 1 116 ? 37.153 -19.593 -4.776  1.00 9.29  ?  116  PHE   B CG   1 
ATOM   5870 C  CD1  . PHE   B 1 116 ? 37.805 -19.414 -3.569  1.00 10.12 ?  116  PHE   B CD1  1 
ATOM   5871 C  CD2  . PHE   B 1 116 ? 37.448 -20.732 -5.512  1.00 9.74  ?  116  PHE   B CD2  1 
ATOM   5872 C  CE1  . PHE   B 1 116 ? 38.739 -20.350 -3.120  1.00 9.88  ?  116  PHE   B CE1  1 
ATOM   5873 C  CE2  . PHE   B 1 116 ? 38.383 -21.663 -5.068  1.00 9.80  ?  116  PHE   B CE2  1 
ATOM   5874 C  CZ   . PHE   B 1 116 ? 39.021 -21.474 -3.871  1.00 9.66  ?  116  PHE   B CZ   1 
ATOM   5875 H  H    . PHE   B 1 116 ? 35.431 -17.849 -3.051  1.00 11.17 ?  116  PHE   B H    1 
ATOM   5876 H  HA   . PHE   B 1 116 ? 37.021 -16.855 -4.875  1.00 11.47 ?  116  PHE   B HA   1 
ATOM   5877 H  HB2  . PHE   B 1 116 ? 35.212 -19.019 -5.092  1.00 11.33 ?  116  PHE   B HB2  1 
ATOM   5878 H  HB3  . PHE   B 1 116 ? 36.173 -18.614 -6.282  1.00 11.33 ?  116  PHE   B HB3  1 
ATOM   5879 H  HD1  . PHE   B 1 116 ? 37.608 -18.664 -3.052  1.00 12.14 ?  116  PHE   B HD1  1 
ATOM   5880 H  HD2  . PHE   B 1 116 ? 37.011 -20.880 -6.321  1.00 11.69 ?  116  PHE   B HD2  1 
ATOM   5881 H  HE1  . PHE   B 1 116 ? 39.174 -20.210 -2.311  1.00 11.86 ?  116  PHE   B HE1  1 
ATOM   5882 H  HE2  . PHE   B 1 116 ? 38.573 -22.416 -5.578  1.00 11.76 ?  116  PHE   B HE2  1 
ATOM   5883 H  HZ   . PHE   B 1 116 ? 39.656 -22.082 -3.572  1.00 11.59 ?  116  PHE   B HZ   1 
ATOM   5884 N  N    . ASN   B 1 117 ? 33.941 -16.161 -5.307  1.00 9.87  ?  117  ASN   B N    1 
ATOM   5885 C  CA   . ASN   B 1 117 ? 32.991 -15.457 -6.167  1.00 9.84  ?  117  ASN   B CA   1 
ATOM   5886 C  C    . ASN   B 1 117 ? 33.304 -13.978 -6.312  1.00 10.34 ?  117  ASN   B C    1 
ATOM   5887 O  O    . ASN   B 1 117 ? 32.703 -13.317 -7.164  1.00 11.35 ?  117  ASN   B O    1 
ATOM   5888 C  CB   . ASN   B 1 117 ? 31.565 -15.676 -5.679  1.00 9.99  ?  117  ASN   B CB   1 
ATOM   5889 C  CG   . ASN   B 1 117 ? 31.115 -17.087 -5.927  1.00 10.35 ?  117  ASN   B CG   1 
ATOM   5890 O  OD1  . ASN   B 1 117 ? 31.467 -17.678 -6.948  1.00 11.00 ?  117  ASN   B OD1  1 
ATOM   5891 N  ND2  . ASN   B 1 117 ? 30.380 -17.654 -4.989  1.00 10.31 ?  117  ASN   B ND2  1 
ATOM   5892 H  H    . ASN   B 1 117 ? 33.619 -16.418 -4.547  1.00 11.84 ?  117  ASN   B H    1 
ATOM   5893 H  HA   . ASN   B 1 117 ? 33.048 -15.847 -7.045  1.00 11.80 ?  117  ASN   B HA   1 
ATOM   5894 H  HB2  . ASN   B 1 117 ? 31.516 -15.504 -4.722  1.00 11.98 ?  117  ASN   B HB2  1 
ATOM   5895 H  HB3  . ASN   B 1 117 ? 30.968 -15.068 -6.152  1.00 11.98 ?  117  ASN   B HB3  1 
ATOM   5896 H  HD21 . ASN   B 1 117 ? 30.102 -18.457 -5.087  1.00 12.37 ?  117  ASN   B HD21 1 
ATOM   5897 H  HD22 . ASN   B 1 117 ? 30.162 -17.203 -4.286  1.00 12.37 ?  117  ASN   B HD22 1 
ATOM   5898 N  N    . GLN   B 1 118 ? 34.242 -13.455 -5.532  1.00 10.13 ?  118  GLN   B N    1 
ATOM   5899 C  CA   . GLN   B 1 118 ? 34.673 -12.068 -5.666  1.00 10.49 ?  118  GLN   B CA   1 
ATOM   5900 C  C    . GLN   B 1 118 ? 35.737 -11.878 -6.740  1.00 10.62 ?  118  GLN   B C    1 
ATOM   5901 O  O    . GLN   B 1 118 ? 36.214 -10.750 -6.922  1.00 12.16 ?  118  GLN   B O    1 
ATOM   5902 C  CB   . GLN   B 1 118 ? 35.148 -11.541 -4.311  1.00 11.25 ?  118  GLN   B CB   1 
ATOM   5903 C  CG   . GLN   B 1 118 ? 34.065 -11.586 -3.247  1.00 11.36 ?  118  GLN   B CG   1 
ATOM   5904 C  CD   . GLN   B 1 118 ? 32.892 -10.677 -3.576  1.00 11.21 ?  118  GLN   B CD   1 
ATOM   5905 O  OE1  . GLN   B 1 118 ? 33.080 -9.538  -4.023  1.00 11.96 ?  118  GLN   B OE1  1 
ATOM   5906 N  NE2  . GLN   B 1 118 ? 31.680 -11.172 -3.370  1.00 11.60 ?  118  GLN   B NE2  1 
ATOM   5907 H  H    . GLN   B 1 118 ? 34.660 -13.886 -4.909  1.00 12.15 ?  118  GLN   B H    1 
ATOM   5908 H  HA   . GLN   B 1 118 ? 33.904 -11.540 -5.929  1.00 12.58 ?  118  GLN   B HA   1 
ATOM   5909 H  HB2  . GLN   B 1 118 ? 35.894 -12.070 -4.002  1.00 13.50 ?  118  GLN   B HB2  1 
ATOM   5910 H  HB3  . GLN   B 1 118 ? 35.419 -10.610 -4.411  1.00 13.50 ?  118  GLN   B HB3  1 
ATOM   5911 H  HG2  . GLN   B 1 118 ? 33.732 -12.496 -3.173  1.00 13.64 ?  118  GLN   B HG2  1 
ATOM   5912 H  HG3  . GLN   B 1 118 ? 34.442 -11.303 -2.397  1.00 13.64 ?  118  GLN   B HG3  1 
ATOM   5913 H  HE21 . GLN   B 1 118 ? 31.588 -11.971 -3.059  1.00 13.93 ?  118  GLN   B HE21 1 
ATOM   5914 H  HE22 . GLN   B 1 118 ? 30.990 -10.695 -3.543  1.00 13.93 ?  118  GLN   B HE22 1 
ATOM   5915 N  N    . HIS   B 1 119 ? 36.092 -12.934 -7.474  1.00 10.25 ?  119  HIS   B N    1 
ATOM   5916 C  CA   . HIS   B 1 119 ? 37.128 -12.884 -8.497  1.00 10.48 ?  119  HIS   B CA   1 
ATOM   5917 C  C    . HIS   B 1 119 ? 36.650 -13.611 -9.738  1.00 10.39 ?  119  HIS   B C    1 
ATOM   5918 O  O    . HIS   B 1 119 ? 36.144 -14.729 -9.641  1.00 11.22 ?  119  HIS   B O    1 
ATOM   5919 C  CB   . HIS   B 1 119 ? 38.413 -13.513 -7.959  1.00 11.09 ?  119  HIS   B CB   1 
ATOM   5920 C  CG   . HIS   B 1 119 ? 38.892 -12.826 -6.727  1.00 12.41 ?  119  HIS   B CG   1 
ATOM   5921 N  ND1  . HIS   B 1 119 ? 39.689 -11.703 -6.770  1.00 14.10 ?  119  HIS   B ND1  1 
ATOM   5922 C  CD2  . HIS   B 1 119 ? 38.591 -13.030 -5.424  1.00 13.36 ?  119  HIS   B CD2  1 
ATOM   5923 C  CE1  . HIS   B 1 119 ? 39.889 -11.270 -5.538  1.00 14.95 ?  119  HIS   B CE1  1 
ATOM   5924 N  NE2  . HIS   B 1 119 ? 39.231 -12.054 -4.704  1.00 15.04 ?  119  HIS   B NE2  1 
ATOM   5925 H  H    . HIS   B 1 119 ? 35.728 -13.711 -7.398  1.00 12.30 ?  119  HIS   B H    1 
ATOM   5926 H  HA   . HIS   B 1 119 ? 37.311 -11.956 -8.728  1.00 12.58 ?  119  HIS   B HA   1 
ATOM   5927 H  HB2  . HIS   B 1 119 ? 38.249 -14.440 -7.745  1.00 13.31 ?  119  HIS   B HB2  1 
ATOM   5928 H  HB3  . HIS   B 1 119 ? 39.109 -13.439 -8.634  1.00 13.31 ?  119  HIS   B HB3  1 
ATOM   5929 H  HD2  . HIS   B 1 119 ? 38.053 -13.710 -5.080  1.00 16.03 ?  119  HIS   B HD2  1 
ATOM   5930 H  HE1  . HIS   B 1 119 ? 40.426 -10.548 -5.289  1.00 17.94 ?  119  HIS   B HE1  1 
ATOM   5931 H  HE2  . HIS   B 1 119 ? 39.229 -11.985 -3.841  1.00 18.05 ?  119  HIS   B HE2  1 
ATOM   5932 N  N    . GLU   B 1 120 ? 36.805 -12.986 -10.905 1.00 10.76 ?  120  GLU   B N    1 
ATOM   5933 C  CA   . GLU   B 1 120 ? 36.215 -13.558 -12.111 1.00 12.16 ?  120  GLU   B CA   1 
ATOM   5934 C  C    . GLU   B 1 120 ? 36.879 -14.865 -12.525 1.00 11.17 ?  120  GLU   B C    1 
ATOM   5935 O  O    . GLU   B 1 120 ? 36.216 -15.736 -13.102 1.00 11.54 ?  120  GLU   B O    1 
ATOM   5936 C  CB   . GLU   B 1 120 ? 36.253 -12.542 -13.249 1.00 16.25 ?  120  GLU   B CB   1 
ATOM   5937 C  CG   . GLU   B 1 120 ? 35.294 -11.388 -13.030 1.00 22.01 ?  120  GLU   B CG   1 
ATOM   5938 C  CD   . GLU   B 1 120 ? 35.076 -10.555 -14.272 1.00 27.11 ?  120  GLU   B CD   1 
ATOM   5939 O  OE1  . GLU   B 1 120 ? 36.059 -10.311 -15.005 1.00 29.03 ?  120  GLU   B OE1  1 
ATOM   5940 O  OE2  . GLU   B 1 120 ? 33.920 -10.147 -14.511 1.00 29.74 -1 120  GLU   B OE2  1 
ATOM   5941 H  H    . GLU   B 1 120 ? 37.241 -12.247 -11.027 1.00 12.91 ?  120  GLU   B H    1 
ATOM   5942 H  HA   . GLU   B 1 120 ? 35.290 -13.753 -11.931 1.00 14.59 ?  120  GLU   B HA   1 
ATOM   5943 H  HB2  . GLU   B 1 120 ? 37.147 -12.174 -13.327 1.00 19.50 ?  120  GLU   B HB2  1 
ATOM   5944 H  HB3  . GLU   B 1 120 ? 36.003 -12.982 -14.078 1.00 19.50 ?  120  GLU   B HB3  1 
ATOM   5945 H  HG2  . GLU   B 1 120 ? 34.431 -11.740 -12.760 1.00 26.41 ?  120  GLU   B HG2  1 
ATOM   5946 H  HG3  . GLU   B 1 120 ? 35.647 -10.809 -12.338 1.00 26.41 ?  120  GLU   B HG3  1 
ATOM   5947 N  N    . VAL   B 1 121 ? 38.177 -15.011 -12.262 1.00 10.88 ?  121  VAL   B N    1 
ATOM   5948 C  CA   . VAL   B 1 121 ? 38.927 -16.215 -12.618 1.00 10.77 ?  121  VAL   B CA   1 
ATOM   5949 C  C    . VAL   B 1 121 ? 40.040 -16.423 -11.599 1.00 10.48 ?  121  VAL   B C    1 
ATOM   5950 O  O    . VAL   B 1 121 ? 40.722 -15.473 -11.203 1.00 11.08 ?  121  VAL   B O    1 
ATOM   5951 C  CB   . VAL   B 1 121 ? 39.436 -16.163 -14.078 1.00 12.63 ?  121  VAL   B CB   1 
ATOM   5952 C  CG1  . VAL   B 1 121 ? 40.303 -14.929 -14.331 1.00 13.77 ?  121  VAL   B CG1  1 
ATOM   5953 C  CG2  . VAL   B 1 121 ? 40.165 -17.448 -14.443 1.00 13.74 ?  121  VAL   B CG2  1 
ATOM   5954 H  H    . VAL   B 1 121 ? 38.661 -14.414 -11.872 1.00 13.05 ?  121  VAL   B H    1 
ATOM   5955 H  HA   . VAL   B 1 121 ? 38.322 -16.971 -12.553 1.00 12.93 ?  121  VAL   B HA   1 
ATOM   5956 H  HB   . VAL   B 1 121 ? 38.663 -16.097 -14.665 1.00 15.16 ?  121  VAL   B HB   1 
ATOM   5957 H  HG11 . VAL   B 1 121 ? 40.605 -14.939 -15.254 1.00 16.52 ?  121  VAL   B HG11 1 
ATOM   5958 H  HG12 . VAL   B 1 121 ? 39.774 -14.130 -14.169 1.00 16.52 ?  121  VAL   B HG12 1 
ATOM   5959 H  HG13 . VAL   B 1 121 ? 41.064 -14.948 -13.734 1.00 16.52 ?  121  VAL   B HG13 1 
ATOM   5960 H  HG21 . VAL   B 1 121 ? 40.366 -17.436 -15.393 1.00 16.49 ?  121  VAL   B HG21 1 
ATOM   5961 H  HG22 . VAL   B 1 121 ? 40.988 -17.501 -13.933 1.00 16.49 ?  121  VAL   B HG22 1 
ATOM   5962 H  HG23 . VAL   B 1 121 ? 39.596 -18.205 -14.236 1.00 16.49 ?  121  VAL   B HG23 1 
ATOM   5963 N  N    . LEU   B 1 122 ? 40.223 -17.676 -11.171 1.00 9.91  ?  122  LEU   B N    1 
ATOM   5964 C  CA   . LEU   B 1 122 ? 41.206 -18.030 -10.152 1.00 9.79  ?  122  LEU   B CA   1 
ATOM   5965 C  C    . LEU   B 1 122 ? 41.860 -19.361 -10.482 1.00 9.70  ?  122  LEU   B C    1 
ATOM   5966 O  O    . LEU   B 1 122 ? 41.198 -20.279 -10.984 1.00 10.57 ?  122  LEU   B O    1 
ATOM   5967 C  CB   . LEU   B 1 122 ? 40.556 -18.264 -8.775  1.00 11.51 ?  122  LEU   B CB   1 
ATOM   5968 C  CG   . LEU   B 1 122 ? 39.526 -17.242 -8.283  1.00 11.39 ?  122  LEU   B CG   1 
ATOM   5969 C  CD1  . LEU   B 1 122 ? 38.126 -17.604 -8.749  1.00 12.34 ?  122  LEU   B CD1  1 
ATOM   5970 C  CD2  . LEU   B 1 122 ? 39.580 -17.135 -6.774  1.00 10.83 ?  122  LEU   B CD2  1 
ATOM   5971 H  H    . LEU   B 1 122 ? 39.786 -18.355 -11.471 1.00 11.90 ?  122  LEU   B H    1 
ATOM   5972 H  HA   . LEU   B 1 122 ? 41.885 -17.338 -10.076 1.00 11.75 ?  122  LEU   B HA   1 
ATOM   5973 H  HB2  . LEU   B 1 122 ? 40.113 -19.121 -8.798  1.00 13.81 ?  122  LEU   B HB2  1 
ATOM   5974 H  HB3  . LEU   B 1 122 ? 41.264 -18.285 -8.113  1.00 13.81 ?  122  LEU   B HB3  1 
ATOM   5975 H  HG   . LEU   B 1 122 ? 39.743 -16.371 -8.648  1.00 13.66 ?  122  LEU   B HG   1 
ATOM   5976 H  HD11 . LEU   B 1 122 ? 37.495 -16.959 -8.394  1.00 14.80 ?  122  LEU   B HD11 1 
ATOM   5977 H  HD12 . LEU   B 1 122 ? 38.100 -17.588 -9.720  1.00 14.80 ?  122  LEU   B HD12 1 
ATOM   5978 H  HD13 . LEU   B 1 122 ? 37.904 -18.493 -8.430  1.00 14.80 ?  122  LEU   B HD13 1 
ATOM   5979 H  HD21 . LEU   B 1 122 ? 38.899 -16.513 -6.472  1.00 12.99 ?  122  LEU   B HD21 1 
ATOM   5980 H  HD22 . LEU   B 1 122 ? 39.424 -18.010 -6.385  1.00 12.99 ?  122  LEU   B HD22 1 
ATOM   5981 H  HD23 . LEU   B 1 122 ? 40.459 -16.811 -6.510  1.00 12.99 ?  122  LEU   B HD23 1 
ATOM   5982 N  N    . LEU   B 1 123 ? 43.149 -19.467 -10.131 1.00 9.40  ?  123  LEU   B N    1 
ATOM   5983 C  CA   . LEU   B 1 123 ? 43.862 -20.736 -10.012 1.00 9.64  ?  123  LEU   B CA   1 
ATOM   5984 C  C    . LEU   B 1 123 ? 43.835 -21.137 -8.542  1.00 9.25  ?  123  LEU   B C    1 
ATOM   5985 O  O    . LEU   B 1 123 ? 44.188 -20.317 -7.687  1.00 9.98  ?  123  LEU   B O    1 
ATOM   5986 C  CB   . LEU   B 1 123 ? 45.311 -20.557 -10.475 1.00 9.94  ?  123  LEU   B CB   1 
ATOM   5987 C  CG   . LEU   B 1 123 ? 46.251 -21.745 -10.245 1.00 10.49 ?  123  LEU   B CG   1 
ATOM   5988 C  CD1  . LEU   B 1 123 ? 45.817 -22.980 -11.033 1.00 11.29 ?  123  LEU   B CD1  1 
ATOM   5989 C  CD2  . LEU   B 1 123 ? 47.670 -21.353 -10.607 1.00 11.39 ?  123  LEU   B CD2  1 
ATOM   5990 H  H    . LEU   B 1 123 ? 43.648 -18.785 -9.941  1.00 11.29 ?  123  LEU   B H    1 
ATOM   5991 H  HA   . LEU   B 1 123 ? 43.425 -21.420 -10.544 1.00 11.56 ?  123  LEU   B HA   1 
ATOM   5992 H  HB2  . LEU   B 1 123 ? 45.299 -20.379 -11.429 1.00 11.93 ?  123  LEU   B HB2  1 
ATOM   5993 H  HB3  . LEU   B 1 123 ? 45.686 -19.799 -10.008 1.00 11.93 ?  123  LEU   B HB3  1 
ATOM   5994 H  HG   . LEU   B 1 123 ? 46.245 -21.980 -9.307  1.00 12.58 ?  123  LEU   B HG   1 
ATOM   5995 H  HD11 . LEU   B 1 123 ? 46.451 -23.694 -10.874 1.00 13.55 ?  123  LEU   B HD11 1 
ATOM   5996 H  HD12 . LEU   B 1 123 ? 44.933 -23.246 -10.733 1.00 13.55 ?  123  LEU   B HD12 1 
ATOM   5997 H  HD13 . LEU   B 1 123 ? 45.793 -22.759 -11.977 1.00 13.55 ?  123  LEU   B HD13 1 
ATOM   5998 H  HD21 . LEU   B 1 123 ? 48.257 -22.111 -10.460 1.00 13.67 ?  123  LEU   B HD21 1 
ATOM   5999 H  HD22 . LEU   B 1 123 ? 47.699 -21.089 -11.541 1.00 13.67 ?  123  LEU   B HD22 1 
ATOM   6000 H  HD23 . LEU   B 1 123 ? 47.945 -20.609 -10.047 1.00 13.67 ?  123  LEU   B HD23 1 
ATOM   6001 N  N    . ALA   B 1 124 ? 43.400 -22.367 -8.235  1.00 9.18  ?  124  ALA   B N    1 
ATOM   6002 C  CA   . ALA   B 1 124 ? 43.143 -22.685 -6.838  1.00 9.23  ?  124  ALA   B CA   1 
ATOM   6003 C  C    . ALA   B 1 124 ? 43.424 -24.145 -6.519  1.00 9.11  ?  124  ALA   B C    1 
ATOM   6004 O  O    . ALA   B 1 124 ? 43.292 -25.020 -7.386  1.00 9.79  ?  124  ALA   B O    1 
ATOM   6005 C  CB   . ALA   B 1 124 ? 41.691 -22.380 -6.460  1.00 9.90  ?  124  ALA   B CB   1 
ATOM   6006 H  H    . ALA   B 1 124 ? 43.243 -23.009 -8.796  1.00 11.01 ?  124  ALA   B H    1 
ATOM   6007 H  HA   . ALA   B 1 124 ? 43.717 -22.133 -6.293  1.00 11.07 ?  124  ALA   B HA   1 
ATOM   6008 H  HB1  . ALA   B 1 124 ? 41.549 -22.600 -5.526  1.00 11.88 ?  124  ALA   B HB1  1 
ATOM   6009 H  HB2  . ALA   B 1 124 ? 41.519 -21.434 -6.604  1.00 11.88 ?  124  ALA   B HB2  1 
ATOM   6010 H  HB3  . ALA   B 1 124 ? 41.096 -22.908 -7.018  1.00 11.88 ?  124  ALA   B HB3  1 
ATOM   6011 N  N    . PRO   B 1 125 ? 43.720 -24.442 -5.257  1.00 9.38  ?  125  PRO   B N    1 
ATOM   6012 C  CA   . PRO   B 1 125 ? 43.657 -25.810 -4.738  1.00 10.32 ?  125  PRO   B CA   1 
ATOM   6013 C  C    . PRO   B 1 125 ? 42.260 -26.088 -4.187  1.00 10.28 ?  125  PRO   B C    1 
ATOM   6014 O  O    . PRO   B 1 125 ? 41.464 -25.176 -3.971  1.00 10.85 ?  125  PRO   B O    1 
ATOM   6015 C  CB   . PRO   B 1 125 ? 44.651 -25.735 -3.572  1.00 11.48 ?  125  PRO   B CB   1 
ATOM   6016 C  CG   . PRO   B 1 125 ? 44.401 -24.345 -2.993  1.00 11.37 ?  125  PRO   B CG   1 
ATOM   6017 C  CD   . PRO   B 1 125 ? 44.042 -23.475 -4.190  1.00 9.94  ?  125  PRO   B CD   1 
ATOM   6018 H  HA   . PRO   B 1 125 ? 43.930 -26.476 -5.388  1.00 12.39 ?  125  PRO   B HA   1 
ATOM   6019 H  HB2  . PRO   B 1 125 ? 44.455 -26.422 -2.912  1.00 13.78 ?  125  PRO   B HB2  1 
ATOM   6020 H  HB3  . PRO   B 1 125 ? 45.562 -25.817 -3.897  1.00 13.78 ?  125  PRO   B HB3  1 
ATOM   6021 H  HG2  . PRO   B 1 125 ? 43.666 -24.371 -2.361  1.00 13.65 ?  125  PRO   B HG2  1 
ATOM   6022 H  HG3  . PRO   B 1 125 ? 45.209 -24.012 -2.559  1.00 13.65 ?  125  PRO   B HG3  1 
ATOM   6023 H  HD2  . PRO   B 1 125 ? 43.274 -22.919 -3.991  1.00 11.93 ?  125  PRO   B HD2  1 
ATOM   6024 H  HD3  . PRO   B 1 125 ? 44.809 -22.929 -4.452  1.00 11.93 ?  125  PRO   B HD3  1 
ATOM   6025 N  N    . LEU   B 1 126 ? 41.990 -27.368 -3.918  1.00 10.85 ?  126  LEU   B N    1 
ATOM   6026 C  CA   . LEU   B 1 126 ? 40.771 -27.736 -3.202  1.00 11.46 ?  126  LEU   B CA   1 
ATOM   6027 C  C    . LEU   B 1 126 ? 40.887 -27.332 -1.739  1.00 11.50 ?  126  LEU   B C    1 
ATOM   6028 O  O    . LEU   B 1 126 ? 41.772 -27.799 -1.016  1.00 13.21 ?  126  LEU   B O    1 
ATOM   6029 C  CB   . LEU   B 1 126 ? 40.507 -29.231 -3.312  1.00 12.74 ?  126  LEU   B CB   1 
ATOM   6030 C  CG   . LEU   B 1 126 ? 39.984 -29.711 -4.667  1.00 13.64 ?  126  LEU   B CG   1 
ATOM   6031 C  CD1  . LEU   B 1 126 ? 40.027 -31.222 -4.753  1.00 15.19 ?  126  LEU   B CD1  1 
ATOM   6032 C  CD2  . LEU   B 1 126 ? 38.563 -29.202 -4.927  1.00 13.70 ?  126  LEU   B CD2  1 
ATOM   6033 H  H    . LEU   B 1 126 ? 42.491 -28.036 -4.128  1.00 13.02 ?  126  LEU   B H    1 
ATOM   6034 H  HA   . LEU   B 1 126 ? 40.018 -27.259 -3.595  1.00 13.75 ?  126  LEU   B HA   1 
ATOM   6035 H  HB2  . LEU   B 1 126 ? 41.333 -29.698 -3.136  1.00 15.28 ?  126  LEU   B HB2  1 
ATOM   6036 H  HB3  . LEU   B 1 126 ? 39.844 -29.471 -2.647  1.00 15.28 ?  126  LEU   B HB3  1 
ATOM   6037 H  HG   . LEU   B 1 126 ? 40.559 -29.358 -5.368  1.00 16.37 ?  126  LEU   B HG   1 
ATOM   6038 H  HD11 . LEU   B 1 126 ? 39.690 -31.500 -5.620  1.00 18.23 ?  126  LEU   B HD11 1 
ATOM   6039 H  HD12 . LEU   B 1 126 ? 40.940 -31.522 -4.639  1.00 18.23 ?  126  LEU   B HD12 1 
ATOM   6040 H  HD13 . LEU   B 1 126 ? 39.466 -31.592 -4.049  1.00 18.23 ?  126  LEU   B HD13 1 
ATOM   6041 H  HD21 . LEU   B 1 126 ? 38.222 -29.616 -5.736  1.00 16.44 ?  126  LEU   B HD21 1 
ATOM   6042 H  HD22 . LEU   B 1 126 ? 38.001 -29.435 -4.174  1.00 16.44 ?  126  LEU   B HD22 1 
ATOM   6043 H  HD23 . LEU   B 1 126 ? 38.586 -28.237 -5.037  1.00 16.44 ?  126  LEU   B HD23 1 
ATOM   6044 N  N    . LEU   B 1 127 ? 39.958 -26.500 -1.287  1.00 11.19 ?  127  LEU   B N    1 
ATOM   6045 C  CA   . LEU   B 1 127 ? 40.014 -26.009 0.078   1.00 11.43 ?  127  LEU   B CA   1 
ATOM   6046 C  C    . LEU   B 1 127 ? 39.743 -27.131 1.073   1.00 11.24 ?  127  LEU   B C    1 
ATOM   6047 O  O    . LEU   B 1 127 ? 38.920 -28.023 0.849   1.00 11.51 ?  127  LEU   B O    1 
ATOM   6048 C  CB   . LEU   B 1 127 ? 38.996 -24.886 0.289   1.00 11.94 ?  127  LEU   B CB   1 
ATOM   6049 C  CG   . LEU   B 1 127 ? 39.173 -23.617 -0.541  1.00 12.85 ?  127  LEU   B CG   1 
ATOM   6050 C  CD1  . LEU   B 1 127 ? 38.046 -22.652 -0.217  1.00 12.69 ?  127  LEU   B CD1  1 
ATOM   6051 C  CD2  . LEU   B 1 127 ? 40.530 -22.971 -0.284  1.00 13.24 ?  127  LEU   B CD2  1 
ATOM   6052 H  H    . LEU   B 1 127 ? 39.281 -26.202 -1.747  1.00 13.43 ?  127  LEU   B H    1 
ATOM   6053 H  HA   . LEU   B 1 127 ? 40.898 -25.650 0.247   1.00 13.72 ?  127  LEU   B HA   1 
ATOM   6054 H  HB2  . LEU   B 1 127 ? 38.112 -25.233 0.087   1.00 14.33 ?  127  LEU   B HB2  1 
ATOM   6055 H  HB3  . LEU   B 1 127 ? 39.026 -24.619 1.221   1.00 14.33 ?  127  LEU   B HB3  1 
ATOM   6056 H  HG   . LEU   B 1 127 ? 39.111 -23.834 -1.482  1.00 15.42 ?  127  LEU   B HG   1 
ATOM   6057 H  HD11 . LEU   B 1 127 ? 38.161 -21.840 -0.739  1.00 15.23 ?  127  LEU   B HD11 1 
ATOM   6058 H  HD12 . LEU   B 1 127 ? 37.198 -23.066 -0.436  1.00 15.23 ?  127  LEU   B HD12 1 
ATOM   6059 H  HD13 . LEU   B 1 127 ? 38.075 -22.437 0.730   1.00 15.23 ?  127  LEU   B HD13 1 
ATOM   6060 H  HD21 . LEU   B 1 127 ? 40.569 -22.115 -0.742  1.00 15.89 ?  127  LEU   B HD21 1 
ATOM   6061 H  HD22 . LEU   B 1 127 ? 40.642 -22.837 0.672   1.00 15.89 ?  127  LEU   B HD22 1 
ATOM   6062 H  HD23 . LEU   B 1 127 ? 41.225 -23.557 -0.619  1.00 15.89 ?  127  LEU   B HD23 1 
ATOM   6063 N  N    . SER   B 1 128 ? 40.424 -27.043 2.205   1.00 11.23 ?  128  SER   B N    1 
ATOM   6064 C  CA   . SER   B 1 128 ? 40.321 -27.958 3.332   1.00 11.71 ?  128  SER   B CA   1 
ATOM   6065 C  C    . SER   B 1 128 ? 40.815 -29.367 3.012   1.00 12.99 ?  128  SER   B C    1 
ATOM   6066 O  O    . SER   B 1 128 ? 40.724 -30.248 3.873   1.00 14.27 ?  128  SER   B O    1 
ATOM   6067 C  CB   . SER   B 1 128 ? 38.923 -27.969 3.964   1.00 11.98 ?  128  SER   B CB   1 
ATOM   6068 O  OG   . SER   B 1 128 ? 38.611 -26.697 4.522   1.00 12.81 ?  128  SER   B OG   1 
ATOM   6069 H  H    . SER   B 1 128 ? 40.984 -26.406 2.354   1.00 13.48 ?  128  SER   B H    1 
ATOM   6070 H  HA   . SER   B 1 128 ? 40.911 -27.616 4.014   1.00 14.05 ?  128  SER   B HA   1 
ATOM   6071 H  HB2  . SER   B 1 128 ? 38.261 -28.196 3.290   1.00 14.38 ?  128  SER   B HB2  1 
ATOM   6072 H  HB3  . SER   B 1 128 ? 38.903 -28.645 4.674   1.00 14.38 ?  128  SER   B HB3  1 
ATOM   6073 H  HG   . SER   B 1 128 ? 39.179 -26.507 5.111   1.00 15.38 ?  128  SER   B HG   1 
ATOM   6074 N  N    . ALA   B 1 129 ? 41.375 -29.597 1.821   1.00 13.96 ?  129  ALA   B N    1 
ATOM   6075 C  CA   . ALA   B 1 129 ? 41.915 -30.898 1.463   1.00 14.81 ?  129  ALA   B CA   1 
ATOM   6076 C  C    . ALA   B 1 129 ? 43.308 -31.074 2.055   1.00 13.95 ?  129  ALA   B C    1 
ATOM   6077 O  O    . ALA   B 1 129 ? 43.867 -30.178 2.698   1.00 13.53 ?  129  ALA   B O    1 
ATOM   6078 C  CB   . ALA   B 1 129 ? 41.956 -31.059 -0.055  1.00 16.51 ?  129  ALA   B CB   1 
ATOM   6079 H  H    . ALA   B 1 129 ? 41.441 -29.009 1.194   1.00 16.75 ?  129  ALA   B H    1 
ATOM   6080 H  HA   . ALA   B 1 129 ? 41.340 -31.589 1.822   1.00 17.77 ?  129  ALA   B HA   1 
ATOM   6081 H  HB1  . ALA   B 1 129 ? 42.311 -31.938 -0.267  1.00 19.81 ?  129  ALA   B HB1  1 
ATOM   6082 H  HB2  . ALA   B 1 129 ? 41.056 -30.974 -0.407  1.00 19.81 ?  129  ALA   B HB2  1 
ATOM   6083 H  HB3  . ALA   B 1 129 ? 42.527 -30.373 -0.431  1.00 19.81 ?  129  ALA   B HB3  1 
ATOM   6084 N  N    . GLY   B 1 130 ? 43.871 -32.258 1.827   1.00 13.70 ?  130  GLY   B N    1 
ATOM   6085 C  CA   . GLY   B 1 130 ? 45.258 -32.492 2.176   1.00 14.42 ?  130  GLY   B CA   1 
ATOM   6086 C  C    . GLY   B 1 130 ? 45.476 -32.398 3.667   1.00 14.34 ?  130  GLY   B C    1 
ATOM   6087 O  O    . GLY   B 1 130 ? 44.782 -33.045 4.467   1.00 14.99 ?  130  GLY   B O    1 
ATOM   6088 H  H    . GLY   B 1 130 ? 43.474 -32.930 1.464   1.00 16.43 ?  130  GLY   B H    1 
ATOM   6089 H  HA2  . GLY   B 1 130 ? 45.523 -33.378 1.877   1.00 17.30 ?  130  GLY   B HA2  1 
ATOM   6090 H  HA3  . GLY   B 1 130 ? 45.822 -31.838 1.736   1.00 17.30 ?  130  GLY   B HA3  1 
ATOM   6091 N  N    . ILE   B 1 131 ? 46.449 -31.566 4.052   1.00 14.65 ?  131  ILE   B N    1 
ATOM   6092 C  CA   . ILE   B 1 131 ? 46.809 -31.439 5.455   1.00 15.48 ?  131  ILE   B CA   1 
ATOM   6093 C  C    . ILE   B 1 131 ? 45.694 -30.839 6.294   1.00 15.08 ?  131  ILE   B C    1 
ATOM   6094 O  O    . ILE   B 1 131 ? 45.774 -30.909 7.524   1.00 16.16 ?  131  ILE   B O    1 
ATOM   6095 C  CB   . ILE   B 1 131 ? 48.134 -30.669 5.656   1.00 17.51 ?  131  ILE   B CB   1 
ATOM   6096 C  CG1  . ILE   B 1 131 ? 47.976 -29.190 5.274   1.00 18.22 ?  131  ILE   B CG1  1 
ATOM   6097 C  CG2  . ILE   B 1 131 ? 49.254 -31.316 4.849   1.00 18.57 ?  131  ILE   B CG2  1 
ATOM   6098 C  CD1  . ILE   B 1 131 ? 49.206 -28.348 5.571   1.00 19.07 ?  131  ILE   B CD1  1 
ATOM   6099 H  H    . ILE   B 1 131 ? 46.910 -31.071 3.518   1.00 17.57 ?  131  ILE   B H    1 
ATOM   6100 H  HA   . ILE   B 1 131 ? 46.953 -32.333 5.797   1.00 18.58 ?  131  ILE   B HA   1 
ATOM   6101 H  HB   . ILE   B 1 131 ? 48.364 -30.716 6.597   1.00 21.01 ?  131  ILE   B HB   1 
ATOM   6102 H  HG12 . ILE   B 1 131 ? 47.791 -29.132 4.323   1.00 21.86 ?  131  ILE   B HG12 1 
ATOM   6103 H  HG13 . ILE   B 1 131 ? 47.232 -28.808 5.773   1.00 21.86 ?  131  ILE   B HG13 1 
ATOM   6104 H  HG21 . ILE   B 1 131 ? 50.099 -30.928 5.122   1.00 22.29 ?  131  ILE   B HG21 1 
ATOM   6105 H  HG22 . ILE   B 1 131 ? 49.253 -32.268 5.021   1.00 22.29 ?  131  ILE   B HG22 1 
ATOM   6106 H  HG23 . ILE   B 1 131 ? 49.097 -31.147 3.907   1.00 22.29 ?  131  ILE   B HG23 1 
ATOM   6107 H  HD11 . ILE   B 1 131 ? 48.994 -27.416 5.411   1.00 22.89 ?  131  ILE   B HD11 1 
ATOM   6108 H  HD12 . ILE   B 1 131 ? 49.457 -28.476 6.499   1.00 22.89 ?  131  ILE   B HD12 1 
ATOM   6109 H  HD13 . ILE   B 1 131 ? 49.927 -28.630 4.989   1.00 22.89 ?  131  ILE   B HD13 1 
ATOM   6110 N  N    . PHE   B 1 132 ? 44.662 -30.257 5.670   1.00 13.86 ?  132  PHE   B N    1 
ATOM   6111 C  CA   . PHE   B 1 132 ? 43.507 -29.752 6.406   1.00 13.92 ?  132  PHE   B CA   1 
ATOM   6112 C  C    . PHE   B 1 132 ? 42.480 -30.839 6.725   1.00 15.16 ?  132  PHE   B C    1 
ATOM   6113 O  O    . PHE   B 1 132 ? 41.568 -30.587 7.518   1.00 17.03 ?  132  PHE   B O    1 
ATOM   6114 C  CB   . PHE   B 1 132 ? 42.833 -28.610 5.636   1.00 13.07 ?  132  PHE   B CB   1 
ATOM   6115 C  CG   . PHE   B 1 132 ? 43.539 -27.273 5.748   1.00 12.90 ?  132  PHE   B CG   1 
ATOM   6116 C  CD1  . PHE   B 1 132 ? 44.838 -27.093 5.281   1.00 13.92 ?  132  PHE   B CD1  1 
ATOM   6117 C  CD2  . PHE   B 1 132 ? 42.867 -26.174 6.264   1.00 12.59 ?  132  PHE   B CD2  1 
ATOM   6118 C  CE1  . PHE   B 1 132 ? 45.459 -25.853 5.372   1.00 14.50 ?  132  PHE   B CE1  1 
ATOM   6119 C  CE2  . PHE   B 1 132 ? 43.478 -24.936 6.354   1.00 13.02 ?  132  PHE   B CE2  1 
ATOM   6120 C  CZ   . PHE   B 1 132 ? 44.771 -24.775 5.906   1.00 14.13 ?  132  PHE   B CZ   1 
ATOM   6121 H  H    . PHE   B 1 132 ? 44.606 -30.147 4.815   1.00 16.63 ?  132  PHE   B H    1 
ATOM   6122 H  HA   . PHE   B 1 132 ? 43.819 -29.389 7.247   1.00 16.70 ?  132  PHE   B HA   1 
ATOM   6123 H  HB2  . PHE   B 1 132 ? 42.809 -28.843 4.697   1.00 15.68 ?  132  PHE   B HB2  1 
ATOM   6124 H  HB3  . PHE   B 1 132 ? 41.932 -28.495 5.973   1.00 15.68 ?  132  PHE   B HB3  1 
ATOM   6125 H  HD1  . PHE   B 1 132 ? 45.305 -27.817 4.928   1.00 16.71 ?  132  PHE   B HD1  1 
ATOM   6126 H  HD2  . PHE   B 1 132 ? 41.993 -26.277 6.569   1.00 15.11 ?  132  PHE   B HD2  1 
ATOM   6127 H  HE1  . PHE   B 1 132 ? 46.334 -25.748 5.073   1.00 17.40 ?  132  PHE   B HE1  1 
ATOM   6128 H  HE2  . PHE   B 1 132 ? 43.014 -24.212 6.716   1.00 15.62 ?  132  PHE   B HE2  1 
ATOM   6129 H  HZ   . PHE   B 1 132 ? 45.186 -23.941 5.972   1.00 16.96 ?  132  PHE   B HZ   1 
ATOM   6130 N  N    . GLY   B 1 133 ? 42.585 -32.032 6.124   1.00 14.72 ?  133  GLY   B N    1 
ATOM   6131 C  CA   . GLY   B 1 133 ? 41.874 -33.203 6.610   1.00 15.67 ?  133  GLY   B CA   1 
ATOM   6132 C  C    . GLY   B 1 133 ? 40.479 -33.463 6.075   1.00 15.97 ?  133  GLY   B C    1 
ATOM   6133 O  O    . GLY   B 1 133 ? 39.890 -34.484 6.444   1.00 18.05 ?  133  GLY   B O    1 
ATOM   6134 H  H    . GLY   B 1 133 ? 43.073 -32.178 5.431   1.00 17.67 ?  133  GLY   B H    1 
ATOM   6135 H  HA2  . GLY   B 1 133 ? 42.411 -33.983 6.411   1.00 18.81 ?  133  GLY   B HA2  1 
ATOM   6136 H  HA3  . GLY   B 1 133 ? 41.801 -33.132 7.573   1.00 18.81 ?  133  GLY   B HA3  1 
ATOM   6137 N  N    . ALA   B 1 134 ? 39.921 -32.596 5.237   1.00 15.11 ?  134  ALA   B N    1 
ATOM   6138 C  CA   . ALA   B 1 134 ? 38.598 -32.874 4.700   1.00 15.50 ?  134  ALA   B CA   1 
ATOM   6139 C  C    . ALA   B 1 134 ? 38.688 -33.866 3.544   1.00 15.44 ?  134  ALA   B C    1 
ATOM   6140 O  O    . ALA   B 1 134 ? 39.741 -34.051 2.930   1.00 16.37 ?  134  ALA   B O    1 
ATOM   6141 C  CB   . ALA   B 1 134 ? 37.925 -31.587 4.228   1.00 16.16 ?  134  ALA   B CB   1 
ATOM   6142 H  H    . ALA   B 1 134 ? 40.277 -31.855 4.969   1.00 18.13 ?  134  ALA   B H    1 
ATOM   6143 H  HA   . ALA   B 1 134 ? 38.049 -33.264 5.398   1.00 18.60 ?  134  ALA   B HA   1 
ATOM   6144 H  HB1  . ALA   B 1 134 ? 37.040 -31.801 3.893   1.00 19.39 ?  134  ALA   B HB1  1 
ATOM   6145 H  HB2  . ALA   B 1 134 ? 37.857 -30.974 4.976   1.00 19.39 ?  134  ALA   B HB2  1 
ATOM   6146 H  HB3  . ALA   B 1 134 ? 38.460 -31.192 3.523   1.00 19.39 ?  134  ALA   B HB3  1 
ATOM   6147 N  N    . ASP   B 1 135 ? 37.559 -34.501 3.253   1.00 15.37 ?  135  ASP   B N    1 
ATOM   6148 C  CA   . ASP   B 1 135 ? 37.472 -35.400 2.111   1.00 16.07 ?  135  ASP   B CA   1 
ATOM   6149 C  C    . ASP   B 1 135 ? 37.567 -34.560 0.845   1.00 15.04 ?  135  ASP   B C    1 
ATOM   6150 O  O    . ASP   B 1 135 ? 36.713 -33.689 0.632   1.00 15.01 ?  135  ASP   B O    1 
ATOM   6151 C  CB   . ASP   B 1 135 ? 36.129 -36.130 2.168   1.00 18.16 ?  135  ASP   B CB   1 
ATOM   6152 C  CG   . ASP   B 1 135 ? 35.938 -37.119 1.034   1.00 19.91 ?  135  ASP   B CG   1 
ATOM   6153 O  OD1  . ASP   B 1 135 ? 36.795 -37.167 0.127   1.00 19.72 ?  135  ASP   B OD1  1 
ATOM   6154 O  OD2  . ASP   B 1 135 ? 34.934 -37.870 1.065   1.00 22.61 -1 135  ASP   B OD2  1 
ATOM   6155 H  H    . ASP   B 1 135 ? 36.827 -34.426 3.697   1.00 18.44 ?  135  ASP   B H    1 
ATOM   6156 H  HA   . ASP   B 1 135 ? 38.194 -36.050 2.143   1.00 19.29 ?  135  ASP   B HA   1 
ATOM   6157 H  HB2  . ASP   B 1 135 ? 36.076 -36.621 2.998   1.00 21.79 ?  135  ASP   B HB2  1 
ATOM   6158 H  HB3  . ASP   B 1 135 ? 35.418 -35.474 2.118   1.00 21.79 ?  135  ASP   B HB3  1 
ATOM   6159 N  N    . PRO   B 1 136 ? 38.575 -34.760 -0.007  1.00 15.29 ?  136  PRO   B N    1 
ATOM   6160 C  CA   . PRO   B 1 136 ? 38.667 -33.929 -1.217  1.00 14.75 ?  136  PRO   B CA   1 
ATOM   6161 C  C    . PRO   B 1 136 ? 37.478 -34.083 -2.145  1.00 13.99 ?  136  PRO   B C    1 
ATOM   6162 O  O    . PRO   B 1 136 ? 37.153 -33.134 -2.869  1.00 13.15 ?  136  PRO   B O    1 
ATOM   6163 C  CB   . PRO   B 1 136 ? 39.982 -34.389 -1.865  1.00 15.89 ?  136  PRO   B CB   1 
ATOM   6164 C  CG   . PRO   B 1 136 ? 40.190 -35.777 -1.348  1.00 16.68 ?  136  PRO   B CG   1 
ATOM   6165 C  CD   . PRO   B 1 136 ? 39.649 -35.762 0.054   1.00 16.48 ?  136  PRO   B CD   1 
ATOM   6166 H  HA   . PRO   B 1 136 ? 38.743 -32.993 -0.972  1.00 17.69 ?  136  PRO   B HA   1 
ATOM   6167 H  HB2  . PRO   B 1 136 ? 39.888 -34.387 -2.833  1.00 19.07 ?  136  PRO   B HB2  1 
ATOM   6168 H  HB3  . PRO   B 1 136 ? 40.702 -33.799 -1.591  1.00 19.07 ?  136  PRO   B HB3  1 
ATOM   6169 H  HG2  . PRO   B 1 136 ? 39.700 -36.406 -1.898  1.00 20.01 ?  136  PRO   B HG2  1 
ATOM   6170 H  HG3  . PRO   B 1 136 ? 41.136 -35.982 -1.347  1.00 20.01 ?  136  PRO   B HG3  1 
ATOM   6171 H  HD2  . PRO   B 1 136 ? 39.286 -36.631 0.285   1.00 19.78 ?  136  PRO   B HD2  1 
ATOM   6172 H  HD3  . PRO   B 1 136 ? 40.332 -35.481 0.682   1.00 19.78 ?  136  PRO   B HD3  1 
ATOM   6173 N  N    . ILE   B 1 137 ? 36.821 -35.248 -2.149  1.00 14.32 ?  137  ILE   B N    1 
ATOM   6174 C  CA   . ILE   B 1 137 ? 35.607 -35.415 -2.943  1.00 14.87 ?  137  ILE   B CA   1 
ATOM   6175 C  C    . ILE   B 1 137 ? 34.531 -34.453 -2.463  1.00 14.48 ?  137  ILE   B C    1 
ATOM   6176 O  O    . ILE   B 1 137 ? 33.815 -33.840 -3.264  1.00 14.26 ?  137  ILE   B O    1 
ATOM   6177 C  CB   . ILE   B 1 137 ? 35.133 -36.883 -2.888  1.00 16.99 ?  137  ILE   B CB   1 
ATOM   6178 C  CG1  . ILE   B 1 137 ? 36.104 -37.781 -3.655  1.00 19.47 ?  137  ILE   B CG1  1 
ATOM   6179 C  CG2  . ILE   B 1 137 ? 33.723 -37.024 -3.449  1.00 17.56 ?  137  ILE   B CG2  1 
ATOM   6180 C  CD1  . ILE   B 1 137 ? 35.827 -39.266 -3.494  1.00 21.65 ?  137  ILE   B CD1  1 
ATOM   6181 H  H    . ILE   B 1 137 ? 37.051 -35.949 -1.708  1.00 17.18 ?  137  ILE   B H    1 
ATOM   6182 H  HA   . ILE   B 1 137 ? 35.798 -35.205 -3.870  1.00 17.85 ?  137  ILE   B HA   1 
ATOM   6183 H  HB   . ILE   B 1 137 ? 35.116 -37.168 -1.965  1.00 20.39 ?  137  ILE   B HB   1 
ATOM   6184 H  HG12 . ILE   B 1 137 ? 36.044 -37.572 -4.601  1.00 23.36 ?  137  ILE   B HG12 1 
ATOM   6185 H  HG13 . ILE   B 1 137 ? 37.000 -37.611 -3.335  1.00 23.36 ?  137  ILE   B HG13 1 
ATOM   6186 H  HG21 . ILE   B 1 137 ? 33.520 -37.966 -3.583  1.00 21.08 ?  137  ILE   B HG21 1 
ATOM   6187 H  HG22 . ILE   B 1 137 ? 33.089 -36.647 -2.820  1.00 21.08 ?  137  ILE   B HG22 1 
ATOM   6188 H  HG23 . ILE   B 1 137 ? 33.669 -36.557 -4.297  1.00 21.08 ?  137  ILE   B HG23 1 
ATOM   6189 H  HD11 . ILE   B 1 137 ? 36.602 -39.764 -3.796  1.00 25.98 ?  137  ILE   B HD11 1 
ATOM   6190 H  HD12 . ILE   B 1 137 ? 35.656 -39.456 -2.558  1.00 25.98 ?  137  ILE   B HD12 1 
ATOM   6191 H  HD13 . ILE   B 1 137 ? 35.052 -39.507 -4.026  1.00 25.98 ?  137  ILE   B HD13 1 
ATOM   6192 N  N    . HIS   B 1 138 ? 34.405 -34.302 -1.148  1.00 14.54 ?  138  HIS   B N    1 
ATOM   6193 C  CA   . HIS   B 1 138 ? 33.450 -33.343 -0.611  1.00 14.74 ?  138  HIS   B CA   1 
ATOM   6194 C  C    . HIS   B 1 138 ? 33.865 -31.913 -0.921  1.00 13.86 ?  138  HIS   B C    1 
ATOM   6195 O  O    . HIS   B 1 138 ? 33.017 -31.072 -1.234  1.00 14.18 ?  138  HIS   B O    1 
ATOM   6196 C  CB   . HIS   B 1 138 ? 33.316 -33.535 0.891   1.00 16.27 ?  138  HIS   B CB   1 
ATOM   6197 C  CG   . HIS   B 1 138 ? 32.388 -32.554 1.526   1.00 17.49 ?  138  HIS   B CG   1 
ATOM   6198 N  ND1  . HIS   B 1 138 ? 31.050 -32.482 1.201   1.00 18.83 ?  138  HIS   B ND1  1 
ATOM   6199 C  CD2  . HIS   B 1 138 ? 32.607 -31.579 2.439   1.00 18.00 ?  138  HIS   B CD2  1 
ATOM   6200 C  CE1  . HIS   B 1 138 ? 30.481 -31.517 1.901   1.00 18.85 ?  138  HIS   B CE1  1 
ATOM   6201 N  NE2  . HIS   B 1 138 ? 31.405 -30.952 2.659   1.00 18.40 ?  138  HIS   B NE2  1 
ATOM   6202 H  H    . HIS   B 1 138 ? 34.858 -34.734 -0.561  1.00 17.45 ?  138  HIS   B H    1 
ATOM   6203 H  HA   . HIS   B 1 138 ? 32.581 -33.505 -1.017  1.00 17.69 ?  138  HIS   B HA   1 
ATOM   6204 H  HB2  . HIS   B 1 138 ? 32.970 -34.428 1.061   1.00 19.52 ?  138  HIS   B HB2  1 
ATOM   6205 H  HB3  . HIS   B 1 138 ? 34.185 -33.434 1.298   1.00 19.52 ?  138  HIS   B HB3  1 
ATOM   6206 H  HD1  . HIS   B 1 138 ? 30.646 -32.995 0.634   1.00 22.59 ?  138  HIS   B HD1  1 
ATOM   6207 H  HD2  . HIS   B 1 138 ? 33.411 -31.381 2.849   1.00 21.60 ?  138  HIS   B HD2  1 
ATOM   6208 H  HE1  . HIS   B 1 138 ? 29.578 -31.283 1.865   1.00 22.62 ?  138  HIS   B HE1  1 
ATOM   6209 N  N    . SER   B 1 139 ? 35.160 -31.612 -0.846  1.00 13.41 ?  139  SER   B N    1 
ATOM   6210 C  CA   . SER   B 1 139 ? 35.596 -30.260 -1.164  1.00 12.63 ?  139  SER   B CA   1 
ATOM   6211 C  C    . SER   B 1 139 ? 35.257 -29.903 -2.603  1.00 11.77 ?  139  SER   B C    1 
ATOM   6212 O  O    . SER   B 1 139 ? 34.813 -28.785 -2.880  1.00 12.00 ?  139  SER   B O    1 
ATOM   6213 C  CB   . SER   B 1 139 ? 37.090 -30.121 -0.901  1.00 12.91 ?  139  SER   B CB   1 
ATOM   6214 O  OG   . SER   B 1 139 ? 37.499 -28.788 -1.163  1.00 12.98 ?  139  SER   B OG   1 
ATOM   6215 H  H    . SER   B 1 139 ? 35.782 -32.160 -0.629  1.00 16.09 ?  139  SER   B H    1 
ATOM   6216 H  HA   . SER   B 1 139 ? 35.125 -29.642 -0.589  1.00 15.16 ?  139  SER   B HA   1 
ATOM   6217 H  HB2  . SER   B 1 139 ? 37.271 -30.335 0.027   1.00 15.49 ?  139  SER   B HB2  1 
ATOM   6218 H  HB3  . SER   B 1 139 ? 37.577 -30.722 -1.485  1.00 15.49 ?  139  SER   B HB3  1 
ATOM   6219 H  HG   . SER   B 1 139 ? 38.323 -28.704 -1.013  1.00 15.57 ?  139  SER   B HG   1 
ATOM   6220 N  N    . LEU   B 1 140 ? 35.449 -30.841 -3.532  1.00 12.09 ?  140  LEU   B N    1 
ATOM   6221 C  CA   . LEU   B 1 140 ? 35.078 -30.590 -4.919  1.00 12.11 ?  140  LEU   B CA   1 
ATOM   6222 C  C    . LEU   B 1 140 ? 33.573 -30.364 -5.046  1.00 12.21 ?  140  LEU   B C    1 
ATOM   6223 O  O    . LEU   B 1 140 ? 33.133 -29.473 -5.778  1.00 12.22 ?  140  LEU   B O    1 
ATOM   6224 C  CB   . LEU   B 1 140 ? 35.549 -31.746 -5.799  1.00 12.30 ?  140  LEU   B CB   1 
ATOM   6225 C  CG   . LEU   B 1 140 ? 35.175 -31.642 -7.270  1.00 12.33 ?  140  LEU   B CG   1 
ATOM   6226 C  CD1  . LEU   B 1 140 ? 35.734 -30.374 -7.884  1.00 13.12 ?  140  LEU   B CD1  1 
ATOM   6227 C  CD2  . LEU   B 1 140 ? 35.654 -32.869 -8.014  1.00 13.39 ?  140  LEU   B CD2  1 
ATOM   6228 H  H    . LEU   B 1 140 ? 35.786 -31.616 -3.390  1.00 14.51 ?  140  LEU   B H    1 
ATOM   6229 H  HA   . LEU   B 1 140 ? 35.527 -29.783 -5.221  1.00 14.54 ?  140  LEU   B HA   1 
ATOM   6230 H  HB2  . LEU   B 1 140 ? 36.516 -31.799 -5.750  1.00 14.76 ?  140  LEU   B HB2  1 
ATOM   6231 H  HB3  . LEU   B 1 140 ? 35.161 -32.568 -5.463  1.00 14.76 ?  140  LEU   B HB3  1 
ATOM   6232 H  HG   . LEU   B 1 140 ? 34.211 -31.604 -7.346  1.00 14.79 ?  140  LEU   B HG   1 
ATOM   6233 H  HD11 . LEU   B 1 140 ? 35.587 -30.399 -8.843  1.00 15.75 ?  140  LEU   B HD11 1 
ATOM   6234 H  HD12 . LEU   B 1 140 ? 35.272 -29.606 -7.503  1.00 15.75 ?  140  LEU   B HD12 1 
ATOM   6235 H  HD13 . LEU   B 1 140 ? 36.681 -30.317 -7.694  1.00 15.75 ?  140  LEU   B HD13 1 
ATOM   6236 H  HD21 . LEU   B 1 140 ? 35.404 -32.782 -8.948  1.00 16.07 ?  140  LEU   B HD21 1 
ATOM   6237 H  HD22 . LEU   B 1 140 ? 36.614 -32.933 -7.929  1.00 16.07 ?  140  LEU   B HD22 1 
ATOM   6238 H  HD23 . LEU   B 1 140 ? 35.228 -33.649 -7.628  1.00 16.07 ?  140  LEU   B HD23 1 
ATOM   6239 N  N    . ARG   B 1 141 ? 32.775 -31.154 -4.325  1.00 12.25 ?  141  ARG   B N    1 
ATOM   6240 C  CA   . ARG   B 1 141 ? 31.323 -30.984 -4.307  1.00 13.35 ?  141  ARG   B CA   1 
ATOM   6241 C  C    . ARG   B 1 141 ? 30.943 -29.573 -3.877  1.00 12.71 ?  141  ARG   B C    1 
ATOM   6242 O  O    . ARG   B 1 141 ? 30.139 -28.894 -4.533  1.00 12.87 ?  141  ARG   B O    1 
ATOM   6243 C  CB   . ARG   B 1 141 ? 30.746 -32.015 -3.328  1.00 15.05 ?  141  ARG   B CB   1 
ATOM   6244 C  CG   . ARG   B 1 141 ? 29.286 -31.894 -2.992  1.00 17.22 ?  141  ARG   B CG   1 
ATOM   6245 C  CD   . ARG   B 1 141 ? 28.489 -32.525 -4.054  1.00 19.05 ?  141  ARG   B CD   1 
ATOM   6246 N  NE   . ARG   B 1 141 ? 28.215 -31.613 -5.151  1.00 19.34 ?  141  ARG   B NE   1 
ATOM   6247 C  CZ   . ARG   B 1 141 ? 28.192 -31.959 -6.430  1.00 18.74 ?  141  ARG   B CZ   1 
ATOM   6248 N  NH1  . ARG   B 1 141 ? 28.624 -33.143 -6.837  1.00 18.79 ?  141  ARG   B NH1  1 
ATOM   6249 N  NH2  . ARG   B 1 141 ? 27.719 -31.094 -7.323  1.00 19.37 ?  141  ARG   B NH2  1 
ATOM   6250 H  H    . ARG   B 1 141 ? 33.057 -31.805 -3.837  1.00 14.70 ?  141  ARG   B H    1 
ATOM   6251 H  HA   . ARG   B 1 141 ? 30.963 -31.153 -5.191  1.00 16.02 ?  141  ARG   B HA   1 
ATOM   6252 H  HB2  . ARG   B 1 141 ? 30.896 -32.903 -3.699  1.00 18.06 ?  141  ARG   B HB2  1 
ATOM   6253 H  HB3  . ARG   B 1 141 ? 31.235 -31.945 -2.495  1.00 18.06 ?  141  ARG   B HB3  1 
ATOM   6254 H  HG2  . ARG   B 1 141 ? 29.115 -32.349 -2.155  1.00 20.66 ?  141  ARG   B HG2  1 
ATOM   6255 H  HG3  . ARG   B 1 141 ? 29.034 -30.957 -2.924  1.00 20.66 ?  141  ARG   B HG3  1 
ATOM   6256 H  HD2  . ARG   B 1 141 ? 28.970 -33.300 -4.398  1.00 22.86 ?  141  ARG   B HD2  1 
ATOM   6257 H  HD3  . ARG   B 1 141 ? 27.648 -32.811 -3.679  1.00 22.86 ?  141  ARG   B HD3  1 
ATOM   6258 H  HE   . ARG   B 1 141 ? 28.052 -30.792 -4.952  1.00 23.21 ?  141  ARG   B HE   1 
ATOM   6259 H  HH11 . ARG   B 1 141 ? 28.927 -33.714 -6.271  1.00 22.55 ?  141  ARG   B HH11 1 
ATOM   6260 H  HH12 . ARG   B 1 141 ? 28.608 -33.336 -7.671  1.00 22.55 ?  141  ARG   B HH12 1 
ATOM   6261 H  HH21 . ARG   B 1 141 ? 27.441 -30.319 -7.068  1.00 23.24 ?  141  ARG   B HH21 1 
ATOM   6262 H  HH22 . ARG   B 1 141 ? 27.714 -31.296 -8.158  1.00 23.24 ?  141  ARG   B HH22 1 
ATOM   6263 N  N    . VAL   B 1 142 ? 31.492 -29.127 -2.750  1.00 12.42 ?  142  VAL   B N    1 
ATOM   6264 C  CA   . VAL   B 1 142 ? 31.161 -27.795 -2.259  1.00 12.18 ?  142  VAL   B CA   1 
ATOM   6265 C  C    . VAL   B 1 142 ? 31.634 -26.735 -3.245  1.00 12.22 ?  142  VAL   B C    1 
ATOM   6266 O  O    . VAL   B 1 142 ? 30.934 -25.749 -3.497  1.00 12.55 ?  142  VAL   B O    1 
ATOM   6267 C  CB   . VAL   B 1 142 ? 31.717 -27.574 -0.840  1.00 13.00 ?  142  VAL   B CB   1 
ATOM   6268 C  CG1  . VAL   B 1 142 ? 31.396 -26.151 -0.353  1.00 13.08 ?  142  VAL   B CG1  1 
ATOM   6269 C  CG2  . VAL   B 1 142 ? 31.152 -28.608 0.119   1.00 13.97 ?  142  VAL   B CG2  1 
ATOM   6270 H  H    . VAL   B 1 142 ? 32.049 -29.566 -2.264  1.00 14.90 ?  142  VAL   B H    1 
ATOM   6271 H  HA   . VAL   B 1 142 ? 30.200 -27.724 -2.201  1.00 14.62 ?  142  VAL   B HA   1 
ATOM   6272 H  HB   . VAL   B 1 142 ? 32.683 -27.675 -0.855  1.00 15.60 ?  142  VAL   B HB   1 
ATOM   6273 H  HG11 . VAL   B 1 142 ? 31.588 -26.093 0.595   1.00 15.70 ?  142  VAL   B HG11 1 
ATOM   6274 H  HG12 . VAL   B 1 142 ? 31.946 -25.518 -0.841  1.00 15.70 ?  142  VAL   B HG12 1 
ATOM   6275 H  HG13 . VAL   B 1 142 ? 30.458 -25.969 -0.513  1.00 15.70 ?  142  VAL   B HG13 1 
ATOM   6276 H  HG21 . VAL   B 1 142 ? 31.480 -28.421 1.012   1.00 16.77 ?  142  VAL   B HG21 1 
ATOM   6277 H  HG22 . VAL   B 1 142 ? 30.187 -28.561 0.099   1.00 16.77 ?  142  VAL   B HG22 1 
ATOM   6278 H  HG23 . VAL   B 1 142 ? 31.448 -29.490 -0.162  1.00 16.77 ?  142  VAL   B HG23 1 
ATOM   6279 N  N    . CYS   B 1 143 ? 32.815 -26.935 -3.837  1.00 11.47 ?  143  CYS   B N    1 
ATOM   6280 C  CA   . CYS   B 1 143 ? 33.308 -25.992 -4.837  1.00 11.66 ?  143  CYS   B CA   1 
ATOM   6281 C  C    . CYS   B 1 143 ? 32.305 -25.846 -5.977  1.00 11.80 ?  143  CYS   B C    1 
ATOM   6282 O  O    . CYS   B 1 143 ? 31.896 -24.736 -6.332  1.00 12.02 ?  143  CYS   B O    1 
ATOM   6283 C  CB   . CYS   B 1 143 ? 34.658 -26.479 -5.367  1.00 11.87 ?  143  CYS   B CB   1 
ATOM   6284 S  SG   . CYS   B 1 143 ? 35.407 -25.374 -6.579  1.00 12.33 ?  143  CYS   B SG   1 
ATOM   6285 H  H    . CYS   B 1 143 ? 33.338 -27.599 -3.681  1.00 13.77 ?  143  CYS   B H    1 
ATOM   6286 H  HA   . CYS   B 1 143 ? 33.433 -25.123 -4.427  1.00 13.99 ?  143  CYS   B HA   1 
ATOM   6287 H  HB2  . CYS   B 1 143 ? 35.278 -26.560 -4.626  1.00 14.25 ?  143  CYS   B HB2  1 
ATOM   6288 H  HB3  . CYS   B 1 143 ? 34.537 -27.339 -5.787  1.00 14.25 ?  143  CYS   B HB3  1 
ATOM   6289 H  HG   . CYS   B 1 143 ? 36.473 -25.814 -6.914  1.00 14.79 ?  143  CYS   B HG   1 
ATOM   6290 N  N    . VAL   B 1 144 ? 31.897 -26.966 -6.570  1.00 12.10 ?  144  VAL   B N    1 
ATOM   6291 C  CA   . VAL   B 1 144 ? 30.988 -26.902 -7.710  1.00 13.21 ?  144  VAL   B CA   1 
ATOM   6292 C  C    . VAL   B 1 144 ? 29.649 -26.288 -7.329  1.00 13.20 ?  144  VAL   B C    1 
ATOM   6293 O  O    . VAL   B 1 144 ? 29.032 -25.577 -8.134  1.00 14.28 ?  144  VAL   B O    1 
ATOM   6294 C  CB   . VAL   B 1 144 ? 30.826 -28.309 -8.290  1.00 15.69 ?  144  VAL   B CB   1 
ATOM   6295 C  CG1  . VAL   B 1 144 ? 29.565 -28.422 -9.141  1.00 18.09 ?  144  VAL   B CG1  1 
ATOM   6296 C  CG2  . VAL   B 1 144 ? 32.082 -28.707 -9.061  1.00 15.85 ?  144  VAL   B CG2  1 
ATOM   6297 H  H    . VAL   B 1 144 ? 32.132 -27.763 -6.343  1.00 14.52 ?  144  VAL   B H    1 
ATOM   6298 H  HA   . VAL   B 1 144 ? 31.378 -26.343 -8.398  1.00 15.85 ?  144  VAL   B HA   1 
ATOM   6299 H  HB   . VAL   B 1 144 ? 30.730 -28.935 -7.554  1.00 18.83 ?  144  VAL   B HB   1 
ATOM   6300 H  HG11 . VAL   B 1 144 ? 29.649 -29.202 -9.714  1.00 21.71 ?  144  VAL   B HG11 1 
ATOM   6301 H  HG12 . VAL   B 1 144 ? 28.799 -28.526 -8.557  1.00 21.71 ?  144  VAL   B HG12 1 
ATOM   6302 H  HG13 . VAL   B 1 144 ? 29.476 -27.625 -9.681  1.00 21.71 ?  144  VAL   B HG13 1 
ATOM   6303 H  HG21 . VAL   B 1 144 ? 31.963 -29.602 -9.416  1.00 19.02 ?  144  VAL   B HG21 1 
ATOM   6304 H  HG22 . VAL   B 1 144 ? 32.216 -28.078 -9.788  1.00 19.02 ?  144  VAL   B HG22 1 
ATOM   6305 H  HG23 . VAL   B 1 144 ? 32.840 -28.686 -8.459  1.00 19.02 ?  144  VAL   B HG23 1 
ATOM   6306 N  N    . ASP   B 1 145 ? 29.187 -26.534 -6.107  1.00 13.38 ?  145  ASP   B N    1 
ATOM   6307 C  CA   . ASP   B 1 145 ? 27.878 -26.069 -5.670  1.00 13.79 ?  145  ASP   B CA   1 
ATOM   6308 C  C    . ASP   B 1 145 ? 27.904 -24.645 -5.125  1.00 13.16 ?  145  ASP   B C    1 
ATOM   6309 O  O    . ASP   B 1 145 ? 26.842 -24.103 -4.798  1.00 15.17 ?  145  ASP   B O    1 
ATOM   6310 C  CB   . ASP   B 1 145 ? 27.308 -26.996 -4.587  1.00 15.42 ?  145  ASP   B CB   1 
ATOM   6311 C  CG   . ASP   B 1 145 ? 26.930 -28.367 -5.105  1.00 17.31 ?  145  ASP   B CG   1 
ATOM   6312 O  OD1  . ASP   B 1 145 ? 26.818 -28.556 -6.333  1.00 17.67 ?  145  ASP   B OD1  1 
ATOM   6313 O  OD2  . ASP   B 1 145 ? 26.735 -29.258 -4.255  1.00 19.35 -1 145  ASP   B OD2  1 
ATOM   6314 H  H    . ASP   B 1 145 ? 29.629 -26.952 -5.504  1.00 16.06 ?  145  ASP   B H    1 
ATOM   6315 H  HA   . ASP   B 1 145 ? 27.278 -26.070 -6.427  1.00 16.55 ?  145  ASP   B HA   1 
ATOM   6316 H  HB2  . ASP   B 1 145 ? 27.966 -27.120 -3.897  1.00 18.50 ?  145  ASP   B HB2  1 
ATOM   6317 H  HB3  . ASP   B 1 145 ? 26.505 -26.589 -4.223  1.00 18.50 ?  145  ASP   B HB3  1 
ATOM   6318 N  N    . THR   B 1 146 ? 29.082 -24.036 -5.001  1.00 11.76 ?  146  THR   B N    1 
ATOM   6319 C  CA   . THR   B 1 146 ? 29.220 -22.713 -4.395  1.00 11.55 ?  146  THR   B CA   1 
ATOM   6320 C  C    . THR   B 1 146 ? 29.850 -21.682 -5.313  1.00 11.35 ?  146  THR   B C    1 
ATOM   6321 O  O    . THR   B 1 146 ? 29.393 -20.526 -5.356  1.00 11.62 ?  146  THR   B O    1 
ATOM   6322 C  CB   . THR   B 1 146 ? 30.047 -22.820 -3.105  1.00 11.94 ?  146  THR   B CB   1 
ATOM   6323 O  OG1  . THR   B 1 146 ? 29.479 -23.818 -2.253  1.00 11.97 ?  146  THR   B OG1  1 
ATOM   6324 C  CG2  . THR   B 1 146 ? 30.115 -21.480 -2.380  1.00 12.12 ?  146  THR   B CG2  1 
ATOM   6325 H  H    . THR   B 1 146 ? 29.834 -24.367 -5.266  1.00 14.11 ?  146  THR   B H    1 
ATOM   6326 H  HA   . THR   B 1 146 ? 28.348 -22.385 -4.154  1.00 13.85 ?  146  THR   B HA   1 
ATOM   6327 H  HB   . THR   B 1 146 ? 30.958 -23.071 -3.328  1.00 14.33 ?  146  THR   B HB   1 
ATOM   6328 H  HG1  . THR   B 1 146 ? 29.526 -24.576 -2.632  1.00 14.36 ?  146  THR   B HG1  1 
ATOM   6329 H  HG21 . THR   B 1 146 ? 30.476 -21.602 -1.489  1.00 14.54 ?  146  THR   B HG21 1 
ATOM   6330 H  HG22 . THR   B 1 146 ? 30.690 -20.866 -2.868  1.00 14.54 ?  146  THR   B HG22 1 
ATOM   6331 H  HG23 . THR   B 1 146 ? 29.229 -21.096 -2.313  1.00 14.54 ?  146  THR   B HG23 1 
ATOM   6332 N  N    . VAL   B 1 147 ? 30.906 -22.054 -6.022  1.00 11.36 ?  147  VAL   B N    1 
ATOM   6333 C  CA   . VAL   B 1 147 ? 31.628 -21.106 -6.854  1.00 10.74 ?  147  VAL   B CA   1 
ATOM   6334 C  C    . VAL   B 1 147 ? 30.894 -20.969 -8.175  1.00 11.11 ?  147  VAL   B C    1 
ATOM   6335 O  O    . VAL   B 1 147 ? 30.526 -21.972 -8.803  1.00 11.79 ?  147  VAL   B O    1 
ATOM   6336 C  CB   . VAL   B 1 147 ? 33.081 -21.563 -7.066  1.00 10.77 ?  147  VAL   B CB   1 
ATOM   6337 C  CG1  . VAL   B 1 147 ? 33.839 -20.538 -7.881  1.00 11.28 ?  147  VAL   B CG1  1 
ATOM   6338 C  CG2  . VAL   B 1 147 ? 33.773 -21.790 -5.731  1.00 11.25 ?  147  VAL   B CG2  1 
ATOM   6339 H  H    . VAL   B 1 147 ? 31.232 -22.855 -6.043  1.00 13.64 ?  147  VAL   B H    1 
ATOM   6340 H  HA   . VAL   B 1 147 ? 31.647 -20.242 -6.421  1.00 12.89 ?  147  VAL   B HA   1 
ATOM   6341 H  HB   . VAL   B 1 147 ? 33.089 -22.401 -7.562  1.00 12.93 ?  147  VAL   B HB   1 
ATOM   6342 H  HG11 . VAL   B 1 147 ? 34.783 -20.761 -7.870  1.00 13.54 ?  147  VAL   B HG11 1 
ATOM   6343 H  HG12 . VAL   B 1 147 ? 33.508 -20.544 -8.792  1.00 13.54 ?  147  VAL   B HG12 1 
ATOM   6344 H  HG13 . VAL   B 1 147 ? 33.703 -19.662 -7.483  1.00 13.54 ?  147  VAL   B HG13 1 
ATOM   6345 H  HG21 . VAL   B 1 147 ? 34.711 -21.992 -5.890  1.00 13.51 ?  147  VAL   B HG21 1 
ATOM   6346 H  HG22 . VAL   B 1 147 ? 33.696 -20.985 -5.198  1.00 13.51 ?  147  VAL   B HG22 1 
ATOM   6347 H  HG23 . VAL   B 1 147 ? 33.348 -22.533 -5.278  1.00 13.51 ?  147  VAL   B HG23 1 
ATOM   6348 N  N    . ARG   B 1 148 ? 30.682 -19.719 -8.591  1.00 11.15 ?  148  ARG   B N    1 
ATOM   6349 C  CA   . ARG   B 1 148 ? 30.062 -19.395 -9.864  1.00 11.27 ?  148  ARG   B CA   1 
ATOM   6350 C  C    . ARG   B 1 148 ? 31.016 -18.720 -10.834 1.00 11.46 ?  148  ARG   B C    1 
ATOM   6351 O  O    . ARG   B 1 148 ? 30.729 -18.698 -12.035 1.00 12.90 ?  148  ARG   B O    1 
ATOM   6352 C  CB   . ARG   B 1 148 ? 28.826 -18.508 -9.642  1.00 12.10 ?  148  ARG   B CB   1 
ATOM   6353 C  CG   . ARG   B 1 148 ? 27.751 -19.222 -8.838  1.00 12.90 ?  148  ARG   B CG   1 
ATOM   6354 C  CD   . ARG   B 1 148 ? 26.540 -18.347 -8.520  1.00 13.68 ?  148  ARG   B CD   1 
ATOM   6355 N  NE   . ARG   B 1 148 ? 26.919 -17.150 -7.782  1.00 13.26 ?  148  ARG   B NE   1 
ATOM   6356 C  CZ   . ARG   B 1 148 ? 27.224 -17.120 -6.491  1.00 12.19 ?  148  ARG   B CZ   1 
ATOM   6357 N  NH1  . ARG   B 1 148 ? 27.168 -18.209 -5.738  1.00 12.40 ?  148  ARG   B NH1  1 
ATOM   6358 N  NH2  . ARG   B 1 148 ? 27.616 -15.972 -5.944  1.00 12.43 ?  148  ARG   B NH2  1 
ATOM   6359 H  H    . ARG   B 1 148 ? 30.895 -19.019 -8.127  1.00 13.38 ?  148  ARG   B H    1 
ATOM   6360 H  HA   . ARG   B 1 148 ? 29.760 -20.217 -10.274 1.00 13.52 ?  148  ARG   B HA   1 
ATOM   6361 H  HB2  . ARG   B 1 148 ? 29.088 -17.708 -9.153  1.00 14.52 ?  148  ARG   B HB2  1 
ATOM   6362 H  HB3  . ARG   B 1 148 ? 28.450 -18.263 -10.501 1.00 14.52 ?  148  ARG   B HB3  1 
ATOM   6363 H  HG2  . ARG   B 1 148 ? 27.440 -19.987 -9.347  1.00 15.48 ?  148  ARG   B HG2  1 
ATOM   6364 H  HG3  . ARG   B 1 148 ? 28.132 -19.517 -7.998  1.00 15.48 ?  148  ARG   B HG3  1 
ATOM   6365 H  HD2  . ARG   B 1 148 ? 26.120 -18.071 -9.350  1.00 16.42 ?  148  ARG   B HD2  1 
ATOM   6366 H  HD3  . ARG   B 1 148 ? 25.913 -18.854 -7.981  1.00 16.42 ?  148  ARG   B HD3  1 
ATOM   6367 H  HE   . ARG   B 1 148 ? 26.950 -16.409 -8.214  1.00 15.91 ?  148  ARG   B HE   1 
ATOM   6368 H  HH11 . ARG   B 1 148 ? 26.913 -18.956 -6.075  1.00 14.88 ?  148  ARG   B HH11 1 
ATOM   6369 H  HH12 . ARG   B 1 148 ? 27.364 -18.162 -4.900  1.00 14.88 ?  148  ARG   B HH12 1 
ATOM   6370 H  HH21 . ARG   B 1 148 ? 27.662 -15.260 -6.424  1.00 14.92 ?  148  ARG   B HH21 1 
ATOM   6371 H  HH22 . ARG   B 1 148 ? 27.815 -15.937 -5.108  1.00 14.92 ?  148  ARG   B HH22 1 
ATOM   6372 N  N    . THR   B 1 149 ? 32.126 -18.172 -10.346 1.00 11.48 ?  149  THR   B N    1 
ATOM   6373 C  CA   . THR   B 1 149 ? 33.160 -17.611 -11.199 1.00 11.36 ?  149  THR   B CA   1 
ATOM   6374 C  C    . THR   B 1 149 ? 34.047 -18.746 -11.710 1.00 10.77 ?  149  THR   B C    1 
ATOM   6375 O  O    . THR   B 1 149 ? 33.855 -19.916 -11.370 1.00 11.54 ?  149  THR   B O    1 
ATOM   6376 C  CB   . THR   B 1 149 ? 33.929 -16.558 -10.416 1.00 11.29 ?  149  THR   B CB   1 
ATOM   6377 O  OG1  . THR   B 1 149 ? 34.389 -17.161 -9.204  1.00 11.36 ?  149  THR   B OG1  1 
ATOM   6378 C  CG2  . THR   B 1 149 ? 33.033 -15.361 -10.106 1.00 11.75 ?  149  THR   B CG2  1 
ATOM   6379 H  H    . THR   B 1 149 ? 32.296 -18.107 -9.502  1.00 13.77 ?  149  THR   B H    1 
ATOM   6380 H  HA   . THR   B 1 149 ? 32.743 -17.180 -11.960 1.00 13.63 ?  149  THR   B HA   1 
ATOM   6381 H  HB   . THR   B 1 149 ? 34.685 -16.256 -10.937 1.00 13.54 ?  149  THR   B HB   1 
ATOM   6382 H  HG1  . THR   B 1 149 ? 34.808 -16.588 -8.745  1.00 13.63 ?  149  THR   B HG1  1 
ATOM   6383 H  HG21 . THR   B 1 149 ? 33.537 -14.683 -9.630  1.00 14.10 ?  149  THR   B HG21 1 
ATOM   6384 H  HG22 . THR   B 1 149 ? 32.693 -14.978 -10.932 1.00 14.10 ?  149  THR   B HG22 1 
ATOM   6385 H  HG23 . THR   B 1 149 ? 32.281 -15.638 -9.558  1.00 14.10 ?  149  THR   B HG23 1 
ATOM   6386 N  N    . ASN   B 1 150 ? 35.009 -18.424 -12.561 1.00 10.90 ?  150  ASN   B N    1 
ATOM   6387 C  CA   . ASN   B 1 150 ? 35.771 -19.448 -13.263 1.00 11.37 ?  150  ASN   B CA   1 
ATOM   6388 C  C    . ASN   B 1 150 ? 36.938 -19.901 -12.397 1.00 11.16 ?  150  ASN   B C    1 
ATOM   6389 O  O    . ASN   B 1 150 ? 37.866 -19.132 -12.138 1.00 12.05 ?  150  ASN   B O    1 
ATOM   6390 C  CB   . ASN   B 1 150 ? 36.242 -18.917 -14.608 1.00 13.27 ?  150  ASN   B CB   1 
ATOM   6391 C  CG   . ASN   B 1 150 ? 35.095 -18.697 -15.553 1.00 15.77 ?  150  ASN   B CG   1 
ATOM   6392 O  OD1  . ASN   B 1 150 ? 34.192 -19.524 -15.639 1.00 17.00 ?  150  ASN   B OD1  1 
ATOM   6393 N  ND2  . ASN   B 1 150 ? 35.101 -17.568 -16.241 1.00 17.55 ?  150  ASN   B ND2  1 
ATOM   6394 H  H    . ASN   B 1 150 ? 35.253 -17.614 -12.737 1.00 13.08 ?  150  ASN   B H    1 
ATOM   6395 H  HA   . ASN   B 1 150 ? 35.189 -20.212 -13.422 1.00 13.65 ?  150  ASN   B HA   1 
ATOM   6396 H  HB2  . ASN   B 1 150 ? 36.690 -18.066 -14.470 1.00 15.92 ?  150  ASN   B HB2  1 
ATOM   6397 H  HB3  . ASN   B 1 150 ? 36.846 -19.556 -15.006 1.00 15.92 ?  150  ASN   B HB3  1 
ATOM   6398 H  HD21 . ASN   B 1 150 ? 34.467 -17.393 -16.795 1.00 21.06 ?  150  ASN   B HD21 1 
ATOM   6399 H  HD22 . ASN   B 1 150 ? 35.750 -17.005 -16.146 1.00 21.06 ?  150  ASN   B HD22 1 
ATOM   6400 N  N    . VAL   B 1 151 ? 36.900 -21.152 -11.955 1.00 10.77 ?  151  VAL   B N    1 
ATOM   6401 C  CA   . VAL   B 1 151 ? 37.919 -21.683 -11.066 1.00 11.04 ?  151  VAL   B CA   1 
ATOM   6402 C  C    . VAL   B 1 151 ? 38.624 -22.852 -11.744 1.00 10.65 ?  151  VAL   B C    1 
ATOM   6403 O  O    . VAL   B 1 151 ? 37.982 -23.788 -12.246 1.00 11.69 ?  151  VAL   B O    1 
ATOM   6404 C  CB   . VAL   B 1 151 ? 37.356 -22.021 -9.670  1.00 12.31 ?  151  VAL   B CB   1 
ATOM   6405 C  CG1  . VAL   B 1 151 ? 36.188 -23.013 -9.753  1.00 13.06 ?  151  VAL   B CG1  1 
ATOM   6406 C  CG2  . VAL   B 1 151 ? 38.461 -22.525 -8.760  1.00 12.82 ?  151  VAL   B CG2  1 
ATOM   6407 H  H    . VAL   B 1 151 ? 36.283 -21.719 -12.158 1.00 12.92 ?  151  VAL   B H    1 
ATOM   6408 H  HA   . VAL   B 1 151 ? 38.588 -20.989 -10.933 1.00 13.25 ?  151  VAL   B HA   1 
ATOM   6409 H  HB   . VAL   B 1 151 ? 37.014 -21.202 -9.276  1.00 14.77 ?  151  VAL   B HB   1 
ATOM   6410 H  HG11 . VAL   B 1 151 ? 35.871 -23.207 -8.857  1.00 15.67 ?  151  VAL   B HG11 1 
ATOM   6411 H  HG12 . VAL   B 1 151 ? 35.470 -22.617 -10.276 1.00 15.67 ?  151  VAL   B HG12 1 
ATOM   6412 H  HG13 . VAL   B 1 151 ? 36.492 -23.830 -10.179 1.00 15.67 ?  151  VAL   B HG13 1 
ATOM   6413 H  HG21 . VAL   B 1 151 ? 38.114 -22.600 -7.856  1.00 15.39 ?  151  VAL   B HG21 1 
ATOM   6414 H  HG22 . VAL   B 1 151 ? 38.757 -23.397 -9.070  1.00 15.39 ?  151  VAL   B HG22 1 
ATOM   6415 H  HG23 . VAL   B 1 151 ? 39.201 -21.899 -8.777  1.00 15.39 ?  151  VAL   B HG23 1 
ATOM   6416 N  N    . TYR   B 1 152 ? 39.956 -22.762 -11.769 1.00 10.18 ?  152  TYR   B N    1 
ATOM   6417 C  CA   . TYR   B 1 152 ? 40.859 -23.743 -12.351 1.00 10.61 ?  152  TYR   B CA   1 
ATOM   6418 C  C    . TYR   B 1 152 ? 41.577 -24.423 -11.189 1.00 10.04 ?  152  TYR   B C    1 
ATOM   6419 O  O    . TYR   B 1 152 ? 42.417 -23.808 -10.526 1.00 10.76 ?  152  TYR   B O    1 
ATOM   6420 C  CB   . TYR   B 1 152 ? 41.830 -23.031 -13.294 1.00 11.53 ?  152  TYR   B CB   1 
ATOM   6421 C  CG   . TYR   B 1 152 ? 41.151 -22.570 -14.556 1.00 12.01 ?  152  TYR   B CG   1 
ATOM   6422 C  CD1  . TYR   B 1 152 ? 40.486 -21.350 -14.617 1.00 12.38 ?  152  TYR   B CD1  1 
ATOM   6423 C  CD2  . TYR   B 1 152 ? 41.153 -23.373 -15.686 1.00 13.14 ?  152  TYR   B CD2  1 
ATOM   6424 C  CE1  . TYR   B 1 152 ? 39.846 -20.945 -15.773 1.00 13.73 ?  152  TYR   B CE1  1 
ATOM   6425 C  CE2  . TYR   B 1 152 ? 40.521 -22.977 -16.844 1.00 13.97 ?  152  TYR   B CE2  1 
ATOM   6426 C  CZ   . TYR   B 1 152 ? 39.866 -21.762 -16.884 1.00 14.09 ?  152  TYR   B CZ   1 
ATOM   6427 O  OH   . TYR   B 1 152 ? 39.236 -21.374 -18.042 1.00 16.41 ?  152  TYR   B OH   1 
ATOM   6428 H  H    . TYR   B 1 152 ? 40.390 -22.097 -11.423 1.00 12.21 ?  152  TYR   B H    1 
ATOM   6429 H  HA   . TYR   B 1 152 ? 40.353 -24.407 -12.851 1.00 12.73 ?  152  TYR   B HA   1 
ATOM   6430 H  HB2  . TYR   B 1 152 ? 42.194 -22.253 -12.841 1.00 13.83 ?  152  TYR   B HB2  1 
ATOM   6431 H  HB3  . TYR   B 1 152 ? 42.546 -23.639 -13.536 1.00 13.83 ?  152  TYR   B HB3  1 
ATOM   6432 H  HD1  . TYR   B 1 152 ? 40.466 -20.798 -13.866 1.00 14.86 ?  152  TYR   B HD1  1 
ATOM   6433 H  HD2  . TYR   B 1 152 ? 41.589 -24.197 -15.658 1.00 15.77 ?  152  TYR   B HD2  1 
ATOM   6434 H  HE1  . TYR   B 1 152 ? 39.406 -20.129 -15.802 1.00 16.47 ?  152  TYR   B HE1  1 
ATOM   6435 H  HE2  . TYR   B 1 152 ? 40.532 -23.532 -17.593 1.00 16.77 ?  152  TYR   B HE2  1 
ATOM   6436 H  HH   . TYR   B 1 152 ? 39.331 -21.973 -18.627 1.00 19.69 ?  152  TYR   B HH   1 
ATOM   6437 N  N    . LEU   B 1 153 ? 41.212 -25.681 -10.924 1.00 10.27 ?  153  LEU   B N    1 
ATOM   6438 C  CA   . LEU   B 1 153 ? 41.721 -26.430 -9.784  1.00 9.79  ?  153  LEU   B CA   1 
ATOM   6439 C  C    . LEU   B 1 153 ? 42.954 -27.228 -10.180 1.00 10.41 ?  153  LEU   B C    1 
ATOM   6440 O  O    . LEU   B 1 153 ? 42.934 -27.956 -11.175 1.00 11.65 ?  153  LEU   B O    1 
ATOM   6441 C  CB   . LEU   B 1 153 ? 40.647 -27.393 -9.274  1.00 10.61 ?  153  LEU   B CB   1 
ATOM   6442 C  CG   . LEU   B 1 153 ? 39.393 -26.743 -8.691  1.00 11.08 ?  153  LEU   B CG   1 
ATOM   6443 C  CD1  . LEU   B 1 153 ? 38.298 -27.794 -8.547  1.00 12.19 ?  153  LEU   B CD1  1 
ATOM   6444 C  CD2  . LEU   B 1 153 ? 39.703 -26.103 -7.349  1.00 11.71 ?  153  LEU   B CD2  1 
ATOM   6445 H  H    . LEU   B 1 153 ? 40.647 -26.131 -11.405 1.00 12.33 ?  153  LEU   B H    1 
ATOM   6446 H  HA   . LEU   B 1 153 ? 41.944 -25.816 -9.073  1.00 11.75 ?  153  LEU   B HA   1 
ATOM   6447 H  HB2  . LEU   B 1 153 ? 40.361 -27.957 -10.009 1.00 12.73 ?  153  LEU   B HB2  1 
ATOM   6448 H  HB3  . LEU   B 1 153 ? 41.036 -27.945 -8.576  1.00 12.73 ?  153  LEU   B HB3  1 
ATOM   6449 H  HG   . LEU   B 1 153 ? 39.076 -26.047 -9.289  1.00 13.30 ?  153  LEU   B HG   1 
ATOM   6450 H  HD11 . LEU   B 1 153 ? 37.501 -27.367 -8.196  1.00 14.63 ?  153  LEU   B HD11 1 
ATOM   6451 H  HD12 . LEU   B 1 153 ? 38.118 -28.172 -9.418  1.00 14.63 ?  153  LEU   B HD12 1 
ATOM   6452 H  HD13 . LEU   B 1 153 ? 38.605 -28.479 -7.937  1.00 14.63 ?  153  LEU   B HD13 1 
ATOM   6453 H  HD21 . LEU   B 1 153 ? 38.890 -25.740 -6.969  1.00 14.05 ?  153  LEU   B HD21 1 
ATOM   6454 H  HD22 . LEU   B 1 153 ? 40.072 -26.781 -6.755  1.00 14.05 ?  153  LEU   B HD22 1 
ATOM   6455 H  HD23 . LEU   B 1 153 ? 40.356 -25.395 -7.477  1.00 14.05 ?  153  LEU   B HD23 1 
ATOM   6456 N  N    . ALA   B 1 154 ? 44.006 -27.125 -9.375  1.00 10.58 ?  154  ALA   B N    1 
ATOM   6457 C  CA   . ALA   B 1 154 ? 45.234 -27.880 -9.567  1.00 11.73 ?  154  ALA   B CA   1 
ATOM   6458 C  C    . ALA   B 1 154 ? 45.304 -28.961 -8.498  1.00 12.35 ?  154  ALA   B C    1 
ATOM   6459 O  O    . ALA   B 1 154 ? 45.227 -28.665 -7.298  1.00 13.68 ?  154  ALA   B O    1 
ATOM   6460 C  CB   . ALA   B 1 154 ? 46.454 -26.966 -9.492  1.00 12.95 ?  154  ALA   B CB   1 
ATOM   6461 H  H    . ALA   B 1 154 ? 44.024 -26.601 -8.684  1.00 12.69 ?  154  ALA   B H    1 
ATOM   6462 H  HA   . ALA   B 1 154 ? 45.220 -28.303 -10.432 1.00 14.08 ?  154  ALA   B HA   1 
ATOM   6463 H  HB1  . ALA   B 1 154 ? 47.255 -27.495 -9.620  1.00 15.54 ?  154  ALA   B HB1  1 
ATOM   6464 H  HB2  . ALA   B 1 154 ? 46.387 -26.290 -10.186 1.00 15.54 ?  154  ALA   B HB2  1 
ATOM   6465 H  HB3  . ALA   B 1 154 ? 46.479 -26.535 -8.619  1.00 15.54 ?  154  ALA   B HB3  1 
ATOM   6466 N  N    . VAL   B 1 155 ? 45.423 -30.208 -8.936  1.00 11.64 ?  155  VAL   B N    1 
ATOM   6467 C  CA   . VAL   B 1 155 ? 45.526 -31.356 -8.047  1.00 11.61 ?  155  VAL   B CA   1 
ATOM   6468 C  C    . VAL   B 1 155 ? 46.865 -32.029 -8.327  1.00 11.64 ?  155  VAL   B C    1 
ATOM   6469 O  O    . VAL   B 1 155 ? 47.101 -32.515 -9.441  1.00 13.67 ?  155  VAL   B O    1 
ATOM   6470 C  CB   . VAL   B 1 155 ? 44.364 -32.343 -8.248  1.00 13.09 ?  155  VAL   B CB   1 
ATOM   6471 C  CG1  . VAL   B 1 155 ? 44.549 -33.546 -7.346  1.00 13.27 ?  155  VAL   B CG1  1 
ATOM   6472 C  CG2  . VAL   B 1 155 ? 43.025 -31.657 -7.974  1.00 14.25 ?  155  VAL   B CG2  1 
ATOM   6473 H  H    . VAL   B 1 155 ? 45.453 -30.418 -9.772  1.00 13.97 ?  155  VAL   B H    1 
ATOM   6474 H  HA   . VAL   B 1 155 ? 45.515 -31.059 -7.125  1.00 13.93 ?  155  VAL   B HA   1 
ATOM   6475 H  HB   . VAL   B 1 155 ? 44.362 -32.649 -9.171  1.00 15.71 ?  155  VAL   B HB   1 
ATOM   6476 H  HG11 . VAL   B 1 155 ? 43.717 -34.044 -7.304  1.00 15.92 ?  155  VAL   B HG11 1 
ATOM   6477 H  HG12 . VAL   B 1 155 ? 45.250 -34.116 -7.708  1.00 15.92 ?  155  VAL   B HG12 1 
ATOM   6478 H  HG13 . VAL   B 1 155 ? 44.797 -33.245 -6.458  1.00 15.92 ?  155  VAL   B HG13 1 
ATOM   6479 H  HG21 . VAL   B 1 155 ? 42.310 -32.305 -8.078  1.00 17.09 ?  155  VAL   B HG21 1 
ATOM   6480 H  HG22 . VAL   B 1 155 ? 43.028 -31.313 -7.066  1.00 17.09 ?  155  VAL   B HG22 1 
ATOM   6481 H  HG23 . VAL   B 1 155 ? 42.905 -30.929 -8.603  1.00 17.09 ?  155  VAL   B HG23 1 
ATOM   6482 N  N    . PHE   B 1 156 ? 47.733 -32.072 -7.312  1.00 12.34 ?  156  PHE   B N    1 
ATOM   6483 C  CA   . PHE   B 1 156 ? 49.111 -32.522 -7.513  1.00 13.29 ?  156  PHE   B CA   1 
ATOM   6484 C  C    . PHE   B 1 156 ? 49.212 -34.021 -7.802  1.00 14.41 ?  156  PHE   B C    1 
ATOM   6485 O  O    . PHE   B 1 156 ? 49.938 -34.444 -8.713  1.00 16.00 ?  156  PHE   B O    1 
ATOM   6486 C  CB   . PHE   B 1 156 ? 49.935 -32.153 -6.281  1.00 13.29 ?  156  PHE   B CB   1 
ATOM   6487 C  CG   . PHE   B 1 156 ? 51.357 -32.614 -6.338  1.00 14.03 ?  156  PHE   B CG   1 
ATOM   6488 C  CD1  . PHE   B 1 156 ? 52.234 -32.081 -7.263  1.00 15.72 ?  156  PHE   B CD1  1 
ATOM   6489 C  CD2  . PHE   B 1 156 ? 51.818 -33.571 -5.456  1.00 14.36 ?  156  PHE   B CD2  1 
ATOM   6490 C  CE1  . PHE   B 1 156 ? 53.553 -32.497 -7.314  1.00 16.70 ?  156  PHE   B CE1  1 
ATOM   6491 C  CE2  . PHE   B 1 156 ? 53.138 -33.992 -5.503  1.00 15.68 ?  156  PHE   B CE2  1 
ATOM   6492 C  CZ   . PHE   B 1 156 ? 53.999 -33.454 -6.437  1.00 16.23 ?  156  PHE   B CZ   1 
ATOM   6493 H  H    . PHE   B 1 156 ? 47.544 -31.848 -6.498  1.00 14.81 ?  156  PHE   B H    1 
ATOM   6494 H  HA   . PHE   B 1 156 ? 49.481 -32.044 -8.266  1.00 15.95 ?  156  PHE   B HA   1 
ATOM   6495 H  HB2  . PHE   B 1 156 ? 49.946 -31.186 -6.189  1.00 15.95 ?  156  PHE   B HB2  1 
ATOM   6496 H  HB3  . PHE   B 1 156 ? 49.527 -32.551 -5.495  1.00 15.95 ?  156  PHE   B HB3  1 
ATOM   6497 H  HD1  . PHE   B 1 156 ? 51.936 -31.429 -7.858  1.00 18.86 ?  156  PHE   B HD1  1 
ATOM   6498 H  HD2  . PHE   B 1 156 ? 51.237 -33.941 -4.828  1.00 17.23 ?  156  PHE   B HD2  1 
ATOM   6499 H  HE1  . PHE   B 1 156 ? 54.133 -32.129 -7.943  1.00 20.05 ?  156  PHE   B HE1  1 
ATOM   6500 H  HE2  . PHE   B 1 156 ? 53.439 -34.645 -4.910  1.00 18.81 ?  156  PHE   B HE2  1 
ATOM   6501 H  HZ   . PHE   B 1 156 ? 54.883 -33.738 -6.469  1.00 19.48 ?  156  PHE   B HZ   1 
ATOM   6502 N  N    . ASP   B 1 157 ? 48.544 -34.842 -7.009  1.00 14.69 ?  157  ASP   B N    1 
ATOM   6503 C  CA   . ASP   B 1 157 ? 48.695 -36.288 -7.116  1.00 16.06 ?  157  ASP   B CA   1 
ATOM   6504 C  C    . ASP   B 1 157 ? 47.775 -36.832 -8.206  1.00 16.16 ?  157  ASP   B C    1 
ATOM   6505 O  O    . ASP   B 1 157 ? 46.550 -36.705 -8.109  1.00 15.60 ?  157  ASP   B O    1 
ATOM   6506 C  CB   . ASP   B 1 157 ? 48.354 -36.912 -5.768  1.00 17.43 ?  157  ASP   B CB   1 
ATOM   6507 C  CG   . ASP   B 1 157 ? 48.482 -38.425 -5.765  1.00 19.26 ?  157  ASP   B CG   1 
ATOM   6508 O  OD1  . ASP   B 1 157 ? 48.804 -39.031 -6.815  1.00 19.75 ?  157  ASP   B OD1  1 
ATOM   6509 O  OD2  . ASP   B 1 157 ? 48.269 -39.019 -4.687  1.00 21.41 -1 157  ASP   B OD2  1 
ATOM   6510 H  H    . ASP   B 1 157 ? 47.996 -34.590 -6.404  1.00 17.63 ?  157  ASP   B H    1 
ATOM   6511 H  HA   . ASP   B 1 157 ? 49.615 -36.508 -7.344  1.00 19.28 ?  157  ASP   B HA   1 
ATOM   6512 H  HB2  . ASP   B 1 157 ? 48.949 -36.545 -5.098  1.00 20.91 ?  157  ASP   B HB2  1 
ATOM   6513 H  HB3  . ASP   B 1 157 ? 47.437 -36.691 -5.551  1.00 20.91 ?  157  ASP   B HB3  1 
ATOM   6514 N  N    A LYS   B 1 158 ? 48.370 -37.451 -9.232  0.50 16.83 ?  158  LYS   B N    1 
ATOM   6515 N  N    B LYS   B 1 158 ? 48.369 -37.453 -9.231  0.50 16.86 ?  158  LYS   B N    1 
ATOM   6516 C  CA   A LYS   B 1 158 ? 47.596 -38.049 -10.320 0.50 17.86 ?  158  LYS   B CA   1 
ATOM   6517 C  CA   B LYS   B 1 158 ? 47.595 -38.047 -10.321 0.50 17.92 ?  158  LYS   B CA   1 
ATOM   6518 C  C    A LYS   B 1 158 ? 46.535 -39.013 -9.796  0.50 17.78 ?  158  LYS   B C    1 
ATOM   6519 C  C    B LYS   B 1 158 ? 46.537 -39.017 -9.800  0.50 17.82 ?  158  LYS   B C    1 
ATOM   6520 O  O    A LYS   B 1 158 ? 45.430 -39.092 -10.345 0.50 17.66 ?  158  LYS   B O    1 
ATOM   6521 O  O    B LYS   B 1 158 ? 45.434 -39.103 -10.354 0.50 17.73 ?  158  LYS   B O    1 
ATOM   6522 C  CB   A LYS   B 1 158 ? 48.550 -38.762 -11.287 0.50 19.20 ?  158  LYS   B CB   1 
ATOM   6523 C  CB   B LYS   B 1 158 ? 48.549 -38.751 -11.295 0.50 19.25 ?  158  LYS   B CB   1 
ATOM   6524 C  CG   A LYS   B 1 158 ? 47.882 -39.691 -12.291 0.50 20.77 ?  158  LYS   B CG   1 
ATOM   6525 C  CG   B LYS   B 1 158 ? 47.879 -39.637 -12.337 0.50 20.78 ?  158  LYS   B CG   1 
ATOM   6526 C  CD   A LYS   B 1 158 ? 46.986 -38.938 -13.252 0.50 22.21 ?  158  LYS   B CD   1 
ATOM   6527 C  CD   B LYS   B 1 158 ? 47.011 -38.840 -13.289 0.50 22.25 ?  158  LYS   B CD   1 
ATOM   6528 C  CE   A LYS   B 1 158 ? 46.424 -39.866 -14.314 0.50 23.27 ?  158  LYS   B CE   1 
ATOM   6529 C  CE   B LYS   B 1 158 ? 46.449 -39.729 -14.384 0.50 23.31 ?  158  LYS   B CE   1 
ATOM   6530 N  NZ   A LYS   B 1 158 ? 45.347 -39.215 -15.109 0.50 23.34 ?  158  LYS   B NZ   1 
ATOM   6531 N  NZ   B LYS   B 1 158 ? 45.399 -39.037 -15.183 0.50 23.56 ?  158  LYS   B NZ   1 
ATOM   6532 H  H    A LYS   B 1 158 ? 49.224 -37.540 -9.320  0.50 20.20 ?  158  LYS   B H    1 
ATOM   6533 H  H    B LYS   B 1 158 ? 49.223 -37.545 -9.317  0.50 20.24 ?  158  LYS   B H    1 
ATOM   6534 H  HA   A LYS   B 1 158 ? 47.149 -37.346 -10.815 0.50 21.44 ?  158  LYS   B HA   1 
ATOM   6535 H  HA   B LYS   B 1 158 ? 47.145 -37.342 -10.811 0.50 21.50 ?  158  LYS   B HA   1 
ATOM   6536 H  HB2  A LYS   B 1 158 ? 49.038 -38.092 -11.798 0.50 23.04 ?  158  LYS   B HB2  1 
ATOM   6537 H  HB2  B LYS   B 1 158 ? 49.057 -38.075 -11.778 0.50 23.09 ?  158  LYS   B HB2  1 
ATOM   6538 H  HB3  A LYS   B 1 158 ? 49.178 -39.294 -10.774 0.50 23.04 ?  158  LYS   B HB3  1 
ATOM   6539 H  HB3  B LYS   B 1 158 ? 49.159 -39.308 -10.789 0.50 23.09 ?  158  LYS   B HB3  1 
ATOM   6540 H  HG2  A LYS   B 1 158 ? 48.569 -40.133 -12.813 0.50 24.93 ?  158  LYS   B HG2  1 
ATOM   6541 H  HG2  B LYS   B 1 158 ? 48.566 -40.079 -12.862 0.50 24.94 ?  158  LYS   B HG2  1 
ATOM   6542 H  HG3  A LYS   B 1 158 ? 47.349 -40.356 -11.827 0.50 24.93 ?  158  LYS   B HG3  1 
ATOM   6543 H  HG3  B LYS   B 1 158 ? 47.325 -40.304 -11.900 0.50 24.94 ?  158  LYS   B HG3  1 
ATOM   6544 H  HD2  A LYS   B 1 158 ? 46.245 -38.547 -12.763 0.50 26.66 ?  158  LYS   B HD2  1 
ATOM   6545 H  HD2  B LYS   B 1 158 ? 46.269 -38.451 -12.801 0.50 26.70 ?  158  LYS   B HD2  1 
ATOM   6546 H  HD3  A LYS   B 1 158 ? 47.501 -38.244 -13.695 0.50 26.66 ?  158  LYS   B HD3  1 
ATOM   6547 H  HD3  B LYS   B 1 158 ? 47.544 -38.144 -13.705 0.50 26.70 ?  158  LYS   B HD3  1 
ATOM   6548 H  HE2  A LYS   B 1 158 ? 47.133 -40.123 -14.922 0.50 27.93 ?  158  LYS   B HE2  1 
ATOM   6549 H  HE2  B LYS   B 1 158 ? 47.164 -39.988 -14.986 0.50 27.97 ?  158  LYS   B HE2  1 
ATOM   6550 H  HE3  A LYS   B 1 158 ? 46.050 -40.653 -13.887 0.50 27.93 ?  158  LYS   B HE3  1 
ATOM   6551 H  HE3  B LYS   B 1 158 ? 46.051 -40.519 -13.982 0.50 27.97 ?  158  LYS   B HE3  1 
ATOM   6552 H  HZ1  A LYS   B 1 158 ? 45.034 -39.778 -15.722 0.50 28.01 ?  158  LYS   B HZ1  1 
ATOM   6553 H  HZ1  B LYS   B 1 158 ? 45.087 -39.581 -15.815 0.50 28.27 ?  158  LYS   B HZ1  1 
ATOM   6554 H  HZ2  A LYS   B 1 158 ? 44.678 -38.970 -14.574 0.50 28.01 ?  158  LYS   B HZ2  1 
ATOM   6555 H  HZ2  B LYS   B 1 158 ? 44.725 -38.794 -14.654 0.50 28.27 ?  158  LYS   B HZ2  1 
ATOM   6556 H  HZ3  A LYS   B 1 158 ? 45.667 -38.491 -15.518 0.50 28.01 ?  158  LYS   B HZ3  1 
ATOM   6557 H  HZ3  B LYS   B 1 158 ? 45.739 -38.311 -15.568 0.50 28.27 ?  158  LYS   B HZ3  1 
ATOM   6558 N  N    . ASN   B 1 159 ? 46.859 -39.775 -8.749  1.00 18.09 ?  159  ASN   B N    1 
ATOM   6559 C  CA   . ASN   B 1 159 ? 45.901 -40.754 -8.238  1.00 19.05 ?  159  ASN   B CA   1 
ATOM   6560 C  C    . ASN   B 1 159 ? 44.711 -40.085 -7.554  1.00 18.13 ?  159  ASN   B C    1 
ATOM   6561 O  O    . ASN   B 1 159 ? 43.581 -40.580 -7.658  1.00 18.19 ?  159  ASN   B O    1 
ATOM   6562 C  CB   . ASN   B 1 159 ? 46.602 -41.741 -7.310  1.00 20.89 ?  159  ASN   B CB   1 
ATOM   6563 C  CG   . ASN   B 1 159 ? 47.643 -42.566 -8.032  1.00 22.82 ?  159  ASN   B CG   1 
ATOM   6564 O  OD1  . ASN   B 1 159 ? 47.397 -43.081 -9.128  1.00 23.83 ?  159  ASN   B OD1  1 
ATOM   6565 N  ND2  . ASN   B 1 159 ? 48.817 -42.704 -7.421  1.00 23.57 ?  159  ASN   B ND2  1 
ATOM   6566 H  H    A ASN   B 1 159 ? 47.608 -39.742 -8.331  0.50 21.71 ?  159  ASN   B H    1 
ATOM   6567 H  H    B ASN   B 1 159 ? 47.606 -39.740 -8.329  0.50 21.71 ?  159  ASN   B H    1 
ATOM   6568 H  HA   . ASN   B 1 159 ? 45.556 -41.257 -8.992  1.00 22.86 ?  159  ASN   B HA   1 
ATOM   6569 H  HB2  . ASN   B 1 159 ? 47.044 -41.256 -6.600  1.00 25.07 ?  159  ASN   B HB2  1 
ATOM   6570 H  HB3  . ASN   B 1 159 ? 45.946 -42.353 -6.946  1.00 25.07 ?  159  ASN   B HB3  1 
ATOM   6571 H  HD21 . ASN   B 1 159 ? 49.450 -43.160 -7.793  1.00 28.28 ?  159  ASN   B HD21 1 
ATOM   6572 H  HD22 . ASN   B 1 159 ? 48.951 -42.342 -6.652  1.00 28.28 ?  159  ASN   B HD22 1 
ATOM   6573 N  N    . LEU   B 1 160 ? 44.926 -38.953 -6.877  1.00 16.90 ?  160  LEU   B N    1 
ATOM   6574 C  CA   . LEU   B 1 160 ? 43.791 -38.224 -6.325  1.00 15.90 ?  160  LEU   B CA   1 
ATOM   6575 C  C    . LEU   B 1 160 ? 42.996 -37.553 -7.434  1.00 15.14 ?  160  LEU   B C    1 
ATOM   6576 O  O    . LEU   B 1 160 ? 41.760 -37.564 -7.415  1.00 14.48 ?  160  LEU   B O    1 
ATOM   6577 C  CB   . LEU   B 1 160 ? 44.253 -37.194 -5.296  1.00 15.35 ?  160  LEU   B CB   1 
ATOM   6578 C  CG   . LEU   B 1 160 ? 43.122 -36.309 -4.751  1.00 15.21 ?  160  LEU   B CG   1 
ATOM   6579 C  CD1  . LEU   B 1 160 ? 42.009 -37.154 -4.126  1.00 16.14 ?  160  LEU   B CD1  1 
ATOM   6580 C  CD2  . LEU   B 1 160 ? 43.655 -35.303 -3.743  1.00 15.53 ?  160  LEU   B CD2  1 
ATOM   6581 H  H    . LEU   B 1 160 ? 45.699 -38.593 -6.736  1.00 20.28 ?  160  LEU   B H    1 
ATOM   6582 H  HA   . LEU   B 1 160 ? 43.209 -38.854 -5.880  1.00 19.07 ?  160  LEU   B HA   1 
ATOM   6583 H  HB2  . LEU   B 1 160 ? 44.658 -37.662 -4.548  1.00 18.42 ?  160  LEU   B HB2  1 
ATOM   6584 H  HB3  . LEU   B 1 160 ? 44.916 -36.613 -5.711  1.00 18.42 ?  160  LEU   B HB3  1 
ATOM   6585 H  HG   . LEU   B 1 160 ? 42.736 -35.810 -5.486  1.00 18.25 ?  160  LEU   B HG   1 
ATOM   6586 H  HD11 . LEU   B 1 160 ? 41.375 -36.567 -3.694  1.00 19.37 ?  160  LEU   B HD11 1 
ATOM   6587 H  HD12 . LEU   B 1 160 ? 41.567 -37.667 -4.822  1.00 19.37 ?  160  LEU   B HD12 1 
ATOM   6588 H  HD13 . LEU   B 1 160 ? 42.401 -37.759 -3.472  1.00 19.37 ?  160  LEU   B HD13 1 
ATOM   6589 H  HD21 . LEU   B 1 160 ? 42.918 -34.747 -3.441  1.00 18.63 ?  160  LEU   B HD21 1 
ATOM   6590 H  HD22 . LEU   B 1 160 ? 44.040 -35.779 -2.994  1.00 18.63 ?  160  LEU   B HD22 1 
ATOM   6591 H  HD23 . LEU   B 1 160 ? 44.328 -34.753 -4.173  1.00 18.63 ?  160  LEU   B HD23 1 
ATOM   6592 N  N    . TYR   B 1 161 ? 43.691 -36.980 -8.419  1.00 15.28 ?  161  TYR   B N    1 
ATOM   6593 C  CA   . TYR   B 1 161 ? 43.017 -36.411 -9.580  1.00 15.05 ?  161  TYR   B CA   1 
ATOM   6594 C  C    . TYR   B 1 161 ? 42.074 -37.429 -10.207 1.00 14.93 ?  161  TYR   B C    1 
ATOM   6595 O  O    . TYR   B 1 161 ? 40.904 -37.132 -10.472 1.00 14.76 ?  161  TYR   B O    1 
ATOM   6596 C  CB   . TYR   B 1 161 ? 44.058 -35.929 -10.595 1.00 15.67 ?  161  TYR   B CB   1 
ATOM   6597 C  CG   . TYR   B 1 161 ? 43.478 -35.464 -11.907 1.00 16.03 ?  161  TYR   B CG   1 
ATOM   6598 C  CD1  . TYR   B 1 161 ? 43.077 -34.148 -12.071 1.00 15.87 ?  161  TYR   B CD1  1 
ATOM   6599 C  CD2  . TYR   B 1 161 ? 43.313 -36.337 -12.976 1.00 16.87 ?  161  TYR   B CD2  1 
ATOM   6600 C  CE1  . TYR   B 1 161 ? 42.542 -33.709 -13.255 1.00 16.91 ?  161  TYR   B CE1  1 
ATOM   6601 C  CE2  . TYR   B 1 161 ? 42.771 -35.905 -14.166 1.00 17.89 ?  161  TYR   B CE2  1 
ATOM   6602 C  CZ   . TYR   B 1 161 ? 42.391 -34.588 -14.302 1.00 17.67 ?  161  TYR   B CZ   1 
ATOM   6603 O  OH   . TYR   B 1 161 ? 41.850 -34.145 -15.483 1.00 19.53 ?  161  TYR   B OH   1 
ATOM   6604 H  H    . TYR   B 1 161 ? 44.546 -36.917 -8.444  1.00 18.34 ?  161  TYR   B H    1 
ATOM   6605 H  HA   . TYR   B 1 161 ? 42.489 -35.646 -9.301  1.00 18.06 ?  161  TYR   B HA   1 
ATOM   6606 H  HB2  . TYR   B 1 161 ? 44.546 -35.182 -10.210 1.00 18.81 ?  161  TYR   B HB2  1 
ATOM   6607 H  HB3  . TYR   B 1 161 ? 44.669 -36.654 -10.787 1.00 18.81 ?  161  TYR   B HB3  1 
ATOM   6608 H  HD1  . TYR   B 1 161 ? 43.180 -33.540 -11.370 1.00 19.04 ?  161  TYR   B HD1  1 
ATOM   6609 H  HD2  . TYR   B 1 161 ? 43.567 -37.224 -12.889 1.00 20.24 ?  161  TYR   B HD2  1 
ATOM   6610 H  HE1  . TYR   B 1 161 ? 42.284 -32.815 -13.345 1.00 20.29 ?  161  TYR   B HE1  1 
ATOM   6611 H  HE2  . TYR   B 1 161 ? 42.664 -36.493 -14.876 1.00 21.46 ?  161  TYR   B HE2  1 
ATOM   6612 H  HH   . TYR   B 1 161 ? 41.814 -34.784 -16.031 1.00 23.43 ?  161  TYR   B HH   1 
ATOM   6613 N  N    . ASP   B 1 162 ? 42.569 -38.649 -10.439 1.00 15.42 ?  162  ASP   B N    1 
ATOM   6614 C  CA   . ASP   B 1 162 ? 41.740 -39.683 -11.049 1.00 15.82 ?  162  ASP   B CA   1 
ATOM   6615 C  C    . ASP   B 1 162 ? 40.538 -40.021 -10.173 1.00 15.32 ?  162  ASP   B C    1 
ATOM   6616 O  O    . ASP   B 1 162 ? 39.434 -40.241 -10.683 1.00 15.83 ?  162  ASP   B O    1 
ATOM   6617 C  CB   . ASP   B 1 162 ? 42.572 -40.944 -11.306 1.00 17.31 ?  162  ASP   B CB   1 
ATOM   6618 C  CG   . ASP   B 1 162 ? 43.575 -40.784 -12.439 1.00 18.39 ?  162  ASP   B CG   1 
ATOM   6619 O  OD1  . ASP   B 1 162 ? 43.443 -39.843 -13.244 1.00 18.62 ?  162  ASP   B OD1  1 
ATOM   6620 O  OD2  . ASP   B 1 162 ? 44.482 -41.642 -12.537 1.00 20.09 -1 162  ASP   B OD2  1 
ATOM   6621 H  H    . ASP   B 1 162 ? 43.374 -38.892 -10.262 1.00 18.50 ?  162  ASP   B H    1 
ATOM   6622 H  HA   . ASP   B 1 162 ? 41.407 -39.362 -11.899 1.00 18.98 ?  162  ASP   B HA   1 
ATOM   6623 H  HB2  . ASP   B 1 162 ? 43.074 -41.160 -10.507 1.00 20.78 ?  162  ASP   B HB2  1 
ATOM   6624 H  HB3  . ASP   B 1 162 ? 41.978 -41.670 -11.539 1.00 20.78 ?  162  ASP   B HB3  1 
ATOM   6625 N  N    . LYS   B 1 163 ? 40.736 -40.098 -8.855  1.00 14.82 ?  163  LYS   B N    1 
ATOM   6626 C  CA   . LYS   B 1 163 ? 39.615 -40.380 -7.963  1.00 15.51 ?  163  LYS   B CA   1 
ATOM   6627 C  C    . LYS   B 1 163 ? 38.565 -39.277 -8.025  1.00 14.36 ?  163  LYS   B C    1 
ATOM   6628 O  O    . LYS   B 1 163 ? 37.357 -39.549 -8.038  1.00 15.32 ?  163  LYS   B O    1 
ATOM   6629 C  CB   . LYS   B 1 163 ? 40.109 -40.562 -6.529  1.00 18.69 ?  163  LYS   B CB   1 
ATOM   6630 C  CG   . LYS   B 1 163 ? 39.012 -41.018 -5.590  1.00 24.84 ?  163  LYS   B CG   1 
ATOM   6631 C  CD   . LYS   B 1 163 ? 39.519 -41.322 -4.195  1.00 30.46 ?  163  LYS   B CD   1 
ATOM   6632 C  CE   . LYS   B 1 163 ? 38.425 -41.990 -3.372  1.00 34.16 ?  163  LYS   B CE   1 
ATOM   6633 N  NZ   . LYS   B 1 163 ? 38.388 -41.501 -1.967  1.00 36.99 ?  163  LYS   B NZ   1 
ATOM   6634 H  H    . LYS   B 1 163 ? 41.495 -39.988 -8.462  1.00 17.78 ?  163  LYS   B H    1 
ATOM   6635 H  HA   . LYS   B 1 163 ? 39.196 -41.205 -8.241  1.00 18.62 ?  163  LYS   B HA   1 
ATOM   6636 H  HB2  . LYS   B 1 163 ? 40.810 -41.233 -6.519  1.00 22.43 ?  163  LYS   B HB2  1 
ATOM   6637 H  HB3  . LYS   B 1 163 ? 40.453 -39.718 -6.200  1.00 22.43 ?  163  LYS   B HB3  1 
ATOM   6638 H  HG2  . LYS   B 1 163 ? 38.344 -40.319 -5.518  1.00 29.81 ?  163  LYS   B HG2  1 
ATOM   6639 H  HG3  . LYS   B 1 163 ? 38.607 -41.827 -5.945  1.00 29.81 ?  163  LYS   B HG3  1 
ATOM   6640 H  HD2  . LYS   B 1 163 ? 40.276 -41.927 -4.250  1.00 36.55 ?  163  LYS   B HD2  1 
ATOM   6641 H  HD3  . LYS   B 1 163 ? 39.774 -40.497 -3.756  1.00 36.55 ?  163  LYS   B HD3  1 
ATOM   6642 H  HE2  . LYS   B 1 163 ? 37.563 -41.807 -3.779  1.00 40.99 ?  163  LYS   B HE2  1 
ATOM   6643 H  HE3  . LYS   B 1 163 ? 38.584 -42.948 -3.352  1.00 40.99 ?  163  LYS   B HE3  1 
ATOM   6644 H  HZ1  . LYS   B 1 163 ? 37.737 -41.912 -1.519  1.00 44.39 ?  163  LYS   B HZ1  1 
ATOM   6645 H  HZ2  . LYS   B 1 163 ? 39.164 -41.667 -1.567  1.00 44.39 ?  163  LYS   B HZ2  1 
ATOM   6646 H  HZ3  . LYS   B 1 163 ? 38.237 -40.624 -1.955  1.00 44.39 ?  163  LYS   B HZ3  1 
ATOM   6647 N  N    . LEU   B 1 164 ? 39.014 -38.022 -8.065  1.00 13.34 ?  164  LEU   B N    1 
ATOM   6648 C  CA   . LEU   B 1 164 ? 38.103 -36.883 -8.119  1.00 12.69 ?  164  LEU   B CA   1 
ATOM   6649 C  C    . LEU   B 1 164 ? 37.319 -36.858 -9.427  1.00 12.78 ?  164  LEU   B C    1 
ATOM   6650 O  O    . LEU   B 1 164 ? 36.097 -36.664 -9.427  1.00 13.93 ?  164  LEU   B O    1 
ATOM   6651 C  CB   . LEU   B 1 164 ? 38.899 -35.587 -7.953  1.00 12.34 ?  164  LEU   B CB   1 
ATOM   6652 C  CG   . LEU   B 1 164 ? 39.438 -35.313 -6.554  1.00 13.18 ?  164  LEU   B CG   1 
ATOM   6653 C  CD1  . LEU   B 1 164 ? 40.535 -34.258 -6.615  1.00 13.27 ?  164  LEU   B CD1  1 
ATOM   6654 C  CD2  . LEU   B 1 164 ? 38.331 -34.872 -5.618  1.00 14.99 ?  164  LEU   B CD2  1 
ATOM   6655 H  H    . LEU   B 1 164 ? 39.850 -37.800 -8.062  1.00 16.00 ?  164  LEU   B H    1 
ATOM   6656 H  HA   . LEU   B 1 164 ? 37.474 -36.944 -7.394  1.00 15.23 ?  164  LEU   B HA   1 
ATOM   6657 H  HB2  . LEU   B 1 164 ? 39.663 -35.613 -8.557  1.00 14.81 ?  164  LEU   B HB2  1 
ATOM   6658 H  HB3  . LEU   B 1 164 ? 38.329 -34.841 -8.196  1.00 14.81 ?  164  LEU   B HB3  1 
ATOM   6659 H  HG   . LEU   B 1 164 ? 39.829 -36.124 -6.203  1.00 15.82 ?  164  LEU   B HG   1 
ATOM   6660 H  HD11 . LEU   B 1 164 ? 40.864 -34.085 -5.717  1.00 15.93 ?  164  LEU   B HD11 1 
ATOM   6661 H  HD12 . LEU   B 1 164 ? 41.266 -34.586 -7.170  1.00 15.93 ?  164  LEU   B HD12 1 
ATOM   6662 H  HD13 . LEU   B 1 164 ? 40.179 -33.440 -6.997  1.00 15.93 ?  164  LEU   B HD13 1 
ATOM   6663 H  HD21 . LEU   B 1 164 ? 38.711 -34.668 -4.750  1.00 17.99 ?  164  LEU   B HD21 1 
ATOM   6664 H  HD22 . LEU   B 1 164 ? 37.898 -34.083 -5.984  1.00 17.99 ?  164  LEU   B HD22 1 
ATOM   6665 H  HD23 . LEU   B 1 164 ? 37.685 -35.592 -5.535  1.00 17.99 ?  164  LEU   B HD23 1 
ATOM   6666 N  N    . VAL   B 1 165 ? 38.010 -37.022 -10.557 1.00 14.20 ?  165  VAL   B N    1 
ATOM   6667 C  CA   . VAL   B 1 165 ? 37.352 -36.955 -11.858 1.00 15.53 ?  165  VAL   B CA   1 
ATOM   6668 C  C    . VAL   B 1 165 ? 36.432 -38.152 -12.046 1.00 17.31 ?  165  VAL   B C    1 
ATOM   6669 O  O    . VAL   B 1 165 ? 35.275 -38.015 -12.464 1.00 18.49 ?  165  VAL   B O    1 
ATOM   6670 C  CB   . VAL   B 1 165 ? 38.398 -36.873 -12.984 1.00 16.65 ?  165  VAL   B CB   1 
ATOM   6671 C  CG1  . VAL   B 1 165 ? 37.734 -36.982 -14.339 1.00 17.92 ?  165  VAL   B CG1  1 
ATOM   6672 C  CG2  . VAL   B 1 165 ? 39.187 -35.589 -12.879 1.00 16.60 ?  165  VAL   B CG2  1 
ATOM   6673 H  H    . VAL   B 1 165 ? 38.859 -37.160 -10.598 1.00 17.04 ?  165  VAL   B H    1 
ATOM   6674 H  HA   . VAL   B 1 165 ? 36.808 -36.155 -11.900 1.00 18.63 ?  165  VAL   B HA   1 
ATOM   6675 H  HB   . VAL   B 1 165 ? 39.024 -37.606 -12.893 1.00 19.98 ?  165  VAL   B HB   1 
ATOM   6676 H  HG11 . VAL   B 1 165 ? 38.346 -36.668 -15.019 1.00 21.51 ?  165  VAL   B HG11 1 
ATOM   6677 H  HG12 . VAL   B 1 165 ? 37.518 -37.916 -14.503 1.00 21.51 ?  165  VAL   B HG12 1 
ATOM   6678 H  HG13 . VAL   B 1 165 ? 36.926 -36.451 -14.341 1.00 21.51 ?  165  VAL   B HG13 1 
ATOM   6679 H  HG21 . VAL   B 1 165 ? 39.820 -35.542 -13.613 1.00 19.91 ?  165  VAL   B HG21 1 
ATOM   6680 H  HG22 . VAL   B 1 165 ? 38.574 -34.835 -12.926 1.00 19.91 ?  165  VAL   B HG22 1 
ATOM   6681 H  HG23 . VAL   B 1 165 ? 39.660 -35.573 -12.032 1.00 19.91 ?  165  VAL   B HG23 1 
ATOM   6682 N  N    . SER   B 1 166 ? 36.944 -39.352 -11.752 1.00 18.36 ?  166  SER   B N    1 
ATOM   6683 C  CA   . SER   B 1 166 ? 36.191 -40.565 -12.039 1.00 19.74 ?  166  SER   B CA   1 
ATOM   6684 C  C    . SER   B 1 166 ? 34.934 -40.661 -11.188 1.00 20.07 ?  166  SER   B C    1 
ATOM   6685 O  O    . SER   B 1 166 ? 33.965 -41.290 -11.612 1.00 21.38 ?  166  SER   B O    1 
ATOM   6686 C  CB   . SER   B 1 166 ? 37.062 -41.817 -11.873 1.00 20.98 ?  166  SER   B CB   1 
ATOM   6687 O  OG   . SER   B 1 166 ? 37.415 -42.044 -10.520 1.00 21.14 ?  166  SER   B OG   1 
ATOM   6688 H  H    . SER   B 1 166 ? 37.723 -39.486 -11.403 1.00 22.03 ?  166  SER   B H    1 
ATOM   6689 H  HA   . SER   B 1 166 ? 35.918 -40.539 -12.969 1.00 23.69 ?  166  SER   B HA   1 
ATOM   6690 H  HB2  . SER   B 1 166 ? 36.568 -42.587 -12.200 1.00 25.18 ?  166  SER   B HB2  1 
ATOM   6691 H  HB3  . SER   B 1 166 ? 37.876 -41.709 -12.393 1.00 25.18 ?  166  SER   B HB3  1 
ATOM   6692 H  HG   . SER   B 1 166 ? 37.850 -41.392 -10.226 1.00 25.37 ?  166  SER   B HG   1 
ATOM   6693 N  N    . SER   B 1 167 ? 34.917 -40.050 -10.005 1.00 18.73 ?  167  SER   B N    1 
ATOM   6694 C  CA   . SER   B 1 167 ? 33.758 -40.111 -9.123  1.00 18.20 ?  167  SER   B CA   1 
ATOM   6695 C  C    . SER   B 1 167 ? 32.843 -38.890 -9.220  1.00 17.67 ?  167  SER   B C    1 
ATOM   6696 O  O    . SER   B 1 167 ? 31.767 -38.894 -8.611  1.00 18.02 ?  167  SER   B O    1 
ATOM   6697 C  CB   . SER   B 1 167 ? 34.197 -40.296 -7.665  1.00 17.86 ?  167  SER   B CB   1 
ATOM   6698 O  OG   . SER   B 1 167 ? 34.873 -39.143 -7.187  1.00 17.55 ?  167  SER   B OG   1 
ATOM   6699 H  H    . SER   B 1 167 ? 35.574 -39.603 -9.686  1.00 22.48 ?  167  SER   B H    1 
ATOM   6700 H  HA   . SER   B 1 167 ? 33.231 -40.891 -9.369  1.00 21.84 ?  167  SER   B HA   1 
ATOM   6701 H  HB2  . SER   B 1 167 ? 33.409 -40.458 -7.121  1.00 21.44 ?  167  SER   B HB2  1 
ATOM   6702 H  HB3  . SER   B 1 167 ? 34.792 -41.066 -7.613  1.00 21.44 ?  167  SER   B HB3  1 
ATOM   6703 H  HG   . SER   B 1 167 ? 35.554 -39.008 -7.658  1.00 21.06 ?  167  SER   B HG   1 
ATOM   6704 N  N    . PHE   B 1 168 ? 33.225 -37.852 -9.965  1.00 17.13 ?  168  PHE   B N    1 
ATOM   6705 C  CA   . PHE   B 1 168 ? 32.387 -36.652 -10.020 1.00 16.44 ?  168  PHE   B CA   1 
ATOM   6706 C  C    . PHE   B 1 168 ? 31.069 -36.917 -10.744 1.00 14.21 ?  168  PHE   B C    1 
ATOM   6707 O  O    . PHE   B 1 168 ? 30.024 -36.326 -10.404 1.00 14.88 ?  168  PHE   B O    1 
ATOM   6708 C  CB   . PHE   B 1 168 ? 33.146 -35.515 -10.700 1.00 17.29 ?  168  PHE   B CB   1 
ATOM   6709 C  CG   . PHE   B 1 168 ? 32.346 -34.264 -10.819 1.00 17.44 ?  168  PHE   B CG   1 
ATOM   6710 C  CD1  . PHE   B 1 168 ? 32.029 -33.528 -9.687  1.00 18.65 ?  168  PHE   B CD1  1 
ATOM   6711 C  CD2  . PHE   B 1 168 ? 31.883 -33.839 -12.045 1.00 17.10 ?  168  PHE   B CD2  1 
ATOM   6712 C  CE1  . PHE   B 1 168 ? 31.272 -32.380 -9.778  1.00 19.14 ?  168  PHE   B CE1  1 
ATOM   6713 C  CE2  . PHE   B 1 168 ? 31.136 -32.676 -12.151 1.00 18.05 ?  168  PHE   B CE2  1 
ATOM   6714 C  CZ   . PHE   B 1 168 ? 30.821 -31.946 -11.015 1.00 18.57 ?  168  PHE   B CZ   1 
ATOM   6715 H  H    . PHE   B 1 168 ? 33.954 -37.813 -10.425 1.00 20.55 ?  168  PHE   B H    1 
ATOM   6716 H  HA   . PHE   B 1 168 ? 32.184 -36.375 -9.116  1.00 19.73 ?  168  PHE   B HA   1 
ATOM   6717 H  HB2  . PHE   B 1 168 ? 33.941 -35.309 -10.181 1.00 20.75 ?  168  PHE   B HB2  1 
ATOM   6718 H  HB3  . PHE   B 1 168 ? 33.399 -35.790 -11.594 1.00 20.75 ?  168  PHE   B HB3  1 
ATOM   6719 H  HD1  . PHE   B 1 168 ? 32.326 -33.819 -8.855  1.00 22.38 ?  168  PHE   B HD1  1 
ATOM   6720 H  HD2  . PHE   B 1 168 ? 32.093 -34.321 -12.809 1.00 20.51 ?  168  PHE   B HD2  1 
ATOM   6721 H  HE1  . PHE   B 1 168 ? 31.066 -31.892 -9.013  1.00 22.96 ?  168  PHE   B HE1  1 
ATOM   6722 H  HE2  . PHE   B 1 168 ? 30.829 -32.392 -12.986 1.00 21.66 ?  168  PHE   B HE2  1 
ATOM   6723 H  HZ   . PHE   B 1 168 ? 30.311 -31.169 -11.086 1.00 22.29 ?  168  PHE   B HZ   1 
ATOM   6724 N  N    . LEU   B 1 169 ? 31.102 -37.803 -11.735 1.00 14.51 ?  169  LEU   B N    1 
ATOM   6725 C  CA   . LEU   B 1 169 ? 29.924 -38.115 -12.532 1.00 16.96 ?  169  LEU   B CA   1 
ATOM   6726 C  C    . LEU   B 1 169 ? 29.911 -39.554 -13.021 1.00 19.93 ?  169  LEU   B C    1 
ATOM   6727 O  O    . LEU   B 1 169 ? 29.000 -39.972 -13.736 1.00 22.42 ?  169  LEU   B O    1 
ATOM   6728 C  CB   . LEU   B 1 169 ? 29.857 -37.190 -13.741 1.00 18.81 ?  169  LEU   B CB   1 
ATOM   6729 C  CG   . LEU   B 1 169 ? 28.630 -36.285 -13.823 1.00 21.84 ?  169  LEU   B CG   1 
ATOM   6730 C  CD1  . LEU   B 1 169 ? 28.592 -35.585 -15.168 1.00 22.83 ?  169  LEU   B CD1  1 
ATOM   6731 C  CD2  . LEU   B 1 169 ? 27.351 -37.068 -13.584 1.00 22.07 ?  169  LEU   B CD2  1 
ATOM   6732 O  OXT  . LEU   B 1 169 ? 30.817 -40.320 -12.724 1.00 20.72 -1 169  LEU   B OXT  1 
ATOM   6733 H  H    . LEU   B 1 169 ? 31.810 -38.238 -11.974 1.00 17.41 ?  169  LEU   B H    1 
ATOM   6734 H  HA   . LEU   B 1 169 ? 29.141 -37.973 -11.984 1.00 20.35 ?  169  LEU   B HA   1 
ATOM   6735 H  HB2  . LEU   B 1 169 ? 30.639 -36.616 -13.733 1.00 22.57 ?  169  LEU   B HB2  1 
ATOM   6736 H  HB3  . LEU   B 1 169 ? 29.865 -37.734 -14.544 1.00 22.57 ?  169  LEU   B HB3  1 
ATOM   6737 H  HG   . LEU   B 1 169 ? 28.696 -35.603 -13.136 1.00 26.21 ?  169  LEU   B HG   1 
ATOM   6738 H  HD11 . LEU   B 1 169 ? 27.821 -34.997 -15.195 1.00 27.39 ?  169  LEU   B HD11 1 
ATOM   6739 H  HD12 . LEU   B 1 169 ? 29.406 -35.070 -15.278 1.00 27.39 ?  169  LEU   B HD12 1 
ATOM   6740 H  HD13 . LEU   B 1 169 ? 28.525 -36.253 -15.868 1.00 27.39 ?  169  LEU   B HD13 1 
ATOM   6741 H  HD21 . LEU   B 1 169 ? 26.614 -36.613 -14.014 1.00 26.49 ?  169  LEU   B HD21 1 
ATOM   6742 H  HD22 . LEU   B 1 169 ? 27.455 -37.959 -13.960 1.00 26.49 ?  169  LEU   B HD22 1 
ATOM   6743 H  HD23 . LEU   B 1 169 ? 27.195 -37.131 -12.630 1.00 26.49 ?  169  LEU   B HD23 1 
HETATM 6744 S  S    B DMS   C 2 .   ? 12.511 5.376   6.199   0.50 23.81 ?  301  DMS   A S    1 
HETATM 6745 O  O    B DMS   C 2 .   ? 13.796 6.169   6.121   0.50 24.08 ?  301  DMS   A O    1 
HETATM 6746 C  C1   B DMS   C 2 .   ? 11.884 5.250   4.496   0.50 24.69 ?  301  DMS   A C1   1 
HETATM 6747 C  C2   B DMS   C 2 .   ? 11.232 6.424   6.964   0.50 24.66 ?  301  DMS   A C2   1 
HETATM 6748 H  H11  B DMS   C 2 .   ? 11.112 4.562   4.528   0.50 29.63 ?  301  DMS   A H11  1 
HETATM 6749 H  H12  B DMS   C 2 .   ? 12.675 4.935   3.905   0.50 29.63 ?  301  DMS   A H12  1 
HETATM 6750 H  H13  B DMS   C 2 .   ? 11.565 6.207   4.261   0.50 29.63 ?  301  DMS   A H13  1 
HETATM 6751 H  H21  B DMS   C 2 .   ? 11.707 7.051   7.641   0.50 29.59 ?  301  DMS   A H21  1 
HETATM 6752 H  H22  B DMS   C 2 .   ? 10.797 6.938   6.173   0.50 29.59 ?  301  DMS   A H22  1 
HETATM 6753 H  H23  B DMS   C 2 .   ? 10.578 5.777   7.433   0.50 29.59 ?  301  DMS   A H23  1 
HETATM 6754 N  N2   B A1BAR D 3 .   ? 13.791 -0.298  4.817   0.50 12.85 ?  302  A1BAR A N2   1 
HETATM 6755 C  C3   B A1BAR D 3 .   ? 13.761 -1.425  -0.172  0.50 14.05 ?  302  A1BAR A C3   1 
HETATM 6756 C  C6   B A1BAR D 3 .   ? 11.291 -0.329  2.077   0.50 13.99 ?  302  A1BAR A C6   1 
HETATM 6757 C  C9   B A1BAR D 3 .   ? 14.977 2.022   5.434   0.50 10.73 ?  302  A1BAR A C9   1 
HETATM 6758 C  C12  B A1BAR D 3 .   ? 15.731 3.839   4.346   0.50 10.84 ?  302  A1BAR A C12  1 
HETATM 6759 C  C1   B A1BAR D 3 .   ? 16.181 -1.293  0.646   0.50 13.94 ?  302  A1BAR A C1   1 
HETATM 6760 C  C10  B A1BAR D 3 .   ? 14.734 1.779   4.038   0.50 11.15 ?  302  A1BAR A C10  1 
HETATM 6761 C  C11  B A1BAR D 3 .   ? 15.236 2.987   3.360   0.50 11.22 ?  302  A1BAR A C11  1 
HETATM 6762 C  C13  B A1BAR D 3 .   ? 14.561 0.552   1.293   0.50 12.73 ?  302  A1BAR A C13  1 
HETATM 6763 C  C2   B A1BAR D 3 .   ? 14.929 -0.471  0.190   0.50 13.58 ?  302  A1BAR A C2   1 
HETATM 6764 C  C4   B A1BAR D 3 .   ? 12.958 -1.989  1.032   0.50 13.78 ?  302  A1BAR A C4   1 
HETATM 6765 C  C5   B A1BAR D 3 .   ? 12.721 -1.025  2.241   0.50 13.27 ?  302  A1BAR A C5   1 
HETATM 6766 C  C7   B A1BAR D 3 .   ? 14.085 0.512   3.771   0.50 12.18 ?  302  A1BAR A C7   1 
HETATM 6767 C  C8   B A1BAR D 3 .   ? 14.081 0.074   6.104   0.50 12.57 ?  302  A1BAR A C8   1 
HETATM 6768 N  N1   B A1BAR D 3 .   ? 13.757 0.057   2.450   0.50 12.83 ?  302  A1BAR A N1   1 
HETATM 6769 N  N3   B A1BAR D 3 .   ? 14.667 1.209   6.458   0.50 12.23 ?  302  A1BAR A N3   1 
HETATM 6770 N  N4   B A1BAR D 3 .   ? 15.566 3.232   5.546   0.50 10.49 ?  302  A1BAR A N4   1 
HETATM 6771 O  O1   B A1BAR D 3 .   ? 11.085 0.692   3.024   0.50 13.61 ?  302  A1BAR A O1   1 
HETATM 6772 H  H7   B A1BAR D 3 .   ? 14.165 -2.268  -0.773  0.50 16.85 ?  302  A1BAR A H7   1 
HETATM 6773 H  H6   B A1BAR D 3 .   ? 13.057 -0.914  -0.901  0.50 16.85 ?  302  A1BAR A H6   1 
HETATM 6774 H  H11  B A1BAR D 3 .   ? 10.509 -1.112  2.182   0.50 16.79 ?  302  A1BAR A H11  1 
HETATM 6775 H  H10  B A1BAR D 3 .   ? 11.204 0.096   1.054   0.50 16.79 ?  302  A1BAR A H10  1 
HETATM 6776 H  H15  B A1BAR D 3 .   ? 16.226 4.822   4.350   0.50 13.01 ?  302  A1BAR A H15  1 
HETATM 6777 H  H4   B A1BAR D 3 .   ? 16.135 -2.376  0.382   0.50 16.72 ?  302  A1BAR A H4   1 
HETATM 6778 H  H5   B A1BAR D 3 .   ? 16.343 -1.277  1.745   0.50 16.72 ?  302  A1BAR A H5   1 
HETATM 6779 H  H3   B A1BAR D 3 .   ? 17.132 -0.926  0.201   0.50 16.72 ?  302  A1BAR A H3   1 
HETATM 6780 H  H14  B A1BAR D 3 .   ? 15.288 3.278   2.309   0.50 13.47 ?  302  A1BAR A H14  1 
HETATM 6781 H  H17  B A1BAR D 3 .   ? 14.068 1.446   0.813   0.50 15.27 ?  302  A1BAR A H17  1 
HETATM 6782 H  H18  B A1BAR D 3 .   ? 15.541 0.946   1.656   0.50 15.27 ?  302  A1BAR A H18  1 
HETATM 6783 H  H1   B A1BAR D 3 .   ? 15.245 0.104   -0.723  0.50 16.29 ?  302  A1BAR A H1   1 
HETATM 6784 H  H9   B A1BAR D 3 .   ? 13.462 -2.920  1.403   0.50 16.53 ?  302  A1BAR A H9   1 
HETATM 6785 H  H8   B A1BAR D 3 .   ? 11.961 -2.357  0.670   0.50 16.53 ?  302  A1BAR A H8   1 
HETATM 6786 H  H2   B A1BAR D 3 .   ? 12.691 -1.662  3.170   0.50 15.92 ?  302  A1BAR A H2   1 
HETATM 6787 H  H13  B A1BAR D 3 .   ? 13.828 -0.633  6.939   0.50 15.08 ?  302  A1BAR A H13  1 
HETATM 6788 H  H16  B A1BAR D 3 .   ? 15.863 3.667   6.458   0.50 12.59 ?  302  A1BAR A H16  1 
HETATM 6789 H  H12  B A1BAR D 3 .   ? 11.743 1.401   2.905   0.50 16.34 ?  302  A1BAR A H12  1 
HETATM 6790 CL CL   B CL    E 4 .   ? 15.773 2.900   -1.162  0.50 12.03 ?  303  CL    A CL   1 
HETATM 6791 O  O    . HOH   F 5 .   ? 11.618 -10.762 -9.985  1.00 43.03 ?  1301 HOH   A O    1 
HETATM 6792 O  O    A HOH   F 5 .   ? 4.675  3.889   0.716   0.50 19.76 ?  1302 HOH   A O    1 
HETATM 6793 O  O    . HOH   F 5 .   ? 14.779 -4.761  20.532  1.00 40.57 ?  1303 HOH   A O    1 
HETATM 6794 O  O    . HOH   F 5 .   ? 28.829 0.425   -9.735  1.00 21.18 ?  1304 HOH   A O    1 
HETATM 6795 O  O    . HOH   F 5 .   ? 15.260 -12.298 18.704  1.00 41.29 ?  1305 HOH   A O    1 
HETATM 6796 O  O    . HOH   F 5 .   ? 22.916 -12.000 22.006  1.00 49.45 ?  1306 HOH   A O    1 
HETATM 6797 O  O    . HOH   F 5 .   ? 34.412 -1.866  12.517  1.00 39.34 ?  1307 HOH   A O    1 
HETATM 6798 O  O    . HOH   F 5 .   ? 23.868 -15.736 -9.117  1.00 32.29 ?  1308 HOH   A O    1 
HETATM 6799 O  O    . HOH   F 5 .   ? 17.231 -18.143 15.091  1.00 26.36 ?  1309 HOH   A O    1 
HETATM 6800 O  O    B HOH   F 5 .   ? 3.920  0.161   9.303   0.50 32.20 ?  1310 HOH   A O    1 
HETATM 6801 O  O    . HOH   F 5 .   ? 42.420 10.534  5.205   1.00 19.09 ?  1311 HOH   A O    1 
HETATM 6802 O  O    . HOH   F 5 .   ? 7.652  -6.314  -6.532  1.00 40.33 ?  1312 HOH   A O    1 
HETATM 6803 O  O    . HOH   F 5 .   ? 28.252 -0.117  -13.370 1.00 34.72 ?  1313 HOH   A O    1 
HETATM 6804 O  O    . HOH   F 5 .   ? 14.931 3.844   17.664  1.00 33.97 ?  1314 HOH   A O    1 
HETATM 6805 O  O    . HOH   F 5 .   ? 7.988  -12.693 -0.783  1.00 22.27 ?  1315 HOH   A O    1 
HETATM 6806 O  O    . HOH   F 5 .   ? 14.161 -4.509  -11.791 1.00 36.93 ?  1316 HOH   A O    1 
HETATM 6807 O  O    . HOH   F 5 .   ? 28.339 -6.249  19.568  1.00 39.79 ?  1317 HOH   A O    1 
HETATM 6808 O  O    B HOH   F 5 .   ? 15.124 7.786   4.566   0.50 27.60 ?  1318 HOH   A O    1 
HETATM 6809 O  O    . HOH   F 5 .   ? 0.748  -4.768  0.183   1.00 30.63 ?  1319 HOH   A O    1 
HETATM 6810 O  O    . HOH   F 5 .   ? 9.917  -21.394 5.790   1.00 16.33 ?  1320 HOH   A O    1 
HETATM 6811 O  O    . HOH   F 5 .   ? 30.236 -13.298 -8.477  1.00 20.65 ?  1321 HOH   A O    1 
HETATM 6812 O  O    . HOH   F 5 .   ? 26.758 11.359  1.694   1.00 13.79 ?  1322 HOH   A O    1 
HETATM 6813 O  O    . HOH   F 5 .   ? 3.660  -9.410  9.826   1.00 46.63 ?  1323 HOH   A O    1 
HETATM 6814 O  O    . HOH   F 5 .   ? 14.790 -14.012 16.739  1.00 24.64 ?  1324 HOH   A O    1 
HETATM 6815 O  O    . HOH   F 5 .   ? 19.894 -12.610 -8.807  1.00 25.05 ?  1325 HOH   A O    1 
HETATM 6816 O  O    . HOH   F 5 .   ? 13.547 -15.217 -7.364  1.00 25.39 ?  1326 HOH   A O    1 
HETATM 6817 O  O    . HOH   F 5 .   ? 9.115  -10.187 19.401  1.00 44.20 ?  1327 HOH   A O    1 
HETATM 6818 O  O    B HOH   F 5 .   ? 13.411 -1.123  -6.934  0.50 19.15 ?  1328 HOH   A O    1 
HETATM 6819 O  O    . HOH   F 5 .   ? 30.822 6.252   -12.269 1.00 26.63 ?  1329 HOH   A O    1 
HETATM 6820 O  O    . HOH   F 5 .   ? 14.433 -24.708 11.601  1.00 36.30 ?  1330 HOH   A O    1 
HETATM 6821 O  O    . HOH   F 5 .   ? 37.509 2.813   10.231  1.00 27.33 ?  1331 HOH   A O    1 
HETATM 6822 O  O    . HOH   F 5 .   ? 26.489 -19.327 -1.771  1.00 12.78 ?  1332 HOH   A O    1 
HETATM 6823 O  O    . HOH   F 5 .   ? 31.037 -18.149 7.826   1.00 18.23 ?  1333 HOH   A O    1 
HETATM 6824 O  O    A HOH   F 5 .   ? 14.630 -3.677  3.162   0.50 17.58 ?  1334 HOH   A O    1 
HETATM 6825 O  O    . HOH   F 5 .   ? 25.677 -0.861  -7.382  1.00 15.15 ?  1335 HOH   A O    1 
HETATM 6826 O  O    . HOH   F 5 .   ? -1.602 -4.962  7.816   1.00 40.56 ?  1336 HOH   A O    1 
HETATM 6827 O  O    . HOH   F 5 .   ? 33.923 -1.060  -8.930  1.00 25.44 ?  1337 HOH   A O    1 
HETATM 6828 O  O    . HOH   F 5 .   ? 18.753 -19.409 13.590  1.00 32.02 ?  1338 HOH   A O    1 
HETATM 6829 O  O    A HOH   F 5 .   ? 17.482 -1.730  0.502   0.50 17.88 ?  1339 HOH   A O    1 
HETATM 6830 O  O    . HOH   F 5 .   ? 36.225 -5.081  -0.534  1.00 27.65 ?  1340 HOH   A O    1 
HETATM 6831 O  O    A HOH   F 5 .   ? 6.970  -8.203  11.926  0.50 15.64 ?  1341 HOH   A O    1 
HETATM 6832 O  O    B HOH   F 5 .   ? 11.325 3.104   1.873   0.50 23.39 ?  1342 HOH   A O    1 
HETATM 6833 O  O    . HOH   F 5 .   ? 18.952 -21.985 6.965   1.00 30.62 ?  1343 HOH   A O    1 
HETATM 6834 O  O    . HOH   F 5 .   ? 18.541 9.325   9.065   1.00 19.99 ?  1344 HOH   A O    1 
HETATM 6835 O  O    . HOH   F 5 .   ? 38.543 5.003   6.960   1.00 14.61 ?  1345 HOH   A O    1 
HETATM 6836 O  O    . HOH   F 5 .   ? 37.276 11.920  4.965   1.00 32.97 ?  1346 HOH   A O    1 
HETATM 6837 O  O    . HOH   F 5 .   ? 27.256 13.709  2.875   1.00 28.76 ?  1347 HOH   A O    1 
HETATM 6838 O  O    . HOH   F 5 .   ? 44.256 7.075   6.396   1.00 25.08 ?  1348 HOH   A O    1 
HETATM 6839 O  O    . HOH   F 5 .   ? 38.237 10.116  7.135   1.00 36.70 ?  1349 HOH   A O    1 
HETATM 6840 O  O    . HOH   F 5 .   ? -0.657 -8.576  2.250   1.00 50.61 ?  1350 HOH   A O    1 
HETATM 6841 O  O    . HOH   F 5 .   ? 20.591 -19.702 -5.006  1.00 25.22 ?  1351 HOH   A O    1 
HETATM 6842 O  O    . HOH   F 5 .   ? 22.298 -19.304 11.408  1.00 30.44 ?  1352 HOH   A O    1 
HETATM 6843 O  O    . HOH   F 5 .   ? 38.044 -1.344  -1.978  1.00 17.78 ?  1353 HOH   A O    1 
HETATM 6844 O  O    A HOH   F 5 .   ? 12.313 0.211   14.943  0.50 22.12 ?  1354 HOH   A O    1 
HETATM 6845 O  O    . HOH   F 5 .   ? 9.370  -12.208 17.396  1.00 58.74 ?  1355 HOH   A O    1 
HETATM 6846 O  O    . HOH   F 5 .   ? 24.356 3.521   -1.780  1.00 12.57 ?  1356 HOH   A O    1 
HETATM 6847 O  O    . HOH   F 5 .   ? 17.132 -17.813 -4.977  1.00 24.93 ?  1357 HOH   A O    1 
HETATM 6848 O  O    B HOH   F 5 .   ? 21.159 2.613   0.016   0.50 11.08 ?  1358 HOH   A O    1 
HETATM 6849 O  O    B HOH   F 5 .   ? 18.652 -1.487  -1.729  0.50 28.42 ?  1359 HOH   A O    1 
HETATM 6850 O  O    . HOH   F 5 .   ? 27.829 0.825   -7.166  1.00 13.26 ?  1360 HOH   A O    1 
HETATM 6851 O  O    . HOH   F 5 .   ? 28.576 -10.582 -14.088 1.00 39.05 ?  1361 HOH   A O    1 
HETATM 6852 O  O    . HOH   F 5 .   ? 14.340 -21.170 -4.221  1.00 27.62 ?  1362 HOH   A O    1 
HETATM 6853 O  O    A HOH   F 5 .   ? 8.203  -21.427 4.048   0.50 30.74 ?  1363 HOH   A O    1 
HETATM 6854 O  O    . HOH   F 5 .   ? 24.009 -2.141  -2.099  1.00 9.81  ?  1364 HOH   A O    1 
HETATM 6855 O  O    . HOH   F 5 .   ? 35.800 -12.696 6.808   1.00 14.30 ?  1365 HOH   A O    1 
HETATM 6856 O  O    . HOH   F 5 .   ? 42.468 4.239   5.253   1.00 32.06 ?  1366 HOH   A O    1 
HETATM 6857 O  O    . HOH   F 5 .   ? 31.684 8.243   14.821  1.00 22.90 ?  1367 HOH   A O    1 
HETATM 6858 O  O    . HOH   F 5 .   ? 6.758  -3.367  13.087  1.00 30.07 ?  1368 HOH   A O    1 
HETATM 6859 O  O    . HOH   F 5 .   ? 39.683 -1.017  -5.254  1.00 18.37 ?  1369 HOH   A O    1 
HETATM 6860 O  O    B HOH   F 5 .   ? 15.165 -2.921  3.741   0.50 13.78 ?  1370 HOH   A O    1 
HETATM 6861 O  O    . HOH   F 5 .   ? 22.362 5.338   19.056  1.00 42.12 ?  1371 HOH   A O    1 
HETATM 6862 O  O    A HOH   F 5 .   ? 14.275 0.545   6.871   0.50 27.94 ?  1372 HOH   A O    1 
HETATM 6863 O  O    . HOH   F 5 .   ? 31.800 -9.363  -6.659  1.00 21.18 ?  1373 HOH   A O    1 
HETATM 6864 O  O    . HOH   F 5 .   ? 15.515 11.955  7.858   1.00 33.21 ?  1374 HOH   A O    1 
HETATM 6865 O  O    . HOH   F 5 .   ? 31.065 -13.936 -2.440  1.00 12.26 ?  1375 HOH   A O    1 
HETATM 6866 O  O    . HOH   F 5 .   ? 43.802 8.420   -3.158  1.00 24.33 ?  1376 HOH   A O    1 
HETATM 6867 O  O    . HOH   F 5 .   ? 33.685 -7.159  4.273   1.00 15.19 ?  1377 HOH   A O    1 
HETATM 6868 O  O    . HOH   F 5 .   ? 30.795 3.078   8.273   1.00 10.65 ?  1378 HOH   A O    1 
HETATM 6869 O  O    . HOH   F 5 .   ? 17.047 -19.301 4.951   1.00 13.38 ?  1379 HOH   A O    1 
HETATM 6870 O  O    B HOH   F 5 .   ? 21.235 -2.085  -2.555  0.50 14.20 ?  1380 HOH   A O    1 
HETATM 6871 O  O    . HOH   F 5 .   ? 16.539 -22.056 1.020   1.00 28.55 ?  1381 HOH   A O    1 
HETATM 6872 O  O    . HOH   F 5 .   ? 22.730 12.495  1.681   1.00 12.76 ?  1382 HOH   A O    1 
HETATM 6873 O  O    . HOH   F 5 .   ? 27.557 -10.635 14.065  1.00 15.31 ?  1383 HOH   A O    1 
HETATM 6874 O  O    . HOH   F 5 .   ? 21.894 -21.927 8.424   1.00 26.91 ?  1384 HOH   A O    1 
HETATM 6875 O  O    . HOH   F 5 .   ? 23.436 11.346  4.129   1.00 10.77 ?  1385 HOH   A O    1 
HETATM 6876 O  O    . HOH   F 5 .   ? 24.318 -7.792  14.475  1.00 15.01 ?  1386 HOH   A O    1 
HETATM 6877 O  O    . HOH   F 5 .   ? 31.764 -7.313  -9.833  1.00 20.04 ?  1387 HOH   A O    1 
HETATM 6878 O  O    . HOH   F 5 .   ? 14.486 -0.520  -12.022 1.00 24.52 ?  1388 HOH   A O    1 
HETATM 6879 O  O    . HOH   F 5 .   ? 15.129 -8.088  -9.647  1.00 21.72 ?  1389 HOH   A O    1 
HETATM 6880 O  O    A HOH   F 5 .   ? 21.227 -2.406  -2.001  0.50 10.18 ?  1390 HOH   A O    1 
HETATM 6881 O  O    . HOH   F 5 .   ? 14.124 -23.086 7.477   1.00 16.91 ?  1391 HOH   A O    1 
HETATM 6882 O  O    . HOH   F 5 .   ? 37.209 -2.937  9.738   1.00 39.48 ?  1392 HOH   A O    1 
HETATM 6883 O  O    . HOH   F 5 .   ? 14.025 -4.941  17.585  1.00 25.41 ?  1393 HOH   A O    1 
HETATM 6884 O  O    B HOH   F 5 .   ? 2.735  -3.406  9.898   0.50 28.27 ?  1394 HOH   A O    1 
HETATM 6885 O  O    . HOH   F 5 .   ? 21.238 10.236  15.071  1.00 32.51 ?  1395 HOH   A O    1 
HETATM 6886 O  O    . HOH   F 5 .   ? 43.293 7.821   2.625   1.00 21.81 ?  1396 HOH   A O    1 
HETATM 6887 O  O    . HOH   F 5 .   ? 24.764 -17.562 12.753  1.00 22.29 ?  1397 HOH   A O    1 
HETATM 6888 O  O    A HOH   F 5 .   ? 20.058 4.540   -7.483  0.50 14.80 ?  1398 HOH   A O    1 
HETATM 6889 O  O    B HOH   F 5 .   ? 22.600 5.615   -1.755  0.50 17.93 ?  1399 HOH   A O    1 
HETATM 6890 O  O    . HOH   F 5 .   ? 11.040 1.570   12.900  1.00 25.12 ?  1400 HOH   A O    1 
HETATM 6891 O  O    . HOH   F 5 .   ? 11.799 -10.811 17.128  1.00 25.90 ?  1401 HOH   A O    1 
HETATM 6892 O  O    . HOH   F 5 .   ? 37.519 -2.011  5.749   1.00 24.79 ?  1402 HOH   A O    1 
HETATM 6893 O  O    . HOH   F 5 .   ? 27.399 2.331   18.729  1.00 27.13 ?  1403 HOH   A O    1 
HETATM 6894 O  O    . HOH   F 5 .   ? 20.574 -20.016 2.826   1.00 16.16 ?  1404 HOH   A O    1 
HETATM 6895 O  O    . HOH   F 5 .   ? 15.845 2.075   24.768  1.00 48.24 ?  1405 HOH   A O    1 
HETATM 6896 O  O    A HOH   F 5 .   ? 13.277 -1.447  -6.453  0.50 13.66 ?  1406 HOH   A O    1 
HETATM 6897 O  O    . HOH   F 5 .   ? 15.261 -21.598 14.272  1.00 16.77 ?  1407 HOH   A O    1 
HETATM 6898 O  O    A HOH   F 5 .   ? 18.939 -0.681  -1.568  0.50 9.05  ?  1408 HOH   A O    1 
HETATM 6899 O  O    . HOH   F 5 .   ? 32.776 -9.273  5.906   1.00 19.06 ?  1409 HOH   A O    1 
HETATM 6900 O  O    . HOH   F 5 .   ? 27.349 -6.122  -14.003 1.00 35.08 ?  1410 HOH   A O    1 
HETATM 6901 O  O    B HOH   F 5 .   ? 11.919 -1.924  -3.422  0.50 13.24 ?  1411 HOH   A O    1 
HETATM 6902 O  O    . HOH   F 5 .   ? 30.762 1.850   16.679  1.00 19.17 ?  1412 HOH   A O    1 
HETATM 6903 O  O    . HOH   F 5 .   ? 24.524 1.983   -7.046  1.00 21.20 ?  1413 HOH   A O    1 
HETATM 6904 O  O    A HOH   F 5 .   ? 21.328 3.144   -0.291  0.50 7.86  ?  1414 HOH   A O    1 
HETATM 6905 O  O    . HOH   F 5 .   ? 26.897 4.127   -0.641  1.00 11.32 ?  1415 HOH   A O    1 
HETATM 6906 O  O    A HOH   F 5 .   ? -0.483 -3.128  3.203   0.50 29.74 ?  1416 HOH   A O    1 
HETATM 6907 O  O    . HOH   F 5 .   ? 23.920 -20.273 -1.328  1.00 14.61 ?  1417 HOH   A O    1 
HETATM 6908 O  O    A HOH   F 5 .   ? 15.798 -0.970  5.336   0.50 33.18 ?  1418 HOH   A O    1 
HETATM 6909 O  O    . HOH   F 5 .   ? 30.412 -12.942 13.519  1.00 18.13 ?  1419 HOH   A O    1 
HETATM 6910 O  O    . HOH   F 5 .   ? 30.127 -10.134 13.029  1.00 20.02 ?  1420 HOH   A O    1 
HETATM 6911 O  O    . HOH   F 5 .   ? 35.044 -5.212  -3.098  1.00 16.45 ?  1421 HOH   A O    1 
HETATM 6912 O  O    A HOH   F 5 .   ? 6.484  -5.646  11.260  0.50 16.95 ?  1422 HOH   A O    1 
HETATM 6913 O  O    . HOH   F 5 .   ? 10.424 -13.744 -1.630  1.00 16.04 ?  1423 HOH   A O    1 
HETATM 6914 O  O    . HOH   F 5 .   ? 10.414 -22.121 -1.209  1.00 52.97 ?  1424 HOH   A O    1 
HETATM 6915 O  O    . HOH   F 5 .   ? 40.903 -8.230  -6.806  1.00 36.05 ?  1425 HOH   A O    1 
HETATM 6916 O  O    A HOH   F 5 .   ? 11.056 -0.404  2.012   0.50 28.67 ?  1426 HOH   A O    1 
HETATM 6917 O  O    . HOH   F 5 .   ? 36.730 -4.991  5.386   1.00 23.24 ?  1427 HOH   A O    1 
HETATM 6918 O  O    . HOH   F 5 .   ? 32.602 -10.669 3.177   1.00 28.96 ?  1428 HOH   A O    1 
HETATM 6919 O  O    . HOH   F 5 .   ? 16.182 16.691  8.781   1.00 29.98 ?  1429 HOH   A O    1 
HETATM 6920 O  O    . HOH   F 5 .   ? 22.641 8.058   18.357  1.00 44.12 ?  1430 HOH   A O    1 
HETATM 6921 O  O    . HOH   F 5 .   ? 32.675 -4.365  -9.907  1.00 26.04 ?  1431 HOH   A O    1 
HETATM 6922 O  O    . HOH   F 5 .   ? 41.556 1.533   4.952   1.00 36.15 ?  1432 HOH   A O    1 
HETATM 6923 O  O    A HOH   F 5 .   ? 18.517 -2.455  -16.282 0.50 24.42 ?  1433 HOH   A O    1 
HETATM 6924 O  O    . HOH   F 5 .   ? 4.985  2.671   5.163   1.00 30.55 ?  1434 HOH   A O    1 
HETATM 6925 O  O    . HOH   F 5 .   ? 44.935 -0.540  2.950   1.00 42.46 ?  1435 HOH   A O    1 
HETATM 6926 O  O    . HOH   F 5 .   ? 27.103 -3.214  19.349  1.00 32.02 ?  1436 HOH   A O    1 
HETATM 6927 O  O    A HOH   F 5 .   ? 19.367 -11.086 24.196  0.50 43.22 ?  1437 HOH   A O    1 
HETATM 6928 O  O    . HOH   F 5 .   ? 20.558 -17.756 24.794  1.00 52.46 ?  1438 HOH   A O    1 
HETATM 6929 O  O    A HOH   F 5 .   ? 18.843 2.020   -0.689  0.50 9.38  ?  1439 HOH   A O    1 
HETATM 6930 O  O    A HOH   F 5 .   ? 16.234 -14.343 20.249  0.50 27.59 ?  1440 HOH   A O    1 
HETATM 6931 O  O    . HOH   F 5 .   ? 23.638 -8.036  17.090  1.00 19.53 ?  1441 HOH   A O    1 
HETATM 6932 O  O    . HOH   F 5 .   ? 21.688 -13.980 -8.122  1.00 46.60 ?  1442 HOH   A O    1 
HETATM 6933 O  O    A HOH   F 5 .   ? 24.059 3.956   -4.864  0.50 17.87 ?  1443 HOH   A O    1 
HETATM 6934 O  O    A HOH   F 5 .   ? 16.235 2.933   -1.371  0.50 17.71 ?  1444 HOH   A O    1 
HETATM 6935 O  O    . HOH   F 5 .   ? 37.704 -8.810  -3.412  1.00 23.35 ?  1445 HOH   A O    1 
HETATM 6936 O  O    A HOH   F 5 .   ? 18.384 -16.095 16.469  0.50 24.91 ?  1446 HOH   A O    1 
HETATM 6937 O  O    A HOH   F 5 .   ? 9.381  -16.346 -1.923  0.50 32.50 ?  1447 HOH   A O    1 
HETATM 6938 O  O    . HOH   F 5 .   ? 27.617 6.916   -6.359  1.00 32.19 ?  1448 HOH   A O    1 
HETATM 6939 O  O    A HOH   F 5 .   ? 16.002 6.934   3.066   0.50 12.62 ?  1449 HOH   A O    1 
HETATM 6940 O  O    . HOH   F 5 .   ? 23.319 -20.968 1.321   1.00 16.27 ?  1450 HOH   A O    1 
HETATM 6941 O  O    . HOH   F 5 .   ? 23.198 7.702   -3.194  1.00 22.04 ?  1451 HOH   A O    1 
HETATM 6942 O  O    . HOH   F 5 .   ? 34.413 -8.092  -0.504  1.00 28.14 ?  1452 HOH   A O    1 
HETATM 6943 O  O    . HOH   F 5 .   ? 30.555 14.757  2.819   1.00 16.84 ?  1453 HOH   A O    1 
HETATM 6944 O  O    . HOH   F 5 .   ? 18.403 4.950   -15.081 1.00 49.69 ?  1454 HOH   A O    1 
HETATM 6945 O  O    . HOH   F 5 .   ? 31.337 -12.818 0.046   1.00 18.05 ?  1455 HOH   A O    1 
HETATM 6946 O  O    B HOH   F 5 .   ? 18.278 1.722   -0.393  0.50 16.49 ?  1456 HOH   A O    1 
HETATM 6947 O  O    A HOH   F 5 .   ? 21.555 -14.721 18.067  0.50 36.33 ?  1457 HOH   A O    1 
HETATM 6948 O  O    A HOH   F 5 .   ? 21.389 -9.391  21.287  0.50 28.71 ?  1458 HOH   A O    1 
HETATM 6949 O  O    A HOH   F 5 .   ? 14.020 -0.362  3.533   0.50 33.21 ?  1459 HOH   A O    1 
HETATM 6950 O  O    . HOH   F 5 .   ? 29.954 -16.072 10.662  1.00 31.79 ?  1460 HOH   A O    1 
HETATM 6951 O  O    B HOH   F 5 .   ? 16.289 7.785   8.750   0.50 23.99 ?  1461 HOH   A O    1 
HETATM 6952 O  O    . HOH   F 5 .   ? 29.733 -2.005  -12.765 1.00 46.92 ?  1462 HOH   A O    1 
HETATM 6953 O  O    . HOH   F 5 .   ? 25.365 8.294   -4.821  1.00 19.65 ?  1463 HOH   A O    1 
HETATM 6954 O  O    . HOH   F 5 .   ? 24.821 5.610   20.735  1.00 51.07 ?  1464 HOH   A O    1 
HETATM 6955 O  O    . HOH   F 5 .   ? 32.458 -15.988 10.878  1.00 33.29 ?  1465 HOH   A O    1 
HETATM 6956 O  O    . HOH   F 5 .   ? 19.881 -17.298 -5.037  1.00 23.88 ?  1466 HOH   A O    1 
HETATM 6957 O  O    . HOH   F 5 .   ? 23.212 -22.337 -3.288  1.00 34.79 ?  1467 HOH   A O    1 
HETATM 6958 O  O    . HOH   F 5 .   ? 24.575 14.528  7.865   1.00 29.45 ?  1468 HOH   A O    1 
HETATM 6959 O  O    . HOH   F 5 .   ? 26.852 11.582  -1.166  1.00 25.31 ?  1469 HOH   A O    1 
HETATM 6960 O  O    . HOH   F 5 .   ? 39.715 -7.067  -3.559  1.00 48.84 ?  1470 HOH   A O    1 
HETATM 6961 O  O    . HOH   F 5 .   ? 15.737 -21.484 3.724   1.00 20.89 ?  1471 HOH   A O    1 
HETATM 6962 O  O    . HOH   F 5 .   ? 23.434 13.669  5.586   1.00 17.60 ?  1472 HOH   A O    1 
HETATM 6963 O  O    . HOH   F 5 .   ? 18.717 10.764  11.352  1.00 30.29 ?  1473 HOH   A O    1 
HETATM 6964 O  O    . HOH   F 5 .   ? 11.063 -14.977 -6.049  1.00 30.48 ?  1474 HOH   A O    1 
HETATM 6965 O  O    . HOH   F 5 .   ? 25.815 10.766  -3.615  1.00 20.76 ?  1475 HOH   A O    1 
HETATM 6966 O  O    A HOH   F 5 .   ? 21.929 5.263   -5.777  0.50 22.20 ?  1476 HOH   A O    1 
HETATM 6967 O  O    . HOH   F 5 .   ? 11.980 -13.443 16.479  1.00 50.50 ?  1477 HOH   A O    1 
HETATM 6968 O  O    . HOH   F 5 .   ? 27.557 -11.427 16.536  1.00 35.72 ?  1478 HOH   A O    1 
HETATM 6969 O  O    B HOH   F 5 .   ? 6.038  4.081   3.185   0.50 36.56 ?  1479 HOH   A O    1 
HETATM 6970 O  O    B HOH   F 5 .   ? 10.752 6.265   10.865  0.50 25.54 ?  1480 HOH   A O    1 
HETATM 6971 O  O    . HOH   F 5 .   ? 12.277 1.598   17.332  1.00 37.61 ?  1481 HOH   A O    1 
HETATM 6972 O  O    . HOH   F 5 .   ? 17.414 -18.741 19.801  1.00 48.24 ?  1482 HOH   A O    1 
HETATM 6973 O  O    . HOH   F 5 .   ? 18.132 -16.309 -8.735  1.00 38.98 ?  1483 HOH   A O    1 
HETATM 6974 O  O    . HOH   F 5 .   ? 15.700 -17.180 -6.915  1.00 29.60 ?  1484 HOH   A O    1 
HETATM 6975 O  O    . HOH   F 5 .   ? 20.514 -16.000 -7.330  1.00 27.09 ?  1485 HOH   A O    1 
HETATM 6976 O  O    . HOH   F 5 .   ? 23.166 11.885  -3.988  1.00 18.11 ?  1486 HOH   A O    1 
HETATM 6977 O  O    . HOH   F 5 .   ? 28.836 8.946   17.552  1.00 33.72 ?  1487 HOH   A O    1 
HETATM 6978 O  O    . HOH   F 5 .   ? 16.803 -20.567 16.258  1.00 26.67 ?  1488 HOH   A O    1 
HETATM 6979 O  O    . HOH   F 5 .   ? 35.195 7.455   12.301  1.00 49.89 ?  1489 HOH   A O    1 
HETATM 6980 O  O    B HOH   F 5 .   ? 11.097 0.424   -2.029  0.50 17.97 ?  1490 HOH   A O    1 
HETATM 6981 O  O    . HOH   F 5 .   ? 40.916 -3.991  -0.331  1.00 37.98 ?  1491 HOH   A O    1 
HETATM 6982 O  O    . HOH   F 5 .   ? 13.982 -10.291 -10.807 1.00 33.58 ?  1492 HOH   A O    1 
HETATM 6983 O  O    B HOH   F 5 .   ? 12.740 2.548   -0.792  0.50 15.92 ?  1493 HOH   A O    1 
HETATM 6984 O  O    . HOH   F 5 .   ? 31.364 -0.581  -10.608 1.00 28.21 ?  1494 HOH   A O    1 
HETATM 6985 O  O    . HOH   F 5 .   ? 30.946 0.745   19.146  1.00 38.28 ?  1495 HOH   A O    1 
HETATM 6986 O  O    B HOH   F 5 .   ? 15.979 9.791   6.461   0.50 26.16 ?  1496 HOH   A O    1 
HETATM 6987 O  O    . HOH   F 5 .   ? 28.524 -4.703  -12.301 1.00 37.04 ?  1497 HOH   A O    1 
HETATM 6988 O  O    B HOH   F 5 .   ? 10.474 -1.650  -5.856  0.50 24.22 ?  1498 HOH   A O    1 
HETATM 6989 O  O    . HOH   F 5 .   ? 41.658 9.321   -4.025  1.00 30.21 ?  1499 HOH   A O    1 
HETATM 6990 O  O    . HOH   F 5 .   ? 28.610 -7.944  -15.252 1.00 45.21 ?  1500 HOH   A O    1 
HETATM 6991 O  O    . HOH   F 5 .   ? 44.429 10.440  -1.630  1.00 32.11 ?  1501 HOH   A O    1 
HETATM 6992 O  O    . HOH   F 5 .   ? 7.946  -3.019  -5.571  1.00 45.39 ?  1502 HOH   A O    1 
HETATM 6993 O  O    . HOH   F 5 .   ? 15.983 -6.835  -11.788 1.00 44.65 ?  1503 HOH   A O    1 
HETATM 6994 O  O    . HOH   F 5 .   ? 39.175 2.380   7.502   1.00 32.35 ?  1504 HOH   A O    1 
HETATM 6995 O  O    . HOH   F 5 .   ? 18.537 -23.192 1.900   1.00 41.73 ?  1505 HOH   A O    1 
HETATM 6996 O  O    . HOH   F 5 .   ? 30.719 5.842   -14.721 1.00 35.55 ?  1506 HOH   A O    1 
HETATM 6997 O  O    . HOH   F 5 .   ? 40.409 -0.271  -7.869  1.00 31.23 ?  1507 HOH   A O    1 
HETATM 6998 O  O    . HOH   F 5 .   ? 16.178 -23.370 5.742   1.00 29.46 ?  1508 HOH   A O    1 
HETATM 6999 O  O    . HOH   F 5 .   ? 14.075 -25.363 8.929   1.00 31.00 ?  1509 HOH   A O    1 
HETATM 7000 O  O    . HOH   F 5 .   ? 20.038 -22.359 4.211   1.00 27.11 ?  1510 HOH   A O    1 
HETATM 7001 O  O    . HOH   F 5 .   ? 23.234 -23.795 1.718   1.00 29.25 ?  1511 HOH   A O    1 
HETATM 7002 O  O    A HOH   F 5 .   ? 23.366 -13.006 19.285  0.50 31.14 ?  1512 HOH   A O    1 
HETATM 7003 O  O    . HOH   F 5 .   ? 30.726 -5.763  -11.834 1.00 46.57 ?  1513 HOH   A O    1 
HETATM 7004 O  O    . HOH   F 5 .   ? 37.440 -6.639  7.516   1.00 23.55 ?  1514 HOH   A O    1 
HETATM 7005 O  O    . HOH   F 5 .   ? 39.579 -0.042  6.552   1.00 27.73 ?  1515 HOH   A O    1 
HETATM 7006 O  O    . HOH   F 5 .   ? 28.951 14.363  0.911   1.00 45.75 ?  1516 HOH   A O    1 
HETATM 7007 O  O    . HOH   F 5 .   ? 38.016 13.902  6.708   1.00 47.13 ?  1517 HOH   A O    1 
HETATM 7008 O  O    . HOH   F 5 .   ? 22.036 -24.059 4.497   1.00 25.18 ?  1518 HOH   A O    1 
HETATM 7009 O  O    . HOH   F 5 .   ? 36.491 -6.524  10.122  1.00 41.35 ?  1519 HOH   A O    1 
HETATM 7010 O  O    . HOH   F 5 .   ? 17.431 -6.751  -14.159 1.00 40.79 ?  1520 HOH   A O    1 
HETATM 7011 O  O    A HOH   F 5 .   ? 14.838 8.626   4.970   0.50 21.79 ?  1521 HOH   A O    1 
HETATM 7012 O  O    B HOH   F 5 .   ? 6.207  6.865   2.050   0.50 28.55 ?  1522 HOH   A O    1 
HETATM 7013 O  O    . HOH   F 5 .   ? 24.032 9.078   -7.188  1.00 34.33 ?  1523 HOH   A O    1 
HETATM 7014 O  O    . HOH   F 5 .   ? 16.346 -21.121 18.784  1.00 35.81 ?  1524 HOH   A O    1 
HETATM 7015 O  O    . HOH   F 5 .   ? 16.000 -12.400 27.501  1.00 41.72 ?  1525 HOH   A O    1 
HETATM 7016 O  O    . HOH   F 5 .   ? 14.647 -22.779 19.902  1.00 33.76 ?  1526 HOH   A O    1 
HETATM 7017 O  O    . HOH   G 5 .   ? 29.847 -22.432 5.497   1.00 18.35 ?  201  HOH   B O    1 
HETATM 7018 O  O    . HOH   G 5 .   ? 41.671 -35.922 -17.265 1.00 30.54 ?  202  HOH   B O    1 
HETATM 7019 O  O    . HOH   G 5 .   ? 27.866 -41.774 -15.137 1.00 34.32 ?  203  HOH   B O    1 
HETATM 7020 O  O    . HOH   G 5 .   ? 49.335 -22.702 -19.785 1.00 47.66 ?  204  HOH   B O    1 
HETATM 7021 O  O    . HOH   G 5 .   ? 41.436 -7.767  5.503   1.00 37.75 ?  205  HOH   B O    1 
HETATM 7022 O  O    . HOH   G 5 .   ? 48.090 -6.905  15.522  1.00 33.16 ?  206  HOH   B O    1 
HETATM 7023 O  O    . HOH   G 5 .   ? 27.718 -29.145 -1.866  1.00 34.85 ?  207  HOH   B O    1 
HETATM 7024 O  O    . HOH   G 5 .   ? 29.941 -26.291 4.060   1.00 26.55 ?  208  HOH   B O    1 
HETATM 7025 O  O    . HOH   G 5 .   ? 37.951 -39.458 -0.252  1.00 40.16 ?  209  HOH   B O    1 
HETATM 7026 O  O    . HOH   G 5 .   ? 59.161 -18.770 6.761   1.00 35.83 ?  210  HOH   B O    1 
HETATM 7027 O  O    . HOH   G 5 .   ? 56.375 -19.732 7.115   1.00 31.26 ?  211  HOH   B O    1 
HETATM 7028 O  O    . HOH   G 5 .   ? 54.447 -9.372  -8.796  1.00 17.93 ?  212  HOH   B O    1 
HETATM 7029 O  O    . HOH   G 5 .   ? 52.996 -13.420 -20.295 1.00 32.18 ?  213  HOH   B O    1 
HETATM 7030 O  O    . HOH   G 5 .   ? 55.387 -16.490 -14.360 1.00 33.39 ?  214  HOH   B O    1 
HETATM 7031 O  O    . HOH   G 5 .   ? 58.240 -12.925 8.343   1.00 30.44 ?  215  HOH   B O    1 
HETATM 7032 O  O    . HOH   G 5 .   ? 44.477 -7.208  2.039   1.00 34.55 ?  216  HOH   B O    1 
HETATM 7033 O  O    . HOH   G 5 .   ? 47.399 -7.372  -3.904  1.00 41.39 ?  217  HOH   B O    1 
HETATM 7034 O  O    . HOH   G 5 .   ? 30.207 -40.992 -8.180  1.00 14.93 ?  218  HOH   B O    1 
HETATM 7035 O  O    . HOH   G 5 .   ? 29.820 -34.120 -0.481  1.00 32.83 ?  219  HOH   B O    1 
HETATM 7036 O  O    . HOH   G 5 .   ? 50.231 -3.462  7.123   1.00 33.96 ?  220  HOH   B O    1 
HETATM 7037 O  O    . HOH   G 5 .   ? 57.734 -24.427 5.041   1.00 35.28 ?  221  HOH   B O    1 
HETATM 7038 O  O    . HOH   G 5 .   ? 41.491 -39.132 -14.941 1.00 20.25 ?  222  HOH   B O    1 
HETATM 7039 O  O    . HOH   G 5 .   ? 57.132 -26.822 -7.602  1.00 38.87 ?  223  HOH   B O    1 
HETATM 7040 O  O    . HOH   G 5 .   ? 40.626 -16.037 14.077  1.00 23.46 ?  224  HOH   B O    1 
HETATM 7041 O  O    . HOH   G 5 .   ? 50.742 -6.108  0.147   1.00 25.61 ?  225  HOH   B O    1 
HETATM 7042 O  O    . HOH   G 5 .   ? 34.544 -36.348 -7.255  1.00 16.62 ?  226  HOH   B O    1 
HETATM 7043 O  O    . HOH   G 5 .   ? 56.699 -30.750 -7.789  1.00 28.85 ?  227  HOH   B O    1 
HETATM 7044 O  O    . HOH   G 5 .   ? 57.395 -16.242 -12.228 1.00 17.49 ?  228  HOH   B O    1 
HETATM 7045 O  O    . HOH   G 5 .   ? 41.408 -9.651  13.026  1.00 20.88 ?  229  HOH   B O    1 
HETATM 7046 O  O    . HOH   G 5 .   ? 34.917 -24.649 13.842  1.00 26.78 ?  230  HOH   B O    1 
HETATM 7047 O  O    . HOH   G 5 .   ? 39.332 -10.868 6.101   1.00 24.61 ?  231  HOH   B O    1 
HETATM 7048 O  O    . HOH   G 5 .   ? 35.947 -43.251 -8.564  1.00 31.66 ?  232  HOH   B O    1 
HETATM 7049 O  O    . HOH   G 5 .   ? 35.095 -7.999  -3.008  1.00 17.00 ?  233  HOH   B O    1 
HETATM 7050 O  O    . HOH   G 5 .   ? 32.794 -43.750 -11.389 1.00 18.76 ?  234  HOH   B O    1 
HETATM 7051 O  O    . HOH   G 5 .   ? 44.949 -43.497 -10.582 1.00 25.90 ?  235  HOH   B O    1 
HETATM 7052 O  O    . HOH   G 5 .   ? 51.698 -6.507  4.396   1.00 18.15 ?  236  HOH   B O    1 
HETATM 7053 O  O    . HOH   G 5 .   ? 46.413 -1.586  13.248  1.00 28.37 ?  237  HOH   B O    1 
HETATM 7054 O  O    . HOH   G 5 .   ? 37.051 -19.728 -18.149 1.00 39.77 ?  238  HOH   B O    1 
HETATM 7055 O  O    . HOH   G 5 .   ? 50.743 -12.972 -0.505  1.00 10.90 ?  239  HOH   B O    1 
HETATM 7056 O  O    . HOH   G 5 .   ? 45.159 -34.951 6.792   1.00 37.43 ?  240  HOH   B O    1 
HETATM 7057 O  O    . HOH   G 5 .   ? 25.425 -25.948 -1.355  1.00 32.21 ?  241  HOH   B O    1 
HETATM 7058 O  O    . HOH   G 5 .   ? 28.395 -19.652 -13.122 1.00 21.83 ?  242  HOH   B O    1 
HETATM 7059 O  O    . HOH   G 5 .   ? 30.865 -28.771 4.251   1.00 24.98 ?  243  HOH   B O    1 
HETATM 7060 O  O    . HOH   G 5 .   ? 42.662 -22.872 3.832   1.00 10.40 ?  244  HOH   B O    1 
HETATM 7061 O  O    . HOH   G 5 .   ? 38.461 -11.055 -2.252  1.00 18.18 ?  245  HOH   B O    1 
HETATM 7062 O  O    . HOH   G 5 .   ? 42.583 -25.373 2.610   1.00 13.49 ?  246  HOH   B O    1 
HETATM 7063 O  O    . HOH   G 5 .   ? 57.593 -24.388 -3.858  1.00 19.78 ?  247  HOH   B O    1 
HETATM 7064 O  O    . HOH   G 5 .   ? 43.099 -43.223 -8.296  1.00 26.70 ?  248  HOH   B O    1 
HETATM 7065 O  O    . HOH   G 5 .   ? 41.872 -23.513 9.281   1.00 15.35 ?  249  HOH   B O    1 
HETATM 7066 O  O    . HOH   G 5 .   ? 38.965 -12.004 12.271  1.00 31.83 ?  250  HOH   B O    1 
HETATM 7067 O  O    . HOH   G 5 .   ? 39.507 -11.112 0.330   1.00 15.53 ?  251  HOH   B O    1 
HETATM 7068 O  O    . HOH   G 5 .   ? 43.171 -32.336 -17.117 1.00 21.24 ?  252  HOH   B O    1 
HETATM 7069 O  O    . HOH   G 5 .   ? 44.532 -27.798 -0.747  1.00 19.51 ?  253  HOH   B O    1 
HETATM 7070 O  O    . HOH   G 5 .   ? 40.327 -12.742 -11.520 1.00 13.82 ?  254  HOH   B O    1 
HETATM 7071 O  O    . HOH   G 5 .   ? 58.177 -10.621 -4.070  1.00 19.09 ?  255  HOH   B O    1 
HETATM 7072 O  O    . HOH   G 5 .   ? 29.705 -25.202 -10.807 1.00 14.91 ?  256  HOH   B O    1 
HETATM 7073 O  O    . HOH   G 5 .   ? 34.278 -18.520 11.442  1.00 22.73 ?  257  HOH   B O    1 
HETATM 7074 O  O    . HOH   G 5 .   ? 33.548 -17.028 8.053   1.00 17.83 ?  258  HOH   B O    1 
HETATM 7075 O  O    . HOH   G 5 .   ? 30.876 -15.747 2.669   1.00 12.29 ?  259  HOH   B O    1 
HETATM 7076 O  O    . HOH   G 5 .   ? 51.590 -13.831 11.022  1.00 26.27 ?  260  HOH   B O    1 
HETATM 7077 O  O    . HOH   G 5 .   ? 28.477 -30.802 -14.830 1.00 26.60 ?  261  HOH   B O    1 
HETATM 7078 O  O    . HOH   G 5 .   ? 50.991 -39.945 -8.308  1.00 31.16 ?  262  HOH   B O    1 
HETATM 7079 O  O    . HOH   G 5 .   ? 56.980 -8.672  8.371   1.00 18.87 ?  263  HOH   B O    1 
HETATM 7080 O  O    . HOH   G 5 .   ? 57.513 -9.241  1.374   1.00 18.27 ?  264  HOH   B O    1 
HETATM 7081 O  O    . HOH   G 5 .   ? 31.809 -17.960 -14.517 1.00 31.99 ?  265  HOH   B O    1 
HETATM 7082 O  O    . HOH   G 5 .   ? 48.027 -22.791 5.814   1.00 15.28 ?  266  HOH   B O    1 
HETATM 7083 O  O    . HOH   G 5 .   ? 42.381 -9.937  9.331   1.00 19.29 ?  267  HOH   B O    1 
HETATM 7084 O  O    . HOH   G 5 .   ? 48.486 -36.466 -15.661 1.00 43.37 ?  268  HOH   B O    1 
HETATM 7085 O  O    . HOH   G 5 .   ? 46.623 -31.268 -4.858  1.00 21.16 ?  269  HOH   B O    1 
HETATM 7086 O  O    . HOH   G 5 .   ? 49.307 -28.700 -6.960  1.00 14.10 ?  270  HOH   B O    1 
HETATM 7087 O  O    . HOH   G 5 .   ? 27.144 -31.794 -9.990  1.00 18.40 ?  271  HOH   B O    1 
HETATM 7088 O  O    . HOH   G 5 .   ? 34.903 -33.275 -19.260 1.00 27.67 ?  272  HOH   B O    1 
HETATM 7089 O  O    . HOH   G 5 .   ? 34.491 -12.804 2.631   1.00 21.51 ?  273  HOH   B O    1 
HETATM 7090 O  O    . HOH   G 5 .   ? 28.270 -34.325 -9.436  1.00 17.17 ?  274  HOH   B O    1 
HETATM 7091 O  O    . HOH   G 5 .   ? 43.368 -15.787 -12.165 1.00 13.04 ?  275  HOH   B O    1 
HETATM 7092 O  O    . HOH   G 5 .   ? 56.166 -23.440 -14.788 1.00 24.96 ?  276  HOH   B O    1 
HETATM 7093 O  O    . HOH   G 5 .   ? 30.536 -42.225 -10.637 1.00 27.65 ?  277  HOH   B O    1 
HETATM 7094 O  O    . HOH   G 5 .   ? 42.750 -20.306 -20.743 1.00 38.54 ?  278  HOH   B O    1 
HETATM 7095 O  O    . HOH   G 5 .   ? 49.785 -0.497  10.240  1.00 30.74 ?  279  HOH   B O    1 
HETATM 7096 O  O    . HOH   G 5 .   ? 41.192 -5.533  11.506  1.00 44.95 ?  280  HOH   B O    1 
HETATM 7097 O  O    . HOH   G 5 .   ? 42.256 -10.052 -14.944 1.00 36.19 ?  281  HOH   B O    1 
HETATM 7098 O  O    . HOH   G 5 .   ? 27.944 -22.862 -7.996  1.00 15.93 ?  282  HOH   B O    1 
HETATM 7099 O  O    . HOH   G 5 .   ? 52.613 -10.425 12.940  1.00 21.57 ?  283  HOH   B O    1 
HETATM 7100 O  O    . HOH   G 5 .   ? 36.822 -12.779 -1.523  1.00 25.23 ?  284  HOH   B O    1 
HETATM 7101 O  O    . HOH   G 5 .   ? 48.419 -25.053 3.086   1.00 11.85 ?  285  HOH   B O    1 
HETATM 7102 O  O    . HOH   G 5 .   ? 46.878 -29.563 9.788   1.00 30.24 ?  286  HOH   B O    1 
HETATM 7103 O  O    . HOH   G 5 .   ? 59.830 -15.290 8.115   1.00 29.66 ?  287  HOH   B O    1 
HETATM 7104 O  O    . HOH   G 5 .   ? 47.087 -33.959 -4.703  1.00 16.26 ?  288  HOH   B O    1 
HETATM 7105 O  O    . HOH   G 5 .   ? 48.742 -20.036 5.900   1.00 12.78 ?  289  HOH   B O    1 
HETATM 7106 O  O    . HOH   G 5 .   ? 42.414 -34.679 3.776   1.00 24.60 ?  290  HOH   B O    1 
HETATM 7107 O  O    . HOH   G 5 .   ? 27.599 -26.783 -15.747 1.00 33.29 ?  291  HOH   B O    1 
HETATM 7108 O  O    . HOH   G 5 .   ? 33.492 -15.304 -13.938 1.00 19.38 ?  292  HOH   B O    1 
HETATM 7109 O  O    . HOH   G 5 .   ? 47.927 -24.447 -17.855 1.00 30.19 ?  293  HOH   B O    1 
HETATM 7110 O  O    . HOH   G 5 .   ? 37.390 -35.650 7.283   1.00 30.86 ?  294  HOH   B O    1 
HETATM 7111 O  O    . HOH   G 5 .   ? 45.369 -33.374 -15.987 1.00 21.61 ?  295  HOH   B O    1 
HETATM 7112 O  O    . HOH   G 5 .   ? 57.166 -12.056 12.312  1.00 35.82 ?  296  HOH   B O    1 
HETATM 7113 O  O    . HOH   G 5 .   ? 51.233 -37.574 -9.670  1.00 25.07 ?  297  HOH   B O    1 
HETATM 7114 O  O    . HOH   G 5 .   ? 43.587 -15.405 18.183  1.00 29.11 ?  298  HOH   B O    1 
HETATM 7115 O  O    . HOH   G 5 .   ? 44.615 -27.473 1.952   1.00 13.98 ?  299  HOH   B O    1 
HETATM 7116 O  O    . HOH   G 5 .   ? 25.941 -21.481 -3.468  1.00 14.79 ?  300  HOH   B O    1 
HETATM 7117 O  O    . HOH   G 5 .   ? 37.588 -18.230 13.115  1.00 29.30 ?  301  HOH   B O    1 
HETATM 7118 O  O    . HOH   G 5 .   ? 53.452 -30.191 4.466   1.00 17.15 ?  302  HOH   B O    1 
HETATM 7119 O  O    . HOH   G 5 .   ? 52.599 -35.631 -8.705  1.00 29.18 ?  303  HOH   B O    1 
HETATM 7120 O  O    . HOH   G 5 .   ? 57.649 -22.098 3.079   1.00 25.78 ?  304  HOH   B O    1 
HETATM 7121 O  O    . HOH   G 5 .   ? 62.815 -20.147 -0.880  1.00 38.30 ?  305  HOH   B O    1 
HETATM 7122 O  O    . HOH   G 5 .   ? 35.076 -33.591 4.511   1.00 27.86 ?  306  HOH   B O    1 
HETATM 7123 O  O    . HOH   G 5 .   ? 51.648 -5.900  -7.932  1.00 48.54 ?  307  HOH   B O    1 
HETATM 7124 O  O    . HOH   G 5 .   ? 42.737 -12.172 -18.499 1.00 27.07 ?  308  HOH   B O    1 
HETATM 7125 O  O    . HOH   G 5 .   ? 40.239 -10.825 -9.517  1.00 15.77 ?  309  HOH   B O    1 
HETATM 7126 O  O    . HOH   G 5 .   ? 49.983 -24.668 5.833   1.00 33.46 ?  310  HOH   B O    1 
HETATM 7127 O  O    . HOH   G 5 .   ? 44.023 -29.359 -4.709  1.00 21.89 ?  311  HOH   B O    1 
HETATM 7128 O  O    . HOH   G 5 .   ? 45.897 -40.403 -3.639  1.00 29.45 ?  312  HOH   B O    1 
HETATM 7129 O  O    . HOH   G 5 .   ? 62.712 -13.595 4.749   1.00 26.39 ?  313  HOH   B O    1 
HETATM 7130 O  O    . HOH   G 5 .   ? 53.246 -16.104 -12.699 1.00 28.28 ?  314  HOH   B O    1 
HETATM 7131 O  O    . HOH   G 5 .   ? 41.737 -8.089  1.327   1.00 22.66 ?  315  HOH   B O    1 
HETATM 7132 O  O    . HOH   G 5 .   ? 52.500 -29.172 -13.107 1.00 23.19 ?  316  HOH   B O    1 
HETATM 7133 O  O    . HOH   G 5 .   ? 45.755 -36.270 -16.125 1.00 35.32 ?  317  HOH   B O    1 
HETATM 7134 O  O    . HOH   G 5 .   ? 37.829 -10.229 -10.714 1.00 15.79 ?  318  HOH   B O    1 
HETATM 7135 O  O    . HOH   G 5 .   ? 32.825 -34.594 -5.939  1.00 15.60 ?  319  HOH   B O    1 
HETATM 7136 O  O    . HOH   G 5 .   ? 37.147 -30.498 -21.054 1.00 28.50 ?  320  HOH   B O    1 
HETATM 7137 O  O    . HOH   G 5 .   ? 43.244 -21.437 10.669  1.00 14.43 ?  321  HOH   B O    1 
HETATM 7138 O  O    . HOH   G 5 .   ? 41.258 -24.537 15.789  1.00 41.40 ?  322  HOH   B O    1 
HETATM 7139 O  O    . HOH   G 5 .   ? 38.378 -12.787 7.922   1.00 17.05 ?  323  HOH   B O    1 
HETATM 7140 O  O    . HOH   G 5 .   ? 26.341 -21.035 -6.252  1.00 14.83 ?  324  HOH   B O    1 
HETATM 7141 O  O    . HOH   G 5 .   ? 48.087 -32.579 -16.731 1.00 41.23 ?  325  HOH   B O    1 
HETATM 7142 O  O    . HOH   G 5 .   ? 53.659 -12.551 -22.276 1.00 34.77 ?  326  HOH   B O    1 
HETATM 7143 O  O    . HOH   G 5 .   ? 44.622 -24.611 9.557   1.00 17.94 ?  327  HOH   B O    1 
HETATM 7144 O  O    . HOH   G 5 .   ? 59.884 -17.253 -10.581 1.00 33.53 ?  328  HOH   B O    1 
HETATM 7145 O  O    . HOH   G 5 .   ? 36.744 -12.419 4.287   1.00 17.43 ?  329  HOH   B O    1 
HETATM 7146 O  O    . HOH   G 5 .   ? 43.117 -34.591 0.052   1.00 19.87 ?  330  HOH   B O    1 
HETATM 7147 O  O    . HOH   G 5 .   ? 38.347 -9.349  -13.268 1.00 28.17 ?  331  HOH   B O    1 
HETATM 7148 O  O    . HOH   G 5 .   ? 51.463 -32.979 -10.895 1.00 39.77 ?  332  HOH   B O    1 
HETATM 7149 O  O    . HOH   G 5 .   ? 44.123 -1.724  7.583   1.00 42.86 ?  333  HOH   B O    1 
HETATM 7150 O  O    . HOH   G 5 .   ? 33.671 -31.149 11.100  1.00 34.84 ?  334  HOH   B O    1 
HETATM 7151 O  O    . HOH   G 5 .   ? 47.201 -24.522 8.141   1.00 24.46 ?  335  HOH   B O    1 
HETATM 7152 O  O    . HOH   G 5 .   ? 42.861 -43.457 -14.460 1.00 42.01 ?  336  HOH   B O    1 
HETATM 7153 O  O    . HOH   G 5 .   ? 27.821 -14.699 -9.469  1.00 35.63 ?  337  HOH   B O    1 
HETATM 7154 O  O    . HOH   G 5 .   ? 48.565 -11.875 -13.865 1.00 25.50 ?  338  HOH   B O    1 
HETATM 7155 O  O    . HOH   G 5 .   ? 47.469 -27.435 1.985   1.00 13.43 ?  339  HOH   B O    1 
HETATM 7156 O  O    . HOH   G 5 .   ? 39.447 -23.546 -20.351 1.00 37.48 ?  340  HOH   B O    1 
HETATM 7157 O  O    . HOH   G 5 .   ? 46.861 -19.936 12.264  1.00 29.02 ?  341  HOH   B O    1 
HETATM 7158 O  O    . HOH   G 5 .   ? 28.856 -42.887 -12.388 1.00 37.19 ?  342  HOH   B O    1 
HETATM 7159 O  O    . HOH   G 5 .   ? 36.976 -14.966 -16.500 1.00 38.05 ?  343  HOH   B O    1 
HETATM 7160 O  O    . HOH   G 5 .   ? 38.383 -12.245 -16.249 1.00 41.62 ?  344  HOH   B O    1 
HETATM 7161 O  O    . HOH   G 5 .   ? 39.790 -44.189 -11.262 1.00 38.61 ?  345  HOH   B O    1 
HETATM 7162 O  O    . HOH   G 5 .   ? 33.012 -14.685 1.050   1.00 19.28 ?  346  HOH   B O    1 
HETATM 7163 O  O    . HOH   G 5 .   ? 37.010 -45.254 -9.701  1.00 36.75 ?  347  HOH   B O    1 
HETATM 7164 O  O    . HOH   G 5 .   ? 38.627 -22.311 15.049  1.00 40.15 ?  348  HOH   B O    1 
HETATM 7165 O  O    . HOH   G 5 .   ? 44.184 -37.377 -17.867 1.00 29.99 ?  349  HOH   B O    1 
HETATM 7166 O  O    . HOH   G 5 .   ? 33.722 -9.432  -8.803  1.00 29.45 ?  350  HOH   B O    1 
HETATM 7167 O  O    . HOH   G 5 .   ? 40.390 -43.462 -9.137  1.00 25.21 ?  351  HOH   B O    1 
HETATM 7168 O  O    . HOH   G 5 .   ? 27.758 -26.600 -0.582  1.00 27.68 ?  352  HOH   B O    1 
HETATM 7169 O  O    . HOH   G 5 .   ? 55.648 -8.264  10.784  1.00 24.54 ?  353  HOH   B O    1 
HETATM 7170 O  O    . HOH   G 5 .   ? 62.535 -20.082 -4.917  1.00 45.85 ?  354  HOH   B O    1 
HETATM 7171 O  O    . HOH   G 5 .   ? 23.253 -23.702 6.809   1.00 35.66 ?  355  HOH   B O    1 
HETATM 7172 O  O    . HOH   G 5 .   ? 34.650 -10.327 7.500   1.00 22.46 ?  356  HOH   B O    1 
HETATM 7173 O  O    . HOH   G 5 .   ? 56.622 -7.298  3.065   1.00 26.32 ?  357  HOH   B O    1 
HETATM 7174 O  O    . HOH   G 5 .   ? 36.150 -8.473  -9.707  1.00 33.70 ?  358  HOH   B O    1 
HETATM 7175 O  O    . HOH   G 5 .   ? 34.064 -7.849  11.537  1.00 40.41 ?  359  HOH   B O    1 
HETATM 7176 O  O    . HOH   G 5 .   ? 43.111 -12.709 -21.236 1.00 40.72 ?  360  HOH   B O    1 
HETATM 7177 O  O    . HOH   G 5 .   ? 61.494 -19.870 1.610   1.00 32.29 ?  361  HOH   B O    1 
HETATM 7178 O  O    . HOH   G 5 .   ? 56.879 -21.493 -16.442 1.00 40.64 ?  362  HOH   B O    1 
HETATM 7179 O  O    . HOH   G 5 .   ? 27.164 -25.950 -11.370 1.00 31.87 ?  363  HOH   B O    1 
HETATM 7180 O  O    . HOH   G 5 .   ? 40.269 -8.839  9.876   1.00 38.32 ?  364  HOH   B O    1 
HETATM 7181 O  O    . HOH   G 5 .   ? 32.537 -23.600 14.056  1.00 39.15 ?  365  HOH   B O    1 
HETATM 7182 O  O    . HOH   G 5 .   ? 54.276 -5.780  2.967   1.00 35.80 ?  366  HOH   B O    1 
HETATM 7183 O  O    . HOH   G 5 .   ? 48.391 -26.537 8.782   1.00 38.79 ?  367  HOH   B O    1 
HETATM 7184 O  O    . HOH   G 5 .   ? 59.082 -10.542 9.051   1.00 41.44 ?  368  HOH   B O    1 
HETATM 7185 O  O    . HOH   G 5 .   ? 39.891 -7.097  7.821   1.00 41.65 ?  369  HOH   B O    1 
HETATM 7186 O  O    . HOH   G 5 .   ? 40.041 -11.356 -13.931 1.00 29.20 ?  370  HOH   B O    1 
HETATM 7187 O  O    . HOH   G 5 .   ? 36.286 -8.730  8.924   1.00 36.92 ?  371  HOH   B O    1 
HETATM 7188 O  O    . HOH   G 5 .   ? 41.847 -9.974  -17.425 1.00 52.88 ?  372  HOH   B O    1 
HETATM 7189 O  O    . HOH   G 5 .   ? 55.978 -7.796  -0.591  1.00 36.79 ?  373  HOH   B O    1 
HETATM 7190 O  O    . HOH   G 5 .   ? 52.029 -12.891 13.308  1.00 29.57 ?  374  HOH   B O    1 
HETATM 7191 O  O    . HOH   G 5 .   ? 41.891 -6.801  -4.874  1.00 47.13 ?  375  HOH   B O    1 
HETATM 7192 O  O    . HOH   G 5 .   ? 63.053 -12.430 6.937   1.00 35.34 ?  376  HOH   B O    1 
HETATM 7193 O  O    . HOH   G 5 .   ? 38.069 -10.592 10.035  1.00 29.24 ?  377  HOH   B O    1 
HETATM 7194 O  O    . HOH   G 5 .   ? 44.027 -5.596  -3.531  1.00 44.76 ?  378  HOH   B O    1 
HETATM 7195 O  O    . HOH   G 5 .   ? 36.518 -22.837 13.296  1.00 22.91 ?  379  HOH   B O    1 
HETATM 7196 O  O    . HOH   G 5 .   ? 42.659 -17.102 -23.190 1.00 40.18 ?  380  HOH   B O    1 
HETATM 7197 O  O    . HOH   G 5 .   ? 40.250 -7.653  3.177   1.00 37.08 ?  381  HOH   B O    1 
HETATM 7198 O  O    . HOH   G 5 .   ? 39.645 -14.050 15.675  1.00 50.60 ?  382  HOH   B O    1 
HETATM 7199 O  O    . HOH   G 5 .   ? 52.845 -29.905 7.150   1.00 21.77 ?  383  HOH   B O    1 
HETATM 7200 O  O    . HOH   G 5 .   ? 60.476 -22.301 2.774   1.00 48.09 ?  384  HOH   B O    1 
HETATM 7201 O  O    . HOH   G 5 .   ? 35.451 -33.730 7.305   1.00 40.33 ?  385  HOH   B O    1 
HETATM 7202 O  O    . HOH   G 5 .   ? 23.919 -20.852 -7.637  1.00 25.81 ?  386  HOH   B O    1 
HETATM 7203 O  O    . HOH   G 5 .   ? 25.779 -18.835 -11.927 1.00 38.74 ?  387  HOH   B O    1 
HETATM 7204 O  O    . HOH   G 5 .   ? 46.821 -5.322  2.917   1.00 41.17 ?  388  HOH   B O    1 
HETATM 7205 O  O    . HOH   G 5 .   ? 35.281 -20.340 13.316  1.00 29.36 ?  389  HOH   B O    1 
HETATM 7206 O  O    . HOH   G 5 .   ? 40.729 -6.634  -0.842  1.00 23.38 ?  390  HOH   B O    1 
HETATM 7207 O  O    . HOH   G 5 .   ? 44.154 -31.696 -3.846  1.00 33.65 ?  391  HOH   B O    1 
HETATM 7208 O  O    . HOH   G 5 .   ? 40.921 -9.706  15.856  1.00 47.65 ?  392  HOH   B O    1 
HETATM 7209 O  O    . HOH   G 5 .   ? 27.934 -27.057 2.266   1.00 32.61 ?  393  HOH   B O    1 
HETATM 7210 O  O    . HOH   G 5 .   ? 26.612 -27.931 -13.410 1.00 35.47 ?  394  HOH   B O    1 
HETATM 7211 O  O    . HOH   G 5 .   ? 24.563 -20.622 -10.451 1.00 35.77 ?  395  HOH   B O    1 
HETATM 7212 O  O    . HOH   G 5 .   ? 50.630 -30.815 8.656   1.00 26.43 ?  396  HOH   B O    1 
HETATM 7213 O  O    . HOH   G 5 .   ? 34.423 -33.489 9.607   1.00 31.07 ?  397  HOH   B O    1 
HETATM 7214 O  O    . HOH   G 5 .   ? 26.841 -30.612 -12.686 1.00 26.81 ?  398  HOH   B O    1 
HETATM 7215 O  O    . HOH   G 5 .   ? 45.758 -20.188 15.194  1.00 52.13 ?  399  HOH   B O    1 
HETATM 7216 O  O    . HOH   G 5 .   ? 57.609 -6.481  -2.332  1.00 33.10 ?  400  HOH   B O    1 
HETATM 7217 O  O    . HOH   G 5 .   ? 40.784 -11.810 -22.376 1.00 43.91 ?  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   ? 0.4309 0.4707 0.5191 -0.0431 -0.0143 0.1102  3    VAL   A N   
2    N  N   B VAL   A 3   ? 0.5500 0.5697 0.6258 0.0296  0.0194  0.0585  3    VAL   A N   
3    C  CA  A VAL   A 3   ? 0.4274 0.4686 0.5083 -0.0450 -0.0127 0.1098  3    VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.5495 0.5692 0.6241 0.0294  0.0188  0.0588  3    VAL   A CA  
5    C  C   A VAL   A 3   ? 0.4089 0.4580 0.4732 -0.0529 -0.0138 0.1133  3    VAL   A C   
6    C  C   B VAL   A 3   ? 0.5433 0.5661 0.6079 0.0278  0.0129  0.0581  3    VAL   A C   
7    O  O   A VAL   A 3   ? 0.4128 0.4601 0.4852 -0.0511 -0.0147 0.1151  3    VAL   A O   
8    O  O   B VAL   A 3   ? 0.5450 0.5675 0.6158 0.0280  0.0102  0.0598  3    VAL   A O   
9    C  CB  A VAL   A 3   ? 0.4404 0.4753 0.5224 -0.0410 -0.0102 0.1068  3    VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.5539 0.5713 0.6350 0.0296  0.0233  0.0593  3    VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.4453 0.4776 0.5259 -0.0393 -0.0097 0.1054  3    VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.5553 0.5719 0.6386 0.0294  0.0247  0.0593  3    VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.4447 0.4779 0.5257 -0.0399 -0.0089 0.1071  3    VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.5560 0.5723 0.6388 0.0293  0.0248  0.0596  3    VAL   A CG2 
31   N  N   A ASN   A 4   ? 0.3837 0.4437 0.4155 -0.0629 -0.0128 0.1144  4    ASN   A N   
32   N  N   B ASN   A 4   ? 0.5343 0.5604 0.5784 0.0252  0.0096  0.0555  4    ASN   A N   
33   C  CA  A ASN   A 4   ? 0.3567 0.4282 0.3524 -0.0736 -0.0112 0.1124  4    ASN   A CA  
34   C  CA  B ASN   A 4   ? 0.5233 0.5532 0.5448 0.0219  0.0065  0.0520  4    ASN   A CA  
35   C  C   A ASN   A 4   ? 0.3292 0.4141 0.3079 -0.0824 -0.0051 0.0912  4    ASN   A C   
36   C  C   B ASN   A 4   ? 0.4991 0.5358 0.5106 0.0129  0.0101  0.0398  4    ASN   A C   
37   O  O   A ASN   A 4   ? 0.3283 0.4134 0.2997 -0.0837 -0.0054 0.0967  4    ASN   A O   
38   O  O   B ASN   A 4   ? 0.5029 0.5394 0.5090 0.0139  0.0106  0.0392  4    ASN   A O   
39   C  CB  A ASN   A 4   ? 0.3560 0.4264 0.3286 -0.0749 -0.0178 0.1300  4    ASN   A CB  
40   C  CB  B ASN   A 4   ? 0.5339 0.5603 0.5431 0.0270  0.0006  0.0599  4    ASN   A CB  
41   C  CG  A ASN   A 4   ? 0.3535 0.4236 0.3048 -0.0771 -0.0267 0.1466  4    ASN   A CG  
42   C  CG  B ASN   A 4   ? 0.5421 0.5652 0.5408 0.0308  -0.0058 0.0669  4    ASN   A CG  
43   O  OD1 A ASN   A 4   ? 0.3558 0.4225 0.3035 -0.0752 -0.0336 0.1496  4    ASN   A OD1 
44   O  OD1 B ASN   A 4   ? 0.5452 0.5669 0.5425 0.0324  -0.0079 0.0697  4    ASN   A OD1 
45   N  ND2 A ASN   A 4   ? 0.3500 0.4220 0.2961 -0.0781 -0.0308 0.1573  4    ASN   A ND2 
46   N  ND2 B ASN   A 4   ? 0.5447 0.5671 0.5374 0.0321  -0.0091 0.0696  4    ASN   A ND2 
59   N  N   A SER   A 5   ? 0.3036 0.3984 0.2726 -0.0893 0.0017  0.0637  5    SER   A N   
60   N  N   B SER   A 5   ? 0.4681 0.5127 0.4786 0.0029  0.0134  0.0286  5    SER   A N   
61   C  CA  A SER   A 5   ? 0.2829 0.3850 0.2460 -0.0903 0.0094  0.0307  5    SER   A CA  
62   C  CA  B SER   A 5   ? 0.4347 0.4878 0.4442 -0.0086 0.0221  0.0186  5    SER   A CA  
63   C  C   A SER   A 5   ? 0.2612 0.3631 0.2134 -0.0854 0.0131  0.0012  5    SER   A C   
64   C  C   B SER   A 5   ? 0.3944 0.4521 0.4039 -0.0216 0.0316  0.0098  5    SER   A C   
65   O  O   A SER   A 5   ? 0.2678 0.3698 0.2125 -0.0767 0.0085  -0.0162 5    SER   A O   
66   O  O   B SER   A 5   ? 0.3948 0.4548 0.4078 -0.0220 0.0333  0.0051  5    SER   A O   
67   C  CB  A SER   A 5   ? 0.2870 0.3933 0.2567 -0.0927 0.0104  0.0265  5    SER   A CB  
68   C  CB  B SER   A 5   ? 0.4399 0.4964 0.4521 -0.0078 0.0238  0.0188  5    SER   A CB  
69   O  OG  A SER   A 5   ? 0.2897 0.3990 0.2680 -0.0937 0.0112  0.0259  5    SER   A OG  
70   O  OG  B SER   A 5   ? 0.4427 0.4987 0.4546 -0.0076 0.0264  0.0181  5    SER   A OG  
81   N  N   A PHE   A 6   ? 0.2317 0.3319 0.1845 -0.0895 0.0298  -0.0055 6    PHE   A N   
82   N  N   B PHE   A 6   ? 0.3528 0.4132 0.3550 -0.0353 0.0401  0.0085  6    PHE   A N   
83   C  CA  A PHE   A 6   ? 0.2103 0.2996 0.1601 -0.0875 0.0405  -0.0018 6    PHE   A CA  
84   C  CA  B PHE   A 6   ? 0.3121 0.3716 0.3025 -0.0497 0.0497  0.0088  6    PHE   A CA  
85   C  C   A PHE   A 6   ? 0.2071 0.2971 0.1633 -0.0914 0.0530  -0.0062 6    PHE   A C   
86   C  C   B PHE   A 6   ? 0.2992 0.3597 0.2977 -0.0565 0.0607  -0.0004 6    PHE   A C   
87   O  O   A PHE   A 6   ? 0.2105 0.3009 0.1694 -0.0978 0.0524  -0.0027 6    PHE   A O   
88   O  O   B PHE   A 6   ? 0.3015 0.3613 0.3087 -0.0598 0.0617  0.0036  6    PHE   A O   
89   C  CB  A PHE   A 6   ? 0.1978 0.2717 0.1533 -0.0750 0.0407  0.0079  6    PHE   A CB  
90   C  CB  B PHE   A 6   ? 0.2865 0.3414 0.2600 -0.0539 0.0451  0.0137  6    PHE   A CB  
91   C  CG  A PHE   A 6   ? 0.1890 0.2497 0.1459 -0.0638 0.0413  0.0227  6    PHE   A CG  
92   C  CG  B PHE   A 6   ? 0.2639 0.3150 0.2191 -0.0570 0.0424  0.0165  6    PHE   A CG  
93   C  CD1 A PHE   A 6   ? 0.1871 0.2427 0.1479 -0.0541 0.0319  0.0228  6    PHE   A CD1 
94   C  CD1 B PHE   A 6   ? 0.2527 0.3044 0.1975 -0.0565 0.0397  0.0186  6    PHE   A CD1 
95   C  CD2 A PHE   A 6   ? 0.1970 0.2442 0.1687 -0.0473 0.0383  0.0244  6    PHE   A CD2 
96   C  CD2 B PHE   A 6   ? 0.2601 0.3051 0.2173 -0.0534 0.0395  0.0128  6    PHE   A CD2 
97   C  CE1 A PHE   A 6   ? 0.1871 0.2358 0.1587 -0.0520 0.0297  0.0264  6    PHE   A CE1 
98   C  CE1 B PHE   A 6   ? 0.2463 0.2960 0.1915 -0.0581 0.0401  0.0177  6    PHE   A CE1 
99   C  CE2 A PHE   A 6   ? 0.1968 0.2404 0.1794 -0.0412 0.0310  0.0193  6    PHE   A CE2 
100  C  CE2 B PHE   A 6   ? 0.2534 0.2974 0.2105 -0.0535 0.0366  0.0089  6    PHE   A CE2 
101  C  CZ  A PHE   A 6   ? 0.1920 0.2352 0.1697 -0.0492 0.0304  0.0228  6    PHE   A CZ  
102  C  CZ  B PHE   A 6   ? 0.2485 0.2937 0.1962 -0.0573 0.0389  0.0116  6    PHE   A CZ  
121  N  N   A SER   A 7   ? 0.2011 0.2884 0.1786 -0.0891 0.0676  -0.0057 7    SER   A N   
122  N  N   B SER   A 7   ? 0.2816 0.3441 0.2768 -0.0592 0.0686  -0.0128 7    SER   A N   
123  C  CA  A SER   A 7   ? 0.2023 0.2819 0.2049 -0.0832 0.0658  -0.0191 7    SER   A CA  
124  C  CA  B SER   A 7   ? 0.2718 0.3336 0.2698 -0.0559 0.0676  -0.0282 7    SER   A CA  
125  C  C   A SER   A 7   ? 0.1860 0.2513 0.1882 -0.0838 0.0721  -0.0231 7    SER   A C   
126  C  C   B SER   A 7   ? 0.2540 0.3136 0.2503 -0.0489 0.0679  -0.0257 7    SER   A C   
127  O  O   A SER   A 7   ? 0.1955 0.2395 0.1886 -0.0928 0.0697  -0.0243 7    SER   A O   
128  O  O   B SER   A 7   ? 0.2589 0.3139 0.2440 -0.0481 0.0602  -0.0256 7    SER   A O   
129  C  CB  A SER   A 7   ? 0.2196 0.3019 0.2478 -0.0724 0.0596  -0.0201 7    SER   A CB  
130  C  CB  B SER   A 7   ? 0.2785 0.3411 0.2816 -0.0599 0.0678  -0.0409 7    SER   A CB  
131  O  OG  A SER   A 7   ? 0.2319 0.3107 0.2801 -0.0676 0.0567  -0.0185 7    SER   A OG  
132  O  OG  B SER   A 7   ? 0.2829 0.3419 0.2962 -0.0629 0.0662  -0.0480 7    SER   A OG  
143  N  N   A GLY   A 8   ? 0.1695 0.2329 0.1855 -0.0749 0.0593  -0.0286 8    GLY   A N   
144  N  N   B GLY   A 8   ? 0.2374 0.2953 0.2378 -0.0438 0.0687  -0.0227 8    GLY   A N   
145  C  CA  A GLY   A 8   ? 0.1602 0.2154 0.1828 -0.0541 0.0554  -0.0302 8    GLY   A CA  
146  C  CA  B GLY   A 8   ? 0.2180 0.2728 0.2258 -0.0394 0.0677  -0.0175 8    GLY   A CA  
147  C  C   A GLY   A 8   ? 0.1508 0.2019 0.1758 -0.0332 0.0441  -0.0246 8    GLY   A C   
148  C  C   B GLY   A 8   ? 0.2009 0.2510 0.2071 -0.0351 0.0586  -0.0141 8    GLY   A C   
149  O  O   A GLY   A 8   ? 0.1548 0.2038 0.1906 -0.0186 0.0339  -0.0275 8    GLY   A O   
150  O  O   B GLY   A 8   ? 0.2035 0.2532 0.2285 -0.0296 0.0589  -0.0208 8    GLY   A O   
157  N  N   A TYR   A 9   ? 0.1401 0.1905 0.1568 -0.0256 0.0395  -0.0116 9    TYR   A N   
158  N  N   B TYR   A 9   ? 0.1804 0.2279 0.1850 -0.0331 0.0440  -0.0027 9    TYR   A N   
159  C  CA  A TYR   A 9   ? 0.1410 0.1814 0.1425 -0.0238 0.0348  -0.0025 9    TYR   A CA  
160  C  CA  B TYR   A 9   ? 0.1670 0.2076 0.1683 -0.0270 0.0343  0.0139  9    TYR   A CA  
161  C  C   A TYR   A 9   ? 0.1495 0.1629 0.1460 -0.0203 0.0361  0.0062  9    TYR   A C   
162  C  C   B TYR   A 9   ? 0.1684 0.1830 0.1605 -0.0257 0.0401  0.0260  9    TYR   A C   
163  O  O   A TYR   A 9   ? 0.1731 0.1762 0.1461 -0.0240 0.0397  -0.0012 9    TYR   A O   
164  O  O   B TYR   A 9   ? 0.1827 0.1931 0.1694 -0.0249 0.0489  0.0247  9    TYR   A O   
165  C  CB  A TYR   A 9   ? 0.1374 0.1960 0.1519 -0.0137 0.0294  -0.0075 9    TYR   A CB  
166  C  CB  B TYR   A 9   ? 0.1533 0.2188 0.1756 -0.0161 0.0171  0.0106  9    TYR   A CB  
167  C  CG  A TYR   A 9   ? 0.1350 0.2062 0.1612 -0.0094 0.0397  -0.0183 9    TYR   A CG  
168  C  CG  B TYR   A 9   ? 0.1414 0.2251 0.1698 -0.0140 0.0131  0.0008  9    TYR   A CG  
169  C  CD1 A TYR   A 9   ? 0.1391 0.2160 0.1733 -0.0153 0.0490  -0.0232 9    TYR   A CD1 
170  C  CD1 B TYR   A 9   ? 0.1406 0.2328 0.1769 -0.0198 0.0148  -0.0050 9    TYR   A CD1 
171  C  CD2 A TYR   A 9   ? 0.1317 0.2031 0.1697 -0.0140 0.0328  -0.0087 9    TYR   A CD2 
172  C  CD2 B TYR   A 9   ? 0.1363 0.2224 0.1708 -0.0123 0.0075  -0.0015 9    TYR   A CD2 
173  C  CE1 A TYR   A 9   ? 0.1395 0.2184 0.1822 -0.0198 0.0493  -0.0299 9    TYR   A CE1 
174  C  CE1 B TYR   A 9   ? 0.1440 0.2347 0.1881 -0.0231 0.0173  -0.0174 9    TYR   A CE1 
175  C  CE2 A TYR   A 9   ? 0.1306 0.2077 0.1771 -0.0195 0.0384  -0.0160 9    TYR   A CE2 
176  C  CE2 B TYR   A 9   ? 0.1380 0.2262 0.1782 -0.0152 0.0181  -0.0128 9    TYR   A CE2 
177  C  CZ  A TYR   A 9   ? 0.1282 0.2159 0.1872 -0.0284 0.0489  -0.0227 9    TYR   A CZ  
178  C  CZ  B TYR   A 9   ? 0.1426 0.2341 0.1941 -0.0243 0.0238  -0.0179 9    TYR   A CZ  
179  O  OH  A TYR   A 9   ? 0.1251 0.2232 0.2070 -0.0413 0.0488  -0.0285 9    TYR   A OH  
180  O  OH  B TYR   A 9   ? 0.1579 0.2425 0.2221 -0.0320 0.0287  -0.0210 9    TYR   A OH  
199  N  N   A LEU   A 10  ? 0.1398 0.1408 0.1601 -0.0154 0.0238  0.0045  10   LEU   A N   
200  N  N   B LEU   A 10  ? 0.1611 0.1620 0.1568 -0.0242 0.0252  0.0302  10   LEU   A N   
201  C  CA  A LEU   A 10  ? 0.1275 0.1368 0.1580 -0.0152 0.0231  0.0176  10   LEU   A CA  
202  C  CA  B LEU   A 10  ? 0.1509 0.1571 0.1550 -0.0254 0.0261  0.0272  10   LEU   A CA  
203  C  C   A LEU   A 10  ? 0.1194 0.1307 0.1649 -0.0174 0.0298  0.0213  10   LEU   A C   
204  C  C   B LEU   A 10  ? 0.1452 0.1484 0.1416 -0.0284 0.0197  0.0358  10   LEU   A C   
205  O  O   A LEU   A 10  ? 0.1218 0.1286 0.1785 -0.0105 0.0384  0.0236  10   LEU   A O   
206  O  O   B LEU   A 10  ? 0.1514 0.1493 0.1569 -0.0250 0.0320  0.0427  10   LEU   A O   
207  C  CB  A LEU   A 10  ? 0.1306 0.1437 0.1765 -0.0085 0.0189  0.0180  10   LEU   A CB  
208  C  CB  B LEU   A 10  ? 0.1534 0.1567 0.1806 -0.0274 0.0183  0.0296  10   LEU   A CB  
209  C  CG  A LEU   A 10  ? 0.1489 0.1549 0.2036 -0.0094 0.0089  0.0214  10   LEU   A CG  
210  C  CG  B LEU   A 10  ? 0.1654 0.1652 0.2124 -0.0206 0.0023  0.0206  10   LEU   A CG  
211  C  CD1 A LEU   A 10  ? 0.1594 0.1600 0.2184 -0.0130 0.0114  0.0262  10   LEU   A CD1 
212  C  CD1 B LEU   A 10  ? 0.1717 0.1718 0.2346 -0.0286 -0.0024 0.0170  10   LEU   A CD1 
213  C  CD2 A LEU   A 10  ? 0.1550 0.1622 0.2066 -0.0034 0.0142  0.0055  10   LEU   A CD2 
214  C  CD2 B LEU   A 10  ? 0.1790 0.1791 0.2386 -0.0123 -0.0017 0.0162  10   LEU   A CD2 
237  N  N   A LYS   A 11  ? 0.1251 0.1314 0.1630 -0.0219 0.0378  0.0194  11   LYS   A N   
238  N  N   B LYS   A 11  ? 0.1477 0.1454 0.1341 -0.0333 0.0093  0.0342  11   LYS   A N   
239  C  CA  A LYS   A 11  ? 0.1268 0.1279 0.1664 -0.0231 0.0363  0.0152  11   LYS   A CA  
240  C  CA  B LYS   A 11  ? 0.1525 0.1406 0.1404 -0.0309 0.0086  0.0296  11   LYS   A CA  
241  C  C   A LYS   A 11  ? 0.1227 0.1242 0.1644 -0.0181 0.0350  0.0068  11   LYS   A C   
242  C  C   B LYS   A 11  ? 0.1393 0.1302 0.1321 -0.0334 0.0176  0.0219  11   LYS   A C   
243  O  O   A LYS   A 11  ? 0.1250 0.1336 0.1890 -0.0310 0.0417  -0.0041 11   LYS   A O   
244  O  O   B LYS   A 11  ? 0.1332 0.1321 0.1610 -0.0395 0.0207  -0.0058 11   LYS   A O   
245  C  CB  A LYS   A 11  ? 0.1393 0.1340 0.1632 -0.0239 0.0355  0.0159  11   LYS   A CB  
246  C  CB  B LYS   A 11  ? 0.1703 0.1412 0.1385 -0.0268 0.0033  0.0294  11   LYS   A CB  
247  C  CG  A LYS   A 11  ? 0.1527 0.1306 0.1697 -0.0279 0.0384  0.0209  11   LYS   A CG  
248  C  CG  B LYS   A 11  ? 0.1827 0.1401 0.1351 -0.0271 -0.0009 0.0302  11   LYS   A CG  
249  C  CD  A LYS   A 11  ? 0.1686 0.1350 0.1746 -0.0224 0.0329  0.0232  11   LYS   A CD  
250  C  CD  B LYS   A 11  ? 0.1936 0.1470 0.1360 -0.0207 -0.0075 0.0342  11   LYS   A CD  
251  C  CE  A LYS   A 11  ? 0.1752 0.1265 0.1766 -0.0275 0.0254  0.0222  11   LYS   A CE  
252  C  CE  B LYS   A 11  ? 0.2003 0.1449 0.1355 -0.0177 -0.0096 0.0418  11   LYS   A CE  
253  N  NZ  A LYS   A 11  ? 0.1772 0.1253 0.1837 -0.0233 0.0052  0.0116  11   LYS   A NZ  
254  N  NZ  B LYS   A 11  ? 0.1993 0.1476 0.1404 -0.0111 -0.0212 0.0424  11   LYS   A NZ  
281  N  N   A LEU   A 12  ? 0.1194 0.1186 0.1440 -0.0214 0.0309  -0.0027 12   LEU   A N   
282  N  N   B LEU   A 12  ? 0.1306 0.1370 0.1302 -0.0232 0.0145  0.0189  12   LEU   A N   
283  C  CA  A LEU   A 12  ? 0.1268 0.1225 0.1411 -0.0163 0.0162  0.0012  12   LEU   A CA  
284  C  CA  B LEU   A 12  ? 0.1278 0.1422 0.1324 -0.0170 0.0167  0.0210  12   LEU   A CA  
285  C  C   A LEU   A 12  ? 0.1281 0.1176 0.1500 -0.0202 0.0159  0.0092  12   LEU   A C   
286  C  C   B LEU   A 12  ? 0.1282 0.1366 0.1394 -0.0142 0.0246  0.0228  12   LEU   A C   
287  O  O   A LEU   A 12  ? 0.1306 0.1165 0.1578 -0.0214 0.0154  -0.0037 12   LEU   A O   
288  O  O   B LEU   A 12  ? 0.1386 0.1322 0.1374 -0.0018 0.0179  0.0242  12   LEU   A O   
289  C  CB  A LEU   A 12  ? 0.1359 0.1217 0.1427 -0.0092 0.0049  0.0065  12   LEU   A CB  
290  C  CB  B LEU   A 12  ? 0.1332 0.1494 0.1438 -0.0154 0.0142  0.0184  12   LEU   A CB  
291  C  CG  A LEU   A 12  ? 0.1462 0.1247 0.1565 0.0019  0.0097  0.0083  12   LEU   A CG  
292  C  CG  B LEU   A 12  ? 0.1384 0.1537 0.1611 -0.0128 0.0209  0.0120  12   LEU   A CG  
293  C  CD1 A LEU   A 12  ? 0.1570 0.1275 0.1702 0.0138  0.0116  0.0222  12   LEU   A CD1 
294  C  CD1 B LEU   A 12  ? 0.1519 0.1605 0.1740 -0.0078 0.0267  0.0102  12   LEU   A CD1 
295  C  CD2 A LEU   A 12  ? 0.1501 0.1299 0.1721 0.0122  0.0093  0.0033  12   LEU   A CD2 
296  C  CD2 B LEU   A 12  ? 0.1387 0.1552 0.1756 -0.0145 0.0120  -0.0006 12   LEU   A CD2 
319  N  N   A THR   A 13  ? 0.1250 0.1205 0.1505 -0.0140 0.0126  0.0118  13   THR   A N   
320  N  N   B THR   A 13  ? 0.1195 0.1301 0.1465 -0.0132 0.0229  0.0166  13   THR   A N   
321  C  CA  A THR   A 13  ? 0.1281 0.1253 0.1544 -0.0046 0.0181  0.0113  13   THR   A CA  
322  C  CA  B THR   A 13  ? 0.1231 0.1308 0.1550 -0.0182 0.0262  0.0185  13   THR   A CA  
323  C  C   A THR   A 13  ? 0.1235 0.1268 0.1591 -0.0039 0.0137  0.0201  13   THR   A C   
324  C  C   B THR   A 13  ? 0.1250 0.1391 0.1636 -0.0243 0.0253  0.0318  13   THR   A C   
325  O  O   A THR   A 13  ? 0.1246 0.1252 0.1661 -0.0008 0.0207  0.0175  13   THR   A O   
326  O  O   B THR   A 13  ? 0.1337 0.1375 0.1699 -0.0243 0.0106  0.0317  13   THR   A O   
327  C  CB  A THR   A 13  ? 0.1346 0.1326 0.1699 -0.0041 0.0264  0.0088  13   THR   A CB  
328  C  CB  B THR   A 13  ? 0.1240 0.1340 0.1659 -0.0107 0.0265  0.0210  13   THR   A CB  
329  O  OG1 A THR   A 13  ? 0.1403 0.1246 0.1849 -0.0088 0.0150  0.0034  13   THR   A OG1 
330  O  OG1 B THR   A 13  ? 0.1176 0.1356 0.1675 -0.0167 0.0316  0.0262  13   THR   A OG1 
331  C  CG2 A THR   A 13  ? 0.1390 0.1435 0.1817 -0.0018 0.0381  0.0017  13   THR   A CG2 
332  C  CG2 B THR   A 13  ? 0.1301 0.1443 0.1724 -0.0098 0.0321  0.0133  13   THR   A CG2 
347  N  N   A ASP   A 14  ? 0.1260 0.1348 0.1720 -0.0044 0.0128  0.0284  14   ASP   A N   
348  N  N   B ASP   A 14  ? 0.1286 0.1438 0.1801 -0.0270 0.0191  0.0453  14   ASP   A N   
349  C  CA  A ASP   A 14  ? 0.1292 0.1425 0.1951 -0.0058 0.0039  0.0405  14   ASP   A CA  
350  C  CA  B ASP   A 14  ? 0.1346 0.1535 0.1979 -0.0252 0.0109  0.0621  14   ASP   A CA  
351  C  C   A ASP   A 14  ? 0.1289 0.1405 0.1827 -0.0091 -0.0005 0.0427  14   ASP   A C   
352  C  C   B ASP   A 14  ? 0.1330 0.1452 0.1910 -0.0211 0.0024  0.0603  14   ASP   A C   
353  O  O   A ASP   A 14  ? 0.1351 0.1449 0.1784 -0.0041 -0.0095 0.0456  14   ASP   A O   
354  O  O   B ASP   A 14  ? 0.1423 0.1504 0.2028 -0.0222 -0.0021 0.0669  14   ASP   A O   
355  C  CB  A ASP   A 14  ? 0.1443 0.1656 0.2462 -0.0160 0.0004  0.0528  14   ASP   A CB  
356  C  CB  B ASP   A 14  ? 0.1472 0.1723 0.2450 -0.0349 0.0057  0.0757  14   ASP   A CB  
357  C  CG  A ASP   A 14  ? 0.1621 0.2054 0.3195 -0.0250 -0.0030 0.0514  14   ASP   A CG  
358  C  CG  B ASP   A 14  ? 0.1508 0.2102 0.3103 -0.0439 -0.0045 0.0703  14   ASP   A CG  
359  O  OD1 A ASP   A 14  ? 0.1648 0.2201 0.3398 -0.0216 -0.0228 0.0560  14   ASP   A OD1 
360  O  OD1 B ASP   A 14  ? 0.1527 0.2167 0.3272 -0.0439 -0.0107 0.0731  14   ASP   A OD1 
361  O  OD2 A ASP   A 14  ? 0.1802 0.2241 0.3566 -0.0337 0.0042  0.0392  14   ASP   A OD2 
362  O  OD2 B ASP   A 14  ? 0.1592 0.2395 0.3502 -0.0441 -0.0104 0.0582  14   ASP   A OD2 
371  N  N   . ASN   A 15  ? 0.1270 0.1372 0.1820 -0.0224 0.0069  0.0481  15   ASN   A N   
372  C  CA  . ASN   A 15  ? 0.1302 0.1398 0.1881 -0.0168 -0.0036 0.0374  15   ASN   A CA  
373  C  C   . ASN   A 15  ? 0.1261 0.1323 0.1920 -0.0161 0.0034  0.0399  15   ASN   A C   
374  O  O   . ASN   A 15  ? 0.1314 0.1381 0.2472 -0.0152 -0.0178 0.0404  15   ASN   A O   
375  C  CB  . ASN   A 15  ? 0.1290 0.1394 0.1798 -0.0183 -0.0008 0.0378  15   ASN   A CB  
376  C  CG  . ASN   A 15  ? 0.1252 0.1455 0.1841 -0.0113 0.0050  0.0349  15   ASN   A CG  
377  O  OD1 . ASN   A 15  ? 0.1370 0.1520 0.2045 -0.0321 0.0008  0.0351  15   ASN   A OD1 
378  N  ND2 . ASN   A 15  ? 0.1313 0.1554 0.1752 -0.0203 0.0144  0.0295  15   ASN   A ND2 
386  N  N   A VAL   A 16  ? 0.1258 0.1267 0.1642 -0.0112 0.0085  0.0313  16   VAL   A N   
387  N  N   B VAL   A 16  ? 0.1310 0.1328 0.1743 -0.0130 -0.0013 0.0465  16   VAL   A N   
388  C  CA  A VAL   A 16  ? 0.1204 0.1249 0.1585 -0.0087 0.0123  0.0215  16   VAL   A CA  
389  C  CA  B VAL   A 16  ? 0.1305 0.1330 0.1545 -0.0127 0.0048  0.0470  16   VAL   A CA  
390  C  C   A VAL   A 16  ? 0.1145 0.1192 0.1427 -0.0133 0.0072  0.0231  16   VAL   A C   
391  C  C   B VAL   A 16  ? 0.1289 0.1372 0.1488 -0.0197 0.0059  0.0436  16   VAL   A C   
392  O  O   A VAL   A 16  ? 0.1088 0.1187 0.1328 -0.0180 0.0087  0.0152  16   VAL   A O   
393  O  O   B VAL   A 16  ? 0.1314 0.1431 0.1515 -0.0227 0.0117  0.0344  16   VAL   A O   
394  C  CB  A VAL   A 16  ? 0.1322 0.1359 0.1664 0.0039  0.0227  0.0189  16   VAL   A CB  
395  C  CB  B VAL   A 16  ? 0.1408 0.1342 0.1493 -0.0005 0.0193  0.0427  16   VAL   A CB  
396  C  CG1 A VAL   A 16  ? 0.1436 0.1372 0.1643 0.0089  0.0159  0.0043  16   VAL   A CG1 
397  C  CG1 B VAL   A 16  ? 0.1490 0.1309 0.1384 0.0011  0.0200  0.0362  16   VAL   A CG1 
398  C  CG2 A VAL   A 16  ? 0.1384 0.1524 0.1754 0.0062  0.0301  0.0181  16   VAL   A CG2 
399  C  CG2 B VAL   A 16  ? 0.1453 0.1496 0.1699 0.0075  0.0324  0.0385  16   VAL   A CG2 
418  N  N   A TYR   A 17  ? 0.1147 0.1156 0.1419 -0.0109 0.0205  0.0181  17   TYR   A N   
419  N  N   B TYR   A 17  ? 0.1286 0.1298 0.1535 -0.0250 0.0030  0.0374  17   TYR   A N   
420  C  CA  A TYR   A 17  ? 0.1210 0.1227 0.1321 -0.0065 0.0237  0.0155  17   TYR   A CA  
421  C  CA  B TYR   A 17  ? 0.1323 0.1295 0.1436 -0.0265 0.0013  0.0364  17   TYR   A CA  
422  C  C   A TYR   A 17  ? 0.1220 0.1159 0.1379 -0.0092 0.0165  0.0127  17   TYR   A C   
423  C  C   B TYR   A 17  ? 0.1253 0.1315 0.1566 -0.0237 0.0030  0.0337  17   TYR   A C   
424  O  O   A TYR   A 17  ? 0.1180 0.1109 0.1485 -0.0041 0.0254  0.0240  17   TYR   A O   
425  O  O   B TYR   A 17  ? 0.1171 0.1343 0.1684 -0.0241 0.0058  0.0371  17   TYR   A O   
426  C  CB  A TYR   A 17  ? 0.1246 0.1309 0.1357 -0.0063 0.0204  0.0132  17   TYR   A CB  
427  C  CB  B TYR   A 17  ? 0.1513 0.1248 0.1480 -0.0288 -0.0089 0.0358  17   TYR   A CB  
428  C  CG  A TYR   A 17  ? 0.1345 0.1446 0.1475 -0.0048 0.0194  0.0181  17   TYR   A CG  
429  C  CG  B TYR   A 17  ? 0.1677 0.1325 0.1381 -0.0292 -0.0154 0.0241  17   TYR   A CG  
430  C  CD1 A TYR   A 17  ? 0.1380 0.1527 0.1568 0.0005  0.0221  0.0222  17   TYR   A CD1 
431  C  CD1 B TYR   A 17  ? 0.1742 0.1464 0.1515 -0.0210 -0.0071 0.0282  17   TYR   A CD1 
432  C  CD2 A TYR   A 17  ? 0.1404 0.1499 0.1514 -0.0042 0.0257  0.0194  17   TYR   A CD2 
433  C  CD2 B TYR   A 17  ? 0.1797 0.1379 0.1331 -0.0353 -0.0102 0.0230  17   TYR   A CD2 
434  C  CE1 A TYR   A 17  ? 0.1434 0.1523 0.1629 -0.0010 0.0249  0.0251  17   TYR   A CE1 
435  C  CE1 B TYR   A 17  ? 0.1786 0.1505 0.1683 -0.0227 -0.0071 0.0290  17   TYR   A CE1 
436  C  CE2 A TYR   A 17  ? 0.1441 0.1473 0.1576 -0.0006 0.0254  0.0151  17   TYR   A CE2 
437  C  CE2 B TYR   A 17  ? 0.1859 0.1452 0.1493 -0.0318 -0.0087 0.0199  17   TYR   A CE2 
438  C  CZ  A TYR   A 17  ? 0.1412 0.1449 0.1583 -0.0035 0.0194  0.0283  17   TYR   A CZ  
439  C  CZ  B TYR   A 17  ? 0.1841 0.1441 0.1566 -0.0301 -0.0089 0.0228  17   TYR   A CZ  
440  O  OH  A TYR   A 17  ? 0.1378 0.1478 0.1673 0.0018  0.0233  0.0409  17   TYR   A OH  
441  O  OH  B TYR   A 17  ? 0.1948 0.1455 0.1663 -0.0249 -0.0095 0.0196  17   TYR   A OH  
460  N  N   A ILE   A 18  ? 0.1277 0.1168 0.1398 -0.0072 0.0151  0.0148  18   ILE   A N   
461  N  N   B ILE   A 18  ? 0.1240 0.1347 0.1541 -0.0201 0.0139  0.0358  18   ILE   A N   
462  C  CA  A ILE   A 18  ? 0.1301 0.1200 0.1487 -0.0064 0.0133  0.0115  18   ILE   A CA  
463  C  CA  B ILE   A 18  ? 0.1237 0.1342 0.1411 -0.0160 0.0223  0.0246  18   ILE   A CA  
464  C  C   A ILE   A 18  ? 0.1299 0.1232 0.1539 -0.0180 0.0106  0.0091  18   ILE   A C   
465  C  C   B ILE   A 18  ? 0.1234 0.1506 0.1432 -0.0222 0.0216  0.0173  18   ILE   A C   
466  O  O   A ILE   A 18  ? 0.1298 0.1291 0.1553 -0.0207 0.0185  0.0154  18   ILE   A O   
467  O  O   B ILE   A 18  ? 0.1204 0.1590 0.1545 -0.0235 0.0290  0.0185  18   ILE   A O   
468  C  CB  A ILE   A 18  ? 0.1362 0.1241 0.1404 0.0088  0.0165  0.0138  18   ILE   A CB  
469  C  CB  B ILE   A 18  ? 0.1262 0.1263 0.1211 -0.0057 0.0218  0.0281  18   ILE   A CB  
470  C  CG1 A ILE   A 18  ? 0.1432 0.1230 0.1391 0.0193  0.0101  0.0213  18   ILE   A CG1 
471  C  CG1 B ILE   A 18  ? 0.1378 0.1325 0.1313 -0.0088 0.0265  0.0257  18   ILE   A CG1 
472  C  CG2 A ILE   A 18  ? 0.1292 0.1216 0.1327 0.0129  0.0164  -0.0002 18   ILE   A CG2 
473  C  CG2 B ILE   A 18  ? 0.1248 0.1302 0.1179 -0.0095 0.0151  0.0276  18   ILE   A CG2 
474  C  CD1 A ILE   A 18  ? 0.1591 0.1326 0.1552 0.0222  0.0048  0.0203  18   ILE   A CD1 
475  C  CD1 B ILE   A 18  ? 0.1553 0.1412 0.1606 -0.0028 0.0279  0.0108  18   ILE   A CD1 
498  N  N   A LYS   A 19  ? 0.1308 0.1281 0.1545 -0.0198 0.0264  0.0090  19   LYS   A N   
499  N  N   B LYS   A 19  ? 0.1296 0.1595 0.1509 -0.0199 0.0274  0.0085  19   LYS   A N   
500  C  CA  A LYS   A 19  ? 0.1347 0.1359 0.1747 -0.0151 0.0302  0.0135  19   LYS   A CA  
501  C  CA  B LYS   A 19  ? 0.1402 0.1721 0.1532 -0.0115 0.0284  -0.0036 19   LYS   A CA  
502  C  C   A LYS   A 19  ? 0.1260 0.1338 0.1959 -0.0083 0.0316  0.0264  19   LYS   A C   
503  C  C   B LYS   A 19  ? 0.1395 0.1746 0.1649 0.0064  0.0281  -0.0075 19   LYS   A C   
504  O  O   A LYS   A 19  ? 0.1232 0.1341 0.2033 -0.0023 0.0270  0.0329  19   LYS   A O   
505  O  O   B LYS   A 19  ? 0.1387 0.1642 0.1619 0.0114  0.0210  -0.0005 19   LYS   A O   
506  C  CB  A LYS   A 19  ? 0.1432 0.1499 0.1704 -0.0244 0.0340  0.0054  19   LYS   A CB  
507  C  CB  B LYS   A 19  ? 0.1519 0.1873 0.1504 -0.0155 0.0321  -0.0076 19   LYS   A CB  
508  C  CG  A LYS   A 19  ? 0.1664 0.1653 0.1717 -0.0244 0.0306  -0.0115 19   LYS   A CG  
509  C  CG  B LYS   A 19  ? 0.1684 0.1990 0.1501 -0.0198 0.0279  -0.0116 19   LYS   A CG  
510  C  CD  A LYS   A 19  ? 0.1834 0.1829 0.1711 -0.0285 0.0247  -0.0181 19   LYS   A CD  
511  C  CD  B LYS   A 19  ? 0.1839 0.2115 0.1526 -0.0260 0.0284  -0.0076 19   LYS   A CD  
512  C  CE  A LYS   A 19  ? 0.1976 0.1930 0.1820 -0.0312 0.0163  -0.0224 19   LYS   A CE  
513  C  CE  B LYS   A 19  ? 0.1937 0.2209 0.1574 -0.0277 0.0209  -0.0128 19   LYS   A CE  
514  N  NZ  A LYS   A 19  ? 0.2064 0.2024 0.1742 -0.0306 0.0136  -0.0331 19   LYS   A NZ  
515  N  NZ  B LYS   A 19  ? 0.1984 0.2256 0.1558 -0.0292 0.0256  -0.0174 19   LYS   A NZ  
542  N  N   A ASN   A 20  ? 0.1272 0.1374 0.2194 -0.0096 0.0304  0.0283  20   ASN   A N   
543  N  N   B ASN   A 20  ? 0.1494 0.1916 0.1970 0.0137  0.0279  -0.0171 20   ASN   A N   
544  C  CA  A ASN   A 20  ? 0.1353 0.1540 0.2497 0.0154  0.0421  0.0282  20   ASN   A CA  
545  C  CA  B ASN   A 20  ? 0.1592 0.2097 0.2393 0.0172  0.0278  -0.0159 20   ASN   A CA  
546  C  C   A ASN   A 20  ? 0.1526 0.1562 0.2716 0.0127  0.0484  0.0079  20   ASN   A C   
547  C  C   B ASN   A 20  ? 0.1758 0.2078 0.2470 0.0146  0.0308  -0.0247 20   ASN   A C   
548  O  O   A ASN   A 20  ? 0.1766 0.1638 0.2810 0.0019  0.0507  -0.0070 20   ASN   A O   
549  O  O   B ASN   A 20  ? 0.1944 0.2165 0.2483 0.0071  0.0307  -0.0378 20   ASN   A O   
550  C  CB  A ASN   A 20  ? 0.1332 0.1673 0.2733 0.0273  0.0419  0.0539  20   ASN   A CB  
551  C  CB  B ASN   A 20  ? 0.1589 0.2280 0.2778 0.0208  0.0254  -0.0071 20   ASN   A CB  
552  C  CG  A ASN   A 20  ? 0.1355 0.1717 0.3144 0.0384  0.0356  0.0783  20   ASN   A CG  
553  C  CG  B ASN   A 20  ? 0.1636 0.2396 0.3171 0.0260  0.0213  -0.0001 20   ASN   A CG  
554  O  OD1 A ASN   A 20  ? 0.1540 0.1831 0.3548 0.0355  0.0456  0.0670  20   ASN   A OD1 
555  O  OD1 B ASN   A 20  ? 0.1654 0.2501 0.3469 0.0298  0.0257  -0.0097 20   ASN   A OD1 
556  N  ND2 A ASN   A 20  ? 0.1420 0.1718 0.3251 0.0347  0.0238  0.0882  20   ASN   A ND2 
557  N  ND2 B ASN   A 20  ? 0.1715 0.2405 0.3236 0.0272  0.0191  0.0110  20   ASN   A ND2 
570  N  N   A ALA   A 21  ? 0.1532 0.1577 0.2812 0.0155  0.0357  0.0037  21   ALA   A N   
571  N  N   B ALA   A 21  ? 0.1805 0.1980 0.2536 0.0098  0.0208  -0.0193 21   ALA   A N   
572  C  CA  A ALA   A 21  ? 0.1573 0.1544 0.2731 0.0150  0.0281  0.0057  21   ALA   A CA  
573  C  CA  B ALA   A 21  ? 0.1869 0.1872 0.2555 0.0006  0.0172  -0.0077 21   ALA   A CA  
574  C  C   A ALA   A 21  ? 0.1555 0.1605 0.2617 0.0137  0.0174  0.0152  21   ALA   A C   
575  C  C   B ALA   A 21  ? 0.1800 0.1745 0.2467 -0.0005 0.0161  0.0031  21   ALA   A C   
576  O  O   A ALA   A 21  ? 0.1592 0.1607 0.2658 0.0095  0.0086  0.0242  21   ALA   A O   
577  O  O   B ALA   A 21  ? 0.1753 0.1597 0.2411 -0.0030 0.0121  0.0012  21   ALA   A O   
578  C  CB  A ALA   A 21  ? 0.1662 0.1479 0.2746 0.0145  0.0277  0.0024  21   ALA   A CB  
579  C  CB  B ALA   A 21  ? 0.1979 0.1899 0.2687 -0.0052 0.0158  -0.0084 21   ALA   A CB  
590  N  N   A ASP   A 22  ? 0.1559 0.1640 0.2418 0.0101  0.0138  0.0174  22   ASP   A N   
591  N  N   B ASP   A 22  ? 0.1826 0.1733 0.2426 -0.0052 0.0162  0.0150  22   ASP   A N   
592  C  CA  A ASP   A 22  ? 0.1528 0.1615 0.2035 0.0128  0.0144  0.0114  22   ASP   A CA  
593  C  CA  B ASP   A 22  ? 0.1843 0.1684 0.2348 -0.0053 0.0093  0.0162  22   ASP   A CA  
594  C  C   A ASP   A 22  ? 0.1513 0.1627 0.1620 0.0077  0.0206  0.0165  22   ASP   A C   
595  C  C   B ASP   A 22  ? 0.1633 0.1600 0.1866 -0.0125 0.0217  0.0138  22   ASP   A C   
596  O  O   A ASP   A 22  ? 0.1597 0.1780 0.1636 0.0043  0.0254  0.0089  22   ASP   A O   
597  O  O   B ASP   A 22  ? 0.1601 0.1619 0.1771 -0.0151 0.0212  0.0014  22   ASP   A O   
598  C  CB  A ASP   A 22  ? 0.1575 0.1615 0.2306 0.0162  0.0117  0.0027  22   ASP   A CB  
599  C  CB  B ASP   A 22  ? 0.2046 0.1766 0.2746 0.0022  0.0033  0.0135  22   ASP   A CB  
600  C  CG  A ASP   A 22  ? 0.1570 0.1577 0.2602 0.0140  0.0011  0.0025  22   ASP   A CG  
601  C  CG  B ASP   A 22  ? 0.2197 0.1802 0.3004 0.0028  -0.0076 0.0200  22   ASP   A CG  
602  O  OD1 A ASP   A 22  ? 0.1526 0.1527 0.2920 -0.0039 -0.0098 0.0046  22   ASP   A OD1 
603  O  OD1 B ASP   A 22  ? 0.2194 0.1755 0.2952 -0.0001 -0.0104 0.0291  22   ASP   A OD1 
604  O  OD2 A ASP   A 22  ? 0.1644 0.1587 0.2641 0.0282  0.0181  0.0065  22   ASP   A OD2 
605  O  OD2 B ASP   A 22  ? 0.2338 0.1950 0.3315 0.0022  -0.0064 0.0199  22   ASP   A OD2 
614  N  N   A ILE   A 23  ? 0.1551 0.1542 0.1447 0.0080  0.0237  0.0157  23   ILE   A N   
615  N  N   B ILE   A 23  ? 0.1558 0.1573 0.1601 -0.0129 0.0241  0.0166  23   ILE   A N   
616  C  CA  A ILE   A 23  ? 0.1557 0.1434 0.1369 0.0077  0.0246  0.0155  23   ILE   A CA  
617  C  CA  B ILE   A 23  ? 0.1478 0.1566 0.1423 -0.0103 0.0181  0.0251  23   ILE   A CA  
618  C  C   A ILE   A 23  ? 0.1549 0.1479 0.1243 0.0056  0.0318  0.0161  23   ILE   A C   
619  C  C   B ILE   A 23  ? 0.1462 0.1582 0.1407 -0.0152 0.0161  0.0280  23   ILE   A C   
620  O  O   A ILE   A 23  ? 0.1604 0.1544 0.1328 0.0066  0.0271  0.0117  23   ILE   A O   
621  O  O   B ILE   A 23  ? 0.1467 0.1543 0.1433 -0.0196 0.0154  0.0207  23   ILE   A O   
622  C  CB  A ILE   A 23  ? 0.1635 0.1388 0.1324 0.0148  0.0216  0.0111  23   ILE   A CB  
623  C  CB  B ILE   A 23  ? 0.1518 0.1517 0.1228 -0.0019 0.0105  0.0265  23   ILE   A CB  
624  C  CG1 A ILE   A 23  ? 0.1704 0.1362 0.1278 0.0194  0.0159  0.0096  23   ILE   A CG1 
625  C  CG1 B ILE   A 23  ? 0.1596 0.1567 0.1177 -0.0017 0.0011  0.0109  23   ILE   A CG1 
626  C  CG2 A ILE   A 23  ? 0.1594 0.1392 0.1379 0.0210  0.0208  0.0243  23   ILE   A CG2 
627  C  CG2 B ILE   A 23  ? 0.1457 0.1469 0.1219 0.0022  0.0120  0.0339  23   ILE   A CG2 
628  C  CD1 A ILE   A 23  ? 0.1795 0.1408 0.1424 0.0183  0.0160  0.0016  23   ILE   A CD1 
629  C  CD1 B ILE   A 23  ? 0.1645 0.1575 0.1236 0.0045  -0.0059 0.0041  23   ILE   A CD1 
652  N  N   A VAL   A 24  ? 0.1583 0.1501 0.1363 0.0019  0.0297  0.0108  24   VAL   A N   
653  N  N   B VAL   A 24  ? 0.1499 0.1649 0.1637 -0.0164 0.0078  0.0265  24   VAL   A N   
654  C  CA  A VAL   A 24  ? 0.1707 0.1619 0.1591 -0.0064 0.0267  -0.0067 24   VAL   A CA  
655  C  CA  B VAL   A 24  ? 0.1651 0.1746 0.1839 -0.0172 0.0109  0.0215  24   VAL   A CA  
656  C  C   A VAL   A 24  ? 0.1806 0.1793 0.1694 -0.0132 0.0150  -0.0044 24   VAL   A C   
657  C  C   B VAL   A 24  ? 0.1742 0.1963 0.1826 -0.0182 0.0154  0.0087  24   VAL   A C   
658  O  O   A VAL   A 24  ? 0.1862 0.1795 0.1714 -0.0108 0.0132  -0.0016 24   VAL   A O   
659  O  O   B VAL   A 24  ? 0.1768 0.1975 0.1836 -0.0164 0.0115  0.0029  24   VAL   A O   
660  C  CB  A VAL   A 24  ? 0.1729 0.1640 0.1781 -0.0047 0.0412  -0.0149 24   VAL   A CB  
661  C  CB  B VAL   A 24  ? 0.1698 0.1705 0.2191 -0.0191 0.0119  0.0318  24   VAL   A CB  
662  C  CG1 A VAL   A 24  ? 0.1754 0.1669 0.1808 -0.0033 0.0513  -0.0255 24   VAL   A CG1 
663  C  CG1 B VAL   A 24  ? 0.1822 0.1797 0.2453 -0.0204 0.0091  0.0273  24   VAL   A CG1 
664  C  CG2 A VAL   A 24  ? 0.1800 0.1695 0.1950 -0.0009 0.0511  -0.0062 24   VAL   A CG2 
665  C  CG2 B VAL   A 24  ? 0.1729 0.1655 0.2314 -0.0183 0.0205  0.0376  24   VAL   A CG2 
684  N  N   A GLU   A 25  ? 0.1865 0.1975 0.1751 -0.0235 0.0163  -0.0109 25   GLU   A N   
685  N  N   B GLU   A 25  ? 0.1781 0.2173 0.1776 -0.0253 0.0320  -0.0041 25   GLU   A N   
686  C  CA  A GLU   A 25  ? 0.2007 0.2211 0.1837 -0.0214 0.0276  -0.0129 25   GLU   A CA  
687  C  CA  B GLU   A 25  ? 0.1912 0.2416 0.1901 -0.0328 0.0431  -0.0089 25   GLU   A CA  
688  C  C   A GLU   A 25  ? 0.1920 0.2238 0.1616 -0.0262 0.0372  -0.0081 25   GLU   A C   
689  C  C   B GLU   A 25  ? 0.1839 0.2508 0.1678 -0.0363 0.0508  -0.0092 25   GLU   A C   
690  O  O   A GLU   A 25  ? 0.1970 0.2311 0.1716 -0.0270 0.0370  -0.0048 25   GLU   A O   
691  O  O   B GLU   A 25  ? 0.1889 0.2564 0.1699 -0.0365 0.0574  -0.0161 25   GLU   A O   
692  C  CB  A GLU   A 25  ? 0.2225 0.2422 0.2293 -0.0188 0.0305  -0.0176 25   GLU   A CB  
693  C  CB  B GLU   A 25  ? 0.2099 0.2542 0.2296 -0.0351 0.0489  -0.0094 25   GLU   A CB  
694  C  CG  A GLU   A 25  ? 0.2449 0.2606 0.2806 -0.0181 0.0201  -0.0263 25   GLU   A CG  
695  C  CG  B GLU   A 25  ? 0.2331 0.2712 0.2859 -0.0364 0.0435  -0.0099 25   GLU   A CG  
696  C  CD  A GLU   A 25  ? 0.2641 0.2781 0.3291 -0.0197 0.0101  -0.0303 25   GLU   A CD  
697  C  CD  B GLU   A 25  ? 0.2509 0.2864 0.3363 -0.0390 0.0339  -0.0108 25   GLU   A CD  
698  O  OE1 A GLU   A 25  ? 0.2741 0.2854 0.3392 -0.0191 -0.0006 -0.0369 25   GLU   A OE1 
699  O  OE1 B GLU   A 25  ? 0.2595 0.2935 0.3589 -0.0381 0.0281  -0.0103 25   GLU   A OE1 
700  O  OE2 A GLU   A 25  ? 0.2687 0.2850 0.3582 -0.0209 0.0064  -0.0361 25   GLU   A OE2 
701  O  OE2 B GLU   A 25  ? 0.2593 0.2899 0.3596 -0.0413 0.0296  -0.0138 25   GLU   A OE2 
714  N  N   A GLU   A 26  ? 0.1842 0.2175 0.1606 -0.0402 0.0424  -0.0079 26   GLU   A N   
715  N  N   B GLU   A 26  ? 0.1802 0.2519 0.1634 -0.0423 0.0476  -0.0068 26   GLU   A N   
716  C  CA  A GLU   A 26  ? 0.1932 0.2172 0.1526 -0.0528 0.0397  -0.0072 26   GLU   A CA  
717  C  CA  B GLU   A 26  ? 0.1898 0.2528 0.1547 -0.0451 0.0435  -0.0006 26   GLU   A CA  
718  C  C   A GLU   A 26  ? 0.1921 0.2158 0.1222 -0.0480 0.0305  -0.0053 26   GLU   A C   
719  C  C   B GLU   A 26  ? 0.1888 0.2335 0.1340 -0.0419 0.0378  0.0014  26   GLU   A C   
720  O  O   A GLU   A 26  ? 0.1998 0.2148 0.1071 -0.0516 0.0281  -0.0118 26   GLU   A O   
721  O  O   B GLU   A 26  ? 0.1943 0.2323 0.1351 -0.0364 0.0415  0.0017  26   GLU   A O   
722  C  CB  A GLU   A 26  ? 0.2075 0.2169 0.1965 -0.0624 0.0402  -0.0068 26   GLU   A CB  
723  C  CB  B GLU   A 26  ? 0.2032 0.2717 0.1850 -0.0492 0.0247  -0.0020 26   GLU   A CB  
724  C  CG  A GLU   A 26  ? 0.2215 0.2239 0.2637 -0.0655 0.0567  -0.0149 26   GLU   A CG  
725  C  CG  B GLU   A 26  ? 0.2122 0.2895 0.2196 -0.0524 0.0314  -0.0066 26   GLU   A CG  
726  C  CD  A GLU   A 26  ? 0.2305 0.2255 0.2954 -0.0734 0.0834  -0.0200 26   GLU   A CD  
727  C  CD  B GLU   A 26  ? 0.2185 0.3015 0.2329 -0.0626 0.0382  -0.0095 26   GLU   A CD  
728  O  OE1 A GLU   A 26  ? 0.2264 0.2367 0.3021 -0.0641 0.1104  -0.0588 26   GLU   A OE1 
729  O  OE1 B GLU   A 26  ? 0.2204 0.3152 0.2108 -0.0579 0.0527  -0.0208 26   GLU   A OE1 
730  O  OE2 A GLU   A 26  ? 0.2351 0.2213 0.2809 -0.0790 0.0941  -0.0053 26   GLU   A OE2 
731  O  OE2 B GLU   A 26  ? 0.2195 0.2976 0.2286 -0.0734 0.0410  -0.0125 26   GLU   A OE2 
744  N  N   . ALA   A 27  ? 0.1792 0.2149 0.1268 -0.0409 0.0334  0.0015  27   ALA   A N   
745  C  CA  . ALA   A 27  ? 0.1837 0.2171 0.1120 -0.0344 0.0277  0.0051  27   ALA   A CA  
746  C  C   . ALA   A 27  ? 0.2097 0.2431 0.1194 -0.0450 0.0342  -0.0179 27   ALA   A C   
747  O  O   . ALA   A 27  ? 0.2117 0.2415 0.1251 -0.0518 0.0186  -0.0113 27   ALA   A O   
748  C  CB  . ALA   A 27  ? 0.1693 0.1987 0.1198 -0.0371 0.0229  0.0042  27   ALA   A CB  
755  N  N   A LYS   A 28  ? 0.2309 0.2659 0.1435 -0.0415 0.0310  -0.0400 28   LYS   A N   
756  N  N   B LYS   A 28  ? 0.2305 0.2637 0.1414 -0.0384 0.0263  -0.0360 28   LYS   A N   
757  C  CA  A LYS   A 28  ? 0.2602 0.2978 0.1841 -0.0381 0.0296  -0.0549 28   LYS   A CA  
758  C  CA  B LYS   A 28  ? 0.2598 0.2940 0.1810 -0.0320 0.0203  -0.0473 28   LYS   A CA  
759  C  C   A LYS   A 28  ? 0.2770 0.3257 0.1707 -0.0420 0.0390  -0.0458 28   LYS   A C   
760  C  C   B LYS   A 28  ? 0.2797 0.3237 0.1751 -0.0365 0.0274  -0.0398 28   LYS   A C   
761  O  O   A LYS   A 28  ? 0.2822 0.3344 0.1927 -0.0420 0.0198  -0.0436 28   LYS   A O   
762  O  O   B LYS   A 28  ? 0.2882 0.3334 0.1983 -0.0357 0.0103  -0.0402 28   LYS   A O   
763  C  CB  A LYS   A 28  ? 0.2725 0.3059 0.2434 -0.0291 0.0259  -0.0690 28   LYS   A CB  
764  C  CB  B LYS   A 28  ? 0.2697 0.2985 0.2314 -0.0204 0.0156  -0.0572 28   LYS   A CB  
765  C  CG  A LYS   A 28  ? 0.2826 0.3136 0.2954 -0.0230 0.0216  -0.0759 28   LYS   A CG  
766  C  CG  B LYS   A 28  ? 0.2792 0.3036 0.2778 -0.0125 0.0105  -0.0608 28   LYS   A CG  
767  C  CD  A LYS   A 28  ? 0.2900 0.3231 0.3498 -0.0193 0.0152  -0.0766 28   LYS   A CD  
768  C  CD  B LYS   A 28  ? 0.2907 0.3139 0.3371 -0.0061 0.0081  -0.0558 28   LYS   A CD  
769  C  CE  A LYS   A 28  ? 0.2929 0.3293 0.3894 -0.0190 0.0077  -0.0792 28   LYS   A CE  
770  C  CE  B LYS   A 28  ? 0.2984 0.3218 0.3836 -0.0045 0.0086  -0.0498 28   LYS   A CE  
771  N  NZ  A LYS   A 28  ? 0.2951 0.3324 0.4139 -0.0180 0.0060  -0.0808 28   LYS   A NZ  
772  N  NZ  B LYS   A 28  ? 0.3007 0.3254 0.4047 -0.0032 0.0093  -0.0498 28   LYS   A NZ  
799  N  N   A LYS   A 29  ? 0.2865 0.3444 0.1586 -0.0466 0.0731  -0.0257 29   LYS   A N   
800  N  N   B LYS   A 29  ? 0.2894 0.3429 0.1664 -0.0425 0.0613  -0.0200 29   LYS   A N   
801  C  CA  A LYS   A 29  ? 0.3032 0.3649 0.1855 -0.0488 0.0880  -0.0088 29   LYS   A CA  
802  C  CA  B LYS   A 29  ? 0.3052 0.3635 0.1867 -0.0459 0.0810  -0.0054 29   LYS   A CA  
803  C  C   A LYS   A 29  ? 0.3005 0.3602 0.1600 -0.0558 0.0776  -0.0019 29   LYS   A C   
804  C  C   B LYS   A 29  ? 0.3013 0.3593 0.1566 -0.0543 0.0753  -0.0002 29   LYS   A C   
805  O  O   A LYS   A 29  ? 0.3089 0.3687 0.1781 -0.0514 0.0665  0.0004  29   LYS   A O   
806  O  O   B LYS   A 29  ? 0.3079 0.3668 0.1625 -0.0513 0.0715  0.0042  29   LYS   A O   
807  C  CB  A LYS   A 29  ? 0.3193 0.3876 0.2464 -0.0431 0.1075  -0.0022 29   LYS   A CB  
808  C  CB  B LYS   A 29  ? 0.3222 0.3859 0.2424 -0.0400 0.1007  0.0002  29   LYS   A CB  
809  C  CG  A LYS   A 29  ? 0.3364 0.4075 0.3142 -0.0382 0.1149  0.0007  29   LYS   A CG  
810  C  CG  B LYS   A 29  ? 0.3403 0.4058 0.3077 -0.0347 0.1088  0.0031  29   LYS   A CG  
811  C  CD  A LYS   A 29  ? 0.3514 0.4233 0.3771 -0.0341 0.1183  -0.0002 29   LYS   A CD  
812  C  CD  B LYS   A 29  ? 0.3554 0.4214 0.3698 -0.0302 0.1132  0.0022  29   LYS   A CD  
813  C  CE  A LYS   A 29  ? 0.3617 0.4342 0.4218 -0.0311 0.1215  -0.0019 29   LYS   A CE  
814  C  CE  B LYS   A 29  ? 0.3658 0.4321 0.4139 -0.0270 0.1176  0.0004  29   LYS   A CE  
815  N  NZ  A LYS   A 29  ? 0.3663 0.4404 0.4497 -0.0296 0.1224  -0.0039 29   LYS   A NZ  
816  N  NZ  B LYS   A 29  ? 0.3704 0.4381 0.4416 -0.0254 0.1192  -0.0014 29   LYS   A NZ  
843  N  N   . VAL   A 30  ? 0.2892 0.3462 0.1464 -0.0646 0.0692  0.0016  30   VAL   A N   
844  C  CA  . VAL   A 30  ? 0.2810 0.3256 0.1352 -0.0795 0.0383  0.0202  30   VAL   A CA  
845  C  C   . VAL   A 30  ? 0.2782 0.3041 0.1064 -0.0761 0.0288  0.0303  30   VAL   A C   
846  O  O   . VAL   A 30  ? 0.2882 0.3056 0.1165 -0.0807 0.0225  0.0328  30   VAL   A O   
847  C  CB  . VAL   A 30  ? 0.2741 0.3193 0.1704 -0.0881 0.0165  0.0261  30   VAL   A CB  
848  C  CG1 . VAL   A 30  ? 0.2758 0.3196 0.1873 -0.0880 0.0034  0.0234  30   VAL   A CG1 
849  C  CG2 . VAL   A 30  ? 0.2723 0.3213 0.2020 -0.0945 0.0137  0.0279  30   VAL   A CG2 
860  N  N   . LYS   A 31  ? 0.2698 0.2918 0.0973 -0.0784 0.0156  0.0244  31   LYS   A N   
861  C  CA  . LYS   A 31  ? 0.2846 0.2908 0.1112 -0.0686 -0.0082 0.0166  31   LYS   A CA  
862  C  C   . LYS   A 31  ? 0.2615 0.2638 0.0925 -0.0539 -0.0093 0.0459  31   LYS   A C   
863  O  O   . LYS   A 31  ? 0.2718 0.2791 0.1139 -0.0471 -0.0238 0.0574  31   LYS   A O   
864  C  CB  . LYS   A 31  ? 0.3314 0.3225 0.2055 -0.0656 -0.0284 -0.0084 31   LYS   A CB  
865  C  CG  . LYS   A 31  ? 0.3822 0.3584 0.3393 -0.0537 -0.0452 -0.0265 31   LYS   A CG  
866  C  CD  . LYS   A 31  ? 0.4172 0.3905 0.4428 -0.0431 -0.0565 -0.0386 31   LYS   A CD  
867  C  CE  . LYS   A 31  ? 0.4460 0.4112 0.5120 -0.0357 -0.0664 -0.0508 31   LYS   A CE  
868  N  NZ  . LYS   A 31  ? 0.4648 0.4156 0.5492 -0.0308 -0.0715 -0.0586 31   LYS   A NZ  
882  N  N   . PRO   A 32  ? 0.2261 0.2339 0.0800 -0.0482 -0.0042 0.0381  32   PRO   A N   
883  C  CA  . PRO   A 32  ? 0.2193 0.2135 0.1167 -0.0480 -0.0109 0.0422  32   PRO   A CA  
884  C  C   . PRO   A 32  ? 0.2178 0.2063 0.1213 -0.0396 -0.0212 0.0445  32   PRO   A C   
885  O  O   . PRO   A 32  ? 0.2110 0.2008 0.1370 -0.0450 -0.0326 0.0428  32   PRO   A O   
886  C  CB  . PRO   A 32  ? 0.2114 0.2205 0.1350 -0.0432 -0.0120 0.0317  32   PRO   A CB  
887  C  CG  . PRO   A 32  ? 0.2087 0.2264 0.0929 -0.0371 -0.0145 0.0273  32   PRO   A CG  
888  C  CD  . PRO   A 32  ? 0.2120 0.2277 0.0844 -0.0410 -0.0068 0.0270  32   PRO   A CD  
896  N  N   . THR   A 33  ? 0.2287 0.2049 0.1114 -0.0309 -0.0113 0.0527  33   THR   A N   
897  C  CA  . THR   A 33  ? 0.2281 0.2047 0.1198 -0.0190 -0.0262 0.0498  33   THR   A CA  
898  C  C   . THR   A 33  ? 0.1981 0.1906 0.1142 -0.0258 -0.0309 0.0427  33   THR   A C   
899  O  O   . THR   A 33  ? 0.1873 0.1968 0.1335 -0.0276 -0.0402 0.0410  33   THR   A O   
900  C  CB  . THR   A 33  ? 0.2544 0.2243 0.1392 -0.0099 -0.0318 0.0671  33   THR   A CB  
901  O  OG1 . THR   A 33  ? 0.2775 0.2381 0.1692 -0.0012 -0.0199 0.0785  33   THR   A OG1 
902  C  CG2 . THR   A 33  ? 0.2592 0.2345 0.1704 -0.0055 -0.0321 0.0639  33   THR   A CG2 
910  N  N   . VAL   A 34  ? 0.1786 0.1772 0.0973 -0.0292 -0.0211 0.0395  34   VAL   A N   
911  C  CA  . VAL   A 34  ? 0.1671 0.1619 0.1027 -0.0210 -0.0143 0.0347  34   VAL   A CA  
912  C  C   . VAL   A 34  ? 0.1552 0.1565 0.0908 -0.0199 -0.0080 0.0289  34   VAL   A C   
913  O  O   . VAL   A 34  ? 0.1546 0.1583 0.1135 -0.0283 -0.0035 0.0377  34   VAL   A O   
914  C  CB  . VAL   A 34  ? 0.1663 0.1563 0.1265 -0.0202 -0.0088 0.0235  34   VAL   A CB  
915  C  CG1 . VAL   A 34  ? 0.1696 0.1558 0.1267 -0.0209 0.0015  0.0138  34   VAL   A CG1 
916  C  CG2 . VAL   A 34  ? 0.1667 0.1706 0.1559 -0.0143 -0.0172 0.0283  34   VAL   A CG2 
926  N  N   . VAL   A 35  ? 0.1395 0.1436 0.0898 -0.0230 -0.0083 0.0238  35   VAL   A N   
927  C  CA  . VAL   A 35  ? 0.1351 0.1411 0.0875 -0.0191 -0.0019 0.0176  35   VAL   A CA  
928  C  C   . VAL   A 35  ? 0.1259 0.1288 0.0835 -0.0182 -0.0040 0.0220  35   VAL   A C   
929  O  O   . VAL   A 35  ? 0.1196 0.1380 0.1038 -0.0239 0.0024  0.0118  35   VAL   A O   
930  C  CB  . VAL   A 35  ? 0.1444 0.1517 0.0917 -0.0115 0.0076  0.0117  35   VAL   A CB  
931  C  CG1 . VAL   A 35  ? 0.1549 0.1490 0.1163 -0.0050 0.0001  0.0057  35   VAL   A CG1 
932  C  CG2 . VAL   A 35  ? 0.1428 0.1550 0.1253 -0.0084 0.0088  0.0022  35   VAL   A CG2 
942  N  N   . VAL   A 36  ? 0.1130 0.1299 0.0821 -0.0142 0.0071  0.0202  36   VAL   A N   
943  C  CA  . VAL   A 36  ? 0.1138 0.1215 0.0855 -0.0073 0.0023  0.0135  36   VAL   A CA  
944  C  C   . VAL   A 36  ? 0.1103 0.1202 0.0920 -0.0097 0.0074  0.0135  36   VAL   A C   
945  O  O   . VAL   A 36  ? 0.1156 0.1213 0.1104 -0.0031 0.0137  0.0143  36   VAL   A O   
946  C  CB  . VAL   A 36  ? 0.1161 0.1114 0.1061 -0.0124 -0.0009 0.0143  36   VAL   A CB  
947  C  CG1 . VAL   A 36  ? 0.1200 0.1117 0.1069 -0.0167 0.0047  0.0134  36   VAL   A CG1 
948  C  CG2 . VAL   A 36  ? 0.1263 0.1179 0.1172 -0.0029 -0.0041 0.0204  36   VAL   A CG2 
958  N  N   A ASN   A 37  ? 0.1068 0.1137 0.1001 -0.0037 0.0026  0.0165  37   ASN   A N   
959  N  N   B ASN   A 37  ? 0.1052 0.1114 0.0905 -0.0015 0.0055  0.0162  37   ASN   A N   
960  C  CA  A ASN   A 37  ? 0.1089 0.1142 0.0983 -0.0031 0.0069  0.0187  37   ASN   A CA  
961  C  CA  B ASN   A 37  ? 0.1017 0.1075 0.0831 -0.0007 0.0072  0.0125  37   ASN   A CA  
962  C  C   A ASN   A 37  ? 0.1068 0.1126 0.0896 -0.0082 0.0130  0.0278  37   ASN   A C   
963  C  C   B ASN   A 37  ? 0.1005 0.0986 0.0949 0.0070  0.0123  0.0095  37   ASN   A C   
964  O  O   A ASN   A 37  ? 0.1149 0.1238 0.0947 -0.0041 0.0065  0.0240  37   ASN   A O   
965  O  O   B ASN   A 37  ? 0.1058 0.1095 0.1028 0.0154  0.0086  0.0023  37   ASN   A O   
966  C  CB  A ASN   A 37  ? 0.1137 0.1117 0.1042 0.0027  -0.0007 0.0110  37   ASN   A CB  
967  C  CB  B ASN   A 37  ? 0.1068 0.1053 0.0855 0.0010  -0.0002 0.0047  37   ASN   A CB  
968  C  CG  A ASN   A 37  ? 0.1144 0.1104 0.0997 0.0052  -0.0018 0.0062  37   ASN   A CG  
969  C  CG  B ASN   A 37  ? 0.1067 0.1047 0.0900 -0.0033 0.0073  0.0029  37   ASN   A CG  
970  O  OD1 A ASN   A 37  ? 0.1141 0.1102 0.1037 0.0084  -0.0037 0.0039  37   ASN   A OD1 
971  O  OD1 B ASN   A 37  ? 0.1064 0.1095 0.0933 -0.0064 0.0030  0.0097  37   ASN   A OD1 
972  N  ND2 A ASN   A 37  ? 0.1134 0.1076 0.0914 0.0027  -0.0087 0.0172  37   ASN   A ND2 
973  N  ND2 B ASN   A 37  ? 0.1113 0.1040 0.1019 -0.0075 0.0075  0.0038  37   ASN   A ND2 
986  N  N   A ALA   A 38  ? 0.1067 0.1197 0.0984 -0.0083 0.0087  0.0199  38   ALA   A N   
987  N  N   B ALA   A 38  ? 0.1050 0.0973 0.0992 0.0081  0.0089  0.0068  38   ALA   A N   
988  C  CA  A ALA   A 38  ? 0.1086 0.1058 0.0890 -0.0024 -0.0006 -0.0000 38   ALA   A CA  
989  C  CA  B ALA   A 38  ? 0.1198 0.1025 0.1084 0.0008  0.0008  0.0130  38   ALA   A CA  
990  C  C   A ALA   A 38  ? 0.1033 0.1065 0.0804 0.0008  -0.0053 0.0010  38   ALA   A C   
991  C  C   B ALA   A 38  ? 0.1174 0.1081 0.1062 0.0037  -0.0117 0.0071  38   ALA   A C   
992  O  O   A ALA   A 38  ? 0.1043 0.1024 0.0923 -0.0009 -0.0093 -0.0051 38   ALA   A O   
993  O  O   B ALA   A 38  ? 0.1126 0.1043 0.1198 -0.0069 -0.0145 0.0155  38   ALA   A O   
994  C  CB  A ALA   A 38  ? 0.1059 0.1010 0.0934 -0.0105 -0.0055 -0.0075 38   ALA   A CB  
995  C  CB  B ALA   A 38  ? 0.1323 0.1111 0.1268 -0.0019 -0.0030 0.0024  38   ALA   A CB  
1006 N  N   A ALA   A 39  ? 0.1077 0.1057 0.0818 0.0052  0.0053  0.0092  39   ALA   A N   
1007 N  N   B ALA   A 39  ? 0.1254 0.1190 0.1276 0.0056  -0.0049 0.0110  39   ALA   A N   
1008 C  CA  A ALA   A 39  ? 0.1047 0.1095 0.0874 0.0053  0.0086  0.0090  39   ALA   A CA  
1009 C  CA  B ALA   A 39  ? 0.1231 0.1252 0.1255 0.0011  -0.0110 0.0065  39   ALA   A CA  
1010 C  C   A ALA   A 39  ? 0.1090 0.1118 0.0882 -0.0029 0.0073  0.0080  39   ALA   A C   
1011 C  C   B ALA   A 39  ? 0.1118 0.1159 0.1262 -0.0024 -0.0116 0.0047  39   ALA   A C   
1012 O  O   A ALA   A 39  ? 0.1138 0.1151 0.0847 -0.0106 0.0156  0.0134  39   ALA   A O   
1013 O  O   B ALA   A 39  ? 0.1240 0.1182 0.1347 -0.0001 -0.0153 -0.0044 39   ALA   A O   
1014 C  CB  A ALA   A 39  ? 0.1021 0.1134 0.1078 0.0088  0.0032  0.0030  39   ALA   A CB  
1015 C  CB  B ALA   A 39  ? 0.1312 0.1372 0.1225 -0.0019 -0.0162 0.0077  39   ALA   A CB  
1026 N  N   A ASN   A 40  ? 0.1112 0.1181 0.0957 -0.0047 0.0125  0.0035  40   ASN   A N   
1027 N  N   B ASN   A 40  ? 0.1096 0.1130 0.1163 -0.0079 0.0040  0.0085  40   ASN   A N   
1028 C  CA  A ASN   A 40  ? 0.1141 0.1165 0.0979 0.0032  0.0010  -0.0026 40   ASN   A CA  
1029 C  CA  B ASN   A 40  ? 0.1114 0.1081 0.1139 -0.0040 -0.0087 0.0109  40   ASN   A CA  
1030 C  C   A ASN   A 40  ? 0.1145 0.1062 0.0754 0.0006  0.0058  0.0056  40   ASN   A C   
1031 C  C   B ASN   A 40  ? 0.1120 0.1014 0.1022 -0.0076 0.0029  0.0236  40   ASN   A C   
1032 O  O   A ASN   A 40  ? 0.1200 0.1140 0.0736 -0.0043 0.0061  0.0060  40   ASN   A O   
1033 O  O   B ASN   A 40  ? 0.1102 0.1070 0.1072 -0.0105 0.0027  0.0274  40   ASN   A O   
1034 C  CB  A ASN   A 40  ? 0.1225 0.1280 0.1143 0.0100  -0.0172 -0.0022 40   ASN   A CB  
1035 C  CB  B ASN   A 40  ? 0.1258 0.1125 0.1247 0.0029  -0.0109 0.0134  40   ASN   A CB  
1036 C  CG  A ASN   A 40  ? 0.1355 0.1342 0.1398 0.0081  -0.0166 0.0072  40   ASN   A CG  
1037 C  CG  B ASN   A 40  ? 0.1274 0.1128 0.1313 -0.0007 -0.0120 0.0096  40   ASN   A CG  
1038 O  OD1 A ASN   A 40  ? 0.1425 0.1323 0.1451 0.0060  -0.0206 0.0173  40   ASN   A OD1 
1039 O  OD1 B ASN   A 40  ? 0.1339 0.1200 0.1503 -0.0015 -0.0079 -0.0009 40   ASN   A OD1 
1040 N  ND2 A ASN   A 40  ? 0.1404 0.1453 0.1657 0.0107  -0.0026 -0.0015 40   ASN   A ND2 
1041 N  ND2 B ASN   A 40  ? 0.1175 0.1199 0.1443 -0.0076 0.0030  -0.0029 40   ASN   A ND2 
1054 N  N   A VAL   A 41  ? 0.1145 0.1107 0.0667 -0.0057 0.0038  0.0057  41   VAL   A N   
1055 N  N   B VAL   A 41  ? 0.1206 0.1173 0.1099 -0.0025 -0.0022 0.0244  41   VAL   A N   
1056 C  CA  A VAL   A 41  ? 0.1096 0.1107 0.0810 -0.0026 0.0047  0.0092  41   VAL   A CA  
1057 C  CA  B VAL   A 41  ? 0.1273 0.1273 0.1152 -0.0027 0.0037  0.0189  41   VAL   A CA  
1058 C  C   A VAL   A 41  ? 0.1054 0.1102 0.0999 0.0015  0.0089  0.0085  41   VAL   A C   
1059 C  C   B VAL   A 41  ? 0.1197 0.1219 0.1043 -0.0060 0.0124  0.0172  41   VAL   A C   
1060 O  O   A VAL   A 41  ? 0.1077 0.1009 0.1204 0.0059  0.0038  -0.0014 41   VAL   A O   
1061 O  O   B VAL   A 41  ? 0.1252 0.1177 0.1141 -0.0053 0.0078  0.0134  41   VAL   A O   
1062 C  CB  A VAL   A 41  ? 0.1088 0.1153 0.0780 0.0030  0.0107  0.0089  41   VAL   A CB  
1063 C  CB  B VAL   A 41  ? 0.1386 0.1438 0.1246 -0.0015 0.0118  0.0238  41   VAL   A CB  
1064 C  CG1 A VAL   A 41  ? 0.1138 0.1233 0.0796 0.0074  -0.0010 0.0041  41   VAL   A CG1 
1065 C  CG1 B VAL   A 41  ? 0.1532 0.1499 0.1262 -0.0046 0.0151  0.0122  41   VAL   A CG1 
1066 C  CG2 A VAL   A 41  ? 0.1171 0.1162 0.0686 0.0040  0.0145  0.0057  41   VAL   A CG2 
1067 C  CG2 B VAL   A 41  ? 0.1430 0.1548 0.1449 -0.0013 0.0027  0.0280  41   VAL   A CG2 
1086 N  N   A TYR   A 42  ? 0.0993 0.1083 0.1139 -0.0013 0.0078  0.0111  42   TYR   A N   
1087 N  N   B TYR   A 42  ? 0.1119 0.1201 0.1044 -0.0044 0.0148  0.0292  42   TYR   A N   
1088 C  CA  A TYR   A 42  ? 0.1068 0.1049 0.1175 -0.0052 0.0111  0.0160  42   TYR   A CA  
1089 C  CA  B TYR   A 42  ? 0.1040 0.1199 0.1150 -0.0090 0.0211  0.0316  42   TYR   A CA  
1090 C  C   A TYR   A 42  ? 0.1069 0.0994 0.1277 -0.0043 0.0062  0.0101  42   TYR   A C   
1091 C  C   B TYR   A 42  ? 0.1126 0.1207 0.1029 -0.0082 0.0109  0.0382  42   TYR   A C   
1092 O  O   A TYR   A 42  ? 0.1106 0.1009 0.1456 -0.0126 0.0108  -0.0070 42   TYR   A O   
1093 O  O   B TYR   A 42  ? 0.1113 0.1278 0.1300 -0.0130 0.0062  0.0253  42   TYR   A O   
1094 C  CB  A TYR   A 42  ? 0.1250 0.1216 0.1140 -0.0050 0.0127  0.0239  42   TYR   A CB  
1095 C  CB  B TYR   A 42  ? 0.1117 0.1229 0.1237 -0.0044 0.0079  0.0372  42   TYR   A CB  
1096 C  CG  A TYR   A 42  ? 0.1283 0.1343 0.1146 -0.0059 0.0063  0.0328  42   TYR   A CG  
1097 C  CG  B TYR   A 42  ? 0.1243 0.1383 0.1298 0.0020  -0.0046 0.0374  42   TYR   A CG  
1098 C  CD1 A TYR   A 42  ? 0.1350 0.1481 0.1209 -0.0135 0.0090  0.0337  42   TYR   A CD1 
1099 C  CD1 B TYR   A 42  ? 0.1278 0.1467 0.1264 0.0008  0.0011  0.0424  42   TYR   A CD1 
1100 C  CD2 A TYR   A 42  ? 0.1279 0.1534 0.1290 0.0028  -0.0036 0.0296  42   TYR   A CD2 
1101 C  CD2 B TYR   A 42  ? 0.1412 0.1599 0.1478 0.0091  -0.0062 0.0295  42   TYR   A CD2 
1102 C  CE1 A TYR   A 42  ? 0.1411 0.1577 0.1158 -0.0075 0.0057  0.0325  42   TYR   A CE1 
1103 C  CE1 B TYR   A 42  ? 0.1366 0.1574 0.1331 0.0034  0.0066  0.0341  42   TYR   A CE1 
1104 C  CE2 A TYR   A 42  ? 0.1350 0.1628 0.1424 -0.0013 -0.0075 0.0260  42   TYR   A CE2 
1105 C  CE2 B TYR   A 42  ? 0.1516 0.1702 0.1547 0.0113  0.0011  0.0266  42   TYR   A CE2 
1106 C  CZ  A TYR   A 42  ? 0.1427 0.1621 0.1317 -0.0081 -0.0022 0.0287  42   TYR   A CZ  
1107 C  CZ  B TYR   A 42  ? 0.1502 0.1665 0.1358 0.0036  0.0059  0.0220  42   TYR   A CZ  
1108 O  OH  A TYR   A 42  ? 0.1550 0.1755 0.1533 -0.0112 -0.0110 0.0286  42   TYR   A OH  
1109 O  OH  B TYR   A 42  ? 0.1568 0.1828 0.1355 -0.0019 0.0042  0.0207  42   TYR   A OH  
1128 N  N   A LEU   A 43  ? 0.1125 0.1046 0.1194 -0.0043 0.0043  -0.0051 43   LEU   A N   
1129 N  N   B LEU   A 43  ? 0.1145 0.1217 0.1028 -0.0079 0.0100  0.0208  43   LEU   A N   
1130 C  CA  A LEU   A 43  ? 0.1071 0.1041 0.1167 -0.0074 -0.0012 0.0003  43   LEU   A CA  
1131 C  CA  B LEU   A 43  ? 0.1115 0.1197 0.1093 -0.0078 0.0107  0.0259  43   LEU   A CA  
1132 C  C   A LEU   A 43  ? 0.1053 0.1101 0.1167 -0.0004 -0.0069 -0.0041 43   LEU   A C   
1133 C  C   B LEU   A 43  ? 0.1125 0.1207 0.1038 -0.0105 0.0002  0.0154  43   LEU   A C   
1134 O  O   A LEU   A 43  ? 0.1198 0.1184 0.1408 0.0147  -0.0137 -0.0033 43   LEU   A O   
1135 O  O   B LEU   A 43  ? 0.1212 0.1238 0.1133 -0.0104 -0.0114 0.0122  43   LEU   A O   
1136 C  CB  A LEU   A 43  ? 0.1166 0.1071 0.1227 -0.0115 -0.0009 -0.0058 43   LEU   A CB  
1137 C  CB  B LEU   A 43  ? 0.1079 0.1179 0.1283 -0.0068 0.0047  0.0248  43   LEU   A CB  
1138 C  CG  A LEU   A 43  ? 0.1197 0.1096 0.1315 -0.0084 -0.0023 -0.0068 43   LEU   A CG  
1139 C  CG  B LEU   A 43  ? 0.1058 0.1148 0.1386 -0.0001 0.0023  0.0216  43   LEU   A CG  
1140 C  CD1 A LEU   A 43  ? 0.1254 0.1198 0.1494 -0.0067 -0.0069 0.0024  43   LEU   A CD1 
1141 C  CD1 B LEU   A 43  ? 0.1055 0.1213 0.1527 0.0017  -0.0032 0.0277  43   LEU   A CD1 
1142 C  CD2 A LEU   A 43  ? 0.1199 0.1130 0.1229 -0.0088 -0.0052 0.0001  43   LEU   A CD2 
1143 C  CD2 B LEU   A 43  ? 0.1100 0.1108 0.1320 0.0009  -0.0007 0.0375  43   LEU   A CD2 
1166 N  N   A LYS   A 44  ? 0.1131 0.1079 0.1100 -0.0023 0.0034  0.0033  44   LYS   A N   
1167 N  N   B LYS   A 44  ? 0.1122 0.1191 0.1055 -0.0073 -0.0028 0.0176  44   LYS   A N   
1168 C  CA  A LYS   A 44  ? 0.1241 0.1083 0.1217 -0.0072 0.0158  0.0108  44   LYS   A CA  
1169 C  CA  B LYS   A 44  ? 0.1246 0.1188 0.1140 -0.0061 -0.0071 0.0201  44   LYS   A CA  
1170 C  C   A LYS   A 44  ? 0.1143 0.1080 0.1074 0.0034  0.0121  0.0093  44   LYS   A C   
1171 C  C   B LYS   A 44  ? 0.1189 0.1168 0.1108 -0.0059 -0.0070 0.0134  44   LYS   A C   
1172 O  O   A LYS   A 44  ? 0.1161 0.1295 0.1331 0.0057  0.0013  0.0038  44   LYS   A O   
1173 O  O   B LYS   A 44  ? 0.1153 0.1307 0.1154 -0.0100 -0.0056 -0.0044 44   LYS   A O   
1174 C  CB  A LYS   A 44  ? 0.1423 0.1209 0.1522 -0.0114 0.0235  0.0290  44   LYS   A CB  
1175 C  CB  B LYS   A 44  ? 0.1461 0.1372 0.1610 0.0025  0.0055  0.0153  44   LYS   A CB  
1176 C  CG  A LYS   A 44  ? 0.1650 0.1364 0.2057 -0.0188 0.0420  0.0462  44   LYS   A CG  
1177 C  CG  B LYS   A 44  ? 0.1669 0.1634 0.2333 0.0093  0.0182  0.0221  44   LYS   A CG  
1178 C  CD  A LYS   A 44  ? 0.1993 0.1810 0.3144 -0.0249 0.0369  0.0279  44   LYS   A CD  
1179 C  CD  B LYS   A 44  ? 0.1941 0.2058 0.3299 0.0000  0.0033  0.0108  44   LYS   A CD  
1180 C  CE  A LYS   A 44  ? 0.2227 0.2068 0.3873 -0.0292 0.0357  0.0175  44   LYS   A CE  
1181 C  CE  B LYS   A 44  ? 0.2101 0.2278 0.3912 -0.0108 -0.0057 0.0052  44   LYS   A CE  
1182 N  NZ  A LYS   A 44  ? 0.2357 0.2251 0.4234 -0.0302 0.0356  0.0155  44   LYS   A NZ  
1183 N  NZ  B LYS   A 44  ? 0.2146 0.2273 0.4159 -0.0237 -0.0106 -0.0010 44   LYS   A NZ  
1210 N  N   A HIS   A 45  ? 0.1065 0.1012 0.1027 0.0003  0.0166  0.0129  45   HIS   A N   
1211 N  N   B HIS   A 45  ? 0.1225 0.1122 0.1191 -0.0085 -0.0203 0.0146  45   HIS   A N   
1212 C  CA  A HIS   A 45  ? 0.1022 0.1039 0.1055 0.0015  0.0091  0.0086  45   HIS   A CA  
1213 C  CA  B HIS   A 45  ? 0.1225 0.1209 0.1258 -0.0023 -0.0212 0.0170  45   HIS   A CA  
1214 C  C   A HIS   A 45  ? 0.1060 0.1161 0.1216 0.0054  0.0150  0.0081  45   HIS   A C   
1215 C  C   B HIS   A 45  ? 0.1290 0.1295 0.1290 -0.0027 -0.0137 0.0142  45   HIS   A C   
1216 O  O   A HIS   A 45  ? 0.1039 0.1133 0.1336 0.0011  0.0164  0.0045  45   HIS   A O   
1217 O  O   B HIS   A 45  ? 0.1388 0.1354 0.1437 0.0092  -0.0117 0.0035  45   HIS   A O   
1218 C  CB  A HIS   A 45  ? 0.1020 0.1036 0.0959 -0.0053 0.0167  0.0071  45   HIS   A CB  
1219 C  CB  B HIS   A 45  ? 0.1201 0.1232 0.1341 0.0030  -0.0264 0.0088  45   HIS   A CB  
1220 C  CG  A HIS   A 45  ? 0.1072 0.1038 0.1014 -0.0063 0.0126  0.0110  45   HIS   A CG  
1221 C  CG  B HIS   A 45  ? 0.1133 0.1196 0.1179 -0.0023 -0.0105 0.0094  45   HIS   A CG  
1222 N  ND1 A HIS   A 45  ? 0.1122 0.1094 0.1152 -0.0021 0.0112  0.0126  45   HIS   A ND1 
1223 N  ND1 B HIS   A 45  ? 0.1075 0.1220 0.1275 -0.0011 -0.0142 0.0128  45   HIS   A ND1 
1224 C  CD2 A HIS   A 45  ? 0.1106 0.1121 0.1130 -0.0130 0.0007  0.0211  45   HIS   A CD2 
1225 C  CD2 B HIS   A 45  ? 0.1106 0.1194 0.1076 -0.0055 -0.0061 0.0075  45   HIS   A CD2 
1226 C  CE1 A HIS   A 45  ? 0.1131 0.1134 0.1152 -0.0042 0.0078  0.0256  45   HIS   A CE1 
1227 C  CE1 B HIS   A 45  ? 0.1065 0.1190 0.1078 -0.0025 -0.0092 0.0139  45   HIS   A CE1 
1228 N  NE2 A HIS   A 45  ? 0.1147 0.1174 0.1154 -0.0012 0.0027  0.0315  45   HIS   A NE2 
1229 N  NE2 B HIS   A 45  ? 0.1095 0.1207 0.0982 -0.0008 -0.0055 0.0071  45   HIS   A NE2 
1244 N  N   A GLY   A 46  ? 0.1111 0.1224 0.1336 0.0137  -0.0030 0.0131  46   GLY   A N   
1245 N  N   B GLY   A 46  ? 0.1238 0.1232 0.1262 -0.0147 -0.0205 0.0256  46   GLY   A N   
1246 C  CA  A GLY   A 46  ? 0.1128 0.1249 0.1436 0.0105  -0.0053 0.0195  46   GLY   A CA  
1247 C  CA  B GLY   A 46  ? 0.1233 0.1285 0.1396 -0.0091 -0.0101 0.0315  46   GLY   A CA  
1248 C  C   A GLY   A 46  ? 0.1166 0.1208 0.1320 0.0142  -0.0101 0.0328  46   GLY   A C   
1249 C  C   B GLY   A 46  ? 0.1228 0.1269 0.1260 -0.0037 -0.0060 0.0363  46   GLY   A C   
1250 O  O   A GLY   A 46  ? 0.1285 0.1199 0.1324 0.0167  -0.0103 0.0481  46   GLY   A O   
1251 O  O   B GLY   A 46  ? 0.1307 0.1346 0.1419 -0.0044 -0.0023 0.0293  46   GLY   A O   
1258 N  N   A GLY   A 47  ? 0.1141 0.1191 0.1285 0.0141  -0.0112 0.0264  47   GLY   A N   
1259 N  N   B GLY   A 47  ? 0.1241 0.1309 0.1241 0.0018  0.0004  0.0185  47   GLY   A N   
1260 C  CA  A GLY   A 47  ? 0.1202 0.1305 0.1300 0.0199  -0.0178 0.0202  47   GLY   A CA  
1261 C  CA  B GLY   A 47  ? 0.1190 0.1339 0.1276 -0.0023 -0.0032 0.0171  47   GLY   A CA  
1262 C  C   A GLY   A 47  ? 0.1163 0.1217 0.1176 0.0161  -0.0135 0.0136  47   GLY   A C   
1263 C  C   B GLY   A 47  ? 0.1124 0.1234 0.1160 -0.0009 -0.0017 0.0052  47   GLY   A C   
1264 O  O   A GLY   A 47  ? 0.1147 0.1123 0.1213 0.0222  -0.0081 0.0151  47   GLY   A O   
1265 O  O   B GLY   A 47  ? 0.1107 0.1197 0.1291 -0.0021 -0.0110 0.0147  47   GLY   A O   
1272 N  N   A GLY   A 48  ? 0.1147 0.1288 0.1196 0.0157  -0.0096 0.0032  48   GLY   A N   
1273 N  N   B GLY   A 48  ? 0.1096 0.1289 0.1189 0.0010  -0.0011 0.0114  48   GLY   A N   
1274 C  CA  A GLY   A 48  ? 0.1124 0.1286 0.1264 0.0076  -0.0052 -0.0067 48   GLY   A CA  
1275 C  CA  B GLY   A 48  ? 0.1128 0.1222 0.1045 -0.0027 -0.0011 0.0018  48   GLY   A CA  
1276 C  C   A GLY   A 48  ? 0.1108 0.1288 0.1153 0.0018  0.0042  -0.0063 48   GLY   A C   
1277 C  C   B GLY   A 48  ? 0.1175 0.1197 0.1044 -0.0061 -0.0023 0.0066  48   GLY   A C   
1278 O  O   A GLY   A 48  ? 0.1210 0.1318 0.1152 -0.0009 0.0078  -0.0040 48   GLY   A O   
1279 O  O   B GLY   A 48  ? 0.1301 0.1199 0.1063 -0.0016 -0.0017 -0.0027 48   GLY   A O   
1286 N  N   A VAL   A 49  ? 0.1149 0.1265 0.1337 -0.0034 -0.0015 -0.0015 49   VAL   A N   
1287 N  N   B VAL   A 49  ? 0.1137 0.1154 0.1077 -0.0069 -0.0107 0.0009  49   VAL   A N   
1288 C  CA  A VAL   A 49  ? 0.1219 0.1168 0.1248 -0.0051 0.0059  0.0041  49   VAL   A CA  
1289 C  CA  B VAL   A 49  ? 0.1145 0.1180 0.1076 -0.0006 -0.0065 0.0069  49   VAL   A CA  
1290 C  C   A VAL   A 49  ? 0.1181 0.1129 0.1086 -0.0063 0.0021  0.0095  49   VAL   A C   
1291 C  C   B VAL   A 49  ? 0.1121 0.1130 0.0953 0.0043  -0.0023 -0.0032 49   VAL   A C   
1292 O  O   A VAL   A 49  ? 0.1158 0.1172 0.1055 -0.0138 -0.0005 0.0044  49   VAL   A O   
1293 O  O   B VAL   A 49  ? 0.1107 0.1114 0.0927 0.0097  0.0000  -0.0006 49   VAL   A O   
1294 C  CB  A VAL   A 49  ? 0.1374 0.1182 0.1464 -0.0069 0.0019  0.0027  49   VAL   A CB  
1295 C  CB  B VAL   A 49  ? 0.1190 0.1221 0.1273 0.0014  -0.0124 0.0069  49   VAL   A CB  
1296 C  CG1 A VAL   A 49  ? 0.1352 0.1131 0.1607 -0.0017 0.0012  -0.0030 49   VAL   A CG1 
1297 C  CG1 B VAL   A 49  ? 0.1058 0.1188 0.1192 0.0082  -0.0071 0.0159  49   VAL   A CG1 
1298 C  CG2 A VAL   A 49  ? 0.1452 0.1258 0.1684 -0.0191 -0.0069 0.0095  49   VAL   A CG2 
1299 C  CG2 B VAL   A 49  ? 0.1308 0.1284 0.1558 -0.0071 -0.0297 0.0151  49   VAL   A CG2 
1318 N  N   A ALA   A 50  ? 0.1117 0.1118 0.1005 -0.0096 -0.0044 0.0193  50   ALA   A N   
1319 N  N   B ALA   A 50  ? 0.1076 0.1134 0.0969 0.0022  -0.0027 -0.0036 50   ALA   A N   
1320 C  CA  A ALA   A 50  ? 0.1092 0.1094 0.0983 -0.0088 -0.0042 0.0235  50   ALA   A CA  
1321 C  CA  B ALA   A 50  ? 0.1077 0.1110 0.1057 0.0017  -0.0036 -0.0035 50   ALA   A CA  
1322 C  C   A ALA   A 50  ? 0.1051 0.1135 0.0952 -0.0111 -0.0015 0.0170  50   ALA   A C   
1323 C  C   B ALA   A 50  ? 0.1081 0.1137 0.0917 0.0042  -0.0048 -0.0026 50   ALA   A C   
1324 O  O   A ALA   A 50  ? 0.1081 0.1127 0.1105 -0.0100 -0.0022 0.0157  50   ALA   A O   
1325 O  O   B ALA   A 50  ? 0.1108 0.1164 0.1025 0.0102  -0.0046 -0.0049 50   ALA   A O   
1326 C  CB  A ALA   A 50  ? 0.1134 0.1098 0.0952 -0.0015 -0.0085 0.0223  50   ALA   A CB  
1327 C  CB  B ALA   A 50  ? 0.1093 0.1129 0.1130 0.0030  -0.0024 -0.0178 50   ALA   A CB  
1338 N  N   A GLY   A 51  ? 0.1096 0.1073 0.1113 -0.0070 -0.0073 0.0174  51   GLY   A N   
1339 N  N   B GLY   A 51  ? 0.1142 0.1039 0.1071 0.0046  -0.0135 -0.0009 51   GLY   A N   
1340 C  CA  A GLY   A 51  ? 0.1165 0.1083 0.1165 -0.0014 -0.0096 0.0089  51   GLY   A CA  
1341 C  CA  B GLY   A 51  ? 0.1240 0.1023 0.1060 0.0075  -0.0165 -0.0089 51   GLY   A CA  
1342 C  C   A GLY   A 51  ? 0.1081 0.1144 0.1005 0.0011  -0.0083 0.0043  51   GLY   A C   
1343 C  C   B GLY   A 51  ? 0.1216 0.1110 0.1174 0.0124  -0.0130 -0.0046 51   GLY   A C   
1344 O  O   A GLY   A 51  ? 0.1073 0.1190 0.0990 -0.0104 -0.0063 0.0054  51   GLY   A O   
1345 O  O   B GLY   A 51  ? 0.1307 0.1131 0.1323 0.0110  -0.0088 -0.0067 51   GLY   A O   
1352 N  N   A ALA   A 52  ? 0.1060 0.1119 0.0841 0.0068  -0.0064 -0.0084 52   ALA   A N   
1353 N  N   B ALA   A 52  ? 0.1200 0.1172 0.1224 0.0037  -0.0034 -0.0033 52   ALA   A N   
1354 C  CA  A ALA   A 52  ? 0.1139 0.1174 0.0968 0.0049  -0.0024 -0.0041 52   ALA   A CA  
1355 C  CA  B ALA   A 52  ? 0.1163 0.1110 0.1310 0.0036  -0.0046 0.0019  52   ALA   A CA  
1356 C  C   A ALA   A 52  ? 0.1124 0.1207 0.0749 0.0033  0.0010  -0.0058 52   ALA   A C   
1357 C  C   B ALA   A 52  ? 0.1111 0.1140 0.1214 0.0009  -0.0021 -0.0002 52   ALA   A C   
1358 O  O   A ALA   A 52  ? 0.1207 0.1289 0.0785 0.0062  -0.0029 -0.0035 52   ALA   A O   
1359 O  O   B ALA   A 52  ? 0.1145 0.1081 0.1399 -0.0013 0.0054  -0.0050 52   ALA   A O   
1360 C  CB  A ALA   A 52  ? 0.1206 0.1215 0.1110 0.0068  0.0060  -0.0050 52   ALA   A CB  
1361 C  CB  B ALA   A 52  ? 0.1228 0.1165 0.1504 -0.0004 -0.0074 0.0006  52   ALA   A CB  
1372 N  N   A LEU   A 53  ? 0.1062 0.1125 0.0907 -0.0045 -0.0008 -0.0079 53   LEU   A N   
1373 N  N   B LEU   A 53  ? 0.1073 0.1201 0.1061 0.0030  -0.0056 0.0036  53   LEU   A N   
1374 C  CA  A LEU   A 53  ? 0.1123 0.1183 0.1005 -0.0022 0.0029  -0.0008 53   LEU   A CA  
1375 C  CA  B LEU   A 53  ? 0.1087 0.1273 0.0929 0.0031  -0.0055 0.0092  53   LEU   A CA  
1376 C  C   A LEU   A 53  ? 0.1134 0.1214 0.0917 0.0028  -0.0068 0.0006  53   LEU   A C   
1377 C  C   B LEU   A 53  ? 0.1111 0.1327 0.0740 0.0075  0.0023  0.0054  53   LEU   A C   
1378 O  O   A LEU   A 53  ? 0.1193 0.1266 0.1065 -0.0004 -0.0096 -0.0025 53   LEU   A O   
1379 O  O   B LEU   A 53  ? 0.1184 0.1407 0.0891 0.0003  0.0082  0.0033  53   LEU   A O   
1380 C  CB  A LEU   A 53  ? 0.1185 0.1290 0.1117 -0.0033 0.0034  0.0116  53   LEU   A CB  
1381 C  CB  B LEU   A 53  ? 0.1064 0.1268 0.0931 0.0032  -0.0097 0.0033  53   LEU   A CB  
1382 C  CG  A LEU   A 53  ? 0.1203 0.1307 0.1197 -0.0002 0.0057  0.0169  53   LEU   A CG  
1383 C  CG  B LEU   A 53  ? 0.1091 0.1240 0.1015 0.0012  -0.0126 0.0004  53   LEU   A CG  
1384 C  CD1 A LEU   A 53  ? 0.1199 0.1369 0.1208 0.0085  0.0036  0.0217  53   LEU   A CD1 
1385 C  CD1 B LEU   A 53  ? 0.1169 0.1283 0.1145 0.0043  -0.0010 -0.0159 53   LEU   A CD1 
1386 C  CD2 A LEU   A 53  ? 0.1307 0.1432 0.1351 -0.0014 0.0069  0.0190  53   LEU   A CD2 
1387 C  CD2 B LEU   A 53  ? 0.1164 0.1262 0.1169 0.0015  -0.0028 0.0030  53   LEU   A CD2 
1410 N  N   A ASN   A 54  ? 0.1134 0.1146 0.1043 -0.0057 -0.0071 0.0028  54   ASN   A N   
1411 N  N   B ASN   A 54  ? 0.1107 0.1239 0.0860 0.0059  0.0008  0.0060  54   ASN   A N   
1412 C  CA  A ASN   A 54  ? 0.1072 0.1122 0.1199 -0.0080 -0.0061 0.0001  54   ASN   A CA  
1413 C  CA  B ASN   A 54  ? 0.1040 0.1208 0.0906 0.0087  -0.0027 -0.0010 54   ASN   A CA  
1414 C  C   A ASN   A 54  ? 0.1145 0.1190 0.1123 -0.0129 -0.0029 0.0015  54   ASN   A C   
1415 C  C   B ASN   A 54  ? 0.1155 0.1252 0.0823 -0.0000 -0.0059 -0.0024 54   ASN   A C   
1416 O  O   A ASN   A 54  ? 0.1180 0.1298 0.1324 -0.0153 -0.0021 -0.0019 54   ASN   A O   
1417 O  O   B ASN   A 54  ? 0.1214 0.1373 0.0826 0.0059  -0.0114 -0.0136 54   ASN   A O   
1418 C  CB  A ASN   A 54  ? 0.1033 0.1069 0.1339 -0.0128 -0.0096 -0.0046 54   ASN   A CB  
1419 C  CB  B ASN   A 54  ? 0.1018 0.1179 0.0927 0.0134  -0.0057 -0.0034 54   ASN   A CB  
1420 C  CG  A ASN   A 54  ? 0.1060 0.1099 0.1413 -0.0108 -0.0035 0.0043  54   ASN   A CG  
1421 C  CG  B ASN   A 54  ? 0.1037 0.1196 0.0837 0.0162  -0.0037 -0.0069 54   ASN   A CG  
1422 O  OD1 A ASN   A 54  ? 0.1096 0.1053 0.1539 -0.0097 -0.0136 0.0183  54   ASN   A OD1 
1423 O  OD1 B ASN   A 54  ? 0.1081 0.1234 0.0855 0.0138  -0.0074 -0.0079 54   ASN   A OD1 
1424 N  ND2 A ASN   A 54  ? 0.1079 0.1147 0.1459 -0.0066 -0.0009 0.0051  54   ASN   A ND2 
1425 N  ND2 B ASN   A 54  ? 0.1084 0.1179 0.0910 0.0111  -0.0128 -0.0029 54   ASN   A ND2 
1438 N  N   . LYS   A 55  ? 0.1169 0.1235 0.1133 -0.0045 -0.0012 -0.0062 55   LYS   A N   
1439 C  CA  . LYS   A 55  ? 0.1230 0.1299 0.1157 0.0052  -0.0061 -0.0142 55   LYS   A CA  
1440 C  C   . LYS   A 55  ? 0.1218 0.1381 0.1185 -0.0006 -0.0031 -0.0162 55   LYS   A C   
1441 O  O   . LYS   A 55  ? 0.1309 0.1460 0.1252 0.0053  -0.0063 -0.0225 55   LYS   A O   
1442 C  CB  . LYS   A 55  ? 0.1299 0.1372 0.1370 0.0177  -0.0096 -0.0165 55   LYS   A CB  
1443 C  CG  . LYS   A 55  ? 0.1391 0.1614 0.1600 0.0247  -0.0195 -0.0206 55   LYS   A CG  
1444 C  CD  . LYS   A 55  ? 0.1488 0.1823 0.1671 0.0313  -0.0088 -0.0130 55   LYS   A CD  
1445 C  CE  . LYS   A 55  ? 0.1744 0.2124 0.1866 0.0434  -0.0232 -0.0224 55   LYS   A CE  
1446 N  NZ  . LYS   A 55  ? 0.1814 0.2215 0.1954 0.0484  -0.0236 -0.0242 55   LYS   A NZ  
1461 N  N   . ALA   A 56  ? 0.1259 0.1464 0.1128 -0.0042 0.0028  -0.0128 56   ALA   A N   
1462 C  CA  . ALA   A 56  ? 0.1348 0.1605 0.1169 -0.0071 0.0059  -0.0161 56   ALA   A CA  
1463 C  C   . ALA   A 56  ? 0.1393 0.1688 0.0925 -0.0071 0.0039  -0.0185 56   ALA   A C   
1464 O  O   . ALA   A 56  ? 0.1461 0.2029 0.1146 0.0050  0.0074  -0.0174 56   ALA   A O   
1465 C  CB  . ALA   A 56  ? 0.1447 0.1742 0.1320 -0.0163 0.0122  -0.0070 56   ALA   A CB  
1471 N  N   . THR   A 57  ? 0.1246 0.1505 0.1036 -0.0042 0.0048  -0.0128 57   THR   A N   
1472 C  CA  . THR   A 57  ? 0.1313 0.1509 0.1045 -0.0080 -0.0018 -0.0082 57   THR   A CA  
1473 C  C   . THR   A 57  ? 0.1313 0.1540 0.1133 -0.0082 -0.0026 -0.0215 57   THR   A C   
1474 O  O   . THR   A 57  ? 0.1304 0.1555 0.1326 -0.0125 -0.0150 -0.0216 57   THR   A O   
1475 C  CB  . THR   A 57  ? 0.1262 0.1468 0.1031 -0.0084 -0.0042 -0.0104 57   THR   A CB  
1476 O  OG1 . THR   A 57  ? 0.1196 0.1445 0.1079 -0.0050 0.0003  -0.0043 57   THR   A OG1 
1477 C  CG2 . THR   A 57  ? 0.1316 0.1502 0.1021 -0.0075 -0.0014 -0.0075 57   THR   A CG2 
1485 N  N   . ASN   A 58  ? 0.1288 0.1487 0.1318 -0.0090 0.0038  -0.0278 58   ASN   A N   
1486 C  CA  . ASN   A 58  ? 0.1534 0.1465 0.1553 -0.0088 0.0064  -0.0383 58   ASN   A CA  
1487 C  C   . ASN   A 58  ? 0.1358 0.1312 0.1327 -0.0008 -0.0032 -0.0219 58   ASN   A C   
1488 O  O   . ASN   A 58  ? 0.1393 0.1430 0.1473 -0.0111 -0.0057 -0.0237 58   ASN   A O   
1489 C  CB  . ASN   A 58  ? 0.1962 0.1631 0.1868 -0.0132 0.0297  -0.0535 58   ASN   A CB  
1490 C  CG  . ASN   A 58  ? 0.2380 0.1885 0.2557 -0.0093 0.0281  -0.0378 58   ASN   A CG  
1491 O  OD1 . ASN   A 58  ? 0.2604 0.1857 0.2875 0.0235  0.0562  -0.0290 58   ASN   A OD1 
1492 N  ND2 . ASN   A 58  ? 0.2474 0.1977 0.2793 -0.0141 0.0159  -0.0405 58   ASN   A ND2 
1499 N  N   . ASN   A 59  ? 0.1206 0.1266 0.1257 -0.0053 -0.0139 -0.0164 59   ASN   A N   
1500 C  CA  . ASN   A 59  ? 0.1194 0.1170 0.1197 -0.0079 -0.0078 -0.0098 59   ASN   A CA  
1501 C  C   . ASN   A 59  ? 0.1195 0.1186 0.1174 -0.0043 -0.0115 -0.0082 59   ASN   A C   
1502 O  O   . ASN   A 59  ? 0.1181 0.1263 0.1275 -0.0053 -0.0028 0.0035  59   ASN   A O   
1503 C  CB  . ASN   A 59  ? 0.1247 0.1165 0.1294 -0.0013 -0.0214 -0.0121 59   ASN   A CB  
1504 C  CG  . ASN   A 59  ? 0.1302 0.1209 0.1264 -0.0003 -0.0280 -0.0021 59   ASN   A CG  
1505 O  OD1 . ASN   A 59  ? 0.1342 0.1284 0.1306 -0.0102 -0.0246 0.0057  59   ASN   A OD1 
1506 N  ND2 . ASN   A 59  ? 0.1370 0.1268 0.1450 -0.0130 -0.0182 0.0047  59   ASN   A ND2 
1513 N  N   . ALA   A 60  ? 0.1166 0.1210 0.1153 0.0007  -0.0097 -0.0051 60   ALA   A N   
1514 C  CA  . ALA   A 60  ? 0.1170 0.1269 0.1229 -0.0030 -0.0087 0.0003  60   ALA   A CA  
1515 C  C   . ALA   A 60  ? 0.1182 0.1216 0.1255 -0.0014 -0.0061 -0.0011 60   ALA   A C   
1516 O  O   . ALA   A 60  ? 0.1132 0.1241 0.1519 -0.0037 -0.0112 -0.0046 60   ALA   A O   
1517 C  CB  . ALA   A 60  ? 0.1279 0.1366 0.1250 -0.0034 -0.0145 -0.0128 60   ALA   A CB  
1523 N  N   . MET   A 61  ? 0.1115 0.1170 0.1194 -0.0061 -0.0052 -0.0080 61   MET   A N   
1524 C  CA  . MET   A 61  ? 0.1137 0.1146 0.1179 -0.0043 -0.0020 0.0038  61   MET   A CA  
1525 C  C   . MET   A 61  ? 0.1113 0.1123 0.1162 -0.0054 -0.0039 -0.0036 61   MET   A C   
1526 O  O   . MET   A 61  ? 0.1167 0.1125 0.1268 -0.0011 0.0072  0.0016  61   MET   A O   
1527 C  CB  . MET   A 61  ? 0.1157 0.1174 0.1068 -0.0061 -0.0017 0.0063  61   MET   A CB  
1528 C  CG  . MET   A 61  ? 0.1212 0.1258 0.1248 -0.0019 -0.0008 -0.0009 61   MET   A CG  
1529 S  SD  . MET   A 61  ? 0.1211 0.1260 0.1484 -0.0074 -0.0030 -0.0150 61   MET   A SD  
1530 C  CE  . MET   A 61  ? 0.1384 0.1354 0.1769 -0.0135 0.0139  -0.0171 61   MET   A CE  
1540 N  N   . GLN   A 62  ? 0.1117 0.1106 0.1180 -0.0065 -0.0042 -0.0006 62   GLN   A N   
1541 C  CA  . GLN   A 62  ? 0.1186 0.1075 0.1213 -0.0054 -0.0005 0.0036  62   GLN   A CA  
1542 C  C   . GLN   A 62  ? 0.1177 0.1067 0.1238 -0.0034 0.0065  0.0067  62   GLN   A C   
1543 O  O   . GLN   A 62  ? 0.1175 0.1191 0.1356 -0.0055 0.0057  -0.0017 62   GLN   A O   
1544 C  CB  . GLN   A 62  ? 0.1167 0.1040 0.1326 -0.0021 -0.0033 0.0026  62   GLN   A CB  
1545 C  CG  . GLN   A 62  ? 0.1213 0.1049 0.1235 -0.0054 -0.0109 0.0086  62   GLN   A CG  
1546 C  CD  . GLN   A 62  ? 0.1265 0.1102 0.1214 0.0000  0.0033  0.0156  62   GLN   A CD  
1547 O  OE1 . GLN   A 62  ? 0.1307 0.1220 0.1312 -0.0050 -0.0059 0.0041  62   GLN   A OE1 
1548 N  NE2 . GLN   A 62  ? 0.1339 0.1172 0.1362 0.0020  0.0066  0.0012  62   GLN   A NE2 
1557 N  N   . VAL   A 63  ? 0.1155 0.1104 0.1362 -0.0077 0.0067  -0.0125 63   VAL   A N   
1558 C  CA  . VAL   A 63  ? 0.1191 0.1229 0.1673 -0.0153 0.0010  -0.0176 63   VAL   A CA  
1559 C  C   . VAL   A 63  ? 0.1042 0.1216 0.1574 -0.0149 -0.0090 -0.0147 63   VAL   A C   
1560 O  O   . VAL   A 63  ? 0.1106 0.1234 0.1734 -0.0150 -0.0019 -0.0104 63   VAL   A O   
1561 C  CB  . VAL   A 63  ? 0.1296 0.1375 0.1948 -0.0154 -0.0100 -0.0379 63   VAL   A CB  
1562 C  CG1 . VAL   A 63  ? 0.1478 0.1572 0.2319 -0.0174 -0.0129 -0.0618 63   VAL   A CG1 
1563 C  CG2 . VAL   A 63  ? 0.1383 0.1309 0.2146 -0.0122 0.0114  -0.0353 63   VAL   A CG2 
1573 N  N   . GLU   A 64  ? 0.1071 0.1287 0.1469 -0.0073 -0.0040 -0.0074 64   GLU   A N   
1574 C  CA  . GLU   A 64  ? 0.1058 0.1265 0.1426 -0.0064 -0.0013 -0.0042 64   GLU   A CA  
1575 C  C   . GLU   A 64  ? 0.1042 0.1172 0.1450 -0.0077 0.0019  -0.0001 64   GLU   A C   
1576 O  O   . GLU   A 64  ? 0.1126 0.1260 0.1446 -0.0048 -0.0071 0.0004  64   GLU   A O   
1577 C  CB  . GLU   A 64  ? 0.1193 0.1388 0.1497 -0.0058 0.0020  -0.0036 64   GLU   A CB  
1578 C  CG  . GLU   A 64  ? 0.1284 0.1435 0.1577 -0.0096 0.0040  0.0012  64   GLU   A CG  
1579 C  CD  . GLU   A 64  ? 0.1389 0.1444 0.1555 -0.0194 0.0069  -0.0019 64   GLU   A CD  
1580 O  OE1 . GLU   A 64  ? 0.1351 0.1527 0.1822 -0.0231 0.0117  -0.0049 64   GLU   A OE1 
1581 O  OE2 . GLU   A 64  ? 0.1552 0.1458 0.1520 -0.0258 -0.0053 0.0032  64   GLU   A OE2 
1588 N  N   . SER   A 65  ? 0.1046 0.1187 0.1365 -0.0011 0.0022  0.0001  65   SER   A N   
1589 C  CA  . SER   A 65  ? 0.1125 0.1179 0.1282 -0.0032 -0.0014 -0.0025 65   SER   A CA  
1590 C  C   . SER   A 65  ? 0.1152 0.1235 0.1263 -0.0041 0.0010  -0.0039 65   SER   A C   
1591 O  O   . SER   A 65  ? 0.1200 0.1285 0.1524 -0.0018 0.0135  -0.0013 65   SER   A O   
1592 C  CB  . SER   A 65  ? 0.1116 0.1166 0.1258 -0.0102 0.0056  0.0045  65   SER   A CB  
1593 O  OG  . SER   A 65  ? 0.1117 0.1238 0.1342 -0.0083 -0.0036 0.0117  65   SER   A OG  
1599 N  N   . ASP   A 66  ? 0.1128 0.1192 0.1417 -0.0030 0.0129  0.0070  66   ASP   A N   
1600 C  CA  . ASP   A 66  ? 0.1228 0.1263 0.1485 -0.0006 0.0110  0.0120  66   ASP   A CA  
1601 C  C   . ASP   A 66  ? 0.1204 0.1255 0.1583 -0.0061 0.0130  0.0085  66   ASP   A C   
1602 O  O   . ASP   A 66  ? 0.1302 0.1386 0.1753 -0.0050 0.0275  0.0192  66   ASP   A O   
1603 C  CB  . ASP   A 66  ? 0.1299 0.1388 0.1783 0.0074  0.0100  0.0301  66   ASP   A CB  
1604 C  CG  . ASP   A 66  ? 0.1518 0.1474 0.2073 0.0035  0.0019  0.0399  66   ASP   A CG  
1605 O  OD1 . ASP   A 66  ? 0.1483 0.1771 0.1869 -0.0046 -0.0042 0.0457  66   ASP   A OD1 
1606 O  OD2 . ASP   A 66  ? 0.1706 0.1557 0.2783 0.0206  -0.0129 0.0231  66   ASP   A OD2 
1611 N  N   . ASP   A 67  ? 0.1141 0.1270 0.1683 -0.0032 0.0092  0.0155  67   ASP   A N   
1612 C  CA  . ASP   A 67  ? 0.1154 0.1415 0.1906 -0.0035 0.0064  0.0242  67   ASP   A CA  
1613 C  C   . ASP   A 67  ? 0.1197 0.1414 0.1802 0.0013  0.0122  0.0282  67   ASP   A C   
1614 O  O   . ASP   A 67  ? 0.1150 0.1523 0.2009 0.0008  0.0251  0.0318  67   ASP   A O   
1615 C  CB  . ASP   A 67  ? 0.1245 0.1502 0.2244 -0.0027 -0.0145 0.0279  67   ASP   A CB  
1616 C  CG  . ASP   A 67  ? 0.1233 0.1612 0.2549 -0.0087 -0.0273 0.0349  67   ASP   A CG  
1617 O  OD1 . ASP   A 67  ? 0.1328 0.1776 0.3357 -0.0117 -0.0334 0.0553  67   ASP   A OD1 
1618 O  OD2 . ASP   A 67  ? 0.1235 0.1679 0.2339 0.0035  -0.0219 0.0255  67   ASP   A OD2 
1623 N  N   A TYR   A 68  ? 0.1188 0.1306 0.1672 0.0023  0.0222  0.0276  68   TYR   A N   
1624 N  N   B TYR   A 68  ? 0.1204 0.1320 0.1673 0.0022  0.0134  0.0338  68   TYR   A N   
1625 C  CA  A TYR   A 68  ? 0.1277 0.1248 0.1684 0.0036  0.0329  0.0218  68   TYR   A CA  
1626 C  CA  B TYR   A 68  ? 0.1310 0.1282 0.1644 0.0028  0.0169  0.0340  68   TYR   A CA  
1627 C  C   A TYR   A 68  ? 0.1234 0.1261 0.1718 0.0021  0.0301  0.0188  68   TYR   A C   
1628 C  C   B TYR   A 68  ? 0.1245 0.1286 0.1703 0.0028  0.0248  0.0219  68   TYR   A C   
1629 O  O   A TYR   A 68  ? 0.1273 0.1263 0.1816 0.0020  0.0354  0.0203  68   TYR   A O   
1630 O  O   B TYR   A 68  ? 0.1292 0.1315 0.1785 0.0053  0.0350  0.0179  68   TYR   A O   
1631 C  CB  A TYR   A 68  ? 0.1324 0.1231 0.1813 0.0085  0.0480  0.0151  68   TYR   A CB  
1632 C  CB  B TYR   A 68  ? 0.1396 0.1284 0.1688 0.0038  0.0160  0.0425  68   TYR   A CB  
1633 C  CG  A TYR   A 68  ? 0.1320 0.1327 0.2070 0.0025  0.0666  0.0104  68   TYR   A CG  
1634 C  CG  B TYR   A 68  ? 0.1418 0.1382 0.1803 -0.0013 0.0163  0.0407  68   TYR   A CG  
1635 C  CD1 A TYR   A 68  ? 0.1369 0.1434 0.2391 -0.0145 0.0618  -0.0079 68   TYR   A CD1 
1636 C  CD1 B TYR   A 68  ? 0.1487 0.1425 0.1804 -0.0045 0.0016  0.0356  68   TYR   A CD1 
1637 C  CD2 A TYR   A 68  ? 0.1472 0.1382 0.2426 0.0110  0.0667  0.0092  68   TYR   A CD2 
1638 C  CD2 B TYR   A 68  ? 0.1484 0.1399 0.1813 0.0007  0.0101  0.0444  68   TYR   A CD2 
1639 C  CE1 A TYR   A 68  ? 0.1381 0.1508 0.2794 -0.0166 0.0622  -0.0255 68   TYR   A CE1 
1640 C  CE1 B TYR   A 68  ? 0.1554 0.1373 0.1663 -0.0028 -0.0002 0.0491  68   TYR   A CE1 
1641 C  CE2 A TYR   A 68  ? 0.1478 0.1461 0.2774 0.0097  0.0745  -0.0085 68   TYR   A CE2 
1642 C  CE2 B TYR   A 68  ? 0.1463 0.1388 0.1625 -0.0037 0.0061  0.0347  68   TYR   A CE2 
1643 C  CZ  A TYR   A 68  ? 0.1407 0.1511 0.3088 -0.0087 0.0606  -0.0391 68   TYR   A CZ  
1644 C  CZ  B TYR   A 68  ? 0.1572 0.1322 0.1475 -0.0000 0.0067  0.0461  68   TYR   A CZ  
1645 O  OH  A TYR   A 68  ? 0.1561 0.1635 0.3599 -0.0081 0.0426  -0.0708 68   TYR   A OH  
1646 O  OH  B TYR   A 68  ? 0.1759 0.1249 0.1470 0.0047  -0.0054 0.0368  68   TYR   A OH  
1665 N  N   . ILE   A 69  ? 0.1189 0.1216 0.1672 0.0022  0.0278  0.0203  69   ILE   A N   
1666 C  CA  . ILE   A 69  ? 0.1275 0.1250 0.1645 0.0018  0.0203  0.0101  69   ILE   A CA  
1667 C  C   . ILE   A 69  ? 0.1294 0.1294 0.1495 0.0025  0.0202  0.0204  69   ILE   A C   
1668 O  O   . ILE   A 69  ? 0.1386 0.1372 0.1494 -0.0028 0.0323  0.0204  69   ILE   A O   
1669 C  CB  . ILE   A 69  ? 0.1351 0.1426 0.1659 0.0027  0.0238  0.0008  69   ILE   A CB  
1670 C  CG1 . ILE   A 69  ? 0.1320 0.1569 0.1661 0.0057  0.0195  -0.0158 69   ILE   A CG1 
1671 C  CG2 . ILE   A 69  ? 0.1558 0.1584 0.1785 0.0098  0.0153  -0.0065 69   ILE   A CG2 
1672 C  CD1 . ILE   A 69  ? 0.1354 0.1635 0.1833 -0.0042 0.0203  -0.0203 69   ILE   A CD1 
1685 N  N   . ALA   A 70  ? 0.1317 0.1276 0.1539 -0.0062 0.0234  0.0163  70   ALA   A N   
1686 C  CA  . ALA   A 70  ? 0.1363 0.1416 0.1807 -0.0149 0.0291  0.0252  70   ALA   A CA  
1687 C  C   . ALA   A 70  ? 0.1349 0.1617 0.1751 -0.0113 0.0305  0.0243  70   ALA   A C   
1688 O  O   . ALA   A 70  ? 0.1518 0.1899 0.1970 0.0059  0.0506  0.0397  70   ALA   A O   
1689 C  CB  . ALA   A 70  ? 0.1349 0.1359 0.2078 -0.0170 0.0267  0.0159  70   ALA   A CB  
1695 N  N   . THR   A 71  ? 0.1308 0.1564 0.1694 -0.0042 0.0272  0.0270  71   THR   A N   
1696 C  CA  . THR   A 71  ? 0.1366 0.1676 0.2009 0.0093  0.0334  0.0265  71   THR   A CA  
1697 C  C   . THR   A 71  ? 0.1321 0.1624 0.2213 0.0116  0.0426  0.0228  71   THR   A C   
1698 O  O   . THR   A 71  ? 0.1359 0.1851 0.2596 0.0092  0.0490  0.0030  71   THR   A O   
1699 C  CB  . THR   A 71  ? 0.1608 0.1888 0.2243 0.0179  -0.0025 0.0334  71   THR   A CB  
1700 O  OG1 . THR   A 71  ? 0.1837 0.2074 0.2323 0.0099  -0.0280 0.0249  71   THR   A OG1 
1701 C  CG2 . THR   A 71  ? 0.1746 0.2054 0.2528 0.0255  -0.0121 0.0409  71   THR   A CG2 
1709 N  N   . ASN   A 72  ? 0.1357 0.1486 0.2067 0.0130  0.0396  0.0226  72   ASN   A N   
1710 C  CA  . ASN   A 72  ? 0.1420 0.1436 0.2039 0.0210  0.0445  0.0239  72   ASN   A CA  
1711 C  C   . ASN   A 72  ? 0.1549 0.1449 0.1934 0.0150  0.0518  0.0148  72   ASN   A C   
1712 O  O   . ASN   A 72  ? 0.1735 0.1476 0.2186 0.0194  0.0470  0.0007  72   ASN   A O   
1713 C  CB  . ASN   A 72  ? 0.1556 0.1533 0.2069 0.0243  0.0452  0.0252  72   ASN   A CB  
1714 C  CG  . ASN   A 72  ? 0.1777 0.1628 0.2124 0.0319  0.0450  0.0273  72   ASN   A CG  
1715 O  OD1 . ASN   A 72  ? 0.1938 0.1894 0.2340 0.0244  0.0523  0.0268  72   ASN   A OD1 
1716 N  ND2 . ASN   A 72  ? 0.1921 0.1660 0.2129 0.0534  0.0237  0.0223  72   ASN   A ND2 
1723 N  N   . GLY   A 73  ? 0.1562 0.1426 0.1775 0.0078  0.0476  0.0134  73   GLY   A N   
1724 C  CA  . GLY   A 73  ? 0.1607 0.1416 0.1590 -0.0007 0.0442  0.0129  73   GLY   A CA  
1725 C  C   . GLY   A 73  ? 0.1570 0.1299 0.1454 0.0016  0.0572  0.0238  73   GLY   A C   
1726 O  O   . GLY   A 73  ? 0.1537 0.1396 0.1669 0.0108  0.0437  0.0256  73   GLY   A O   
1730 N  N   . PRO   A 74  ? 0.1687 0.1315 0.1570 -0.0113 0.0494  0.0155  74   PRO   A N   
1731 C  CA  . PRO   A 74  ? 0.1637 0.1303 0.1592 -0.0058 0.0497  0.0204  74   PRO   A CA  
1732 C  C   . PRO   A 74  ? 0.1565 0.1206 0.1515 -0.0016 0.0380  0.0074  74   PRO   A C   
1733 O  O   . PRO   A 74  ? 0.1653 0.1247 0.1767 0.0050  0.0392  -0.0024 74   PRO   A O   
1734 C  CB  . PRO   A 74  ? 0.1767 0.1609 0.1855 -0.0013 0.0421  0.0278  74   PRO   A CB  
1735 C  CG  . PRO   A 74  ? 0.1999 0.1896 0.2223 -0.0177 0.0380  0.0164  74   PRO   A CG  
1736 C  CD  . PRO   A 74  ? 0.1859 0.1665 0.1726 -0.0227 0.0384  0.0080  74   PRO   A CD  
1744 N  N   . LEU   A 75  ? 0.1525 0.1115 0.1418 0.0002  0.0282  0.0041  75   LEU   A N   
1745 C  CA  . LEU   A 75  ? 0.1531 0.1153 0.1228 -0.0018 0.0103  0.0047  75   LEU   A CA  
1746 C  C   . LEU   A 75  ? 0.1653 0.1240 0.1221 0.0021  0.0175  0.0153  75   LEU   A C   
1747 O  O   . LEU   A 75  ? 0.2083 0.1390 0.1363 0.0083  0.0078  0.0067  75   LEU   A O   
1748 C  CB  . LEU   A 75  ? 0.1596 0.1235 0.1143 -0.0063 0.0064  0.0153  75   LEU   A CB  
1749 C  CG  . LEU   A 75  ? 0.1718 0.1570 0.1284 -0.0347 0.0054  0.0101  75   LEU   A CG  
1750 C  CD1 . LEU   A 75  ? 0.1775 0.1995 0.1423 -0.0335 0.0083  -0.0029 75   LEU   A CD1 
1751 C  CD2 . LEU   A 75  ? 0.1962 0.1957 0.1783 -0.0148 0.0089  0.0164  75   LEU   A CD2 
1763 N  N   . LYS   A 76  ? 0.1645 0.1228 0.1418 -0.0082 0.0160  -0.0006 76   LYS   A N   
1764 C  CA  . LYS   A 76  ? 0.1604 0.1387 0.1382 -0.0076 0.0128  -0.0083 76   LYS   A CA  
1765 C  C   . LYS   A 76  ? 0.1596 0.1240 0.1065 -0.0047 0.0172  0.0074  76   LYS   A C   
1766 O  O   . LYS   A 76  ? 0.1544 0.1224 0.1087 -0.0019 0.0171  0.0116  76   LYS   A O   
1767 C  CB  . LYS   A 76  ? 0.1599 0.1593 0.1822 0.0038  0.0088  -0.0223 76   LYS   A CB  
1768 C  CG  . LYS   A 76  ? 0.1670 0.1566 0.2361 0.0071  0.0100  -0.0213 76   LYS   A CG  
1769 C  CD  . LYS   A 76  ? 0.1751 0.1596 0.2729 0.0144  0.0048  -0.0300 76   LYS   A CD  
1770 C  CE  . LYS   A 76  ? 0.1870 0.1781 0.3332 0.0088  0.0045  -0.0378 76   LYS   A CE  
1771 N  NZ  . LYS   A 76  ? 0.1834 0.1794 0.3787 -0.0044 0.0020  -0.0471 76   LYS   A NZ  
1785 N  N   . VAL   A 77  ? 0.1723 0.1320 0.1073 -0.0056 0.0327  0.0159  77   VAL   A N   
1786 C  CA  . VAL   A 77  ? 0.1631 0.1309 0.1078 0.0006  0.0207  0.0149  77   VAL   A CA  
1787 C  C   . VAL   A 77  ? 0.1540 0.1323 0.1105 0.0070  0.0144  0.0051  77   VAL   A C   
1788 O  O   . VAL   A 77  ? 0.1617 0.1334 0.1084 0.0138  0.0277  0.0008  77   VAL   A O   
1789 C  CB  . VAL   A 77  ? 0.1772 0.1453 0.1276 0.0032  0.0113  0.0189  77   VAL   A CB  
1790 C  CG1 . VAL   A 77  ? 0.1736 0.1529 0.1496 0.0101  0.0012  0.0054  77   VAL   A CG1 
1791 C  CG2 . VAL   A 77  ? 0.2000 0.1536 0.1412 0.0001  0.0011  0.0265  77   VAL   A CG2 
1801 N  N   . GLY   A 78  ? 0.1468 0.1234 0.1042 0.0044  0.0206  0.0068  78   GLY   A N   
1802 C  CA  . GLY   A 78  ? 0.1456 0.1198 0.1195 0.0013  0.0240  0.0114  78   GLY   A CA  
1803 C  C   . GLY   A 78  ? 0.1365 0.1193 0.1172 0.0026  0.0294  0.0145  78   GLY   A C   
1804 O  O   . GLY   A 78  ? 0.1354 0.1230 0.1341 0.0012  0.0217  0.0230  78   GLY   A O   
1808 N  N   . GLY   A 79  ? 0.1378 0.1144 0.1160 -0.0010 0.0211  0.0166  79   GLY   A N   
1809 C  CA  . GLY   A 79  ? 0.1316 0.1216 0.1332 -0.0011 0.0206  0.0124  79   GLY   A CA  
1810 C  C   . GLY   A 79  ? 0.1184 0.1126 0.1237 0.0020  0.0160  0.0097  79   GLY   A C   
1811 O  O   . GLY   A 79  ? 0.1279 0.1254 0.1275 0.0200  0.0127  0.0063  79   GLY   A O   
1815 N  N   . SER   A 80  ? 0.1117 0.1297 0.1446 -0.0013 0.0129  -0.0036 80   SER   A N   
1816 C  CA  . SER   A 80  ? 0.1128 0.1216 0.1310 -0.0000 0.0085  0.0019  80   SER   A CA  
1817 C  C   . SER   A 80  ? 0.1141 0.1214 0.1312 -0.0014 0.0137  0.0098  80   SER   A C   
1818 O  O   . SER   A 80  ? 0.1121 0.1414 0.1659 0.0079  0.0149  -0.0002 80   SER   A O   
1819 C  CB  . SER   A 80  ? 0.1216 0.1251 0.1556 -0.0047 0.0091  0.0065  80   SER   A CB  
1820 O  OG  . SER   A 80  ? 0.1485 0.1246 0.1922 0.0045  -0.0071 0.0185  80   SER   A OG  
1826 N  N   . CYS   A 81  ? 0.1109 0.1195 0.1350 0.0025  0.0010  0.0104  81   CYS   A N   
1827 C  CA  . CYS   A 81  ? 0.1079 0.1264 0.1269 -0.0013 -0.0078 0.0179  81   CYS   A CA  
1828 C  C   . CYS   A 81  ? 0.1075 0.1212 0.1298 -0.0047 -0.0029 0.0299  81   CYS   A C   
1829 O  O   . CYS   A 81  ? 0.1096 0.1457 0.1449 0.0021  0.0013  0.0366  81   CYS   A O   
1830 C  CB  . CYS   A 81  ? 0.1180 0.1362 0.1408 -0.0143 -0.0009 0.0231  81   CYS   A CB  
1831 S  SG  . CYS   A 81  ? 0.1341 0.1231 0.1358 -0.0137 0.0017  0.0140  81   CYS   A SG  
1837 N  N   . VAL   A 82  ? 0.1122 0.1308 0.1260 0.0022  -0.0114 0.0187  82   VAL   A N   
1838 C  CA  . VAL   A 82  ? 0.1232 0.1363 0.1282 0.0028  -0.0066 0.0263  82   VAL   A CA  
1839 C  C   . VAL   A 82  ? 0.1210 0.1341 0.1295 0.0001  -0.0112 0.0237  82   VAL   A C   
1840 O  O   . VAL   A 82  ? 0.1162 0.1473 0.1607 -0.0013 -0.0054 0.0013  82   VAL   A O   
1841 C  CB  . VAL   A 82  ? 0.1533 0.1473 0.1427 0.0061  -0.0021 0.0272  82   VAL   A CB  
1842 C  CG1 . VAL   A 82  ? 0.1740 0.1573 0.1630 0.0133  0.0053  0.0283  82   VAL   A CG1 
1843 C  CG2 . VAL   A 82  ? 0.1571 0.1546 0.1671 -0.0001 -0.0017 0.0334  82   VAL   A CG2 
1853 N  N   . LEU   A 83  ? 0.1177 0.1310 0.1255 -0.0065 -0.0094 0.0105  83   LEU   A N   
1854 C  CA  . LEU   A 83  ? 0.1223 0.1360 0.1134 -0.0074 -0.0123 0.0051  83   LEU   A CA  
1855 C  C   . LEU   A 83  ? 0.1246 0.1377 0.1169 -0.0106 -0.0171 0.0108  83   LEU   A C   
1856 O  O   . LEU   A 83  ? 0.1320 0.1395 0.1271 -0.0113 -0.0089 0.0147  83   LEU   A O   
1857 C  CB  . LEU   A 83  ? 0.1314 0.1408 0.1184 -0.0107 -0.0146 0.0173  83   LEU   A CB  
1858 C  CG  . LEU   A 83  ? 0.1429 0.1524 0.1299 -0.0091 0.0007  0.0134  83   LEU   A CG  
1859 C  CD1 . LEU   A 83  ? 0.1584 0.1506 0.1324 -0.0251 -0.0006 0.0198  83   LEU   A CD1 
1860 C  CD2 . LEU   A 83  ? 0.1387 0.1711 0.1417 -0.0114 0.0178  0.0176  83   LEU   A CD2 
1872 N  N   . SER   A 84  ? 0.1349 0.1411 0.1246 -0.0120 -0.0121 0.0173  84   SER   A N   
1873 C  CA  . SER   A 84  ? 0.1474 0.1480 0.1135 -0.0106 -0.0076 0.0145  84   SER   A CA  
1874 C  C   . SER   A 84  ? 0.1504 0.1453 0.1032 -0.0119 -0.0021 0.0096  84   SER   A C   
1875 O  O   . SER   A 84  ? 0.1494 0.1549 0.1043 -0.0096 -0.0103 0.0086  84   SER   A O   
1876 C  CB  . SER   A 84  ? 0.1508 0.1683 0.1223 -0.0094 -0.0116 0.0066  84   SER   A CB  
1877 O  OG  . SER   A 84  ? 0.1556 0.1883 0.1298 -0.0086 -0.0209 -0.0025 84   SER   A OG  
1883 N  N   . GLY   A 85  ? 0.1616 0.1562 0.1120 -0.0176 0.0088  0.0088  85   GLY   A N   
1884 C  CA  . GLY   A 85  ? 0.1666 0.1661 0.1270 -0.0278 0.0124  -0.0038 85   GLY   A CA  
1885 C  C   . GLY   A 85  ? 0.1637 0.1708 0.1008 -0.0168 -0.0043 0.0028  85   GLY   A C   
1886 O  O   . GLY   A 85  ? 0.1591 0.1812 0.1127 -0.0239 0.0057  -0.0026 85   GLY   A O   
1890 N  N   . HIS   A 86  ? 0.1695 0.1610 0.0969 -0.0111 -0.0068 0.0050  86   HIS   A N   
1891 C  CA  . HIS   A 86  ? 0.1806 0.1694 0.0959 -0.0129 -0.0051 0.0038  86   HIS   A CA  
1892 C  C   . HIS   A 86  ? 0.1985 0.1794 0.0997 -0.0109 -0.0095 0.0033  86   HIS   A C   
1893 O  O   . HIS   A 86  ? 0.2110 0.2013 0.1055 -0.0063 0.0015  0.0046  86   HIS   A O   
1894 C  CB  . HIS   A 86  ? 0.1746 0.1626 0.1096 -0.0108 0.0003  0.0068  86   HIS   A CB  
1895 C  CG  . HIS   A 86  ? 0.1728 0.1570 0.1107 -0.0063 0.0059  0.0128  86   HIS   A CG  
1896 N  ND1 . HIS   A 86  ? 0.1814 0.1602 0.1369 -0.0167 0.0043  0.0114  86   HIS   A ND1 
1897 C  CD2 . HIS   A 86  ? 0.1717 0.1553 0.1035 0.0043  0.0118  0.0189  86   HIS   A CD2 
1898 C  CE1 . HIS   A 86  ? 0.1740 0.1614 0.1406 -0.0140 0.0168  0.0212  86   HIS   A CE1 
1899 N  NE2 . HIS   A 86  ? 0.1722 0.1558 0.1319 0.0049  0.0130  0.0285  86   HIS   A NE2 
1907 N  N   . ASN   A 87  ? 0.2095 0.1871 0.1064 -0.0047 0.0109  0.0009  87   ASN   A N   
1908 C  CA  . ASN   A 87  ? 0.2298 0.2025 0.1130 -0.0073 0.0342  -0.0097 87   ASN   A CA  
1909 C  C   . ASN   A 87  ? 0.2267 0.2160 0.1394 -0.0124 0.0534  -0.0002 87   ASN   A C   
1910 O  O   . ASN   A 87  ? 0.2487 0.2331 0.1843 -0.0272 0.0836  -0.0058 87   ASN   A O   
1911 C  CB  . ASN   A 87  ? 0.2475 0.2116 0.1193 0.0013  0.0381  -0.0137 87   ASN   A CB  
1912 C  CG  . ASN   A 87  ? 0.2603 0.2184 0.1324 0.0104  0.0424  -0.0009 87   ASN   A CG  
1913 O  OD1 . ASN   A 87  ? 0.2734 0.2138 0.1323 0.0259  0.0383  0.0087  87   ASN   A OD1 
1914 N  ND2 . ASN   A 87  ? 0.2615 0.2388 0.1404 0.0071  0.0476  0.0056  87   ASN   A ND2 
1921 N  N   . LEU   A 88  ? 0.1982 0.2062 0.1302 -0.0150 0.0283  0.0160  88   LEU   A N   
1922 C  CA  . LEU   A 88  ? 0.1830 0.2027 0.1501 -0.0152 0.0265  0.0270  88   LEU   A CA  
1923 C  C   . LEU   A 88  ? 0.1750 0.2009 0.1451 -0.0164 0.0184  0.0365  88   LEU   A C   
1924 O  O   . LEU   A 88  ? 0.1751 0.2058 0.1864 -0.0171 0.0256  0.0549  88   LEU   A O   
1925 C  CB  . LEU   A 88  ? 0.1818 0.2143 0.1522 -0.0168 -0.0030 0.0444  88   LEU   A CB  
1926 C  CG  . LEU   A 88  ? 0.1943 0.2284 0.1838 -0.0204 -0.0122 0.0415  88   LEU   A CG  
1927 C  CD1 . LEU   A 88  ? 0.2043 0.2371 0.1775 -0.0229 -0.0077 0.0274  88   LEU   A CD1 
1928 C  CD2 . LEU   A 88  ? 0.2073 0.2389 0.2239 -0.0155 -0.0135 0.0292  88   LEU   A CD2 
1940 N  N   . ALA   A 89  ? 0.1744 0.1951 0.1194 -0.0131 0.0147  0.0121  89   ALA   A N   
1941 C  CA  . ALA   A 89  ? 0.1798 0.1925 0.1040 -0.0162 0.0072  0.0165  89   ALA   A CA  
1942 C  C   . ALA   A 89  ? 0.1815 0.1953 0.1150 -0.0109 -0.0116 0.0156  89   ALA   A C   
1943 O  O   . ALA   A 89  ? 0.1779 0.1888 0.1547 -0.0182 -0.0210 -0.0073 89   ALA   A O   
1944 C  CB  . ALA   A 89  ? 0.1770 0.1949 0.0898 -0.0203 0.0005  0.0186  89   ALA   A CB  
1950 N  N   . LYS   A 90  ? 0.1915 0.2058 0.1128 -0.0184 -0.0285 0.0253  90   LYS   A N   
1951 C  CA  . LYS   A 90  ? 0.1982 0.2174 0.1119 -0.0148 -0.0378 0.0234  90   LYS   A CA  
1952 C  C   . LYS   A 90  ? 0.1771 0.2023 0.1127 -0.0122 -0.0329 0.0161  90   LYS   A C   
1953 O  O   . LYS   A 90  ? 0.1811 0.2157 0.1360 -0.0213 -0.0295 0.0043  90   LYS   A O   
1954 C  CB  . LYS   A 90  ? 0.2239 0.2475 0.1583 -0.0076 -0.0427 0.0471  90   LYS   A CB  
1955 C  CG  . LYS   A 90  ? 0.2551 0.2763 0.2532 0.0003  -0.0454 0.0576  90   LYS   A CG  
1956 C  CD  . LYS   A 90  ? 0.2963 0.3107 0.3517 0.0014  -0.0359 0.0619  90   LYS   A CD  
1957 C  CE  . LYS   A 90  ? 0.3271 0.3410 0.4257 -0.0008 -0.0237 0.0586  90   LYS   A CE  
1958 N  NZ  . LYS   A 90  ? 0.3384 0.3465 0.4746 -0.0024 -0.0146 0.0525  90   LYS   A NZ  
1972 N  N   . HIS   A 91  ? 0.1691 0.1760 0.0965 -0.0122 -0.0302 0.0125  91   HIS   A N   
1973 C  CA  . HIS   A 91  ? 0.1579 0.1637 0.1066 -0.0092 -0.0285 0.0155  91   HIS   A CA  
1974 C  C   . HIS   A 91  ? 0.1427 0.1496 0.0950 -0.0145 -0.0171 0.0166  91   HIS   A C   
1975 O  O   . HIS   A 91  ? 0.1395 0.1602 0.0995 -0.0145 -0.0042 0.0217  91   HIS   A O   
1976 C  CB  . HIS   A 91  ? 0.1703 0.1898 0.1503 0.0113  -0.0391 0.0105  91   HIS   A CB  
1977 C  CG  . HIS   A 91  ? 0.2078 0.2372 0.2140 0.0209  -0.0670 0.0120  91   HIS   A CG  
1978 N  ND1 . HIS   A 91  ? 0.2161 0.2651 0.2583 0.0224  -0.0724 -0.0094 91   HIS   A ND1 
1979 C  CD2 . HIS   A 91  ? 0.2324 0.2577 0.2356 0.0266  -0.0814 0.0264  91   HIS   A CD2 
1980 C  CE1 . HIS   A 91  ? 0.2256 0.2738 0.2715 0.0275  -0.0769 0.0021  91   HIS   A CE1 
1981 N  NE2 . HIS   A 91  ? 0.2413 0.2733 0.2651 0.0317  -0.0816 0.0151  91   HIS   A NE2 
1989 N  N   . CYS   A 92  ? 0.1345 0.1461 0.0890 -0.0140 -0.0128 0.0156  92   CYS   A N   
1990 C  CA  . CYS   A 92  ? 0.1261 0.1380 0.1068 -0.0148 -0.0035 0.0151  92   CYS   A CA  
1991 C  C   . CYS   A 92  ? 0.1181 0.1318 0.1064 -0.0155 -0.0015 0.0202  92   CYS   A C   
1992 O  O   . CYS   A 92  ? 0.1209 0.1419 0.1176 -0.0165 -0.0072 0.0136  92   CYS   A O   
1993 C  CB  . CYS   A 92  ? 0.1294 0.1394 0.1230 -0.0045 -0.0088 0.0145  92   CYS   A CB  
1994 S  SG  . CYS   A 92  ? 0.1279 0.1277 0.1109 -0.0111 -0.0049 0.0115  92   CYS   A SG  
2000 N  N   . LEU   A 93  ? 0.1185 0.1183 0.1094 -0.0096 0.0045  0.0189  93   LEU   A N   
2001 C  CA  . LEU   A 93  ? 0.1113 0.1181 0.1000 -0.0026 0.0032  0.0094  93   LEU   A CA  
2002 C  C   . LEU   A 93  ? 0.1089 0.1091 0.0986 -0.0028 0.0022  0.0062  93   LEU   A C   
2003 O  O   . LEU   A 93  ? 0.1072 0.1188 0.0981 -0.0017 0.0009  0.0151  93   LEU   A O   
2004 C  CB  . LEU   A 93  ? 0.1196 0.1155 0.1153 0.0010  -0.0025 0.0190  93   LEU   A CB  
2005 C  CG  . LEU   A 93  ? 0.1261 0.1157 0.1191 -0.0010 0.0062  0.0270  93   LEU   A CG  
2006 C  CD1 . LEU   A 93  ? 0.1324 0.1203 0.1498 0.0053  0.0156  0.0171  93   LEU   A CD1 
2007 C  CD2 . LEU   A 93  ? 0.1452 0.1187 0.1444 -0.0025 0.0033  0.0135  93   LEU   A CD2 
2019 N  N   . HIS   A 94  ? 0.1039 0.1108 0.1080 0.0010  0.0049  0.0164  94   HIS   A N   
2020 C  CA  . HIS   A 94  ? 0.1056 0.1113 0.1025 -0.0046 -0.0039 0.0168  94   HIS   A CA  
2021 C  C   . HIS   A 94  ? 0.1052 0.1096 0.1044 -0.0074 -0.0007 0.0123  94   HIS   A C   
2022 O  O   . HIS   A 94  ? 0.1030 0.1283 0.1346 0.0027  0.0006  -0.0074 94   HIS   A O   
2023 C  CB  . HIS   A 94  ? 0.1058 0.1107 0.1111 -0.0018 -0.0035 0.0146  94   HIS   A CB  
2024 C  CG  . HIS   A 94  ? 0.1076 0.1135 0.1063 -0.0017 0.0018  0.0129  94   HIS   A CG  
2025 N  ND1 . HIS   A 94  ? 0.1109 0.1078 0.1143 -0.0066 0.0023  0.0168  94   HIS   A ND1 
2026 C  CD2 . HIS   A 94  ? 0.1131 0.1221 0.1154 -0.0024 -0.0040 0.0076  94   HIS   A CD2 
2027 C  CE1 . HIS   A 94  ? 0.1165 0.1088 0.1099 -0.0070 -0.0040 0.0079  94   HIS   A CE1 
2028 N  NE2 . HIS   A 94  ? 0.1173 0.1156 0.1126 -0.0073 -0.0047 0.0089  94   HIS   A NE2 
2036 N  N   . VAL   A 95  ? 0.1037 0.1025 0.0899 -0.0043 0.0082  0.0017  95   VAL   A N   
2037 C  CA  . VAL   A 95  ? 0.1104 0.1060 0.1010 -0.0018 0.0081  0.0149  95   VAL   A CA  
2038 C  C   . VAL   A 95  ? 0.1092 0.1054 0.0832 -0.0122 0.0005  0.0024  95   VAL   A C   
2039 O  O   . VAL   A 95  ? 0.1176 0.1187 0.0985 0.0097  0.0050  0.0066  95   VAL   A O   
2040 C  CB  . VAL   A 95  ? 0.1139 0.1109 0.1176 -0.0096 0.0069  0.0045  95   VAL   A CB  
2041 C  CG1 . VAL   A 95  ? 0.1324 0.1174 0.1296 -0.0144 -0.0009 -0.0022 95   VAL   A CG1 
2042 C  CG2 . VAL   A 95  ? 0.1181 0.1099 0.1109 -0.0135 0.0065  0.0192  95   VAL   A CG2 
2052 N  N   . VAL   A 96  ? 0.1145 0.1105 0.0826 -0.0022 0.0044  0.0106  96   VAL   A N   
2053 C  CA  . VAL   A 96  ? 0.1227 0.1107 0.0998 -0.0003 0.0100  0.0141  96   VAL   A CA  
2054 C  C   . VAL   A 96  ? 0.1262 0.1201 0.1020 -0.0008 0.0136  0.0147  96   VAL   A C   
2055 O  O   . VAL   A 96  ? 0.1342 0.1210 0.1249 -0.0029 0.0183  -0.0016 96   VAL   A O   
2056 C  CB  . VAL   A 96  ? 0.1262 0.1185 0.1116 0.0008  0.0220  0.0146  96   VAL   A CB  
2057 C  CG1 . VAL   A 96  ? 0.1343 0.1254 0.0947 0.0007  0.0122  0.0117  96   VAL   A CG1 
2058 C  CG2 . VAL   A 96  ? 0.1292 0.1262 0.1273 -0.0121 0.0153  0.0123  96   VAL   A CG2 
2068 N  N   A GLY   A 97  ? 0.1230 0.1218 0.1099 -0.0068 0.0081  0.0083  97   GLY   A N   
2069 N  N   B GLY   A 97  ? 0.1256 0.1241 0.0945 -0.0075 0.0065  0.0108  97   GLY   A N   
2070 C  CA  A GLY   A 97  ? 0.1318 0.1307 0.1107 -0.0059 0.0010  0.0110  97   GLY   A CA  
2071 C  CA  B GLY   A 97  ? 0.1357 0.1334 0.0874 -0.0085 0.0020  0.0160  97   GLY   A CA  
2072 C  C   A GLY   A 97  ? 0.1324 0.1366 0.0872 -0.0044 0.0030  0.0076  97   GLY   A C   
2073 C  C   B GLY   A 97  ? 0.1386 0.1389 0.0854 -0.0061 0.0050  0.0123  97   GLY   A C   
2074 O  O   A GLY   A 97  ? 0.1388 0.1367 0.1020 -0.0011 0.0073  0.0059  97   GLY   A O   
2075 O  O   B GLY   A 97  ? 0.1484 0.1428 0.1005 -0.0067 0.0017  0.0170  97   GLY   A O   
2082 N  N   A PRO   A 98  ? 0.1370 0.1333 0.0581 0.0045  -0.0074 0.0115  98   PRO   A N   
2083 N  N   B PRO   A 98  ? 0.1459 0.1379 0.1089 0.0031  0.0056  0.0189  98   PRO   A N   
2084 C  CA  A PRO   A 98  ? 0.1439 0.1458 0.0617 0.0090  0.0017  0.0029  98   PRO   A CA  
2085 C  CA  B PRO   A 98  ? 0.1582 0.1420 0.1266 0.0035  0.0083  0.0103  98   PRO   A CA  
2086 C  C   A PRO   A 98  ? 0.1390 0.1523 0.0609 0.0037  0.0018  0.0116  98   PRO   A C   
2087 C  C   B PRO   A 98  ? 0.1801 0.1411 0.1267 -0.0007 0.0050  0.0212  98   PRO   A C   
2088 O  O   A PRO   A 98  ? 0.1304 0.1413 0.0764 0.0053  0.0027  0.0159  98   PRO   A O   
2089 O  O   B PRO   A 98  ? 0.1766 0.1351 0.1531 0.0032  0.0109  0.0178  98   PRO   A O   
2090 C  CB  A PRO   A 98  ? 0.1533 0.1496 0.0598 0.0152  -0.0050 -0.0038 98   PRO   A CB  
2091 C  CB  B PRO   A 98  ? 0.1575 0.1348 0.1291 0.0125  0.0029  0.0096  98   PRO   A CB  
2092 C  CG  A PRO   A 98  ? 0.1485 0.1382 0.0743 0.0146  -0.0071 -0.0128 98   PRO   A CG  
2093 C  CG  B PRO   A 98  ? 0.1600 0.1311 0.1444 0.0126  -0.0015 0.0219  98   PRO   A CG  
2094 C  CD  A PRO   A 98  ? 0.1409 0.1307 0.0586 0.0100  -0.0053 0.0090  98   PRO   A CD  
2095 C  CD  B PRO   A 98  ? 0.1506 0.1318 0.1211 0.0107  0.0010  0.0214  98   PRO   A CD  
2110 N  N   A ASN   A 99  ? 0.1439 0.1702 0.0771 0.0050  0.0103  0.0256  99   ASN   A N   
2111 N  N   B ASN   A 99  ? 0.2096 0.1442 0.1082 0.0008  0.0031  0.0349  99   ASN   A N   
2112 C  CA  A ASN   A 99  ? 0.1632 0.1825 0.0849 -0.0013 0.0094  0.0252  99   ASN   A CA  
2113 C  CA  B ASN   A 99  ? 0.2431 0.1524 0.1081 0.0067  -0.0056 0.0456  99   ASN   A CA  
2114 C  C   A ASN   A 99  ? 0.1868 0.2037 0.0774 -0.0153 0.0092  0.0310  99   ASN   A C   
2115 C  C   B ASN   A 99  ? 0.2670 0.1607 0.1041 0.0072  -0.0202 0.0492  99   ASN   A C   
2116 O  O   A ASN   A 99  ? 0.1993 0.2194 0.0950 -0.0108 0.0044  0.0256  99   ASN   A O   
2117 O  O   B ASN   A 99  ? 0.2666 0.1506 0.1025 0.0117  -0.0227 0.0300  99   ASN   A O   
2118 C  CB  A ASN   A 99  ? 0.1620 0.1820 0.0913 -0.0033 0.0025  0.0330  99   ASN   A CB  
2119 C  CB  B ASN   A 99  ? 0.2520 0.1521 0.1349 0.0148  -0.0122 0.0429  99   ASN   A CB  
2120 C  CG  A ASN   A 99  ? 0.1610 0.1795 0.0995 -0.0000 -0.0039 0.0258  99   ASN   A CG  
2121 C  CG  B ASN   A 99  ? 0.2613 0.1618 0.1590 0.0160  -0.0146 0.0365  99   ASN   A CG  
2122 O  OD1 A ASN   A 99  ? 0.1694 0.1890 0.1057 0.0098  -0.0040 0.0148  99   ASN   A OD1 
2123 O  OD1 B ASN   A 99  ? 0.2630 0.1676 0.1547 0.0169  -0.0148 0.0421  99   ASN   A OD1 
2124 N  ND2 A ASN   A 99  ? 0.1610 0.1782 0.1202 -0.0005 -0.0136 0.0296  99   ASN   A ND2 
2125 N  ND2 B ASN   A 99  ? 0.2659 0.1671 0.1887 0.0208  -0.0234 0.0226  99   ASN   A ND2 
2138 N  N   A VAL   A 100 ? 0.2019 0.2103 0.0877 -0.0307 -0.0159 0.0277  100  VAL   A N   
2139 N  N   B VAL   A 100 ? 0.2879 0.1857 0.1332 0.0016  -0.0317 0.0455  100  VAL   A N   
2140 C  CA  A VAL   A 100 ? 0.2254 0.2272 0.1232 -0.0363 -0.0245 0.0267  100  VAL   A CA  
2141 C  CA  B VAL   A 100 ? 0.3104 0.2016 0.1730 -0.0044 -0.0445 0.0436  100  VAL   A CA  
2142 C  C   A VAL   A 100 ? 0.2358 0.2437 0.1207 -0.0408 -0.0212 0.0477  100  VAL   A C   
2143 C  C   B VAL   A 100 ? 0.3230 0.2070 0.1737 -0.0040 -0.0575 0.0455  100  VAL   A C   
2144 O  O   A VAL   A 100 ? 0.2405 0.2532 0.1242 -0.0396 -0.0070 0.0477  100  VAL   A O   
2145 O  O   B VAL   A 100 ? 0.3281 0.2038 0.1725 -0.0108 -0.0519 0.0387  100  VAL   A O   
2146 C  CB  A VAL   A 100 ? 0.2407 0.2258 0.1740 -0.0400 -0.0367 0.0210  100  VAL   A CB  
2147 C  CB  B VAL   A 100 ? 0.3200 0.2150 0.2070 -0.0065 -0.0482 0.0365  100  VAL   A CB  
2148 C  CG1 A VAL   A 100 ? 0.2420 0.2267 0.1991 -0.0480 -0.0330 0.0210  100  VAL   A CG1 
2149 C  CG1 B VAL   A 100 ? 0.3217 0.2158 0.2275 -0.0056 -0.0488 0.0374  100  VAL   A CG1 
2150 C  CG2 A VAL   A 100 ? 0.2483 0.2223 0.1862 -0.0416 -0.0400 0.0204  100  VAL   A CG2 
2151 C  CG2 B VAL   A 100 ? 0.3222 0.2219 0.2157 -0.0059 -0.0483 0.0290  100  VAL   A CG2 
2170 N  N   A ASN   A 101 ? 0.2429 0.2498 0.1353 -0.0456 -0.0257 0.0693  101  ASN   A N   
2171 N  N   B ASN   A 101 ? 0.3312 0.2193 0.1743 0.0027  -0.0692 0.0552  101  ASN   A N   
2172 C  CA  A ASN   A 101 ? 0.2614 0.2587 0.1528 -0.0493 -0.0270 0.0828  101  ASN   A CA  
2173 C  CA  B ASN   A 101 ? 0.3425 0.2329 0.1852 0.0073  -0.0671 0.0613  101  ASN   A CA  
2174 C  C   A ASN   A 101 ? 0.2832 0.2840 0.1685 -0.0558 -0.0010 0.1017  101  ASN   A C   
2175 C  C   B ASN   A 101 ? 0.3579 0.2506 0.1800 0.0055  -0.0443 0.0768  101  ASN   A C   
2176 O  O   A ASN   A 101 ? 0.2956 0.2892 0.2009 -0.0534 0.0010  0.0990  101  ASN   A O   
2177 O  O   B ASN   A 101 ? 0.3642 0.2531 0.1690 0.0044  -0.0371 0.0856  101  ASN   A O   
2178 C  CB  A ASN   A 101 ? 0.2610 0.2437 0.1477 -0.0438 -0.0485 0.0739  101  ASN   A CB  
2179 C  CB  B ASN   A 101 ? 0.3373 0.2267 0.1990 0.0087  -0.0780 0.0576  101  ASN   A CB  
2180 C  CG  A ASN   A 101 ? 0.2611 0.2339 0.1434 -0.0382 -0.0648 0.0450  101  ASN   A CG  
2181 C  CG  B ASN   A 101 ? 0.3355 0.2290 0.2248 0.0073  -0.0829 0.0465  101  ASN   A CG  
2182 O  OD1 A ASN   A 101 ? 0.2589 0.2359 0.1593 -0.0268 -0.0638 0.0147  101  ASN   A OD1 
2183 O  OD1 B ASN   A 101 ? 0.3406 0.2335 0.2501 -0.0015 -0.0766 0.0389  101  ASN   A OD1 
2184 N  ND2 A ASN   A 101 ? 0.2650 0.2257 0.1348 -0.0426 -0.0659 0.0464  101  ASN   A ND2 
2185 N  ND2 B ASN   A 101 ? 0.3326 0.2250 0.2405 0.0119  -0.0817 0.0375  101  ASN   A ND2 
2198 N  N   A LYS   A 102 ? 0.2904 0.3066 0.1901 -0.0623 0.0126  0.1000  102  LYS   A N   
2199 N  N   B LYS   A 102 ? 0.3654 0.2704 0.2060 0.0018  -0.0239 0.0705  102  LYS   A N   
2200 C  CA  A LYS   A 102 ? 0.3028 0.3270 0.2034 -0.0623 0.0113  0.0910  102  LYS   A CA  
2201 C  CA  B LYS   A 102 ? 0.3748 0.2883 0.2096 -0.0034 -0.0074 0.0761  102  LYS   A CA  
2202 C  C   A LYS   A 102 ? 0.3097 0.3435 0.1890 -0.0502 0.0064  0.0774  102  LYS   A C   
2203 C  C   B LYS   A 102 ? 0.3706 0.2828 0.1906 -0.0045 -0.0142 0.0805  102  LYS   A C   
2204 O  O   A LYS   A 102 ? 0.3138 0.3517 0.1959 -0.0444 0.0092  0.0718  102  LYS   A O   
2205 O  O   B LYS   A 102 ? 0.3716 0.2804 0.1932 -0.0083 -0.0123 0.0824  102  LYS   A O   
2206 C  CB  A LYS   A 102 ? 0.3125 0.3320 0.2394 -0.0700 0.0088  0.0848  102  LYS   A CB  
2207 C  CB  B LYS   A 102 ? 0.3887 0.3122 0.2646 -0.0097 0.0086  0.0619  102  LYS   A CB  
2208 C  CG  A LYS   A 102 ? 0.3196 0.3313 0.2652 -0.0788 0.0035  0.0797  102  LYS   A CG  
2209 C  CG  B LYS   A 102 ? 0.3998 0.3326 0.3247 -0.0151 0.0201  0.0489  102  LYS   A CG  
2210 C  CD  A LYS   A 102 ? 0.3278 0.3329 0.2893 -0.0825 -0.0025 0.0690  102  LYS   A CD  
2211 C  CD  B LYS   A 102 ? 0.4094 0.3531 0.3830 -0.0181 0.0264  0.0359  102  LYS   A CD  
2212 C  CE  A LYS   A 102 ? 0.3353 0.3345 0.3129 -0.0826 -0.0080 0.0569  102  LYS   A CE  
2213 C  CE  B LYS   A 102 ? 0.4167 0.3678 0.4288 -0.0207 0.0287  0.0278  102  LYS   A CE  
2214 N  NZ  A LYS   A 102 ? 0.3385 0.3336 0.3239 -0.0866 -0.0103 0.0479  102  LYS   A NZ  
2215 N  NZ  B LYS   A 102 ? 0.4207 0.3760 0.4566 -0.0224 0.0300  0.0246  102  LYS   A NZ  
2242 N  N   A GLY   A 103 ? 0.3112 0.3533 0.1897 -0.0412 0.0010  0.0530  103  GLY   A N   
2243 N  N   B GLY   A 103 ? 0.3640 0.2802 0.1764 -0.0044 -0.0263 0.0732  103  GLY   A N   
2244 C  CA  A GLY   A 103 ? 0.3142 0.3608 0.1959 -0.0328 0.0019  0.0340  103  GLY   A CA  
2245 C  CA  B GLY   A 103 ? 0.3554 0.2739 0.1713 -0.0103 -0.0286 0.0699  103  GLY   A CA  
2246 C  C   A GLY   A 103 ? 0.3118 0.3669 0.1952 -0.0287 0.0102  0.0215  103  GLY   A C   
2247 C  C   B GLY   A 103 ? 0.3393 0.2625 0.1457 -0.0166 -0.0253 0.0702  103  GLY   A C   
2248 O  O   A GLY   A 103 ? 0.3175 0.3700 0.2088 -0.0293 0.0158  0.0142  103  GLY   A O   
2249 O  O   B GLY   A 103 ? 0.3459 0.2648 0.1605 -0.0156 -0.0263 0.0697  103  GLY   A O   
2256 N  N   A GLU   A 104 ? 0.2996 0.3671 0.1751 -0.0274 0.0170  0.0140  104  GLU   A N   
2257 N  N   B GLU   A 104 ? 0.3151 0.2469 0.1229 -0.0195 -0.0299 0.0628  104  GLU   A N   
2258 C  CA  A GLU   A 104 ? 0.2824 0.3645 0.1613 -0.0313 0.0202  0.0105  104  GLU   A CA  
2259 C  CA  B GLU   A 104 ? 0.2892 0.2278 0.0986 -0.0253 -0.0293 0.0478  104  GLU   A CA  
2260 C  C   A GLU   A 104 ? 0.2834 0.3717 0.1745 -0.0274 0.0211  0.0012  104  GLU   A C   
2261 C  C   B GLU   A 104 ? 0.2672 0.2178 0.1084 -0.0193 -0.0203 0.0262  104  GLU   A C   
2262 O  O   A GLU   A 104 ? 0.2803 0.3722 0.1939 -0.0290 0.0180  -0.0068 104  GLU   A O   
2263 O  O   B GLU   A 104 ? 0.2626 0.2161 0.1490 -0.0181 -0.0239 0.0192  104  GLU   A O   
2264 C  CB  A GLU   A 104 ? 0.2626 0.3549 0.1497 -0.0413 0.0247  0.0210  104  GLU   A CB  
2265 C  CB  B GLU   A 104 ? 0.2777 0.2226 0.0971 -0.0320 -0.0239 0.0551  104  GLU   A CB  
2266 C  CG  A GLU   A 104 ? 0.2468 0.3454 0.1544 -0.0506 0.0238  0.0271  104  GLU   A CG  
2267 C  CG  B GLU   A 104 ? 0.2742 0.2256 0.1139 -0.0379 -0.0214 0.0572  104  GLU   A CG  
2268 C  CD  A GLU   A 104 ? 0.2308 0.3360 0.1581 -0.0590 0.0275  0.0358  104  GLU   A CD  
2269 C  CD  B GLU   A 104 ? 0.2717 0.2272 0.1122 -0.0420 -0.0209 0.0672  104  GLU   A CD  
2270 O  OE1 A GLU   A 104 ? 0.2163 0.3296 0.1219 -0.0628 0.0291  0.0387  104  GLU   A OE1 
2271 O  OE1 B GLU   A 104 ? 0.2688 0.2261 0.1154 -0.0429 -0.0168 0.0649  104  GLU   A OE1 
2272 O  OE2 A GLU   A 104 ? 0.2356 0.3369 0.1927 -0.0612 0.0251  0.0398  104  GLU   A OE2 
2273 O  OE2 B GLU   A 104 ? 0.2742 0.2280 0.1166 -0.0457 -0.0212 0.0736  104  GLU   A OE2 
2286 N  N   A ASP   A 105 ? 0.2876 0.3788 0.1845 -0.0204 0.0231  -0.0052 105  ASP   A N   
2287 N  N   B ASP   A 105 ? 0.2577 0.2106 0.1207 -0.0153 -0.0106 0.0183  105  ASP   A N   
2288 C  CA  A ASP   A 105 ? 0.2880 0.3834 0.2023 -0.0150 0.0255  -0.0190 105  ASP   A CA  
2289 C  CA  B ASP   A 105 ? 0.2480 0.2057 0.1437 -0.0052 0.0035  -0.0072 105  ASP   A CA  
2290 C  C   A ASP   A 105 ? 0.2616 0.3723 0.1808 -0.0239 0.0091  -0.0341 105  ASP   A C   
2291 C  C   B ASP   A 105 ? 0.2258 0.1898 0.1191 -0.0113 0.0088  -0.0028 105  ASP   A C   
2292 O  O   A ASP   A 105 ? 0.2552 0.3723 0.1474 -0.0212 0.0071  -0.0443 105  ASP   A O   
2293 O  O   B ASP   A 105 ? 0.2101 0.1861 0.0817 -0.0144 0.0082  -0.0088 105  ASP   A O   
2294 C  CB  A ASP   A 105 ? 0.3112 0.3970 0.2471 -0.0030 0.0374  -0.0152 105  ASP   A CB  
2295 C  CB  B ASP   A 105 ? 0.2558 0.2208 0.1936 0.0106  0.0050  -0.0275 105  ASP   A CB  
2296 C  CG  A ASP   A 105 ? 0.3310 0.4085 0.2906 0.0062  0.0403  -0.0126 105  ASP   A CG  
2297 C  CG  B ASP   A 105 ? 0.2642 0.2330 0.2391 0.0265  -0.0008 -0.0475 105  ASP   A CG  
2298 O  OD1 A ASP   A 105 ? 0.3367 0.4124 0.2991 0.0096  0.0401  -0.0193 105  ASP   A OD1 
2299 O  OD1 B ASP   A 105 ? 0.2683 0.2351 0.2364 0.0255  -0.0109 -0.0614 105  ASP   A OD1 
2300 O  OD2 A ASP   A 105 ? 0.3397 0.4134 0.3158 0.0096  0.0414  -0.0031 105  ASP   A OD2 
2301 O  OD2 B ASP   A 105 ? 0.2702 0.2416 0.2814 0.0328  -0.0101 -0.0405 105  ASP   A OD2 
2310 N  N   A ILE   A 106 ? 0.2407 0.3578 0.1994 -0.0374 -0.0146 -0.0420 106  ILE   A N   
2311 N  N   B ILE   A 106 ? 0.2208 0.1905 0.1404 -0.0048 -0.0024 0.0044  106  ILE   A N   
2312 C  CA  A ILE   A 106 ? 0.2150 0.3398 0.2208 -0.0501 -0.0294 -0.0575 106  ILE   A CA  
2313 C  CA  B ILE   A 106 ? 0.2151 0.1935 0.1623 -0.0054 -0.0102 -0.0021 106  ILE   A CA  
2314 C  C   A ILE   A 106 ? 0.1922 0.3168 0.2274 -0.0689 -0.0317 -0.0817 106  ILE   A C   
2315 C  C   B ILE   A 106 ? 0.2126 0.1850 0.1704 -0.0060 -0.0099 0.0179  106  ILE   A C   
2316 O  O   A ILE   A 106 ? 0.1718 0.3113 0.2335 -0.0755 -0.0216 -0.0846 106  ILE   A O   
2317 O  O   B ILE   A 106 ? 0.2021 0.1896 0.1814 -0.0043 -0.0010 0.0149  106  ILE   A O   
2318 C  CB  A ILE   A 106 ? 0.2169 0.3426 0.2494 -0.0410 -0.0361 -0.0453 106  ILE   A CB  
2319 C  CB  B ILE   A 106 ? 0.2167 0.2145 0.2039 -0.0078 -0.0274 -0.0110 106  ILE   A CB  
2320 C  CG1 A ILE   A 106 ? 0.2145 0.3397 0.2680 -0.0331 -0.0369 -0.0321 106  ILE   A CG1 
2321 C  CG1 B ILE   A 106 ? 0.2126 0.2265 0.2137 -0.0049 -0.0313 -0.0136 106  ILE   A CG1 
2322 C  CG2 A ILE   A 106 ? 0.2196 0.3454 0.2573 -0.0383 -0.0405 -0.0473 106  ILE   A CG2 
2323 C  CG2 B ILE   A 106 ? 0.2210 0.2215 0.2193 -0.0098 -0.0320 -0.0203 106  ILE   A CG2 
2324 C  CD1 A ILE   A 106 ? 0.2135 0.3373 0.2793 -0.0267 -0.0305 -0.0249 106  ILE   A CD1 
2325 C  CD1 B ILE   A 106 ? 0.2071 0.2331 0.2236 -0.0021 -0.0283 -0.0124 106  ILE   A CD1 
2348 N  N   A GLN   A 107 ? 0.2023 0.3007 0.2455 -0.0712 -0.0270 -0.0981 107  GLN   A N   
2349 N  N   B GLN   A 107 ? 0.2236 0.1747 0.1937 0.0047  -0.0152 0.0281  107  GLN   A N   
2350 C  CA  A GLN   A 107 ? 0.2183 0.2853 0.2883 -0.0598 -0.0077 -0.0974 107  GLN   A CA  
2351 C  CA  B GLN   A 107 ? 0.2397 0.1809 0.2341 0.0068  -0.0128 0.0289  107  GLN   A CA  
2352 C  C   A GLN   A 107 ? 0.1970 0.2507 0.2706 -0.0529 0.0174  -0.0831 107  GLN   A C   
2353 C  C   B GLN   A 107 ? 0.2203 0.1643 0.2079 0.0148  -0.0043 0.0466  107  GLN   A C   
2354 O  O   A GLN   A 107 ? 0.2044 0.2515 0.3154 -0.0494 0.0303  -0.0703 107  GLN   A O   
2355 O  O   B GLN   A 107 ? 0.2245 0.1638 0.2097 0.0100  -0.0154 0.0466  107  GLN   A O   
2356 C  CB  A GLN   A 107 ? 0.2512 0.3066 0.3606 -0.0596 -0.0103 -0.0925 107  GLN   A CB  
2357 C  CB  B GLN   A 107 ? 0.2702 0.2119 0.2982 -0.0035 -0.0230 0.0211  107  GLN   A CB  
2358 C  CG  A GLN   A 107 ? 0.2823 0.3288 0.4327 -0.0578 -0.0163 -0.0818 107  GLN   A CG  
2359 C  CG  B GLN   A 107 ? 0.2991 0.2441 0.3603 -0.0118 -0.0361 0.0223  107  GLN   A CG  
2360 C  CD  A GLN   A 107 ? 0.3066 0.3447 0.4934 -0.0571 -0.0208 -0.0704 107  GLN   A CD  
2361 C  CD  B GLN   A 107 ? 0.3244 0.2737 0.4122 -0.0169 -0.0436 0.0287  107  GLN   A CD  
2362 O  OE1 A GLN   A 107 ? 0.3173 0.3522 0.5215 -0.0552 -0.0240 -0.0675 107  GLN   A OE1 
2363 O  OE1 B GLN   A 107 ? 0.3337 0.2841 0.4254 -0.0188 -0.0422 0.0371  107  GLN   A OE1 
2364 N  NE2 A GLN   A 107 ? 0.3130 0.3490 0.5118 -0.0594 -0.0217 -0.0681 107  GLN   A NE2 
2365 N  NE2 B GLN   A 107 ? 0.3305 0.2842 0.4304 -0.0184 -0.0491 0.0289  107  GLN   A NE2 
2382 N  N   A LEU   A 108 ? 0.1671 0.2109 0.2013 -0.0486 0.0243  -0.0843 108  LEU   A N   
2383 N  N   B LEU   A 108 ? 0.2012 0.1598 0.1827 0.0046  0.0180  0.0372  108  LEU   A N   
2384 C  CA  A LEU   A 108 ? 0.1556 0.1829 0.1738 -0.0277 0.0202  -0.0481 108  LEU   A CA  
2385 C  CA  B LEU   A 108 ? 0.1841 0.1520 0.1708 0.0093  0.0262  0.0252  108  LEU   A CA  
2386 C  C   A LEU   A 108 ? 0.1389 0.1519 0.1592 -0.0131 0.0166  -0.0103 108  LEU   A C   
2387 C  C   B LEU   A 108 ? 0.1540 0.1342 0.1577 0.0045  0.0261  0.0278  108  LEU   A C   
2388 O  O   A LEU   A 108 ? 0.1393 0.1552 0.1703 -0.0058 0.0156  -0.0101 108  LEU   A O   
2389 O  O   B LEU   A 108 ? 0.1548 0.1338 0.1718 0.0094  0.0367  0.0276  108  LEU   A O   
2390 C  CB  A LEU   A 108 ? 0.1603 0.1892 0.1533 -0.0346 0.0295  -0.0410 108  LEU   A CB  
2391 C  CB  B LEU   A 108 ? 0.1944 0.1642 0.1584 0.0077  0.0360  0.0232  108  LEU   A CB  
2392 C  CG  A LEU   A 108 ? 0.1680 0.2077 0.1697 -0.0328 0.0416  -0.0297 108  LEU   A CG  
2393 C  CG  B LEU   A 108 ? 0.2048 0.1802 0.1756 0.0105  0.0409  0.0222  108  LEU   A CG  
2394 C  CD1 A LEU   A 108 ? 0.1813 0.2135 0.1702 -0.0365 0.0442  -0.0287 108  LEU   A CD1 
2395 C  CD1 B LEU   A 108 ? 0.2129 0.1869 0.1770 0.0063  0.0449  0.0217  108  LEU   A CD1 
2396 C  CD2 A LEU   A 108 ? 0.1692 0.2209 0.2041 -0.0284 0.0434  -0.0128 108  LEU   A CD2 
2397 C  CD2 B LEU   A 108 ? 0.2084 0.1932 0.2104 0.0152  0.0359  0.0230  108  LEU   A CD2 
2420 N  N   . LEU   A 109 ? 0.1354 0.1425 0.1575 0.0006  0.0174  0.0218  109  LEU   A N   
2421 C  CA  . LEU   A 109 ? 0.1372 0.1345 0.1481 -0.0030 0.0053  0.0224  109  LEU   A CA  
2422 C  C   . LEU   A 109 ? 0.1234 0.1261 0.1333 -0.0085 0.0132  0.0111  109  LEU   A C   
2423 O  O   . LEU   A 109 ? 0.1323 0.1178 0.1533 -0.0061 0.0068  0.0025  109  LEU   A O   
2424 C  CB  . LEU   A 109 ? 0.1406 0.1401 0.1641 0.0069  -0.0003 0.0355  109  LEU   A CB  
2425 C  CG  . LEU   A 109 ? 0.1359 0.1506 0.1768 0.0039  0.0071  0.0456  109  LEU   A CG  
2426 C  CD1 . LEU   A 109 ? 0.1406 0.1443 0.1883 0.0042  0.0167  0.0249  109  LEU   A CD1 
2427 C  CD2 . LEU   A 109 ? 0.1342 0.1697 0.2066 0.0038  0.0072  0.0407  109  LEU   A CD2 
2440 N  N   . LYS   A 110 ? 0.1281 0.1232 0.1386 -0.0065 0.0063  0.0054  110  LYS   A N   
2441 C  CA  . LYS   A 110 ? 0.1264 0.1182 0.1435 -0.0083 0.0018  0.0136  110  LYS   A CA  
2442 C  C   . LYS   A 110 ? 0.1265 0.1112 0.1278 -0.0077 0.0082  0.0078  110  LYS   A C   
2443 O  O   . LYS   A 110 ? 0.1225 0.1137 0.1387 -0.0068 0.0074  0.0043  110  LYS   A O   
2444 C  CB  . LYS   A 110 ? 0.1282 0.1242 0.1561 -0.0080 -0.0021 0.0016  110  LYS   A CB  
2445 C  CG  . LYS   A 110 ? 0.1320 0.1258 0.1650 -0.0047 0.0012  -0.0026 110  LYS   A CG  
2446 C  CD  . LYS   A 110 ? 0.1357 0.1281 0.1903 -0.0085 -0.0022 -0.0034 110  LYS   A CD  
2447 C  CE  . LYS   A 110 ? 0.1451 0.1297 0.2060 -0.0104 0.0166  -0.0074 110  LYS   A CE  
2448 N  NZ  . LYS   A 110 ? 0.1486 0.1341 0.2184 -0.0160 0.0197  -0.0007 110  LYS   A NZ  
2462 N  N   . SER   A 111 ? 0.1271 0.1191 0.1336 -0.0056 0.0017  0.0040  111  SER   A N   
2463 C  CA  . SER   A 111 ? 0.1206 0.1227 0.1404 -0.0013 0.0089  0.0005  111  SER   A CA  
2464 C  C   . SER   A 111 ? 0.1150 0.1143 0.1298 -0.0082 0.0072  0.0128  111  SER   A C   
2465 O  O   . SER   A 111 ? 0.1256 0.1075 0.1503 -0.0046 0.0070  0.0103  111  SER   A O   
2466 C  CB  . SER   A 111 ? 0.1331 0.1403 0.1542 -0.0022 0.0182  -0.0034 111  SER   A CB  
2467 O  OG  . SER   A 111 ? 0.1804 0.1630 0.1699 0.0028  0.0290  -0.0100 111  SER   A OG  
2473 N  N   . ALA   A 112 ? 0.1191 0.1138 0.1331 -0.0029 0.0135  0.0085  112  ALA   A N   
2474 C  CA  . ALA   A 112 ? 0.1209 0.1099 0.1309 -0.0043 0.0181  0.0050  112  ALA   A CA  
2475 C  C   . ALA   A 112 ? 0.1195 0.1052 0.1327 -0.0022 0.0088  0.0038  112  ALA   A C   
2476 O  O   . ALA   A 112 ? 0.1192 0.1053 0.1424 -0.0112 0.0154  0.0083  112  ALA   A O   
2477 C  CB  . ALA   A 112 ? 0.1330 0.1112 0.1455 -0.0058 0.0137  0.0092  112  ALA   A CB  
2483 N  N   . TYR   A 113 ? 0.1090 0.1084 0.1396 -0.0042 0.0118  0.0113  113  TYR   A N   
2484 C  CA  . TYR   A 113 ? 0.1103 0.1046 0.1323 -0.0037 0.0133  0.0154  113  TYR   A CA  
2485 C  C   . TYR   A 113 ? 0.1065 0.1035 0.1323 -0.0108 0.0087  0.0104  113  TYR   A C   
2486 O  O   . TYR   A 113 ? 0.1119 0.1122 0.1399 -0.0016 0.0151  0.0102  113  TYR   A O   
2487 C  CB  . TYR   A 113 ? 0.1074 0.1145 0.1525 -0.0047 0.0036  0.0254  113  TYR   A CB  
2488 C  CG  . TYR   A 113 ? 0.1122 0.1218 0.1419 -0.0105 0.0094  0.0299  113  TYR   A CG  
2489 C  CD1 . TYR   A 113 ? 0.1177 0.1342 0.1357 -0.0048 0.0089  0.0331  113  TYR   A CD1 
2490 C  CD2 . TYR   A 113 ? 0.1145 0.1321 0.1430 -0.0117 0.0003  0.0308  113  TYR   A CD2 
2491 C  CE1 . TYR   A 113 ? 0.1218 0.1386 0.1400 -0.0020 0.0134  0.0343  113  TYR   A CE1 
2492 C  CE2 . TYR   A 113 ? 0.1186 0.1424 0.1381 -0.0093 0.0007  0.0326  113  TYR   A CE2 
2493 C  CZ  . TYR   A 113 ? 0.1165 0.1419 0.1428 0.0043  0.0124  0.0397  113  TYR   A CZ  
2494 O  OH  . TYR   A 113 ? 0.1178 0.1519 0.1657 0.0144  0.0092  0.0399  113  TYR   A OH  
2504 N  N   . GLU   A 114 ? 0.1083 0.1072 0.1451 -0.0009 0.0145  0.0106  114  GLU   A N   
2505 C  CA  . GLU   A 114 ? 0.1139 0.1049 0.1508 0.0027  0.0080  0.0164  114  GLU   A CA  
2506 C  C   . GLU   A 114 ? 0.1087 0.1082 0.1472 0.0024  0.0128  0.0126  114  GLU   A C   
2507 O  O   . GLU   A 114 ? 0.1198 0.1072 0.1445 0.0013  0.0081  0.0085  114  GLU   A O   
2508 C  CB  . GLU   A 114 ? 0.1106 0.1123 0.1516 -0.0013 0.0074  0.0123  114  GLU   A CB  
2509 C  CG  . GLU   A 114 ? 0.1198 0.1129 0.1472 -0.0009 0.0122  0.0053  114  GLU   A CG  
2510 C  CD  . GLU   A 114 ? 0.1293 0.1136 0.1586 -0.0034 0.0087  0.0013  114  GLU   A CD  
2511 O  OE1 . GLU   A 114 ? 0.1342 0.1101 0.1672 -0.0094 0.0143  -0.0008 114  GLU   A OE1 
2512 O  OE2 . GLU   A 114 ? 0.1434 0.1185 0.1857 -0.0118 0.0155  -0.0155 114  GLU   A OE2 
2519 N  N   . ASN   A 115 ? 0.1077 0.1119 0.1334 -0.0018 0.0056  0.0056  115  ASN   A N   
2520 C  CA  . ASN   A 115 ? 0.1107 0.1131 0.1342 -0.0073 0.0103  0.0102  115  ASN   A CA  
2521 C  C   . ASN   A 115 ? 0.1142 0.1065 0.1263 -0.0128 0.0065  0.0045  115  ASN   A C   
2522 O  O   . ASN   A 115 ? 0.1176 0.1244 0.1312 -0.0109 0.0085  0.0149  115  ASN   A O   
2523 C  CB  . ASN   A 115 ? 0.1164 0.1166 0.1338 -0.0111 0.0095  0.0105  115  ASN   A CB  
2524 C  CG  . ASN   A 115 ? 0.1180 0.1411 0.1429 -0.0145 0.0168  0.0125  115  ASN   A CG  
2525 O  OD1 . ASN   A 115 ? 0.1223 0.2340 0.1700 -0.0189 0.0245  0.0293  115  ASN   A OD1 
2526 N  ND2 . ASN   A 115 ? 0.1246 0.1240 0.1364 -0.0103 0.0240  0.0156  115  ASN   A ND2 
2533 N  N   . PHE   A 116 ? 0.1104 0.1149 0.1308 -0.0036 0.0124  0.0201  116  PHE   A N   
2534 C  CA  . PHE   A 116 ? 0.1117 0.1193 0.1227 -0.0026 0.0071  0.0172  116  PHE   A CA  
2535 C  C   . PHE   A 116 ? 0.1133 0.1273 0.1303 -0.0053 0.0113  0.0146  116  PHE   A C   
2536 O  O   . PHE   A 116 ? 0.1193 0.1309 0.1491 0.0025  0.0137  0.0220  116  PHE   A O   
2537 C  CB  . PHE   A 116 ? 0.1145 0.1092 0.1362 -0.0034 0.0173  0.0131  116  PHE   A CB  
2538 C  CG  . PHE   A 116 ? 0.1178 0.1119 0.1335 -0.0023 0.0129  0.0062  116  PHE   A CG  
2539 C  CD1 . PHE   A 116 ? 0.1200 0.1137 0.1352 -0.0084 0.0124  0.0157  116  PHE   A CD1 
2540 C  CD2 . PHE   A 116 ? 0.1168 0.1206 0.1446 -0.0005 0.0193  0.0117  116  PHE   A CD2 
2541 C  CE1 . PHE   A 116 ? 0.1193 0.1092 0.1456 -0.0104 0.0097  0.0124  116  PHE   A CE1 
2542 C  CE2 . PHE   A 116 ? 0.1149 0.1146 0.1542 -0.0013 0.0208  0.0115  116  PHE   A CE2 
2543 C  CZ  . PHE   A 116 ? 0.1213 0.1073 0.1416 -0.0026 0.0071  0.0137  116  PHE   A CZ  
2553 N  N   . ASN   A 117 ? 0.1127 0.1203 0.1377 -0.0033 0.0170  0.0175  117  ASN   A N   
2554 C  CA  . ASN   A 117 ? 0.1145 0.1163 0.1442 -0.0013 0.0169  0.0292  117  ASN   A CA  
2555 C  C   . ASN   A 117 ? 0.1150 0.1251 0.1545 0.0033  0.0131  0.0235  117  ASN   A C   
2556 O  O   . ASN   A 117 ? 0.1274 0.1288 0.1698 -0.0020 -0.0079 0.0372  117  ASN   A O   
2557 C  CB  . ASN   A 117 ? 0.1151 0.1168 0.1497 -0.0001 0.0151  0.0261  117  ASN   A CB  
2558 C  CG  . ASN   A 117 ? 0.1165 0.1162 0.1516 -0.0047 0.0211  0.0217  117  ASN   A CG  
2559 O  OD1 . ASN   A 117 ? 0.1219 0.1378 0.1602 -0.0096 0.0208  0.0179  117  ASN   A OD1 
2560 N  ND2 . ASN   A 117 ? 0.1126 0.1204 0.1493 -0.0001 0.0149  0.0221  117  ASN   A ND2 
2567 N  N   . GLN   A 118 ? 0.1118 0.1228 0.1642 -0.0033 0.0005  0.0235  118  GLN   A N   
2568 C  CA  . GLN   A 118 ? 0.1233 0.1357 0.1623 -0.0011 -0.0044 0.0195  118  GLN   A CA  
2569 C  C   . GLN   A 118 ? 0.1231 0.1401 0.1502 -0.0037 -0.0046 0.0231  118  GLN   A C   
2570 O  O   . GLN   A 118 ? 0.1221 0.1726 0.1811 0.0031  -0.0099 0.0044  118  GLN   A O   
2571 C  CB  . GLN   A 118 ? 0.1174 0.1368 0.1675 -0.0052 0.0107  0.0236  118  GLN   A CB  
2572 C  CG  . GLN   A 118 ? 0.1191 0.1388 0.1646 0.0031  0.0104  0.0303  118  GLN   A CG  
2573 C  CD  . GLN   A 118 ? 0.1121 0.1407 0.1797 0.0019  0.0113  0.0210  118  GLN   A CD  
2574 O  OE1 . GLN   A 118 ? 0.1212 0.1546 0.1901 0.0115  -0.0034 0.0149  118  GLN   A OE1 
2575 N  NE2 . GLN   A 118 ? 0.1215 0.1365 0.1904 0.0051  0.0050  0.0226  118  GLN   A NE2 
2584 N  N   . HIS   A 119 ? 0.1255 0.1368 0.1349 0.0011  -0.0003 0.0272  119  HIS   A N   
2585 C  CA  . HIS   A 119 ? 0.1336 0.1462 0.1358 -0.0052 -0.0014 0.0330  119  HIS   A CA  
2586 C  C   . HIS   A 119 ? 0.1416 0.1518 0.1351 -0.0042 0.0049  0.0279  119  HIS   A C   
2587 O  O   . HIS   A 119 ? 0.1485 0.1610 0.1471 -0.0231 -0.0008 0.0258  119  HIS   A O   
2588 C  CB  . HIS   A 119 ? 0.1346 0.1428 0.1619 0.0007  0.0217  0.0319  119  HIS   A CB  
2589 C  CG  . HIS   A 119 ? 0.1358 0.1461 0.2013 0.0049  0.0143  0.0383  119  HIS   A CG  
2590 N  ND1 . HIS   A 119 ? 0.1480 0.1630 0.2607 -0.0049 0.0165  0.0280  119  HIS   A ND1 
2591 C  CD2 . HIS   A 119 ? 0.1465 0.1536 0.2253 0.0152  0.0316  0.0576  119  HIS   A CD2 
2592 C  CE1 . HIS   A 119 ? 0.1478 0.1610 0.2774 -0.0064 0.0279  0.0517  119  HIS   A CE1 
2593 N  NE2 . HIS   A 119 ? 0.1596 0.1560 0.2694 0.0092  0.0410  0.0624  119  HIS   A NE2 
2601 N  N   . GLU   A 120 ? 0.1468 0.1708 0.1374 0.0037  -0.0022 0.0504  120  GLU   A N   
2602 C  CA  . GLU   A 120 ? 0.1645 0.2015 0.1615 0.0148  0.0064  0.0772  120  GLU   A CA  
2603 C  C   . GLU   A 120 ? 0.1509 0.1837 0.1433 -0.0043 0.0031  0.0691  120  GLU   A C   
2604 O  O   . GLU   A 120 ? 0.1496 0.1787 0.1532 -0.0082 0.0061  0.0624  120  GLU   A O   
2605 C  CB  . GLU   A 120 ? 0.2243 0.2664 0.2243 0.0405  0.0081  0.1370  120  GLU   A CB  
2606 C  CG  . GLU   A 120 ? 0.3242 0.3434 0.3474 0.0574  0.0161  0.1490  120  GLU   A CG  
2607 C  CD  . GLU   A 120 ? 0.3980 0.4030 0.4670 0.0709  0.0330  0.1476  120  GLU   A CD  
2608 O  OE1 . GLU   A 120 ? 0.4175 0.4238 0.4945 0.0741  0.0397  0.1461  120  GLU   A OE1 
2609 O  OE2 . GLU   A 120 ? 0.4480 0.4480 0.5221 0.0754  0.0375  0.1472  120  GLU   A OE2 
2616 N  N   . VAL   A 121 ? 0.1493 0.1813 0.1247 -0.0035 0.0015  0.0561  121  VAL   A N   
2617 C  CA  . VAL   A 121 ? 0.1523 0.1899 0.1146 -0.0065 0.0093  0.0558  121  VAL   A CA  
2618 C  C   . VAL   A 121 ? 0.1384 0.1705 0.1028 -0.0173 0.0054  0.0426  121  VAL   A C   
2619 O  O   . VAL   A 121 ? 0.1426 0.1754 0.1320 -0.0260 -0.0097 0.0332  121  VAL   A O   
2620 C  CB  . VAL   A 121 ? 0.1908 0.2288 0.1541 0.0073  0.0220  0.0651  121  VAL   A CB  
2621 C  CG1 . VAL   A 121 ? 0.1961 0.2478 0.1591 0.0158  0.0340  0.0706  121  VAL   A CG1 
2622 C  CG2 . VAL   A 121 ? 0.2133 0.2446 0.2037 0.0021  0.0217  0.0544  121  VAL   A CG2 
2632 N  N   . LEU   A 122 ? 0.1329 0.1467 0.1165 -0.0182 0.0088  0.0390  122  LEU   A N   
2633 C  CA  . LEU   A 122 ? 0.1357 0.1389 0.1212 -0.0142 0.0214  0.0331  122  LEU   A CA  
2634 C  C   . LEU   A 122 ? 0.1346 0.1364 0.1121 -0.0171 0.0093  0.0340  122  LEU   A C   
2635 O  O   . LEU   A 122 ? 0.1305 0.1421 0.1497 -0.0212 0.0098  0.0296  122  LEU   A O   
2636 C  CB  . LEU   A 122 ? 0.1532 0.1426 0.1526 -0.0070 0.0163  0.0394  122  LEU   A CB  
2637 C  CG  . LEU   A 122 ? 0.1573 0.1489 0.1390 -0.0063 0.0139  0.0308  122  LEU   A CG  
2638 C  CD1 . LEU   A 122 ? 0.1689 0.1500 0.1557 -0.0101 0.0181  0.0291  122  LEU   A CD1 
2639 C  CD2 . LEU   A 122 ? 0.1552 0.1377 0.1393 -0.0049 0.0268  0.0217  122  LEU   A CD2 
2651 N  N   . LEU   A 123 ? 0.1302 0.1341 0.1153 -0.0159 0.0054  0.0265  123  LEU   A N   
2652 C  CA  . LEU   A 123 ? 0.1272 0.1298 0.1143 -0.0132 0.0134  0.0269  123  LEU   A CA  
2653 C  C   . LEU   A 123 ? 0.1242 0.1285 0.0992 -0.0123 0.0088  0.0235  123  LEU   A C   
2654 O  O   . LEU   A 123 ? 0.1230 0.1489 0.1092 -0.0236 0.0069  0.0240  123  LEU   A O   
2655 C  CB  . LEU   A 123 ? 0.1357 0.1438 0.1190 -0.0144 0.0174  0.0270  123  LEU   A CB  
2656 C  CG  . LEU   A 123 ? 0.1398 0.1568 0.1270 -0.0112 0.0198  0.0172  123  LEU   A CG  
2657 C  CD1 . LEU   A 123 ? 0.1415 0.1626 0.1535 -0.0002 0.0130  0.0159  123  LEU   A CD1 
2658 C  CD2 . LEU   A 123 ? 0.1531 0.1638 0.1200 -0.0049 0.0064  0.0061  123  LEU   A CD2 
2670 N  N   A ALA   A 124 ? 0.1177 0.1193 0.0914 -0.0095 0.0047  0.0220  124  ALA   A N   
2671 N  N   B ALA   A 124 ? 0.1262 0.1244 0.1139 -0.0199 0.0064  0.0163  124  ALA   A N   
2672 C  CA  A ALA   A 124 ? 0.1051 0.1105 0.0908 0.0048  0.0020  0.0186  124  ALA   A CA  
2673 C  CA  B ALA   A 124 ? 0.1270 0.1237 0.1348 -0.0194 0.0020  0.0242  124  ALA   A CA  
2674 C  C   A ALA   A 124 ? 0.1004 0.1108 0.0933 0.0030  0.0123  0.0139  124  ALA   A C   
2675 C  C   B ALA   A 124 ? 0.1185 0.1144 0.1263 -0.0171 0.0091  0.0213  124  ALA   A C   
2676 O  O   A ALA   A 124 ? 0.1011 0.1210 0.1053 0.0025  0.0201  0.0168  124  ALA   A O   
2677 O  O   B ALA   A 124 ? 0.1175 0.1136 0.1373 -0.0126 0.0194  0.0144  124  ALA   A O   
2678 C  CB  A ALA   A 124 ? 0.0980 0.1062 0.1133 0.0096  0.0050  0.0257  124  ALA   A CB  
2679 C  CB  B ALA   A 124 ? 0.1376 0.1262 0.1550 -0.0206 0.0007  0.0366  124  ALA   A CB  
2690 N  N   A PRO   A 125 ? 0.1025 0.1172 0.1060 0.0028  0.0191  0.0234  125  PRO   A N   
2691 N  N   B PRO   A 125 ? 0.1078 0.1111 0.1047 -0.0086 0.0074  0.0274  125  PRO   A N   
2692 C  CA  A PRO   A 125 ? 0.1157 0.1273 0.1259 -0.0007 0.0061  0.0211  125  PRO   A CA  
2693 C  CA  B PRO   A 125 ? 0.1089 0.1215 0.1107 -0.0074 0.0068  0.0287  125  PRO   A CA  
2694 C  C   A PRO   A 125 ? 0.1075 0.1254 0.1133 -0.0068 0.0096  0.0286  125  PRO   A C   
2695 C  C   B PRO   A 125 ? 0.1127 0.1340 0.1173 -0.0048 0.0007  0.0238  125  PRO   A C   
2696 O  O   A PRO   A 125 ? 0.1143 0.1155 0.1222 -0.0108 -0.0040 0.0288  125  PRO   A O   
2697 O  O   B PRO   A 125 ? 0.1192 0.1346 0.1262 -0.0042 -0.0091 0.0113  125  PRO   A O   
2698 C  CB  A PRO   A 125 ? 0.1203 0.1272 0.1326 -0.0012 0.0066  0.0189  125  PRO   A CB  
2699 C  CB  B PRO   A 125 ? 0.1007 0.1119 0.1095 -0.0067 0.0097  0.0384  125  PRO   A CB  
2700 C  CG  A PRO   A 125 ? 0.1257 0.1248 0.1370 -0.0021 0.0119  0.0114  125  PRO   A CG  
2701 C  CG  B PRO   A 125 ? 0.0941 0.1028 0.1000 -0.0008 0.0173  0.0233  125  PRO   A CG  
2702 C  CD  A PRO   A 125 ? 0.1144 0.1224 0.1321 0.0041  0.0132  0.0117  125  PRO   A CD  
2703 C  CD  B PRO   A 125 ? 0.0991 0.0980 0.0994 -0.0040 0.0150  0.0194  125  PRO   A CD  
2718 N  N   A LEU   A 126 ? 0.1064 0.1365 0.0990 -0.0044 0.0070  0.0304  126  LEU   A N   
2719 N  N   B LEU   A 126 ? 0.1208 0.1456 0.1232 -0.0003 -0.0072 0.0241  126  LEU   A N   
2720 C  CA  A LEU   A 126 ? 0.1136 0.1441 0.1162 -0.0034 0.0026  0.0237  126  LEU   A CA  
2721 C  CA  B LEU   A 126 ? 0.1197 0.1394 0.1195 0.0002  -0.0053 0.0270  126  LEU   A CA  
2722 C  C   A LEU   A 126 ? 0.1267 0.1473 0.1207 0.0044  -0.0035 0.0302  126  LEU   A C   
2723 C  C   B LEU   A 126 ? 0.1205 0.1328 0.1183 0.0042  -0.0000 0.0273  126  LEU   A C   
2724 O  O   A LEU   A 126 ? 0.1389 0.1554 0.1337 0.0150  0.0017  0.0305  126  LEU   A O   
2725 O  O   B LEU   A 126 ? 0.1310 0.1381 0.1228 0.0088  0.0012  0.0294  126  LEU   A O   
2726 C  CB  A LEU   A 126 ? 0.1196 0.1392 0.1339 -0.0036 -0.0003 0.0212  126  LEU   A CB  
2727 C  CB  B LEU   A 126 ? 0.1295 0.1493 0.1372 -0.0056 -0.0057 0.0237  126  LEU   A CB  
2728 C  CG  A LEU   A 126 ? 0.1191 0.1429 0.1566 0.0077  0.0041  0.0185  126  LEU   A CG  
2729 C  CG  B LEU   A 126 ? 0.1336 0.1542 0.1637 -0.0094 0.0011  0.0127  126  LEU   A CG  
2730 C  CD1 A LEU   A 126 ? 0.1295 0.1485 0.1749 0.0088  0.0024  0.0222  126  LEU   A CD1 
2731 C  CD1 B LEU   A 126 ? 0.1415 0.1517 0.1928 -0.0093 -0.0058 -0.0064 126  LEU   A CD1 
2732 C  CD2 A LEU   A 126 ? 0.1253 0.1415 0.1607 -0.0005 0.0079  0.0185  126  LEU   A CD2 
2733 C  CD2 B LEU   A 126 ? 0.1324 0.1572 0.1705 -0.0147 0.0062  0.0218  126  LEU   A CD2 
2756 N  N   A LEU   A 127 ? 0.1327 0.1423 0.1291 0.0010  0.0007  0.0174  127  LEU   A N   
2757 N  N   B LEU   A 127 ? 0.1195 0.1269 0.1303 0.0009  0.0073  0.0270  127  LEU   A N   
2758 C  CA  A LEU   A 127 ? 0.1273 0.1326 0.1097 -0.0016 0.0005  0.0138  127  LEU   A CA  
2759 C  CA  B LEU   A 127 ? 0.1164 0.1269 0.1289 -0.0023 0.0057  0.0272  127  LEU   A CA  
2760 C  C   A LEU   A 127 ? 0.1248 0.1278 0.0946 -0.0006 0.0016  0.0122  127  LEU   A C   
2761 C  C   B LEU   A 127 ? 0.1133 0.1259 0.1334 -0.0055 0.0065  0.0136  127  LEU   A C   
2762 O  O   A LEU   A 127 ? 0.1335 0.1270 0.1092 -0.0023 -0.0071 0.0178  127  LEU   A O   
2763 O  O   B LEU   A 127 ? 0.1211 0.1295 0.1439 -0.0081 0.0080  0.0220  127  LEU   A O   
2764 C  CB  A LEU   A 127 ? 0.1248 0.1307 0.1012 0.0029  0.0019  0.0194  127  LEU   A CB  
2765 C  CB  B LEU   A 127 ? 0.1195 0.1378 0.1315 -0.0018 0.0026  0.0216  127  LEU   A CB  
2766 C  CG  A LEU   A 127 ? 0.1243 0.1198 0.1120 0.0086  -0.0024 0.0180  127  LEU   A CG  
2767 C  CG  B LEU   A 127 ? 0.1286 0.1563 0.1342 0.0017  -0.0046 0.0250  127  LEU   A CG  
2768 C  CD1 A LEU   A 127 ? 0.1251 0.1089 0.1229 0.0027  -0.0084 0.0110  127  LEU   A CD1 
2769 C  CD1 B LEU   A 127 ? 0.1319 0.1660 0.1451 0.0109  0.0034  0.0255  127  LEU   A CD1 
2770 C  CD2 A LEU   A 127 ? 0.1329 0.1156 0.1317 0.0081  -0.0119 0.0219  127  LEU   A CD2 
2771 C  CD2 B LEU   A 127 ? 0.1389 0.1685 0.1417 -0.0057 -0.0147 0.0093  127  LEU   A CD2 
2794 N  N   A SER   A 128 ? 0.1284 0.1316 0.0933 0.0012  0.0044  0.0155  128  SER   A N   
2795 N  N   B SER   A 128 ? 0.1200 0.1265 0.1393 -0.0066 0.0026  0.0157  128  SER   A N   
2796 C  CA  A SER   A 128 ? 0.1391 0.1320 0.0904 0.0029  0.0026  0.0178  128  SER   A CA  
2797 C  CA  B SER   A 128 ? 0.1233 0.1251 0.1195 -0.0051 -0.0018 0.0134  128  SER   A CA  
2798 C  C   A SER   A 128 ? 0.1447 0.1382 0.1010 0.0081  0.0070  0.0219  128  SER   A C   
2799 C  C   B SER   A 128 ? 0.1242 0.1198 0.1086 -0.0009 -0.0152 0.0196  128  SER   A C   
2800 O  O   A SER   A 128 ? 0.1539 0.1562 0.1198 0.0036  0.0181  0.0198  128  SER   A O   
2801 O  O   B SER   A 128 ? 0.1207 0.1291 0.1148 0.0010  -0.0139 0.0128  128  SER   A O   
2802 C  CB  A SER   A 128 ? 0.1359 0.1273 0.0905 0.0036  -0.0040 0.0210  128  SER   A CB  
2803 C  CB  B SER   A 128 ? 0.1271 0.1311 0.1211 -0.0030 -0.0057 0.0186  128  SER   A CB  
2804 O  OG  A SER   A 128 ? 0.1411 0.1406 0.1027 0.0042  0.0003  0.0127  128  SER   A OG  
2805 O  OG  B SER   A 128 ? 0.1311 0.1336 0.1228 0.0001  0.0034  0.0215  128  SER   A OG  
2816 N  N   A ALA   A 129 ? 0.1424 0.1381 0.1238 0.0032  0.0103  0.0135  129  ALA   A N   
2817 N  N   B ALA   A 129 ? 0.1260 0.1202 0.1311 -0.0006 -0.0184 0.0232  129  ALA   A N   
2818 C  CA  A ALA   A 129 ? 0.1392 0.1358 0.1351 0.0027  0.0097  0.0091  129  ALA   A CA  
2819 C  CA  B ALA   A 129 ? 0.1293 0.1221 0.1397 0.0025  -0.0197 0.0192  129  ALA   A CA  
2820 C  C   A ALA   A 129 ? 0.1422 0.1310 0.1356 -0.0013 0.0070  -0.0016 129  ALA   A C   
2821 C  C   B ALA   A 129 ? 0.1378 0.1249 0.1252 0.0034  -0.0271 0.0111  129  ALA   A C   
2822 O  O   A ALA   A 129 ? 0.1505 0.1369 0.1251 -0.0075 0.0121  0.0054  129  ALA   A O   
2823 O  O   B ALA   A 129 ? 0.1470 0.1331 0.1314 -0.0030 -0.0284 0.0218  129  ALA   A O   
2824 C  CB  A ALA   A 129 ? 0.1407 0.1402 0.1509 0.0104  0.0150  0.0067  129  ALA   A CB  
2825 C  CB  B ALA   A 129 ? 0.1311 0.1282 0.1548 0.0009  -0.0179 0.0219  129  ALA   A CB  
2836 N  N   A GLY   A 130 ? 0.1475 0.1257 0.1693 0.0001  0.0162  -0.0148 130  GLY   A N   
2837 N  N   B GLY   A 130 ? 0.1438 0.1238 0.1295 0.0029  -0.0245 0.0031  130  GLY   A N   
2838 C  CA  A GLY   A 130 ? 0.1636 0.1260 0.1812 -0.0011 0.0159  -0.0134 130  GLY   A CA  
2839 C  CA  B GLY   A 130 ? 0.1596 0.1244 0.1345 0.0049  -0.0276 0.0015  130  GLY   A CA  
2840 C  C   A GLY   A 130 ? 0.1687 0.1280 0.1747 -0.0027 0.0158  -0.0054 130  GLY   A C   
2841 C  C   B GLY   A 130 ? 0.1632 0.1262 0.1268 0.0104  -0.0432 0.0148  130  GLY   A C   
2842 O  O   A GLY   A 130 ? 0.1731 0.1325 0.1869 -0.0057 0.0161  -0.0066 130  GLY   A O   
2843 O  O   B GLY   A 130 ? 0.1609 0.1304 0.1312 0.0141  -0.0535 0.0190  130  GLY   A O   
2850 N  N   A ILE   A 131 ? 0.1782 0.1292 0.1611 -0.0099 0.0056  0.0056  131  ILE   A N   
2851 N  N   B ILE   A 131 ? 0.1771 0.1287 0.1388 0.0034  -0.0308 0.0209  131  ILE   A N   
2852 C  CA  A ILE   A 131 ? 0.1837 0.1336 0.1394 -0.0169 -0.0139 0.0076  131  ILE   A CA  
2853 C  CA  B ILE   A 131 ? 0.1880 0.1331 0.1311 -0.0001 -0.0304 0.0195  131  ILE   A CA  
2854 C  C   A ILE   A 131 ? 0.1721 0.1385 0.1210 -0.0153 -0.0169 0.0194  131  ILE   A C   
2855 C  C   B ILE   A 131 ? 0.1799 0.1364 0.1223 -0.0034 -0.0334 0.0209  131  ILE   A C   
2856 O  O   A ILE   A 131 ? 0.1831 0.1452 0.1379 -0.0119 -0.0163 0.0272  131  ILE   A O   
2857 O  O   B ILE   A 131 ? 0.1872 0.1389 0.1413 -0.0022 -0.0293 0.0213  131  ILE   A O   
2858 C  CB  A ILE   A 131 ? 0.1999 0.1398 0.1397 -0.0276 -0.0212 -0.0002 131  ILE   A CB  
2859 C  CB  B ILE   A 131 ? 0.2063 0.1432 0.1399 -0.0035 -0.0208 0.0180  131  ILE   A CB  
2860 C  CG1 A ILE   A 131 ? 0.2058 0.1569 0.1372 -0.0387 -0.0207 -0.0008 131  ILE   A CG1 
2861 C  CG1 B ILE   A 131 ? 0.2149 0.1622 0.1414 -0.0101 -0.0210 0.0226  131  ILE   A CG1 
2862 C  CG2 A ILE   A 131 ? 0.2087 0.1333 0.1488 -0.0203 -0.0178 -0.0063 131  ILE   A CG2 
2863 C  CG2 B ILE   A 131 ? 0.2140 0.1388 0.1626 0.0039  -0.0151 0.0063  131  ILE   A CG2 
2864 C  CD1 A ILE   A 131 ? 0.2085 0.1661 0.1425 -0.0391 -0.0231 -0.0051 131  ILE   A CD1 
2865 C  CD1 B ILE   A 131 ? 0.2199 0.1709 0.1537 -0.0145 -0.0202 0.0252  131  ILE   A CD1 
2888 N  N   A PHE   A 132 ? 0.1629 0.1380 0.1200 -0.0034 -0.0126 0.0196  132  PHE   A N   
2889 N  N   B PHE   A 132 ? 0.1755 0.1362 0.1300 0.0042  -0.0305 0.0244  132  PHE   A N   
2890 C  CA  A PHE   A 132 ? 0.1596 0.1468 0.1084 -0.0049 -0.0034 0.0126  132  PHE   A CA  
2891 C  CA  B PHE   A 132 ? 0.1761 0.1446 0.1327 -0.0029 -0.0211 0.0155  132  PHE   A CA  
2892 C  C   A PHE   A 132 ? 0.1531 0.1534 0.0930 -0.0078 -0.0034 0.0082  132  PHE   A C   
2893 C  C   B PHE   A 132 ? 0.1784 0.1577 0.1509 -0.0049 -0.0310 0.0177  132  PHE   A C   
2894 O  O   A PHE   A 132 ? 0.1474 0.1624 0.0970 -0.0131 -0.0056 0.0049  132  PHE   A O   
2895 O  O   B PHE   A 132 ? 0.1866 0.1765 0.1726 -0.0110 -0.0269 0.0137  132  PHE   A O   
2896 C  CB  A PHE   A 132 ? 0.1582 0.1438 0.1239 -0.0035 -0.0123 0.0215  132  PHE   A CB  
2897 C  CB  B PHE   A 132 ? 0.1729 0.1362 0.1193 -0.0049 -0.0143 0.0151  132  PHE   A CB  
2898 C  CG  A PHE   A 132 ? 0.1588 0.1398 0.1264 0.0035  -0.0189 0.0192  132  PHE   A CG  
2899 C  CG  B PHE   A 132 ? 0.1734 0.1343 0.1083 -0.0027 -0.0148 0.0004  132  PHE   A CG  
2900 C  CD1 A PHE   A 132 ? 0.1579 0.1477 0.1435 0.0112  -0.0244 0.0084  132  PHE   A CD1 
2901 C  CD1 B PHE   A 132 ? 0.1739 0.1446 0.1325 0.0029  -0.0144 -0.0142 132  PHE   A CD1 
2902 C  CD2 A PHE   A 132 ? 0.1583 0.1482 0.1411 0.0042  -0.0224 0.0146  132  PHE   A CD2 
2903 C  CD2 B PHE   A 132 ? 0.1762 0.1449 0.1196 0.0014  -0.0129 -0.0166 132  PHE   A CD2 
2904 C  CE1 A PHE   A 132 ? 0.1591 0.1513 0.1390 0.0112  -0.0270 0.0042  132  PHE   A CE1 
2905 C  CE1 B PHE   A 132 ? 0.1762 0.1514 0.1326 0.0037  -0.0102 -0.0226 132  PHE   A CE1 
2906 C  CE2 A PHE   A 132 ? 0.1538 0.1512 0.1442 0.0056  -0.0273 0.0153  132  PHE   A CE2 
2907 C  CE2 B PHE   A 132 ? 0.1736 0.1542 0.1361 0.0073  -0.0090 -0.0208 132  PHE   A CE2 
2908 C  CZ  A PHE   A 132 ? 0.1554 0.1483 0.1337 0.0050  -0.0324 0.0149  132  PHE   A CZ  
2909 C  CZ  B PHE   A 132 ? 0.1743 0.1523 0.1321 0.0021  -0.0092 -0.0221 132  PHE   A CZ  
2928 N  N   A GLY   A 133 ? 0.1563 0.1552 0.0981 -0.0035 -0.0064 0.0075  133  GLY   A N   
2929 N  N   B GLY   A 133 ? 0.1750 0.1565 0.1461 -0.0040 -0.0367 0.0242  133  GLY   A N   
2930 C  CA  A GLY   A 133 ? 0.1624 0.1668 0.1067 -0.0038 -0.0179 -0.0022 133  GLY   A CA  
2931 C  CA  B GLY   A 133 ? 0.1704 0.1604 0.1451 -0.0041 -0.0374 0.0122  133  GLY   A CA  
2932 C  C   A GLY   A 133 ? 0.1708 0.1770 0.1257 -0.0100 -0.0320 -0.0030 133  GLY   A C   
2933 C  C   B GLY   A 133 ? 0.1695 0.1646 0.1460 -0.0029 -0.0417 0.0004  133  GLY   A C   
2934 O  O   A GLY   A 133 ? 0.1762 0.1872 0.1365 -0.0084 -0.0324 -0.0104 133  GLY   A O   
2935 O  O   B GLY   A 133 ? 0.1647 0.1739 0.1583 0.0007  -0.0317 -0.0117 133  GLY   A O   
2942 N  N   A ALA   A 134 ? 0.1687 0.1699 0.1263 -0.0192 -0.0239 0.0024  134  ALA   A N   
2943 N  N   B ALA   A 134 ? 0.1683 0.1521 0.1300 -0.0036 -0.0314 0.0018  134  ALA   A N   
2944 C  CA  A ALA   A 134 ? 0.1687 0.1740 0.1490 -0.0184 -0.0242 0.0002  134  ALA   A CA  
2945 C  CA  B ALA   A 134 ? 0.1715 0.1488 0.1440 -0.0059 -0.0289 -0.0045 134  ALA   A CA  
2946 C  C   A ALA   A 134 ? 0.1669 0.1788 0.1509 -0.0189 -0.0179 0.0127  134  ALA   A C   
2947 C  C   B ALA   A 134 ? 0.1687 0.1477 0.1338 -0.0067 -0.0242 -0.0005 134  ALA   A C   
2948 O  O   A ALA   A 134 ? 0.1734 0.1810 0.1714 -0.0231 -0.0064 0.0115  134  ALA   A O   
2949 O  O   B ALA   A 134 ? 0.1673 0.1504 0.1553 -0.0118 -0.0098 0.0011  134  ALA   A O   
2950 C  CB  A ALA   A 134 ? 0.1738 0.1744 0.1675 -0.0137 -0.0267 -0.0067 134  ALA   A CB  
2951 C  CB  B ALA   A 134 ? 0.1773 0.1451 0.1661 -0.0029 -0.0272 -0.0075 134  ALA   A CB  
2962 N  N   A ASP   A 135 ? 0.1666 0.1811 0.1567 -0.0168 -0.0177 0.0280  135  ASP   A N   
2963 N  N   B ASP   A 135 ? 0.1774 0.1527 0.1411 -0.0098 -0.0290 0.0076  135  ASP   A N   
2964 C  CA  A ASP   A 135 ? 0.1660 0.1865 0.1789 -0.0206 -0.0240 0.0399  135  ASP   A CA  
2965 C  CA  B ASP   A 135 ? 0.1810 0.1555 0.1673 -0.0136 -0.0336 0.0083  135  ASP   A CA  
2966 C  C   A ASP   A 135 ? 0.1533 0.1765 0.1792 -0.0132 -0.0173 0.0526  135  ASP   A C   
2967 C  C   B ASP   A 135 ? 0.1678 0.1461 0.1729 -0.0096 -0.0289 0.0098  135  ASP   A C   
2968 O  O   A ASP   A 135 ? 0.1459 0.1756 0.1810 -0.0059 -0.0161 0.0460  135  ASP   A O   
2969 O  O   B ASP   A 135 ? 0.1653 0.1437 0.1798 -0.0104 -0.0223 0.0181  135  ASP   A O   
2970 C  CB  A ASP   A 135 ? 0.1756 0.2040 0.2155 -0.0324 -0.0362 0.0325  135  ASP   A CB  
2971 C  CB  B ASP   A 135 ? 0.1960 0.1763 0.1922 -0.0210 -0.0420 0.0051  135  ASP   A CB  
2972 C  CG  A ASP   A 135 ? 0.1857 0.2179 0.2508 -0.0461 -0.0417 0.0198  135  ASP   A CG  
2973 C  CG  B ASP   A 135 ? 0.2095 0.1990 0.2311 -0.0245 -0.0440 0.0067  135  ASP   A CG  
2974 O  OD1 A ASP   A 135 ? 0.1824 0.2211 0.2467 -0.0546 -0.0538 0.0197  135  ASP   A OD1 
2975 O  OD1 B ASP   A 135 ? 0.2133 0.2002 0.2406 -0.0238 -0.0465 0.0113  135  ASP   A OD1 
2976 O  OD2 A ASP   A 135 ? 0.2060 0.2293 0.2922 -0.0474 -0.0158 0.0147  135  ASP   A OD2 
2977 O  OD2 B ASP   A 135 ? 0.2180 0.2191 0.2646 -0.0300 -0.0460 0.0012  135  ASP   A OD2 
2986 N  N   A PRO   A 136 ? 0.1467 0.1664 0.1828 -0.0065 -0.0079 0.0628  136  PRO   A N   
2987 N  N   B PRO   A 136 ? 0.1563 0.1375 0.1800 -0.0015 -0.0200 0.0175  136  PRO   A N   
2988 C  CA  A PRO   A 136 ? 0.1422 0.1652 0.1878 -0.0039 -0.0012 0.0524  136  PRO   A CA  
2989 C  CA  B PRO   A 136 ? 0.1488 0.1413 0.1868 -0.0023 -0.0135 0.0100  136  PRO   A CA  
2990 C  C   A PRO   A 136 ? 0.1206 0.1611 0.1792 -0.0011 0.0027  0.0483  136  PRO   A C   
2991 C  C   B PRO   A 136 ? 0.1350 0.1440 0.1811 0.0004  -0.0135 0.0096  136  PRO   A C   
2992 O  O   A PRO   A 136 ? 0.1172 0.1624 0.1817 -0.0021 0.0035  0.0506  136  PRO   A O   
2993 O  O   B PRO   A 136 ? 0.1367 0.1379 0.1683 0.0006  -0.0082 0.0111  136  PRO   A O   
2994 C  CB  A PRO   A 136 ? 0.1582 0.1642 0.2095 -0.0024 0.0019  0.0473  136  PRO   A CB  
2995 C  CB  B PRO   A 136 ? 0.1592 0.1369 0.2069 -0.0022 -0.0142 0.0055  136  PRO   A CB  
2996 C  CG  A PRO   A 136 ? 0.1654 0.1659 0.2228 -0.0032 0.0000  0.0494  136  PRO   A CG  
2997 C  CG  B PRO   A 136 ? 0.1671 0.1375 0.2132 -0.0003 -0.0176 0.0087  136  PRO   A CG  
2998 C  CD  A PRO   A 136 ? 0.1587 0.1627 0.2058 -0.0001 -0.0037 0.0609  136  PRO   A CD  
2999 C  CD  B PRO   A 136 ? 0.1632 0.1365 0.2015 0.0010  -0.0150 0.0173  136  PRO   A CD  
3014 N  N   A ILE   A 137 ? 0.1204 0.1609 0.1778 0.0020  -0.0068 0.0419  137  ILE   A N   
3015 N  N   B ILE   A 137 ? 0.1308 0.1429 0.1931 -0.0012 -0.0238 0.0079  137  ILE   A N   
3016 C  CA  A ILE   A 137 ? 0.1197 0.1667 0.1841 -0.0081 -0.0084 0.0427  137  ILE   A CA  
3017 C  CA  B ILE   A 137 ? 0.1320 0.1468 0.1999 -0.0051 -0.0236 0.0012  137  ILE   A CA  
3018 C  C   A ILE   A 137 ? 0.1245 0.1614 0.1646 -0.0105 -0.0102 0.0340  137  ILE   A C   
3019 C  C   B ILE   A 137 ? 0.1313 0.1419 0.1800 -0.0095 -0.0138 0.0029  137  ILE   A C   
3020 O  O   A ILE   A 137 ? 0.1269 0.1585 0.1690 -0.0169 -0.0014 0.0259  137  ILE   A O   
3021 O  O   B ILE   A 137 ? 0.1305 0.1436 0.1862 -0.0095 -0.0040 0.0070  137  ILE   A O   
3022 C  CB  A ILE   A 137 ? 0.1240 0.1839 0.2267 -0.0133 -0.0206 0.0466  137  ILE   A CB  
3023 C  CB  B ILE   A 137 ? 0.1441 0.1586 0.2361 -0.0047 -0.0374 -0.0028 137  ILE   A CB  
3024 C  CG1 A ILE   A 137 ? 0.1352 0.1978 0.2656 -0.0111 -0.0155 0.0537  137  ILE   A CG1 
3025 C  CG1 B ILE   A 137 ? 0.1578 0.1718 0.2823 0.0056  -0.0460 0.0113  137  ILE   A CG1 
3026 C  CG2 A ILE   A 137 ? 0.1273 0.1836 0.2293 -0.0096 -0.0261 0.0388  137  ILE   A CG2 
3027 C  CG2 B ILE   A 137 ? 0.1519 0.1598 0.2427 -0.0008 -0.0387 -0.0115 137  ILE   A CG2 
3028 C  CD1 A ILE   A 137 ? 0.1470 0.2093 0.2836 -0.0052 -0.0104 0.0597  137  ILE   A CD1 
3029 C  CD1 B ILE   A 137 ? 0.1710 0.1838 0.3112 0.0067  -0.0460 0.0193  137  ILE   A CD1 
3052 N  N   A HIS   A 138 ? 0.1316 0.1621 0.1509 -0.0076 -0.0115 0.0273  138  HIS   A N   
3053 N  N   B HIS   A 138 ? 0.1324 0.1426 0.1679 -0.0104 -0.0020 -0.0058 138  HIS   A N   
3054 C  CA  A HIS   A 138 ? 0.1403 0.1708 0.1427 -0.0028 -0.0087 0.0163  138  HIS   A CA  
3055 C  CA  B HIS   A 138 ? 0.1340 0.1335 0.1592 -0.0188 -0.0013 -0.0027 138  HIS   A CA  
3056 C  C   A HIS   A 138 ? 0.1323 0.1614 0.1363 -0.0026 -0.0026 0.0187  138  HIS   A C   
3057 C  C   B HIS   A 138 ? 0.1277 0.1256 0.1411 -0.0122 0.0015  -0.0005 138  HIS   A C   
3058 O  O   A HIS   A 138 ? 0.1406 0.1612 0.1486 -0.0066 -0.0002 0.0164  138  HIS   A O   
3059 O  O   B HIS   A 138 ? 0.1370 0.1292 0.1448 -0.0137 0.0077  -0.0047 138  HIS   A O   
3060 C  CB  A HIS   A 138 ? 0.1565 0.1840 0.1473 -0.0036 -0.0179 0.0119  138  HIS   A CB  
3061 C  CB  B HIS   A 138 ? 0.1454 0.1434 0.1614 -0.0103 0.0013  -0.0180 138  HIS   A CB  
3062 C  CG  A HIS   A 138 ? 0.1687 0.1881 0.1564 -0.0054 -0.0144 0.0064  138  HIS   A CG  
3063 C  CG  B HIS   A 138 ? 0.1571 0.1550 0.1750 -0.0087 -0.0005 -0.0251 138  HIS   A CG  
3064 N  ND1 A HIS   A 138 ? 0.1798 0.1948 0.1757 -0.0068 -0.0066 -0.0027 138  HIS   A ND1 
3065 N  ND1 B HIS   A 138 ? 0.1699 0.1637 0.2038 -0.0050 -0.0001 -0.0297 138  HIS   A ND1 
3066 C  CD2 A HIS   A 138 ? 0.1739 0.1940 0.1559 -0.0031 -0.0144 0.0043  138  HIS   A CD2 
3067 C  CD2 B HIS   A 138 ? 0.1608 0.1587 0.1812 -0.0033 0.0012  -0.0192 138  HIS   A CD2 
3068 C  CE1 A HIS   A 138 ? 0.1857 0.2017 0.1745 -0.0050 -0.0087 -0.0026 138  HIS   A CE1 
3069 C  CE1 B HIS   A 138 ? 0.1716 0.1647 0.2057 0.0012  -0.0044 -0.0264 138  HIS   A CE1 
3070 N  NE2 A HIS   A 138 ? 0.1810 0.1989 0.1601 -0.0021 -0.0071 0.0022  138  HIS   A NE2 
3071 N  NE2 B HIS   A 138 ? 0.1677 0.1652 0.1966 0.0010  0.0034  -0.0203 138  HIS   A NE2 
3086 N  N   A SER   A 139 ? 0.1214 0.1485 0.1348 0.0030  0.0036  0.0184  139  SER   A N   
3087 N  N   B SER   A 139 ? 0.1230 0.1172 0.1345 -0.0098 -0.0017 0.0139  139  SER   A N   
3088 C  CA  A SER   A 139 ? 0.1162 0.1369 0.1316 -0.0025 0.0023  0.0176  139  SER   A CA  
3089 C  CA  B SER   A 139 ? 0.1174 0.1160 0.1316 -0.0010 0.0014  0.0064  139  SER   A CA  
3090 C  C   A SER   A 139 ? 0.1116 0.1335 0.1333 -0.0034 0.0066  0.0128  139  SER   A C   
3091 C  C   B SER   A 139 ? 0.1137 0.1121 0.1281 0.0007  0.0081  -0.0027 139  SER   A C   
3092 O  O   A SER   A 139 ? 0.1089 0.1309 0.1324 -0.0074 0.0144  0.0131  139  SER   A O   
3093 O  O   B SER   A 139 ? 0.1161 0.1113 0.1386 0.0008  -0.0008 0.0087  139  SER   A O   
3094 C  CB  A SER   A 139 ? 0.1168 0.1279 0.1252 -0.0056 0.0101  0.0151  139  SER   A CB  
3095 C  CB  B SER   A 139 ? 0.1215 0.1114 0.1441 -0.0010 -0.0076 0.0070  139  SER   A CB  
3096 O  OG  A SER   A 139 ? 0.1137 0.1141 0.1228 -0.0069 0.0080  0.0220  139  SER   A OG  
3097 O  OG  B SER   A 139 ? 0.1326 0.1073 0.1531 -0.0021 -0.0096 -0.0005 139  SER   A OG  
3108 N  N   A LEU   A 140 ? 0.1152 0.1393 0.1364 -0.0004 -0.0024 0.0126  140  LEU   A N   
3109 N  N   B LEU   A 140 ? 0.1114 0.1143 0.1182 -0.0045 0.0128  0.0163  140  LEU   A N   
3110 C  CA  A LEU   A 140 ? 0.1133 0.1384 0.1272 0.0002  -0.0020 0.0098  140  LEU   A CA  
3111 C  CA  B LEU   A 140 ? 0.1129 0.1105 0.1103 -0.0048 0.0101  0.0198  140  LEU   A CA  
3112 C  C   A LEU   A 140 ? 0.1130 0.1449 0.1152 -0.0011 0.0079  0.0074  140  LEU   A C   
3113 C  C   B LEU   A 140 ? 0.1060 0.1168 0.1232 -0.0049 0.0099  0.0164  140  LEU   A C   
3114 O  O   A LEU   A 140 ? 0.1148 0.1451 0.1205 0.0014  0.0101  0.0027  140  LEU   A O   
3115 O  O   B LEU   A 140 ? 0.1128 0.1183 0.1376 -0.0036 0.0036  0.0039  140  LEU   A O   
3116 C  CB  A LEU   A 140 ? 0.1177 0.1338 0.1398 -0.0005 -0.0007 0.0036  140  LEU   A CB  
3117 C  CB  B LEU   A 140 ? 0.1112 0.1134 0.1128 -0.0079 0.0079  0.0145  140  LEU   A CB  
3118 C  CG  A LEU   A 140 ? 0.1163 0.1336 0.1550 -0.0066 0.0119  -0.0004 140  LEU   A CG  
3119 C  CG  B LEU   A 140 ? 0.1138 0.1215 0.1221 -0.0129 0.0156  0.0134  140  LEU   A CG  
3120 C  CD1 A LEU   A 140 ? 0.1194 0.1338 0.1703 0.0036  0.0102  -0.0052 140  LEU   A CD1 
3121 C  CD1 B LEU   A 140 ? 0.1182 0.1279 0.1159 -0.0082 0.0169  0.0164  140  LEU   A CD1 
3122 C  CD2 A LEU   A 140 ? 0.1266 0.1343 0.1657 -0.0044 0.0235  -0.0043 140  LEU   A CD2 
3123 C  CD2 B LEU   A 140 ? 0.1186 0.1295 0.1362 -0.0088 0.0154  0.0215  140  LEU   A CD2 
3146 N  N   A ARG   A 141 ? 0.1175 0.1515 0.1235 -0.0052 0.0055  -0.0004 141  ARG   A N   
3147 N  N   B ARG   A 141 ? 0.1120 0.1267 0.1343 -0.0060 0.0053  0.0162  141  ARG   A N   
3148 C  CA  A ARG   A 141 ? 0.1276 0.1720 0.1346 -0.0175 0.0023  -0.0193 141  ARG   A CA  
3149 C  CA  B ARG   A 141 ? 0.1173 0.1423 0.1382 -0.0114 0.0078  0.0042  141  ARG   A CA  
3150 C  C   A ARG   A 141 ? 0.1225 0.1507 0.1377 -0.0194 0.0006  -0.0151 141  ARG   A C   
3151 C  C   B ARG   A 141 ? 0.1244 0.1284 0.1344 -0.0066 0.0078  0.0080  141  ARG   A C   
3152 O  O   A ARG   A 141 ? 0.1214 0.1463 0.1674 -0.0161 0.0108  -0.0158 141  ARG   A O   
3153 O  O   B ARG   A 141 ? 0.1232 0.1301 0.1427 -0.0132 0.0077  0.0040  141  ARG   A O   
3154 C  CB  A ARG   A 141 ? 0.1446 0.2134 0.1697 -0.0201 0.0011  -0.0326 141  ARG   A CB  
3155 C  CB  B ARG   A 141 ? 0.1215 0.1753 0.1336 -0.0193 0.0088  -0.0025 141  ARG   A CB  
3156 C  CG  A ARG   A 141 ? 0.1697 0.2429 0.2063 -0.0265 -0.0040 -0.0369 141  ARG   A CG  
3157 C  CG  B ARG   A 141 ? 0.1424 0.2027 0.1557 -0.0280 0.0058  -0.0060 141  ARG   A CG  
3158 C  CD  A ARG   A 141 ? 0.1791 0.2593 0.2253 -0.0425 -0.0067 -0.0290 141  ARG   A CD  
3159 C  CD  B ARG   A 141 ? 0.1546 0.2098 0.1852 -0.0326 -0.0025 -0.0033 141  ARG   A CD  
3160 N  NE  A ARG   A 141 ? 0.1779 0.2748 0.2418 -0.0540 -0.0055 -0.0170 141  ARG   A NE  
3161 N  NE  B ARG   A 141 ? 0.1659 0.2252 0.1887 -0.0231 0.0070  0.0131  141  ARG   A NE  
3162 C  CZ  A ARG   A 141 ? 0.1757 0.2905 0.2493 -0.0668 -0.0061 -0.0126 141  ARG   A CZ  
3163 C  CZ  B ARG   A 141 ? 0.1740 0.2314 0.1962 -0.0243 0.0203  0.0234  141  ARG   A CZ  
3164 N  NH1 A ARG   A 141 ? 0.1792 0.2998 0.2596 -0.0615 -0.0099 -0.0075 141  ARG   A NH1 
3165 N  NH1 B ARG   A 141 ? 0.1795 0.2419 0.2007 -0.0289 0.0138  0.0187  141  ARG   A NH1 
3166 N  NH2 A ARG   A 141 ? 0.1713 0.2985 0.2497 -0.0717 -0.0060 -0.0137 141  ARG   A NH2 
3167 N  NH2 B ARG   A 141 ? 0.1780 0.2362 0.2151 -0.0176 0.0287  0.0268  141  ARG   A NH2 
3194 N  N   A VAL   A 142 ? 0.1156 0.1394 0.1304 -0.0100 0.0011  -0.0134 142  VAL   A N   
3195 N  N   B VAL   A 142 ? 0.1236 0.1236 0.1340 0.0048  0.0164  0.0007  142  VAL   A N   
3196 C  CA  A VAL   A 142 ? 0.1152 0.1344 0.1392 -0.0065 0.0136  -0.0041 142  VAL   A CA  
3197 C  CA  B VAL   A 142 ? 0.1292 0.1175 0.1373 0.0027  0.0165  -0.0049 142  VAL   A CA  
3198 C  C   A VAL   A 142 ? 0.1100 0.1331 0.1383 -0.0094 0.0167  0.0009  142  VAL   A C   
3199 C  C   B VAL   A 142 ? 0.1182 0.1143 0.1357 -0.0006 0.0120  0.0007  142  VAL   A C   
3200 O  O   A VAL   A 142 ? 0.1114 0.1328 0.1460 -0.0026 0.0075  -0.0007 142  VAL   A O   
3201 O  O   B VAL   A 142 ? 0.1183 0.1139 0.1533 0.0011  0.0084  0.0054  142  VAL   A O   
3202 C  CB  A VAL   A 142 ? 0.1195 0.1299 0.1305 -0.0064 0.0181  0.0007  142  VAL   A CB  
3203 C  CB  B VAL   A 142 ? 0.1417 0.1244 0.1388 0.0067  0.0160  -0.0029 142  VAL   A CB  
3204 C  CG1 A VAL   A 142 ? 0.1170 0.1161 0.1273 -0.0148 0.0313  0.0037  142  VAL   A CG1 
3205 C  CG1 B VAL   A 142 ? 0.1509 0.1282 0.1415 0.0118  0.0169  -0.0101 142  VAL   A CG1 
3206 C  CG2 A VAL   A 142 ? 0.1259 0.1392 0.1522 -0.0049 0.0185  -0.0065 142  VAL   A CG2 
3207 C  CG2 B VAL   A 142 ? 0.1509 0.1313 0.1456 0.0123  0.0058  -0.0054 142  VAL   A CG2 
3226 N  N   A CYS   A 143 ? 0.1082 0.1319 0.1321 -0.0057 0.0134  0.0031  143  CYS   A N   
3227 N  N   B CYS   A 143 ? 0.1200 0.1211 0.1253 -0.0023 0.0115  0.0045  143  CYS   A N   
3228 C  CA  A CYS   A 143 ? 0.1132 0.1346 0.1393 -0.0051 0.0107  0.0063  143  CYS   A CA  
3229 C  CA  B CYS   A 143 ? 0.1188 0.1283 0.1283 -0.0027 0.0162  0.0083  143  CYS   A CA  
3230 C  C   A CYS   A 143 ? 0.1122 0.1314 0.1435 -0.0076 0.0111  0.0167  143  CYS   A C   
3231 C  C   B CYS   A 143 ? 0.1141 0.1328 0.1423 -0.0025 0.0170  0.0194  143  CYS   A C   
3232 O  O   A CYS   A 143 ? 0.1107 0.1167 0.1252 -0.0026 0.0120  0.0046  143  CYS   A O   
3233 O  O   B CYS   A 143 ? 0.1101 0.1286 0.1415 0.0077  0.0246  0.0197  143  CYS   A O   
3234 C  CB  A CYS   A 143 ? 0.1219 0.1350 0.1376 -0.0055 0.0032  0.0096  143  CYS   A CB  
3235 C  CB  B CYS   A 143 ? 0.1268 0.1323 0.1149 -0.0011 0.0227  0.0135  143  CYS   A CB  
3236 S  SG  A CYS   A 143 ? 0.1340 0.1375 0.1320 0.0007  0.0015  -0.0027 143  CYS   A SG  
3237 S  SG  B CYS   A 143 ? 0.1390 0.1359 0.1140 -0.0043 -0.0003 0.0106  143  CYS   A SG  
3248 N  N   . VAL   A 144 ? 0.1135 0.1432 0.1653 -0.0073 0.0116  0.0359  144  VAL   A N   
3249 C  CA  . VAL   A 144 ? 0.1178 0.1510 0.1994 -0.0158 0.0218  0.0357  144  VAL   A CA  
3250 C  C   . VAL   A 144 ? 0.1228 0.1396 0.1922 -0.0248 0.0025  0.0263  144  VAL   A C   
3251 O  O   . VAL   A 144 ? 0.1370 0.1429 0.1985 -0.0060 0.0023  0.0329  144  VAL   A O   
3252 C  CB  . VAL   A 144 ? 0.1373 0.1740 0.2603 -0.0051 0.0352  0.0338  144  VAL   A CB  
3253 C  CG1 . VAL   A 144 ? 0.1492 0.1905 0.2976 -0.0118 0.0248  0.0284  144  VAL   A CG1 
3254 C  CG2 . VAL   A 144 ? 0.1211 0.1782 0.2682 -0.0068 0.0415  0.0550  144  VAL   A CG2 
3265 N  N   . ASP   A 145 ? 0.1284 0.1380 0.1982 -0.0219 0.0130  0.0211  145  ASP   A N   
3266 C  CA  . ASP   A 145 ? 0.1399 0.1477 0.1949 -0.0260 0.0048  0.0063  145  ASP   A CA  
3267 C  C   . ASP   A 145 ? 0.1373 0.1341 0.2055 -0.0161 0.0069  -0.0020 145  ASP   A C   
3268 O  O   . ASP   A 145 ? 0.1521 0.1431 0.2700 -0.0196 0.0044  -0.0326 145  ASP   A O   
3269 C  CB  . ASP   A 145 ? 0.1478 0.1836 0.2104 -0.0319 -0.0093 0.0007  145  ASP   A CB  
3270 C  CG  . ASP   A 145 ? 0.1629 0.2208 0.2382 -0.0519 -0.0178 0.0037  145  ASP   A CG  
3271 O  OD1 . ASP   A 145 ? 0.1636 0.2346 0.2566 -0.0627 -0.0134 0.0129  145  ASP   A OD1 
3272 O  OD2 . ASP   A 145 ? 0.1838 0.2467 0.2519 -0.0574 -0.0338 0.0009  145  ASP   A OD2 
3277 N  N   . THR   A 146 ? 0.1237 0.1311 0.1685 -0.0159 0.0095  0.0137  146  THR   A N   
3278 C  CA  . THR   A 146 ? 0.1166 0.1256 0.1594 -0.0065 0.0063  0.0134  146  THR   A CA  
3279 C  C   . THR   A 146 ? 0.1137 0.1195 0.1576 -0.0014 0.0076  0.0196  146  THR   A C   
3280 O  O   . THR   A 146 ? 0.1293 0.1342 0.1690 0.0047  0.0012  0.0146  146  THR   A O   
3281 C  CB  . THR   A 146 ? 0.1206 0.1308 0.1542 -0.0049 0.0070  0.0191  146  THR   A CB  
3282 O  OG1 . THR   A 146 ? 0.1167 0.1467 0.1630 -0.0011 0.0036  0.0138  146  THR   A OG1 
3283 C  CG2 . THR   A 146 ? 0.1187 0.1281 0.1794 -0.0048 0.0134  0.0201  146  THR   A CG2 
3291 N  N   . VAL   A 147 ? 0.1139 0.1220 0.1573 -0.0033 0.0124  0.0158  147  VAL   A N   
3292 C  CA  . VAL   A 147 ? 0.1128 0.1300 0.1518 -0.0073 0.0216  0.0164  147  VAL   A CA  
3293 C  C   . VAL   A 147 ? 0.1195 0.1244 0.1716 -0.0112 0.0167  0.0242  147  VAL   A C   
3294 O  O   . VAL   A 147 ? 0.1206 0.1271 0.1907 -0.0150 0.0126  0.0301  147  VAL   A O   
3295 C  CB  . VAL   A 147 ? 0.1313 0.1280 0.1521 -0.0080 0.0205  0.0215  147  VAL   A CB  
3296 C  CG1 . VAL   A 147 ? 0.1637 0.1329 0.1568 -0.0072 0.0147  0.0303  147  VAL   A CG1 
3297 C  CG2 . VAL   A 147 ? 0.1361 0.1291 0.1505 -0.0113 0.0131  0.0209  147  VAL   A CG2 
3307 N  N   . ARG   A 148 ? 0.1189 0.1281 0.1755 -0.0123 0.0144  0.0380  148  ARG   A N   
3308 C  CA  . ARG   A 148 ? 0.1220 0.1262 0.1783 -0.0090 0.0083  0.0478  148  ARG   A CA  
3309 C  C   . ARG   A 148 ? 0.1331 0.1320 0.1795 -0.0128 0.0125  0.0564  148  ARG   A C   
3310 O  O   . ARG   A 148 ? 0.1607 0.1444 0.1934 -0.0171 0.0192  0.0509  148  ARG   A O   
3311 C  CB  . ARG   A 148 ? 0.1308 0.1292 0.1989 -0.0066 0.0163  0.0421  148  ARG   A CB  
3312 C  CG  . ARG   A 148 ? 0.1457 0.1275 0.2286 -0.0075 0.0333  0.0265  148  ARG   A CG  
3313 C  CD  . ARG   A 148 ? 0.1589 0.1287 0.2547 -0.0058 0.0425  0.0431  148  ARG   A CD  
3314 N  NE  . ARG   A 148 ? 0.1521 0.1340 0.2551 0.0040  0.0410  0.0522  148  ARG   A NE  
3315 C  CZ  . ARG   A 148 ? 0.1519 0.1261 0.2365 0.0050  0.0432  0.0398  148  ARG   A CZ  
3316 N  NH1 . ARG   A 148 ? 0.1575 0.1236 0.2426 -0.0038 0.0404  0.0196  148  ARG   A NH1 
3317 N  NH2 . ARG   A 148 ? 0.1496 0.1447 0.2315 0.0182  0.0464  0.0540  148  ARG   A NH2 
3331 N  N   . THR   A 149 ? 0.1357 0.1390 0.1648 -0.0156 0.0038  0.0494  149  THR   A N   
3332 C  CA  . THR   A 149 ? 0.1364 0.1444 0.1648 -0.0134 0.0085  0.0489  149  THR   A CA  
3333 C  C   . THR   A 149 ? 0.1347 0.1415 0.1572 -0.0192 0.0052  0.0500  149  THR   A C   
3334 O  O   . THR   A 149 ? 0.1310 0.1511 0.1796 -0.0222 0.0088  0.0408  149  THR   A O   
3335 C  CB  . THR   A 149 ? 0.1356 0.1563 0.1661 -0.0115 0.0087  0.0407  149  THR   A CB  
3336 O  OG1 . THR   A 149 ? 0.1405 0.1432 0.1735 -0.0261 -0.0018 0.0331  149  THR   A OG1 
3337 C  CG2 . THR   A 149 ? 0.1349 0.1696 0.1767 -0.0034 0.0035  0.0386  149  THR   A CG2 
3345 N  N   . ASN   A 150 ? 0.1348 0.1463 0.1592 -0.0098 -0.0032 0.0518  150  ASN   A N   
3346 C  CA  . ASN   A 150 ? 0.1430 0.1517 0.1575 -0.0118 0.0071  0.0479  150  ASN   A CA  
3347 C  C   . ASN   A 150 ? 0.1261 0.1392 0.1615 -0.0170 0.0075  0.0435  150  ASN   A C   
3348 O  O   . ASN   A 150 ? 0.1378 0.1509 0.1957 -0.0108 -0.0098 0.0395  150  ASN   A O   
3349 C  CB  . ASN   A 150 ? 0.1863 0.1850 0.1852 -0.0184 0.0217  0.0681  150  ASN   A CB  
3350 C  CG  . ASN   A 150 ? 0.2350 0.2164 0.2554 -0.0138 0.0089  0.0786  150  ASN   A CG  
3351 O  OD1 . ASN   A 150 ? 0.2546 0.2266 0.2744 -0.0207 0.0082  0.0932  150  ASN   A OD1 
3352 N  ND2 . ASN   A 150 ? 0.2626 0.2362 0.2896 -0.0040 -0.0066 0.0824  150  ASN   A ND2 
3359 N  N   . VAL   A 151 ? 0.1279 0.1334 0.1613 -0.0160 0.0035  0.0426  151  VAL   A N   
3360 C  CA  . VAL   A 151 ? 0.1376 0.1357 0.1540 -0.0195 0.0078  0.0347  151  VAL   A CA  
3361 C  C   . VAL   A 151 ? 0.1255 0.1300 0.1510 -0.0236 0.0035  0.0395  151  VAL   A C   
3362 O  O   . VAL   A 151 ? 0.1340 0.1375 0.1891 -0.0175 0.0054  0.0352  151  VAL   A O   
3363 C  CB  . VAL   A 151 ? 0.1650 0.1562 0.1554 -0.0121 0.0094  0.0306  151  VAL   A CB  
3364 C  CG1 . VAL   A 151 ? 0.1570 0.1755 0.1738 -0.0146 0.0071  0.0255  151  VAL   A CG1 
3365 C  CG2 . VAL   A 151 ? 0.1790 0.1552 0.1529 -0.0077 0.0225  0.0290  151  VAL   A CG2 
3375 N  N   . TYR   A 152 ? 0.1263 0.1344 0.1527 -0.0207 0.0028  0.0330  152  TYR   A N   
3376 C  CA  . TYR   A 152 ? 0.1243 0.1381 0.1385 -0.0158 0.0062  0.0286  152  TYR   A CA  
3377 C  C   . TYR   A 152 ? 0.1237 0.1326 0.1387 -0.0174 0.0146  0.0293  152  TYR   A C   
3378 O  O   . TYR   A 152 ? 0.1339 0.1358 0.1463 -0.0249 0.0176  0.0269  152  TYR   A O   
3379 C  CB  . TYR   A 152 ? 0.1386 0.1463 0.1409 -0.0120 0.0233  0.0354  152  TYR   A CB  
3380 C  CG  . TYR   A 152 ? 0.1584 0.1635 0.1460 -0.0205 0.0292  0.0381  152  TYR   A CG  
3381 C  CD1 . TYR   A 152 ? 0.1728 0.1852 0.1614 -0.0075 0.0288  0.0487  152  TYR   A CD1 
3382 C  CD2 . TYR   A 152 ? 0.1610 0.1782 0.1400 -0.0323 0.0284  0.0364  152  TYR   A CD2 
3383 C  CE1 . TYR   A 152 ? 0.1956 0.2030 0.1743 -0.0031 0.0134  0.0594  152  TYR   A CE1 
3384 C  CE2 . TYR   A 152 ? 0.1838 0.1998 0.1541 -0.0324 0.0240  0.0434  152  TYR   A CE2 
3385 C  CZ  . TYR   A 152 ? 0.2098 0.2059 0.1680 -0.0180 0.0166  0.0649  152  TYR   A CZ  
3386 O  OH  . TYR   A 152 ? 0.2401 0.2269 0.1981 -0.0079 0.0159  0.0851  152  TYR   A OH  
3396 N  N   A LEU   A 153 ? 0.1179 0.1266 0.1441 -0.0180 0.0199  0.0297  153  LEU   A N   
3397 N  N   B LEU   A 153 ? 0.1253 0.1329 0.1417 -0.0167 0.0111  0.0315  153  LEU   A N   
3398 C  CA  A LEU   A 153 ? 0.1129 0.1185 0.1512 -0.0097 0.0193  0.0321  153  LEU   A CA  
3399 C  CA  B LEU   A 153 ? 0.1236 0.1315 0.1422 -0.0013 0.0076  0.0334  153  LEU   A CA  
3400 C  C   A LEU   A 153 ? 0.1163 0.1199 0.1559 -0.0164 0.0284  0.0193  153  LEU   A C   
3401 C  C   B LEU   A 153 ? 0.1255 0.1416 0.1406 -0.0035 0.0115  0.0256  153  LEU   A C   
3402 O  O   A LEU   A 153 ? 0.1215 0.1278 0.1843 -0.0210 0.0375  0.0064  153  LEU   A O   
3403 O  O   B LEU   A 153 ? 0.1306 0.1501 0.1602 -0.0031 0.0239  0.0257  153  LEU   A O   
3404 C  CB  A LEU   A 153 ? 0.1137 0.1139 0.1575 -0.0106 0.0166  0.0301  153  LEU   A CB  
3405 C  CB  B LEU   A 153 ? 0.1225 0.1267 0.1495 0.0084  0.0063  0.0349  153  LEU   A CB  
3406 C  CG  A LEU   A 153 ? 0.1196 0.1200 0.1636 -0.0146 0.0182  0.0151  153  LEU   A CG  
3407 C  CG  B LEU   A 153 ? 0.1281 0.1281 0.1375 0.0097  0.0054  0.0256  153  LEU   A CG  
3408 C  CD1 A LEU   A 153 ? 0.1283 0.1161 0.1663 -0.0108 0.0139  0.0149  153  LEU   A CD1 
3409 C  CD1 B LEU   A 153 ? 0.1352 0.1294 0.1392 0.0083  -0.0039 0.0221  153  LEU   A CD1 
3410 C  CD2 A LEU   A 153 ? 0.1287 0.1283 0.1638 -0.0232 0.0305  -0.0018 153  LEU   A CD2 
3411 C  CD2 B LEU   A 153 ? 0.1348 0.1343 0.1439 0.0068  0.0160  0.0190  153  LEU   A CD2 
3434 N  N   A ALA   A 154 ? 0.1156 0.1144 0.1516 -0.0107 0.0256  0.0234  154  ALA   A N   
3435 N  N   B ALA   A 154 ? 0.1209 0.1398 0.1257 0.0018  0.0101  0.0206  154  ALA   A N   
3436 C  CA  A ALA   A 154 ? 0.1232 0.1179 0.1568 -0.0100 0.0175  0.0183  154  ALA   A CA  
3437 C  CA  B ALA   A 154 ? 0.1300 0.1452 0.1464 0.0062  0.0073  0.0119  154  ALA   A CA  
3438 C  C   A ALA   A 154 ? 0.1226 0.1078 0.1609 -0.0061 0.0213  0.0242  154  ALA   A C   
3439 C  C   B ALA   A 154 ? 0.1312 0.1458 0.1539 0.0045  -0.0026 0.0176  154  ALA   A C   
3440 O  O   A ALA   A 154 ? 0.1285 0.1136 0.1681 -0.0089 0.0277  0.0200  154  ALA   A O   
3441 O  O   B ALA   A 154 ? 0.1378 0.1480 0.1521 -0.0016 -0.0028 0.0207  154  ALA   A O   
3442 C  CB  A ALA   A 154 ? 0.1312 0.1247 0.1601 -0.0009 0.0073  -0.0001 154  ALA   A CB  
3443 C  CB  B ALA   A 154 ? 0.1390 0.1478 0.1548 0.0134  -0.0029 0.0020  154  ALA   A CB  
3454 N  N   A VAL   A 155 ? 0.1282 0.1181 0.1567 0.0014  0.0222  0.0290  155  VAL   A N   
3455 N  N   B VAL   A 155 ? 0.1349 0.1539 0.1665 0.0060  -0.0121 0.0252  155  VAL   A N   
3456 C  CA  A VAL   A 155 ? 0.1360 0.1305 0.1853 -0.0012 0.0120  0.0479  155  VAL   A CA  
3457 C  CA  B VAL   A 155 ? 0.1400 0.1585 0.1763 0.0001  -0.0115 0.0356  155  VAL   A CA  
3458 C  C   A VAL   A 155 ? 0.1423 0.1396 0.2195 0.0098  0.0088  0.0657  155  VAL   A C   
3459 C  C   B VAL   A 155 ? 0.1550 0.1698 0.2021 0.0121  -0.0085 0.0380  155  VAL   A C   
3460 O  O   A VAL   A 155 ? 0.1417 0.1440 0.2293 0.0149  0.0229  0.0679  155  VAL   A O   
3461 O  O   B VAL   A 155 ? 0.1559 0.1689 0.2175 0.0200  -0.0015 0.0403  155  VAL   A O   
3462 C  CB  A VAL   A 155 ? 0.1497 0.1400 0.1872 -0.0005 -0.0044 0.0377  155  VAL   A CB  
3463 C  CB  B VAL   A 155 ? 0.1377 0.1552 0.1844 -0.0092 -0.0149 0.0327  155  VAL   A CB  
3464 C  CG1 A VAL   A 155 ? 0.1624 0.1486 0.1922 0.0023  -0.0135 0.0390  155  VAL   A CG1 
3465 C  CG1 B VAL   A 155 ? 0.1453 0.1622 0.1989 -0.0114 -0.0285 0.0226  155  VAL   A CG1 
3466 C  CG2 A VAL   A 155 ? 0.1556 0.1456 0.1954 0.0055  -0.0107 0.0349  155  VAL   A CG2 
3467 C  CG2 B VAL   A 155 ? 0.1301 0.1478 0.1785 -0.0130 -0.0150 0.0301  155  VAL   A CG2 
3486 N  N   A PHE   A 156 ? 0.1508 0.1458 0.2443 0.0175  0.0058  0.0869  156  PHE   A N   
3487 N  N   B PHE   A 156 ? 0.1727 0.1804 0.2113 0.0229  -0.0048 0.0358  156  PHE   A N   
3488 C  CA  A PHE   A 156 ? 0.1631 0.1549 0.2723 0.0209  0.0095  0.0938  156  PHE   A CA  
3489 C  CA  B PHE   A 156 ? 0.1828 0.1915 0.2291 0.0341  -0.0024 0.0518  156  PHE   A CA  
3490 C  C   A PHE   A 156 ? 0.1681 0.1636 0.2814 0.0240  0.0171  0.0986  156  PHE   A C   
3491 C  C   B PHE   A 156 ? 0.1783 0.2003 0.2492 0.0324  0.0025  0.0733  156  PHE   A C   
3492 O  O   A PHE   A 156 ? 0.1704 0.1745 0.2930 0.0155  0.0367  0.0778  156  PHE   A O   
3493 O  O   B PHE   A 156 ? 0.1822 0.2080 0.2623 0.0348  0.0043  0.0763  156  PHE   A O   
3494 C  CB  A PHE   A 156 ? 0.1834 0.1610 0.2897 0.0157  -0.0026 0.0987  156  PHE   A CB  
3495 C  CB  B PHE   A 156 ? 0.1973 0.1996 0.2460 0.0414  -0.0002 0.0427  156  PHE   A CB  
3496 C  CG  A PHE   A 156 ? 0.2071 0.1690 0.3140 0.0190  -0.0152 0.0862  156  PHE   A CG  
3497 C  CG  B PHE   A 156 ? 0.2145 0.2055 0.2604 0.0474  0.0014  0.0328  156  PHE   A CG  
3498 C  CD1 A PHE   A 156 ? 0.2195 0.1784 0.3235 0.0184  -0.0198 0.0769  156  PHE   A CD1 
3499 C  CD1 B PHE   A 156 ? 0.2236 0.2125 0.2706 0.0468  0.0035  0.0259  156  PHE   A CD1 
3500 C  CD2 A PHE   A 156 ? 0.2203 0.1786 0.3252 0.0248  -0.0180 0.0833  156  PHE   A CD2 
3501 C  CD2 B PHE   A 156 ? 0.2223 0.2083 0.2626 0.0506  0.0041  0.0327  156  PHE   A CD2 
3502 C  CE1 A PHE   A 156 ? 0.2338 0.1883 0.3360 0.0232  -0.0207 0.0641  156  PHE   A CE1 
3503 C  CE1 B PHE   A 156 ? 0.2317 0.2138 0.2764 0.0495  0.0042  0.0236  156  PHE   A CE1 
3504 C  CE2 A PHE   A 156 ? 0.2332 0.1891 0.3328 0.0302  -0.0221 0.0672  156  PHE   A CE2 
3505 C  CE2 B PHE   A 156 ? 0.2311 0.2107 0.2688 0.0518  0.0026  0.0290  156  PHE   A CE2 
3506 C  CZ  A PHE   A 156 ? 0.2375 0.1915 0.3390 0.0297  -0.0220 0.0545  156  PHE   A CZ  
3507 C  CZ  B PHE   A 156 ? 0.2329 0.2140 0.2738 0.0510  0.0062  0.0247  156  PHE   A CZ  
3526 N  N   A ASP   A 157 ? 0.1851 0.1763 0.2857 0.0226  0.0079  0.1131  157  ASP   A N   
3527 N  N   B ASP   A 157 ? 0.1755 0.2088 0.2501 0.0227  -0.0068 0.0912  157  ASP   A N   
3528 C  CA  A ASP   A 157 ? 0.1983 0.1951 0.2896 0.0235  -0.0090 0.1155  157  ASP   A CA  
3529 C  CA  B ASP   A 157 ? 0.1704 0.2226 0.2688 0.0102  -0.0157 0.1043  157  ASP   A CA  
3530 C  C   A ASP   A 157 ? 0.1924 0.2053 0.2946 0.0299  -0.0048 0.1200  157  ASP   A C   
3531 C  C   B ASP   A 157 ? 0.1627 0.2232 0.2848 0.0059  -0.0119 0.1032  157  ASP   A C   
3532 O  O   A ASP   A 157 ? 0.1858 0.1959 0.2854 0.0285  -0.0009 0.1317  157  ASP   A O   
3533 O  O   B ASP   A 157 ? 0.1572 0.2209 0.2814 0.0039  -0.0093 0.1039  157  ASP   A O   
3534 C  CB  A ASP   A 157 ? 0.2154 0.2077 0.3008 0.0238  -0.0262 0.1107  157  ASP   A CB  
3535 C  CB  B ASP   A 157 ? 0.1729 0.2355 0.2807 0.0035  -0.0191 0.1178  157  ASP   A CB  
3536 C  CG  A ASP   A 157 ? 0.2360 0.2213 0.3251 0.0225  -0.0371 0.0990  157  ASP   A CG  
3537 C  CG  B ASP   A 157 ? 0.1778 0.2432 0.2985 0.0003  -0.0221 0.1330  157  ASP   A CG  
3538 O  OD1 A ASP   A 157 ? 0.2498 0.2279 0.3475 0.0240  -0.0437 0.0814  157  ASP   A OD1 
3539 O  OD1 B ASP   A 157 ? 0.1829 0.2401 0.3141 -0.0035 -0.0224 0.1496  157  ASP   A OD1 
3540 O  OD2 A ASP   A 157 ? 0.2404 0.2287 0.3298 0.0186  -0.0407 0.1008  157  ASP   A OD2 
3541 O  OD2 B ASP   A 157 ? 0.1765 0.2500 0.2984 -0.0071 -0.0189 0.1262  157  ASP   A OD2 
3550 N  N   A LYS   A 158 ? 0.1894 0.2242 0.3102 0.0351  -0.0064 0.1084  158  LYS   A N   
3551 N  N   B LYS   A 158 ? 0.1624 0.2255 0.3056 -0.0017 -0.0163 0.0963  158  LYS   A N   
3552 C  CA  A LYS   A 158 ? 0.1812 0.2468 0.3162 0.0420  -0.0003 0.1021  158  LYS   A CA  
3553 C  CA  B LYS   A 158 ? 0.1725 0.2359 0.3200 -0.0095 -0.0100 0.0924  158  LYS   A CA  
3554 C  C   A LYS   A 158 ? 0.1762 0.2609 0.3068 0.0456  -0.0025 0.1029  158  LYS   A C   
3555 C  C   B LYS   A 158 ? 0.1610 0.2364 0.3067 -0.0160 -0.0142 0.1042  158  LYS   A C   
3556 O  O   A LYS   A 158 ? 0.1841 0.2643 0.3083 0.0407  0.0055  0.0974  158  LYS   A O   
3557 O  O   B LYS   A 158 ? 0.1598 0.2293 0.3016 -0.0221 -0.0130 0.1116  158  LYS   A O   
3558 C  CB  A LYS   A 158 ? 0.1808 0.2568 0.3222 0.0423  0.0091  0.1062  158  LYS   A CB  
3559 C  CB  B LYS   A 158 ? 0.1967 0.2540 0.3488 -0.0065 -0.0004 0.0789  158  LYS   A CB  
3560 C  CG  A LYS   A 158 ? 0.1835 0.2698 0.3305 0.0381  0.0172  0.1131  158  LYS   A CG  
3561 C  CG  B LYS   A 158 ? 0.2184 0.2714 0.3783 -0.0055 0.0068  0.0746  158  LYS   A CG  
3562 C  CD  A LYS   A 158 ? 0.1887 0.2815 0.3396 0.0331  0.0307  0.1219  158  LYS   A CD  
3563 C  CD  B LYS   A 158 ? 0.2343 0.2833 0.4017 -0.0053 0.0132  0.0732  158  LYS   A CD  
3564 C  CE  A LYS   A 158 ? 0.1945 0.2897 0.3474 0.0254  0.0453  0.1310  158  LYS   A CE  
3565 C  CE  B LYS   A 158 ? 0.2449 0.2901 0.4180 -0.0059 0.0178  0.0728  158  LYS   A CE  
3566 N  NZ  A LYS   A 158 ? 0.1993 0.2927 0.3485 0.0239  0.0522  0.1361  158  LYS   A NZ  
3567 N  NZ  B LYS   A 158 ? 0.2522 0.2956 0.4330 -0.0069 0.0215  0.0672  158  LYS   A NZ  
3594 N  N   A ASN   A 159 ? 0.1676 0.2713 0.3076 0.0501  -0.0160 0.1054  159  ASN   A N   
3595 N  N   B ASN   A 159 ? 0.1648 0.2540 0.3199 -0.0060 -0.0200 0.1010  159  ASN   A N   
3596 C  CA  A ASN   A 159 ? 0.1695 0.2803 0.3084 0.0488  -0.0217 0.1124  159  ASN   A CA  
3597 C  CA  B ASN   A 159 ? 0.1718 0.2710 0.3279 0.0001  -0.0228 0.1020  159  ASN   A CA  
3598 C  C   A ASN   A 159 ? 0.1602 0.2816 0.2838 0.0378  -0.0094 0.1080  159  ASN   A C   
3599 C  C   B ASN   A 159 ? 0.1535 0.2679 0.2931 -0.0056 -0.0233 0.1020  159  ASN   A C   
3600 O  O   A ASN   A 159 ? 0.1574 0.2872 0.2784 0.0395  -0.0108 0.0944  159  ASN   A O   
3601 O  O   B ASN   A 159 ? 0.1456 0.2796 0.2948 -0.0118 -0.0287 0.0929  159  ASN   A O   
3602 C  CB  A ASN   A 159 ? 0.1815 0.2881 0.3387 0.0526  -0.0307 0.1205  159  ASN   A CB  
3603 C  CB  B ASN   A 159 ? 0.1996 0.2893 0.3776 0.0069  -0.0184 0.1008  159  ASN   A CB  
3604 C  CG  A ASN   A 159 ? 0.2002 0.2974 0.3765 0.0497  -0.0223 0.1195  159  ASN   A CG  
3605 C  CG  B ASN   A 159 ? 0.2275 0.3043 0.4270 0.0041  -0.0099 0.0936  159  ASN   A CG  
3606 O  OD1 A ASN   A 159 ? 0.2077 0.3052 0.3865 0.0436  -0.0184 0.1189  159  ASN   A OD1 
3607 O  OD1 B ASN   A 159 ? 0.2379 0.3102 0.4408 0.0012  -0.0074 0.0869  159  ASN   A OD1 
3608 N  ND2 A ASN   A 159 ? 0.2077 0.3007 0.3997 0.0491  -0.0128 0.1127  159  ASN   A ND2 
3609 N  ND2 B ASN   A 159 ? 0.2402 0.3103 0.4524 0.0008  -0.0054 0.0889  159  ASN   A ND2 
3622 N  N   A LEU   A 160 ? 0.1543 0.2732 0.2723 0.0284  -0.0079 0.1094  160  LEU   A N   
3623 N  N   B LEU   A 160 ? 0.1481 0.2553 0.2690 -0.0055 -0.0267 0.1095  160  LEU   A N   
3624 C  CA  A LEU   A 160 ? 0.1553 0.2658 0.2598 0.0131  0.0037  0.1059  160  LEU   A CA  
3625 C  CA  B LEU   A 160 ? 0.1529 0.2511 0.2548 -0.0039 -0.0121 0.1107  160  LEU   A CA  
3626 C  C   A LEU   A 160 ? 0.1401 0.2561 0.2545 0.0100  0.0112  0.1023  160  LEU   A C   
3627 C  C   B LEU   A 160 ? 0.1417 0.2419 0.2451 -0.0023 0.0032  0.1068  160  LEU   A C   
3628 O  O   A LEU   A 160 ? 0.1382 0.2626 0.2714 0.0087  0.0079  0.0998  160  LEU   A O   
3629 O  O   B LEU   A 160 ? 0.1377 0.2481 0.2572 -0.0008 -0.0045 0.0976  160  LEU   A O   
3630 C  CB  A LEU   A 160 ? 0.1659 0.2690 0.2462 0.0006  0.0070  0.1042  160  LEU   A CB  
3631 C  CB  B LEU   A 160 ? 0.1678 0.2575 0.2460 -0.0056 -0.0110 0.1113  160  LEU   A CB  
3632 C  CG  A LEU   A 160 ? 0.1717 0.2716 0.2417 -0.0168 0.0132  0.0916  160  LEU   A CG  
3633 C  CG  B LEU   A 160 ? 0.1777 0.2665 0.2517 -0.0152 -0.0041 0.0959  160  LEU   A CG  
3634 C  CD1 A LEU   A 160 ? 0.1807 0.2763 0.2501 -0.0224 0.0161  0.0806  160  LEU   A CD1 
3635 C  CD1 B LEU   A 160 ? 0.1875 0.2720 0.2604 -0.0189 -0.0013 0.0858  160  LEU   A CD1 
3636 C  CD2 A LEU   A 160 ? 0.1713 0.2700 0.2312 -0.0211 0.0184  0.0868  160  LEU   A CD2 
3637 C  CD2 B LEU   A 160 ? 0.1805 0.2699 0.2516 -0.0162 0.0042  0.0867  160  LEU   A CD2 
3660 N  N   A TYR   A 161 ? 0.1334 0.2402 0.2490 0.0108  0.0104  0.0996  161  TYR   A N   
3661 N  N   B TYR   A 161 ? 0.1391 0.2286 0.2438 0.0003  0.0155  0.1047  161  TYR   A N   
3662 C  CA  A TYR   A 161 ? 0.1303 0.2257 0.2419 0.0088  0.0068  0.0990  161  TYR   A CA  
3663 C  CA  B TYR   A 161 ? 0.1421 0.2176 0.2420 0.0026  0.0236  0.1029  161  TYR   A CA  
3664 C  C   A TYR   A 161 ? 0.1216 0.2374 0.2298 0.0056  0.0086  0.0952  161  TYR   A C   
3665 C  C   B TYR   A 161 ? 0.1375 0.2330 0.2472 -0.0000 0.0237  0.1003  161  TYR   A C   
3666 O  O   A TYR   A 161 ? 0.1189 0.2375 0.2066 0.0003  0.0094  0.1004  161  TYR   A O   
3667 O  O   B TYR   A 161 ? 0.1347 0.2338 0.2308 -0.0037 0.0282  0.0944  161  TYR   A O   
3668 C  CB  A TYR   A 161 ? 0.1381 0.2052 0.2527 0.0073  0.0026  0.0854  161  TYR   A CB  
3669 C  CB  B TYR   A 161 ? 0.1514 0.1967 0.2441 0.0065  0.0289  0.0885  161  TYR   A CB  
3670 C  CG  A TYR   A 161 ? 0.1403 0.1891 0.2488 0.0022  -0.0051 0.0701  161  TYR   A CG  
3671 C  CG  B TYR   A 161 ? 0.1515 0.1808 0.2412 0.0110  0.0327  0.0703  161  TYR   A CG  
3672 C  CD1 A TYR   A 161 ? 0.1431 0.1822 0.2507 -0.0005 -0.0061 0.0617  161  TYR   A CD1 
3673 C  CD1 B TYR   A 161 ? 0.1530 0.1729 0.2418 0.0109  0.0351  0.0622  161  TYR   A CD1 
3674 C  CD2 A TYR   A 161 ? 0.1424 0.1895 0.2430 -0.0022 -0.0130 0.0614  161  TYR   A CD2 
3675 C  CD2 B TYR   A 161 ? 0.1561 0.1813 0.2449 0.0134  0.0322  0.0609  161  TYR   A CD2 
3676 C  CE1 A TYR   A 161 ? 0.1561 0.1762 0.2509 -0.0025 -0.0090 0.0564  161  TYR   A CE1 
3677 C  CE1 B TYR   A 161 ? 0.1651 0.1738 0.2502 0.0122  0.0289  0.0576  161  TYR   A CE1 
3678 C  CE2 A TYR   A 161 ? 0.1531 0.1835 0.2402 -0.0034 -0.0104 0.0618  161  TYR   A CE2 
3679 C  CE2 B TYR   A 161 ? 0.1657 0.1758 0.2512 0.0121  0.0328  0.0657  161  TYR   A CE2 
3680 C  CZ  A TYR   A 161 ? 0.1632 0.1742 0.2468 -0.0046 -0.0111 0.0611  161  TYR   A CZ  
3681 C  CZ  B TYR   A 161 ? 0.1793 0.1718 0.2569 0.0091  0.0297  0.0696  161  TYR   A CZ  
3682 O  OH  A TYR   A 161 ? 0.1726 0.1620 0.2583 -0.0036 -0.0176 0.0604  161  TYR   A OH  
3683 O  OH  B TYR   A 161 ? 0.2027 0.1748 0.2789 0.0025  0.0235  0.0732  161  TYR   A OH  
3702 N  N   A ASP   A 162 ? 0.1210 0.2503 0.2402 0.0076  0.0111  0.0895  162  ASP   A N   
3703 N  N   B ASP   A 162 ? 0.1367 0.2480 0.2674 0.0025  0.0234  0.1069  162  ASP   A N   
3704 C  CA  A ASP   A 162 ? 0.1216 0.2674 0.2472 -0.0002 0.0214  0.0857  162  ASP   A CA  
3705 C  CA  B ASP   A 162 ? 0.1387 0.2700 0.2860 -0.0014 0.0225  0.1021  162  ASP   A CA  
3706 C  C   A ASP   A 162 ? 0.1209 0.2835 0.2577 -0.0078 0.0239  0.0843  162  ASP   A C   
3707 C  C   B ASP   A 162 ? 0.1361 0.2877 0.2906 -0.0077 0.0217  0.0995  162  ASP   A C   
3708 O  O   A ASP   A 162 ? 0.1201 0.2832 0.2706 -0.0116 0.0314  0.0744  162  ASP   A O   
3709 O  O   B ASP   A 162 ? 0.1340 0.2878 0.3031 -0.0113 0.0278  0.0921  162  ASP   A O   
3710 C  CB  A ASP   A 162 ? 0.1342 0.2736 0.2462 0.0013  0.0346  0.0824  162  ASP   A CB  
3711 C  CB  B ASP   A 162 ? 0.1534 0.2786 0.3116 0.0016  0.0228  0.0931  162  ASP   A CB  
3712 C  CG  A ASP   A 162 ? 0.1484 0.2826 0.2564 0.0027  0.0420  0.0792  162  ASP   A CG  
3713 C  CG  B ASP   A 162 ? 0.1703 0.2895 0.3324 0.0064  0.0197  0.0863  162  ASP   A CG  
3714 O  OD1 A ASP   A 162 ? 0.1642 0.2910 0.2706 0.0049  0.0318  0.0728  162  ASP   A OD1 
3715 O  OD1 B ASP   A 162 ? 0.1745 0.2948 0.3411 0.0082  0.0145  0.0848  162  ASP   A OD1 
3716 O  OD2 A ASP   A 162 ? 0.1570 0.2837 0.2667 0.0006  0.0558  0.0771  162  ASP   A OD2 
3717 O  OD2 B ASP   A 162 ? 0.1859 0.2921 0.3361 0.0107  0.0271  0.0861  162  ASP   A OD2 
3726 N  N   A LYS   A 163 ? 0.1316 0.2989 0.2657 -0.0114 0.0019  0.0830  163  LYS   A N   
3727 N  N   B LYS   A 163 ? 0.1464 0.3043 0.2946 -0.0101 0.0061  0.0965  163  LYS   A N   
3728 C  CA  A LYS   A 163 ? 0.1433 0.3118 0.2676 -0.0173 -0.0091 0.0758  163  LYS   A CA  
3729 C  CA  B LYS   A 163 ? 0.1602 0.3184 0.2919 -0.0134 0.0062  0.0908  163  LYS   A CA  
3730 C  C   A LYS   A 163 ? 0.1378 0.3035 0.2577 -0.0200 0.0059  0.0744  163  LYS   A C   
3731 C  C   B LYS   A 163 ? 0.1499 0.3088 0.2654 -0.0150 0.0137  0.0799  163  LYS   A C   
3732 O  O   A LYS   A 163 ? 0.1394 0.3176 0.2742 -0.0208 0.0074  0.0646  163  LYS   A O   
3733 O  O   B LYS   A 163 ? 0.1522 0.3208 0.2786 -0.0187 0.0166  0.0691  163  LYS   A O   
3734 C  CB  A LYS   A 163 ? 0.1717 0.3322 0.2961 -0.0175 -0.0217 0.0672  163  LYS   A CB  
3735 C  CB  B LYS   A 163 ? 0.1947 0.3416 0.3301 -0.0130 0.0006  0.0919  163  LYS   A CB  
3736 C  CG  A LYS   A 163 ? 0.1998 0.3496 0.3326 -0.0211 -0.0160 0.0627  163  LYS   A CG  
3737 C  CG  B LYS   A 163 ? 0.2254 0.3607 0.3728 -0.0152 0.0098  0.0978  163  LYS   A CG  
3738 C  CD  A LYS   A 163 ? 0.2197 0.3621 0.3692 -0.0237 -0.0164 0.0590  163  LYS   A CD  
3739 C  CD  B LYS   A 163 ? 0.2542 0.3757 0.4177 -0.0185 0.0152  0.1034  163  LYS   A CD  
3740 C  CE  A LYS   A 163 ? 0.2378 0.3706 0.3972 -0.0254 -0.0132 0.0565  163  LYS   A CE  
3741 C  CE  B LYS   A 163 ? 0.2738 0.3846 0.4504 -0.0222 0.0180  0.1101  163  LYS   A CE  
3742 N  NZ  A LYS   A 163 ? 0.2445 0.3748 0.4143 -0.0281 -0.0130 0.0571  163  LYS   A NZ  
3743 N  NZ  B LYS   A 163 ? 0.2803 0.3894 0.4709 -0.0252 0.0200  0.1112  163  LYS   A NZ  
3770 N  N   A LEU   A 164 ? 0.1296 0.2799 0.2314 -0.0294 0.0080  0.0742  164  LEU   A N   
3771 N  N   B LEU   A 164 ? 0.1353 0.2871 0.2314 -0.0212 0.0063  0.0743  164  LEU   A N   
3772 C  CA  A LEU   A 164 ? 0.1354 0.2602 0.2192 -0.0304 0.0180  0.0705  164  LEU   A CA  
3773 C  CA  B LEU   A 164 ? 0.1303 0.2681 0.2116 -0.0207 0.0114  0.0653  164  LEU   A CA  
3774 C  C   A LEU   A 164 ? 0.1419 0.2516 0.2218 -0.0236 0.0277  0.0620  164  LEU   A C   
3775 C  C   B LEU   A 164 ? 0.1296 0.2607 0.2156 -0.0213 0.0192  0.0620  164  LEU   A C   
3776 O  O   A LEU   A 164 ? 0.1513 0.2563 0.2282 -0.0250 0.0378  0.0446  164  LEU   A O   
3777 O  O   B LEU   A 164 ? 0.1387 0.2650 0.2170 -0.0285 0.0274  0.0501  164  LEU   A O   
3778 C  CB  A LEU   A 164 ? 0.1357 0.2514 0.2119 -0.0369 0.0200  0.0772  164  LEU   A CB  
3779 C  CB  B LEU   A 164 ? 0.1287 0.2581 0.2036 -0.0180 0.0143  0.0566  164  LEU   A CB  
3780 C  CG  A LEU   A 164 ? 0.1393 0.2491 0.2059 -0.0361 0.0137  0.0733  164  LEU   A CG  
3781 C  CG  B LEU   A 164 ? 0.1370 0.2537 0.2078 -0.0153 0.0036  0.0479  164  LEU   A CG  
3782 C  CD1 A LEU   A 164 ? 0.1350 0.2468 0.1975 -0.0340 0.0152  0.0683  164  LEU   A CD1 
3783 C  CD1 B LEU   A 164 ? 0.1374 0.2514 0.2105 -0.0133 -0.0056 0.0381  164  LEU   A CD1 
3784 C  CD2 A LEU   A 164 ? 0.1468 0.2530 0.2001 -0.0358 0.0131  0.0740  164  LEU   A CD2 
3785 C  CD2 B LEU   A 164 ? 0.1440 0.2535 0.2038 -0.0168 0.0130  0.0459  164  LEU   A CD2 
3808 N  N   A VAL   A 165 ? 0.1448 0.2419 0.2201 -0.0201 0.0310  0.0614  165  VAL   A N   
3809 N  N   B VAL   A 165 ? 0.1250 0.2506 0.2198 -0.0205 0.0199  0.0643  165  VAL   A N   
3810 C  CA  A VAL   A 165 ? 0.1504 0.2350 0.2156 -0.0158 0.0382  0.0620  165  VAL   A CA  
3811 C  CA  B VAL   A 165 ? 0.1280 0.2448 0.2249 -0.0184 0.0236  0.0713  165  VAL   A CA  
3812 C  C   A VAL   A 165 ? 0.1493 0.2448 0.2139 -0.0108 0.0317  0.0615  165  VAL   A C   
3813 C  C   B VAL   A 165 ? 0.1175 0.2510 0.2306 -0.0203 0.0207  0.0706  165  VAL   A C   
3814 O  O   A VAL   A 165 ? 0.1483 0.2463 0.2028 -0.0134 0.0357  0.0587  165  VAL   A O   
3815 O  O   B VAL   A 165 ? 0.1190 0.2550 0.2219 -0.0194 0.0189  0.0615  165  VAL   A O   
3816 C  CB  A VAL   A 165 ? 0.1626 0.2248 0.2255 -0.0148 0.0410  0.0543  165  VAL   A CB  
3817 C  CB  B VAL   A 165 ? 0.1475 0.2381 0.2313 -0.0112 0.0250  0.0678  165  VAL   A CB  
3818 C  CG1 A VAL   A 165 ? 0.1652 0.2229 0.2297 -0.0192 0.0476  0.0515  165  VAL   A CG1 
3819 C  CG1 B VAL   A 165 ? 0.1520 0.2386 0.2388 -0.0131 0.0307  0.0582  165  VAL   A CG1 
3820 C  CG2 A VAL   A 165 ? 0.1715 0.2206 0.2324 -0.0153 0.0413  0.0556  165  VAL   A CG2 
3821 C  CG2 B VAL   A 165 ? 0.1574 0.2349 0.2329 -0.0041 0.0237  0.0717  165  VAL   A CG2 
3840 N  N   A SER   A 166 ? 0.1524 0.2559 0.2348 -0.0062 0.0237  0.0562  166  SER   A N   
3841 N  N   B SER   A 166 ? 0.1052 0.2550 0.2499 -0.0256 0.0234  0.0702  166  SER   A N   
3842 C  CA  A SER   A 166 ? 0.1609 0.2693 0.2422 -0.0062 0.0121  0.0558  166  SER   A CA  
3843 C  CA  B SER   A 166 ? 0.1107 0.2632 0.2605 -0.0249 0.0119  0.0649  166  SER   A CA  
3844 C  C   A SER   A 166 ? 0.1646 0.2758 0.2305 -0.0031 -0.0073 0.0569  166  SER   A C   
3845 C  C   B SER   A 166 ? 0.1210 0.2691 0.2525 -0.0238 0.0019  0.0661  166  SER   A C   
3846 O  O   A SER   A 166 ? 0.1725 0.2840 0.2362 -0.0086 -0.0079 0.0549  166  SER   A O   
3847 O  O   B SER   A 166 ? 0.1292 0.2698 0.2519 -0.0271 -0.0011 0.0712  166  SER   A O   
3848 C  CB  A SER   A 166 ? 0.1726 0.2746 0.2673 -0.0058 0.0138  0.0518  166  SER   A CB  
3849 C  CB  B SER   A 166 ? 0.1224 0.2656 0.2848 -0.0195 -0.0004 0.0571  166  SER   A CB  
3850 O  OG  A SER   A 166 ? 0.1813 0.2772 0.2826 -0.0034 0.0223  0.0562  166  SER   A OG  
3851 O  OG  B SER   A 166 ? 0.1365 0.2655 0.3002 -0.0119 -0.0056 0.0568  166  SER   A OG  
3862 N  N   A SER   A 167 ? 0.1629 0.2684 0.2072 0.0046  -0.0158 0.0593  167  SER   A N   
3863 N  N   B SER   A 167 ? 0.1273 0.2679 0.2416 -0.0193 0.0080  0.0618  167  SER   A N   
3864 C  CA  A SER   A 167 ? 0.1730 0.2600 0.2016 0.0008  -0.0154 0.0484  167  SER   A CA  
3865 C  CA  B SER   A 167 ? 0.1465 0.2670 0.2225 -0.0132 0.0171  0.0550  167  SER   A CA  
3866 C  C   A SER   A 167 ? 0.1766 0.2510 0.2087 -0.0026 -0.0027 0.0469  167  SER   A C   
3867 C  C   B SER   A 167 ? 0.1453 0.2700 0.2053 -0.0050 0.0254  0.0510  167  SER   A C   
3868 O  O   A SER   A 167 ? 0.1867 0.2483 0.2228 -0.0021 -0.0059 0.0498  167  SER   A O   
3869 O  O   B SER   A 167 ? 0.1546 0.2712 0.2184 -0.0096 0.0278  0.0492  167  SER   A O   
3870 C  CB  A SER   A 167 ? 0.1800 0.2611 0.1997 0.0029  -0.0175 0.0472  167  SER   A CB  
3871 C  CB  B SER   A 167 ? 0.1619 0.2655 0.2341 -0.0111 0.0259  0.0428  167  SER   A CB  
3872 O  OG  A SER   A 167 ? 0.1800 0.2597 0.2007 0.0034  -0.0037 0.0473  167  SER   A OG  
3873 O  OG  B SER   A 167 ? 0.1687 0.2671 0.2371 -0.0071 0.0424  0.0302  167  SER   A OG  
3884 N  N   A PHE   A 168 ? 0.1712 0.2449 0.2044 -0.0048 0.0064  0.0429  168  PHE   A N   
3885 N  N   B PHE   A 168 ? 0.1360 0.2714 0.1805 0.0110  0.0277  0.0429  168  PHE   A N   
3886 C  CA  A PHE   A 168 ? 0.1799 0.2437 0.2237 -0.0063 0.0109  0.0338  168  PHE   A CA  
3887 C  CA  B PHE   A 168 ? 0.1330 0.2765 0.1762 0.0114  0.0398  0.0371  168  PHE   A CA  
3888 C  C   A PHE   A 168 ? 0.1941 0.2533 0.2704 -0.0057 0.0319  0.0210  168  PHE   A C   
3889 C  C   B PHE   A 168 ? 0.1415 0.2838 0.2082 0.0003  0.0499  0.0347  168  PHE   A C   
3890 O  O   A PHE   A 168 ? 0.1971 0.2556 0.2961 -0.0088 0.0392  0.0272  168  PHE   A O   
3891 O  O   B PHE   A 168 ? 0.1406 0.2869 0.2150 0.0016  0.0602  0.0316  168  PHE   A O   
3892 C  CB  A PHE   A 168 ? 0.1728 0.2340 0.1948 -0.0127 -0.0038 0.0292  168  PHE   A CB  
3893 C  CB  B PHE   A 168 ? 0.1358 0.2810 0.1714 0.0094  0.0295  0.0354  168  PHE   A CB  
3894 C  CG  A PHE   A 168 ? 0.1685 0.2263 0.1761 -0.0184 -0.0108 0.0200  168  PHE   A CG  
3895 C  CG  B PHE   A 168 ? 0.1422 0.2849 0.1814 0.0068  0.0217  0.0398  168  PHE   A CG  
3896 C  CD1 A PHE   A 168 ? 0.1647 0.2263 0.1746 -0.0243 -0.0153 0.0186  168  PHE   A CD1 
3897 C  CD1 B PHE   A 168 ? 0.1463 0.2883 0.1930 0.0033  0.0183  0.0458  168  PHE   A CD1 
3898 C  CD2 A PHE   A 168 ? 0.1646 0.2217 0.1651 -0.0199 -0.0049 0.0144  168  PHE   A CD2 
3899 C  CD2 B PHE   A 168 ? 0.1411 0.2836 0.1825 0.0057  0.0183  0.0418  168  PHE   A CD2 
3900 C  CE1 A PHE   A 168 ? 0.1529 0.2239 0.1616 -0.0283 -0.0233 0.0094  168  PHE   A CE1 
3901 C  CE1 B PHE   A 168 ? 0.1435 0.2888 0.1971 -0.0013 0.0166  0.0483  168  PHE   A CE1 
3902 C  CE2 A PHE   A 168 ? 0.1628 0.2166 0.1601 -0.0271 -0.0068 0.0141  168  PHE   A CE2 
3903 C  CE2 B PHE   A 168 ? 0.1436 0.2837 0.1898 -0.0010 0.0092  0.0467  168  PHE   A CE2 
3904 C  CZ  A PHE   A 168 ? 0.1544 0.2199 0.1625 -0.0293 -0.0207 0.0110  168  PHE   A CZ  
3905 C  CZ  B PHE   A 168 ? 0.1444 0.2851 0.1957 -0.0048 0.0136  0.0473  168  PHE   A CZ  
3924 N  N   A LEU   A 169 ? 0.2095 0.2575 0.2977 -0.0044 0.0390  0.0019  169  LEU   A N   
3925 N  N   B LEU   A 169 ? 0.1581 0.2914 0.2350 -0.0071 0.0426  0.0376  169  LEU   A N   
3926 C  CA  A LEU   A 169 ? 0.2257 0.2636 0.3211 -0.0003 0.0416  -0.0088 169  LEU   A CA  
3927 C  CA  B LEU   A 169 ? 0.1794 0.3021 0.2749 -0.0149 0.0310  0.0263  169  LEU   A CA  
3928 C  C   A LEU   A 169 ? 0.2157 0.2615 0.3370 -0.0012 0.0610  -0.0046 169  LEU   A C   
3929 C  C   B LEU   A 169 ? 0.1962 0.3106 0.3005 -0.0107 0.0270  0.0140  169  LEU   A C   
3930 O  O   A LEU   A 169 ? 0.2232 0.2647 0.3435 0.0015  0.0556  -0.0063 169  LEU   A O   
3931 O  O   B LEU   A 169 ? 0.2134 0.3172 0.3177 -0.0103 0.0259  0.0160  169  LEU   A O   
3932 C  CB  A LEU   A 169 ? 0.2490 0.2739 0.3177 0.0040  0.0349  -0.0185 169  LEU   A CB  
3933 C  CB  B LEU   A 169 ? 0.1860 0.3046 0.2800 -0.0230 0.0240  0.0265  169  LEU   A CB  
3934 C  CG  A LEU   A 169 ? 0.2669 0.2813 0.3122 0.0077  0.0323  -0.0309 169  LEU   A CG  
3935 C  CG  B LEU   A 169 ? 0.1916 0.3062 0.2828 -0.0321 0.0228  0.0300  169  LEU   A CG  
3936 C  CD1 A LEU   A 169 ? 0.2738 0.2844 0.3123 0.0089  0.0287  -0.0315 169  LEU   A CD1 
3937 C  CD1 B LEU   A 169 ? 0.1945 0.3096 0.3002 -0.0357 0.0121  0.0268  169  LEU   A CD1 
3938 C  CD2 A LEU   A 169 ? 0.2708 0.2841 0.3052 0.0074  0.0376  -0.0352 169  LEU   A CD2 
3939 C  CD2 B LEU   A 169 ? 0.1997 0.3066 0.2801 -0.0357 0.0297  0.0318  169  LEU   A CD2 
3940 O  OXT A LEU   A 169 ? 0.2009 0.2622 0.3357 -0.0035 0.0894  -0.0073 169  LEU   A OXT 
3941 O  OXT B LEU   A 169 ? 0.1961 0.3148 0.3082 -0.0137 0.0122  0.0066  169  LEU   A OXT 
3964 N  N   A SER   B 1   ? 0.3602 0.3549 0.3718 -0.0944 -0.0841 0.0461  1    SER   B N   
3965 N  N   B SER   B 1   ? 0.3226 0.3039 0.2758 -0.1124 -0.0565 0.0395  1    SER   B N   
3966 C  CA  A SER   B 1   ? 0.3511 0.3533 0.3684 -0.0979 -0.0894 0.0448  1    SER   B CA  
3967 C  CA  B SER   B 1   ? 0.3127 0.3062 0.2823 -0.1175 -0.0668 0.0344  1    SER   B CA  
3968 C  C   A SER   B 1   ? 0.3291 0.3501 0.3454 -0.0958 -0.0939 0.0562  1    SER   B C   
3969 C  C   B SER   B 1   ? 0.2911 0.3136 0.2668 -0.1138 -0.0727 0.0565  1    SER   B C   
3970 O  O   A SER   B 1   ? 0.3334 0.3514 0.3229 -0.0936 -0.0958 0.0514  1    SER   B O   
3971 O  O   B SER   B 1   ? 0.2953 0.3146 0.2378 -0.1087 -0.0774 0.0542  1    SER   B O   
3972 C  CB  A SER   B 1   ? 0.3612 0.3532 0.3864 -0.1011 -0.0836 0.0352  1    SER   B CB  
3973 C  CB  B SER   B 1   ? 0.3229 0.2997 0.3021 -0.1214 -0.0595 0.0111  1    SER   B CB  
3974 O  OG  A SER   B 1   ? 0.3720 0.3585 0.4182 -0.1008 -0.0750 0.0327  1    SER   B OG  
3975 O  OG  B SER   B 1   ? 0.3359 0.3016 0.3388 -0.1187 -0.0495 -0.0004 1    SER   B OG  
3990 N  N   A MET   B 2   ? 0.3055 0.3435 0.3449 -0.0931 -0.0901 0.0813  2    MET   B N   
3991 N  N   B MET   B 2   ? 0.2723 0.3181 0.2788 -0.1086 -0.0612 0.0957  2    MET   B N   
3992 C  CA  A MET   B 2   ? 0.2859 0.3369 0.3582 -0.0796 -0.0869 0.0944  2    MET   B CA  
3993 C  CA  B MET   B 2   ? 0.2616 0.3233 0.2963 -0.0876 -0.0561 0.1107  2    MET   B CA  
3994 C  C   A MET   B 2   ? 0.2468 0.3090 0.3175 -0.0723 -0.0953 0.1145  2    MET   B C   
3995 C  C   B MET   B 2   ? 0.2334 0.3043 0.2540 -0.0711 -0.0514 0.1224  2    MET   B C   
3996 O  O   A MET   B 2   ? 0.2393 0.3182 0.3106 -0.0595 -0.1102 0.1202  2    MET   B O   
3997 O  O   B MET   B 2   ? 0.2276 0.3144 0.2556 -0.0604 -0.0508 0.1133  2    MET   B O   
3998 C  CB  A MET   B 2   ? 0.3098 0.3608 0.4315 -0.0644 -0.0699 0.0764  2    MET   B CB  
3999 C  CB  B MET   B 2   ? 0.2868 0.3515 0.3738 -0.0715 -0.0556 0.0965  2    MET   B CB  
4000 C  CG  A MET   B 2   ? 0.3315 0.3803 0.5031 -0.0501 -0.0512 0.0663  2    MET   B CG  
4001 C  CG  B MET   B 2   ? 0.3082 0.3748 0.4386 -0.0575 -0.0505 0.0955  2    MET   B CG  
4002 S  SD  A MET   B 2   ? 0.3508 0.3977 0.5660 -0.0398 -0.0380 0.0584  2    MET   B SD  
4003 S  SD  B MET   B 2   ? 0.3279 0.3956 0.4916 -0.0461 -0.0480 0.0945  2    MET   B SD  
4004 C  CE  A MET   B 2   ? 0.3534 0.4001 0.5713 -0.0383 -0.0323 0.0591  2    MET   B CE  
4005 C  CE  B MET   B 2   ? 0.3291 0.3983 0.4996 -0.0457 -0.0484 0.0890  2    MET   B CE  
4024 N  N   A VAL   B 3   ? 0.2175 0.2690 0.2934 -0.0813 -0.0853 0.1223  3    VAL   B N   
4025 N  N   B VAL   B 3   ? 0.2126 0.2737 0.2272 -0.0698 -0.0402 0.1296  3    VAL   B N   
4026 C  CA  A VAL   B 3   ? 0.2034 0.2375 0.2797 -0.0765 -0.0760 0.1124  3    VAL   B CA  
4027 C  CA  B VAL   B 3   ? 0.2057 0.2496 0.2254 -0.0558 -0.0329 0.1056  3    VAL   B CA  
4028 C  C   A VAL   B 3   ? 0.1825 0.2203 0.2395 -0.0660 -0.0716 0.1097  3    VAL   B C   
4029 C  C   B VAL   B 3   ? 0.1900 0.2349 0.2058 -0.0469 -0.0381 0.0988  3    VAL   B C   
4030 O  O   A VAL   B 3   ? 0.1721 0.2086 0.2427 -0.0633 -0.0758 0.1254  3    VAL   B O   
4031 O  O   B VAL   B 3   ? 0.1927 0.2415 0.2026 -0.0270 -0.0395 0.0909  3    VAL   B O   
4032 C  CB  A VAL   B 3   ? 0.2169 0.2351 0.3163 -0.0766 -0.0693 0.0933  3    VAL   B CB  
4033 C  CB  B VAL   B 3   ? 0.2199 0.2430 0.2527 -0.0492 -0.0272 0.0887  3    VAL   B CB  
4034 C  CG1 A VAL   B 3   ? 0.2260 0.2330 0.3298 -0.0745 -0.0677 0.0876  3    VAL   B CG1 
4035 C  CG1 B VAL   B 3   ? 0.2288 0.2401 0.2687 -0.0482 -0.0256 0.0827  3    VAL   B CG1 
4036 C  CG2 A VAL   B 3   ? 0.2192 0.2380 0.3312 -0.0743 -0.0625 0.0924  3    VAL   B CG2 
4037 C  CG2 B VAL   B 3   ? 0.2213 0.2413 0.2532 -0.0458 -0.0221 0.0890  3    VAL   B CG2 
4056 N  N   . ASN   B 4   ? 0.1749 0.2159 0.2053 -0.0572 -0.0571 0.0915  4    ASN   B N   
4057 C  CA  . ASN   B 4   ? 0.1752 0.2129 0.1706 -0.0546 -0.0500 0.0565  4    ASN   B CA  
4058 C  C   . ASN   B 4   ? 0.1802 0.2254 0.1530 -0.0556 -0.0393 0.0416  4    ASN   B C   
4059 O  O   . ASN   B 4   ? 0.1807 0.2278 0.1837 -0.0571 -0.0288 0.0229  4    ASN   B O   
4060 C  CB  . ASN   B 4   ? 0.1705 0.2033 0.1527 -0.0522 -0.0572 0.0436  4    ASN   B CB  
4061 C  CG  . ASN   B 4   ? 0.1756 0.1882 0.1328 -0.0498 -0.0440 0.0355  4    ASN   B CG  
4062 O  OD1 . ASN   B 4   ? 0.1774 0.1778 0.1373 -0.0494 -0.0459 0.0317  4    ASN   B OD1 
4063 N  ND2 . ASN   B 4   ? 0.1949 0.1957 0.1525 -0.0231 -0.0342 0.0323  4    ASN   B ND2 
4071 N  N   . SER   B 5   ? 0.1915 0.2460 0.1629 -0.0539 -0.0179 0.0388  5    SER   B N   
4072 C  CA  . SER   B 5   ? 0.2189 0.2809 0.1843 -0.0388 -0.0004 0.0451  5    SER   B CA  
4073 C  C   . SER   B 5   ? 0.2344 0.2821 0.2199 -0.0547 0.0272  0.0404  5    SER   B C   
4074 O  O   . SER   B 5   ? 0.2491 0.2776 0.3017 -0.0505 0.0547  0.0397  5    SER   B O   
4075 C  CB  . SER   B 5   ? 0.2334 0.3033 0.2057 -0.0275 0.0043  0.0575  5    SER   B CB  
4076 O  OG  . SER   B 5   ? 0.2485 0.3215 0.2563 -0.0214 0.0063  0.0630  5    SER   B OG  
4082 N  N   . PHE   B 6   ? 0.2493 0.2944 0.1879 -0.0600 0.0380  0.0344  6    PHE   B N   
4083 C  CA  . PHE   B 6   ? 0.2604 0.2937 0.1618 -0.0754 0.0438  0.0138  6    PHE   B CA  
4084 C  C   . PHE   B 6   ? 0.3093 0.3180 0.2055 -0.0820 0.0656  -0.0145 6    PHE   B C   
4085 O  O   . PHE   B 6   ? 0.3231 0.3439 0.2380 -0.0762 0.0481  -0.0318 6    PHE   B O   
4086 C  CB  . PHE   B 6   ? 0.2321 0.2733 0.1495 -0.0717 0.0179  0.0109  6    PHE   B CB  
4087 C  CG  . PHE   B 6   ? 0.2002 0.2456 0.1338 -0.0641 0.0052  0.0087  6    PHE   B CG  
4088 C  CD1 . PHE   B 6   ? 0.1983 0.2170 0.1193 -0.0589 -0.0061 0.0090  6    PHE   B CD1 
4089 C  CD2 . PHE   B 6   ? 0.1746 0.2423 0.1423 -0.0573 0.0037  0.0312  6    PHE   B CD2 
4090 C  CE1 . PHE   B 6   ? 0.1910 0.1962 0.1322 -0.0511 -0.0131 0.0038  6    PHE   B CE1 
4091 C  CE2 . PHE   B 6   ? 0.1736 0.2265 0.1673 -0.0454 0.0041  0.0292  6    PHE   B CE2 
4092 C  CZ  . PHE   B 6   ? 0.1760 0.2027 0.1533 -0.0446 -0.0012 0.0131  6    PHE   B CZ  
4102 N  N   . SER   B 7   ? 0.3430 0.3023 0.2172 -0.1003 0.1000  -0.0358 7    SER   B N   
4103 C  CA  . SER   B 7   ? 0.3759 0.3098 0.2735 -0.0995 0.1192  -0.0473 7    SER   B CA  
4104 C  C   . SER   B 7   ? 0.3711 0.2969 0.2841 -0.1022 0.1382  -0.0575 7    SER   B C   
4105 O  O   . SER   B 7   ? 0.3745 0.2967 0.3198 -0.1064 0.1375  -0.0566 7    SER   B O   
4106 C  CB  . SER   B 7   ? 0.4005 0.3248 0.3240 -0.0964 0.1255  -0.0482 7    SER   B CB  
4107 O  OG  . SER   B 7   ? 0.4158 0.3338 0.3739 -0.0902 0.1230  -0.0452 7    SER   B OG  
4113 N  N   . GLY   B 8   ? 0.3683 0.2869 0.2968 -0.0897 0.1411  -0.0696 8    GLY   B N   
4114 C  CA  . GLY   B 8   ? 0.3538 0.2710 0.3059 -0.0855 0.1398  -0.0731 8    GLY   B CA  
4115 C  C   . GLY   B 8   ? 0.3333 0.2473 0.2948 -0.0845 0.1389  -0.0688 8    GLY   B C   
4116 O  O   . GLY   B 8   ? 0.3401 0.2523 0.3260 -0.0763 0.1448  -0.0756 8    GLY   B O   
4120 N  N   . TYR   B 9   ? 0.3095 0.2274 0.2512 -0.0762 0.1145  -0.0733 9    TYR   B N   
4121 C  CA  . TYR   B 9   ? 0.2839 0.2000 0.2226 -0.0668 0.0825  -0.0578 9    TYR   B CA  
4122 C  C   . TYR   B 9   ? 0.2763 0.2015 0.1993 -0.0611 0.0494  -0.0452 9    TYR   B C   
4123 O  O   . TYR   B 9   ? 0.2887 0.2255 0.2407 -0.0619 0.0501  -0.0255 9    TYR   B O   
4124 C  CB  . TYR   B 9   ? 0.2769 0.1822 0.2221 -0.0557 0.0753  -0.0560 9    TYR   B CB  
4125 C  CG  . TYR   B 9   ? 0.2690 0.1681 0.2300 -0.0552 0.0718  -0.0567 9    TYR   B CG  
4126 C  CD1 . TYR   B 9   ? 0.2712 0.1674 0.2459 -0.0685 0.0750  -0.0445 9    TYR   B CD1 
4127 C  CD2 . TYR   B 9   ? 0.2549 0.1602 0.2216 -0.0520 0.0691  -0.0574 9    TYR   B CD2 
4128 C  CE1 . TYR   B 9   ? 0.2648 0.1753 0.2507 -0.0738 0.0763  -0.0560 9    TYR   B CE1 
4129 C  CE2 . TYR   B 9   ? 0.2532 0.1627 0.2331 -0.0513 0.0677  -0.0569 9    TYR   B CE2 
4130 C  CZ  . TYR   B 9   ? 0.2565 0.1737 0.2442 -0.0672 0.0722  -0.0649 9    TYR   B CZ  
4131 O  OH  . TYR   B 9   ? 0.2549 0.1893 0.2603 -0.0776 0.0624  -0.0778 9    TYR   B OH  
4141 N  N   . LEU   B 10  ? 0.2572 0.1781 0.1755 -0.0534 0.0211  -0.0368 10   LEU   B N   
4142 C  CA  . LEU   B 10  ? 0.2545 0.1730 0.1761 -0.0582 -0.0069 -0.0333 10   LEU   B CA  
4143 C  C   . LEU   B 10  ? 0.2350 0.1728 0.1744 -0.0561 -0.0202 -0.0300 10   LEU   B C   
4144 O  O   . LEU   B 10  ? 0.2198 0.1717 0.1758 -0.0454 -0.0156 -0.0186 10   LEU   B O   
4145 C  CB  . LEU   B 10  ? 0.2754 0.1750 0.1996 -0.0632 -0.0234 -0.0167 10   LEU   B CB  
4146 C  CG  . LEU   B 10  ? 0.2952 0.1820 0.2370 -0.0575 -0.0529 -0.0027 10   LEU   B CG  
4147 C  CD1 . LEU   B 10  ? 0.3092 0.1920 0.2686 -0.0555 -0.0516 -0.0064 10   LEU   B CD1 
4148 C  CD2 . LEU   B 10  ? 0.3011 0.1916 0.2635 -0.0562 -0.0576 0.0120  10   LEU   B CD2 
4160 N  N   . LYS   B 11  ? 0.2461 0.1993 0.1866 -0.0526 -0.0305 -0.0203 11   LYS   B N   
4161 C  CA  . LYS   B 11  ? 0.2687 0.2267 0.2143 -0.0416 -0.0425 -0.0282 11   LYS   B CA  
4162 C  C   . LYS   B 11  ? 0.2526 0.2068 0.2126 -0.0609 -0.0390 -0.0410 11   LYS   B C   
4163 O  O   . LYS   B 11  ? 0.2688 0.2250 0.2499 -0.0766 -0.0336 -0.0680 11   LYS   B O   
4164 C  CB  . LYS   B 11  ? 0.3030 0.2749 0.2691 -0.0160 -0.0499 -0.0209 11   LYS   B CB  
4165 C  CG  . LYS   B 11  ? 0.3326 0.3062 0.3332 -0.0019 -0.0533 -0.0168 11   LYS   B CG  
4166 C  CD  . LYS   B 11  ? 0.3570 0.3274 0.3933 0.0072  -0.0569 -0.0171 11   LYS   B CD  
4167 C  CE  . LYS   B 11  ? 0.3761 0.3425 0.4380 0.0088  -0.0595 -0.0189 11   LYS   B CE  
4168 N  NZ  . LYS   B 11  ? 0.3837 0.3527 0.4640 0.0074  -0.0599 -0.0180 11   LYS   B NZ  
4182 N  N   . LEU   B 12  ? 0.2196 0.1803 0.2073 -0.0516 -0.0280 -0.0408 12   LEU   B N   
4183 C  CA  . LEU   B 12  ? 0.2041 0.1617 0.2257 -0.0435 -0.0186 -0.0370 12   LEU   B CA  
4184 C  C   . LEU   B 12  ? 0.1875 0.1626 0.2413 -0.0468 -0.0323 -0.0341 12   LEU   B C   
4185 O  O   . LEU   B 12  ? 0.1891 0.1670 0.2659 -0.0542 -0.0453 -0.0272 12   LEU   B O   
4186 C  CB  . LEU   B 12  ? 0.2073 0.1443 0.2227 -0.0320 -0.0088 -0.0406 12   LEU   B CB  
4187 C  CG  . LEU   B 12  ? 0.2109 0.1425 0.2352 -0.0362 -0.0075 -0.0302 12   LEU   B CG  
4188 C  CD1 . LEU   B 12  ? 0.2200 0.1483 0.2303 -0.0251 -0.0082 -0.0161 12   LEU   B CD1 
4189 C  CD2 . LEU   B 12  ? 0.2185 0.1458 0.2550 -0.0361 -0.0054 -0.0360 12   LEU   B CD2 
4201 N  N   . THR   B 13  ? 0.1814 0.1654 0.2437 -0.0433 -0.0366 -0.0412 13   THR   B N   
4202 C  CA  . THR   B 13  ? 0.1833 0.1732 0.2357 -0.0531 -0.0461 -0.0283 13   THR   B CA  
4203 C  C   . THR   B 13  ? 0.2253 0.1934 0.2475 -0.0618 -0.0597 -0.0163 13   THR   B C   
4204 O  O   . THR   B 13  ? 0.2417 0.1933 0.2589 -0.0631 -0.0306 -0.0225 13   THR   B O   
4205 C  CB  . THR   B 13  ? 0.1699 0.1782 0.2406 -0.0463 -0.0435 -0.0203 13   THR   B CB  
4206 O  OG1 . THR   B 13  ? 0.1624 0.1710 0.2461 -0.0402 -0.0323 -0.0194 13   THR   B OG1 
4207 C  CG2 . THR   B 13  ? 0.1805 0.1869 0.2527 -0.0408 -0.0365 -0.0189 13   THR   B CG2 
4215 N  N   A ASP   B 14  ? 0.2357 0.2043 0.2610 -0.0649 -0.0834 -0.0088 14   ASP   B N   
4216 N  N   B ASP   B 14  ? 0.2376 0.2058 0.2548 -0.0622 -0.0807 -0.0044 14   ASP   B N   
4217 C  CA  A ASP   B 14  ? 0.2466 0.2171 0.2878 -0.0625 -0.0859 0.0052  14   ASP   B CA  
4218 C  CA  B ASP   B 14  ? 0.2499 0.2196 0.2758 -0.0576 -0.0819 0.0118  14   ASP   B CA  
4219 C  C   A ASP   B 14  ? 0.2345 0.2013 0.2473 -0.0613 -0.0718 0.0105  14   ASP   B C   
4220 C  C   B ASP   B 14  ? 0.2357 0.2037 0.2419 -0.0578 -0.0722 0.0124  14   ASP   B C   
4221 O  O   A ASP   B 14  ? 0.2498 0.2070 0.2455 -0.0603 -0.0664 0.0202  14   ASP   B O   
4222 O  O   B ASP   B 14  ? 0.2506 0.2100 0.2421 -0.0539 -0.0700 0.0187  14   ASP   B O   
4223 C  CB  A ASP   B 14  ? 0.2659 0.2446 0.3552 -0.0605 -0.0985 0.0085  14   ASP   B CB  
4224 C  CB  B ASP   B 14  ? 0.2722 0.2485 0.3327 -0.0517 -0.0887 0.0204  14   ASP   B CB  
4225 C  CG  A ASP   B 14  ? 0.2854 0.2672 0.4160 -0.0575 -0.0978 0.0051  14   ASP   B CG  
4226 C  CG  B ASP   B 14  ? 0.2936 0.2727 0.3849 -0.0466 -0.0861 0.0187  14   ASP   B CG  
4227 O  OD1 A ASP   B 14  ? 0.2951 0.2730 0.4312 -0.0631 -0.0959 -0.0027 14   ASP   B OD1 
4228 O  OD1 B ASP   B 14  ? 0.3025 0.2820 0.3960 -0.0478 -0.0797 0.0155  14   ASP   B OD1 
4229 O  OD2 A ASP   B 14  ? 0.2898 0.2762 0.4447 -0.0545 -0.0979 0.0073  14   ASP   B OD2 
4230 O  OD2 B ASP   B 14  ? 0.3002 0.2812 0.4079 -0.0477 -0.0908 0.0160  14   ASP   B OD2 
4239 N  N   . ASN   B 15  ? 0.2057 0.1798 0.2166 -0.0531 -0.0722 0.0072  15   ASN   B N   
4240 C  CA  . ASN   B 15  ? 0.1675 0.1553 0.2004 -0.0326 -0.0458 -0.0003 15   ASN   B CA  
4241 C  C   . ASN   B 15  ? 0.1501 0.1395 0.1894 -0.0213 -0.0351 -0.0099 15   ASN   B C   
4242 O  O   . ASN   B 15  ? 0.1519 0.1356 0.2043 -0.0208 -0.0382 -0.0209 15   ASN   B O   
4243 C  CB  . ASN   B 15  ? 0.1576 0.1465 0.2258 -0.0231 -0.0405 0.0036  15   ASN   B CB  
4244 C  CG  . ASN   B 15  ? 0.1432 0.1475 0.2311 -0.0243 -0.0251 0.0045  15   ASN   B CG  
4245 O  OD1 . ASN   B 15  ? 0.1486 0.1732 0.2534 -0.0386 -0.0295 0.0123  15   ASN   B OD1 
4246 N  ND2 . ASN   B 15  ? 0.1474 0.1286 0.2248 -0.0167 0.0024  -0.0128 15   ASN   B ND2 
4254 N  N   . VAL   B 16  ? 0.1498 0.1349 0.1918 -0.0231 -0.0393 -0.0081 16   VAL   B N   
4255 C  CA  . VAL   B 16  ? 0.1471 0.1386 0.1803 -0.0241 -0.0244 -0.0266 16   VAL   B CA  
4256 C  C   . VAL   B 16  ? 0.1481 0.1417 0.1752 -0.0316 -0.0259 -0.0172 16   VAL   B C   
4257 O  O   . VAL   B 16  ? 0.1536 0.1523 0.1966 -0.0270 -0.0250 -0.0296 16   VAL   B O   
4258 C  CB  . VAL   B 16  ? 0.1519 0.1359 0.1837 -0.0101 -0.0130 -0.0169 16   VAL   B CB  
4259 C  CG1 . VAL   B 16  ? 0.1634 0.1340 0.1811 0.0032  -0.0126 -0.0117 16   VAL   B CG1 
4260 C  CG2 . VAL   B 16  ? 0.1570 0.1427 0.2043 -0.0055 -0.0092 -0.0098 16   VAL   B CG2 
4270 N  N   . TYR   B 17  ? 0.1571 0.1539 0.1726 -0.0306 -0.0193 -0.0210 17   TYR   B N   
4271 C  CA  . TYR   B 17  ? 0.1628 0.1696 0.1697 -0.0321 -0.0175 -0.0088 17   TYR   B CA  
4272 C  C   . TYR   B 17  ? 0.1545 0.1420 0.1633 -0.0376 -0.0136 -0.0143 17   TYR   B C   
4273 O  O   . TYR   B 17  ? 0.1556 0.1483 0.1765 -0.0283 -0.0240 -0.0353 17   TYR   B O   
4274 C  CB  . TYR   B 17  ? 0.1884 0.2154 0.1871 -0.0203 -0.0185 0.0264  17   TYR   B CB  
4275 C  CG  . TYR   B 17  ? 0.2121 0.2605 0.2227 -0.0122 -0.0329 0.0403  17   TYR   B CG  
4276 C  CD1 . TYR   B 17  ? 0.2300 0.2796 0.2435 -0.0071 -0.0447 0.0525  17   TYR   B CD1 
4277 C  CD2 . TYR   B 17  ? 0.2340 0.2895 0.2484 -0.0011 -0.0423 0.0363  17   TYR   B CD2 
4278 C  CE1 . TYR   B 17  ? 0.2460 0.3049 0.2601 0.0028  -0.0563 0.0480  17   TYR   B CE1 
4279 C  CE2 . TYR   B 17  ? 0.2502 0.3152 0.2730 0.0099  -0.0578 0.0419  17   TYR   B CE2 
4280 C  CZ  . TYR   B 17  ? 0.2601 0.3238 0.2761 0.0132  -0.0644 0.0478  17   TYR   B CZ  
4281 O  OH  . TYR   B 17  ? 0.2787 0.3364 0.3000 0.0221  -0.0684 0.0489  17   TYR   B OH  
4291 N  N   . ILE   B 18  ? 0.1647 0.1422 0.1564 -0.0324 -0.0065 -0.0190 18   ILE   B N   
4292 C  CA  . ILE   B 18  ? 0.1668 0.1412 0.1565 -0.0317 -0.0067 -0.0274 18   ILE   B CA  
4293 C  C   . ILE   B 18  ? 0.1797 0.1439 0.1567 -0.0380 -0.0025 -0.0338 18   ILE   B C   
4294 O  O   . ILE   B 18  ? 0.1971 0.1570 0.1694 -0.0365 0.0132  -0.0392 18   ILE   B O   
4295 C  CB  . ILE   B 18  ? 0.1762 0.1428 0.1689 -0.0357 -0.0032 -0.0208 18   ILE   B CB  
4296 C  CG1 . ILE   B 18  ? 0.1736 0.1443 0.1859 -0.0345 0.0004  -0.0095 18   ILE   B CG1 
4297 C  CG2 . ILE   B 18  ? 0.1797 0.1486 0.1817 -0.0422 -0.0089 -0.0168 18   ILE   B CG2 
4298 C  CD1 . ILE   B 18  ? 0.1819 0.1684 0.2133 -0.0272 -0.0154 0.0135  18   ILE   B CD1 
4310 N  N   . LYS   B 19  ? 0.1779 0.1451 0.1696 -0.0259 0.0237  -0.0363 19   LYS   B N   
4311 C  CA  . LYS   B 19  ? 0.1892 0.1499 0.1878 -0.0262 0.0280  -0.0400 19   LYS   B CA  
4312 C  C   . LYS   B 19  ? 0.1710 0.1461 0.1956 -0.0231 0.0292  -0.0505 19   LYS   B C   
4313 O  O   . LYS   B 19  ? 0.1690 0.1501 0.1801 -0.0165 0.0196  -0.0424 19   LYS   B O   
4314 C  CB  . LYS   B 19  ? 0.2125 0.1684 0.2047 -0.0285 0.0370  -0.0299 19   LYS   B CB  
4315 C  CG  . LYS   B 19  ? 0.2375 0.1937 0.2326 -0.0327 0.0537  -0.0371 19   LYS   B CG  
4316 C  CD  . LYS   B 19  ? 0.2664 0.2226 0.2425 -0.0407 0.0588  -0.0313 19   LYS   B CD  
4317 C  CE  . LYS   B 19  ? 0.2925 0.2459 0.2676 -0.0444 0.0561  -0.0301 19   LYS   B CE  
4318 N  NZ  . LYS   B 19  ? 0.3047 0.2601 0.2784 -0.0501 0.0583  -0.0284 19   LYS   B NZ  
4332 N  N   . ASN   B 20  ? 0.1688 0.1554 0.2305 -0.0147 0.0364  -0.0613 20   ASN   B N   
4333 C  CA  . ASN   B 20  ? 0.1753 0.1714 0.2516 -0.0100 0.0411  -0.0740 20   ASN   B CA  
4334 C  C   . ASN   B 20  ? 0.1740 0.1901 0.2523 -0.0200 0.0484  -0.0802 20   ASN   B C   
4335 O  O   . ASN   B 20  ? 0.1881 0.2213 0.2723 -0.0327 0.0504  -0.0827 20   ASN   B O   
4336 C  CB  . ASN   B 20  ? 0.2025 0.1736 0.2873 0.0070  0.0281  -0.0777 20   ASN   B CB  
4337 C  CG  . ASN   B 20  ? 0.2246 0.1787 0.3143 0.0314  0.0238  -0.0831 20   ASN   B CG  
4338 O  OD1 . ASN   B 20  ? 0.2526 0.2065 0.3428 0.0465  0.0191  -0.0844 20   ASN   B OD1 
4339 N  ND2 . ASN   B 20  ? 0.2163 0.1808 0.3095 0.0333  0.0195  -0.0786 20   ASN   B ND2 
4346 N  N   . ALA   B 21  ? 0.1748 0.1763 0.2396 -0.0248 0.0501  -0.0689 21   ALA   B N   
4347 C  CA  . ALA   B 21  ? 0.1828 0.1806 0.2559 -0.0284 0.0383  -0.0510 21   ALA   B CA  
4348 C  C   . ALA   B 21  ? 0.1812 0.1577 0.2436 -0.0203 0.0409  -0.0402 21   ALA   B C   
4349 O  O   . ALA   B 21  ? 0.1921 0.1468 0.2406 -0.0287 0.0424  -0.0324 21   ALA   B O   
4350 C  CB  . ALA   B 21  ? 0.2019 0.2077 0.2626 -0.0398 0.0367  -0.0289 21   ALA   B CB  
4356 N  N   . ASP   B 22  ? 0.1713 0.1504 0.2361 -0.0218 0.0288  -0.0370 22   ASP   B N   
4357 C  CA  . ASP   B 22  ? 0.1688 0.1432 0.2283 -0.0097 0.0277  -0.0260 22   ASP   B CA  
4358 C  C   . ASP   B 22  ? 0.1621 0.1427 0.1793 -0.0148 0.0212  -0.0128 22   ASP   B C   
4359 O  O   . ASP   B 22  ? 0.1631 0.1442 0.1886 -0.0093 0.0139  -0.0065 22   ASP   B O   
4360 C  CB  . ASP   B 22  ? 0.1798 0.1473 0.2753 -0.0058 0.0236  -0.0114 22   ASP   B CB  
4361 C  CG  . ASP   B 22  ? 0.1842 0.1648 0.3145 -0.0016 0.0001  -0.0140 22   ASP   B CG  
4362 O  OD1 . ASP   B 22  ? 0.1939 0.1573 0.3088 0.0011  -0.0270 -0.0153 22   ASP   B OD1 
4363 O  OD2 . ASP   B 22  ? 0.1915 0.1923 0.3721 0.0076  -0.0169 -0.0233 22   ASP   B OD2 
4368 N  N   . ILE   B 23  ? 0.1680 0.1343 0.1626 -0.0101 0.0112  0.0071  23   ILE   B N   
4369 C  CA  . ILE   B 23  ? 0.1611 0.1321 0.1493 -0.0112 -0.0024 0.0056  23   ILE   B CA  
4370 C  C   . ILE   B 23  ? 0.1525 0.1292 0.1501 -0.0037 -0.0011 0.0031  23   ILE   B C   
4371 O  O   . ILE   B 23  ? 0.1423 0.1347 0.1485 -0.0062 -0.0006 0.0071  23   ILE   B O   
4372 C  CB  . ILE   B 23  ? 0.1577 0.1350 0.1535 -0.0205 0.0016  0.0153  23   ILE   B CB  
4373 C  CG1 . ILE   B 23  ? 0.1616 0.1410 0.1692 -0.0102 0.0069  0.0181  23   ILE   B CG1 
4374 C  CG2 . ILE   B 23  ? 0.1638 0.1550 0.1613 -0.0186 0.0018  0.0076  23   ILE   B CG2 
4375 C  CD1 . ILE   B 23  ? 0.1674 0.1565 0.1846 -0.0017 0.0074  0.0159  23   ILE   B CD1 
4387 N  N   . VAL   B 24  ? 0.1565 0.1280 0.1639 -0.0099 -0.0041 0.0012  24   VAL   B N   
4388 C  CA  . VAL   B 24  ? 0.1499 0.1377 0.1771 -0.0063 -0.0150 -0.0053 24   VAL   B CA  
4389 C  C   . VAL   B 24  ? 0.1506 0.1432 0.1810 -0.0087 -0.0063 -0.0033 24   VAL   B C   
4390 O  O   . VAL   B 24  ? 0.1457 0.1487 0.1947 -0.0172 -0.0018 0.0116  24   VAL   B O   
4391 C  CB  . VAL   B 24  ? 0.1570 0.1542 0.1838 0.0051  -0.0214 -0.0058 24   VAL   B CB  
4392 C  CG1 . VAL   B 24  ? 0.1532 0.1561 0.2090 -0.0068 -0.0206 0.0001  24   VAL   B CG1 
4393 C  CG2 . VAL   B 24  ? 0.1612 0.1837 0.1889 0.0090  -0.0140 -0.0107 24   VAL   B CG2 
4403 N  N   . GLU   B 25  ? 0.1688 0.1571 0.1762 -0.0095 -0.0001 -0.0034 25   GLU   B N   
4404 C  CA  . GLU   B 25  ? 0.1762 0.1808 0.2001 0.0058  0.0097  -0.0041 25   GLU   B CA  
4405 C  C   . GLU   B 25  ? 0.1709 0.1684 0.1743 -0.0092 0.0139  0.0026  25   GLU   B C   
4406 O  O   . GLU   B 25  ? 0.1727 0.1872 0.1872 -0.0084 0.0232  0.0102  25   GLU   B O   
4407 C  CB  . GLU   B 25  ? 0.2068 0.2204 0.2753 0.0312  0.0236  -0.0088 25   GLU   B CB  
4408 C  CG  . GLU   B 25  ? 0.2494 0.2838 0.3838 0.0382  0.0225  -0.0175 25   GLU   B CG  
4409 C  CD  . GLU   B 25  ? 0.2847 0.3360 0.4703 0.0326  0.0213  -0.0237 25   GLU   B CD  
4410 O  OE1 . GLU   B 25  ? 0.2972 0.3544 0.5000 0.0359  0.0300  -0.0237 25   GLU   B OE1 
4411 O  OE2 . GLU   B 25  ? 0.2949 0.3512 0.5037 0.0275  0.0128  -0.0316 25   GLU   B OE2 
4418 N  N   A GLU   B 26  ? 0.1701 0.1632 0.1484 -0.0223 0.0064  -0.0011 26   GLU   B N   
4419 N  N   B GLU   B 26  ? 0.1664 0.1667 0.1648 -0.0189 0.0077  0.0091  26   GLU   B N   
4420 C  CA  A GLU   B 26  ? 0.1726 0.1685 0.1553 -0.0300 -0.0044 -0.0045 26   GLU   B CA  
4421 C  CA  B GLU   B 26  ? 0.1641 0.1742 0.1853 -0.0244 -0.0021 0.0133  26   GLU   B CA  
4422 C  C   A GLU   B 26  ? 0.1575 0.1652 0.1529 -0.0234 0.0016  0.0110  26   GLU   B C   
4423 C  C   B GLU   B 26  ? 0.1531 0.1683 0.1655 -0.0203 0.0034  0.0207  26   GLU   B C   
4424 O  O   A GLU   B 26  ? 0.1730 0.1815 0.1616 -0.0190 -0.0044 0.0153  26   GLU   B O   
4425 O  O   B GLU   B 26  ? 0.1686 0.1845 0.1700 -0.0162 -0.0025 0.0249  26   GLU   B O   
4426 C  CB  A GLU   B 26  ? 0.1952 0.1801 0.1644 -0.0355 -0.0035 0.0009  26   GLU   B CB  
4427 C  CB  B GLU   B 26  ? 0.1766 0.1888 0.2211 -0.0267 -0.0013 0.0284  26   GLU   B CB  
4428 C  CG  A GLU   B 26  ? 0.2223 0.1889 0.1985 -0.0353 0.0080  -0.0059 26   GLU   B CG  
4429 C  CG  B GLU   B 26  ? 0.1922 0.2026 0.2715 -0.0211 0.0113  0.0274  26   GLU   B CG  
4430 C  CD  A GLU   B 26  ? 0.2376 0.1919 0.2056 -0.0420 0.0233  -0.0182 26   GLU   B CD  
4431 C  CD  B GLU   B 26  ? 0.1923 0.2055 0.2933 -0.0238 0.0242  0.0181  26   GLU   B CD  
4432 O  OE1 A GLU   B 26  ? 0.2435 0.1852 0.1817 -0.0326 0.0453  -0.0280 26   GLU   B OE1 
4433 O  OE1 B GLU   B 26  ? 0.1916 0.2065 0.3254 -0.0335 0.0470  0.0103  26   GLU   B OE1 
4434 O  OE2 A GLU   B 26  ? 0.2424 0.2071 0.2291 -0.0501 0.0292  0.0018  26   GLU   B OE2 
4435 O  OE2 B GLU   B 26  ? 0.1905 0.2040 0.2834 -0.0133 0.0251  0.0033  26   GLU   B OE2 
4448 N  N   . ALA   B 27  ? 0.1397 0.1559 0.1588 -0.0199 0.0074  0.0148  27   ALA   B N   
4449 C  CA  . ALA   B 27  ? 0.1435 0.1531 0.1705 -0.0100 0.0003  0.0278  27   ALA   B CA  
4450 C  C   . ALA   B 27  ? 0.1439 0.1641 0.1964 -0.0110 0.0142  0.0366  27   ALA   B C   
4451 O  O   . ALA   B 27  ? 0.1522 0.1670 0.2072 -0.0061 0.0108  0.0380  27   ALA   B O   
4452 C  CB  . ALA   B 27  ? 0.1583 0.1338 0.1779 -0.0142 0.0021  0.0256  27   ALA   B CB  
4459 N  N   . LYS   B 28  ? 0.1395 0.1856 0.2329 -0.0156 0.0242  0.0563  28   LYS   B N   
4460 C  CA  . LYS   B 28  ? 0.1569 0.2279 0.2615 -0.0108 0.0545  0.0857  28   LYS   B CA  
4461 C  C   . LYS   B 28  ? 0.1875 0.2529 0.2449 0.0029  0.0659  0.0726  28   LYS   B C   
4462 O  O   . LYS   B 28  ? 0.2113 0.2550 0.2597 -0.0002 0.0629  0.0755  28   LYS   B O   
4463 C  CB  . LYS   B 28  ? 0.1718 0.2628 0.3142 0.0008  0.0672  0.1102  28   LYS   B CB  
4464 C  CG  . LYS   B 28  ? 0.1907 0.3070 0.3530 0.0134  0.0636  0.1302  28   LYS   B CG  
4465 C  CD  . LYS   B 28  ? 0.2271 0.3658 0.4091 0.0219  0.0781  0.1313  28   LYS   B CD  
4466 C  CE  . LYS   B 28  ? 0.2562 0.4037 0.4546 0.0352  0.0840  0.1334  28   LYS   B CE  
4467 N  NZ  . LYS   B 28  ? 0.2560 0.4110 0.4784 0.0456  0.0814  0.1357  28   LYS   B NZ  
4481 N  N   A LYS   B 29  ? 0.2050 0.2706 0.2406 0.0148  0.0649  0.0633  29   LYS   B N   
4482 N  N   B LYS   B 29  ? 0.2038 0.2706 0.2390 0.0136  0.0637  0.0639  29   LYS   B N   
4483 C  CA  A LYS   B 29  ? 0.2359 0.2943 0.2651 0.0149  0.0586  0.0570  29   LYS   B CA  
4484 C  CA  B LYS   B 29  ? 0.2336 0.2946 0.2625 0.0124  0.0564  0.0582  29   LYS   B CA  
4485 C  C   A LYS   B 29  ? 0.2321 0.2969 0.2367 0.0157  0.0473  0.0668  29   LYS   B C   
4486 C  C   B LYS   B 29  ? 0.2289 0.2978 0.2340 0.0129  0.0440  0.0677  29   LYS   B C   
4487 O  O   A LYS   B 29  ? 0.2463 0.3093 0.2430 0.0206  0.0425  0.0653  29   LYS   B O   
4488 O  O   B LYS   B 29  ? 0.2400 0.3121 0.2407 0.0156  0.0341  0.0654  29   LYS   B O   
4489 C  CB  A LYS   B 29  ? 0.2734 0.3178 0.3339 0.0116  0.0570  0.0399  29   LYS   B CB  
4490 C  CB  B LYS   B 29  ? 0.2710 0.3176 0.3311 0.0089  0.0548  0.0421  29   LYS   B CB  
4491 C  CG  A LYS   B 29  ? 0.3030 0.3372 0.4028 0.0077  0.0582  0.0306  29   LYS   B CG  
4492 C  CG  B LYS   B 29  ? 0.3008 0.3364 0.3994 0.0045  0.0563  0.0339  29   LYS   B CG  
4493 C  CD  A LYS   B 29  ? 0.3261 0.3508 0.4571 0.0036  0.0639  0.0207  29   LYS   B CD  
4494 C  CD  B LYS   B 29  ? 0.3237 0.3495 0.4530 0.0001  0.0607  0.0247  29   LYS   B CD  
4495 C  CE  A LYS   B 29  ? 0.3426 0.3588 0.4944 0.0005  0.0690  0.0133  29   LYS   B CE  
4496 C  CE  B LYS   B 29  ? 0.3396 0.3572 0.4901 -0.0034 0.0656  0.0181  29   LYS   B CE  
4497 N  NZ  A LYS   B 29  ? 0.3520 0.3638 0.5186 -0.0014 0.0708  0.0087  29   LYS   B NZ  
4498 N  NZ  B LYS   B 29  ? 0.3484 0.3622 0.5144 -0.0051 0.0667  0.0142  29   LYS   B NZ  
4525 N  N   . VAL   B 30  ? 0.2124 0.2880 0.2178 0.0068  0.0376  0.0753  30   VAL   B N   
4526 C  CA  . VAL   B 30  ? 0.1931 0.2752 0.2509 -0.0066 0.0015  0.0862  30   VAL   B CA  
4527 C  C   . VAL   B 30  ? 0.1675 0.2667 0.2492 -0.0098 0.0100  0.1082  30   VAL   B C   
4528 O  O   . VAL   B 30  ? 0.1811 0.2842 0.2488 -0.0047 0.0193  0.1182  30   VAL   B O   
4529 C  CB  . VAL   B 30  ? 0.1989 0.2677 0.2975 -0.0223 -0.0265 0.0774  30   VAL   B CB  
4530 C  CG1 . VAL   B 30  ? 0.2036 0.2729 0.2954 -0.0186 -0.0217 0.0756  30   VAL   B CG1 
4531 C  CG2 . VAL   B 30  ? 0.2100 0.2656 0.3195 -0.0273 -0.0398 0.0611  30   VAL   B CG2 
4542 N  N   . LYS   B 31  ? 0.1561 0.2318 0.2857 -0.0209 0.0014  0.1178  31   LYS   B N   
4543 C  CA  . LYS   B 31  ? 0.1460 0.2233 0.3286 -0.0302 -0.0042 0.1175  31   LYS   B CA  
4544 C  C   . LYS   B 31  ? 0.1435 0.1867 0.2745 -0.0297 -0.0246 0.0973  31   LYS   B C   
4545 O  O   . LYS   B 31  ? 0.1543 0.2048 0.2936 -0.0230 -0.0171 0.1165  31   LYS   B O   
4546 C  CB  . LYS   B 31  ? 0.1632 0.2664 0.3995 -0.0293 0.0282  0.1320  31   LYS   B CB  
4547 C  CG  . LYS   B 31  ? 0.1974 0.3076 0.4575 -0.0303 0.0484  0.1328  31   LYS   B CG  
4548 C  CD  . LYS   B 31  ? 0.2290 0.3524 0.5019 -0.0196 0.0528  0.1215  31   LYS   B CD  
4549 C  CE  . LYS   B 31  ? 0.2461 0.3792 0.5418 -0.0140 0.0485  0.1067  31   LYS   B CE  
4550 N  NZ  . LYS   B 31  ? 0.2713 0.3961 0.5570 -0.0068 0.0398  0.0940  31   LYS   B NZ  
4564 N  N   . PRO   B 32  ? 0.1528 0.1522 0.2000 -0.0320 -0.0441 0.0513  32   PRO   B N   
4565 C  CA  . PRO   B 32  ? 0.1618 0.1453 0.1568 -0.0340 -0.0388 0.0314  32   PRO   B CA  
4566 C  C   . PRO   B 32  ? 0.1695 0.1300 0.1638 -0.0369 -0.0515 0.0314  32   PRO   B C   
4567 O  O   . PRO   B 32  ? 0.1861 0.1354 0.2020 -0.0381 -0.0722 0.0298  32   PRO   B O   
4568 C  CB  . PRO   B 32  ? 0.1771 0.1404 0.1561 -0.0346 -0.0299 0.0146  32   PRO   B CB  
4569 C  CG  . PRO   B 32  ? 0.1938 0.1299 0.1624 -0.0313 -0.0467 0.0206  32   PRO   B CG  
4570 C  CD  . PRO   B 32  ? 0.1804 0.1379 0.1797 -0.0230 -0.0534 0.0306  32   PRO   B CD  
4578 N  N   . THR   B 33  ? 0.1763 0.1258 0.1432 -0.0318 -0.0480 0.0240  33   THR   B N   
4579 C  CA  . THR   B 33  ? 0.1861 0.1317 0.1436 -0.0352 -0.0507 0.0227  33   THR   B CA  
4580 C  C   . THR   B 33  ? 0.1868 0.1219 0.1303 -0.0332 -0.0474 0.0129  33   THR   B C   
4581 O  O   . THR   B 33  ? 0.2051 0.1273 0.1565 -0.0418 -0.0555 0.0177  33   THR   B O   
4582 C  CB  . THR   B 33  ? 0.1971 0.1392 0.1485 -0.0181 -0.0574 0.0279  33   THR   B CB  
4583 O  OG1 . THR   B 33  ? 0.1893 0.1517 0.1517 -0.0272 -0.0546 0.0334  33   THR   B OG1 
4584 C  CG2 . THR   B 33  ? 0.2170 0.1443 0.1742 -0.0103 -0.0514 0.0290  33   THR   B CG2 
4592 N  N   . VAL   B 34  ? 0.1720 0.1220 0.1260 -0.0312 -0.0418 0.0112  34   VAL   B N   
4593 C  CA  . VAL   B 34  ? 0.1550 0.1208 0.1201 -0.0276 -0.0343 0.0111  34   VAL   B CA  
4594 C  C   . VAL   B 34  ? 0.1414 0.1155 0.1104 -0.0299 -0.0178 0.0093  34   VAL   B C   
4595 O  O   . VAL   B 34  ? 0.1576 0.1171 0.1210 -0.0248 -0.0301 0.0074  34   VAL   B O   
4596 C  CB  . VAL   B 34  ? 0.1560 0.1292 0.1471 -0.0102 -0.0308 0.0033  34   VAL   B CB  
4597 C  CG1 . VAL   B 34  ? 0.1552 0.1419 0.1557 -0.0098 -0.0154 -0.0018 34   VAL   B CG1 
4598 C  CG2 . VAL   B 34  ? 0.1618 0.1353 0.1779 -0.0041 -0.0257 -0.0006 34   VAL   B CG2 
4608 N  N   . VAL   B 35  ? 0.1339 0.1119 0.1025 -0.0254 -0.0126 0.0075  35   VAL   B N   
4609 C  CA  . VAL   B 35  ? 0.1308 0.1089 0.1054 -0.0185 -0.0094 0.0072  35   VAL   B CA  
4610 C  C   . VAL   B 35  ? 0.1209 0.1085 0.1056 -0.0145 -0.0130 0.0033  35   VAL   B C   
4611 O  O   . VAL   B 35  ? 0.1245 0.1115 0.1170 -0.0213 -0.0024 -0.0037 35   VAL   B O   
4612 C  CB  . VAL   B 35  ? 0.1283 0.1269 0.1073 -0.0142 0.0065  0.0074  35   VAL   B CB  
4613 C  CG1 . VAL   B 35  ? 0.1205 0.1373 0.1310 -0.0173 0.0058  0.0005  35   VAL   B CG1 
4614 C  CG2 . VAL   B 35  ? 0.1336 0.1315 0.1274 -0.0055 0.0079  0.0035  35   VAL   B CG2 
4624 N  N   . VAL   B 36  ? 0.1247 0.1077 0.1030 -0.0133 -0.0130 0.0050  36   VAL   B N   
4625 C  CA  . VAL   B 36  ? 0.1200 0.1034 0.0940 -0.0106 -0.0029 0.0005  36   VAL   B CA  
4626 C  C   . VAL   B 36  ? 0.1175 0.1074 0.0902 -0.0112 0.0014  -0.0021 36   VAL   B C   
4627 O  O   . VAL   B 36  ? 0.1233 0.1133 0.1205 -0.0088 0.0006  -0.0065 36   VAL   B O   
4628 C  CB  . VAL   B 36  ? 0.1184 0.1111 0.1110 -0.0168 -0.0068 0.0048  36   VAL   B CB  
4629 C  CG1 . VAL   B 36  ? 0.1216 0.1228 0.1249 -0.0186 -0.0032 0.0103  36   VAL   B CG1 
4630 C  CG2 . VAL   B 36  ? 0.1214 0.1171 0.1289 -0.0122 -0.0079 0.0094  36   VAL   B CG2 
4640 N  N   . ASN   B 37  ? 0.1206 0.1115 0.0902 -0.0059 -0.0032 0.0002  37   ASN   B N   
4641 C  CA  . ASN   B 37  ? 0.1194 0.1098 0.1031 0.0006  -0.0101 0.0035  37   ASN   B CA  
4642 C  C   . ASN   B 37  ? 0.1193 0.1115 0.1015 0.0034  -0.0070 0.0002  37   ASN   B C   
4643 O  O   . ASN   B 37  ? 0.1296 0.1218 0.1039 0.0049  0.0037  0.0021  37   ASN   B O   
4644 C  CB  . ASN   B 37  ? 0.1208 0.1169 0.1034 0.0066  -0.0090 -0.0002 37   ASN   B CB  
4645 C  CG  . ASN   B 37  ? 0.1198 0.1192 0.1079 0.0024  -0.0081 -0.0005 37   ASN   B CG  
4646 O  OD1 . ASN   B 37  ? 0.1303 0.1237 0.1208 0.0089  -0.0094 -0.0027 37   ASN   B OD1 
4647 N  ND2 . ASN   B 37  ? 0.1244 0.1135 0.1230 0.0032  -0.0138 0.0062  37   ASN   B ND2 
4654 N  N   . ALA   B 38  ? 0.1276 0.1120 0.1017 0.0089  0.0035  0.0026  38   ALA   B N   
4655 C  CA  . ALA   B 38  ? 0.1346 0.1161 0.1047 0.0014  0.0100  0.0101  38   ALA   B CA  
4656 C  C   . ALA   B 38  ? 0.1258 0.1135 0.1085 -0.0015 0.0115  0.0102  38   ALA   B C   
4657 O  O   . ALA   B 38  ? 0.1381 0.1242 0.1228 0.0080  0.0061  0.0099  38   ALA   B O   
4658 C  CB  . ALA   B 38  ? 0.1510 0.1256 0.1247 -0.0097 0.0115  0.0057  38   ALA   B CB  
4664 N  N   . ALA   B 39  ? 0.1287 0.1165 0.1023 0.0065  -0.0017 0.0010  39   ALA   B N   
4665 C  CA  . ALA   B 39  ? 0.1353 0.1239 0.1015 0.0088  -0.0032 0.0012  39   ALA   B CA  
4666 C  C   . ALA   B 39  ? 0.1413 0.1273 0.0945 0.0078  -0.0010 0.0000  39   ALA   B C   
4667 O  O   . ALA   B 39  ? 0.1417 0.1330 0.1180 0.0030  0.0011  0.0073  39   ALA   B O   
4668 C  CB  . ALA   B 39  ? 0.1404 0.1310 0.1252 -0.0016 0.0056  0.0008  39   ALA   B CB  
4674 N  N   . ASN   B 40  ? 0.1454 0.1524 0.0970 -0.0061 0.0058  -0.0067 40   ASN   B N   
4675 C  CA  . ASN   B 40  ? 0.1504 0.1602 0.1120 0.0028  0.0004  -0.0084 40   ASN   B CA  
4676 C  C   . ASN   B 40  ? 0.1559 0.1601 0.0883 0.0081  -0.0034 -0.0026 40   ASN   B C   
4677 O  O   . ASN   B 40  ? 0.1556 0.1518 0.1000 0.0069  -0.0042 0.0047  40   ASN   B O   
4678 C  CB  . ASN   B 40  ? 0.1646 0.1588 0.1323 0.0113  -0.0100 0.0086  40   ASN   B CB  
4679 C  CG  . ASN   B 40  ? 0.1668 0.1612 0.1570 0.0033  -0.0211 0.0156  40   ASN   B CG  
4680 O  OD1 . ASN   B 40  ? 0.1671 0.1586 0.2412 0.0042  -0.0317 0.0179  40   ASN   B OD1 
4681 N  ND2 . ASN   B 40  ? 0.1712 0.1652 0.1610 0.0055  -0.0127 0.0118  40   ASN   B ND2 
4688 N  N   . VAL   B 41  ? 0.1640 0.1668 0.0880 0.0096  0.0084  0.0018  41   VAL   B N   
4689 C  CA  . VAL   B 41  ? 0.1684 0.1777 0.1045 0.0136  0.0034  -0.0111 41   VAL   B CA  
4690 C  C   . VAL   B 41  ? 0.1655 0.1765 0.0994 0.0193  -0.0029 -0.0116 41   VAL   B C   
4691 O  O   . VAL   B 41  ? 0.1637 0.1738 0.1144 0.0160  -0.0105 -0.0163 41   VAL   B O   
4692 C  CB  . VAL   B 41  ? 0.1804 0.1891 0.1282 -0.0021 0.0257  -0.0243 41   VAL   B CB  
4693 C  CG1 . VAL   B 41  ? 0.1761 0.1908 0.1517 -0.0028 0.0357  -0.0288 41   VAL   B CG1 
4694 C  CG2 . VAL   B 41  ? 0.1920 0.2066 0.1357 -0.0064 0.0254  -0.0177 41   VAL   B CG2 
4704 N  N   . TYR   B 42  ? 0.1712 0.1750 0.1099 0.0190  -0.0088 -0.0056 42   TYR   B N   
4705 C  CA  . TYR   B 42  ? 0.1799 0.1806 0.1158 0.0173  -0.0186 -0.0166 42   TYR   B CA  
4706 C  C   . TYR   B 42  ? 0.1616 0.1615 0.1228 0.0156  -0.0183 -0.0140 42   TYR   B C   
4707 O  O   . TYR   B 42  ? 0.1666 0.1633 0.1473 0.0152  -0.0246 -0.0269 42   TYR   B O   
4708 C  CB  . TYR   B 42  ? 0.2037 0.2114 0.1316 0.0124  -0.0251 -0.0086 42   TYR   B CB  
4709 C  CG  . TYR   B 42  ? 0.2089 0.2226 0.1270 0.0026  -0.0252 0.0060  42   TYR   B CG  
4710 C  CD1 . TYR   B 42  ? 0.2043 0.2202 0.0996 -0.0020 -0.0134 -0.0043 42   TYR   B CD1 
4711 C  CD2 . TYR   B 42  ? 0.2218 0.2345 0.1670 -0.0012 -0.0124 0.0107  42   TYR   B CD2 
4712 C  CE1 . TYR   B 42  ? 0.2211 0.2405 0.1024 0.0012  -0.0041 -0.0055 42   TYR   B CE1 
4713 C  CE2 . TYR   B 42  ? 0.2273 0.2466 0.1601 -0.0013 0.0093  0.0179  42   TYR   B CE2 
4714 C  CZ  . TYR   B 42  ? 0.2391 0.2579 0.1326 0.0111  0.0105  0.0048  42   TYR   B CZ  
4715 O  OH  . TYR   B 42  ? 0.2700 0.2850 0.1861 0.0255  0.0244  0.0054  42   TYR   B OH  
4725 N  N   . LEU   B 43  ? 0.1470 0.1452 0.1020 0.0070  -0.0137 -0.0158 43   LEU   B N   
4726 C  CA  . LEU   B 43  ? 0.1476 0.1428 0.1027 0.0047  -0.0080 -0.0049 43   LEU   B CA  
4727 C  C   . LEU   B 43  ? 0.1530 0.1465 0.1138 0.0075  -0.0140 -0.0019 43   LEU   B C   
4728 O  O   . LEU   B 43  ? 0.1519 0.1469 0.1409 0.0085  -0.0176 0.0039  43   LEU   B O   
4729 C  CB  . LEU   B 43  ? 0.1422 0.1361 0.1218 0.0004  -0.0165 -0.0110 43   LEU   B CB  
4730 C  CG  . LEU   B 43  ? 0.1515 0.1355 0.1246 0.0023  -0.0159 -0.0102 43   LEU   B CG  
4731 C  CD1 . LEU   B 43  ? 0.1618 0.1411 0.1596 -0.0033 -0.0402 -0.0128 43   LEU   B CD1 
4732 C  CD2 . LEU   B 43  ? 0.1465 0.1389 0.1304 -0.0040 -0.0218 -0.0079 43   LEU   B CD2 
4744 N  N   . LYS   B 44  ? 0.1511 0.1481 0.1098 0.0096  -0.0095 -0.0104 44   LYS   B N   
4745 C  CA  . LYS   B 44  ? 0.1640 0.1570 0.1132 0.0144  -0.0170 0.0040  44   LYS   B CA  
4746 C  C   . LYS   B 44  ? 0.1547 0.1448 0.1155 0.0147  -0.0102 0.0011  44   LYS   B C   
4747 O  O   . LYS   B 44  ? 0.1719 0.1440 0.1444 0.0057  0.0023  0.0009  44   LYS   B O   
4748 C  CB  . LYS   B 44  ? 0.1897 0.1847 0.1269 0.0149  -0.0270 -0.0010 44   LYS   B CB  
4749 C  CG  . LYS   B 44  ? 0.2180 0.2075 0.1662 0.0123  -0.0482 -0.0072 44   LYS   B CG  
4750 C  CD  . LYS   B 44  ? 0.2520 0.2262 0.2269 0.0022  -0.0551 -0.0132 44   LYS   B CD  
4751 C  CE  . LYS   B 44  ? 0.2835 0.2477 0.2715 -0.0024 -0.0590 -0.0011 44   LYS   B CE  
4752 N  NZ  . LYS   B 44  ? 0.2932 0.2570 0.3042 -0.0009 -0.0635 0.0077  44   LYS   B NZ  
4766 N  N   . HIS   B 45  ? 0.1484 0.1444 0.1191 0.0097  -0.0067 0.0082  45   HIS   B N   
4767 C  CA  . HIS   B 45  ? 0.1513 0.1450 0.1247 0.0108  -0.0050 -0.0043 45   HIS   B CA  
4768 C  C   . HIS   B 45  ? 0.1753 0.1637 0.1607 0.0154  -0.0137 -0.0019 45   HIS   B C   
4769 O  O   . HIS   B 45  ? 0.1818 0.1921 0.2060 0.0424  0.0124  0.0001  45   HIS   B O   
4770 C  CB  . HIS   B 45  ? 0.1425 0.1483 0.1230 -0.0007 -0.0057 -0.0017 45   HIS   B CB  
4771 C  CG  . HIS   B 45  ? 0.1438 0.1439 0.1210 -0.0007 -0.0051 -0.0041 45   HIS   B CG  
4772 N  ND1 . HIS   B 45  ? 0.1501 0.1382 0.1235 0.0037  -0.0155 -0.0063 45   HIS   B ND1 
4773 C  CD2 . HIS   B 45  ? 0.1545 0.1460 0.1310 -0.0063 -0.0077 -0.0015 45   HIS   B CD2 
4774 C  CE1 . HIS   B 45  ? 0.1565 0.1276 0.1122 -0.0002 -0.0184 -0.0087 45   HIS   B CE1 
4775 N  NE2 . HIS   B 45  ? 0.1585 0.1364 0.1214 -0.0007 -0.0145 -0.0030 45   HIS   B NE2 
4783 N  N   A GLY   B 46  ? 0.1832 0.1611 0.1850 0.0173  -0.0289 0.0056  46   GLY   B N   
4784 N  N   B GLY   B 46  ? 0.1848 0.1650 0.1737 0.0182  -0.0295 0.0113  46   GLY   B N   
4785 C  CA  A GLY   B 46  ? 0.1943 0.1700 0.2236 0.0164  -0.0282 0.0053  46   GLY   B CA  
4786 C  CA  B GLY   B 46  ? 0.1971 0.1764 0.2022 0.0172  -0.0302 0.0144  46   GLY   B CA  
4787 C  C   A GLY   B 46  ? 0.1976 0.1827 0.2619 0.0219  -0.0240 0.0025  46   GLY   B C   
4788 C  C   B GLY   B 46  ? 0.2027 0.1907 0.2361 0.0217  -0.0278 0.0159  46   GLY   B C   
4789 O  O   A GLY   B 46  ? 0.1996 0.1908 0.3204 0.0243  -0.0110 -0.0144 46   GLY   B O   
4790 O  O   B GLY   B 46  ? 0.2094 0.2038 0.2582 0.0243  -0.0243 0.0216  46   GLY   B O   
4797 N  N   . GLY   B 47  ? 0.1986 0.1926 0.2434 0.0113  -0.0113 -0.0005 47   GLY   B N   
4798 C  CA  . GLY   B 47  ? 0.1857 0.1668 0.2040 0.0020  -0.0119 0.0041  47   GLY   B CA  
4799 C  C   . GLY   B 47  ? 0.1678 0.1465 0.1662 0.0044  0.0003  0.0065  47   GLY   B C   
4800 O  O   . GLY   B 47  ? 0.1748 0.1369 0.1700 0.0035  -0.0045 0.0108  47   GLY   B O   
4805 N  N   . GLY   B 48  ? 0.1486 0.1344 0.1597 0.0063  -0.0063 0.0170  48   GLY   B N   
4806 C  CA  . GLY   B 48  ? 0.1495 0.1306 0.1515 0.0030  -0.0046 0.0095  48   GLY   B CA  
4807 C  C   . GLY   B 48  ? 0.1410 0.1246 0.1419 0.0044  0.0043  -0.0010 48   GLY   B C   
4808 O  O   . GLY   B 48  ? 0.1395 0.1287 0.1640 0.0018  -0.0061 0.0026  48   GLY   B O   
4812 N  N   . VAL   B 49  ? 0.1418 0.1305 0.1377 0.0086  0.0011  0.0054  49   VAL   B N   
4813 C  CA  . VAL   B 49  ? 0.1447 0.1370 0.1305 0.0085  -0.0122 -0.0079 49   VAL   B CA  
4814 C  C   . VAL   B 49  ? 0.1365 0.1306 0.1131 0.0111  -0.0035 0.0076  49   VAL   B C   
4815 O  O   . VAL   B 49  ? 0.1396 0.1376 0.1278 0.0045  -0.0057 0.0081  49   VAL   B O   
4816 C  CB  . VAL   B 49  ? 0.1432 0.1566 0.1540 0.0038  -0.0213 -0.0037 49   VAL   B CB  
4817 C  CG1 . VAL   B 49  ? 0.1418 0.1599 0.1438 0.0056  -0.0256 0.0058  49   VAL   B CG1 
4818 C  CG2 . VAL   B 49  ? 0.1604 0.1746 0.1818 -0.0109 -0.0355 -0.0023 49   VAL   B CG2 
4828 N  N   . ALA   B 50  ? 0.1305 0.1269 0.1176 0.0048  -0.0003 0.0053  50   ALA   B N   
4829 C  CA  . ALA   B 50  ? 0.1292 0.1198 0.1187 0.0084  -0.0025 0.0065  50   ALA   B CA  
4830 C  C   . ALA   B 50  ? 0.1328 0.1266 0.1223 0.0054  -0.0061 0.0056  50   ALA   B C   
4831 O  O   . ALA   B 50  ? 0.1341 0.1277 0.1229 0.0051  -0.0011 -0.0024 50   ALA   B O   
4832 C  CB  . ALA   B 50  ? 0.1315 0.1222 0.1233 -0.0019 0.0004  0.0085  50   ALA   B CB  
4838 N  N   . GLY   B 51  ? 0.1315 0.1347 0.1244 0.0134  -0.0101 0.0071  51   GLY   B N   
4839 C  CA  . GLY   B 51  ? 0.1369 0.1406 0.1506 0.0178  -0.0121 0.0097  51   GLY   B CA  
4840 C  C   . GLY   B 51  ? 0.1343 0.1323 0.1475 0.0219  -0.0039 0.0073  51   GLY   B C   
4841 O  O   . GLY   B 51  ? 0.1374 0.1446 0.1661 0.0111  -0.0083 -0.0001 51   GLY   B O   
4845 N  N   . ALA   B 52  ? 0.1361 0.1293 0.1412 0.0193  -0.0046 0.0080  52   ALA   B N   
4846 C  CA  . ALA   B 52  ? 0.1363 0.1352 0.1439 0.0234  -0.0021 -0.0033 52   ALA   B CA  
4847 C  C   . ALA   B 52  ? 0.1302 0.1334 0.1300 0.0085  0.0017  -0.0023 52   ALA   B C   
4848 O  O   . ALA   B 52  ? 0.1391 0.1362 0.1473 0.0132  0.0051  0.0040  52   ALA   B O   
4849 C  CB  . ALA   B 52  ? 0.1592 0.1371 0.1493 0.0077  0.0125  -0.0009 52   ALA   B CB  
4855 N  N   . LEU   B 53  ? 0.1271 0.1301 0.1326 0.0138  0.0014  0.0024  53   LEU   B N   
4856 C  CA  . LEU   B 53  ? 0.1270 0.1420 0.1239 0.0128  0.0018  0.0022  53   LEU   B CA  
4857 C  C   . LEU   B 53  ? 0.1324 0.1344 0.1254 0.0122  0.0095  0.0070  53   LEU   B C   
4858 O  O   . LEU   B 53  ? 0.1397 0.1402 0.1393 0.0016  0.0069  0.0173  53   LEU   B O   
4859 C  CB  . LEU   B 53  ? 0.1292 0.1441 0.1284 0.0106  0.0040  0.0125  53   LEU   B CB  
4860 C  CG  . LEU   B 53  ? 0.1251 0.1561 0.1373 0.0046  0.0054  0.0220  53   LEU   B CG  
4861 C  CD1 . LEU   B 53  ? 0.1378 0.1801 0.1626 0.0124  0.0044  0.0085  53   LEU   B CD1 
4862 C  CD2 . LEU   B 53  ? 0.1395 0.1853 0.1664 -0.0091 -0.0118 -0.0143 53   LEU   B CD2 
4874 N  N   . ASN   B 54  ? 0.1294 0.1254 0.1225 0.0080  0.0087  0.0041  54   ASN   B N   
4875 C  CA  . ASN   B 54  ? 0.1365 0.1379 0.1356 0.0064  0.0001  -0.0053 54   ASN   B CA  
4876 C  C   . ASN   B 54  ? 0.1310 0.1404 0.1478 0.0033  0.0040  0.0051  54   ASN   B C   
4877 O  O   . ASN   B 54  ? 0.1312 0.1423 0.1624 -0.0007 0.0047  0.0015  54   ASN   B O   
4878 C  CB  . ASN   B 54  ? 0.1393 0.1456 0.1389 0.0052  0.0046  -0.0064 54   ASN   B CB  
4879 C  CG  . ASN   B 54  ? 0.1371 0.1554 0.1388 0.0021  -0.0044 -0.0007 54   ASN   B CG  
4880 O  OD1 . ASN   B 54  ? 0.1311 0.1585 0.1526 -0.0020 -0.0067 -0.0166 54   ASN   B OD1 
4881 N  ND2 . ASN   B 54  ? 0.1513 0.1759 0.1690 -0.0016 -0.0247 0.0135  54   ASN   B ND2 
4888 N  N   . LYS   B 55  ? 0.1328 0.1471 0.1650 0.0131  0.0064  0.0071  55   LYS   B N   
4889 C  CA  . LYS   B 55  ? 0.1384 0.1565 0.1807 0.0236  -0.0017 0.0006  55   LYS   B CA  
4890 C  C   . LYS   B 55  ? 0.1297 0.1515 0.1742 0.0140  0.0055  -0.0071 55   LYS   B C   
4891 O  O   . LYS   B 55  ? 0.1303 0.1687 0.1964 0.0072  0.0102  -0.0084 55   LYS   B O   
4892 C  CB  . LYS   B 55  ? 0.1486 0.1611 0.2197 0.0275  0.0113  0.0033  55   LYS   B CB  
4893 C  CG  . LYS   B 55  ? 0.1879 0.1917 0.3089 0.0344  0.0348  0.0210  55   LYS   B CG  
4894 C  CD  . LYS   B 55  ? 0.2243 0.2173 0.3889 0.0402  0.0534  0.0298  55   LYS   B CD  
4895 C  CE  . LYS   B 55  ? 0.2510 0.2357 0.4549 0.0425  0.0641  0.0329  55   LYS   B CE  
4896 N  NZ  . LYS   B 55  ? 0.2567 0.2485 0.4900 0.0416  0.0564  0.0393  55   LYS   B NZ  
4910 N  N   . ALA   B 56  ? 0.1275 0.1598 0.1555 0.0108  0.0048  -0.0147 56   ALA   B N   
4911 C  CA  . ALA   B 56  ? 0.1472 0.1735 0.1518 0.0029  0.0084  -0.0060 56   ALA   B CA  
4912 C  C   . ALA   B 56  ? 0.1457 0.1706 0.1537 0.0025  0.0149  0.0015  56   ALA   B C   
4913 O  O   . ALA   B 56  ? 0.1611 0.1832 0.1734 0.0047  0.0322  0.0048  56   ALA   B O   
4914 C  CB  . ALA   B 56  ? 0.1670 0.1922 0.1575 -0.0123 0.0058  -0.0103 56   ALA   B CB  
4920 N  N   . THR   B 57  ? 0.1427 0.1611 0.1576 0.0069  0.0249  0.0014  57   THR   B N   
4921 C  CA  . THR   B 57  ? 0.1456 0.1588 0.1627 0.0020  0.0285  0.0077  57   THR   B CA  
4922 C  C   . THR   B 57  ? 0.1498 0.1673 0.1815 -0.0003 0.0288  0.0060  57   THR   B C   
4923 O  O   . THR   B 57  ? 0.1575 0.1630 0.1920 -0.0093 0.0231  0.0079  57   THR   B O   
4924 C  CB  . THR   B 57  ? 0.1509 0.1491 0.1458 -0.0019 0.0219  0.0200  57   THR   B CB  
4925 O  OG1 . THR   B 57  ? 0.1453 0.1453 0.1569 -0.0017 0.0223  0.0110  57   THR   B OG1 
4926 C  CG2 . THR   B 57  ? 0.1458 0.1485 0.1532 -0.0023 0.0225  0.0141  57   THR   B CG2 
4934 N  N   . ASN   B 58  ? 0.1298 0.1861 0.1969 -0.0131 0.0160  -0.0123 58   ASN   B N   
4935 C  CA  . ASN   B 58  ? 0.1494 0.2283 0.2420 -0.0205 0.0409  -0.0130 58   ASN   B CA  
4936 C  C   . ASN   B 58  ? 0.1314 0.2054 0.2020 -0.0103 0.0128  -0.0096 58   ASN   B C   
4937 O  O   . ASN   B 58  ? 0.1404 0.2150 0.2108 -0.0120 0.0106  -0.0170 58   ASN   B O   
4938 C  CB  . ASN   B 58  ? 0.2332 0.2978 0.3600 -0.0348 0.0779  -0.0063 58   ASN   B CB  
4939 C  CG  . ASN   B 58  ? 0.3234 0.3571 0.5042 -0.0415 0.0884  0.0209  58   ASN   B CG  
4940 O  OD1 . ASN   B 58  ? 0.3464 0.3750 0.5562 -0.0434 0.0888  0.0282  58   ASN   B OD1 
4941 N  ND2 . ASN   B 58  ? 0.3898 0.3898 0.5545 -0.0453 0.0935  0.0283  58   ASN   B ND2 
4948 N  N   . ASN   B 59  ? 0.1347 0.1901 0.1781 -0.0051 0.0083  0.0022  59   ASN   B N   
4949 C  CA  . ASN   B 59  ? 0.1345 0.1899 0.1806 -0.0072 -0.0055 0.0090  59   ASN   B CA  
4950 C  C   . ASN   B 59  ? 0.1308 0.1805 0.1614 -0.0100 -0.0117 -0.0037 59   ASN   B C   
4951 O  O   . ASN   B 59  ? 0.1406 0.1781 0.1642 -0.0133 -0.0086 -0.0035 59   ASN   B O   
4952 C  CB  . ASN   B 59  ? 0.1435 0.2079 0.1936 -0.0032 -0.0226 0.0087  59   ASN   B CB  
4953 C  CG  . ASN   B 59  ? 0.1550 0.2200 0.2038 0.0003  -0.0287 0.0103  59   ASN   B CG  
4954 O  OD1 . ASN   B 59  ? 0.1581 0.2288 0.2058 0.0028  -0.0201 0.0251  59   ASN   B OD1 
4955 N  ND2 . ASN   B 59  ? 0.1651 0.2261 0.2086 -0.0082 -0.0221 0.0015  59   ASN   B ND2 
4962 N  N   . ALA   B 60  ? 0.1353 0.1706 0.1630 -0.0055 0.0020  -0.0056 60   ALA   B N   
4963 C  CA  . ALA   B 60  ? 0.1427 0.1556 0.1698 -0.0180 0.0012  0.0017  60   ALA   B CA  
4964 C  C   . ALA   B 60  ? 0.1422 0.1432 0.1523 -0.0087 -0.0028 0.0066  60   ALA   B C   
4965 O  O   . ALA   B 60  ? 0.1475 0.1470 0.1659 -0.0136 0.0019  -0.0047 60   ALA   B O   
4966 C  CB  . ALA   B 60  ? 0.1571 0.1550 0.1883 -0.0126 0.0043  0.0034  60   ALA   B CB  
4972 N  N   . MET   B 61  ? 0.1320 0.1371 0.1556 -0.0061 0.0010  0.0042  61   MET   B N   
4973 C  CA  . MET   B 61  ? 0.1334 0.1360 0.1508 -0.0085 -0.0059 0.0029  61   MET   B CA  
4974 C  C   . MET   B 61  ? 0.1395 0.1344 0.1439 -0.0104 -0.0071 0.0034  61   MET   B C   
4975 O  O   . MET   B 61  ? 0.1431 0.1374 0.1371 -0.0024 -0.0022 -0.0138 61   MET   B O   
4976 C  CB  . MET   B 61  ? 0.1279 0.1360 0.1400 -0.0012 -0.0017 -0.0013 61   MET   B CB  
4977 C  CG  . MET   B 61  ? 0.1287 0.1419 0.1302 -0.0012 -0.0018 0.0026  61   MET   B CG  
4978 S  SD  . MET   B 61  ? 0.1313 0.1388 0.1541 -0.0013 -0.0005 -0.0078 61   MET   B SD  
4979 C  CE  . MET   B 61  ? 0.1346 0.1564 0.1802 -0.0030 -0.0015 -0.0195 61   MET   B CE  
4989 N  N   . GLN   B 62  ? 0.1367 0.1377 0.1353 -0.0041 -0.0099 0.0044  62   GLN   B N   
4990 C  CA  . GLN   B 62  ? 0.1400 0.1438 0.1382 -0.0036 -0.0131 -0.0016 62   GLN   B CA  
4991 C  C   . GLN   B 62  ? 0.1364 0.1514 0.1456 0.0002  -0.0220 -0.0141 62   GLN   B C   
4992 O  O   . GLN   B 62  ? 0.1520 0.1519 0.1442 0.0016  -0.0193 -0.0160 62   GLN   B O   
4993 C  CB  . GLN   B 62  ? 0.1398 0.1471 0.1452 0.0019  -0.0102 0.0004  62   GLN   B CB  
4994 C  CG  . GLN   B 62  ? 0.1437 0.1532 0.1423 0.0005  -0.0207 -0.0033 62   GLN   B CG  
4995 C  CD  . GLN   B 62  ? 0.1413 0.1498 0.1298 0.0034  -0.0240 0.0041  62   GLN   B CD  
4996 O  OE1 . GLN   B 62  ? 0.1496 0.1490 0.1509 0.0026  -0.0234 -0.0055 62   GLN   B OE1 
4997 N  NE2 . GLN   B 62  ? 0.1491 0.1617 0.1440 -0.0008 -0.0217 -0.0140 62   GLN   B NE2 
5006 N  N   . VAL   B 63  ? 0.1323 0.1575 0.1682 -0.0098 -0.0187 -0.0154 63   VAL   B N   
5007 C  CA  . VAL   B 63  ? 0.1428 0.1599 0.1831 -0.0138 -0.0258 -0.0140 63   VAL   B CA  
5008 C  C   . VAL   B 63  ? 0.1453 0.1486 0.1662 -0.0164 -0.0239 -0.0168 63   VAL   B C   
5009 O  O   . VAL   B 63  ? 0.1547 0.1480 0.1785 -0.0126 -0.0334 -0.0137 63   VAL   B O   
5010 C  CB  . VAL   B 63  ? 0.1449 0.1719 0.2228 -0.0199 -0.0248 -0.0115 63   VAL   B CB  
5011 C  CG1 . VAL   B 63  ? 0.1552 0.1741 0.2368 -0.0299 -0.0173 -0.0090 63   VAL   B CG1 
5012 C  CG2 . VAL   B 63  ? 0.1448 0.1874 0.2439 -0.0161 -0.0305 -0.0121 63   VAL   B CG2 
5022 N  N   . GLU   B 64  ? 0.1473 0.1402 0.1613 -0.0078 -0.0209 -0.0115 64   GLU   B N   
5023 C  CA  . GLU   B 64  ? 0.1487 0.1337 0.1456 -0.0080 -0.0276 -0.0088 64   GLU   B CA  
5024 C  C   . GLU   B 64  ? 0.1455 0.1364 0.1357 -0.0020 -0.0271 -0.0151 64   GLU   B C   
5025 O  O   . GLU   B 64  ? 0.1554 0.1449 0.1445 -0.0093 -0.0248 -0.0177 64   GLU   B O   
5026 C  CB  . GLU   B 64  ? 0.1481 0.1399 0.1493 -0.0114 -0.0241 -0.0063 64   GLU   B CB  
5027 C  CG  . GLU   B 64  ? 0.1507 0.1449 0.1489 -0.0229 -0.0248 -0.0133 64   GLU   B CG  
5028 C  CD  . GLU   B 64  ? 0.1523 0.1594 0.1517 -0.0262 -0.0226 -0.0068 64   GLU   B CD  
5029 O  OE1 . GLU   B 64  ? 0.1621 0.1744 0.1669 -0.0331 -0.0172 -0.0294 64   GLU   B OE1 
5030 O  OE2 . GLU   B 64  ? 0.1683 0.1676 0.1670 -0.0263 -0.0374 -0.0118 64   GLU   B OE2 
5037 N  N   . SER   B 65  ? 0.1447 0.1345 0.1350 -0.0060 -0.0120 -0.0162 65   SER   B N   
5038 C  CA  . SER   B 65  ? 0.1429 0.1328 0.1399 -0.0031 -0.0114 -0.0150 65   SER   B CA  
5039 C  C   . SER   B 65  ? 0.1436 0.1321 0.1358 0.0015  -0.0167 -0.0162 65   SER   B C   
5040 O  O   . SER   B 65  ? 0.1522 0.1420 0.1372 0.0019  -0.0198 -0.0247 65   SER   B O   
5041 C  CB  . SER   B 65  ? 0.1424 0.1397 0.1415 -0.0111 -0.0168 -0.0119 65   SER   B CB  
5042 O  OG  . SER   B 65  ? 0.1443 0.1420 0.1401 -0.0088 -0.0159 -0.0201 65   SER   B OG  
5048 N  N   . ASP   B 66  ? 0.1567 0.1425 0.1315 0.0015  -0.0227 -0.0161 66   ASP   B N   
5049 C  CA  . ASP   B 66  ? 0.1630 0.1489 0.1313 0.0062  -0.0269 -0.0132 66   ASP   B CA  
5050 C  C   . ASP   B 66  ? 0.1651 0.1564 0.1294 -0.0000 -0.0270 -0.0202 66   ASP   B C   
5051 O  O   . ASP   B 66  ? 0.1675 0.1618 0.1405 0.0051  -0.0289 -0.0222 66   ASP   B O   
5052 C  CB  . ASP   B 66  ? 0.1755 0.1635 0.1592 0.0116  -0.0384 -0.0166 66   ASP   B CB  
5053 C  CG  . ASP   B 66  ? 0.2021 0.1779 0.1833 0.0236  -0.0513 -0.0088 66   ASP   B CG  
5054 O  OD1 . ASP   B 66  ? 0.2238 0.1715 0.1850 0.0157  -0.0475 -0.0063 66   ASP   B OD1 
5055 O  OD2 . ASP   B 66  ? 0.2174 0.1985 0.2399 0.0434  -0.0473 -0.0067 66   ASP   B OD2 
5060 N  N   . ASP   B 67  ? 0.1600 0.1457 0.1400 -0.0062 -0.0259 -0.0227 67   ASP   B N   
5061 C  CA  . ASP   B 67  ? 0.1737 0.1433 0.1483 -0.0086 -0.0235 -0.0213 67   ASP   B CA  
5062 C  C   . ASP   B 67  ? 0.1716 0.1445 0.1532 0.0035  -0.0251 -0.0216 67   ASP   B C   
5063 O  O   . ASP   B 67  ? 0.1758 0.1497 0.1660 -0.0009 -0.0176 -0.0250 67   ASP   B O   
5064 C  CB  . ASP   B 67  ? 0.1966 0.1506 0.1617 -0.0120 -0.0376 -0.0171 67   ASP   B CB  
5065 C  CG  . ASP   B 67  ? 0.2293 0.1609 0.1739 -0.0057 -0.0608 -0.0188 67   ASP   B CG  
5066 O  OD1 . ASP   B 67  ? 0.2493 0.1670 0.1908 -0.0122 -0.0605 -0.0124 67   ASP   B OD1 
5067 O  OD2 . ASP   B 67  ? 0.2439 0.1672 0.1971 0.0098  -0.0678 -0.0127 67   ASP   B OD2 
5072 N  N   . TYR   B 68  ? 0.1627 0.1458 0.1441 0.0014  -0.0344 -0.0249 68   TYR   B N   
5073 C  CA  . TYR   B 68  ? 0.1582 0.1617 0.1550 0.0055  -0.0338 -0.0299 68   TYR   B CA  
5074 C  C   . TYR   B 68  ? 0.1503 0.1560 0.1536 0.0052  -0.0327 -0.0369 68   TYR   B C   
5075 O  O   . TYR   B 68  ? 0.1598 0.1649 0.1574 0.0096  -0.0318 -0.0459 68   TYR   B O   
5076 C  CB  . TYR   B 68  ? 0.1631 0.1824 0.1617 0.0084  -0.0350 -0.0394 68   TYR   B CB  
5077 C  CG  . TYR   B 68  ? 0.1748 0.1942 0.1717 0.0187  -0.0307 -0.0613 68   TYR   B CG  
5078 C  CD1 . TYR   B 68  ? 0.1765 0.2009 0.1949 0.0051  -0.0271 -0.0714 68   TYR   B CD1 
5079 C  CD2 . TYR   B 68  ? 0.1831 0.2089 0.1817 0.0254  -0.0440 -0.0574 68   TYR   B CD2 
5080 C  CE1 . TYR   B 68  ? 0.1836 0.2125 0.2151 0.0056  -0.0332 -0.0695 68   TYR   B CE1 
5081 C  CE2 . TYR   B 68  ? 0.1860 0.2154 0.1905 0.0234  -0.0385 -0.0711 68   TYR   B CE2 
5082 C  CZ  . TYR   B 68  ? 0.1812 0.2164 0.2115 0.0121  -0.0348 -0.0698 68   TYR   B CZ  
5083 O  OH  . TYR   B 68  ? 0.1750 0.2307 0.2315 0.0102  -0.0303 -0.0449 68   TYR   B OH  
5093 N  N   . ILE   B 69  ? 0.1535 0.1493 0.1576 0.0060  -0.0290 -0.0382 69   ILE   B N   
5094 C  CA  . ILE   B 69  ? 0.1622 0.1563 0.1639 -0.0005 -0.0212 -0.0389 69   ILE   B CA  
5095 C  C   . ILE   B 69  ? 0.1587 0.1523 0.1475 0.0070  -0.0343 -0.0327 69   ILE   B C   
5096 O  O   . ILE   B 69  ? 0.1619 0.1599 0.1582 0.0043  -0.0231 -0.0406 69   ILE   B O   
5097 C  CB  . ILE   B 69  ? 0.1673 0.1585 0.1898 -0.0002 0.0006  -0.0398 69   ILE   B CB  
5098 C  CG1 . ILE   B 69  ? 0.1662 0.1632 0.1992 -0.0062 0.0066  -0.0440 69   ILE   B CG1 
5099 C  CG2 . ILE   B 69  ? 0.1811 0.1661 0.2111 -0.0021 0.0002  -0.0272 69   ILE   B CG2 
5100 C  CD1 . ILE   B 69  ? 0.1610 0.1688 0.2031 -0.0164 0.0080  -0.0456 69   ILE   B CD1 
5112 N  N   . ALA   B 70  ? 0.1571 0.1536 0.1517 0.0054  -0.0418 -0.0316 70   ALA   B N   
5113 C  CA  . ALA   B 70  ? 0.1656 0.1545 0.1421 0.0032  -0.0407 -0.0245 70   ALA   B CA  
5114 C  C   . ALA   B 70  ? 0.1712 0.1502 0.1471 -0.0002 -0.0432 -0.0369 70   ALA   B C   
5115 O  O   . ALA   B 70  ? 0.1802 0.1512 0.1575 0.0023  -0.0354 -0.0384 70   ALA   B O   
5116 C  CB  . ALA   B 70  ? 0.1654 0.1682 0.1575 0.0017  -0.0429 -0.0260 70   ALA   B CB  
5122 N  N   . THR   B 71  ? 0.1764 0.1545 0.1580 0.0104  -0.0451 -0.0364 71   THR   B N   
5123 C  CA  . THR   B 71  ? 0.1906 0.1589 0.1810 0.0129  -0.0613 -0.0377 71   THR   B CA  
5124 C  C   . THR   B 71  ? 0.1851 0.1601 0.1979 0.0297  -0.0607 -0.0503 71   THR   B C   
5125 O  O   . THR   B 71  ? 0.1964 0.1684 0.2452 0.0279  -0.0526 -0.0663 71   THR   B O   
5126 C  CB  . THR   B 71  ? 0.2119 0.1847 0.2125 0.0033  -0.0643 -0.0170 71   THR   B CB  
5127 O  OG1 . THR   B 71  ? 0.2271 0.2145 0.2373 -0.0158 -0.0607 0.0063  71   THR   B OG1 
5128 C  CG2 . THR   B 71  ? 0.2247 0.1835 0.2425 0.0112  -0.0583 -0.0093 71   THR   B CG2 
5136 N  N   . ASN   B 72  ? 0.1720 0.1690 0.1945 0.0206  -0.0570 -0.0719 72   ASN   B N   
5137 C  CA  . ASN   B 72  ? 0.1703 0.1832 0.2034 0.0217  -0.0483 -0.0765 72   ASN   B CA  
5138 C  C   . ASN   B 72  ? 0.1715 0.1971 0.2100 0.0058  -0.0278 -0.0698 72   ASN   B C   
5139 O  O   . ASN   B 72  ? 0.1730 0.2127 0.2376 0.0060  -0.0131 -0.0722 72   ASN   B O   
5140 C  CB  . ASN   B 72  ? 0.1812 0.2007 0.2105 0.0195  -0.0584 -0.0692 72   ASN   B CB  
5141 C  CG  . ASN   B 72  ? 0.1947 0.2120 0.2228 0.0348  -0.0608 -0.0442 72   ASN   B CG  
5142 O  OD1 . ASN   B 72  ? 0.2192 0.2267 0.2351 0.0233  -0.0397 -0.0507 72   ASN   B OD1 
5143 N  ND2 . ASN   B 72  ? 0.2039 0.2226 0.2639 0.0453  -0.0437 -0.0101 72   ASN   B ND2 
5150 N  N   . GLY   B 73  ? 0.1752 0.1950 0.1849 -0.0031 -0.0294 -0.0668 73   GLY   B N   
5151 C  CA  . GLY   B 73  ? 0.1673 0.2006 0.1563 -0.0028 -0.0206 -0.0564 73   GLY   B CA  
5152 C  C   . GLY   B 73  ? 0.1628 0.2014 0.1196 0.0061  -0.0128 -0.0463 73   GLY   B C   
5153 O  O   . GLY   B 73  ? 0.1589 0.1870 0.1358 0.0075  -0.0181 -0.0356 73   GLY   B O   
5157 N  N   . PRO   B 74  ? 0.1662 0.2113 0.1203 0.0067  -0.0226 -0.0453 74   PRO   B N   
5158 C  CA  . PRO   B 74  ? 0.1604 0.2141 0.1058 0.0042  -0.0165 -0.0314 74   PRO   B CA  
5159 C  C   . PRO   B 74  ? 0.1467 0.1939 0.1204 0.0057  -0.0143 -0.0280 74   PRO   B C   
5160 O  O   . PRO   B 74  ? 0.1502 0.1972 0.1591 0.0078  -0.0137 -0.0379 74   PRO   B O   
5161 C  CB  . PRO   B 74  ? 0.1764 0.2343 0.1116 -0.0018 -0.0168 -0.0285 74   PRO   B CB  
5162 C  CG  . PRO   B 74  ? 0.1975 0.2429 0.1468 0.0020  -0.0124 -0.0233 74   PRO   B CG  
5163 C  CD  . PRO   B 74  ? 0.1926 0.2332 0.1320 0.0058  -0.0105 -0.0345 74   PRO   B CD  
5171 N  N   . LEU   B 75  ? 0.1454 0.1783 0.1181 0.0089  -0.0173 -0.0241 75   LEU   B N   
5172 C  CA  . LEU   B 75  ? 0.1459 0.1731 0.1152 0.0057  -0.0156 -0.0137 75   LEU   B CA  
5173 C  C   . LEU   B 75  ? 0.1506 0.1821 0.1181 0.0086  -0.0083 -0.0128 75   LEU   B C   
5174 O  O   . LEU   B 75  ? 0.1705 0.1951 0.1251 0.0002  -0.0058 -0.0003 75   LEU   B O   
5175 C  CB  . LEU   B 75  ? 0.1551 0.1753 0.1049 -0.0016 -0.0223 -0.0008 75   LEU   B CB  
5176 C  CG  . LEU   B 75  ? 0.1854 0.1915 0.1342 -0.0254 -0.0089 -0.0070 75   LEU   B CG  
5177 C  CD1 . LEU   B 75  ? 0.2171 0.2048 0.1427 -0.0363 0.0136  -0.0072 75   LEU   B CD1 
5178 C  CD2 . LEU   B 75  ? 0.2194 0.2094 0.1972 -0.0160 0.0003  -0.0049 75   LEU   B CD2 
5190 N  N   . LYS   B 76  ? 0.1532 0.2030 0.1440 0.0034  0.0019  -0.0056 76   LYS   B N   
5191 C  CA  . LYS   B 76  ? 0.1591 0.2093 0.1648 0.0047  0.0234  -0.0061 76   LYS   B CA  
5192 C  C   . LYS   B 76  ? 0.1580 0.1947 0.1368 0.0130  0.0108  0.0116  76   LYS   B C   
5193 O  O   . LYS   B 76  ? 0.1575 0.1766 0.1372 0.0044  0.0077  0.0135  76   LYS   B O   
5194 C  CB  . LYS   B 76  ? 0.1781 0.2207 0.2478 -0.0042 0.0402  -0.0387 76   LYS   B CB  
5195 C  CG  . LYS   B 76  ? 0.1920 0.2406 0.3094 0.0061  0.0302  -0.0559 76   LYS   B CG  
5196 C  CD  . LYS   B 76  ? 0.1928 0.2521 0.3653 0.0203  0.0179  -0.0752 76   LYS   B CD  
5197 C  CE  . LYS   B 76  ? 0.2014 0.2675 0.4232 0.0243  0.0030  -0.0854 76   LYS   B CE  
5198 N  NZ  . LYS   B 76  ? 0.2005 0.2719 0.4509 0.0239  -0.0116 -0.1002 76   LYS   B NZ  
5212 N  N   . VAL   B 77  ? 0.1625 0.2054 0.1403 0.0204  0.0152  0.0159  77   VAL   B N   
5213 C  CA  . VAL   B 77  ? 0.1651 0.1929 0.1524 0.0241  0.0246  0.0410  77   VAL   B CA  
5214 C  C   . VAL   B 77  ? 0.1498 0.1717 0.1426 0.0234  0.0230  0.0274  77   VAL   B C   
5215 O  O   . VAL   B 77  ? 0.1566 0.1726 0.1444 0.0282  0.0293  0.0232  77   VAL   B O   
5216 C  CB  . VAL   B 77  ? 0.1759 0.1980 0.1793 0.0232  0.0324  0.0617  77   VAL   B CB  
5217 C  CG1 . VAL   B 77  ? 0.1830 0.1877 0.2149 0.0092  0.0301  0.0708  77   VAL   B CG1 
5218 C  CG2 . VAL   B 77  ? 0.1891 0.2190 0.2038 0.0232  0.0098  0.0697  77   VAL   B CG2 
5228 N  N   . GLY   B 78  ? 0.1470 0.1614 0.1376 0.0181  0.0160  0.0222  78   GLY   B N   
5229 C  CA  . GLY   B 78  ? 0.1440 0.1568 0.1345 0.0110  0.0253  0.0133  78   GLY   B CA  
5230 C  C   . GLY   B 78  ? 0.1416 0.1486 0.1258 0.0092  0.0197  0.0179  78   GLY   B C   
5231 O  O   . GLY   B 78  ? 0.1475 0.1450 0.1376 0.0128  0.0164  0.0192  78   GLY   B O   
5235 N  N   . GLY   B 79  ? 0.1342 0.1532 0.1340 0.0122  0.0152  0.0147  79   GLY   B N   
5236 C  CA  . GLY   B 79  ? 0.1337 0.1469 0.1254 0.0131  0.0057  0.0040  79   GLY   B CA  
5237 C  C   . GLY   B 79  ? 0.1241 0.1381 0.1171 0.0138  0.0080  -0.0040 79   GLY   B C   
5238 O  O   . GLY   B 79  ? 0.1359 0.1389 0.1348 0.0167  0.0164  0.0138  79   GLY   B O   
5242 N  N   . SER   B 80  ? 0.1306 0.1299 0.1306 0.0057  0.0214  -0.0039 80   SER   B N   
5243 C  CA  . SER   B 80  ? 0.1266 0.1285 0.1314 0.0050  0.0089  -0.0059 80   SER   B CA  
5244 C  C   . SER   B 80  ? 0.1286 0.1277 0.1235 0.0056  0.0005  -0.0061 80   SER   B C   
5245 O  O   . SER   B 80  ? 0.1415 0.1312 0.1548 0.0093  0.0065  -0.0136 80   SER   B O   
5246 C  CB  . SER   B 80  ? 0.1383 0.1320 0.1363 -0.0024 0.0067  0.0018  80   SER   B CB  
5247 O  OG  . SER   B 80  ? 0.1423 0.1433 0.1597 0.0026  -0.0093 0.0132  80   SER   B OG  
5253 N  N   . CYS   B 81  ? 0.1282 0.1144 0.1305 0.0028  -0.0067 -0.0066 81   CYS   B N   
5254 C  CA  . CYS   B 81  ? 0.1331 0.1173 0.1328 0.0078  -0.0088 -0.0017 81   CYS   B CA  
5255 C  C   . CYS   B 81  ? 0.1281 0.1129 0.1195 -0.0010 -0.0107 -0.0042 81   CYS   B C   
5256 O  O   . CYS   B 81  ? 0.1515 0.1157 0.1325 0.0068  -0.0016 -0.0072 81   CYS   B O   
5257 C  CB  . CYS   B 81  ? 0.1484 0.1311 0.1321 -0.0035 -0.0122 -0.0056 81   CYS   B CB  
5258 S  SG  . CYS   B 81  ? 0.1457 0.1457 0.1297 -0.0035 -0.0207 -0.0126 81   CYS   B SG  
5264 N  N   . VAL   B 82  ? 0.1307 0.1181 0.1325 -0.0009 -0.0090 -0.0046 82   VAL   B N   
5265 C  CA  . VAL   B 82  ? 0.1408 0.1195 0.1338 -0.0046 -0.0072 0.0002  82   VAL   B CA  
5266 C  C   . VAL   B 82  ? 0.1435 0.1110 0.1355 -0.0031 -0.0035 -0.0048 82   VAL   B C   
5267 O  O   . VAL   B 82  ? 0.1511 0.1128 0.1719 -0.0045 -0.0073 -0.0182 82   VAL   B O   
5268 C  CB  . VAL   B 82  ? 0.1467 0.1343 0.1428 0.0038  -0.0116 0.0061  82   VAL   B CB  
5269 C  CG1 . VAL   B 82  ? 0.1663 0.1581 0.1587 0.0055  -0.0169 0.0119  82   VAL   B CG1 
5270 C  CG2 . VAL   B 82  ? 0.1597 0.1515 0.1573 0.0003  -0.0318 0.0103  82   VAL   B CG2 
5280 N  N   . LEU   B 83  ? 0.1333 0.1123 0.1316 -0.0143 -0.0171 -0.0108 83   LEU   B N   
5281 C  CA  . LEU   B 83  ? 0.1358 0.1183 0.1246 -0.0101 -0.0175 -0.0065 83   LEU   B CA  
5282 C  C   . LEU   B 83  ? 0.1378 0.1168 0.1167 -0.0172 -0.0195 -0.0056 83   LEU   B C   
5283 O  O   . LEU   B 83  ? 0.1413 0.1234 0.1105 -0.0179 -0.0118 0.0026  83   LEU   B O   
5284 C  CB  . LEU   B 83  ? 0.1399 0.1298 0.1229 -0.0069 -0.0203 -0.0157 83   LEU   B CB  
5285 C  CG  . LEU   B 83  ? 0.1589 0.1501 0.1378 -0.0119 -0.0086 -0.0111 83   LEU   B CG  
5286 C  CD1 . LEU   B 83  ? 0.1629 0.1527 0.1423 -0.0171 -0.0181 -0.0054 83   LEU   B CD1 
5287 C  CD2 . LEU   B 83  ? 0.1779 0.1540 0.1634 -0.0023 -0.0079 -0.0236 83   LEU   B CD2 
5299 N  N   . SER   B 84  ? 0.1392 0.1293 0.1454 -0.0214 -0.0179 -0.0019 84   SER   B N   
5300 C  CA  . SER   B 84  ? 0.1452 0.1493 0.1382 -0.0221 -0.0170 0.0128  84   SER   B CA  
5301 C  C   . SER   B 84  ? 0.1326 0.1617 0.0954 -0.0158 -0.0115 0.0145  84   SER   B C   
5302 O  O   . SER   B 84  ? 0.1428 0.1443 0.0975 -0.0145 -0.0096 0.0019  84   SER   B O   
5303 C  CB  . SER   B 84  ? 0.1606 0.1549 0.1792 -0.0311 0.0107  0.0131  84   SER   B CB  
5304 O  OG  . SER   B 84  ? 0.1606 0.1702 0.2270 -0.0412 0.0051  0.0282  84   SER   B OG  
5310 N  N   . GLY   B 85  ? 0.1420 0.1842 0.1067 -0.0159 -0.0139 0.0133  85   GLY   B N   
5311 C  CA  . GLY   B 85  ? 0.1429 0.1912 0.1275 -0.0290 0.0001  -0.0085 85   GLY   B CA  
5312 C  C   . GLY   B 85  ? 0.1392 0.1744 0.1204 -0.0372 -0.0003 0.0067  85   GLY   B C   
5313 O  O   . GLY   B 85  ? 0.1491 0.1711 0.1213 -0.0512 0.0188  -0.0075 85   GLY   B O   
5317 N  N   . HIS   B 86  ? 0.1379 0.1586 0.1337 -0.0335 -0.0190 0.0163  86   HIS   B N   
5318 C  CA  . HIS   B 86  ? 0.1390 0.1540 0.1381 -0.0307 -0.0186 0.0174  86   HIS   B CA  
5319 C  C   . HIS   B 86  ? 0.1384 0.1650 0.1296 -0.0388 -0.0139 0.0309  86   HIS   B C   
5320 O  O   . HIS   B 86  ? 0.1535 0.1768 0.1312 -0.0322 0.0024  0.0268  86   HIS   B O   
5321 C  CB  . HIS   B 86  ? 0.1462 0.1529 0.1368 -0.0200 -0.0218 0.0076  86   HIS   B CB  
5322 C  CG  . HIS   B 86  ? 0.1488 0.1570 0.1338 -0.0090 -0.0179 0.0122  86   HIS   B CG  
5323 N  ND1 . HIS   B 86  ? 0.1590 0.1808 0.1537 -0.0198 -0.0256 -0.0055 86   HIS   B ND1 
5324 C  CD2 . HIS   B 86  ? 0.1513 0.1575 0.1368 -0.0045 -0.0159 0.0066  86   HIS   B CD2 
5325 C  CE1 . HIS   B 86  ? 0.1660 0.1797 0.1411 -0.0122 -0.0068 -0.0193 86   HIS   B CE1 
5326 N  NE2 . HIS   B 86  ? 0.1606 0.1679 0.1329 0.0050  -0.0070 -0.0046 86   HIS   B NE2 
5334 N  N   . ASN   B 87  ? 0.1363 0.1656 0.1355 -0.0318 -0.0029 0.0297  87   ASN   B N   
5335 C  CA  . ASN   B 87  ? 0.1478 0.1877 0.1391 -0.0276 0.0194  0.0180  87   ASN   B CA  
5336 C  C   . ASN   B 87  ? 0.1588 0.1704 0.1275 -0.0276 0.0290  0.0113  87   ASN   B C   
5337 O  O   . ASN   B 87  ? 0.1823 0.1762 0.1598 -0.0206 0.0498  0.0066  87   ASN   B O   
5338 C  CB  . ASN   B 87  ? 0.1515 0.2248 0.1624 -0.0254 0.0236  0.0170  87   ASN   B CB  
5339 C  CG  . ASN   B 87  ? 0.1572 0.2418 0.1757 0.0062  0.0301  0.0293  87   ASN   B CG  
5340 O  OD1 . ASN   B 87  ? 0.1554 0.2252 0.1618 0.0098  0.0436  0.0456  87   ASN   B OD1 
5341 N  ND2 . ASN   B 87  ? 0.1872 0.2570 0.2189 0.0168  0.0381  0.0268  87   ASN   B ND2 
5348 N  N   . LEU   B 88  ? 0.1458 0.1586 0.1170 -0.0260 0.0140  0.0074  88   LEU   B N   
5349 C  CA  . LEU   B 88  ? 0.1571 0.1520 0.1184 -0.0332 0.0070  0.0000  88   LEU   B CA  
5350 C  C   . LEU   B 88  ? 0.1599 0.1425 0.1146 -0.0341 -0.0023 0.0044  88   LEU   B C   
5351 O  O   . LEU   B 88  ? 0.1824 0.1515 0.1435 -0.0194 -0.0238 -0.0072 88   LEU   B O   
5352 C  CB  . LEU   B 88  ? 0.1685 0.1548 0.1403 -0.0375 -0.0072 0.0143  88   LEU   B CB  
5353 C  CG  . LEU   B 88  ? 0.2034 0.1863 0.1585 -0.0301 -0.0253 0.0394  88   LEU   B CG  
5354 C  CD1 . LEU   B 88  ? 0.2125 0.2163 0.1772 -0.0433 -0.0195 0.0518  88   LEU   B CD1 
5355 C  CD2 . LEU   B 88  ? 0.2352 0.2084 0.2210 0.0103  -0.0477 0.0193  88   LEU   B CD2 
5367 N  N   . ALA   B 89  ? 0.1489 0.1418 0.1113 -0.0323 0.0160  0.0027  89   ALA   B N   
5368 C  CA  . ALA   B 89  ? 0.1467 0.1405 0.1011 -0.0313 0.0006  0.0080  89   ALA   B CA  
5369 C  C   . ALA   B 89  ? 0.1556 0.1383 0.1010 -0.0337 0.0104  0.0038  89   ALA   B C   
5370 O  O   . ALA   B 89  ? 0.1389 0.1481 0.1355 -0.0355 0.0122  -0.0277 89   ALA   B O   
5371 C  CB  . ALA   B 89  ? 0.1397 0.1358 0.1152 -0.0294 0.0065  0.0194  89   ALA   B CB  
5377 N  N   . LYS   B 90  ? 0.1866 0.1277 0.1174 -0.0389 -0.0063 0.0098  90   LYS   B N   
5378 C  CA  . LYS   B 90  ? 0.2035 0.1271 0.1088 -0.0402 -0.0130 0.0077  90   LYS   B CA  
5379 C  C   . LYS   B 90  ? 0.1851 0.1185 0.1192 -0.0364 -0.0098 -0.0000 90   LYS   B C   
5380 O  O   . LYS   B 90  ? 0.1965 0.1374 0.1363 -0.0507 -0.0067 -0.0009 90   LYS   B O   
5381 C  CB  . LYS   B 90  ? 0.2192 0.1364 0.1409 -0.0348 0.0002  0.0194  90   LYS   B CB  
5382 C  CG  . LYS   B 90  ? 0.2206 0.1506 0.1461 -0.0155 0.0221  0.0205  90   LYS   B CG  
5383 C  CD  . LYS   B 90  ? 0.2422 0.1800 0.2098 -0.0082 0.0378  0.0021  90   LYS   B CD  
5384 C  CE  . LYS   B 90  ? 0.2469 0.1974 0.2624 -0.0170 0.0503  -0.0028 90   LYS   B CE  
5385 N  NZ  . LYS   B 90  ? 0.2564 0.1921 0.2642 -0.0300 0.0679  0.0018  90   LYS   B NZ  
5399 N  N   . HIS   B 91  ? 0.1561 0.1128 0.1038 -0.0262 -0.0116 0.0030  91   HIS   B N   
5400 C  CA  . HIS   B 91  ? 0.1476 0.1151 0.1159 -0.0166 -0.0085 -0.0032 91   HIS   B CA  
5401 C  C   . HIS   B 91  ? 0.1358 0.1186 0.0981 -0.0204 -0.0039 -0.0029 91   HIS   B C   
5402 O  O   . HIS   B 91  ? 0.1528 0.1199 0.1094 -0.0239 -0.0163 0.0010  91   HIS   B O   
5403 C  CB  . HIS   B 91  ? 0.1648 0.1191 0.1571 -0.0016 -0.0073 0.0043  91   HIS   B CB  
5404 C  CG  . HIS   B 91  ? 0.2010 0.1346 0.2360 0.0085  0.0229  0.0197  91   HIS   B CG  
5405 N  ND1 . HIS   B 91  ? 0.2327 0.1466 0.2952 0.0020  0.0336  0.0067  91   HIS   B ND1 
5406 C  CD2 . HIS   B 91  ? 0.2150 0.1632 0.2844 0.0257  0.0142  0.0492  91   HIS   B CD2 
5407 C  CE1 . HIS   B 91  ? 0.2353 0.1591 0.3149 0.0214  0.0311  0.0162  91   HIS   B CE1 
5408 N  NE2 . HIS   B 91  ? 0.2267 0.1690 0.3169 0.0339  0.0283  0.0546  91   HIS   B NE2 
5416 N  N   . CYS   B 92  ? 0.1316 0.1178 0.1015 -0.0220 -0.0072 -0.0045 92   CYS   B N   
5417 C  CA  . CYS   B 92  ? 0.1306 0.1148 0.1004 -0.0169 -0.0039 -0.0017 92   CYS   B CA  
5418 C  C   . CYS   B 92  ? 0.1273 0.1093 0.0959 -0.0127 -0.0028 0.0013  92   CYS   B C   
5419 O  O   . CYS   B 92  ? 0.1371 0.1160 0.1177 -0.0148 -0.0029 -0.0032 92   CYS   B O   
5420 C  CB  . CYS   B 92  ? 0.1274 0.1233 0.1101 -0.0147 -0.0052 0.0014  92   CYS   B CB  
5421 S  SG  . CYS   B 92  ? 0.1301 0.1259 0.1113 -0.0109 -0.0092 0.0037  92   CYS   B SG  
5427 N  N   . LEU   B 93  ? 0.1186 0.1118 0.1047 -0.0133 -0.0051 -0.0042 93   LEU   B N   
5428 C  CA  . LEU   B 93  ? 0.1222 0.1139 0.1044 -0.0044 -0.0089 0.0004  93   LEU   B CA  
5429 C  C   . LEU   B 93  ? 0.1166 0.1123 0.0946 -0.0009 -0.0081 0.0054  93   LEU   B C   
5430 O  O   . LEU   B 93  ? 0.1219 0.1121 0.1111 -0.0037 -0.0025 -0.0004 93   LEU   B O   
5431 C  CB  . LEU   B 93  ? 0.1273 0.1109 0.1165 0.0019  -0.0070 0.0008  93   LEU   B CB  
5432 C  CG  . LEU   B 93  ? 0.1229 0.1230 0.1385 -0.0005 0.0007  0.0117  93   LEU   B CG  
5433 C  CD1 . LEU   B 93  ? 0.1262 0.1342 0.1362 0.0081  0.0025  -0.0038 93   LEU   B CD1 
5434 C  CD2 . LEU   B 93  ? 0.1213 0.1228 0.1473 -0.0014 -0.0103 0.0020  93   LEU   B CD2 
5446 N  N   . HIS   B 94  ? 0.1163 0.1067 0.0998 -0.0042 -0.0119 0.0047  94   HIS   B N   
5447 C  CA  . HIS   B 94  ? 0.1184 0.1090 0.1012 -0.0027 -0.0024 0.0013  94   HIS   B CA  
5448 C  C   . HIS   B 94  ? 0.1150 0.1143 0.1147 -0.0022 -0.0010 0.0032  94   HIS   B C   
5449 O  O   . HIS   B 94  ? 0.1175 0.1214 0.1531 -0.0014 0.0180  -0.0095 94   HIS   B O   
5450 C  CB  . HIS   B 94  ? 0.1216 0.1134 0.1118 0.0001  -0.0028 0.0027  94   HIS   B CB  
5451 C  CG  . HIS   B 94  ? 0.1228 0.1148 0.1043 -0.0046 -0.0177 0.0021  94   HIS   B CG  
5452 N  ND1 . HIS   B 94  ? 0.1257 0.1182 0.1075 -0.0045 -0.0158 -0.0038 94   HIS   B ND1 
5453 C  CD2 . HIS   B 94  ? 0.1262 0.1158 0.1200 -0.0032 -0.0154 0.0074  94   HIS   B CD2 
5454 C  CE1 . HIS   B 94  ? 0.1275 0.1198 0.0991 -0.0071 -0.0188 0.0009  94   HIS   B CE1 
5455 N  NE2 . HIS   B 94  ? 0.1240 0.1244 0.1152 -0.0110 -0.0168 0.0001  94   HIS   B NE2 
5463 N  N   . VAL   B 95  ? 0.1104 0.1120 0.1169 -0.0002 -0.0014 0.0015  95   VAL   B N   
5464 C  CA  . VAL   B 95  ? 0.1156 0.1179 0.1086 0.0014  0.0000  0.0091  95   VAL   B CA  
5465 C  C   . VAL   B 95  ? 0.1177 0.1186 0.1045 0.0023  0.0104  0.0041  95   VAL   B C   
5466 O  O   . VAL   B 95  ? 0.1211 0.1161 0.1306 0.0038  0.0104  0.0150  95   VAL   B O   
5467 C  CB  . VAL   B 95  ? 0.1260 0.1170 0.1146 -0.0021 -0.0038 0.0001  95   VAL   B CB  
5468 C  CG1 . VAL   B 95  ? 0.1333 0.1345 0.1331 -0.0071 0.0007  0.0126  95   VAL   B CG1 
5469 C  CG2 . VAL   B 95  ? 0.1286 0.1157 0.1192 -0.0007 -0.0118 0.0043  95   VAL   B CG2 
5479 N  N   . VAL   B 96  ? 0.1277 0.1254 0.1096 0.0079  0.0082  0.0111  96   VAL   B N   
5480 C  CA  . VAL   B 96  ? 0.1363 0.1378 0.1040 0.0071  0.0036  0.0157  96   VAL   B CA  
5481 C  C   . VAL   B 96  ? 0.1397 0.1399 0.1213 0.0084  0.0132  0.0130  96   VAL   B C   
5482 O  O   . VAL   B 96  ? 0.1381 0.1452 0.1413 0.0074  0.0196  0.0063  96   VAL   B O   
5483 C  CB  . VAL   B 96  ? 0.1433 0.1569 0.1156 0.0092  0.0092  0.0072  96   VAL   B CB  
5484 C  CG1 . VAL   B 96  ? 0.1403 0.1687 0.1283 0.0116  0.0139  0.0003  96   VAL   B CG1 
5485 C  CG2 . VAL   B 96  ? 0.1562 0.1634 0.1233 0.0120  0.0108  -0.0006 96   VAL   B CG2 
5495 N  N   . GLY   B 97  ? 0.1420 0.1404 0.1199 0.0067  0.0109  0.0143  97   GLY   B N   
5496 C  CA  . GLY   B 97  ? 0.1538 0.1443 0.1262 0.0073  0.0116  0.0199  97   GLY   B CA  
5497 C  C   . GLY   B 97  ? 0.1683 0.1478 0.1312 0.0118  0.0113  0.0167  97   GLY   B C   
5498 O  O   . GLY   B 97  ? 0.1771 0.1581 0.1345 0.0052  0.0060  0.0112  97   GLY   B O   
5502 N  N   . PRO   B 98  ? 0.1770 0.1526 0.1532 0.0137  0.0319  0.0289  98   PRO   B N   
5503 C  CA  . PRO   B 98  ? 0.1908 0.1652 0.1529 0.0192  0.0421  0.0275  98   PRO   B CA  
5504 C  C   . PRO   B 98  ? 0.2042 0.1680 0.1264 0.0287  0.0364  0.0445  98   PRO   B C   
5505 O  O   . PRO   B 98  ? 0.1984 0.1631 0.1509 0.0293  0.0395  0.0401  98   PRO   B O   
5506 C  CB  . PRO   B 98  ? 0.1834 0.1706 0.1798 0.0153  0.0532  0.0227  98   PRO   B CB  
5507 C  CG  . PRO   B 98  ? 0.1767 0.1663 0.1798 0.0134  0.0450  0.0298  98   PRO   B CG  
5508 C  CD  . PRO   B 98  ? 0.1616 0.1530 0.1626 0.0170  0.0390  0.0325  98   PRO   B CD  
5516 N  N   . ASN   B 99  ? 0.2159 0.1845 0.1281 0.0438  0.0378  0.0319  99   ASN   B N   
5517 C  CA  . ASN   B 99  ? 0.2346 0.1936 0.1350 0.0515  0.0295  0.0473  99   ASN   B CA  
5518 C  C   . ASN   B 99  ? 0.2620 0.2230 0.1657 0.0493  0.0577  0.0675  99   ASN   B C   
5519 O  O   . ASN   B 99  ? 0.2749 0.2297 0.1728 0.0428  0.0534  0.0648  99   ASN   B O   
5520 C  CB  . ASN   B 99  ? 0.2407 0.1905 0.1449 0.0489  0.0191  0.0365  99   ASN   B CB  
5521 C  CG  . ASN   B 99  ? 0.2420 0.1970 0.1761 0.0470  0.0115  0.0318  99   ASN   B CG  
5522 O  OD1 . ASN   B 99  ? 0.2453 0.1977 0.2069 0.0527  0.0124  0.0430  99   ASN   B OD1 
5523 N  ND2 . ASN   B 99  ? 0.2435 0.2000 0.1880 0.0447  -0.0096 0.0223  99   ASN   B ND2 
5530 N  N   A VAL   B 100 ? 0.2811 0.2367 0.2118 0.0392  0.0593  0.0878  100  VAL   B N   
5531 N  N   B VAL   B 100 ? 0.2805 0.2358 0.2113 0.0383  0.0589  0.0880  100  VAL   B N   
5532 C  CA  A VAL   B 100 ? 0.3065 0.2505 0.2638 0.0305  0.0624  0.0981  100  VAL   B CA  
5533 C  CA  B VAL   B 100 ? 0.3052 0.2484 0.2624 0.0287  0.0618  0.0986  100  VAL   B CA  
5534 C  C   A VAL   B 100 ? 0.3284 0.2538 0.2527 0.0352  0.0659  0.1116  100  VAL   B C   
5535 C  C   B VAL   B 100 ? 0.3276 0.2517 0.2505 0.0337  0.0650  0.1112  100  VAL   B C   
5536 O  O   A VAL   B 100 ? 0.3336 0.2639 0.2576 0.0312  0.0750  0.1063  100  VAL   B O   
5537 O  O   B VAL   B 100 ? 0.3325 0.2595 0.2521 0.0288  0.0734  0.1051  100  VAL   B O   
5538 C  CB  A VAL   B 100 ? 0.3148 0.2641 0.3277 0.0139  0.0557  0.0980  100  VAL   B CB  
5539 C  CB  B VAL   B 100 ? 0.3125 0.2612 0.3260 0.0111  0.0553  0.1001  100  VAL   B CB  
5540 C  CG1 A VAL   B 100 ? 0.3194 0.2706 0.3520 0.0116  0.0536  0.0963  100  VAL   B CG1 
5541 C  CG1 B VAL   B 100 ? 0.3168 0.2673 0.3504 0.0087  0.0537  0.0994  100  VAL   B CG1 
5542 C  CG2 A VAL   B 100 ? 0.3167 0.2672 0.3458 0.0073  0.0555  0.1014  100  VAL   B CG2 
5543 C  CG2 B VAL   B 100 ? 0.3142 0.2639 0.3446 0.0042  0.0545  0.1035  100  VAL   B CG2 
5562 N  N   . ASN   B 101 ? 0.3452 0.2549 0.2488 0.0436  0.0554  0.1187  101  ASN   B N   
5563 C  CA  . ASN   B 101 ? 0.3887 0.2699 0.2722 0.0522  0.0273  0.1247  101  ASN   B CA  
5564 C  C   . ASN   B 101 ? 0.4351 0.3027 0.2694 0.0544  0.0131  0.1415  101  ASN   B C   
5565 O  O   . ASN   B 101 ? 0.4423 0.3162 0.2926 0.0592  0.0129  0.1151  101  ASN   B O   
5566 C  CB  . ASN   B 101 ? 0.3855 0.2552 0.2900 0.0480  0.0271  0.1092  101  ASN   B CB  
5567 C  CG  . ASN   B 101 ? 0.3818 0.2423 0.2941 0.0435  0.0307  0.1080  101  ASN   B CG  
5568 O  OD1 . ASN   B 101 ? 0.3853 0.2439 0.3209 0.0358  0.0419  0.1010  101  ASN   B OD1 
5569 N  ND2 . ASN   B 101 ? 0.3770 0.2420 0.2834 0.0442  0.0265  0.0982  101  ASN   B ND2 
5577 N  N   . LYS   B 102 ? 0.4702 0.3289 0.2824 0.0445  0.0178  0.1448  102  LYS   B N   
5578 C  CA  . LYS   B 102 ? 0.5038 0.3676 0.3164 0.0319  0.0319  0.1185  102  LYS   B CA  
5579 C  C   . LYS   B 102 ? 0.4960 0.3673 0.2980 0.0331  0.0443  0.1176  102  LYS   B C   
5580 O  O   . LYS   B 102 ? 0.5060 0.3718 0.3055 0.0360  0.0301  0.1131  102  LYS   B O   
5581 C  CB  . LYS   B 102 ? 0.5396 0.4055 0.3857 0.0198  0.0408  0.0815  102  LYS   B CB  
5582 C  CG  . LYS   B 102 ? 0.5663 0.4388 0.4524 0.0112  0.0504  0.0440  102  LYS   B CG  
5583 C  CD  . LYS   B 102 ? 0.5898 0.4650 0.5186 0.0049  0.0597  0.0153  102  LYS   B CD  
5584 C  CE  . LYS   B 102 ? 0.6086 0.4841 0.5715 -0.0005 0.0653  -0.0051 102  LYS   B CE  
5585 N  NZ  . LYS   B 102 ? 0.6144 0.4932 0.5997 -0.0033 0.0664  -0.0168 102  LYS   B NZ  
5599 N  N   . GLY   B 103 ? 0.4736 0.3598 0.2913 0.0299  0.0732  0.1126  103  GLY   B N   
5600 C  CA  . GLY   B 103 ? 0.4496 0.3521 0.3024 0.0279  0.0961  0.0926  103  GLY   B CA  
5601 C  C   . GLY   B 103 ? 0.4212 0.3388 0.2969 0.0221  0.1151  0.0741  103  GLY   B C   
5602 O  O   . GLY   B 103 ? 0.4281 0.3461 0.3104 0.0224  0.1186  0.0733  103  GLY   B O   
5606 N  N   A GLU   B 104 ? 0.4028 0.3302 0.2874 0.0244  0.1217  0.0597  104  GLU   B N   
5607 N  N   B GLU   B 104 ? 0.4013 0.3234 0.2827 0.0134  0.1174  0.0609  104  GLU   B N   
5608 C  CA  A GLU   B 104 ? 0.3835 0.3225 0.2717 0.0285  0.1235  0.0438  104  GLU   B CA  
5609 C  CA  B GLU   B 104 ? 0.3807 0.3095 0.2620 0.0063  0.1146  0.0465  104  GLU   B CA  
5610 C  C   A GLU   B 104 ? 0.3842 0.3267 0.2902 0.0151  0.1450  0.0395  104  GLU   B C   
5611 C  C   B GLU   B 104 ? 0.3786 0.3096 0.2790 -0.0055 0.1343  0.0406  104  GLU   B C   
5612 O  O   A GLU   B 104 ? 0.3865 0.3310 0.3127 0.0122  0.1405  0.0350  104  GLU   B O   
5613 O  O   B GLU   B 104 ? 0.3809 0.3127 0.3042 -0.0073 0.1290  0.0339  104  GLU   B O   
5614 C  CB  A GLU   B 104 ? 0.3671 0.3098 0.2554 0.0472  0.0936  0.0234  104  GLU   B CB  
5615 C  CB  B GLU   B 104 ? 0.3662 0.2940 0.2412 0.0122  0.0817  0.0285  104  GLU   B CB  
5616 C  CG  A GLU   B 104 ? 0.3532 0.2998 0.2391 0.0649  0.0561  -0.0004 104  GLU   B CG  
5617 C  CG  B GLU   B 104 ? 0.3547 0.2814 0.2192 0.0181  0.0409  0.0053  104  GLU   B CG  
5618 C  CD  A GLU   B 104 ? 0.3399 0.2892 0.2197 0.0807  0.0239  -0.0151 104  GLU   B CD  
5619 C  CD  B GLU   B 104 ? 0.3442 0.2678 0.1916 0.0207  0.0076  -0.0071 104  GLU   B CD  
5620 O  OE1 A GLU   B 104 ? 0.3252 0.2786 0.1833 0.0929  0.0302  -0.0169 104  GLU   B OE1 
5621 O  OE1 B GLU   B 104 ? 0.3322 0.2579 0.1614 0.0224  0.0108  -0.0059 104  GLU   B OE1 
5622 O  OE2 A GLU   B 104 ? 0.3416 0.2937 0.2343 0.0800  -0.0046 -0.0244 104  GLU   B OE2 
5623 O  OE2 B GLU   B 104 ? 0.3453 0.2690 0.1910 0.0178  -0.0215 -0.0176 104  GLU   B OE2 
5636 N  N   A ASP   B 105 ? 0.3803 0.3278 0.2933 0.0033  0.1675  0.0394  105  ASP   B N   
5637 N  N   B ASP   B 105 ? 0.3719 0.3081 0.2740 -0.0173 0.1570  0.0415  105  ASP   B N   
5638 C  CA  A ASP   B 105 ? 0.3795 0.3283 0.3165 -0.0061 0.1791  0.0294  105  ASP   B CA  
5639 C  CA  B ASP   B 105 ? 0.3683 0.3059 0.2917 -0.0259 0.1695  0.0315  105  ASP   B CA  
5640 C  C   A ASP   B 105 ? 0.3673 0.3061 0.2926 -0.0124 0.1789  0.0262  105  ASP   B C   
5641 C  C   B ASP   B 105 ? 0.3581 0.2852 0.2709 -0.0323 0.1657  0.0246  105  ASP   B C   
5642 O  O   A ASP   B 105 ? 0.3612 0.3000 0.2828 -0.0096 0.1860  0.0252  105  ASP   B O   
5643 O  O   B ASP   B 105 ? 0.3505 0.2779 0.2612 -0.0320 0.1703  0.0232  105  ASP   B O   
5644 C  CB  A ASP   B 105 ? 0.3905 0.3469 0.3792 -0.0043 0.1785  0.0147  105  ASP   B CB  
5645 C  CB  B ASP   B 105 ? 0.3756 0.3211 0.3453 -0.0236 0.1717  0.0203  105  ASP   B CB  
5646 C  CG  A ASP   B 105 ? 0.3976 0.3607 0.4352 -0.0046 0.1837  0.0054  105  ASP   B CG  
5647 C  CG  B ASP   B 105 ? 0.3786 0.3308 0.3882 -0.0253 0.1825  0.0164  105  ASP   B CG  
5648 O  OD1 A ASP   B 105 ? 0.3974 0.3651 0.4458 -0.0089 0.1914  0.0068  105  ASP   B OD1 
5649 O  OD1 B ASP   B 105 ? 0.3785 0.3352 0.3986 -0.0308 0.1863  0.0179  105  ASP   B OD1 
5650 O  OD2 A ASP   B 105 ? 0.4025 0.3675 0.4696 -0.0014 0.1747  -0.0017 105  ASP   B OD2 
5651 O  OD2 B ASP   B 105 ? 0.3765 0.3336 0.3974 -0.0267 0.1936  0.0193  105  ASP   B OD2 
5660 N  N   A ILE   B 106 ? 0.3590 0.2879 0.3011 -0.0203 0.1661  0.0294  106  ILE   B N   
5661 N  N   B ILE   B 106 ? 0.3522 0.2711 0.2784 -0.0374 0.1522  0.0239  106  ILE   B N   
5662 C  CA  A ILE   B 106 ? 0.3422 0.2680 0.3133 -0.0287 0.1639  0.0265  106  ILE   B CA  
5663 C  CA  B ILE   B 106 ? 0.3382 0.2574 0.2937 -0.0427 0.1483  0.0183  106  ILE   B CA  
5664 C  C   A ILE   B 106 ? 0.3150 0.2621 0.3099 -0.0264 0.1665  0.0177  106  ILE   B C   
5665 C  C   B ILE   B 106 ? 0.3129 0.2561 0.2930 -0.0394 0.1498  0.0061  106  ILE   B C   
5666 O  O   A ILE   B 106 ? 0.3083 0.2470 0.3076 -0.0271 0.1678  0.0161  106  ILE   B O   
5667 O  O   B ILE   B 106 ? 0.3059 0.2415 0.2877 -0.0431 0.1467  0.0005  106  ILE   B O   
5668 C  CB  A ILE   B 106 ? 0.3547 0.2596 0.3324 -0.0360 0.1518  0.0314  106  ILE   B CB  
5669 C  CB  B ILE   B 106 ? 0.3520 0.2523 0.3130 -0.0467 0.1366  0.0237  106  ILE   B CB  
5670 C  CG1 A ILE   B 106 ? 0.3599 0.2568 0.3401 -0.0327 0.1432  0.0262  106  ILE   B CG1 
5671 C  CG1 B ILE   B 106 ? 0.3585 0.2521 0.3230 -0.0397 0.1267  0.0195  106  ILE   B CG1 
5672 C  CG2 A ILE   B 106 ? 0.3585 0.2592 0.3427 -0.0424 0.1523  0.0363  106  ILE   B CG2 
5673 C  CG2 B ILE   B 106 ? 0.3557 0.2526 0.3245 -0.0533 0.1373  0.0273  106  ILE   B CG2 
5674 C  CD1 A ILE   B 106 ? 0.3629 0.2570 0.3401 -0.0291 0.1392  0.0248  106  ILE   B CD1 
5675 C  CD1 B ILE   B 106 ? 0.3619 0.2534 0.3254 -0.0342 0.1228  0.0194  106  ILE   B CD1 
5698 N  N   A GLN   B 107 ? 0.2992 0.2737 0.3241 -0.0244 0.1562  0.0155  107  GLN   B N   
5699 N  N   B GLN   B 107 ? 0.2994 0.2717 0.3124 -0.0327 0.1431  0.0046  107  GLN   B N   
5700 C  CA  A GLN   B 107 ? 0.2824 0.2827 0.3387 -0.0204 0.1390  0.0126  107  GLN   B CA  
5701 C  CA  B GLN   B 107 ? 0.2846 0.2841 0.3318 -0.0242 0.1312  0.0047  107  GLN   B CA  
5702 C  C   A GLN   B 107 ? 0.2536 0.2629 0.3094 -0.0088 0.1162  0.0022  107  GLN   B C   
5703 C  C   B GLN   B 107 ? 0.2554 0.2656 0.3058 -0.0115 0.1133  -0.0024 107  GLN   B C   
5704 O  O   A GLN   B 107 ? 0.2501 0.2642 0.3354 -0.0029 0.0952  -0.0101 107  GLN   B O   
5705 O  O   B GLN   B 107 ? 0.2532 0.2707 0.3322 -0.0072 0.0930  -0.0163 107  GLN   B O   
5706 C  CB  A GLN   B 107 ? 0.3041 0.3128 0.3987 -0.0220 0.1219  0.0166  107  GLN   B CB  
5707 C  CB  B GLN   B 107 ? 0.3077 0.3154 0.3914 -0.0231 0.1159  0.0096  107  GLN   B CB  
5708 C  CG  A GLN   B 107 ? 0.3275 0.3407 0.4594 -0.0188 0.0946  0.0177  107  GLN   B CG  
5709 C  CG  B GLN   B 107 ? 0.3325 0.3443 0.4516 -0.0177 0.0906  0.0120  107  GLN   B CG  
5710 C  CD  A GLN   B 107 ? 0.3441 0.3615 0.5065 -0.0182 0.0751  0.0219  107  GLN   B CD  
5711 C  CD  B GLN   B 107 ? 0.3508 0.3660 0.4988 -0.0151 0.0717  0.0168  107  GLN   B CD  
5712 O  OE1 A GLN   B 107 ? 0.3499 0.3690 0.5232 -0.0171 0.0728  0.0207  107  GLN   B OE1 
5713 O  OE1 B GLN   B 107 ? 0.3576 0.3739 0.5152 -0.0147 0.0701  0.0170  107  GLN   B OE1 
5714 N  NE2 A GLN   B 107 ? 0.3508 0.3677 0.5229 -0.0164 0.0652  0.0266  107  GLN   B NE2 
5715 N  NE2 B GLN   B 107 ? 0.3581 0.3728 0.5149 -0.0124 0.0624  0.0208  107  GLN   B NE2 
5732 N  N   . LEU   B 108 ? 0.2292 0.2417 0.2696 0.0036  0.1050  0.0007  108  LEU   B N   
5733 C  CA  . LEU   B 108 ? 0.2060 0.2143 0.2257 0.0246  0.0676  0.0128  108  LEU   B CA  
5734 C  C   . LEU   B 108 ? 0.1768 0.1729 0.2019 0.0243  0.0414  0.0265  108  LEU   B C   
5735 O  O   . LEU   B 108 ? 0.1782 0.1615 0.1977 0.0231  0.0310  0.0195  108  LEU   B O   
5736 C  CB  . LEU   B 108 ? 0.2214 0.2366 0.2111 0.0265  0.0658  0.0174  108  LEU   B CB  
5737 C  CG  . LEU   B 108 ? 0.2348 0.2643 0.2124 0.0319  0.0513  0.0014  108  LEU   B CG  
5738 C  CD1 . LEU   B 108 ? 0.2417 0.2789 0.1994 0.0254  0.0544  0.0026  108  LEU   B CD1 
5739 C  CD2 . LEU   B 108 ? 0.2470 0.2741 0.2231 0.0374  0.0409  -0.0085 108  LEU   B CD2 
5752 N  N   . LEU   B 109 ? 0.1628 0.1518 0.1909 0.0179  0.0355  0.0216  109  LEU   B N   
5753 C  CA  . LEU   B 109 ? 0.1525 0.1334 0.1937 0.0107  0.0302  0.0272  109  LEU   B CA  
5754 C  C   . LEU   B 109 ? 0.1378 0.1234 0.1963 0.0045  0.0290  0.0193  109  LEU   B C   
5755 O  O   . LEU   B 109 ? 0.1310 0.1251 0.2012 0.0076  0.0291  0.0286  109  LEU   B O   
5756 C  CB  . LEU   B 109 ? 0.1627 0.1260 0.1867 0.0100  0.0213  0.0336  109  LEU   B CB  
5757 C  CG  . LEU   B 109 ? 0.1553 0.1274 0.1922 0.0071  0.0126  0.0181  109  LEU   B CG  
5758 C  CD1 . LEU   B 109 ? 0.1528 0.1354 0.1930 0.0134  0.0204  0.0168  109  LEU   B CD1 
5759 C  CD2 . LEU   B 109 ? 0.1615 0.1346 0.2062 0.0072  0.0122  0.0142  109  LEU   B CD2 
5771 N  N   . LYS   B 110 ? 0.1326 0.1227 0.1828 0.0010  0.0279  0.0237  110  LYS   B N   
5772 C  CA  . LYS   B 110 ? 0.1333 0.1196 0.1880 0.0000  0.0236  0.0136  110  LYS   B CA  
5773 C  C   . LYS   B 110 ? 0.1240 0.1186 0.1793 -0.0023 0.0312  0.0097  110  LYS   B C   
5774 O  O   . LYS   B 110 ? 0.1253 0.1177 0.1820 -0.0060 0.0240  0.0028  110  LYS   B O   
5775 C  CB  . LYS   B 110 ? 0.1346 0.1221 0.2051 -0.0059 0.0269  0.0094  110  LYS   B CB  
5776 C  CG  . LYS   B 110 ? 0.1349 0.1259 0.2130 -0.0113 0.0131  0.0107  110  LYS   B CG  
5777 C  CD  . LYS   B 110 ? 0.1393 0.1227 0.2185 -0.0056 0.0116  0.0074  110  LYS   B CD  
5778 C  CE  . LYS   B 110 ? 0.1352 0.1368 0.2453 0.0029  0.0129  0.0035  110  LYS   B CE  
5779 N  NZ  . LYS   B 110 ? 0.1383 0.1505 0.2434 0.0062  0.0064  0.0046  110  LYS   B NZ  
5793 N  N   . SER   B 111 ? 0.1362 0.1225 0.1794 0.0005  0.0285  0.0111  111  SER   B N   
5794 C  CA  . SER   B 111 ? 0.1425 0.1255 0.1726 0.0028  0.0164  0.0200  111  SER   B CA  
5795 C  C   . SER   B 111 ? 0.1306 0.1198 0.1676 0.0025  0.0171  0.0109  111  SER   B C   
5796 O  O   . SER   B 111 ? 0.1262 0.1275 0.1706 0.0025  0.0096  0.0135  111  SER   B O   
5797 C  CB  . SER   B 111 ? 0.1540 0.1438 0.1797 0.0061  0.0309  0.0199  111  SER   B CB  
5798 O  OG  . SER   B 111 ? 0.1763 0.1827 0.1908 0.0039  0.0415  0.0269  111  SER   B OG  
5804 N  N   . ALA   B 112 ? 0.1270 0.1250 0.1727 0.0076  0.0232  0.0187  112  ALA   B N   
5805 C  CA  . ALA   B 112 ? 0.1256 0.1305 0.1585 0.0044  0.0072  0.0073  112  ALA   B CA  
5806 C  C   . ALA   B 112 ? 0.1148 0.1178 0.1589 0.0035  0.0080  0.0050  112  ALA   B C   
5807 O  O   . ALA   B 112 ? 0.1136 0.1208 0.1721 -0.0034 0.0118  0.0027  112  ALA   B O   
5808 C  CB  . ALA   B 112 ? 0.1325 0.1355 0.1654 0.0078  0.0041  0.0153  112  ALA   B CB  
5814 N  N   . TYR   B 113 ? 0.1128 0.1119 0.1696 0.0017  0.0074  0.0137  113  TYR   B N   
5815 C  CA  . TYR   B 113 ? 0.1110 0.1111 0.1567 -0.0010 0.0120  0.0062  113  TYR   B CA  
5816 C  C   . TYR   B 113 ? 0.1119 0.1084 0.1439 -0.0070 0.0076  -0.0018 113  TYR   B C   
5817 O  O   . TYR   B 113 ? 0.1163 0.1132 0.1418 -0.0040 0.0054  -0.0019 113  TYR   B O   
5818 C  CB  . TYR   B 113 ? 0.1234 0.1067 0.1694 -0.0033 0.0173  0.0094  113  TYR   B CB  
5819 C  CG  . TYR   B 113 ? 0.1218 0.1096 0.1755 -0.0052 0.0083  0.0116  113  TYR   B CG  
5820 C  CD1 . TYR   B 113 ? 0.1292 0.1081 0.1830 -0.0022 0.0159  0.0140  113  TYR   B CD1 
5821 C  CD2 . TYR   B 113 ? 0.1285 0.1096 0.1718 -0.0046 0.0070  0.0083  113  TYR   B CD2 
5822 C  CE1 . TYR   B 113 ? 0.1295 0.1164 0.1855 -0.0041 0.0218  0.0070  113  TYR   B CE1 
5823 C  CE2 . TYR   B 113 ? 0.1323 0.1059 0.1813 0.0022  0.0105  0.0181  113  TYR   B CE2 
5824 C  CZ  . TYR   B 113 ? 0.1247 0.1137 0.1916 0.0053  0.0151  0.0007  113  TYR   B CZ  
5825 O  OH  . TYR   B 113 ? 0.1346 0.1119 0.2033 0.0117  0.0232  0.0040  113  TYR   B OH  
5835 N  N   . GLU   B 114 ? 0.1120 0.1053 0.1642 -0.0010 0.0138  0.0028  114  GLU   B N   
5836 C  CA  . GLU   B 114 ? 0.1110 0.0993 0.1599 0.0005  0.0080  -0.0013 114  GLU   B CA  
5837 C  C   . GLU   B 114 ? 0.1108 0.1087 0.1480 0.0033  0.0059  -0.0008 114  GLU   B C   
5838 O  O   . GLU   B 114 ? 0.1102 0.1094 0.1656 0.0030  0.0070  0.0093  114  GLU   B O   
5839 C  CB  . GLU   B 114 ? 0.1140 0.1068 0.1633 0.0002  0.0126  0.0040  114  GLU   B CB  
5840 C  CG  . GLU   B 114 ? 0.1182 0.1100 0.1636 0.0034  0.0115  0.0081  114  GLU   B CG  
5841 C  CD  . GLU   B 114 ? 0.1169 0.1126 0.1733 -0.0069 0.0132  0.0061  114  GLU   B CD  
5842 O  OE1 . GLU   B 114 ? 0.1157 0.1261 0.1800 -0.0078 0.0214  0.0109  114  GLU   B OE1 
5843 O  OE2 . GLU   B 114 ? 0.1179 0.1328 0.1886 -0.0156 0.0117  0.0089  114  GLU   B OE2 
5850 N  N   . ASN   B 115 ? 0.1130 0.1051 0.1468 -0.0050 0.0029  0.0042  115  ASN   B N   
5851 C  CA  . ASN   B 115 ? 0.1132 0.1115 0.1430 -0.0088 0.0070  0.0039  115  ASN   B CA  
5852 C  C   . ASN   B 115 ? 0.1067 0.1021 0.1472 -0.0094 -0.0017 -0.0025 115  ASN   B C   
5853 O  O   . ASN   B 115 ? 0.1184 0.1111 0.1491 -0.0105 0.0019  0.0019  115  ASN   B O   
5854 C  CB  . ASN   B 115 ? 0.1267 0.1208 0.1490 -0.0054 0.0067  -0.0019 115  ASN   B CB  
5855 C  CG  . ASN   B 115 ? 0.1330 0.1248 0.1517 0.0019  0.0036  -0.0031 115  ASN   B CG  
5856 O  OD1 . ASN   B 115 ? 0.1737 0.1360 0.1692 -0.0050 0.0097  -0.0107 115  ASN   B OD1 
5857 N  ND2 . ASN   B 115 ? 0.1279 0.1322 0.1481 0.0010  0.0038  0.0051  115  ASN   B ND2 
5864 N  N   . PHE   B 116 ? 0.1143 0.1057 0.1336 -0.0020 0.0046  0.0017  116  PHE   B N   
5865 C  CA  . PHE   B 116 ? 0.1175 0.1080 0.1376 -0.0095 -0.0010 0.0038  116  PHE   B CA  
5866 C  C   . PHE   B 116 ? 0.1189 0.0983 0.1384 -0.0099 -0.0035 0.0062  116  PHE   B C   
5867 O  O   . PHE   B 116 ? 0.1226 0.1094 0.1447 -0.0026 0.0008  0.0063  116  PHE   B O   
5868 C  CB  . PHE   B 116 ? 0.1110 0.1114 0.1363 -0.0080 -0.0027 0.0062  116  PHE   B CB  
5869 C  CG  . PHE   B 116 ? 0.1082 0.1096 0.1351 -0.0046 0.0012  -0.0020 116  PHE   B CG  
5870 C  CD1 . PHE   B 116 ? 0.1207 0.1103 0.1535 -0.0032 0.0039  -0.0007 116  PHE   B CD1 
5871 C  CD2 . PHE   B 116 ? 0.1185 0.1197 0.1321 -0.0013 0.0068  -0.0062 116  PHE   B CD2 
5872 C  CE1 . PHE   B 116 ? 0.1180 0.1144 0.1431 -0.0040 -0.0098 0.0012  116  PHE   B CE1 
5873 C  CE2 . PHE   B 116 ? 0.1190 0.1156 0.1379 -0.0005 0.0044  -0.0041 116  PHE   B CE2 
5874 C  CZ  . PHE   B 116 ? 0.1134 0.1167 0.1368 0.0013  -0.0045 0.0025  116  PHE   B CZ  
5884 N  N   . ASN   B 117 ? 0.1159 0.1028 0.1563 -0.0045 -0.0055 0.0060  117  ASN   B N   
5885 C  CA  . ASN   B 117 ? 0.1211 0.1052 0.1475 -0.0014 -0.0013 -0.0022 117  ASN   B CA  
5886 C  C   . ASN   B 117 ? 0.1201 0.1066 0.1663 0.0003  0.0005  0.0048  117  ASN   B C   
5887 O  O   . ASN   B 117 ? 0.1287 0.1158 0.1869 -0.0050 -0.0217 0.0112  117  ASN   B O   
5888 C  CB  . ASN   B 117 ? 0.1167 0.1122 0.1506 -0.0034 -0.0029 -0.0086 117  ASN   B CB  
5889 C  CG  . ASN   B 117 ? 0.1179 0.1159 0.1595 0.0043  0.0009  -0.0092 117  ASN   B CG  
5890 O  OD1 . ASN   B 117 ? 0.1406 0.1162 0.1611 -0.0136 0.0074  -0.0044 117  ASN   B OD1 
5891 N  ND2 . ASN   B 117 ? 0.1227 0.1167 0.1521 -0.0001 0.0074  -0.0047 117  ASN   B ND2 
5898 N  N   . GLN   B 118 ? 0.1235 0.1046 0.1567 -0.0091 -0.0184 0.0013  118  GLN   B N   
5899 C  CA  . GLN   B 118 ? 0.1247 0.1080 0.1657 -0.0010 -0.0126 -0.0014 118  GLN   B CA  
5900 C  C   . GLN   B 118 ? 0.1253 0.1078 0.1704 -0.0025 -0.0056 0.0011  118  GLN   B C   
5901 O  O   . GLN   B 118 ? 0.1459 0.1119 0.2043 -0.0069 0.0097  0.0028  118  GLN   B O   
5902 C  CB  . GLN   B 118 ? 0.1382 0.1137 0.1754 0.0033  -0.0147 0.0001  118  GLN   B CB  
5903 C  CG  . GLN   B 118 ? 0.1458 0.1171 0.1688 0.0052  -0.0102 -0.0111 118  GLN   B CG  
5904 C  CD  . GLN   B 118 ? 0.1472 0.1130 0.1656 0.0013  -0.0026 -0.0123 118  GLN   B CD  
5905 O  OE1 . GLN   B 118 ? 0.1510 0.1153 0.1882 0.0041  0.0109  0.0037  118  GLN   B OE1 
5906 N  NE2 . GLN   B 118 ? 0.1548 0.1168 0.1693 0.0003  -0.0091 -0.0001 118  GLN   B NE2 
5915 N  N   . HIS   B 119 ? 0.1314 0.1089 0.1492 -0.0040 -0.0076 0.0102  119  HIS   B N   
5916 C  CA  . HIS   B 119 ? 0.1401 0.1220 0.1362 -0.0039 -0.0128 0.0048  119  HIS   B CA  
5917 C  C   . HIS   B 119 ? 0.1395 0.1242 0.1309 -0.0075 -0.0187 0.0058  119  HIS   B C   
5918 O  O   . HIS   B 119 ? 0.1489 0.1229 0.1543 -0.0244 -0.0130 0.0093  119  HIS   B O   
5919 C  CB  . HIS   B 119 ? 0.1396 0.1328 0.1489 0.0003  -0.0195 -0.0044 119  HIS   B CB  
5920 C  CG  . HIS   B 119 ? 0.1445 0.1542 0.1729 0.0141  -0.0335 -0.0134 119  HIS   B CG  
5921 N  ND1 . HIS   B 119 ? 0.1644 0.1692 0.2023 0.0069  -0.0416 -0.0372 119  HIS   B ND1 
5922 C  CD2 . HIS   B 119 ? 0.1630 0.1705 0.1742 0.0351  -0.0445 -0.0232 119  HIS   B CD2 
5923 C  CE1 . HIS   B 119 ? 0.1806 0.1807 0.2066 0.0176  -0.0545 -0.0466 119  HIS   B CE1 
5924 N  NE2 . HIS   B 119 ? 0.1841 0.1927 0.1947 0.0321  -0.0510 -0.0353 119  HIS   B NE2 
5932 N  N   . GLU   B 120 ? 0.1549 0.1260 0.1279 -0.0151 -0.0206 0.0098  120  GLU   B N   
5933 C  CA  . GLU   B 120 ? 0.1826 0.1369 0.1426 -0.0029 -0.0333 0.0191  120  GLU   B CA  
5934 C  C   . GLU   B 120 ? 0.1628 0.1299 0.1319 -0.0089 -0.0242 0.0210  120  GLU   B C   
5935 O  O   . GLU   B 120 ? 0.1604 0.1400 0.1383 -0.0129 -0.0255 0.0107  120  GLU   B O   
5936 C  CB  . GLU   B 120 ? 0.2417 0.1675 0.2083 0.0141  -0.0605 0.0313  120  GLU   B CB  
5937 C  CG  . GLU   B 120 ? 0.2884 0.2326 0.3152 0.0201  -0.0777 0.0515  120  GLU   B CG  
5938 C  CD  . GLU   B 120 ? 0.3281 0.2880 0.4140 0.0195  -0.0831 0.0681  120  GLU   B CD  
5939 O  OE1 . GLU   B 120 ? 0.3473 0.3079 0.4479 0.0144  -0.0767 0.0839  120  GLU   B OE1 
5940 O  OE2 . GLU   B 120 ? 0.3482 0.3138 0.4678 0.0191  -0.0843 0.0628  120  GLU   B OE2 
5947 N  N   . VAL   B 121 ? 0.1536 0.1232 0.1365 -0.0186 -0.0166 0.0187  121  VAL   B N   
5948 C  CA  . VAL   B 121 ? 0.1513 0.1323 0.1258 -0.0184 -0.0203 0.0128  121  VAL   B CA  
5949 C  C   . VAL   B 121 ? 0.1462 0.1312 0.1207 -0.0237 -0.0158 0.0106  121  VAL   B C   
5950 O  O   . VAL   B 121 ? 0.1542 0.1274 0.1395 -0.0305 -0.0192 0.0055  121  VAL   B O   
5951 C  CB  . VAL   B 121 ? 0.1724 0.1721 0.1355 -0.0037 -0.0234 0.0197  121  VAL   B CB  
5952 C  CG1 . VAL   B 121 ? 0.1770 0.1810 0.1652 -0.0099 -0.0087 0.0186  121  VAL   B CG1 
5953 C  CG2 . VAL   B 121 ? 0.1911 0.1966 0.1344 0.0025  -0.0152 0.0015  121  VAL   B CG2 
5963 N  N   . LEU   B 122 ? 0.1322 0.1262 0.1182 -0.0176 -0.0202 0.0070  122  LEU   B N   
5964 C  CA  . LEU   B 122 ? 0.1297 0.1318 0.1105 -0.0195 -0.0122 0.0044  122  LEU   B CA  
5965 C  C   . LEU   B 122 ? 0.1279 0.1200 0.1206 -0.0246 -0.0115 0.0037  122  LEU   B C   
5966 O  O   . LEU   B 122 ? 0.1358 0.1218 0.1440 -0.0288 -0.0200 -0.0026 122  LEU   B O   
5967 C  CB  . LEU   B 122 ? 0.1506 0.1451 0.1416 -0.0071 -0.0207 0.0061  122  LEU   B CB  
5968 C  CG  . LEU   B 122 ? 0.1417 0.1495 0.1414 -0.0166 -0.0069 0.0021  122  LEU   B CG  
5969 C  CD1 . LEU   B 122 ? 0.1487 0.1666 0.1534 -0.0179 -0.0127 0.0020  122  LEU   B CD1 
5970 C  CD2 . LEU   B 122 ? 0.1431 0.1478 0.1206 -0.0110 -0.0020 -0.0081 122  LEU   B CD2 
5982 N  N   . LEU   B 123 ? 0.1296 0.1098 0.1180 -0.0222 -0.0098 0.0022  123  LEU   B N   
5983 C  CA  . LEU   B 123 ? 0.1345 0.1143 0.1174 -0.0180 -0.0151 -0.0009 123  LEU   B CA  
5984 C  C   . LEU   B 123 ? 0.1273 0.1112 0.1129 -0.0226 -0.0111 0.0008  123  LEU   B C   
5985 O  O   . LEU   B 123 ? 0.1399 0.1167 0.1226 -0.0279 -0.0132 0.0038  123  LEU   B O   
5986 C  CB  . LEU   B 123 ? 0.1343 0.1201 0.1234 -0.0188 -0.0071 -0.0034 123  LEU   B CB  
5987 C  CG  . LEU   B 123 ? 0.1338 0.1242 0.1404 -0.0118 -0.0019 0.0043  123  LEU   B CG  
5988 C  CD1 . LEU   B 123 ? 0.1465 0.1282 0.1543 -0.0163 -0.0005 -0.0091 123  LEU   B CD1 
5989 C  CD2 . LEU   B 123 ? 0.1397 0.1305 0.1627 -0.0127 0.0066  0.0140  123  LEU   B CD2 
6001 N  N   . ALA   B 124 ? 0.1244 0.1100 0.1143 -0.0187 -0.0009 -0.0025 124  ALA   B N   
6002 C  CA  . ALA   B 124 ? 0.1213 0.1082 0.1210 -0.0114 -0.0061 -0.0063 124  ALA   B CA  
6003 C  C   . ALA   B 124 ? 0.1200 0.1080 0.1181 -0.0122 -0.0052 -0.0067 124  ALA   B C   
6004 O  O   . ALA   B 124 ? 0.1296 0.1146 0.1276 -0.0114 -0.0051 -0.0013 124  ALA   B O   
6005 C  CB  . ALA   B 124 ? 0.1278 0.1145 0.1337 -0.0041 0.0059  -0.0016 124  ALA   B CB  
6011 N  N   . PRO   B 125 ? 0.1260 0.1116 0.1188 -0.0131 -0.0089 0.0070  125  PRO   B N   
6012 C  CA  . PRO   B 125 ? 0.1363 0.1177 0.1383 -0.0123 -0.0073 0.0152  125  PRO   B CA  
6013 C  C   . PRO   B 125 ? 0.1287 0.1113 0.1506 -0.0110 -0.0017 0.0052  125  PRO   B C   
6014 O  O   . PRO   B 125 ? 0.1328 0.1096 0.1698 -0.0087 0.0036  0.0134  125  PRO   B O   
6015 C  CB  . PRO   B 125 ? 0.1395 0.1416 0.1552 -0.0213 -0.0178 0.0326  125  PRO   B CB  
6016 C  CG  . PRO   B 125 ? 0.1489 0.1415 0.1417 -0.0282 -0.0206 0.0162  125  PRO   B CG  
6017 C  CD  . PRO   B 125 ? 0.1405 0.1218 0.1155 -0.0246 -0.0059 0.0022  125  PRO   B CD  
6025 N  N   . LEU   B 126 ? 0.1340 0.1076 0.1707 -0.0133 0.0121  0.0078  126  LEU   B N   
6026 C  CA  . LEU   B 126 ? 0.1413 0.1166 0.1776 -0.0114 0.0205  0.0111  126  LEU   B CA  
6027 C  C   . LEU   B 126 ? 0.1347 0.1213 0.1808 0.0018  0.0235  0.0151  126  LEU   B C   
6028 O  O   . LEU   B 126 ? 0.1565 0.1488 0.1966 0.0190  0.0024  -0.0016 126  LEU   B O   
6029 C  CB  . LEU   B 126 ? 0.1565 0.1192 0.2082 -0.0197 0.0293  0.0068  126  LEU   B CB  
6030 C  CG  . LEU   B 126 ? 0.1719 0.1288 0.2175 -0.0227 0.0323  -0.0109 126  LEU   B CG  
6031 C  CD1 . LEU   B 126 ? 0.1834 0.1342 0.2596 -0.0198 0.0197  -0.0190 126  LEU   B CD1 
6032 C  CD2 . LEU   B 126 ? 0.1728 0.1383 0.2096 -0.0333 0.0188  -0.0128 126  LEU   B CD2 
6044 N  N   . LEU   B 127 ? 0.1376 0.1128 0.1749 0.0044  0.0275  0.0117  127  LEU   B N   
6045 C  CA  . LEU   B 127 ? 0.1322 0.1204 0.1818 -0.0080 0.0206  0.0175  127  LEU   B CA  
6046 C  C   . LEU   B 127 ? 0.1305 0.1185 0.1783 -0.0028 0.0224  0.0162  127  LEU   B C   
6047 O  O   . LEU   B 127 ? 0.1374 0.1207 0.1790 -0.0123 0.0123  0.0179  127  LEU   B O   
6048 C  CB  . LEU   B 127 ? 0.1422 0.1197 0.1919 0.0004  0.0241  0.0253  127  LEU   B CB  
6049 C  CG  . LEU   B 127 ? 0.1580 0.1250 0.2054 0.0029  0.0234  0.0182  127  LEU   B CG  
6050 C  CD1 . LEU   B 127 ? 0.1616 0.1196 0.2011 0.0046  0.0226  0.0133  127  LEU   B CD1 
6051 C  CD2 . LEU   B 127 ? 0.1548 0.1324 0.2161 -0.0091 0.0284  0.0248  127  LEU   B CD2 
6063 N  N   . SER   B 128 ? 0.1336 0.1181 0.1751 0.0037  0.0052  0.0151  128  SER   B N   
6064 C  CA  . SER   B 128 ? 0.1440 0.1247 0.1762 0.0102  0.0026  0.0169  128  SER   B CA  
6065 C  C   . SER   B 128 ? 0.1594 0.1323 0.2017 0.0109  -0.0120 0.0160  128  SER   B C   
6066 O  O   . SER   B 128 ? 0.1785 0.1331 0.2306 0.0091  -0.0128 0.0296  128  SER   B O   
6067 C  CB  . SER   B 128 ? 0.1551 0.1307 0.1693 0.0061  0.0060  0.0231  128  SER   B CB  
6068 O  OG  . SER   B 128 ? 0.1605 0.1438 0.1826 0.0067  0.0075  0.0276  128  SER   B OG  
6074 N  N   . ALA   B 129 ? 0.1703 0.1347 0.2253 0.0306  -0.0080 -0.0020 129  ALA   B N   
6075 C  CA  . ALA   B 129 ? 0.1856 0.1424 0.2347 0.0302  -0.0147 -0.0143 129  ALA   B CA  
6076 C  C   . ALA   B 129 ? 0.1730 0.1382 0.2189 0.0238  0.0011  0.0024  129  ALA   B C   
6077 O  O   . ALA   B 129 ? 0.1615 0.1418 0.2107 0.0188  -0.0036 0.0118  129  ALA   B O   
6078 C  CB  . ALA   B 129 ? 0.2063 0.1610 0.2600 0.0353  -0.0107 -0.0196 129  ALA   B CB  
6084 N  N   . GLY   B 130 ? 0.1699 0.1290 0.2215 0.0245  0.0137  -0.0038 130  GLY   B N   
6085 C  CA  . GLY   B 130 ? 0.1714 0.1409 0.2354 0.0230  0.0300  -0.0031 130  GLY   B CA  
6086 C  C   . GLY   B 130 ? 0.1709 0.1398 0.2343 0.0147  0.0196  0.0092  130  GLY   B C   
6087 O  O   . GLY   B 130 ? 0.1842 0.1500 0.2355 0.0153  0.0124  0.0130  130  GLY   B O   
6091 N  N   . ILE   B 131 ? 0.1621 0.1554 0.2389 0.0265  0.0257  0.0108  131  ILE   B N   
6092 C  CA  . ILE   B 131 ? 0.1824 0.1715 0.2343 0.0277  0.0146  0.0255  131  ILE   B CA  
6093 C  C   . ILE   B 131 ? 0.1999 0.1648 0.2082 0.0179  0.0088  0.0322  131  ILE   B C   
6094 O  O   . ILE   B 131 ? 0.2247 0.1769 0.2125 0.0197  -0.0138 0.0342  131  ILE   B O   
6095 C  CB  . ILE   B 131 ? 0.1879 0.2091 0.2681 0.0249  0.0142  0.0248  131  ILE   B CB  
6096 C  CG1 . ILE   B 131 ? 0.1916 0.2265 0.2740 0.0050  0.0219  0.0251  131  ILE   B CG1 
6097 C  CG2 . ILE   B 131 ? 0.1880 0.2276 0.2901 0.0302  0.0165  0.0175  131  ILE   B CG2 
6098 C  CD1 . ILE   B 131 ? 0.1967 0.2440 0.2840 -0.0127 0.0193  0.0305  131  ILE   B CD1 
6110 N  N   . PHE   B 132 ? 0.1859 0.1460 0.1948 0.0160  0.0252  0.0242  132  PHE   B N   
6111 C  CA  . PHE   B 132 ? 0.1934 0.1482 0.1872 0.0056  0.0395  0.0184  132  PHE   B CA  
6112 C  C   . PHE   B 132 ? 0.2087 0.1618 0.2055 0.0089  0.0450  0.0174  132  PHE   B C   
6113 O  O   . PHE   B 132 ? 0.2238 0.1839 0.2395 0.0039  0.0541  0.0188  132  PHE   B O   
6114 C  CB  . PHE   B 132 ? 0.1792 0.1452 0.1722 0.0092  0.0334  0.0216  132  PHE   B CB  
6115 C  CG  . PHE   B 132 ? 0.1742 0.1462 0.1696 0.0171  0.0235  0.0131  132  PHE   B CG  
6116 C  CD1 . PHE   B 132 ? 0.1784 0.1441 0.2065 0.0152  0.0252  0.0116  132  PHE   B CD1 
6117 C  CD2 . PHE   B 132 ? 0.1742 0.1505 0.1537 0.0204  0.0224  0.0211  132  PHE   B CD2 
6118 C  CE1 . PHE   B 132 ? 0.1839 0.1508 0.2162 0.0121  0.0208  0.0126  132  PHE   B CE1 
6119 C  CE2 . PHE   B 132 ? 0.1824 0.1539 0.1584 0.0218  0.0052  0.0196  132  PHE   B CE2 
6120 C  CZ  . PHE   B 132 ? 0.1869 0.1515 0.1986 0.0121  0.0048  0.0206  132  PHE   B CZ  
6130 N  N   . GLY   B 133 ? 0.2070 0.1529 0.1994 0.0090  0.0325  0.0293  133  GLY   B N   
6131 C  CA  . GLY   B 133 ? 0.2165 0.1633 0.2157 -0.0083 0.0286  0.0384  133  GLY   B CA  
6132 C  C   . GLY   B 133 ? 0.2167 0.1689 0.2210 -0.0242 0.0327  0.0425  133  GLY   B C   
6133 O  O   . GLY   B 133 ? 0.2312 0.1840 0.2705 -0.0388 0.0353  0.0558  133  GLY   B O   
6137 N  N   . ALA   B 134 ? 0.2017 0.1676 0.2047 -0.0273 0.0267  0.0215  134  ALA   B N   
6138 C  CA  . ALA   B 134 ? 0.1990 0.1686 0.2214 -0.0204 0.0356  0.0126  134  ALA   B CA  
6139 C  C   . ALA   B 134 ? 0.2069 0.1599 0.2199 -0.0083 0.0335  0.0218  134  ALA   B C   
6140 O  O   . ALA   B 134 ? 0.2069 0.1771 0.2381 0.0054  0.0264  0.0125  134  ALA   B O   
6141 C  CB  . ALA   B 134 ? 0.1991 0.1685 0.2463 -0.0096 0.0208  0.0020  134  ALA   B CB  
6147 N  N   . ASP   B 135 ? 0.2187 0.1503 0.2148 -0.0091 0.0194  0.0288  135  ASP   B N   
6148 C  CA  . ASP   B 135 ? 0.2339 0.1421 0.2347 -0.0087 0.0030  0.0309  135  ASP   B CA  
6149 C  C   . ASP   B 135 ? 0.2136 0.1342 0.2237 -0.0024 0.0060  0.0210  135  ASP   B C   
6150 O  O   . ASP   B 135 ? 0.2058 0.1332 0.2314 -0.0056 0.0129  0.0246  135  ASP   B O   
6151 C  CB  . ASP   B 135 ? 0.2649 0.1566 0.2686 -0.0298 -0.0011 0.0317  135  ASP   B CB  
6152 C  CG  . ASP   B 135 ? 0.2909 0.1571 0.3087 -0.0488 0.0005  0.0304  135  ASP   B CG  
6153 O  OD1 . ASP   B 135 ? 0.2990 0.1469 0.3034 -0.0351 -0.0001 0.0212  135  ASP   B OD1 
6154 O  OD2 . ASP   B 135 ? 0.3099 0.1902 0.3590 -0.0658 -0.0015 0.0082  135  ASP   B OD2 
6159 N  N   . PRO   B 136 ? 0.2083 0.1384 0.2342 0.0164  -0.0012 0.0187  136  PRO   B N   
6160 C  CA  . PRO   B 136 ? 0.1873 0.1364 0.2366 0.0160  -0.0051 0.0062  136  PRO   B CA  
6161 C  C   . PRO   B 136 ? 0.1710 0.1228 0.2377 0.0138  -0.0020 -0.0016 136  PRO   B C   
6162 O  O   . PRO   B 136 ? 0.1540 0.1191 0.2265 0.0097  -0.0029 0.0038  136  PRO   B O   
6163 C  CB  . PRO   B 136 ? 0.1901 0.1559 0.2579 0.0306  -0.0045 -0.0006 136  PRO   B CB  
6164 C  CG  . PRO   B 136 ? 0.2078 0.1590 0.2669 0.0316  -0.0028 0.0045  136  PRO   B CG  
6165 C  CD  . PRO   B 136 ? 0.2138 0.1529 0.2596 0.0336  0.0012  0.0109  136  PRO   B CD  
6173 N  N   . ILE   B 137 ? 0.1836 0.1146 0.2458 0.0111  -0.0084 -0.0007 137  ILE   B N   
6174 C  CA  . ILE   B 137 ? 0.1918 0.1112 0.2620 -0.0077 0.0004  -0.0006 137  ILE   B CA  
6175 C  C   . ILE   B 137 ? 0.1835 0.1169 0.2498 -0.0109 0.0089  0.0126  137  ILE   B C   
6176 O  O   . ILE   B 137 ? 0.1678 0.1226 0.2515 -0.0127 0.0037  0.0111  137  ILE   B O   
6177 C  CB  . ILE   B 137 ? 0.2170 0.1209 0.3078 -0.0063 -0.0040 0.0041  137  ILE   B CB  
6178 C  CG1 . ILE   B 137 ? 0.2427 0.1400 0.3570 -0.0018 -0.0026 -0.0129 137  ILE   B CG1 
6179 C  CG2 . ILE   B 137 ? 0.2228 0.1232 0.3213 -0.0278 -0.0039 0.0133  137  ILE   B CG2 
6180 C  CD1 . ILE   B 137 ? 0.2627 0.1660 0.3940 0.0093  -0.0040 -0.0116 137  ILE   B CD1 
6192 N  N   . HIS   B 138 ? 0.1916 0.1175 0.2433 -0.0097 0.0180  0.0155  138  HIS   B N   
6193 C  CA  . HIS   B 138 ? 0.1940 0.1268 0.2393 -0.0067 0.0358  0.0178  138  HIS   B CA  
6194 C  C   . HIS   B 138 ? 0.1713 0.1278 0.2277 -0.0036 0.0317  0.0202  138  HIS   B C   
6195 O  O   . HIS   B 138 ? 0.1623 0.1336 0.2428 -0.0010 0.0310  0.0339  138  HIS   B O   
6196 C  CB  . HIS   B 138 ? 0.2188 0.1415 0.2578 -0.0049 0.0525  0.0189  138  HIS   B CB  
6197 C  CG  . HIS   B 138 ? 0.2390 0.1563 0.2691 -0.0095 0.0660  0.0360  138  HIS   B CG  
6198 N  ND1 . HIS   B 138 ? 0.2479 0.1729 0.2945 -0.0069 0.0765  0.0315  138  HIS   B ND1 
6199 C  CD2 . HIS   B 138 ? 0.2534 0.1659 0.2647 -0.0079 0.0772  0.0258  138  HIS   B CD2 
6200 C  CE1 . HIS   B 138 ? 0.2508 0.1744 0.2911 -0.0035 0.0810  0.0310  138  HIS   B CE1 
6201 N  NE2 . HIS   B 138 ? 0.2570 0.1657 0.2764 -0.0008 0.0816  0.0251  138  HIS   B NE2 
6209 N  N   . SER   B 139 ? 0.1673 0.1179 0.2243 0.0029  0.0303  0.0103  139  SER   B N   
6210 C  CA  . SER   B 139 ? 0.1610 0.1094 0.2096 0.0002  0.0186  -0.0006 139  SER   B CA  
6211 C  C   . SER   B 139 ? 0.1370 0.1039 0.2065 0.0001  0.0147  0.0014  139  SER   B C   
6212 O  O   . SER   B 139 ? 0.1459 0.1081 0.2021 0.0024  0.0113  0.0057  139  SER   B O   
6213 C  CB  . SER   B 139 ? 0.1698 0.1126 0.2082 0.0039  0.0103  0.0024  139  SER   B CB  
6214 O  OG  . SER   B 139 ? 0.1655 0.1156 0.2120 0.0020  -0.0048 0.0145  139  SER   B OG  
6220 N  N   . LEU   B 140 ? 0.1401 0.1043 0.2151 -0.0003 0.0172  -0.0020 140  LEU   B N   
6221 C  CA  . LEU   B 140 ? 0.1374 0.1073 0.2156 -0.0032 0.0125  0.0036  140  LEU   B CA  
6222 C  C   . LEU   B 140 ? 0.1317 0.1076 0.2247 -0.0051 0.0112  -0.0025 140  LEU   B C   
6223 O  O   . LEU   B 140 ? 0.1334 0.1110 0.2199 -0.0050 0.0026  0.0009  140  LEU   B O   
6224 C  CB  . LEU   B 140 ? 0.1366 0.1086 0.2222 -0.0099 0.0173  -0.0051 140  LEU   B CB  
6225 C  CG  . LEU   B 140 ? 0.1436 0.1091 0.2157 -0.0114 0.0056  0.0009  140  LEU   B CG  
6226 C  CD1 . LEU   B 140 ? 0.1528 0.1214 0.2244 -0.0116 0.0080  -0.0042 140  LEU   B CD1 
6227 C  CD2 . LEU   B 140 ? 0.1609 0.1177 0.2304 -0.0075 0.0035  -0.0126 140  LEU   B CD2 
6239 N  N   . ARG   B 141 ? 0.1281 0.1079 0.2294 -0.0029 0.0128  -0.0030 141  ARG   B N   
6240 C  CA  . ARG   B 141 ? 0.1310 0.1105 0.2656 -0.0094 0.0266  -0.0063 141  ARG   B CA  
6241 C  C   . ARG   B 141 ? 0.1254 0.1095 0.2482 -0.0120 0.0161  -0.0029 141  ARG   B C   
6242 O  O   . ARG   B 141 ? 0.1293 0.1160 0.2436 -0.0146 0.0049  -0.0121 141  ARG   B O   
6243 C  CB  . ARG   B 141 ? 0.1532 0.1163 0.3024 -0.0156 0.0318  -0.0027 141  ARG   B CB  
6244 C  CG  . ARG   B 141 ? 0.1853 0.1436 0.3253 -0.0156 0.0270  -0.0000 141  ARG   B CG  
6245 C  CD  . ARG   B 141 ? 0.2211 0.1700 0.3326 -0.0120 0.0111  -0.0124 141  ARG   B CD  
6246 N  NE  . ARG   B 141 ? 0.2403 0.1690 0.3255 -0.0245 0.0156  -0.0179 141  ARG   B NE  
6247 C  CZ  . ARG   B 141 ? 0.2511 0.1481 0.3127 -0.0213 0.0214  -0.0316 141  ARG   B CZ  
6248 N  NH1 . ARG   B 141 ? 0.2614 0.1447 0.3079 -0.0198 0.0250  -0.0308 141  ARG   B NH1 
6249 N  NH2 . ARG   B 141 ? 0.2576 0.1606 0.3177 -0.0088 0.0116  -0.0176 141  ARG   B NH2 
6263 N  N   . VAL   B 142 ? 0.1295 0.1082 0.2342 -0.0087 0.0138  -0.0056 142  VAL   B N   
6264 C  CA  . VAL   B 142 ? 0.1223 0.1072 0.2333 -0.0093 0.0189  -0.0065 142  VAL   B CA  
6265 C  C   . VAL   B 142 ? 0.1231 0.1074 0.2339 -0.0042 0.0180  -0.0119 142  VAL   B C   
6266 O  O   . VAL   B 142 ? 0.1313 0.1069 0.2387 0.0000  0.0198  -0.0076 142  VAL   B O   
6267 C  CB  . VAL   B 142 ? 0.1338 0.1196 0.2406 -0.0008 0.0223  0.0068  142  VAL   B CB  
6268 C  CG1 . VAL   B 142 ? 0.1356 0.1197 0.2417 0.0097  0.0308  0.0048  142  VAL   B CG1 
6269 C  CG2 . VAL   B 142 ? 0.1569 0.1193 0.2548 -0.0022 0.0186  0.0120  142  VAL   B CG2 
6279 N  N   . CYS   B 143 ? 0.1219 0.1072 0.2069 -0.0027 0.0120  0.0042  143  CYS   B N   
6280 C  CA  . CYS   B 143 ? 0.1195 0.1117 0.2118 -0.0087 0.0073  0.0013  143  CYS   B CA  
6281 C  C   . CYS   B 143 ? 0.1183 0.1129 0.2172 -0.0044 0.0156  -0.0019 143  CYS   B C   
6282 O  O   . CYS   B 143 ? 0.1217 0.1132 0.2218 -0.0069 0.0048  -0.0012 143  CYS   B O   
6283 C  CB  . CYS   B 143 ? 0.1253 0.1197 0.2062 -0.0052 0.0005  -0.0001 143  CYS   B CB  
6284 S  SG  . CYS   B 143 ? 0.1329 0.1316 0.2038 -0.0044 0.0114  0.0015  143  CYS   B SG  
6290 N  N   . VAL   B 144 ? 0.1230 0.1147 0.2219 -0.0055 0.0069  -0.0151 144  VAL   B N   
6291 C  CA  . VAL   B 144 ? 0.1315 0.1184 0.2519 -0.0122 -0.0025 -0.0190 144  VAL   B CA  
6292 C  C   . VAL   B 144 ? 0.1292 0.1180 0.2543 -0.0097 -0.0019 -0.0033 144  VAL   B C   
6293 O  O   . VAL   B 144 ? 0.1351 0.1402 0.2673 0.0020  0.0026  0.0156  144  VAL   B O   
6294 C  CB  . VAL   B 144 ? 0.1502 0.1271 0.3190 -0.0128 -0.0136 -0.0306 144  VAL   B CB  
6295 C  CG1 . VAL   B 144 ? 0.1725 0.1625 0.3523 -0.0101 -0.0213 -0.0233 144  VAL   B CG1 
6296 C  CG2 . VAL   B 144 ? 0.1574 0.1282 0.3166 0.0007  -0.0289 -0.0378 144  VAL   B CG2 
6306 N  N   . ASP   B 145 ? 0.1293 0.1196 0.2596 -0.0090 -0.0001 -0.0112 145  ASP   B N   
6307 C  CA  . ASP   B 145 ? 0.1271 0.1197 0.2772 -0.0093 0.0100  -0.0149 145  ASP   B CA  
6308 C  C   . ASP   B 145 ? 0.1221 0.1218 0.2562 -0.0058 0.0140  -0.0071 145  ASP   B C   
6309 O  O   . ASP   B 145 ? 0.1269 0.1368 0.3126 -0.0120 0.0162  -0.0234 145  ASP   B O   
6310 C  CB  . ASP   B 145 ? 0.1410 0.1264 0.3185 -0.0151 0.0239  -0.0115 145  ASP   B CB  
6311 C  CG  . ASP   B 145 ? 0.1572 0.1347 0.3657 -0.0234 0.0333  -0.0037 145  ASP   B CG  
6312 O  OD1 . ASP   B 145 ? 0.1621 0.1345 0.3746 -0.0241 0.0015  -0.0173 145  ASP   B OD1 
6313 O  OD2 . ASP   B 145 ? 0.1884 0.1427 0.4042 -0.0278 0.0470  -0.0003 145  ASP   B OD2 
6318 N  N   . THR   B 146 ? 0.1145 0.1151 0.2172 -0.0080 0.0082  -0.0056 146  THR   B N   
6319 C  CA  . THR   B 146 ? 0.1246 0.1144 0.1997 -0.0041 0.0103  -0.0036 146  THR   B CA  
6320 C  C   . THR   B 146 ? 0.1248 0.1122 0.1943 -0.0024 0.0080  -0.0021 146  THR   B C   
6321 O  O   . THR   B 146 ? 0.1278 0.1151 0.1987 -0.0041 0.0001  -0.0048 146  THR   B O   
6322 C  CB  . THR   B 146 ? 0.1287 0.1160 0.2090 -0.0025 0.0194  0.0037  146  THR   B CB  
6323 O  OG1 . THR   B 146 ? 0.1326 0.1086 0.2135 -0.0029 0.0223  0.0075  146  THR   B OG1 
6324 C  CG2 . THR   B 146 ? 0.1365 0.1193 0.2047 -0.0032 0.0199  -0.0002 146  THR   B CG2 
6332 N  N   . VAL   B 147 ? 0.1306 0.1132 0.1879 -0.0026 0.0157  0.0020  147  VAL   B N   
6333 C  CA  . VAL   B 147 ? 0.1256 0.1100 0.1724 -0.0093 0.0011  -0.0105 147  VAL   B CA  
6334 C  C   . VAL   B 147 ? 0.1202 0.1153 0.1866 -0.0157 -0.0023 -0.0040 147  VAL   B C   
6335 O  O   . VAL   B 147 ? 0.1343 0.1250 0.1888 -0.0185 -0.0227 -0.0090 147  VAL   B O   
6336 C  CB  . VAL   B 147 ? 0.1263 0.1239 0.1591 -0.0065 -0.0046 -0.0001 147  VAL   B CB  
6337 C  CG1 . VAL   B 147 ? 0.1275 0.1412 0.1599 -0.0084 -0.0067 0.0061  147  VAL   B CG1 
6338 C  CG2 . VAL   B 147 ? 0.1329 0.1246 0.1701 -0.0125 -0.0001 0.0014  147  VAL   B CG2 
6348 N  N   . ARG   B 148 ? 0.1232 0.1140 0.1864 -0.0045 -0.0042 -0.0057 148  ARG   B N   
6349 C  CA  . ARG   B 148 ? 0.1287 0.1209 0.1785 -0.0052 -0.0174 -0.0112 148  ARG   B CA  
6350 C  C   . ARG   B 148 ? 0.1355 0.1320 0.1678 -0.0046 -0.0202 -0.0102 148  ARG   B C   
6351 O  O   . ARG   B 148 ? 0.1567 0.1643 0.1691 -0.0223 -0.0306 -0.0054 148  ARG   B O   
6352 C  CB  . ARG   B 148 ? 0.1320 0.1312 0.1964 -0.0019 -0.0235 -0.0166 148  ARG   B CB  
6353 C  CG  . ARG   B 148 ? 0.1373 0.1467 0.2063 -0.0097 -0.0170 -0.0320 148  ARG   B CG  
6354 C  CD  . ARG   B 148 ? 0.1429 0.1633 0.2137 0.0057  -0.0223 -0.0347 148  ARG   B CD  
6355 N  NE  . ARG   B 148 ? 0.1446 0.1609 0.1983 0.0219  -0.0216 -0.0305 148  ARG   B NE  
6356 C  CZ  . ARG   B 148 ? 0.1346 0.1545 0.1742 0.0139  -0.0170 -0.0192 148  ARG   B CZ  
6357 N  NH1 . ARG   B 148 ? 0.1358 0.1592 0.1760 -0.0045 -0.0021 -0.0125 148  ARG   B NH1 
6358 N  NH2 . ARG   B 148 ? 0.1601 0.1431 0.1692 0.0150  -0.0144 -0.0144 148  ARG   B NH2 
6372 N  N   . THR   B 149 ? 0.1350 0.1306 0.1705 -0.0122 -0.0230 -0.0022 149  THR   B N   
6373 C  CA  . THR   B 149 ? 0.1386 0.1305 0.1626 -0.0147 -0.0262 0.0076  149  THR   B CA  
6374 C  C   . THR   B 149 ? 0.1358 0.1264 0.1469 -0.0169 -0.0246 0.0054  149  THR   B C   
6375 O  O   . THR   B 149 ? 0.1481 0.1255 0.1648 -0.0218 -0.0123 0.0017  149  THR   B O   
6376 C  CB  . THR   B 149 ? 0.1388 0.1259 0.1642 -0.0173 -0.0184 -0.0022 149  THR   B CB  
6377 O  OG1 . THR   B 149 ? 0.1429 0.1307 0.1578 -0.0216 -0.0227 -0.0018 149  THR   B OG1 
6378 C  CG2 . THR   B 149 ? 0.1427 0.1290 0.1748 -0.0065 -0.0102 0.0027  149  THR   B CG2 
6386 N  N   . ASN   B 150 ? 0.1439 0.1244 0.1459 -0.0167 -0.0234 -0.0011 150  ASN   B N   
6387 C  CA  . ASN   B 150 ? 0.1490 0.1376 0.1456 -0.0200 -0.0202 -0.0092 150  ASN   B CA  
6388 C  C   . ASN   B 150 ? 0.1387 0.1343 0.1509 -0.0124 -0.0233 -0.0047 150  ASN   B C   
6389 O  O   . ASN   B 150 ? 0.1497 0.1315 0.1768 -0.0264 -0.0418 -0.0059 150  ASN   B O   
6390 C  CB  . ASN   B 150 ? 0.1732 0.1710 0.1599 -0.0196 -0.0270 -0.0013 150  ASN   B CB  
6391 C  CG  . ASN   B 150 ? 0.1964 0.2089 0.1938 -0.0171 -0.0305 0.0140  150  ASN   B CG  
6392 O  OD1 . ASN   B 150 ? 0.2107 0.2273 0.2078 -0.0280 -0.0473 0.0091  150  ASN   B OD1 
6393 N  ND2 . ASN   B 150 ? 0.2054 0.2278 0.2336 -0.0015 -0.0387 0.0482  150  ASN   B ND2 
6400 N  N   . VAL   B 151 ? 0.1330 0.1295 0.1467 -0.0165 -0.0181 -0.0049 151  VAL   B N   
6401 C  CA  . VAL   B 151 ? 0.1343 0.1339 0.1514 -0.0181 -0.0159 -0.0042 151  VAL   B CA  
6402 C  C   . VAL   B 151 ? 0.1367 0.1241 0.1439 -0.0247 -0.0155 -0.0067 151  VAL   B C   
6403 O  O   . VAL   B 151 ? 0.1443 0.1334 0.1665 -0.0225 -0.0073 -0.0136 151  VAL   B O   
6404 C  CB  . VAL   B 151 ? 0.1553 0.1473 0.1651 -0.0074 -0.0133 -0.0099 151  VAL   B CB  
6405 C  CG1 . VAL   B 151 ? 0.1634 0.1465 0.1863 -0.0135 0.0054  -0.0222 151  VAL   B CG1 
6406 C  CG2 . VAL   B 151 ? 0.1663 0.1562 0.1647 -0.0002 -0.0184 0.0064  151  VAL   B CG2 
6416 N  N   . TYR   B 152 ? 0.1362 0.1122 0.1383 -0.0219 -0.0107 -0.0044 152  TYR   B N   
6417 C  CA  . TYR   B 152 ? 0.1369 0.1301 0.1362 -0.0231 -0.0091 -0.0085 152  TYR   B CA  
6418 C  C   . TYR   B 152 ? 0.1300 0.1198 0.1319 -0.0152 -0.0022 -0.0124 152  TYR   B C   
6419 O  O   . TYR   B 152 ? 0.1396 0.1208 0.1487 -0.0218 -0.0110 -0.0062 152  TYR   B O   
6420 C  CB  . TYR   B 152 ? 0.1477 0.1461 0.1443 -0.0215 -0.0048 -0.0004 152  TYR   B CB  
6421 C  CG  . TYR   B 152 ? 0.1625 0.1583 0.1354 -0.0350 -0.0110 -0.0051 152  TYR   B CG  
6422 C  CD1 . TYR   B 152 ? 0.1724 0.1669 0.1311 -0.0199 -0.0183 0.0034  152  TYR   B CD1 
6423 C  CD2 . TYR   B 152 ? 0.1837 0.1740 0.1416 -0.0329 -0.0126 -0.0077 152  TYR   B CD2 
6424 C  CE1 . TYR   B 152 ? 0.1875 0.1837 0.1505 -0.0173 -0.0191 0.0149  152  TYR   B CE1 
6425 C  CE2 . TYR   B 152 ? 0.1950 0.1914 0.1446 -0.0314 -0.0149 -0.0113 152  TYR   B CE2 
6426 C  CZ  . TYR   B 152 ? 0.1985 0.2035 0.1335 -0.0254 -0.0312 0.0108  152  TYR   B CZ  
6427 O  OH  . TYR   B 152 ? 0.2283 0.2390 0.1561 -0.0151 -0.0348 0.0097  152  TYR   B OH  
6437 N  N   . LEU   B 153 ? 0.1348 0.1177 0.1378 -0.0252 -0.0087 -0.0098 153  LEU   B N   
6438 C  CA  . LEU   B 153 ? 0.1383 0.1118 0.1219 -0.0178 -0.0029 -0.0073 153  LEU   B CA  
6439 C  C   . LEU   B 153 ? 0.1409 0.1136 0.1412 -0.0204 -0.0039 -0.0166 153  LEU   B C   
6440 O  O   . LEU   B 153 ? 0.1491 0.1345 0.1592 -0.0131 -0.0078 -0.0266 153  LEU   B O   
6441 C  CB  . LEU   B 153 ? 0.1408 0.1150 0.1473 -0.0225 0.0031  -0.0067 153  LEU   B CB  
6442 C  CG  . LEU   B 153 ? 0.1346 0.1216 0.1650 -0.0212 -0.0062 -0.0022 153  LEU   B CG  
6443 C  CD1 . LEU   B 153 ? 0.1448 0.1348 0.1838 -0.0244 0.0044  -0.0057 153  LEU   B CD1 
6444 C  CD2 . LEU   B 153 ? 0.1432 0.1386 0.1632 -0.0270 0.0058  0.0016  153  LEU   B CD2 
6456 N  N   . ALA   B 154 ? 0.1344 0.1171 0.1503 -0.0051 -0.0105 -0.0133 154  ALA   B N   
6457 C  CA  . ALA   B 154 ? 0.1476 0.1259 0.1723 -0.0007 -0.0131 -0.0274 154  ALA   B CA  
6458 C  C   . ALA   B 154 ? 0.1583 0.1267 0.1842 0.0037  -0.0235 -0.0303 154  ALA   B C   
6459 O  O   . ALA   B 154 ? 0.1910 0.1277 0.2009 0.0106  -0.0063 -0.0138 154  ALA   B O   
6460 C  CB  . ALA   B 154 ? 0.1472 0.1391 0.2056 -0.0024 -0.0147 -0.0358 154  ALA   B CB  
6466 N  N   . VAL   B 155 ? 0.1330 0.1184 0.1909 0.0004  -0.0065 -0.0192 155  VAL   B N   
6467 C  CA  . VAL   B 155 ? 0.1245 0.1214 0.1953 -0.0015 -0.0125 -0.0070 155  VAL   B CA  
6468 C  C   . VAL   B 155 ? 0.1271 0.1197 0.1954 -0.0010 -0.0094 -0.0205 155  VAL   B C   
6469 O  O   . VAL   B 155 ? 0.1465 0.1411 0.2318 0.0068  -0.0099 -0.0383 155  VAL   B O   
6470 C  CB  . VAL   B 155 ? 0.1310 0.1363 0.2303 -0.0032 -0.0124 0.0008  155  VAL   B CB  
6471 C  CG1 . VAL   B 155 ? 0.1324 0.1316 0.2400 -0.0093 -0.0121 -0.0088 155  VAL   B CG1 
6472 C  CG2 . VAL   B 155 ? 0.1319 0.1464 0.2629 -0.0002 -0.0118 0.0250  155  VAL   B CG2 
6482 N  N   . PHE   B 156 ? 0.1202 0.1310 0.2178 0.0055  -0.0012 -0.0214 156  PHE   B N   
6483 C  CA  . PHE   B 156 ? 0.1253 0.1372 0.2425 0.0107  -0.0047 -0.0181 156  PHE   B CA  
6484 C  C   . PHE   B 156 ? 0.1272 0.1415 0.2789 0.0155  -0.0090 -0.0410 156  PHE   B C   
6485 O  O   . PHE   B 156 ? 0.1492 0.1620 0.2969 0.0217  -0.0039 -0.0447 156  PHE   B O   
6486 C  CB  . PHE   B 156 ? 0.1316 0.1309 0.2424 0.0047  -0.0148 -0.0117 156  PHE   B CB  
6487 C  CG  . PHE   B 156 ? 0.1353 0.1377 0.2599 0.0003  -0.0147 0.0061  156  PHE   B CG  
6488 C  CD1 . PHE   B 156 ? 0.1391 0.1651 0.2930 0.0069  -0.0113 0.0347  156  PHE   B CD1 
6489 C  CD2 . PHE   B 156 ? 0.1397 0.1501 0.2559 0.0102  -0.0187 0.0071  156  PHE   B CD2 
6490 C  CE1 . PHE   B 156 ? 0.1422 0.1798 0.3127 0.0085  -0.0075 0.0360  156  PHE   B CE1 
6491 C  CE2 . PHE   B 156 ? 0.1435 0.1693 0.2828 0.0125  -0.0155 0.0115  156  PHE   B CE2 
6492 C  CZ  . PHE   B 156 ? 0.1360 0.1786 0.3022 0.0155  -0.0202 0.0214  156  PHE   B CZ  
6502 N  N   . ASP   B 157 ? 0.1288 0.1317 0.2977 0.0138  -0.0185 -0.0272 157  ASP   B N   
6503 C  CA  . ASP   B 157 ? 0.1403 0.1371 0.3328 0.0061  -0.0246 -0.0359 157  ASP   B CA  
6504 C  C   . ASP   B 157 ? 0.1359 0.1397 0.3385 0.0065  -0.0163 -0.0536 157  ASP   B C   
6505 O  O   . ASP   B 157 ? 0.1268 0.1396 0.3262 0.0034  -0.0168 -0.0368 157  ASP   B O   
6506 C  CB  . ASP   B 157 ? 0.1582 0.1526 0.3514 0.0066  -0.0453 -0.0206 157  ASP   B CB  
6507 C  CG  . ASP   B 157 ? 0.1893 0.1653 0.3774 0.0051  -0.0308 -0.0157 157  ASP   B CG  
6508 O  OD1 . ASP   B 157 ? 0.1974 0.1620 0.3910 0.0142  -0.0236 -0.0141 157  ASP   B OD1 
6509 O  OD2 . ASP   B 157 ? 0.2209 0.1858 0.4069 0.0025  -0.0123 -0.0129 157  ASP   B OD2 
6514 N  N   A LYS   B 158 ? 0.1421 0.1572 0.3401 0.0032  -0.0110 -0.0751 158  LYS   B N   
6515 N  N   B LYS   B 158 ? 0.1425 0.1583 0.3400 0.0061  -0.0096 -0.0746 158  LYS   B N   
6516 C  CA  A LYS   B 158 ? 0.1586 0.1745 0.3457 0.0026  -0.0098 -0.0867 158  LYS   B CA  
6517 C  CA  B LYS   B 158 ? 0.1591 0.1764 0.3452 0.0079  -0.0073 -0.0859 158  LYS   B CA  
6518 C  C   A LYS   B 158 ? 0.1569 0.1650 0.3537 0.0036  -0.0163 -0.0832 158  LYS   B C   
6519 C  C   B LYS   B 158 ? 0.1575 0.1660 0.3537 0.0069  -0.0144 -0.0821 158  LYS   B C   
6520 O  O   A LYS   B 158 ? 0.1571 0.1639 0.3502 -0.0041 -0.0163 -0.0954 158  LYS   B O   
6521 O  O   B LYS   B 158 ? 0.1582 0.1645 0.3508 0.0003  -0.0133 -0.0934 158  LYS   B O   
6522 C  CB  A LYS   B 158 ? 0.1806 0.2038 0.3450 0.0034  -0.0029 -0.0960 158  LYS   B CB  
6523 C  CB  B LYS   B 158 ? 0.1811 0.2070 0.3431 0.0125  0.0010  -0.0957 158  LYS   B CB  
6524 C  CG  A LYS   B 158 ? 0.2064 0.2334 0.3496 0.0038  0.0015  -0.0949 158  LYS   B CG  
6525 C  CG  B LYS   B 158 ? 0.2067 0.2371 0.3458 0.0157  0.0062  -0.0962 158  LYS   B CG  
6526 C  CD  A LYS   B 158 ? 0.2247 0.2643 0.3551 0.0034  0.0026  -0.0873 158  LYS   B CD  
6527 C  CD  B LYS   B 158 ? 0.2259 0.2690 0.3505 0.0169  0.0076  -0.0898 158  LYS   B CD  
6528 C  CE  A LYS   B 158 ? 0.2368 0.2866 0.3608 0.0045  0.0000  -0.0829 158  LYS   B CE  
6529 C  CE  B LYS   B 158 ? 0.2387 0.2905 0.3565 0.0205  0.0064  -0.0852 158  LYS   B CE  
6530 N  NZ  A LYS   B 158 ? 0.2343 0.2946 0.3579 -0.0001 -0.0023 -0.0824 158  LYS   B NZ  
6531 N  NZ  B LYS   B 158 ? 0.2390 0.2998 0.3564 0.0202  0.0076  -0.0819 158  LYS   B NZ  
6558 N  N   . ASN   B 159 ? 0.1594 0.1580 0.3699 0.0066  -0.0253 -0.0733 159  ASN   B N   
6559 C  CA  . ASN   B 159 ? 0.1703 0.1504 0.4031 0.0241  -0.0434 -0.0631 159  ASN   B CA  
6560 C  C   . ASN   B 159 ? 0.1566 0.1413 0.3910 0.0215  -0.0542 -0.0458 159  ASN   B C   
6561 O  O   . ASN   B 159 ? 0.1583 0.1382 0.3946 0.0039  -0.0568 -0.0388 159  ASN   B O   
6562 C  CB  . ASN   B 159 ? 0.1894 0.1598 0.4444 0.0355  -0.0459 -0.0660 159  ASN   B CB  
6563 C  CG  . ASN   B 159 ? 0.2157 0.1756 0.4755 0.0320  -0.0596 -0.0795 159  ASN   B CG  
6564 O  OD1 . ASN   B 159 ? 0.2340 0.1867 0.4848 0.0369  -0.0597 -0.0872 159  ASN   B OD1 
6565 N  ND2 . ASN   B 159 ? 0.2169 0.1875 0.4911 0.0344  -0.0688 -0.0716 159  ASN   B ND2 
6573 N  N   . LEU   B 160 ? 0.1460 0.1340 0.3623 0.0168  -0.0477 -0.0404 160  LEU   B N   
6574 C  CA  . LEU   B 160 ? 0.1433 0.1361 0.3246 0.0121  -0.0402 -0.0263 160  LEU   B CA  
6575 C  C   . LEU   B 160 ? 0.1378 0.1260 0.3115 0.0038  -0.0237 -0.0341 160  LEU   B C   
6576 O  O   . LEU   B 160 ? 0.1306 0.1285 0.2913 -0.0016 -0.0236 -0.0240 160  LEU   B O   
6577 C  CB  . LEU   B 160 ? 0.1399 0.1396 0.3036 0.0097  -0.0416 -0.0127 160  LEU   B CB  
6578 C  CG  . LEU   B 160 ? 0.1410 0.1537 0.2833 0.0138  -0.0349 -0.0005 160  LEU   B CG  
6579 C  CD1 . LEU   B 160 ? 0.1528 0.1721 0.2885 0.0010  -0.0204 -0.0112 160  LEU   B CD1 
6580 C  CD2 . LEU   B 160 ? 0.1481 0.1578 0.2841 0.0251  -0.0348 -0.0120 160  LEU   B CD2 
6592 N  N   . TYR   B 161 ? 0.1325 0.1358 0.3124 -0.0034 -0.0022 -0.0417 161  TYR   B N   
6593 C  CA  . TYR   B 161 ? 0.1370 0.1343 0.3004 -0.0105 0.0108  -0.0480 161  TYR   B CA  
6594 C  C   . TYR   B 161 ? 0.1433 0.1344 0.2897 -0.0053 0.0118  -0.0450 161  TYR   B C   
6595 O  O   . TYR   B 161 ? 0.1456 0.1307 0.2845 -0.0123 0.0045  -0.0458 161  TYR   B O   
6596 C  CB  . TYR   B 161 ? 0.1491 0.1407 0.3056 -0.0161 0.0267  -0.0500 161  TYR   B CB  
6597 C  CG  . TYR   B 161 ? 0.1700 0.1449 0.2941 -0.0224 0.0340  -0.0545 161  TYR   B CG  
6598 C  CD1 . TYR   B 161 ? 0.1750 0.1401 0.2879 -0.0339 0.0331  -0.0568 161  TYR   B CD1 
6599 C  CD2 . TYR   B 161 ? 0.1936 0.1553 0.2920 -0.0211 0.0286  -0.0535 161  TYR   B CD2 
6600 C  CE1 . TYR   B 161 ? 0.1936 0.1590 0.2898 -0.0351 0.0350  -0.0517 161  TYR   B CE1 
6601 C  CE2 . TYR   B 161 ? 0.2105 0.1670 0.3021 -0.0286 0.0307  -0.0457 161  TYR   B CE2 
6602 C  CZ  . TYR   B 161 ? 0.2107 0.1689 0.2919 -0.0403 0.0249  -0.0451 161  TYR   B CZ  
6603 O  OH  . TYR   B 161 ? 0.2393 0.1924 0.3102 -0.0453 0.0228  -0.0412 161  TYR   B OH  
6613 N  N   . ASP   B 162 ? 0.1468 0.1357 0.3034 -0.0014 -0.0043 -0.0555 162  ASP   B N   
6614 C  CA  . ASP   B 162 ? 0.1548 0.1405 0.3057 -0.0053 -0.0072 -0.0573 162  ASP   B CA  
6615 C  C   . ASP   B 162 ? 0.1551 0.1304 0.2967 -0.0144 -0.0047 -0.0494 162  ASP   B C   
6616 O  O   . ASP   B 162 ? 0.1639 0.1381 0.2994 -0.0184 -0.0152 -0.0337 162  ASP   B O   
6617 C  CB  . ASP   B 162 ? 0.1740 0.1582 0.3257 0.0038  -0.0130 -0.0706 162  ASP   B CB  
6618 C  CG  . ASP   B 162 ? 0.1771 0.1792 0.3425 0.0074  -0.0141 -0.0804 162  ASP   B CG  
6619 O  OD1 . ASP   B 162 ? 0.1807 0.1990 0.3279 0.0018  -0.0013 -0.0831 162  ASP   B OD1 
6620 O  OD2 . ASP   B 162 ? 0.1914 0.1985 0.3732 0.0259  -0.0063 -0.0754 162  ASP   B OD2 
6625 N  N   . LYS   B 163 ? 0.1522 0.1207 0.2902 -0.0114 -0.0143 -0.0347 163  LYS   B N   
6626 C  CA  . LYS   B 163 ? 0.1638 0.1304 0.2953 -0.0183 -0.0181 -0.0130 163  LYS   B CA  
6627 C  C   . LYS   B 163 ? 0.1374 0.1265 0.2817 -0.0207 -0.0171 -0.0068 163  LYS   B C   
6628 O  O   . LYS   B 163 ? 0.1414 0.1356 0.3051 -0.0248 -0.0135 -0.0087 163  LYS   B O   
6629 C  CB  . LYS   B 163 ? 0.2145 0.1653 0.3304 -0.0125 -0.0144 0.0123  163  LYS   B CB  
6630 C  CG  . LYS   B 163 ? 0.2951 0.2521 0.3968 -0.0179 -0.0031 0.0222  163  LYS   B CG  
6631 C  CD  . LYS   B 163 ? 0.3589 0.3327 0.4656 -0.0245 -0.0006 0.0222  163  LYS   B CD  
6632 C  CE  . LYS   B 163 ? 0.4063 0.3806 0.5110 -0.0297 0.0030  0.0239  163  LYS   B CE  
6633 N  NZ  . LYS   B 163 ? 0.4420 0.4214 0.5421 -0.0327 0.0047  0.0225  163  LYS   B NZ  
6647 N  N   . LEU   B 164 ? 0.1237 0.1260 0.2570 -0.0138 -0.0129 -0.0048 164  LEU   B N   
6648 C  CA  . LEU   B 164 ? 0.1241 0.1175 0.2405 -0.0103 -0.0159 -0.0023 164  LEU   B CA  
6649 C  C   . LEU   B 164 ? 0.1327 0.1175 0.2353 -0.0121 -0.0225 -0.0106 164  LEU   B C   
6650 O  O   . LEU   B 164 ? 0.1356 0.1453 0.2484 -0.0118 -0.0215 -0.0081 164  LEU   B O   
6651 C  CB  . LEU   B 164 ? 0.1211 0.1187 0.2291 -0.0092 -0.0194 -0.0025 164  LEU   B CB  
6652 C  CG  . LEU   B 164 ? 0.1322 0.1325 0.2362 -0.0102 -0.0125 -0.0044 164  LEU   B CG  
6653 C  CD1 . LEU   B 164 ? 0.1369 0.1309 0.2365 -0.0114 -0.0162 -0.0068 164  LEU   B CD1 
6654 C  CD2 . LEU   B 164 ? 0.1501 0.1700 0.2496 -0.0061 0.0064  -0.0201 164  LEU   B CD2 
6666 N  N   . VAL   B 165 ? 0.1580 0.1300 0.2517 -0.0165 -0.0233 -0.0208 165  VAL   B N   
6667 C  CA  . VAL   B 165 ? 0.1860 0.1386 0.2653 -0.0222 -0.0434 -0.0175 165  VAL   B CA  
6668 C  C   . VAL   B 165 ? 0.2133 0.1479 0.2965 -0.0334 -0.0718 -0.0137 165  VAL   B C   
6669 O  O   . VAL   B 165 ? 0.2284 0.1683 0.3060 -0.0391 -0.0757 -0.0045 165  VAL   B O   
6670 C  CB  . VAL   B 165 ? 0.2063 0.1564 0.2698 -0.0141 -0.0150 -0.0262 165  VAL   B CB  
6671 C  CG1 . VAL   B 165 ? 0.2243 0.1666 0.2901 -0.0176 -0.0123 -0.0236 165  VAL   B CG1 
6672 C  CG2 . VAL   B 165 ? 0.1999 0.1626 0.2681 -0.0063 0.0003  -0.0211 165  VAL   B CG2 
6682 N  N   . SER   B 166 ? 0.2284 0.1405 0.3286 -0.0328 -0.0796 -0.0306 166  SER   B N   
6683 C  CA  . SER   B 166 ? 0.2255 0.1417 0.3830 -0.0339 -0.0703 -0.0355 166  SER   B CA  
6684 C  C   . SER   B 166 ? 0.2136 0.1512 0.3977 -0.0390 -0.0697 -0.0140 166  SER   B C   
6685 O  O   . SER   B 166 ? 0.2146 0.1714 0.4264 -0.0492 -0.0821 -0.0299 166  SER   B O   
6686 C  CB  . SER   B 166 ? 0.2248 0.1524 0.4200 -0.0260 -0.0640 -0.0394 166  SER   B CB  
6687 O  OG  . SER   B 166 ? 0.2139 0.1503 0.4389 -0.0223 -0.0662 -0.0253 166  SER   B OG  
6693 N  N   . SER   B 167 ? 0.1992 0.1419 0.3706 -0.0382 -0.0641 0.0252  167  SER   B N   
6694 C  CA  . SER   B 167 ? 0.1895 0.1515 0.3506 -0.0390 -0.0438 0.0292  167  SER   B CA  
6695 C  C   . SER   B 167 ? 0.1814 0.1599 0.3303 -0.0511 -0.0418 0.0443  167  SER   B C   
6696 O  O   . SER   B 167 ? 0.1829 0.1737 0.3280 -0.0557 -0.0368 0.0422  167  SER   B O   
6697 C  CB  . SER   B 167 ? 0.1756 0.1611 0.3421 -0.0379 -0.0190 0.0341  167  SER   B CB  
6698 O  OG  . SER   B 167 ? 0.1718 0.1745 0.3207 -0.0252 -0.0103 0.0317  167  SER   B OG  
6704 N  N   . PHE   B 168 ? 0.1774 0.1578 0.3155 -0.0457 -0.0265 0.0516  168  PHE   B N   
6705 C  CA  . PHE   B 168 ? 0.1847 0.1524 0.2877 -0.0406 -0.0206 0.0326  168  PHE   B CA  
6706 C  C   . PHE   B 168 ? 0.1608 0.1421 0.2370 -0.0224 -0.0040 0.0139  168  PHE   B C   
6707 O  O   . PHE   B 168 ? 0.1893 0.1375 0.2386 0.0009  -0.0055 -0.0005 168  PHE   B O   
6708 C  CB  . PHE   B 168 ? 0.2007 0.1577 0.2987 -0.0462 -0.0400 0.0464  168  PHE   B CB  
6709 C  CG  . PHE   B 168 ? 0.2233 0.1446 0.2947 -0.0498 -0.0474 0.0221  168  PHE   B CG  
6710 C  CD1 . PHE   B 168 ? 0.2502 0.1506 0.3079 -0.0444 -0.0545 0.0168  168  PHE   B CD1 
6711 C  CD2 . PHE   B 168 ? 0.2167 0.1403 0.2926 -0.0413 -0.0498 0.0267  168  PHE   B CD2 
6712 C  CE1 . PHE   B 168 ? 0.2609 0.1551 0.3111 -0.0337 -0.0463 0.0228  168  PHE   B CE1 
6713 C  CE2 . PHE   B 168 ? 0.2376 0.1490 0.2993 -0.0301 -0.0567 0.0207  168  PHE   B CE2 
6714 C  CZ  . PHE   B 168 ? 0.2512 0.1463 0.3081 -0.0217 -0.0530 0.0298  168  PHE   B CZ  
6724 N  N   . LEU   B 169 ? 0.1650 0.1557 0.2304 0.0001  0.0050  -0.0012 169  LEU   B N   
6725 C  CA  . LEU   B 169 ? 0.1892 0.1861 0.2691 -0.0063 0.0002  -0.0181 169  LEU   B CA  
6726 C  C   . LEU   B 169 ? 0.2156 0.2116 0.3300 0.0103  -0.0051 -0.0478 169  LEU   B C   
6727 O  O   . LEU   B 169 ? 0.2330 0.2313 0.3874 0.0062  -0.0043 -0.0725 169  LEU   B O   
6728 C  CB  . LEU   B 169 ? 0.2097 0.2229 0.2820 -0.0106 -0.0083 0.0081  169  LEU   B CB  
6729 C  CG  . LEU   B 169 ? 0.2458 0.2584 0.3257 -0.0012 -0.0058 0.0115  169  LEU   B CG  
6730 C  CD1 . LEU   B 169 ? 0.2570 0.2775 0.3329 -0.0024 -0.0090 0.0260  169  LEU   B CD1 
6731 C  CD2 . LEU   B 169 ? 0.2425 0.2630 0.3333 0.0159  0.0089  -0.0052 169  LEU   B CD2 
6732 O  OXT . LEU   B 169 ? 0.2337 0.2276 0.3259 0.0426  -0.0013 -0.0466 169  LEU   B OXT 
6744 S  S   B DMS   C .   ? 0.3210 0.2959 0.2878 0.1246  0.0130  0.0227  301  DMS   A S   
6745 O  O   B DMS   C .   ? 0.3211 0.2970 0.2968 0.1298  0.0055  0.0204  301  DMS   A O   
6746 C  C1  B DMS   C .   ? 0.3237 0.3054 0.3091 0.1279  0.0141  0.0081  301  DMS   A C1  
6747 C  C2  B DMS   C .   ? 0.3250 0.3006 0.3112 0.1281  0.0156  0.0092  301  DMS   A C2  
6754 N  N2  B A1BAR D .   ? 0.1645 0.1686 0.1553 -0.0099 -0.0218 0.0459  302  A1BAR A N2  
6755 C  C3  B A1BAR D .   ? 0.1805 0.1726 0.1805 0.0050  -0.0177 0.0246  302  A1BAR A C3  
6756 C  C6  B A1BAR D .   ? 0.1778 0.1799 0.1739 0.0033  -0.0065 0.0164  302  A1BAR A C6  
6757 C  C9  B A1BAR D .   ? 0.1466 0.1415 0.1195 0.0068  -0.0168 0.0406  302  A1BAR A C9  
6758 C  C12 B A1BAR D .   ? 0.1293 0.1416 0.1410 0.0123  0.0044  0.0459  302  A1BAR A C12 
6759 C  C1  B A1BAR D .   ? 0.1761 0.1658 0.1876 0.0124  -0.0079 0.0065  302  A1BAR A C1  
6760 C  C10 B A1BAR D .   ? 0.1463 0.1542 0.1233 0.0172  -0.0079 0.0414  302  A1BAR A C10 
6761 C  C11 B A1BAR D .   ? 0.1382 0.1545 0.1337 0.0230  0.0044  0.0375  302  A1BAR A C11 
6762 C  C13 B A1BAR D .   ? 0.1703 0.1665 0.1467 0.0155  -0.0159 0.0314  302  A1BAR A C13 
6763 C  C2  B A1BAR D .   ? 0.1755 0.1658 0.1745 0.0108  -0.0182 0.0179  302  A1BAR A C2  
6764 C  C4  B A1BAR D .   ? 0.1728 0.1735 0.1772 -0.0008 -0.0121 0.0201  302  A1BAR A C4  
6765 C  C5  B A1BAR D .   ? 0.1666 0.1751 0.1623 -0.0023 -0.0043 0.0196  302  A1BAR A C5  
6766 C  C7  B A1BAR D .   ? 0.1532 0.1688 0.1407 0.0090  -0.0143 0.0382  302  A1BAR A C7  
6767 C  C8  B A1BAR D .   ? 0.1637 0.1712 0.1426 -0.0179 -0.0146 0.0513  302  A1BAR A C8  
6768 N  N1  B A1BAR D .   ? 0.1608 0.1744 0.1522 0.0019  -0.0013 0.0197  302  A1BAR A N1  
6769 N  N3  B A1BAR D .   ? 0.1635 0.1665 0.1345 -0.0091 -0.0213 0.0463  302  A1BAR A N3  
6770 N  N4  B A1BAR D .   ? 0.1344 0.1293 0.1350 0.0094  -0.0023 0.0294  302  A1BAR A N4  
6771 O  O1  B A1BAR D .   ? 0.1777 0.1726 0.1670 -0.0027 -0.0119 0.0183  302  A1BAR A O1  
6790 CL CL  B CL    E .   ? 0.1625 0.1361 0.1584 -0.0035 -0.0210 0.0067  303  CL    A CL  
6791 O  O   . HOH   F .   ? 0.5946 0.6328 0.4075 -0.1173 -0.1152 -0.1026 1301 HOH   A O   
6792 O  O   A HOH   F .   ? 0.3122 0.1710 0.2676 0.0186  -0.0311 0.0497  1302 HOH   A O   
6793 O  O   . HOH   F .   ? 0.3933 0.7994 0.3487 -0.1138 0.0440  0.0136  1303 HOH   A O   
6794 O  O   . HOH   F .   ? 0.3495 0.3014 0.1537 -0.0705 0.0551  0.0442  1304 HOH   A O   
6795 O  O   . HOH   F .   ? 0.6150 0.4247 0.5291 -0.1018 0.1863  0.1388  1305 HOH   A O   
6796 O  O   . HOH   F .   ? 0.5909 0.5362 0.7516 -0.1277 -0.1323 0.1820  1306 HOH   A O   
6797 O  O   . HOH   F .   ? 0.5923 0.5525 0.3501 0.2687  -0.0963 0.0645  1307 HOH   A O   
6798 O  O   . HOH   F .   ? 0.5270 0.2512 0.4485 0.0521  -0.0123 0.0192  1308 HOH   A O   
6799 O  O   . HOH   F .   ? 0.2827 0.2505 0.4683 -0.0387 -0.1156 0.1367  1309 HOH   A O   
6800 O  O   B HOH   F .   ? 0.4374 0.4131 0.3731 0.0726  -0.0191 0.0579  1310 HOH   A O   
6801 O  O   . HOH   F .   ? 0.1901 0.1875 0.3478 -0.0500 0.0261  -0.0354 1311 HOH   A O   
6802 O  O   . HOH   F .   ? 0.2968 0.7129 0.5225 -0.0570 -0.0704 0.2173  1312 HOH   A O   
6803 O  O   . HOH   F .   ? 0.4833 0.5580 0.2779 -0.1174 0.1333  0.0993  1313 HOH   A O   
6804 O  O   . HOH   F .   ? 0.4273 0.4930 0.3704 0.1524  0.0993  -0.0695 1314 HOH   A O   
6805 O  O   . HOH   F .   ? 0.1389 0.4681 0.2392 -0.0321 0.0210  0.0475  1315 HOH   A O   
6806 O  O   . HOH   F .   ? 0.5174 0.4729 0.4129 -0.0719 -0.0931 0.0832  1316 HOH   A O   
6807 O  O   . HOH   F .   ? 0.6391 0.5453 0.3276 -0.0478 -0.0608 0.1107  1317 HOH   A O   
6808 O  O   B HOH   F .   ? 0.1870 0.4400 0.4216 0.0730  0.0165  0.0370  1318 HOH   A O   
6809 O  O   . HOH   F .   ? 0.2399 0.5757 0.3483 -0.0316 -0.0569 0.0542  1319 HOH   A O   
6810 O  O   . HOH   F .   ? 0.2356 0.1949 0.1901 -0.0378 0.0151  -0.0058 1320 HOH   A O   
6811 O  O   . HOH   F .   ? 0.1538 0.3490 0.2819 0.0474  -0.0071 0.0191  1321 HOH   A O   
6812 O  O   . HOH   F .   ? 0.1812 0.1526 0.1902 0.0163  -0.0246 0.0014  1322 HOH   A O   
6813 O  O   . HOH   F .   ? 0.5060 0.6149 0.6508 -0.1094 0.1274  0.2972  1323 HOH   A O   
6814 O  O   . HOH   F .   ? 0.3553 0.3082 0.2728 -0.1305 0.0091  0.0787  1324 HOH   A O   
6815 O  O   . HOH   F .   ? 0.1828 0.3250 0.4439 -0.0388 0.0374  -0.1115 1325 HOH   A O   
6816 O  O   . HOH   F .   ? 0.3412 0.2970 0.3265 -0.1062 -0.0059 -0.0177 1326 HOH   A O   
6817 O  O   . HOH   F .   ? 0.6970 0.4831 0.4994 -0.1162 0.1668  0.2009  1327 HOH   A O   
6818 O  O   B HOH   F .   ? 0.2159 0.3481 0.1637 -0.0036 -0.0176 -0.0281 1328 HOH   A O   
6819 O  O   . HOH   F .   ? 0.4243 0.2999 0.2876 -0.1158 0.0224  0.0642  1329 HOH   A O   
6820 O  O   . HOH   F .   ? 0.4574 0.3651 0.5567 0.1203  0.1757  -0.0818 1330 HOH   A O   
6821 O  O   . HOH   F .   ? 0.2085 0.4039 0.4259 -0.0413 -0.0801 0.1916  1331 HOH   A O   
6822 O  O   . HOH   F .   ? 0.1391 0.1403 0.2060 -0.0186 0.0102  0.0083  1332 HOH   A O   
6823 O  O   . HOH   F .   ? 0.2273 0.2100 0.2554 0.0465  0.0296  0.0490  1333 HOH   A O   
6824 O  O   A HOH   F .   ? 0.1396 0.3013 0.2269 0.0769  0.0574  0.1323  1334 HOH   A O   
6825 O  O   . HOH   F .   ? 0.1761 0.2170 0.1826 -0.0250 -0.0011 0.0748  1335 HOH   A O   
6826 O  O   . HOH   F .   ? 0.4288 0.5464 0.5660 -0.0327 0.0737  0.3118  1336 HOH   A O   
6827 O  O   . HOH   F .   ? 0.2979 0.4240 0.2447 -0.0227 0.0678  0.0540  1337 HOH   A O   
6828 O  O   . HOH   F .   ? 0.3850 0.3852 0.4466 -0.1390 -0.0362 0.2085  1338 HOH   A O   
6829 O  O   A HOH   F .   ? 0.3818 0.1452 0.1524 0.0277  0.0013  0.0029  1339 HOH   A O   
6830 O  O   . HOH   F .   ? 0.3669 0.3259 0.3577 -0.0338 0.1561  0.0397  1340 HOH   A O   
6831 O  O   A HOH   F .   ? 0.1714 0.1921 0.2306 -0.0343 0.0452  0.0433  1341 HOH   A O   
6832 O  O   B HOH   F .   ? 0.3916 0.2012 0.2960 -0.0740 -0.0943 0.0640  1342 HOH   A O   
6833 O  O   . HOH   F .   ? 0.5126 0.1865 0.4643 0.0586  -0.0103 -0.0075 1343 HOH   A O   
6834 O  O   . HOH   F .   ? 0.1849 0.2383 0.3364 0.0112  0.0857  -0.0714 1344 HOH   A O   
6835 O  O   . HOH   F .   ? 0.1358 0.2144 0.2047 0.0050  -0.0057 0.0512  1345 HOH   A O   
6836 O  O   . HOH   F .   ? 0.5497 0.3358 0.3671 -0.2046 0.1850  -0.0579 1346 HOH   A O   
6837 O  O   . HOH   F .   ? 0.4542 0.1826 0.4558 0.0461  -0.1323 0.0643  1347 HOH   A O   
6838 O  O   . HOH   F .   ? 0.2124 0.3921 0.3483 0.0844  -0.0525 -0.0034 1348 HOH   A O   
6839 O  O   . HOH   F .   ? 0.5443 0.4847 0.3652 -0.0991 -0.1648 -0.1303 1349 HOH   A O   
6840 O  O   . HOH   F .   ? 0.7170 0.5499 0.6560 -0.1235 -0.1174 0.0706  1350 HOH   A O   
6841 O  O   . HOH   F .   ? 0.2669 0.3557 0.3355 -0.0885 -0.0620 -0.0488 1351 HOH   A O   
6842 O  O   . HOH   F .   ? 0.5223 0.3915 0.2427 0.0592  0.0584  0.1098  1352 HOH   A O   
6843 O  O   . HOH   F .   ? 0.2519 0.2006 0.2230 -0.0572 0.0053  0.0480  1353 HOH   A O   
6844 O  O   A HOH   F .   ? 0.2884 0.2613 0.2909 -0.0070 0.0983  -0.0674 1354 HOH   A O   
6845 O  O   . HOH   F .   ? 0.7630 0.6674 0.8017 -0.1317 -0.0088 -0.0464 1355 HOH   A O   
6846 O  O   . HOH   F .   ? 0.1750 0.1656 0.1368 0.0072  0.0082  0.0149  1356 HOH   A O   
6847 O  O   . HOH   F .   ? 0.2496 0.4196 0.2781 -0.0448 0.0444  -0.0007 1357 HOH   A O   
6848 O  O   B HOH   F .   ? 0.1503 0.1063 0.1643 -0.0133 -0.0036 0.0071  1358 HOH   A O   
6849 O  O   B HOH   F .   ? 0.2109 0.4636 0.4054 0.0773  -0.1199 -0.1272 1359 HOH   A O   
6850 O  O   . HOH   F .   ? 0.2144 0.1537 0.1357 -0.0066 0.0195  0.0171  1360 HOH   A O   
6851 O  O   . HOH   F .   ? 0.5458 0.6054 0.3324 0.2328  -0.0275 -0.0523 1361 HOH   A O   
6852 O  O   . HOH   F .   ? 0.2762 0.3050 0.4680 -0.0432 -0.1161 -0.0588 1362 HOH   A O   
6853 O  O   A HOH   F .   ? 0.5054 0.2541 0.4086 -0.0288 -0.1121 -0.0204 1363 HOH   A O   
6854 O  O   . HOH   F .   ? 0.1212 0.1227 0.1289 -0.0033 0.0108  0.0118  1364 HOH   A O   
6855 O  O   . HOH   F .   ? 0.1346 0.1791 0.2296 0.0115  -0.0063 0.0055  1365 HOH   A O   
6856 O  O   . HOH   F .   ? 0.3753 0.5158 0.3269 0.2409  0.0465  0.0361  1366 HOH   A O   
6857 O  O   . HOH   F .   ? 0.3131 0.3438 0.2132 -0.0757 -0.0461 -0.0667 1367 HOH   A O   
6858 O  O   . HOH   F .   ? 0.3153 0.3409 0.4864 -0.0126 0.1412  -0.0468 1368 HOH   A O   
6859 O  O   . HOH   F .   ? 0.1831 0.1933 0.3217 0.0082  0.0809  -0.0064 1369 HOH   A O   
6860 O  O   B HOH   F .   ? 0.1439 0.1742 0.2056 0.0143  0.0192  0.0522  1370 HOH   A O   
6861 O  O   . HOH   F .   ? 0.5700 0.4576 0.5728 0.0113  0.2967  -0.0717 1371 HOH   A O   
6862 O  O   A HOH   F .   ? 0.3936 0.3537 0.3143 0.1836  -0.0829 -0.1231 1372 HOH   A O   
6863 O  O   . HOH   F .   ? 0.3859 0.2088 0.2098 0.1190  0.0675  0.0270  1373 HOH   A O   
6864 O  O   . HOH   F .   ? 0.3335 0.4790 0.4494 0.0019  -0.0648 0.1196  1374 HOH   A O   
6865 O  O   . HOH   F .   ? 0.1439 0.1239 0.1980 -0.0092 0.0190  -0.0060 1375 HOH   A O   
6866 O  O   . HOH   F .   ? 0.2564 0.4103 0.2576 0.0476  0.0730  0.1679  1376 HOH   A O   
6867 O  O   . HOH   F .   ? 0.1822 0.1818 0.2130 -0.0309 0.0105  0.0278  1377 HOH   A O   
6868 O  O   . HOH   F .   ? 0.1336 0.1400 0.1312 -0.0048 -0.0118 -0.0031 1378 HOH   A O   
6869 O  O   . HOH   F .   ? 0.1575 0.1609 0.1899 -0.0185 0.0132  0.0351  1379 HOH   A O   
6870 O  O   B HOH   F .   ? 0.1945 0.2214 0.1235 -0.0140 -0.0140 -0.0155 1380 HOH   A O   
6871 O  O   . HOH   F .   ? 0.3087 0.2180 0.5580 -0.0653 -0.0737 0.0314  1381 HOH   A O   
6872 O  O   . HOH   F .   ? 0.1607 0.1460 0.1781 0.0158  -0.0213 0.0210  1382 HOH   A O   
6873 O  O   . HOH   F .   ? 0.1808 0.2139 0.1871 -0.0188 -0.0379 0.0346  1383 HOH   A O   
6874 O  O   . HOH   F .   ? 0.3827 0.2081 0.4318 -0.1011 0.1035  0.0228  1384 HOH   A O   
6875 O  O   . HOH   F .   ? 0.1270 0.1298 0.1526 0.0021  -0.0166 0.0068  1385 HOH   A O   
6876 O  O   . HOH   F .   ? 0.2231 0.1806 0.1668 -0.0454 0.0190  0.0248  1386 HOH   A O   
6877 O  O   . HOH   F .   ? 0.2894 0.2821 0.1901 0.0361  0.0749  0.0137  1387 HOH   A O   
6878 O  O   . HOH   F .   ? 0.3521 0.3469 0.2326 -0.0407 -0.1182 0.0693  1388 HOH   A O   
6879 O  O   . HOH   F .   ? 0.2320 0.2920 0.3013 -0.0136 0.0020  -0.0762 1389 HOH   A O   
6880 O  O   A HOH   F .   ? 0.1222 0.1136 0.1509 0.0083  -0.0299 -0.0111 1390 HOH   A O   
6881 O  O   . HOH   F .   ? 0.2382 0.1683 0.2360 -0.0030 0.0083  0.0199  1391 HOH   A O   
6882 O  O   . HOH   F .   ? 0.3618 0.6505 0.4879 -0.0682 -0.1463 0.0582  1392 HOH   A O   
6883 O  O   . HOH   F .   ? 0.2604 0.2866 0.4184 -0.0877 0.1299  -0.0386 1393 HOH   A O   
6884 O  O   B HOH   F .   ? 0.4013 0.3097 0.3632 0.0229  -0.0630 -0.0676 1394 HOH   A O   
6885 O  O   . HOH   F .   ? 0.2908 0.5982 0.3464 0.1083  0.0873  -0.1125 1395 HOH   A O   
6886 O  O   . HOH   F .   ? 0.2051 0.3420 0.2817 -0.0335 -0.0177 0.0543  1396 HOH   A O   
6887 O  O   . HOH   F .   ? 0.2973 0.2279 0.3216 -0.0102 -0.0421 0.0774  1397 HOH   A O   
6888 O  O   A HOH   F .   ? 0.1901 0.1737 0.1984 0.0175  0.0092  0.0601  1398 HOH   A O   
6889 O  O   B HOH   F .   ? 0.1885 0.2826 0.2100 0.1077  0.0604  0.1215  1399 HOH   A O   
6890 O  O   . HOH   F .   ? 0.2394 0.3225 0.3927 -0.0129 0.0781  -0.0810 1400 HOH   A O   
6891 O  O   . HOH   F .   ? 0.3887 0.3171 0.2784 -0.0278 0.0076  0.0096  1401 HOH   A O   
6892 O  O   . HOH   F .   ? 0.2304 0.3758 0.3356 -0.0287 0.0847  -0.0774 1402 HOH   A O   
6893 O  O   . HOH   F .   ? 0.4184 0.4205 0.1919 -0.0041 0.0672  0.0933  1403 HOH   A O   
6894 O  O   . HOH   F .   ? 0.2031 0.1542 0.2567 0.0046  -0.0346 0.0095  1404 HOH   A O   
6895 O  O   . HOH   F .   ? 0.4822 0.7287 0.6221 0.1406  -0.1054 0.0693  1405 HOH   A O   
6896 O  O   A HOH   F .   ? 0.1690 0.1055 0.2444 -0.0002 -0.0566 -0.0005 1406 HOH   A O   
6897 O  O   . HOH   F .   ? 0.1982 0.2016 0.2376 -0.0269 -0.0118 0.0860  1407 HOH   A O   
6898 O  O   A HOH   F .   ? 0.1166 0.1357 0.0917 0.0097  -0.0257 -0.0072 1408 HOH   A O   
6899 O  O   . HOH   F .   ? 0.1842 0.1743 0.3657 0.0439  0.1118  0.1041  1409 HOH   A O   
6900 O  O   . HOH   F .   ? 0.3199 0.6078 0.4050 -0.0780 0.0328  0.1390  1410 HOH   A O   
6901 O  O   B HOH   F .   ? 0.1215 0.1406 0.2408 -0.0025 -0.0046 0.0328  1411 HOH   A O   
6902 O  O   . HOH   F .   ? 0.2816 0.2371 0.2098 -0.0564 -0.0987 0.0326  1412 HOH   A O   
6903 O  O   . HOH   F .   ? 0.2219 0.2268 0.3568 0.0284  -0.0731 -0.0094 1413 HOH   A O   
6904 O  O   A HOH   F .   ? 0.1133 0.0795 0.1059 0.0007  -0.0166 0.0041  1414 HOH   A O   
6905 O  O   . HOH   F .   ? 0.1576 0.1365 0.1359 -0.0193 0.0129  0.0022  1415 HOH   A O   
6906 O  O   A HOH   F .   ? 0.2435 0.4018 0.4848 0.0480  0.0422  0.1119  1416 HOH   A O   
6907 O  O   . HOH   F .   ? 0.1394 0.1547 0.2611 -0.0031 0.0025  0.0196  1417 HOH   A O   
6908 O  O   A HOH   F .   ? 0.3748 0.4847 0.4013 -0.1453 0.1136  0.0612  1418 HOH   A O   
6909 O  O   . HOH   F .   ? 0.2078 0.2577 0.2235 -0.0073 -0.0616 0.0452  1419 HOH   A O   
6910 O  O   . HOH   F .   ? 0.1704 0.2571 0.3330 -0.0083 -0.0139 0.0056  1420 HOH   A O   
6911 O  O   . HOH   F .   ? 0.3163 0.1222 0.1865 -0.0012 -0.0479 0.0080  1421 HOH   A O   
6912 O  O   A HOH   F .   ? 0.1301 0.1908 0.3229 -0.0110 0.0481  0.0590  1422 HOH   A O   
6913 O  O   . HOH   F .   ? 0.1524 0.2137 0.2434 -0.0153 0.0038  0.0608  1423 HOH   A O   
6914 O  O   . HOH   F .   ? 0.7447 0.6465 0.6216 -0.1341 -0.0187 -0.0088 1424 HOH   A O   
6915 O  O   . HOH   F .   ? 0.2695 0.3710 0.7292 -0.0232 0.0664  -0.0503 1425 HOH   A O   
6916 O  O   A HOH   F .   ? 0.4418 0.3007 0.3470 0.1234  0.0193  0.1229  1426 HOH   A O   
6917 O  O   . HOH   F .   ? 0.2137 0.4237 0.2456 0.1570  -0.0046 0.0276  1427 HOH   A O   
6918 O  O   . HOH   F .   ? 0.3757 0.2076 0.5171 -0.0614 -0.2113 0.1056  1428 HOH   A O   
6919 O  O   . HOH   F .   ? 0.3891 0.4412 0.3089 0.1747  -0.0714 -0.1634 1429 HOH   A O   
6920 O  O   . HOH   F .   ? 0.5833 0.6780 0.4149 -0.0185 0.2803  -0.0627 1430 HOH   A O   
6921 O  O   . HOH   F .   ? 0.2758 0.5514 0.1621 -0.0327 0.0518  0.0251  1431 HOH   A O   
6922 O  O   . HOH   F .   ? 0.3938 0.6630 0.3168 -0.1025 -0.0364 0.1580  1432 HOH   A O   
6923 O  O   A HOH   F .   ? 0.4363 0.3100 0.1818 -0.0675 0.0754  0.0610  1433 HOH   A O   
6924 O  O   . HOH   F .   ? 0.3323 0.2373 0.5913 0.0593  0.0798  0.0730  1434 HOH   A O   
6925 O  O   . HOH   F .   ? 0.6760 0.3941 0.5434 0.1860  -0.0658 0.1295  1435 HOH   A O   
6926 O  O   . HOH   F .   ? 0.4263 0.4702 0.3202 -0.0513 -0.1483 0.0368  1436 HOH   A O   
6927 O  O   A HOH   F .   ? 0.5957 0.6014 0.4449 0.0645  -0.1323 0.0908  1437 HOH   A O   
6928 O  O   . HOH   F .   ? 0.6846 0.6561 0.6528 0.0221  -0.0549 0.0302  1438 HOH   A O   
6929 O  O   A HOH   F .   ? 0.1155 0.1166 0.1243 -0.0228 -0.0146 -0.0223 1439 HOH   A O   
6930 O  O   A HOH   F .   ? 0.3173 0.3873 0.3436 -0.0371 -0.0888 -0.0249 1440 HOH   A O   
6931 O  O   . HOH   F .   ? 0.3460 0.2446 0.1515 -0.0823 0.0369  0.0389  1441 HOH   A O   
6932 O  O   . HOH   F .   ? 0.4954 0.6877 0.5875 0.3238  0.0288  0.0778  1442 HOH   A O   
6933 O  O   A HOH   F .   ? 0.1688 0.2005 0.3098 0.0284  -0.0245 -0.0828 1443 HOH   A O   
6934 O  O   A HOH   F .   ? 0.2350 0.1794 0.2584 0.0054  -0.0178 -0.0522 1444 HOH   A O   
6935 O  O   . HOH   F .   ? 0.1706 0.2081 0.5083 -0.0231 -0.0938 0.0580  1445 HOH   A O   
6936 O  O   A HOH   F .   ? 0.2750 0.3253 0.3461 -0.0317 -0.0525 -0.0934 1446 HOH   A O   
6937 O  O   A HOH   F .   ? 0.4498 0.2622 0.5226 0.0056  0.0443  -0.0755 1447 HOH   A O   
6938 O  O   . HOH   F .   ? 0.4154 0.4051 0.4025 -0.0052 -0.0570 0.1061  1448 HOH   A O   
6939 O  O   A HOH   F .   ? 0.1485 0.1470 0.1839 0.0231  -0.0506 0.0280  1449 HOH   A O   
6940 O  O   . HOH   F .   ? 0.2294 0.1510 0.2378 0.0029  -0.0000 0.0107  1450 HOH   A O   
6941 O  O   . HOH   F .   ? 0.2370 0.2206 0.3801 0.0286  0.0349  -0.0185 1451 HOH   A O   
6942 O  O   . HOH   F .   ? 0.4066 0.3511 0.3114 0.2210  -0.0632 -0.0561 1452 HOH   A O   
6943 O  O   . HOH   F .   ? 0.2100 0.1974 0.2325 0.0175  0.0268  0.0288  1453 HOH   A O   
6944 O  O   . HOH   F .   ? 0.6669 0.8071 0.4139 0.2497  -0.1109 0.1659  1454 HOH   A O   
6945 O  O   . HOH   F .   ? 0.1971 0.2639 0.2247 -0.0036 -0.0046 -0.0582 1455 HOH   A O   
6946 O  O   B HOH   F .   ? 0.1691 0.2160 0.2415 -0.0987 0.0269  -0.0726 1456 HOH   A O   
6947 O  O   A HOH   F .   ? 0.4015 0.3751 0.6038 0.1009  -0.0864 0.0712  1457 HOH   A O   
6948 O  O   A HOH   F .   ? 0.2992 0.3872 0.4045 -0.0964 -0.0098 -0.0946 1458 HOH   A O   
6949 O  O   A HOH   F .   ? 0.5729 0.2730 0.4158 0.0279  0.1524  0.1453  1459 HOH   A O   
6950 O  O   . HOH   F .   ? 0.5808 0.2878 0.3392 0.1045  0.0459  0.0895  1460 HOH   A O   
6951 O  O   B HOH   F .   ? 0.1915 0.2741 0.4459 0.0225  0.0148  0.0175  1461 HOH   A O   
6952 O  O   . HOH   F .   ? 0.6757 0.6054 0.5019 -0.0788 0.1601  0.1029  1462 HOH   A O   
6953 O  O   . HOH   F .   ? 0.2147 0.2362 0.2955 0.0354  -0.0245 0.0053  1463 HOH   A O   
6954 O  O   . HOH   F .   ? 0.7316 0.7472 0.4617 -0.0056 -0.1234 -0.0250 1464 HOH   A O   
6955 O  O   . HOH   F .   ? 0.5110 0.3168 0.4370 0.0815  0.1452  0.0225  1465 HOH   A O   
6956 O  O   . HOH   F .   ? 0.2839 0.2954 0.3280 -0.0630 0.0213  -0.0815 1466 HOH   A O   
6957 O  O   . HOH   F .   ? 0.2878 0.4911 0.5429 -0.1438 0.0962  -0.1640 1467 HOH   A O   
6958 O  O   . HOH   F .   ? 0.3441 0.3957 0.3790 0.0426  -0.1598 0.0335  1468 HOH   A O   
6959 O  O   . HOH   F .   ? 0.2865 0.3833 0.2917 -0.0717 -0.0396 0.0341  1469 HOH   A O   
6960 O  O   . HOH   F .   ? 0.6374 0.3703 0.8479 0.1312  0.0941  0.2403  1470 HOH   A O   
6961 O  O   . HOH   F .   ? 0.2266 0.2411 0.3259 -0.0560 0.0398  -0.0140 1471 HOH   A O   
6962 O  O   . HOH   F .   ? 0.2831 0.1657 0.2200 0.0439  -0.0924 -0.0320 1472 HOH   A O   
6963 O  O   . HOH   F .   ? 0.2721 0.3941 0.4848 0.0478  0.0176  -0.1941 1473 HOH   A O   
6964 O  O   . HOH   F .   ? 0.3363 0.5154 0.3063 0.0193  -0.0302 -0.0266 1474 HOH   A O   
6965 O  O   . HOH   F .   ? 0.2517 0.2333 0.3036 0.0077  0.0327  -0.0147 1475 HOH   A O   
6966 O  O   A HOH   F .   ? 0.2379 0.1882 0.4176 0.0798  -0.1154 -0.0360 1476 HOH   A O   
6967 O  O   . HOH   F .   ? 0.6734 0.6098 0.6357 0.2005  0.3280  0.2445  1477 HOH   A O   
6968 O  O   . HOH   F .   ? 0.3674 0.6352 0.3546 -0.0771 -0.0577 0.2336  1478 HOH   A O   
6969 O  O   B HOH   F .   ? 0.5195 0.2065 0.6630 -0.1086 0.0515  0.0207  1479 HOH   A O   
6970 O  O   B HOH   F .   ? 0.3280 0.3144 0.3279 0.0336  0.0496  -0.0552 1480 HOH   A O   
6971 O  O   . HOH   F .   ? 0.4324 0.5306 0.4659 0.0175  0.0792  0.0781  1481 HOH   A O   
6972 O  O   . HOH   F .   ? 0.6741 0.5175 0.6414 -0.0169 0.0879  -0.0280 1482 HOH   A O   
6973 O  O   . HOH   F .   ? 0.5373 0.4973 0.4466 0.0729  -0.1322 -0.0786 1483 HOH   A O   
6974 O  O   . HOH   F .   ? 0.4052 0.4633 0.2561 -0.0126 0.0130  0.0358  1484 HOH   A O   
6975 O  O   . HOH   F .   ? 0.2839 0.4776 0.2679 -0.0226 -0.0184 -0.0248 1485 HOH   A O   
6976 O  O   . HOH   F .   ? 0.2453 0.2115 0.2314 0.0375  0.0113  0.0268  1486 HOH   A O   
6977 O  O   . HOH   F .   ? 0.3994 0.4251 0.4566 -0.2066 -0.0198 -0.0097 1487 HOH   A O   
6978 O  O   . HOH   F .   ? 0.4221 0.2398 0.3516 -0.0555 -0.1122 0.0714  1488 HOH   A O   
6979 O  O   . HOH   F .   ? 0.6050 0.7115 0.5791 -0.1436 -0.1327 0.0275  1489 HOH   A O   
6980 O  O   B HOH   F .   ? 0.1712 0.2222 0.2892 0.0290  0.0107  -0.0645 1490 HOH   A O   
6981 O  O   . HOH   F .   ? 0.5428 0.4853 0.4149 -0.0092 0.0350  -0.1459 1491 HOH   A O   
6982 O  O   . HOH   F .   ? 0.4620 0.4571 0.3569 -0.0883 -0.0440 -0.0053 1492 HOH   A O   
6983 O  O   B HOH   F .   ? 0.2169 0.1671 0.2210 0.0228  -0.0204 0.0386  1493 HOH   A O   
6984 O  O   . HOH   F .   ? 0.5023 0.3178 0.2518 -0.0812 0.1676  -0.0294 1494 HOH   A O   
6985 O  O   . HOH   F .   ? 0.7979 0.3746 0.2822 -0.0804 -0.1105 0.0087  1495 HOH   A O   
6986 O  O   B HOH   F .   ? 0.4576 0.2877 0.2487 0.0300  0.0008  -0.0256 1496 HOH   A O   
6987 O  O   . HOH   F .   ? 0.6024 0.3917 0.4132 -0.0527 0.1423  -0.0005 1497 HOH   A O   
6988 O  O   B HOH   F .   ? 0.3569 0.1850 0.3782 0.0979  0.0587  0.0659  1498 HOH   A O   
6989 O  O   . HOH   F .   ? 0.2661 0.5165 0.3653 0.1267  0.1100  0.2340  1499 HOH   A O   
6990 O  O   . HOH   F .   ? 0.5208 0.5523 0.6446 0.0906  0.1859  -0.1156 1500 HOH   A O   
6991 O  O   . HOH   F .   ? 0.2651 0.4148 0.5400 -0.0057 0.1012  0.1901  1501 HOH   A O   
6992 O  O   . HOH   F .   ? 0.6154 0.6415 0.4678 0.1722  -0.1398 0.0159  1502 HOH   A O   
6993 O  O   . HOH   F .   ? 0.6760 0.5528 0.4676 -0.1165 -0.0934 -0.0960 1503 HOH   A O   
6994 O  O   . HOH   F .   ? 0.2455 0.2373 0.7464 0.0041  -0.1306 0.0115  1504 HOH   A O   
6995 O  O   . HOH   F .   ? 0.4839 0.5787 0.5227 -0.0488 -0.1043 0.0659  1505 HOH   A O   
6996 O  O   . HOH   F .   ? 0.6141 0.2508 0.4857 -0.0823 0.1206  0.0553  1506 HOH   A O   
6997 O  O   . HOH   F .   ? 0.4927 0.2941 0.3996 -0.0063 0.2197  0.0330  1507 HOH   A O   
6998 O  O   . HOH   F .   ? 0.2342 0.3384 0.5466 0.0056  0.0958  -0.1078 1508 HOH   A O   
6999 O  O   . HOH   F .   ? 0.4175 0.2993 0.4612 -0.1040 0.0752  0.0732  1509 HOH   A O   
7000 O  O   . HOH   F .   ? 0.2870 0.1853 0.5577 0.0193  0.1000  0.0900  1510 HOH   A O   
7001 O  O   . HOH   F .   ? 0.4449 0.2568 0.4098 -0.1415 -0.0016 0.0426  1511 HOH   A O   
7002 O  O   A HOH   F .   ? 0.3558 0.4907 0.3366 -0.0209 0.0691  0.0803  1512 HOH   A O   
7003 O  O   . HOH   F .   ? 0.3884 0.8825 0.4987 -0.1047 -0.0422 0.3159  1513 HOH   A O   
7004 O  O   . HOH   F .   ? 0.2254 0.3017 0.3676 0.0401  -0.0536 0.0721  1514 HOH   A O   
7005 O  O   . HOH   F .   ? 0.2821 0.4257 0.3457 0.0658  0.0069  0.0457  1515 HOH   A O   
7006 O  O   . HOH   F .   ? 0.5197 0.6942 0.5243 0.1136  -0.0374 0.1461  1516 HOH   A O   
7007 O  O   . HOH   F .   ? 0.7923 0.4319 0.5667 -0.0419 0.0524  -0.0088 1517 HOH   A O   
7008 O  O   . HOH   F .   ? 0.2997 0.2070 0.4501 0.0127  0.0487  0.0473  1518 HOH   A O   
7009 O  O   . HOH   F .   ? 0.4396 0.6746 0.4571 0.2908  -0.0423 0.0743  1519 HOH   A O   
7010 O  O   . HOH   F .   ? 0.4980 0.6070 0.4450 -0.0471 -0.1050 -0.1282 1520 HOH   A O   
7011 O  O   A HOH   F .   ? 0.2186 0.4138 0.1956 0.0846  0.0334  -0.0342 1521 HOH   A O   
7012 O  O   B HOH   F .   ? 0.4844 0.2581 0.3423 0.1306  0.0958  0.0854  1522 HOH   A O   
7013 O  O   . HOH   F .   ? 0.2487 0.7605 0.2950 0.0997  -0.0131 0.0441  1523 HOH   A O   
7014 O  O   . HOH   F .   ? 0.4467 0.4583 0.4557 0.1376  -0.0687 0.0629  1524 HOH   A O   
7015 O  O   . HOH   F .   ? 0.4921 0.5985 0.4947 -0.0951 -0.0743 0.0717  1525 HOH   A O   
7016 O  O   . HOH   F .   ? 0.3425 0.3908 0.5494 -0.0376 -0.1018 0.2462  1526 HOH   A O   
7017 O  O   . HOH   G .   ? 0.2205 0.2056 0.2709 0.0254  0.0830  0.0322  201  HOH   B O   
7018 O  O   . HOH   G .   ? 0.4540 0.3199 0.3865 -0.0319 -0.0002 -0.1396 202  HOH   B O   
7019 O  O   . HOH   G .   ? 0.2654 0.5625 0.4761 0.0097  0.1341  -0.1735 203  HOH   B O   
7020 O  O   . HOH   G .   ? 0.6266 0.6536 0.5308 0.1988  0.0218  -0.0455 204  HOH   B O   
7021 O  O   . HOH   G .   ? 0.4834 0.5795 0.3713 0.2902  -0.0956 -0.0108 205  HOH   B O   
7022 O  O   . HOH   G .   ? 0.5682 0.4933 0.1982 0.0828  -0.0350 -0.1051 206  HOH   B O   
7023 O  O   . HOH   G .   ? 0.3222 0.2728 0.7293 -0.0221 0.0999  0.0502  207  HOH   B O   
7024 O  O   . HOH   G .   ? 0.2997 0.2003 0.5086 0.0230  0.1967  0.0827  208  HOH   B O   
7025 O  O   . HOH   G .   ? 0.7493 0.2755 0.5013 0.0328  0.1756  0.0071  209  HOH   B O   
7026 O  O   . HOH   G .   ? 0.3290 0.7089 0.3236 0.1118  0.0370  0.2210  210  HOH   B O   
7027 O  O   . HOH   G .   ? 0.2699 0.2579 0.6602 0.0558  -0.1248 0.0477  211  HOH   B O   
7028 O  O   . HOH   G .   ? 0.1879 0.2290 0.2643 0.0203  0.0043  -0.0417 212  HOH   B O   
7029 O  O   . HOH   G .   ? 0.2907 0.3835 0.5484 -0.0647 -0.0015 -0.1694 213  HOH   B O   
7030 O  O   . HOH   G .   ? 0.6016 0.2815 0.3855 -0.1896 0.0441  0.0005  214  HOH   B O   
7031 O  O   . HOH   G .   ? 0.4409 0.3708 0.3450 -0.0171 -0.1114 0.0697  215  HOH   B O   
7032 O  O   . HOH   G .   ? 0.4547 0.4482 0.4097 0.0587  0.0923  -0.1683 216  HOH   B O   
7033 O  O   . HOH   G .   ? 0.5466 0.4375 0.5884 0.0993  -0.0779 0.2608  217  HOH   B O   
7034 O  O   . HOH   G .   ? 0.1477 0.1833 0.2364 -0.0231 -0.0053 0.0101  218  HOH   B O   
7035 O  O   . HOH   G .   ? 0.3922 0.3656 0.4895 -0.1325 0.0211  0.0265  219  HOH   B O   
7036 O  O   . HOH   G .   ? 0.4309 0.4946 0.3648 0.2587  -0.0201 0.0391  220  HOH   B O   
7037 O  O   . HOH   G .   ? 0.3236 0.5113 0.5057 0.2120  0.0330  -0.0902 221  HOH   B O   
7038 O  O   . HOH   G .   ? 0.2116 0.1992 0.3585 -0.0221 -0.0159 -0.0582 222  HOH   B O   
7039 O  O   . HOH   G .   ? 0.3631 0.3699 0.7439 -0.0488 -0.1605 -0.1017 223  HOH   B O   
7040 O  O   . HOH   G .   ? 0.3565 0.3466 0.1881 0.0352  0.0679  0.0421  224  HOH   B O   
7041 O  O   . HOH   G .   ? 0.4598 0.1897 0.3235 0.0092  -0.0961 0.0001  225  HOH   B O   
7042 O  O   . HOH   G .   ? 0.1667 0.1919 0.2730 -0.0128 0.0048  -0.0101 226  HOH   B O   
7043 O  O   . HOH   G .   ? 0.3325 0.2602 0.5037 0.0727  -0.0839 -0.0625 227  HOH   B O   
7044 O  O   . HOH   G .   ? 0.2475 0.1675 0.2495 -0.0328 0.1168  -0.0074 228  HOH   B O   
7045 O  O   . HOH   G .   ? 0.2581 0.2529 0.2824 0.0351  0.0126  -0.0919 229  HOH   B O   
7046 O  O   . HOH   G .   ? 0.4693 0.3115 0.2366 0.0299  0.1022  -0.0262 230  HOH   B O   
7047 O  O   . HOH   G .   ? 0.2491 0.3440 0.3421 -0.0675 0.0445  -0.0907 231  HOH   B O   
7048 O  O   . HOH   G .   ? 0.2898 0.2706 0.6427 0.0020  0.1033  0.0408  232  HOH   B O   
7049 O  O   . HOH   G .   ? 0.1971 0.1237 0.3251 0.0105  -0.0543 -0.0219 233  HOH   B O   
7050 O  O   . HOH   G .   ? 0.2048 0.2351 0.2729 -0.0548 0.0063  -0.0204 234  HOH   B O   
7051 O  O   . HOH   G .   ? 0.3682 0.2329 0.3830 0.0992  -0.0596 -0.0692 235  HOH   B O   
7052 O  O   . HOH   G .   ? 0.3467 0.1710 0.1721 0.0176  -0.0762 -0.0194 236  HOH   B O   
7053 O  O   . HOH   G .   ? 0.3474 0.3073 0.4234 0.0648  -0.1132 -0.1846 237  HOH   B O   
7054 O  O   . HOH   G .   ? 0.4845 0.6921 0.3343 0.2952  0.0638  0.0541  238  HOH   B O   
7055 O  O   . HOH   G .   ? 0.1401 0.1345 0.1394 -0.0122 -0.0055 0.0011  239  HOH   B O   
7056 O  O   . HOH   G .   ? 0.5092 0.5948 0.3183 -0.0744 -0.0241 -0.0719 240  HOH   B O   
7057 O  O   . HOH   G .   ? 0.5065 0.2985 0.4188 -0.2175 0.0193  -0.0057 241  HOH   B O   
7058 O  O   . HOH   G .   ? 0.2130 0.3223 0.2942 -0.0354 -0.0551 -0.0614 242  HOH   B O   
7059 O  O   . HOH   G .   ? 0.2951 0.1995 0.4546 -0.0032 0.1718  0.0067  243  HOH   B O   
7060 O  O   . HOH   G .   ? 0.1303 0.1237 0.1410 -0.0016 0.0047  0.0054  244  HOH   B O   
7061 O  O   . HOH   G .   ? 0.2344 0.2184 0.2381 0.0943  -0.0952 -0.0832 245  HOH   B O   
7062 O  O   . HOH   G .   ? 0.1468 0.1407 0.2251 -0.0081 0.0093  -0.0162 246  HOH   B O   
7063 O  O   . HOH   G .   ? 0.2709 0.2269 0.2538 0.0973  0.0833  0.0194  247  HOH   B O   
7064 O  O   . HOH   G .   ? 0.3016 0.1665 0.5465 -0.0141 -0.1430 -0.0406 248  HOH   B O   
7065 O  O   . HOH   G .   ? 0.2140 0.1984 0.1706 0.0083  -0.0017 0.0096  249  HOH   B O   
7066 O  O   . HOH   G .   ? 0.2686 0.4588 0.4818 0.0661  0.0058  -0.1291 250  HOH   B O   
7067 O  O   . HOH   G .   ? 0.2173 0.1854 0.1874 -0.0309 -0.0364 0.0020  251  HOH   B O   
7068 O  O   . HOH   G .   ? 0.2721 0.2360 0.2988 -0.0362 0.0116  -0.0640 252  HOH   B O   
7069 O  O   . HOH   G .   ? 0.1915 0.3360 0.2138 -0.0289 -0.0176 0.0490  253  HOH   B O   
7070 O  O   . HOH   G .   ? 0.1972 0.1389 0.1892 -0.0297 -0.0328 0.0239  254  HOH   B O   
7071 O  O   . HOH   G .   ? 0.2146 0.3076 0.2029 -0.0621 0.0250  0.0530  255  HOH   B O   
7072 O  O   . HOH   G .   ? 0.1471 0.1528 0.2667 -0.0158 -0.0086 -0.0010 256  HOH   B O   
7073 O  O   . HOH   G .   ? 0.3389 0.3293 0.1955 0.0578  0.0839  0.0079  257  HOH   B O   
7074 O  O   . HOH   G .   ? 0.1791 0.2524 0.2461 0.0477  0.0356  0.0926  258  HOH   B O   
7075 O  O   . HOH   G .   ? 0.1250 0.1522 0.1896 -0.0067 0.0037  0.0120  259  HOH   B O   
7076 O  O   . HOH   G .   ? 0.2591 0.4337 0.3056 -0.0997 -0.0347 -0.0624 260  HOH   B O   
7077 O  O   . HOH   G .   ? 0.1977 0.3975 0.4154 -0.0235 -0.0263 -0.1711 261  HOH   B O   
7078 O  O   . HOH   G .   ? 0.2391 0.4436 0.5013 0.1425  -0.0286 0.0015  262  HOH   B O   
7079 O  O   . HOH   G .   ? 0.2270 0.2786 0.2116 -0.0425 -0.0633 -0.0439 263  HOH   B O   
7080 O  O   . HOH   G .   ? 0.2342 0.1780 0.2818 -0.0483 0.0194  -0.0084 264  HOH   B O   
7081 O  O   . HOH   G .   ? 0.2819 0.5006 0.4331 -0.0319 -0.0926 0.1917  265  HOH   B O   
7082 O  O   . HOH   G .   ? 0.2103 0.2152 0.1549 0.0152  0.0103  0.0068  266  HOH   B O   
7083 O  O   . HOH   G .   ? 0.2508 0.2575 0.2246 -0.0279 -0.0757 -0.0018 267  HOH   B O   
7084 O  O   . HOH   G .   ? 0.7075 0.4359 0.5045 0.2278  -0.0370 -0.1608 268  HOH   B O   
7085 O  O   . HOH   G .   ? 0.2370 0.3484 0.2185 0.1331  -0.0556 -0.0663 269  HOH   B O   
7086 O  O   . HOH   G .   ? 0.1922 0.1426 0.2008 -0.0209 -0.0154 0.0146  270  HOH   B O   
7087 O  O   . HOH   G .   ? 0.2039 0.1823 0.3130 0.0059  -0.0397 -0.0425 271  HOH   B O   
7088 O  O   . HOH   G .   ? 0.3286 0.2551 0.4675 -0.0454 0.0572  -0.1195 272  HOH   B O   
7089 O  O   . HOH   G .   ? 0.2083 0.3252 0.2839 -0.0369 0.0281  -0.0955 273  HOH   B O   
7090 O  O   . HOH   G .   ? 0.1621 0.1342 0.3562 -0.0049 -0.0231 -0.0114 274  HOH   B O   
7091 O  O   . HOH   G .   ? 0.1806 0.1637 0.1512 -0.0423 -0.0424 0.0131  275  HOH   B O   
7092 O  O   . HOH   G .   ? 0.2451 0.3738 0.3293 0.0261  0.0953  0.0074  276  HOH   B O   
7093 O  O   . HOH   G .   ? 0.4415 0.3462 0.2628 0.0638  0.0065  -0.1037 277  HOH   B O   
7094 O  O   . HOH   G .   ? 0.5724 0.6146 0.2775 -0.0242 -0.1182 0.1568  278  HOH   B O   
7095 O  O   . HOH   G .   ? 0.3846 0.3055 0.4777 -0.0166 -0.1213 -0.0985 279  HOH   B O   
7096 O  O   . HOH   G .   ? 0.2683 0.6765 0.7630 0.0371  -0.1137 -0.0725 280  HOH   B O   
7097 O  O   . HOH   G .   ? 0.3161 0.7322 0.3269 0.1693  -0.0891 -0.0013 281  HOH   B O   
7098 O  O   . HOH   G .   ? 0.1459 0.1479 0.3116 -0.0083 0.0069  -0.0062 282  HOH   B O   
7099 O  O   . HOH   G .   ? 0.3744 0.2731 0.1719 0.0782  -0.0759 -0.0163 283  HOH   B O   
7100 O  O   . HOH   G .   ? 0.3560 0.1951 0.4075 -0.0754 -0.2107 0.0612  284  HOH   B O   
7101 O  O   . HOH   G .   ? 0.1488 0.1420 0.1594 0.0006  0.0048  0.0005  285  HOH   B O   
7102 O  O   . HOH   G .   ? 0.3366 0.3448 0.4677 0.1347  -0.0666 -0.0916 286  HOH   B O   
7103 O  O   . HOH   G .   ? 0.2354 0.6443 0.2471 0.0427  -0.0319 -0.0940 287  HOH   B O   
7104 O  O   . HOH   G .   ? 0.1633 0.1820 0.2726 0.0250  -0.0140 0.0005  288  HOH   B O   
7105 O  O   . HOH   G .   ? 0.1544 0.1977 0.1336 -0.0158 -0.0125 0.0013  289  HOH   B O   
7106 O  O   . HOH   G .   ? 0.2661 0.1966 0.4718 0.0210  0.0359  0.0670  290  HOH   B O   
7107 O  O   . HOH   G .   ? 0.2636 0.4684 0.5327 -0.1056 -0.1348 0.1284  291  HOH   B O   
7108 O  O   . HOH   G .   ? 0.2209 0.2531 0.2624 0.0143  -0.0696 0.0199  292  HOH   B O   
7109 O  O   . HOH   G .   ? 0.3925 0.3843 0.3703 -0.0844 0.1134  -0.1138 293  HOH   B O   
7110 O  O   . HOH   G .   ? 0.4395 0.3059 0.4273 -0.0828 0.0525  0.0855  294  HOH   B O   
7111 O  O   . HOH   G .   ? 0.2706 0.2755 0.2750 -0.0095 0.0060  -0.1258 295  HOH   B O   
7112 O  O   . HOH   G .   ? 0.3892 0.5311 0.4407 0.0060  -0.1235 0.0247  296  HOH   B O   
7113 O  O   . HOH   G .   ? 0.1595 0.2976 0.4956 0.0125  -0.0094 -0.1287 297  HOH   B O   
7114 O  O   . HOH   G .   ? 0.4548 0.4449 0.2064 0.1396  -0.0802 -0.0348 298  HOH   B O   
7115 O  O   . HOH   G .   ? 0.1662 0.1486 0.2164 0.0109  0.0090  0.0121  299  HOH   B O   
7116 O  O   . HOH   G .   ? 0.1490 0.1392 0.2736 0.0070  0.0056  -0.0087 300  HOH   B O   
7117 O  O   . HOH   G .   ? 0.4081 0.5122 0.1930 0.0241  0.0580  0.0978  301  HOH   B O   
7118 O  O   . HOH   G .   ? 0.1959 0.1438 0.3120 0.0294  -0.0938 -0.0079 302  HOH   B O   
7119 O  O   . HOH   G .   ? 0.2014 0.2640 0.6432 0.0510  -0.0559 -0.1239 303  HOH   B O   
7120 O  O   . HOH   G .   ? 0.2479 0.2870 0.4447 -0.0275 -0.1347 0.0933  304  HOH   B O   
7121 O  O   . HOH   G .   ? 0.4541 0.3884 0.6127 0.0439  0.0377  0.0465  305  HOH   B O   
7122 O  O   . HOH   G .   ? 0.2937 0.3542 0.4105 -0.1186 0.1265  -0.0444 306  HOH   B O   
7123 O  O   . HOH   G .   ? 0.6874 0.5817 0.5753 0.3027  0.0018  -0.0377 307  HOH   B O   
7124 O  O   . HOH   G .   ? 0.4182 0.3766 0.2337 0.1091  -0.0686 0.0659  308  HOH   B O   
7125 O  O   . HOH   G .   ? 0.1978 0.1512 0.2504 -0.0206 -0.0257 -0.0045 309  HOH   B O   
7126 O  O   . HOH   G .   ? 0.6054 0.3685 0.2975 0.2576  0.1225  0.0825  310  HOH   B O   
7127 O  O   . HOH   G .   ? 0.3298 0.1753 0.3268 0.0706  0.1249  0.0381  311  HOH   B O   
7128 O  O   . HOH   G .   ? 0.2892 0.2843 0.5456 -0.0369 -0.0908 0.1501  312  HOH   B O   
7129 O  O   . HOH   G .   ? 0.2045 0.3004 0.4979 0.0026  -0.0587 -0.0382 313  HOH   B O   
7130 O  O   . HOH   G .   ? 0.5549 0.2795 0.2402 -0.1981 0.1083  -0.0451 314  HOH   B O   
7131 O  O   . HOH   G .   ? 0.3787 0.2131 0.2691 0.1312  0.0914  0.0214  315  HOH   B O   
7132 O  O   . HOH   G .   ? 0.2610 0.3003 0.3200 -0.0456 0.0983  -0.0960 316  HOH   B O   
7133 O  O   . HOH   G .   ? 0.6146 0.3192 0.4082 0.0429  0.1069  -0.1451 317  HOH   B O   
7134 O  O   . HOH   G .   ? 0.2311 0.1403 0.2284 -0.0152 -0.0111 0.0305  318  HOH   B O   
7135 O  O   . HOH   G .   ? 0.1571 0.1813 0.2544 -0.0322 -0.0101 0.0126  319  HOH   B O   
7136 O  O   . HOH   G .   ? 0.4285 0.4096 0.2447 0.0406  -0.0373 -0.0582 320  HOH   B O   
7137 O  O   . HOH   G .   ? 0.2009 0.1893 0.1580 -0.0143 0.0207  0.0089  321  HOH   B O   
7138 O  O   . HOH   G .   ? 0.5799 0.5145 0.4785 -0.1207 -0.0286 0.0711  322  HOH   B O   
7139 O  O   . HOH   G .   ? 0.1553 0.2789 0.2136 -0.0125 -0.0248 0.0673  323  HOH   B O   
7140 O  O   . HOH   G .   ? 0.1436 0.1544 0.2653 -0.0092 -0.0065 -0.0108 324  HOH   B O   
7141 O  O   . HOH   G .   ? 0.5977 0.4628 0.5061 0.1397  0.1687  0.0345  325  HOH   B O   
7142 O  O   . HOH   G .   ? 0.2061 0.5898 0.5252 -0.0927 -0.0299 -0.0594 326  HOH   B O   
7143 O  O   . HOH   G .   ? 0.2528 0.2102 0.2187 0.0178  -0.0239 0.0274  327  HOH   B O   
7144 O  O   . HOH   G .   ? 0.4146 0.3231 0.5363 0.1229  0.2081  0.1956  328  HOH   B O   
7145 O  O   . HOH   G .   ? 0.1810 0.1922 0.2890 0.0360  0.0411  0.0187  329  HOH   B O   
7146 O  O   . HOH   G .   ? 0.1748 0.2885 0.2916 0.0388  -0.0151 -0.0774 330  HOH   B O   
7147 O  O   . HOH   G .   ? 0.4687 0.2167 0.3848 0.0468  0.0836  0.0771  331  HOH   B O   
7148 O  O   . HOH   G .   ? 0.3064 0.4038 0.8011 -0.0418 -0.0815 0.2618  332  HOH   B O   
7149 O  O   . HOH   G .   ? 0.5395 0.4964 0.5927 0.0377  -0.0725 0.2219  333  HOH   B O   
7150 O  O   . HOH   G .   ? 0.6285 0.3518 0.3433 0.0262  0.1299  0.1326  334  HOH   B O   
7151 O  O   . HOH   G .   ? 0.2503 0.1979 0.4812 0.0056  0.0086  0.0436  335  HOH   B O   
7152 O  O   . HOH   G .   ? 0.5677 0.4046 0.6238 -0.0675 -0.1091 -0.1381 336  HOH   B O   
7153 O  O   . HOH   G .   ? 0.8153 0.2198 0.3186 0.0571  -0.1056 -0.0138 337  HOH   B O   
7154 O  O   . HOH   G .   ? 0.2221 0.2240 0.5229 -0.0486 -0.0020 0.1377  338  HOH   B O   
7155 O  O   . HOH   G .   ? 0.1618 0.1351 0.2133 0.0087  -0.0146 0.0105  339  HOH   B O   
7156 O  O   . HOH   G .   ? 0.4805 0.5962 0.3473 0.0302  -0.1085 0.0164  340  HOH   B O   
7157 O  O   . HOH   G .   ? 0.4872 0.3138 0.3015 0.0645  -0.1296 -0.0758 341  HOH   B O   
7158 O  O   . HOH   G .   ? 0.2069 0.5169 0.6894 -0.0044 0.0482  0.1753  342  HOH   B O   
7159 O  O   . HOH   G .   ? 0.4084 0.7079 0.3294 0.0071  -0.0962 0.1394  343  HOH   B O   
7160 O  O   . HOH   G .   ? 0.5940 0.6901 0.2970 -0.0320 -0.0354 0.1724  344  HOH   B O   
7161 O  O   . HOH   G .   ? 0.4357 0.4980 0.5334 0.0428  -0.1058 0.0220  345  HOH   B O   
7162 O  O   . HOH   G .   ? 0.2038 0.1708 0.3579 -0.0051 0.0824  -0.0070 346  HOH   B O   
7163 O  O   . HOH   G .   ? 0.4180 0.5428 0.4353 -0.1109 -0.0472 -0.1012 347  HOH   B O   
7164 O  O   . HOH   G .   ? 0.4929 0.5433 0.4893 -0.1199 0.0427  0.1016  348  HOH   B O   
7165 O  O   . HOH   G .   ? 0.3059 0.4004 0.4331 -0.1372 0.0394  -0.0436 349  HOH   B O   
7166 O  O   . HOH   G .   ? 0.2388 0.6176 0.2627 0.1589  -0.0517 -0.1401 350  HOH   B O   
7167 O  O   . HOH   G .   ? 0.2583 0.2126 0.4871 -0.0128 -0.0964 -0.0518 351  HOH   B O   
7168 O  O   . HOH   G .   ? 0.2276 0.3761 0.4481 0.0193  0.0376  -0.0059 352  HOH   B O   
7169 O  O   . HOH   G .   ? 0.3660 0.2239 0.3426 -0.0822 0.0288  -0.0926 353  HOH   B O   
7170 O  O   . HOH   G .   ? 0.4085 0.5958 0.7377 0.0494  0.0564  -0.0578 354  HOH   B O   
7171 O  O   . HOH   G .   ? 0.4950 0.2836 0.5765 -0.1063 0.2194  0.0124  355  HOH   B O   
7172 O  O   . HOH   G .   ? 0.3140 0.1788 0.3607 0.0464  -0.1170 -0.0445 356  HOH   B O   
7173 O  O   . HOH   G .   ? 0.3287 0.2887 0.3827 -0.0847 0.0124  -0.0949 357  HOH   B O   
7174 O  O   . HOH   G .   ? 0.5269 0.3208 0.4327 0.0202  0.1786  -0.0445 358  HOH   B O   
7175 O  O   . HOH   G .   ? 0.4249 0.5732 0.5371 0.2016  -0.0979 0.1703  359  HOH   B O   
7176 O  O   . HOH   G .   ? 0.4396 0.5228 0.5848 -0.0468 0.0484  -0.0149 360  HOH   B O   
7177 O  O   . HOH   G .   ? 0.4277 0.3304 0.4689 0.0578  -0.1665 -0.0243 361  HOH   B O   
7178 O  O   . HOH   G .   ? 0.5682 0.3548 0.6213 0.0697  0.1432  0.0845  362  HOH   B O   
7179 O  O   . HOH   G .   ? 0.2093 0.3458 0.6558 -0.0537 -0.0711 -0.0864 363  HOH   B O   
7180 O  O   . HOH   G .   ? 0.5475 0.6315 0.2769 0.2816  -0.0504 -0.0334 364  HOH   B O   
7181 O  O   . HOH   G .   ? 0.6504 0.4577 0.3794 0.1366  0.0752  0.0790  365  HOH   B O   
7182 O  O   . HOH   G .   ? 0.4682 0.3102 0.5819 -0.1413 -0.0707 0.0342  366  HOH   B O   
7183 O  O   . HOH   G .   ? 0.4794 0.5793 0.4152 -0.0749 -0.0691 -0.1222 367  HOH   B O   
7184 O  O   . HOH   G .   ? 0.6320 0.6085 0.3341 0.1976  -0.1458 0.0659  368  HOH   B O   
7185 O  O   . HOH   G .   ? 0.4504 0.6220 0.5101 0.2983  0.0700  0.1238  369  HOH   B O   
7186 O  O   . HOH   G .   ? 0.6124 0.2135 0.2834 -0.0063 0.0186  0.0410  370  HOH   B O   
7187 O  O   . HOH   G .   ? 0.5860 0.3482 0.4686 0.0800  -0.1459 0.0224  371  HOH   B O   
7188 O  O   . HOH   G .   ? 0.7546 0.7771 0.4775 0.2783  -0.1357 0.1463  372  HOH   B O   
7189 O  O   . HOH   G .   ? 0.6787 0.4138 0.3052 -0.1127 -0.0904 -0.0966 373  HOH   B O   
7190 O  O   . HOH   G .   ? 0.4553 0.3502 0.3182 0.0760  -0.1384 -0.0364 374  HOH   B O   
7191 O  O   . HOH   G .   ? 0.4453 0.7508 0.5946 0.1620  0.0977  0.3291  375  HOH   B O   
7192 O  O   . HOH   G .   ? 0.4255 0.4222 0.4950 -0.0659 -0.0696 0.0339  376  HOH   B O   
7193 O  O   . HOH   G .   ? 0.2233 0.4341 0.4538 0.0243  -0.0585 -0.1034 377  HOH   B O   
7194 O  O   . HOH   G .   ? 0.8224 0.3433 0.5351 -0.0715 -0.0963 -0.0191 378  HOH   B O   
7195 O  O   . HOH   G .   ? 0.2907 0.3880 0.1917 0.0700  0.0002  -0.0103 379  HOH   B O   
7196 O  O   . HOH   G .   ? 0.5227 0.6586 0.3452 -0.1412 0.0384  -0.1572 380  HOH   B O   
7197 O  O   . HOH   G .   ? 0.3630 0.5502 0.4957 0.1212  -0.0571 0.0110  381  HOH   B O   
7198 O  O   . HOH   G .   ? 0.5752 0.6428 0.7045 0.0287  0.2412  0.1650  382  HOH   B O   
7199 O  O   . HOH   G .   ? 0.2642 0.2455 0.3173 -0.0001 0.0123  0.0384  383  HOH   B O   
7200 O  O   . HOH   G .   ? 0.4231 0.7699 0.6341 0.1633  0.2518  0.0990  384  HOH   B O   
7201 O  O   . HOH   G .   ? 0.5418 0.4005 0.5901 -0.0510 -0.0094 0.0136  385  HOH   B O   
7202 O  O   . HOH   G .   ? 0.2147 0.3933 0.3727 -0.0483 -0.0824 -0.0203 386  HOH   B O   
7203 O  O   . HOH   G .   ? 0.5214 0.5560 0.3945 0.0139  -0.0846 -0.0672 387  HOH   B O   
7204 O  O   . HOH   G .   ? 0.6936 0.4345 0.4362 0.1336  -0.0110 -0.1375 388  HOH   B O   
7205 O  O   . HOH   G .   ? 0.5036 0.3305 0.2816 0.0339  0.0735  -0.0202 389  HOH   B O   
7206 O  O   . HOH   G .   ? 0.3808 0.2187 0.2888 0.0819  -0.0201 0.0106  390  HOH   B O   
7207 O  O   . HOH   G .   ? 0.5154 0.3808 0.3823 0.0115  0.0000  0.0526  391  HOH   B O   
7208 O  O   . HOH   G .   ? 0.8036 0.5967 0.4101 0.2974  -0.0583 -0.0010 392  HOH   B O   
7209 O  O   . HOH   G .   ? 0.4996 0.2212 0.5183 -0.0929 0.0015  0.0756  393  HOH   B O   
7210 O  O   . HOH   G .   ? 0.2459 0.4695 0.6322 -0.1514 -0.0617 -0.0224 394  HOH   B O   
7211 O  O   . HOH   G .   ? 0.4390 0.5925 0.3276 0.1574  -0.0774 -0.1173 395  HOH   B O   
7212 O  O   . HOH   G .   ? 0.3085 0.3281 0.3677 0.0194  0.0376  -0.0641 396  HOH   B O   
7213 O  O   . HOH   G .   ? 0.3989 0.3842 0.3974 0.0121  0.0929  0.0380  397  HOH   B O   
7214 O  O   . HOH   G .   ? 0.2022 0.2700 0.5462 -0.0541 -0.0688 0.0296  398  HOH   B O   
7215 O  O   . HOH   G .   ? 0.6232 0.6752 0.6823 0.2003  -0.0881 0.2539  399  HOH   B O   
7216 O  O   . HOH   G .   ? 0.5563 0.4021 0.2992 -0.2070 -0.0159 0.1202  400  HOH   B O   
7217 O  O   . HOH   G .   ? 0.6623 0.6347 0.3712 0.1000  -0.0949 0.0418  401  HOH   B O   
# 
