data_7HEO
# 
_entry.id   7HEO 
# 
_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   7HEO         pdb_00007heo 10.2210/pdb7heo/pdb 
WWPDB D_1001407378 ?            ?                   
# 
_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                        7HEO 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                    18178.766 2   
'3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'trifluoroacetic acid'                                                        114.023   1   ? ? ? ? 
3 non-polymer syn '(2S)-3-(4-iodophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' 394.210   1   ? ? ? ? 
4 non-polymer syn '(2R)-3-(4-iodophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' 394.210   1   ? ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                                                                35.453    1   ? ? ? ? 
6 water       nat water                                                                         18.015    422 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                                        TFA   
3 '(2S)-3-(4-iodophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' A1A94 
4 '(2R)-3-(4-iodophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' A1A93 
5 'CHLORIDE ION'                                                                CL    
6 water                                                                         HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A93 non-polymer         . '(2R)-3-(4-iodophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' ? 'C15 H15 I N4 O' 
394.210 
A1A94 non-polymer         . '(2S)-3-(4-iodophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' ? 'C15 H15 I N4 O' 
394.210 
ALA   'L-peptide linking' y ALANINE                                                                       ? 'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE                                                                      ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                    ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                               ? 'C4 H7 N O4'     
133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                                ? 'Cl -1'          
35.453  
CYS   'L-peptide linking' y CYSTEINE                                                                      ? 'C3 H7 N O2 S'   
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                     ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                               ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                       ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                     ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                         ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                    ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                       ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                        ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                    ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                 ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                       ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                        ? 'C3 H7 N O3'     
105.093 
TFA   non-polymer         . 'trifluoroacetic acid'                                                        ? 'C2 H F3 O2'     
114.023 
THR   'L-peptide linking' y THREONINE                                                                     ? 'C4 H9 N O3'     
119.119 
TYR   'L-peptide linking' y TYROSINE                                                                      ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                        ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TFA   1   201 201  TFA   TFA A . 
D 3 A1A94 1   202 201  A1A94 LA1 A . 
E 4 A1A93 1   203 301  A1A93 LA2 A . 
F 5 CL    1   204 1    CL    CL  A . 
G 6 HOH   1   301 86   HOH   HOH A . 
G 6 HOH   2   302 292  HOH   HOH A . 
G 6 HOH   3   303 196  HOH   HOH A . 
G 6 HOH   4   304 625  HOH   HOH A . 
G 6 HOH   5   305 247  HOH   HOH A . 
G 6 HOH   6   306 1289 HOH   HOH A . 
G 6 HOH   7   307 1301 HOH   HOH A . 
G 6 HOH   8   308 105  HOH   HOH A . 
G 6 HOH   9   309 1295 HOH   HOH A . 
G 6 HOH   10  310 661  HOH   HOH A . 
G 6 HOH   11  311 393  HOH   HOH A . 
G 6 HOH   12  312 192  HOH   HOH A . 
G 6 HOH   13  313 109  HOH   HOH A . 
G 6 HOH   14  314 39   HOH   HOH A . 
G 6 HOH   15  315 136  HOH   HOH A . 
G 6 HOH   16  316 229  HOH   HOH A . 
G 6 HOH   17  317 76   HOH   HOH A . 
G 6 HOH   18  318 209  HOH   HOH A . 
G 6 HOH   19  319 1310 HOH   HOH A . 
G 6 HOH   20  320 493  HOH   HOH A . 
G 6 HOH   21  321 57   HOH   HOH A . 
G 6 HOH   22  322 21   HOH   HOH A . 
G 6 HOH   23  323 124  HOH   HOH A . 
G 6 HOH   24  324 1283 HOH   HOH A . 
G 6 HOH   25  325 236  HOH   HOH A . 
G 6 HOH   26  326 11   HOH   HOH A . 
G 6 HOH   27  327 70   HOH   HOH A . 
G 6 HOH   28  328 18   HOH   HOH A . 
G 6 HOH   29  329 320  HOH   HOH A . 
G 6 HOH   30  330 409  HOH   HOH A . 
G 6 HOH   31  331 13   HOH   HOH A . 
G 6 HOH   32  332 15   HOH   HOH A . 
G 6 HOH   33  333 36   HOH   HOH A . 
G 6 HOH   34  334 381  HOH   HOH A . 
G 6 HOH   35  335 1300 HOH   HOH A . 
G 6 HOH   36  336 964  HOH   HOH A . 
G 6 HOH   37  337 151  HOH   HOH A . 
G 6 HOH   38  338 630  HOH   HOH A . 
G 6 HOH   39  339 281  HOH   HOH A . 
G 6 HOH   40  340 140  HOH   HOH A . 
G 6 HOH   41  341 241  HOH   HOH A . 
G 6 HOH   42  342 469  HOH   HOH A . 
G 6 HOH   43  343 153  HOH   HOH A . 
G 6 HOH   44  344 5    HOH   HOH A . 
G 6 HOH   45  345 17   HOH   HOH A . 
G 6 HOH   46  346 8    HOH   HOH A . 
G 6 HOH   47  347 132  HOH   HOH A . 
G 6 HOH   48  348 225  HOH   HOH A . 
G 6 HOH   49  349 164  HOH   HOH A . 
G 6 HOH   50  350 165  HOH   HOH A . 
G 6 HOH   51  351 42   HOH   HOH A . 
G 6 HOH   52  352 337  HOH   HOH A . 
G 6 HOH   53  353 2    HOH   HOH A . 
G 6 HOH   54  354 102  HOH   HOH A . 
G 6 HOH   55  355 1275 HOH   HOH A . 
G 6 HOH   56  356 354  HOH   HOH A . 
G 6 HOH   57  357 66   HOH   HOH A . 
G 6 HOH   58  358 92   HOH   HOH A . 
G 6 HOH   59  359 93   HOH   HOH A . 
G 6 HOH   60  360 33   HOH   HOH A . 
G 6 HOH   61  361 162  HOH   HOH A . 
G 6 HOH   62  362 24   HOH   HOH A . 
G 6 HOH   63  363 155  HOH   HOH A . 
G 6 HOH   64  364 396  HOH   HOH A . 
G 6 HOH   65  365 139  HOH   HOH A . 
G 6 HOH   66  366 169  HOH   HOH A . 
G 6 HOH   67  367 662  HOH   HOH A . 
G 6 HOH   68  368 2    HOH   HOH A . 
G 6 HOH   69  369 45   HOH   HOH A . 
G 6 HOH   70  370 159  HOH   HOH A . 
G 6 HOH   71  371 461  HOH   HOH A . 
G 6 HOH   72  372 5    HOH   HOH A . 
G 6 HOH   73  373 19   HOH   HOH A . 
G 6 HOH   74  374 96   HOH   HOH A . 
G 6 HOH   75  375 138  HOH   HOH A . 
G 6 HOH   76  376 939  HOH   HOH A . 
G 6 HOH   77  377 186  HOH   HOH A . 
G 6 HOH   78  378 1308 HOH   HOH A . 
G 6 HOH   79  379 296  HOH   HOH A . 
G 6 HOH   80  380 81   HOH   HOH A . 
G 6 HOH   81  381 140  HOH   HOH A . 
G 6 HOH   82  382 56   HOH   HOH A . 
G 6 HOH   83  383 46   HOH   HOH A . 
G 6 HOH   84  384 62   HOH   HOH A . 
G 6 HOH   85  385 27   HOH   HOH A . 
G 6 HOH   86  386 115  HOH   HOH A . 
G 6 HOH   87  387 49   HOH   HOH A . 
G 6 HOH   88  388 218  HOH   HOH A . 
G 6 HOH   89  389 26   HOH   HOH A . 
G 6 HOH   90  390 134  HOH   HOH A . 
G 6 HOH   91  391 35   HOH   HOH A . 
G 6 HOH   92  392 366  HOH   HOH A . 
G 6 HOH   93  393 4    HOH   HOH A . 
G 6 HOH   94  394 85   HOH   HOH A . 
G 6 HOH   95  395 154  HOH   HOH A . 
G 6 HOH   96  396 6    HOH   HOH A . 
G 6 HOH   97  397 34   HOH   HOH A . 
G 6 HOH   98  398 303  HOH   HOH A . 
G 6 HOH   99  399 116  HOH   HOH A . 
G 6 HOH   100 400 74   HOH   HOH A . 
G 6 HOH   101 401 6    HOH   HOH A . 
G 6 HOH   102 402 58   HOH   HOH A . 
G 6 HOH   103 403 12   HOH   HOH A . 
G 6 HOH   104 404 195  HOH   HOH A . 
G 6 HOH   105 405 199  HOH   HOH A . 
G 6 HOH   106 406 83   HOH   HOH A . 
G 6 HOH   107 407 1290 HOH   HOH A . 
G 6 HOH   108 408 68   HOH   HOH A . 
G 6 HOH   109 409 67   HOH   HOH A . 
G 6 HOH   110 410 1315 HOH   HOH A . 
G 6 HOH   111 411 351  HOH   HOH A . 
G 6 HOH   112 412 148  HOH   HOH A . 
G 6 HOH   113 413 1068 HOH   HOH A . 
G 6 HOH   114 414 3    HOH   HOH A . 
G 6 HOH   115 415 7    HOH   HOH A . 
G 6 HOH   116 416 25   HOH   HOH A . 
G 6 HOH   117 417 121  HOH   HOH A . 
G 6 HOH   118 418 123  HOH   HOH A . 
G 6 HOH   119 419 278  HOH   HOH A . 
G 6 HOH   120 420 333  HOH   HOH A . 
G 6 HOH   121 421 125  HOH   HOH A . 
G 6 HOH   122 422 95   HOH   HOH A . 
G 6 HOH   123 423 53   HOH   HOH A . 
G 6 HOH   124 424 51   HOH   HOH A . 
G 6 HOH   125 425 78   HOH   HOH A . 
G 6 HOH   126 426 1279 HOH   HOH A . 
G 6 HOH   127 427 397  HOH   HOH A . 
G 6 HOH   128 428 1313 HOH   HOH A . 
G 6 HOH   129 429 1309 HOH   HOH A . 
G 6 HOH   130 430 156  HOH   HOH A . 
G 6 HOH   131 431 212  HOH   HOH A . 
G 6 HOH   132 432 122  HOH   HOH A . 
G 6 HOH   133 433 582  HOH   HOH A . 
G 6 HOH   134 434 40   HOH   HOH A . 
G 6 HOH   135 435 1222 HOH   HOH A . 
G 6 HOH   136 436 188  HOH   HOH A . 
G 6 HOH   137 437 405  HOH   HOH A . 
G 6 HOH   138 438 1296 HOH   HOH A . 
G 6 HOH   139 439 1189 HOH   HOH A . 
G 6 HOH   140 440 1286 HOH   HOH A . 
G 6 HOH   141 441 71   HOH   HOH A . 
G 6 HOH   142 442 80   HOH   HOH A . 
G 6 HOH   143 443 3    HOH   HOH A . 
G 6 HOH   144 444 73   HOH   HOH A . 
G 6 HOH   145 445 16   HOH   HOH A . 
G 6 HOH   146 446 944  HOH   HOH A . 
G 6 HOH   147 447 94   HOH   HOH A . 
G 6 HOH   148 448 952  HOH   HOH A . 
G 6 HOH   149 449 1238 HOH   HOH A . 
G 6 HOH   150 450 97   HOH   HOH A . 
G 6 HOH   151 451 79   HOH   HOH A . 
G 6 HOH   152 452 104  HOH   HOH A . 
G 6 HOH   153 453 576  HOH   HOH A . 
G 6 HOH   154 454 1094 HOH   HOH A . 
G 6 HOH   155 455 1119 HOH   HOH A . 
G 6 HOH   156 456 330  HOH   HOH A . 
G 6 HOH   157 457 1134 HOH   HOH A . 
G 6 HOH   158 458 107  HOH   HOH A . 
G 6 HOH   159 459 509  HOH   HOH A . 
G 6 HOH   160 460 163  HOH   HOH A . 
G 6 HOH   161 461 726  HOH   HOH A . 
G 6 HOH   162 462 14   HOH   HOH A . 
G 6 HOH   163 463 408  HOH   HOH A . 
G 6 HOH   164 464 756  HOH   HOH A . 
G 6 HOH   165 465 556  HOH   HOH A . 
G 6 HOH   166 466 63   HOH   HOH A . 
G 6 HOH   167 467 126  HOH   HOH A . 
G 6 HOH   168 468 1276 HOH   HOH A . 
G 6 HOH   169 469 319  HOH   HOH A . 
G 6 HOH   170 470 361  HOH   HOH A . 
G 6 HOH   171 471 280  HOH   HOH A . 
G 6 HOH   172 472 370  HOH   HOH A . 
G 6 HOH   173 473 801  HOH   HOH A . 
G 6 HOH   174 474 342  HOH   HOH A . 
G 6 HOH   175 475 1307 HOH   HOH A . 
G 6 HOH   176 476 250  HOH   HOH A . 
G 6 HOH   177 477 9    HOH   HOH A . 
G 6 HOH   178 478 267  HOH   HOH A . 
G 6 HOH   179 479 224  HOH   HOH A . 
G 6 HOH   180 480 1306 HOH   HOH A . 
G 6 HOH   181 481 1287 HOH   HOH A . 
G 6 HOH   182 482 135  HOH   HOH A . 
G 6 HOH   183 483 919  HOH   HOH A . 
G 6 HOH   184 484 695  HOH   HOH A . 
G 6 HOH   185 485 674  HOH   HOH A . 
G 6 HOH   186 486 202  HOH   HOH A . 
G 6 HOH   187 487 521  HOH   HOH A . 
G 6 HOH   188 488 10   HOH   HOH A . 
G 6 HOH   189 489 326  HOH   HOH A . 
G 6 HOH   190 490 1299 HOH   HOH A . 
G 6 HOH   191 491 309  HOH   HOH A . 
G 6 HOH   192 492 318  HOH   HOH A . 
G 6 HOH   193 493 711  HOH   HOH A . 
G 6 HOH   194 494 941  HOH   HOH A . 
G 6 HOH   195 495 315  HOH   HOH A . 
G 6 HOH   196 496 1314 HOH   HOH A . 
G 6 HOH   197 497 805  HOH   HOH A . 
G 6 HOH   198 498 331  HOH   HOH A . 
G 6 HOH   199 499 263  HOH   HOH A . 
G 6 HOH   200 500 152  HOH   HOH A . 
G 6 HOH   201 501 356  HOH   HOH A . 
G 6 HOH   202 502 208  HOH   HOH A . 
G 6 HOH   203 503 350  HOH   HOH A . 
G 6 HOH   204 504 180  HOH   HOH A . 
G 6 HOH   205 505 1071 HOH   HOH A . 
G 6 HOH   206 506 4    HOH   HOH A . 
G 6 HOH   207 507 363  HOH   HOH A . 
G 6 HOH   208 508 371  HOH   HOH A . 
G 6 HOH   209 509 313  HOH   HOH A . 
G 6 HOH   210 510 12   HOH   HOH A . 
G 6 HOH   211 511 1284 HOH   HOH A . 
G 6 HOH   212 512 185  HOH   HOH A . 
G 6 HOH   213 513 429  HOH   HOH A . 
G 6 HOH   214 514 772  HOH   HOH A . 
G 6 HOH   215 515 70   HOH   HOH A . 
G 6 HOH   216 516 376  HOH   HOH A . 
G 6 HOH   217 517 7    HOH   HOH A . 
G 6 HOH   218 518 1074 HOH   HOH A . 
G 6 HOH   219 519 8    HOH   HOH A . 
G 6 HOH   220 520 1292 HOH   HOH A . 
G 6 HOH   221 521 346  HOH   HOH A . 
G 6 HOH   222 522 1078 HOH   HOH A . 
H 6 HOH   1   201 64   HOH   HOH B . 
H 6 HOH   2   202 531  HOH   HOH B . 
H 6 HOH   3   203 549  HOH   HOH B . 
H 6 HOH   4   204 240  HOH   HOH B . 
H 6 HOH   5   205 364  HOH   HOH B . 
H 6 HOH   6   206 900  HOH   HOH B . 
H 6 HOH   7   207 452  HOH   HOH B . 
H 6 HOH   8   208 654  HOH   HOH B . 
H 6 HOH   9   209 358  HOH   HOH B . 
H 6 HOH   10  210 120  HOH   HOH B . 
H 6 HOH   11  211 758  HOH   HOH B . 
H 6 HOH   12  212 1249 HOH   HOH B . 
H 6 HOH   13  213 398  HOH   HOH B . 
H 6 HOH   14  214 743  HOH   HOH B . 
H 6 HOH   15  215 444  HOH   HOH B . 
H 6 HOH   16  216 50   HOH   HOH B . 
H 6 HOH   17  217 343  HOH   HOH B . 
H 6 HOH   18  218 232  HOH   HOH B . 
H 6 HOH   19  219 282  HOH   HOH B . 
H 6 HOH   20  220 332  HOH   HOH B . 
H 6 HOH   21  221 264  HOH   HOH B . 
H 6 HOH   22  222 353  HOH   HOH B . 
H 6 HOH   23  223 1278 HOH   HOH B . 
H 6 HOH   24  224 276  HOH   HOH B . 
H 6 HOH   25  225 131  HOH   HOH B . 
H 6 HOH   26  226 205  HOH   HOH B . 
H 6 HOH   27  227 1140 HOH   HOH B . 
H 6 HOH   28  228 54   HOH   HOH B . 
H 6 HOH   29  229 82   HOH   HOH B . 
H 6 HOH   30  230 723  HOH   HOH B . 
H 6 HOH   31  231 75   HOH   HOH B . 
H 6 HOH   32  232 166  HOH   HOH B . 
H 6 HOH   33  233 128  HOH   HOH B . 
H 6 HOH   34  234 1312 HOH   HOH B . 
H 6 HOH   35  235 272  HOH   HOH B . 
H 6 HOH   36  236 172  HOH   HOH B . 
H 6 HOH   37  237 129  HOH   HOH B . 
H 6 HOH   38  238 133  HOH   HOH B . 
H 6 HOH   39  239 181  HOH   HOH B . 
H 6 HOH   40  240 60   HOH   HOH B . 
H 6 HOH   41  241 69   HOH   HOH B . 
H 6 HOH   42  242 14   HOH   HOH B . 
H 6 HOH   43  243 127  HOH   HOH B . 
H 6 HOH   44  244 1    HOH   HOH B . 
H 6 HOH   45  245 300  HOH   HOH B . 
H 6 HOH   46  246 110  HOH   HOH B . 
H 6 HOH   47  247 144  HOH   HOH B . 
H 6 HOH   48  248 325  HOH   HOH B . 
H 6 HOH   49  249 9    HOH   HOH B . 
H 6 HOH   50  250 347  HOH   HOH B . 
H 6 HOH   51  251 30   HOH   HOH B . 
H 6 HOH   52  252 391  HOH   HOH B . 
H 6 HOH   53  253 52   HOH   HOH B . 
H 6 HOH   54  254 231  HOH   HOH B . 
H 6 HOH   55  255 72   HOH   HOH B . 
H 6 HOH   56  256 41   HOH   HOH B . 
H 6 HOH   57  257 143  HOH   HOH B . 
H 6 HOH   58  258 252  HOH   HOH B . 
H 6 HOH   59  259 31   HOH   HOH B . 
H 6 HOH   60  260 302  HOH   HOH B . 
H 6 HOH   61  261 47   HOH   HOH B . 
H 6 HOH   62  262 59   HOH   HOH B . 
H 6 HOH   63  263 150  HOH   HOH B . 
H 6 HOH   64  264 242  HOH   HOH B . 
H 6 HOH   65  265 10   HOH   HOH B . 
H 6 HOH   66  266 1277 HOH   HOH B . 
H 6 HOH   67  267 84   HOH   HOH B . 
H 6 HOH   68  268 243  HOH   HOH B . 
H 6 HOH   69  269 103  HOH   HOH B . 
H 6 HOH   70  270 271  HOH   HOH B . 
H 6 HOH   71  271 287  HOH   HOH B . 
H 6 HOH   72  272 61   HOH   HOH B . 
H 6 HOH   73  273 77   HOH   HOH B . 
H 6 HOH   74  274 11   HOH   HOH B . 
H 6 HOH   75  275 117  HOH   HOH B . 
H 6 HOH   76  276 114  HOH   HOH B . 
H 6 HOH   77  277 416  HOH   HOH B . 
H 6 HOH   78  278 20   HOH   HOH B . 
H 6 HOH   79  279 175  HOH   HOH B . 
H 6 HOH   80  280 1305 HOH   HOH B . 
H 6 HOH   81  281 147  HOH   HOH B . 
H 6 HOH   82  282 235  HOH   HOH B . 
H 6 HOH   83  283 22   HOH   HOH B . 
H 6 HOH   84  284 43   HOH   HOH B . 
H 6 HOH   85  285 216  HOH   HOH B . 
H 6 HOH   86  286 1106 HOH   HOH B . 
H 6 HOH   87  287 89   HOH   HOH B . 
H 6 HOH   88  288 106  HOH   HOH B . 
H 6 HOH   89  289 387  HOH   HOH B . 
H 6 HOH   90  290 13   HOH   HOH B . 
H 6 HOH   91  291 1066 HOH   HOH B . 
H 6 HOH   92  292 112  HOH   HOH B . 
H 6 HOH   93  293 137  HOH   HOH B . 
H 6 HOH   94  294 160  HOH   HOH B . 
H 6 HOH   95  295 220  HOH   HOH B . 
H 6 HOH   96  296 88   HOH   HOH B . 
H 6 HOH   97  297 221  HOH   HOH B . 
H 6 HOH   98  298 1285 HOH   HOH B . 
H 6 HOH   99  299 299  HOH   HOH B . 
H 6 HOH   100 300 32   HOH   HOH B . 
H 6 HOH   101 301 316  HOH   HOH B . 
H 6 HOH   102 302 99   HOH   HOH B . 
H 6 HOH   103 303 142  HOH   HOH B . 
H 6 HOH   104 304 635  HOH   HOH B . 
H 6 HOH   105 305 118  HOH   HOH B . 
H 6 HOH   106 306 311  HOH   HOH B . 
H 6 HOH   107 307 38   HOH   HOH B . 
H 6 HOH   108 308 101  HOH   HOH B . 
H 6 HOH   109 309 170  HOH   HOH B . 
H 6 HOH   110 310 215  HOH   HOH B . 
H 6 HOH   111 311 37   HOH   HOH B . 
H 6 HOH   112 312 91   HOH   HOH B . 
H 6 HOH   113 313 48   HOH   HOH B . 
H 6 HOH   114 314 297  HOH   HOH B . 
H 6 HOH   115 315 1274 HOH   HOH B . 
H 6 HOH   116 316 23   HOH   HOH B . 
H 6 HOH   117 317 177  HOH   HOH B . 
H 6 HOH   118 318 141  HOH   HOH B . 
H 6 HOH   119 319 28   HOH   HOH B . 
H 6 HOH   120 320 44   HOH   HOH B . 
H 6 HOH   121 321 197  HOH   HOH B . 
H 6 HOH   122 322 341  HOH   HOH B . 
H 6 HOH   123 323 704  HOH   HOH B . 
H 6 HOH   124 324 161  HOH   HOH B . 
H 6 HOH   125 325 100  HOH   HOH B . 
H 6 HOH   126 326 1126 HOH   HOH B . 
H 6 HOH   127 327 29   HOH   HOH B . 
H 6 HOH   128 328 1291 HOH   HOH B . 
H 6 HOH   129 329 334  HOH   HOH B . 
H 6 HOH   130 330 1294 HOH   HOH B . 
H 6 HOH   131 331 55   HOH   HOH B . 
H 6 HOH   132 332 182  HOH   HOH B . 
H 6 HOH   133 333 717  HOH   HOH B . 
H 6 HOH   134 334 98   HOH   HOH B . 
H 6 HOH   135 335 234  HOH   HOH B . 
H 6 HOH   136 336 339  HOH   HOH B . 
H 6 HOH   137 337 207  HOH   HOH B . 
H 6 HOH   138 338 65   HOH   HOH B . 
H 6 HOH   139 339 445  HOH   HOH B . 
H 6 HOH   140 340 619  HOH   HOH B . 
H 6 HOH   141 341 1293 HOH   HOH B . 
H 6 HOH   142 342 178  HOH   HOH B . 
H 6 HOH   143 343 362  HOH   HOH B . 
H 6 HOH   144 344 960  HOH   HOH B . 
H 6 HOH   145 345 90   HOH   HOH B . 
H 6 HOH   146 346 463  HOH   HOH B . 
H 6 HOH   147 347 335  HOH   HOH B . 
H 6 HOH   148 348 1304 HOH   HOH B . 
H 6 HOH   149 349 623  HOH   HOH B . 
H 6 HOH   150 350 1046 HOH   HOH B . 
H 6 HOH   151 351 191  HOH   HOH B . 
H 6 HOH   152 352 304  HOH   HOH B . 
H 6 HOH   153 353 87   HOH   HOH B . 
H 6 HOH   154 354 290  HOH   HOH B . 
H 6 HOH   155 355 541  HOH   HOH B . 
H 6 HOH   156 356 1280 HOH   HOH B . 
H 6 HOH   157 357 203  HOH   HOH B . 
H 6 HOH   158 358 1077 HOH   HOH B . 
H 6 HOH   159 359 479  HOH   HOH B . 
H 6 HOH   160 360 389  HOH   HOH B . 
H 6 HOH   161 361 718  HOH   HOH B . 
H 6 HOH   162 362 283  HOH   HOH B . 
H 6 HOH   163 363 1072 HOH   HOH B . 
H 6 HOH   164 364 1316 HOH   HOH B . 
H 6 HOH   165 365 898  HOH   HOH B . 
H 6 HOH   166 366 373  HOH   HOH B . 
H 6 HOH   167 367 340  HOH   HOH B . 
H 6 HOH   168 368 291  HOH   HOH B . 
H 6 HOH   169 369 615  HOH   HOH B . 
H 6 HOH   170 370 667  HOH   HOH B . 
H 6 HOH   171 371 1303 HOH   HOH B . 
H 6 HOH   172 372 190  HOH   HOH B . 
H 6 HOH   173 373 310  HOH   HOH B . 
H 6 HOH   174 374 431  HOH   HOH B . 
H 6 HOH   175 375 1173 HOH   HOH B . 
H 6 HOH   176 376 149  HOH   HOH B . 
H 6 HOH   177 377 183  HOH   HOH B . 
H 6 HOH   178 378 1000 HOH   HOH B . 
H 6 HOH   179 379 418  HOH   HOH B . 
H 6 HOH   180 380 1163 HOH   HOH B . 
H 6 HOH   181 381 1311 HOH   HOH B . 
H 6 HOH   182 382 176  HOH   HOH B . 
H 6 HOH   183 383 424  HOH   HOH B . 
H 6 HOH   184 384 981  HOH   HOH B . 
H 6 HOH   185 385 491  HOH   HOH B . 
H 6 HOH   186 386 470  HOH   HOH B . 
H 6 HOH   187 387 265  HOH   HOH B . 
H 6 HOH   188 388 1298 HOH   HOH B . 
H 6 HOH   189 389 248  HOH   HOH B . 
H 6 HOH   190 390 184  HOH   HOH B . 
H 6 HOH   191 391 360  HOH   HOH B . 
H 6 HOH   192 392 355  HOH   HOH B . 
H 6 HOH   193 393 410  HOH   HOH B . 
H 6 HOH   194 394 566  HOH   HOH B . 
H 6 HOH   195 395 274  HOH   HOH B . 
H 6 HOH   196 396 314  HOH   HOH B . 
H 6 HOH   197 397 157  HOH   HOH B . 
H 6 HOH   198 398 792  HOH   HOH B . 
H 6 HOH   199 399 321  HOH   HOH B . 
H 6 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HEO 
_cell.length_a           88.856 
_cell.length_b           88.856 
_cell.length_c           39.516 
_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                         7HEO 
_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          7HEO 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.78 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-24 
_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                     7HEO 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.430 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   156467 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.800 
_reflns.pdbx_Rmerge_I_obs            0.040 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        18.200 
_reflns.B_iso_Wilson_estimate        11.430 
_reflns.pdbx_redundancy              6.500 
_reflns.pdbx_Rrim_I_all              0.043 
_reflns.pdbx_Rpim_I_all              0.017 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1013137 
_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  ? 41917 7478 ? 0.830 ? ? ? 5.600 ? 1.500  ? ? ? ? ? ? 96.200 0.916 0.379 0.831 
1 2 5.590 44.430 ? 7086  1037 ? 0.025 ? ? ? 6.800 ? 59.100 ? ? ? ? ? ? 99.700 0.027 0.010 0.999 
# 
_refine.entry_id                                 7HEO 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             39.7400 
_refine.pdbx_ls_sigma_F                          1.360 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.7000 
_refine.ls_number_reflns_obs                     156392 
_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                          0.1398 
_refine.ls_R_factor_R_work                       0.1391 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1526 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7544 
_refine.ls_number_reflns_R_work                  148848 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.1494 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.0900 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                67.020 
_refine.B_iso_min                                8.080 
_refine.pdbx_overall_phase_error                 15.3800 
_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                        39.7400 
_refine_hist.pdbx_number_atoms_ligand         80 
_refine_hist.number_atoms_solvent             422 
_refine_hist.number_atoms_total               3044 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           13.80 
_refine_hist.pdbx_B_iso_mean_solvent          29.75 
_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 94.0000  4707 . 0.2935 0.3073 . 199 0.0000 4906 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 4938 . 0.2397 0.2310 . 275 0.0000 5213 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 4921 . 0.2076 0.2049 . 268 0.0000 5189 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 4917 . 0.1916 0.2214 . 283 0.0000 5200 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 4921 . 0.1925 0.2218 . 249 0.0000 5170 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 4992 . 0.1829 0.2031 . 230 0.0000 5222 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 100.0000 4887 . 0.1638 0.1799 . 266 0.0000 5153 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5048 . 0.1540 0.1708 . 221 0.0000 5269 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 4897 . 0.1425 0.1609 . 245 0.0000 5142 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 5000 . 0.1319 0.1542 . 254 0.0000 5254 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 4927 . 0.1242 0.1533 . 245 0.0000 5172 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 4914 . 0.1216 0.1571 . 273 0.0000 5187 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5011 . 0.1145 0.1396 . 225 0.0000 5236 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 4934 . 0.1177 0.1333 . 247 0.0000 5181 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 4933 . 0.1204 0.1357 . 252 0.0000 5185 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 4999 . 0.1240 0.1368 . 262 0.0000 5261 . 'X-RAY DIFFRACTION' 
1.3200 1.3500  30 100.0000 4942 . 0.1278 0.1468 . 247 0.0000 5189 . 'X-RAY DIFFRACTION' 
1.3500 1.3800  30 100.0000 4945 . 0.1290 0.1513 . 264 0.0000 5209 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 4981 . 0.1247 0.1568 . 238 0.0000 5219 . 'X-RAY DIFFRACTION' 
1.4300 1.4700  30 100.0000 4976 . 0.1216 0.1283 . 248 0.0000 5224 . 'X-RAY DIFFRACTION' 
1.4700 1.5200  30 100.0000 4990 . 0.1155 0.1299 . 239 0.0000 5229 . 'X-RAY DIFFRACTION' 
1.5200 1.5800  30 100.0000 4978 . 0.1163 0.1287 . 269 0.0000 5247 . 'X-RAY DIFFRACTION' 
1.5800 1.6600  30 100.0000 4933 . 0.1171 0.1267 . 258 0.0000 5191 . 'X-RAY DIFFRACTION' 
1.6600 1.7400  30 100.0000 5037 . 0.1259 0.1466 . 206 0.0000 5243 . 'X-RAY DIFFRACTION' 
1.7400 1.8500  30 100.0000 4951 . 0.1306 0.1413 . 290 0.0000 5241 . 'X-RAY DIFFRACTION' 
1.8500 2.0000  30 100.0000 4990 . 0.1335 0.1362 . 249 0.0000 5239 . 'X-RAY DIFFRACTION' 
2.0000 2.2000  30 100.0000 4952 . 0.1374 0.1359 . 288 0.0000 5240 . 'X-RAY DIFFRACTION' 
2.2000 2.5200  30 100.0000 5031 . 0.1371 0.1437 . 252 0.0000 5283 . 'X-RAY DIFFRACTION' 
2.5200 3.1700  30 100.0000 5020 . 0.1506 0.1564 . 252 0.0000 5272 . 'X-RAY DIFFRACTION' 
3.1700 39.7400 30 100.0000 5176 . 0.1469 0.1740 . 250 0.0000 5426 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HEO 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003686' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HEO 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HEO A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HEO 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 7HEO SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HEO MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HEO SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HEO MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G 
2 1 B,H         
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HEO 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.05   -133.04 
2 1 SER A 128 ? B 68.09   -0.35   
3 1 PHE A 168 ? B -145.11 -60.38  
4 1 HIS B 86  ? ? 57.16   -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 520 ? 5.97 . 
2 1 O ? A HOH 521 ? 5.97 . 
3 1 O ? A HOH 522 ? 7.58 . 
4 1 O ? B HOH 400 ? 6.31 . 
# 
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 
A1A93 O1   O  N N 1   
A1A93 C1   C  N N 2   
A1A93 C2   C  N R 3   
A1A93 C3   C  N N 4   
A1A93 C4   C  Y N 5   
A1A93 C5   C  Y N 6   
A1A93 C6   C  Y N 7   
A1A93 C7   C  Y N 8   
A1A93 C8   C  Y N 9   
A1A93 C10  C  Y N 10  
A1A93 C11  C  Y N 11  
A1A93 C12  C  Y N 12  
A1A93 C13  C  Y N 13  
A1A93 C14  C  Y N 14  
A1A93 C15  C  Y N 15  
A1A93 C9   C  Y N 16  
A1A93 I1   I  N N 17  
A1A93 N1   N  N N 18  
A1A93 N2   N  Y N 19  
A1A93 N3   N  Y N 20  
A1A93 N4   N  Y N 21  
A1A93 H2   H  N N 22  
A1A93 H3   H  N N 23  
A1A93 H4   H  N N 24  
A1A93 H1   H  N N 25  
A1A93 H6   H  N N 26  
A1A93 H5   H  N N 27  
A1A93 H7   H  N N 28  
A1A93 H8   H  N N 29  
A1A93 H9   H  N N 30  
A1A93 H12  H  N N 31  
A1A93 H13  H  N N 32  
A1A93 H14  H  N N 33  
A1A93 H10  H  N N 34  
A1A93 H11  H  N N 35  
A1A93 H15  H  N N 36  
A1A94 N2   N  Y N 37  
A1A94 C3   C  N N 38  
A1A94 C6   C  Y N 39  
A1A94 C9   C  Y N 40  
A1A94 C12  C  Y N 41  
A1A94 C14  C  Y N 42  
A1A94 C1   C  N N 43  
A1A94 C10  C  Y N 44  
A1A94 C11  C  Y N 45  
A1A94 C13  C  Y N 46  
A1A94 C15  C  Y N 47  
A1A94 C2   C  N S 48  
A1A94 C4   C  Y N 49  
A1A94 C5   C  Y N 50  
A1A94 C7   C  Y N 51  
A1A94 C8   C  Y N 52  
A1A94 I1   I  N N 53  
A1A94 N1   N  N N 54  
A1A94 N3   N  Y N 55  
A1A94 N4   N  Y N 56  
A1A94 O1   O  N N 57  
A1A94 H5   H  N N 58  
A1A94 H6   H  N N 59  
A1A94 H8   H  N N 60  
A1A94 H10  H  N N 61  
A1A94 H13  H  N N 62  
A1A94 H4   H  N N 63  
A1A94 H3   H  N N 64  
A1A94 H12  H  N N 65  
A1A94 H14  H  N N 66  
A1A94 H1   H  N N 67  
A1A94 H7   H  N N 68  
A1A94 H9   H  N N 69  
A1A94 H11  H  N N 70  
A1A94 H15  H  N N 71  
A1A94 H2   H  N N 72  
ALA   N    N  N N 73  
ALA   CA   C  N S 74  
ALA   C    C  N N 75  
ALA   O    O  N N 76  
ALA   CB   C  N N 77  
ALA   OXT  O  N N 78  
ALA   H    H  N N 79  
ALA   H2   H  N N 80  
ALA   HA   H  N N 81  
ALA   HB1  H  N N 82  
ALA   HB2  H  N N 83  
ALA   HB3  H  N N 84  
ALA   HXT  H  N N 85  
ARG   N    N  N N 86  
ARG   CA   C  N S 87  
ARG   C    C  N N 88  
ARG   O    O  N N 89  
ARG   CB   C  N N 90  
ARG   CG   C  N N 91  
ARG   CD   C  N N 92  
ARG   NE   N  N N 93  
ARG   CZ   C  N N 94  
ARG   NH1  N  N N 95  
ARG   NH2  N  N N 96  
ARG   OXT  O  N N 97  
ARG   H    H  N N 98  
ARG   H2   H  N N 99  
ARG   HA   H  N N 100 
ARG   HB2  H  N N 101 
ARG   HB3  H  N N 102 
ARG   HG2  H  N N 103 
ARG   HG3  H  N N 104 
ARG   HD2  H  N N 105 
ARG   HD3  H  N N 106 
ARG   HE   H  N N 107 
ARG   HH11 H  N N 108 
ARG   HH12 H  N N 109 
ARG   HH21 H  N N 110 
ARG   HH22 H  N N 111 
ARG   HXT  H  N N 112 
ASN   N    N  N N 113 
ASN   CA   C  N S 114 
ASN   C    C  N N 115 
ASN   O    O  N N 116 
ASN   CB   C  N N 117 
ASN   CG   C  N N 118 
ASN   OD1  O  N N 119 
ASN   ND2  N  N N 120 
ASN   OXT  O  N N 121 
ASN   H    H  N N 122 
ASN   H2   H  N N 123 
ASN   HA   H  N N 124 
ASN   HB2  H  N N 125 
ASN   HB3  H  N N 126 
ASN   HD21 H  N N 127 
ASN   HD22 H  N N 128 
ASN   HXT  H  N N 129 
ASP   N    N  N N 130 
ASP   CA   C  N S 131 
ASP   C    C  N N 132 
ASP   O    O  N N 133 
ASP   CB   C  N N 134 
ASP   CG   C  N N 135 
ASP   OD1  O  N N 136 
ASP   OD2  O  N N 137 
ASP   OXT  O  N N 138 
ASP   H    H  N N 139 
ASP   H2   H  N N 140 
ASP   HA   H  N N 141 
ASP   HB2  H  N N 142 
ASP   HB3  H  N N 143 
ASP   HD2  H  N N 144 
ASP   HXT  H  N N 145 
CL    CL   CL N N 146 
CYS   N    N  N N 147 
CYS   CA   C  N R 148 
CYS   C    C  N N 149 
CYS   O    O  N N 150 
CYS   CB   C  N N 151 
CYS   SG   S  N N 152 
CYS   OXT  O  N N 153 
CYS   H    H  N N 154 
CYS   H2   H  N N 155 
CYS   HA   H  N N 156 
CYS   HB2  H  N N 157 
CYS   HB3  H  N N 158 
CYS   HG   H  N N 159 
CYS   HXT  H  N N 160 
GLN   N    N  N N 161 
GLN   CA   C  N S 162 
GLN   C    C  N N 163 
GLN   O    O  N N 164 
GLN   CB   C  N N 165 
GLN   CG   C  N N 166 
GLN   CD   C  N N 167 
GLN   OE1  O  N N 168 
GLN   NE2  N  N N 169 
GLN   OXT  O  N N 170 
GLN   H    H  N N 171 
GLN   H2   H  N N 172 
GLN   HA   H  N N 173 
GLN   HB2  H  N N 174 
GLN   HB3  H  N N 175 
GLN   HG2  H  N N 176 
GLN   HG3  H  N N 177 
GLN   HE21 H  N N 178 
GLN   HE22 H  N N 179 
GLN   HXT  H  N N 180 
GLU   N    N  N N 181 
GLU   CA   C  N S 182 
GLU   C    C  N N 183 
GLU   O    O  N N 184 
GLU   CB   C  N N 185 
GLU   CG   C  N N 186 
GLU   CD   C  N N 187 
GLU   OE1  O  N N 188 
GLU   OE2  O  N N 189 
GLU   OXT  O  N N 190 
GLU   H    H  N N 191 
GLU   H2   H  N N 192 
GLU   HA   H  N N 193 
GLU   HB2  H  N N 194 
GLU   HB3  H  N N 195 
GLU   HG2  H  N N 196 
GLU   HG3  H  N N 197 
GLU   HE2  H  N N 198 
GLU   HXT  H  N N 199 
GLY   N    N  N N 200 
GLY   CA   C  N N 201 
GLY   C    C  N N 202 
GLY   O    O  N N 203 
GLY   OXT  O  N N 204 
GLY   H    H  N N 205 
GLY   H2   H  N N 206 
GLY   HA2  H  N N 207 
GLY   HA3  H  N N 208 
GLY   HXT  H  N N 209 
HIS   N    N  N N 210 
HIS   CA   C  N S 211 
HIS   C    C  N N 212 
HIS   O    O  N N 213 
HIS   CB   C  N N 214 
HIS   CG   C  Y N 215 
HIS   ND1  N  Y N 216 
HIS   CD2  C  Y N 217 
HIS   CE1  C  Y N 218 
HIS   NE2  N  Y N 219 
HIS   OXT  O  N N 220 
HIS   H    H  N N 221 
HIS   H2   H  N N 222 
HIS   HA   H  N N 223 
HIS   HB2  H  N N 224 
HIS   HB3  H  N N 225 
HIS   HD1  H  N N 226 
HIS   HD2  H  N N 227 
HIS   HE1  H  N N 228 
HIS   HE2  H  N N 229 
HIS   HXT  H  N N 230 
HOH   O    O  N N 231 
HOH   H1   H  N N 232 
HOH   H2   H  N N 233 
ILE   N    N  N N 234 
ILE   CA   C  N S 235 
ILE   C    C  N N 236 
ILE   O    O  N N 237 
ILE   CB   C  N S 238 
ILE   CG1  C  N N 239 
ILE   CG2  C  N N 240 
ILE   CD1  C  N N 241 
ILE   OXT  O  N N 242 
ILE   H    H  N N 243 
ILE   H2   H  N N 244 
ILE   HA   H  N N 245 
ILE   HB   H  N N 246 
ILE   HG12 H  N N 247 
ILE   HG13 H  N N 248 
ILE   HG21 H  N N 249 
ILE   HG22 H  N N 250 
ILE   HG23 H  N N 251 
ILE   HD11 H  N N 252 
ILE   HD12 H  N N 253 
ILE   HD13 H  N N 254 
ILE   HXT  H  N N 255 
LEU   N    N  N N 256 
LEU   CA   C  N S 257 
LEU   C    C  N N 258 
LEU   O    O  N N 259 
LEU   CB   C  N N 260 
LEU   CG   C  N N 261 
LEU   CD1  C  N N 262 
LEU   CD2  C  N N 263 
LEU   OXT  O  N N 264 
LEU   H    H  N N 265 
LEU   H2   H  N N 266 
LEU   HA   H  N N 267 
LEU   HB2  H  N N 268 
LEU   HB3  H  N N 269 
LEU   HG   H  N N 270 
LEU   HD11 H  N N 271 
LEU   HD12 H  N N 272 
LEU   HD13 H  N N 273 
LEU   HD21 H  N N 274 
LEU   HD22 H  N N 275 
LEU   HD23 H  N N 276 
LEU   HXT  H  N N 277 
LYS   N    N  N N 278 
LYS   CA   C  N S 279 
LYS   C    C  N N 280 
LYS   O    O  N N 281 
LYS   CB   C  N N 282 
LYS   CG   C  N N 283 
LYS   CD   C  N N 284 
LYS   CE   C  N N 285 
LYS   NZ   N  N N 286 
LYS   OXT  O  N N 287 
LYS   H    H  N N 288 
LYS   H2   H  N N 289 
LYS   HA   H  N N 290 
LYS   HB2  H  N N 291 
LYS   HB3  H  N N 292 
LYS   HG2  H  N N 293 
LYS   HG3  H  N N 294 
LYS   HD2  H  N N 295 
LYS   HD3  H  N N 296 
LYS   HE2  H  N N 297 
LYS   HE3  H  N N 298 
LYS   HZ1  H  N N 299 
LYS   HZ2  H  N N 300 
LYS   HZ3  H  N N 301 
LYS   HXT  H  N N 302 
MET   N    N  N N 303 
MET   CA   C  N S 304 
MET   C    C  N N 305 
MET   O    O  N N 306 
MET   CB   C  N N 307 
MET   CG   C  N N 308 
MET   SD   S  N N 309 
MET   CE   C  N N 310 
MET   OXT  O  N N 311 
MET   H    H  N N 312 
MET   H2   H  N N 313 
MET   HA   H  N N 314 
MET   HB2  H  N N 315 
MET   HB3  H  N N 316 
MET   HG2  H  N N 317 
MET   HG3  H  N N 318 
MET   HE1  H  N N 319 
MET   HE2  H  N N 320 
MET   HE3  H  N N 321 
MET   HXT  H  N N 322 
PHE   N    N  N N 323 
PHE   CA   C  N S 324 
PHE   C    C  N N 325 
PHE   O    O  N N 326 
PHE   CB   C  N N 327 
PHE   CG   C  Y N 328 
PHE   CD1  C  Y N 329 
PHE   CD2  C  Y N 330 
PHE   CE1  C  Y N 331 
PHE   CE2  C  Y N 332 
PHE   CZ   C  Y N 333 
PHE   OXT  O  N N 334 
PHE   H    H  N N 335 
PHE   H2   H  N N 336 
PHE   HA   H  N N 337 
PHE   HB2  H  N N 338 
PHE   HB3  H  N N 339 
PHE   HD1  H  N N 340 
PHE   HD2  H  N N 341 
PHE   HE1  H  N N 342 
PHE   HE2  H  N N 343 
PHE   HZ   H  N N 344 
PHE   HXT  H  N N 345 
PRO   N    N  N N 346 
PRO   CA   C  N S 347 
PRO   C    C  N N 348 
PRO   O    O  N N 349 
PRO   CB   C  N N 350 
PRO   CG   C  N N 351 
PRO   CD   C  N N 352 
PRO   OXT  O  N N 353 
PRO   H    H  N N 354 
PRO   HA   H  N N 355 
PRO   HB2  H  N N 356 
PRO   HB3  H  N N 357 
PRO   HG2  H  N N 358 
PRO   HG3  H  N N 359 
PRO   HD2  H  N N 360 
PRO   HD3  H  N N 361 
PRO   HXT  H  N N 362 
SER   N    N  N N 363 
SER   CA   C  N S 364 
SER   C    C  N N 365 
SER   O    O  N N 366 
SER   CB   C  N N 367 
SER   OG   O  N N 368 
SER   OXT  O  N N 369 
SER   H    H  N N 370 
SER   H2   H  N N 371 
SER   HA   H  N N 372 
SER   HB2  H  N N 373 
SER   HB3  H  N N 374 
SER   HG   H  N N 375 
SER   HXT  H  N N 376 
TFA   C1   C  N N 377 
TFA   C2   C  N N 378 
TFA   O    O  N N 379 
TFA   F1   F  N N 380 
TFA   F2   F  N N 381 
TFA   F3   F  N N 382 
TFA   OXT  O  N N 383 
TFA   HXT  H  N N 384 
THR   N    N  N N 385 
THR   CA   C  N S 386 
THR   C    C  N N 387 
THR   O    O  N N 388 
THR   CB   C  N R 389 
THR   OG1  O  N N 390 
THR   CG2  C  N N 391 
THR   OXT  O  N N 392 
THR   H    H  N N 393 
THR   H2   H  N N 394 
THR   HA   H  N N 395 
THR   HB   H  N N 396 
THR   HG1  H  N N 397 
THR   HG21 H  N N 398 
THR   HG22 H  N N 399 
THR   HG23 H  N N 400 
THR   HXT  H  N N 401 
TYR   N    N  N N 402 
TYR   CA   C  N S 403 
TYR   C    C  N N 404 
TYR   O    O  N N 405 
TYR   CB   C  N N 406 
TYR   CG   C  Y N 407 
TYR   CD1  C  Y N 408 
TYR   CD2  C  Y N 409 
TYR   CE1  C  Y N 410 
TYR   CE2  C  Y N 411 
TYR   CZ   C  Y N 412 
TYR   OH   O  N N 413 
TYR   OXT  O  N N 414 
TYR   H    H  N N 415 
TYR   H2   H  N N 416 
TYR   HA   H  N N 417 
TYR   HB2  H  N N 418 
TYR   HB3  H  N N 419 
TYR   HD1  H  N N 420 
TYR   HD2  H  N N 421 
TYR   HE1  H  N N 422 
TYR   HE2  H  N N 423 
TYR   HH   H  N N 424 
TYR   HXT  H  N N 425 
VAL   N    N  N N 426 
VAL   CA   C  N S 427 
VAL   C    C  N N 428 
VAL   O    O  N N 429 
VAL   CB   C  N N 430 
VAL   CG1  C  N N 431 
VAL   CG2  C  N N 432 
VAL   OXT  O  N N 433 
VAL   H    H  N N 434 
VAL   H2   H  N N 435 
VAL   HA   H  N N 436 
VAL   HB   H  N N 437 
VAL   HG11 H  N N 438 
VAL   HG12 H  N N 439 
VAL   HG13 H  N N 440 
VAL   HG21 H  N N 441 
VAL   HG22 H  N N 442 
VAL   HG23 H  N N 443 
VAL   HXT  H  N N 444 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1A93 I1  C7   sing N N 1   
A1A93 C8  C7   doub Y N 2   
A1A93 C8  C9   sing Y N 3   
A1A93 C7  C6   sing Y N 4   
A1A93 C9  C4   doub Y N 5   
A1A93 C6  C5   doub Y N 6   
A1A93 C4  C5   sing Y N 7   
A1A93 C4  C3   sing N N 8   
A1A93 O1  C1   sing N N 9   
A1A93 C2  C3   sing N N 10  
A1A93 C2  C1   sing N N 11  
A1A93 C2  N1   sing N N 12  
A1A93 N1  C10  sing N N 13  
A1A93 C10 N2   doub Y N 14  
A1A93 C10 C13  sing Y N 15  
A1A93 C14 C13  sing Y N 16  
A1A93 C14 C15  doub Y N 17  
A1A93 N2  C11  sing Y N 18  
A1A93 C13 C12  doub Y N 19  
A1A93 C15 N4   sing Y N 20  
A1A93 C11 N3   doub Y N 21  
A1A93 C12 N4   sing Y N 22  
A1A93 C12 N3   sing Y N 23  
A1A93 O1  H2   sing N N 24  
A1A93 C1  H3   sing N N 25  
A1A93 C1  H4   sing N N 26  
A1A93 C2  H1   sing N N 27  
A1A93 C3  H6   sing N N 28  
A1A93 C3  H5   sing N N 29  
A1A93 C5  H7   sing N N 30  
A1A93 C6  H8   sing N N 31  
A1A93 C8  H9   sing N N 32  
A1A93 C11 H12  sing N N 33  
A1A93 C14 H13  sing N N 34  
A1A93 C15 H14  sing N N 35  
A1A93 C9  H10  sing N N 36  
A1A93 N1  H11  sing N N 37  
A1A93 N4  H15  sing N N 38  
A1A94 I1  C7   sing N N 39  
A1A94 C6  C5   doub Y N 40  
A1A94 C6  C7   sing Y N 41  
A1A94 C5  C4   sing Y N 42  
A1A94 C7  C8   doub Y N 43  
A1A94 C4  C3   sing N N 44  
A1A94 C4  C9   doub Y N 45  
A1A94 C8  C9   sing Y N 46  
A1A94 C3  C2   sing N N 47  
A1A94 O1  C1   sing N N 48  
A1A94 C1  C2   sing N N 49  
A1A94 C2  N1   sing N N 50  
A1A94 N1  C10  sing N N 51  
A1A94 C10 C13  doub Y N 52  
A1A94 C10 N2   sing Y N 53  
A1A94 C14 C13  sing Y N 54  
A1A94 C14 C15  doub Y N 55  
A1A94 C13 C12  sing Y N 56  
A1A94 N2  C11  doub Y N 57  
A1A94 C15 N4   sing Y N 58  
A1A94 C11 N3   sing Y N 59  
A1A94 C12 N4   sing Y N 60  
A1A94 C12 N3   doub Y N 61  
A1A94 C3  H5   sing N N 62  
A1A94 C3  H6   sing N N 63  
A1A94 C6  H8   sing N N 64  
A1A94 C9  H10  sing N N 65  
A1A94 C14 H13  sing N N 66  
A1A94 C1  H4   sing N N 67  
A1A94 C1  H3   sing N N 68  
A1A94 C11 H12  sing N N 69  
A1A94 C15 H14  sing N N 70  
A1A94 C2  H1   sing N N 71  
A1A94 C5  H7   sing N N 72  
A1A94 C8  H9   sing N N 73  
A1A94 N1  H11  sing N N 74  
A1A94 N4  H15  sing N N 75  
A1A94 O1  H2   sing N N 76  
ALA   N   CA   sing N N 77  
ALA   N   H    sing N N 78  
ALA   N   H2   sing N N 79  
ALA   CA  C    sing N N 80  
ALA   CA  CB   sing N N 81  
ALA   CA  HA   sing N N 82  
ALA   C   O    doub N N 83  
ALA   C   OXT  sing N N 84  
ALA   CB  HB1  sing N N 85  
ALA   CB  HB2  sing N N 86  
ALA   CB  HB3  sing N N 87  
ALA   OXT HXT  sing N N 88  
ARG   N   CA   sing N N 89  
ARG   N   H    sing N N 90  
ARG   N   H2   sing N N 91  
ARG   CA  C    sing N N 92  
ARG   CA  CB   sing N N 93  
ARG   CA  HA   sing N N 94  
ARG   C   O    doub N N 95  
ARG   C   OXT  sing N N 96  
ARG   CB  CG   sing N N 97  
ARG   CB  HB2  sing N N 98  
ARG   CB  HB3  sing N N 99  
ARG   CG  CD   sing N N 100 
ARG   CG  HG2  sing N N 101 
ARG   CG  HG3  sing N N 102 
ARG   CD  NE   sing N N 103 
ARG   CD  HD2  sing N N 104 
ARG   CD  HD3  sing N N 105 
ARG   NE  CZ   sing N N 106 
ARG   NE  HE   sing N N 107 
ARG   CZ  NH1  sing N N 108 
ARG   CZ  NH2  doub N N 109 
ARG   NH1 HH11 sing N N 110 
ARG   NH1 HH12 sing N N 111 
ARG   NH2 HH21 sing N N 112 
ARG   NH2 HH22 sing N N 113 
ARG   OXT HXT  sing N N 114 
ASN   N   CA   sing N N 115 
ASN   N   H    sing N N 116 
ASN   N   H2   sing N N 117 
ASN   CA  C    sing N N 118 
ASN   CA  CB   sing N N 119 
ASN   CA  HA   sing N N 120 
ASN   C   O    doub N N 121 
ASN   C   OXT  sing N N 122 
ASN   CB  CG   sing N N 123 
ASN   CB  HB2  sing N N 124 
ASN   CB  HB3  sing N N 125 
ASN   CG  OD1  doub N N 126 
ASN   CG  ND2  sing N N 127 
ASN   ND2 HD21 sing N N 128 
ASN   ND2 HD22 sing N N 129 
ASN   OXT HXT  sing N N 130 
ASP   N   CA   sing N N 131 
ASP   N   H    sing N N 132 
ASP   N   H2   sing N N 133 
ASP   CA  C    sing N N 134 
ASP   CA  CB   sing N N 135 
ASP   CA  HA   sing N N 136 
ASP   C   O    doub N N 137 
ASP   C   OXT  sing N N 138 
ASP   CB  CG   sing N N 139 
ASP   CB  HB2  sing N N 140 
ASP   CB  HB3  sing N N 141 
ASP   CG  OD1  doub N N 142 
ASP   CG  OD2  sing N N 143 
ASP   OD2 HD2  sing N N 144 
ASP   OXT HXT  sing N N 145 
CYS   N   CA   sing N N 146 
CYS   N   H    sing N N 147 
CYS   N   H2   sing N N 148 
CYS   CA  C    sing N N 149 
CYS   CA  CB   sing N N 150 
CYS   CA  HA   sing N N 151 
CYS   C   O    doub N N 152 
CYS   C   OXT  sing N N 153 
CYS   CB  SG   sing N N 154 
CYS   CB  HB2  sing N N 155 
CYS   CB  HB3  sing N N 156 
CYS   SG  HG   sing N N 157 
CYS   OXT HXT  sing N N 158 
GLN   N   CA   sing N N 159 
GLN   N   H    sing N N 160 
GLN   N   H2   sing N N 161 
GLN   CA  C    sing N N 162 
GLN   CA  CB   sing N N 163 
GLN   CA  HA   sing N N 164 
GLN   C   O    doub N N 165 
GLN   C   OXT  sing N N 166 
GLN   CB  CG   sing N N 167 
GLN   CB  HB2  sing N N 168 
GLN   CB  HB3  sing N N 169 
GLN   CG  CD   sing N N 170 
GLN   CG  HG2  sing N N 171 
GLN   CG  HG3  sing N N 172 
GLN   CD  OE1  doub N N 173 
GLN   CD  NE2  sing N N 174 
GLN   NE2 HE21 sing N N 175 
GLN   NE2 HE22 sing N N 176 
GLN   OXT HXT  sing N N 177 
GLU   N   CA   sing N N 178 
GLU   N   H    sing N N 179 
GLU   N   H2   sing N N 180 
GLU   CA  C    sing N N 181 
GLU   CA  CB   sing N N 182 
GLU   CA  HA   sing N N 183 
GLU   C   O    doub N N 184 
GLU   C   OXT  sing N N 185 
GLU   CB  CG   sing N N 186 
GLU   CB  HB2  sing N N 187 
GLU   CB  HB3  sing N N 188 
GLU   CG  CD   sing N N 189 
GLU   CG  HG2  sing N N 190 
GLU   CG  HG3  sing N N 191 
GLU   CD  OE1  doub N N 192 
GLU   CD  OE2  sing N N 193 
GLU   OE2 HE2  sing N N 194 
GLU   OXT HXT  sing N N 195 
GLY   N   CA   sing N N 196 
GLY   N   H    sing N N 197 
GLY   N   H2   sing N N 198 
GLY   CA  C    sing N N 199 
GLY   CA  HA2  sing N N 200 
GLY   CA  HA3  sing N N 201 
GLY   C   O    doub N N 202 
GLY   C   OXT  sing N N 203 
GLY   OXT HXT  sing N N 204 
HIS   N   CA   sing N N 205 
HIS   N   H    sing N N 206 
HIS   N   H2   sing N N 207 
HIS   CA  C    sing N N 208 
HIS   CA  CB   sing N N 209 
HIS   CA  HA   sing N N 210 
HIS   C   O    doub N N 211 
HIS   C   OXT  sing N N 212 
HIS   CB  CG   sing N N 213 
HIS   CB  HB2  sing N N 214 
HIS   CB  HB3  sing N N 215 
HIS   CG  ND1  sing Y N 216 
HIS   CG  CD2  doub Y N 217 
HIS   ND1 CE1  doub Y N 218 
HIS   ND1 HD1  sing N N 219 
HIS   CD2 NE2  sing Y N 220 
HIS   CD2 HD2  sing N N 221 
HIS   CE1 NE2  sing Y N 222 
HIS   CE1 HE1  sing N N 223 
HIS   NE2 HE2  sing N N 224 
HIS   OXT HXT  sing N N 225 
HOH   O   H1   sing N N 226 
HOH   O   H2   sing N N 227 
ILE   N   CA   sing N N 228 
ILE   N   H    sing N N 229 
ILE   N   H2   sing N N 230 
ILE   CA  C    sing N N 231 
ILE   CA  CB   sing N N 232 
ILE   CA  HA   sing N N 233 
ILE   C   O    doub N N 234 
ILE   C   OXT  sing N N 235 
ILE   CB  CG1  sing N N 236 
ILE   CB  CG2  sing N N 237 
ILE   CB  HB   sing N N 238 
ILE   CG1 CD1  sing N N 239 
ILE   CG1 HG12 sing N N 240 
ILE   CG1 HG13 sing N N 241 
ILE   CG2 HG21 sing N N 242 
ILE   CG2 HG22 sing N N 243 
ILE   CG2 HG23 sing N N 244 
ILE   CD1 HD11 sing N N 245 
ILE   CD1 HD12 sing N N 246 
ILE   CD1 HD13 sing N N 247 
ILE   OXT HXT  sing N N 248 
LEU   N   CA   sing N N 249 
LEU   N   H    sing N N 250 
LEU   N   H2   sing N N 251 
LEU   CA  C    sing N N 252 
LEU   CA  CB   sing N N 253 
LEU   CA  HA   sing N N 254 
LEU   C   O    doub N N 255 
LEU   C   OXT  sing N N 256 
LEU   CB  CG   sing N N 257 
LEU   CB  HB2  sing N N 258 
LEU   CB  HB3  sing N N 259 
LEU   CG  CD1  sing N N 260 
LEU   CG  CD2  sing N N 261 
LEU   CG  HG   sing N N 262 
LEU   CD1 HD11 sing N N 263 
LEU   CD1 HD12 sing N N 264 
LEU   CD1 HD13 sing N N 265 
LEU   CD2 HD21 sing N N 266 
LEU   CD2 HD22 sing N N 267 
LEU   CD2 HD23 sing N N 268 
LEU   OXT HXT  sing N N 269 
LYS   N   CA   sing N N 270 
LYS   N   H    sing N N 271 
LYS   N   H2   sing N N 272 
LYS   CA  C    sing N N 273 
LYS   CA  CB   sing N N 274 
LYS   CA  HA   sing N N 275 
LYS   C   O    doub N N 276 
LYS   C   OXT  sing N N 277 
LYS   CB  CG   sing N N 278 
LYS   CB  HB2  sing N N 279 
LYS   CB  HB3  sing N N 280 
LYS   CG  CD   sing N N 281 
LYS   CG  HG2  sing N N 282 
LYS   CG  HG3  sing N N 283 
LYS   CD  CE   sing N N 284 
LYS   CD  HD2  sing N N 285 
LYS   CD  HD3  sing N N 286 
LYS   CE  NZ   sing N N 287 
LYS   CE  HE2  sing N N 288 
LYS   CE  HE3  sing N N 289 
LYS   NZ  HZ1  sing N N 290 
LYS   NZ  HZ2  sing N N 291 
LYS   NZ  HZ3  sing N N 292 
LYS   OXT HXT  sing N N 293 
MET   N   CA   sing N N 294 
MET   N   H    sing N N 295 
MET   N   H2   sing N N 296 
MET   CA  C    sing N N 297 
MET   CA  CB   sing N N 298 
MET   CA  HA   sing N N 299 
MET   C   O    doub N N 300 
MET   C   OXT  sing N N 301 
MET   CB  CG   sing N N 302 
MET   CB  HB2  sing N N 303 
MET   CB  HB3  sing N N 304 
MET   CG  SD   sing N N 305 
MET   CG  HG2  sing N N 306 
MET   CG  HG3  sing N N 307 
MET   SD  CE   sing N N 308 
MET   CE  HE1  sing N N 309 
MET   CE  HE2  sing N N 310 
MET   CE  HE3  sing N N 311 
MET   OXT HXT  sing N N 312 
PHE   N   CA   sing N N 313 
PHE   N   H    sing N N 314 
PHE   N   H2   sing N N 315 
PHE   CA  C    sing N N 316 
PHE   CA  CB   sing N N 317 
PHE   CA  HA   sing N N 318 
PHE   C   O    doub N N 319 
PHE   C   OXT  sing N N 320 
PHE   CB  CG   sing N N 321 
PHE   CB  HB2  sing N N 322 
PHE   CB  HB3  sing N N 323 
PHE   CG  CD1  doub Y N 324 
PHE   CG  CD2  sing Y N 325 
PHE   CD1 CE1  sing Y N 326 
PHE   CD1 HD1  sing N N 327 
PHE   CD2 CE2  doub Y N 328 
PHE   CD2 HD2  sing N N 329 
PHE   CE1 CZ   doub Y N 330 
PHE   CE1 HE1  sing N N 331 
PHE   CE2 CZ   sing Y N 332 
PHE   CE2 HE2  sing N N 333 
PHE   CZ  HZ   sing N N 334 
PHE   OXT HXT  sing N N 335 
PRO   N   CA   sing N N 336 
PRO   N   CD   sing N N 337 
PRO   N   H    sing N N 338 
PRO   CA  C    sing N N 339 
PRO   CA  CB   sing N N 340 
PRO   CA  HA   sing N N 341 
PRO   C   O    doub N N 342 
PRO   C   OXT  sing N N 343 
PRO   CB  CG   sing N N 344 
PRO   CB  HB2  sing N N 345 
PRO   CB  HB3  sing N N 346 
PRO   CG  CD   sing N N 347 
PRO   CG  HG2  sing N N 348 
PRO   CG  HG3  sing N N 349 
PRO   CD  HD2  sing N N 350 
PRO   CD  HD3  sing N N 351 
PRO   OXT HXT  sing N N 352 
SER   N   CA   sing N N 353 
SER   N   H    sing N N 354 
SER   N   H2   sing N N 355 
SER   CA  C    sing N N 356 
SER   CA  CB   sing N N 357 
SER   CA  HA   sing N N 358 
SER   C   O    doub N N 359 
SER   C   OXT  sing N N 360 
SER   CB  OG   sing N N 361 
SER   CB  HB2  sing N N 362 
SER   CB  HB3  sing N N 363 
SER   OG  HG   sing N N 364 
SER   OXT HXT  sing N N 365 
TFA   C1  C2   sing N N 366 
TFA   C1  O    doub N N 367 
TFA   C1  OXT  sing N N 368 
TFA   C2  F1   sing N N 369 
TFA   C2  F2   sing N N 370 
TFA   C2  F3   sing N N 371 
TFA   OXT HXT  sing N N 372 
THR   N   CA   sing N N 373 
THR   N   H    sing N N 374 
THR   N   H2   sing N N 375 
THR   CA  C    sing N N 376 
THR   CA  CB   sing N N 377 
THR   CA  HA   sing N N 378 
THR   C   O    doub N N 379 
THR   C   OXT  sing N N 380 
THR   CB  OG1  sing N N 381 
THR   CB  CG2  sing N N 382 
THR   CB  HB   sing N N 383 
THR   OG1 HG1  sing N N 384 
THR   CG2 HG21 sing N N 385 
THR   CG2 HG22 sing N N 386 
THR   CG2 HG23 sing N N 387 
THR   OXT HXT  sing N N 388 
TYR   N   CA   sing N N 389 
TYR   N   H    sing N N 390 
TYR   N   H2   sing N N 391 
TYR   CA  C    sing N N 392 
TYR   CA  CB   sing N N 393 
TYR   CA  HA   sing N N 394 
TYR   C   O    doub N N 395 
TYR   C   OXT  sing N N 396 
TYR   CB  CG   sing N N 397 
TYR   CB  HB2  sing N N 398 
TYR   CB  HB3  sing N N 399 
TYR   CG  CD1  doub Y N 400 
TYR   CG  CD2  sing Y N 401 
TYR   CD1 CE1  sing Y N 402 
TYR   CD1 HD1  sing N N 403 
TYR   CD2 CE2  doub Y N 404 
TYR   CD2 HD2  sing N N 405 
TYR   CE1 CZ   doub Y N 406 
TYR   CE1 HE1  sing N N 407 
TYR   CE2 CZ   sing Y N 408 
TYR   CE2 HE2  sing N N 409 
TYR   CZ  OH   sing N N 410 
TYR   OH  HH   sing N N 411 
TYR   OXT HXT  sing N N 412 
VAL   N   CA   sing N N 413 
VAL   N   H    sing N N 414 
VAL   N   H2   sing N N 415 
VAL   CA  C    sing N N 416 
VAL   CA  CB   sing N N 417 
VAL   CA  HA   sing N N 418 
VAL   C   O    doub N N 419 
VAL   C   OXT  sing N N 420 
VAL   CB  CG1  sing N N 421 
VAL   CB  CG2  sing N N 422 
VAL   CB  HB   sing N N 423 
VAL   CG1 HG11 sing N N 424 
VAL   CG1 HG12 sing N N 425 
VAL   CG1 HG13 sing N N 426 
VAL   CG2 HG21 sing N N 427 
VAL   CG2 HG22 sing N N 428 
VAL   CG2 HG23 sing N N 429 
VAL   OXT HXT  sing N N 430 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171110 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         
'PanDDA analysis group deposition of SARS-CoV-2 NSP3 macrodomain ligand screen - FrankenROCS hits and analogues of AVI-313' 
_pdbx_deposit_group.group_description   
'SARS-CoV-2 NSP3 macrodomain in complex with ligands identified by X-ray diffraction using ALS 8.3.1,  SSRL 9-2, and SSRL 12-2' 
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002304 
# 
_atom_sites.entry_id                    7HEO 
_atom_sites.fract_transf_matrix[1][1]   0.011254 
_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]   0.011254 
_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]   0.025306 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
H  
I  
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   ? 19.684 -16.173 22.226  0.60 54.10 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.587 -16.159 22.326  0.40 53.69 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.709 -15.103 22.399  0.60 53.69 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.655 -15.052 22.500  0.40 53.33 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.355 -13.752 22.109  0.60 52.20 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.331 -13.731 22.152  0.40 51.98 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.472 -13.482 22.549  0.60 52.77 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.450 -13.463 22.590  0.40 52.50 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.083 -15.140 23.808  0.60 54.38 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.082 -15.022 23.931  0.40 53.95 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.044 -14.037 23.961  0.60 54.61 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.111 -13.860 24.094  0.40 54.18 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.461 -16.504 24.076  0.60 54.58 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.399 -16.342 24.260  0.40 54.14 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.993 -15.226 21.761  0.60 64.47 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.911 -15.169 21.892  0.40 64.03 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.776 -14.993 24.470  0.60 65.29 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.807 -14.896 24.562  0.40 64.78 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.551 -14.182 24.784  0.60 65.58 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.627 -13.969 24.927  0.40 65.06 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.494 -13.179 23.993  0.60 65.58 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.610 -13.028 24.109  0.40 65.06 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.439 -14.068 23.204  0.60 65.58 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.490 -13.862 23.349  0.40 65.06 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 17.005 -16.481 24.932  0.60 65.54 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 16.987 -16.275 25.135  0.40 65.01 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.828 -16.705 23.369  0.60 65.54 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.723 -16.523 23.589  0.40 65.01 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.162 -17.174 24.093  0.60 65.54 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.062 -17.050 24.260  0.40 65.01 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.648 -12.911 21.356  1.00 49.70 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.109 -11.569 21.019  1.00 44.65 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 17.984 -10.574 21.293  1.00 40.10 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.873 -10.952 21.679  1.00 40.17 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.644 -11.486 19.581  1.00 43.77 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.611 -11.868 18.546  1.00 42.81 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.505 -11.330 18.527  1.00 42.50 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 18.969 -12.807 17.674  1.00 42.42 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.878 -13.103 21.022  0.60 59.69 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.894 -13.116 20.994  0.40 59.69 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.842 -11.342 21.604  1.00 53.62 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 19.927 -10.574 19.402  1.00 52.57 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.398 -12.089 19.490  1.00 52.57 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.420 -13.059 17.062  1.00 50.95 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.752 -13.162 17.721  1.00 50.95 ?  4   ASN   A HD22 1 
ATOM   46   N  N    A SER   A 1 5   ? 18.257 -9.291  21.057  0.60 37.57 ?  5   SER   A N    1 
ATOM   47   N  N    B SER   A 1 5   ? 18.297 -9.291  21.121  0.40 37.80 ?  5   SER   A N    1 
ATOM   48   C  CA   A SER   A 1 5   ? 17.339 -8.223  21.433  0.60 34.86 ?  5   SER   A CA   1 
ATOM   49   C  CA   B SER   A 1 5   ? 17.391 -8.207  21.475  0.40 35.33 ?  5   SER   A CA   1 
ATOM   50   C  C    A SER   A 1 5   ? 16.482 -7.714  20.277  0.60 31.46 ?  5   SER   A C    1 
ATOM   51   C  C    B SER   A 1 5   ? 16.525 -7.746  20.310  0.40 32.18 ?  5   SER   A C    1 
ATOM   52   O  O    A SER   A 1 5   ? 15.877 -6.645  20.402  0.60 31.82 ?  5   SER   A O    1 
ATOM   53   O  O    B SER   A 1 5   ? 15.752 -6.796  20.472  0.40 32.35 ?  5   SER   A O    1 
ATOM   54   C  CB   A SER   A 1 5   ? 18.104 -7.056  22.062  0.60 35.58 ?  5   SER   A CB   1 
ATOM   55   C  CB   B SER   A 1 5   ? 18.179 -7.022  22.048  0.40 35.97 ?  5   SER   A CB   1 
ATOM   56   O  OG   A SER   A 1 5   ? 19.075 -6.540  21.170  0.60 35.90 ?  5   SER   A OG   1 
ATOM   57   O  OG   B SER   A 1 5   ? 19.043 -6.461  21.075  0.40 36.25 ?  5   SER   A OG   1 
ATOM   58   H  H    A SER   A 1 5   ? 18.974 -9.015  20.672  0.60 45.12 ?  5   SER   A H    1 
ATOM   59   H  H    B SER   A 1 5   ? 19.046 -9.022  20.794  0.40 45.40 ?  5   SER   A H    1 
ATOM   60   H  HA   A SER   A 1 5   ? 16.741 -8.566  22.113  0.60 41.87 ?  5   SER   A HA   1 
ATOM   61   H  HA   B SER   A 1 5   ? 16.794 -8.518  22.169  0.40 42.44 ?  5   SER   A HA   1 
ATOM   62   H  HB2  A SER   A 1 5   ? 17.475 -6.350  22.284  0.60 42.74 ?  5   SER   A HB2  1 
ATOM   63   H  HB2  B SER   A 1 5   ? 17.554 -6.341  22.346  0.40 43.21 ?  5   SER   A HB2  1 
ATOM   64   H  HB3  A SER   A 1 5   ? 18.546 -7.367  22.867  0.60 42.74 ?  5   SER   A HB3  1 
ATOM   65   H  HB3  B SER   A 1 5   ? 18.711 -7.331  22.801  0.40 43.21 ?  5   SER   A HB3  1 
ATOM   66   H  HG   A SER   A 1 5   ? 19.487 -5.902  21.532  0.60 43.12 ?  5   SER   A HG   1 
ATOM   67   H  HG   B SER   A 1 5   ? 19.466 -5.813  21.406  0.40 43.54 ?  5   SER   A HG   1 
ATOM   68   N  N    A PHE   A 1 6   ? 16.409 -8.439  19.162  0.60 27.28 ?  6   PHE   A N    1 
ATOM   69   N  N    B PHE   A 1 6   ? 16.630 -8.385  19.148  0.40 28.61 ?  6   PHE   A N    1 
ATOM   70   C  CA   A PHE   A 1 6   ? 15.508 -8.053  18.082  0.60 23.26 ?  6   PHE   A CA   1 
ATOM   71   C  CA   B PHE   A 1 6   ? 15.721 -8.082  18.050  0.40 25.17 ?  6   PHE   A CA   1 
ATOM   72   C  C    A PHE   A 1 6   ? 14.071 -8.403  18.454  0.60 22.78 ?  6   PHE   A C    1 
ATOM   73   C  C    B PHE   A 1 6   ? 14.303 -8.465  18.447  0.40 24.10 ?  6   PHE   A C    1 
ATOM   74   O  O    A PHE   A 1 6   ? 13.815 -9.441  19.067  0.60 23.61 ?  6   PHE   A O    1 
ATOM   75   O  O    B PHE   A 1 6   ? 14.004 -9.646  18.648  0.40 23.83 ?  6   PHE   A O    1 
ATOM   76   C  CB   A PHE   A 1 6   ? 15.901 -8.754  16.783  0.60 20.61 ?  6   PHE   A CB   1 
ATOM   77   C  CB   B PHE   A 1 6   ? 16.141 -8.851  16.801  0.40 23.14 ?  6   PHE   A CB   1 
ATOM   78   C  CG   A PHE   A 1 6   ? 17.186 -8.245  16.184  0.60 18.84 ?  6   PHE   A CG   1 
ATOM   79   C  CG   B PHE   A 1 6   ? 17.400 -8.333  16.164  0.40 21.52 ?  6   PHE   A CG   1 
ATOM   80   C  CD1  A PHE   A 1 6   ? 17.212 -7.052  15.480  0.60 18.06 ?  6   PHE   A CD1  1 
ATOM   81   C  CD1  B PHE   A 1 6   ? 17.387 -7.156  15.435  0.40 20.82 ?  6   PHE   A CD1  1 
ATOM   82   C  CD2  A PHE   A 1 6   ? 18.361 -8.963  16.321  0.60 18.97 ?  6   PHE   A CD2  1 
ATOM   83   C  CD2  B PHE   A 1 6   ? 18.592 -9.027  16.286  0.40 21.08 ?  6   PHE   A CD2  1 
ATOM   84   C  CE1  A PHE   A 1 6   ? 18.393 -6.581  14.928  0.60 17.93 ?  6   PHE   A CE1  1 
ATOM   85   C  CE1  B PHE   A 1 6   ? 18.542 -6.676  14.844  0.40 20.49 ?  6   PHE   A CE1  1 
ATOM   86   C  CE2  A PHE   A 1 6   ? 19.539 -8.502  15.769  0.60 18.90 ?  6   PHE   A CE2  1 
ATOM   87   C  CE2  B PHE   A 1 6   ? 19.749 -8.554  15.696  0.40 20.80 ?  6   PHE   A CE2  1 
ATOM   88   C  CZ   A PHE   A 1 6   ? 19.555 -7.309  15.070  0.60 18.20 ?  6   PHE   A CZ   1 
ATOM   89   C  CZ   B PHE   A 1 6   ? 19.724 -7.376  14.974  0.40 20.42 ?  6   PHE   A CZ   1 
ATOM   90   H  H    A PHE   A 1 6   ? 16.866 -9.155  19.008  0.60 32.78 ?  6   PHE   A H    1 
ATOM   91   H  H    B PHE   A 1 6   ? 17.213 -8.994  18.973  0.40 34.37 ?  6   PHE   A H    1 
ATOM   92   H  HA   A PHE   A 1 6   ? 15.556 -7.101  17.950  0.60 27.95 ?  6   PHE   A HA   1 
ATOM   93   H  HA   B PHE   A 1 6   ? 15.746 -7.132  17.859  0.40 30.24 ?  6   PHE   A HA   1 
ATOM   94   H  HB2  A PHE   A 1 6   ? 16.008 -9.705  16.960  0.60 24.78 ?  6   PHE   A HB2  1 
ATOM   95   H  HB2  B PHE   A 1 6   ? 16.287 -9.780  17.041  0.40 27.81 ?  6   PHE   A HB2  1 
ATOM   96   H  HB3  A PHE   A 1 6   ? 15.193 -8.624  16.132  0.60 24.78 ?  6   PHE   A HB3  1 
ATOM   97   H  HB3  B PHE   A 1 6   ? 15.429 -8.790  16.146  0.40 27.81 ?  6   PHE   A HB3  1 
ATOM   98   H  HD1  A PHE   A 1 6   ? 16.426 -6.560  15.382  0.60 21.71 ?  6   PHE   A HD1  1 
ATOM   99   H  HD1  B PHE   A 1 6   ? 16.592 -6.683  15.346  0.40 25.03 ?  6   PHE   A HD1  1 
ATOM   100  H  HD2  A PHE   A 1 6   ? 18.354 -9.768  16.792  0.60 22.80 ?  6   PHE   A HD2  1 
ATOM   101  H  HD2  B PHE   A 1 6   ? 18.614 -9.821  16.772  0.40 25.34 ?  6   PHE   A HD2  1 
ATOM   102  H  HE1  A PHE   A 1 6   ? 18.397 -5.779  14.457  0.60 21.56 ?  6   PHE   A HE1  1 
ATOM   103  H  HE1  B PHE   A 1 6   ? 18.521 -5.884  14.358  0.40 24.63 ?  6   PHE   A HE1  1 
ATOM   104  H  HE2  A PHE   A 1 6   ? 20.322 -8.993  15.870  0.60 22.73 ?  6   PHE   A HE2  1 
ATOM   105  H  HE2  B PHE   A 1 6   ? 20.544 -9.028  15.787  0.40 25.01 ?  6   PHE   A HE2  1 
ATOM   106  H  HZ   A PHE   A 1 6   ? 20.346 -6.995  14.701  0.60 21.89 ?  6   PHE   A HZ   1 
ATOM   107  H  HZ   B PHE   A 1 6   ? 20.502 -7.055  14.577  0.40 24.54 ?  6   PHE   A HZ   1 
ATOM   108  N  N    A SER   A 1 7   ? 13.127 -7.534  18.078  0.60 21.36 ?  7   SER   A N    1 
ATOM   109  N  N    B SER   A 1 7   ? 13.429 -7.469  18.548  0.40 23.47 ?  7   SER   A N    1 
ATOM   110  C  CA   A SER   A 1 7   ? 11.750 -7.633  18.556  0.60 20.91 ?  7   SER   A CA   1 
ATOM   111  C  CA   B SER   A 1 7   ? 12.094 -7.646  19.096  0.40 23.30 ?  7   SER   A CA   1 
ATOM   112  C  C    A SER   A 1 7   ? 10.749 -7.407  17.426  0.60 18.54 ?  7   SER   A C    1 
ATOM   113  C  C    B SER   A 1 7   ? 11.050 -7.393  18.019  0.40 21.76 ?  7   SER   A C    1 
ATOM   114  O  O    A SER   A 1 7   ? 10.943 -6.536  16.577  0.60 18.27 ?  7   SER   A O    1 
ATOM   115  O  O    B SER   A 1 7   ? 11.170 -6.448  17.232  0.40 21.79 ?  7   SER   A O    1 
ATOM   116  C  CB   A SER   A 1 7   ? 11.502 -6.605  19.671  0.60 22.80 ?  7   SER   A CB   1 
ATOM   117  C  CB   B SER   A 1 7   ? 11.867 -6.681  20.265  0.40 24.55 ?  7   SER   A CB   1 
ATOM   118  O  OG   A SER   A 1 7   ? 10.164 -6.651  20.132  0.60 24.17 ?  7   SER   A OG   1 
ATOM   119  O  OG   B SER   A 1 7   ? 10.536 -6.755  20.740  0.40 25.49 ?  7   SER   A OG   1 
ATOM   120  H  H    A SER   A 1 7   ? 13.261 -6.879  17.543  0.60 25.68 ?  7   SER   A H    1 
ATOM   121  H  H    B SER   A 1 7   ? 13.590 -6.665  18.287  0.40 28.21 ?  7   SER   A H    1 
ATOM   122  H  HA   A SER   A 1 7   ? 11.592 -8.517  18.921  0.60 25.14 ?  7   SER   A HA   1 
ATOM   123  H  HA   B SER   A 1 7   ? 11.989 -8.553  19.422  0.40 28.00 ?  7   SER   A HA   1 
ATOM   124  H  HB2  A SER   A 1 7   ? 12.108 -6.793  20.409  0.60 27.40 ?  7   SER   A HB2  1 
ATOM   125  H  HB2  B SER   A 1 7   ? 12.466 -6.918  20.989  0.40 29.50 ?  7   SER   A HB2  1 
ATOM   126  H  HB3  A SER   A 1 7   ? 11.676 -5.716  19.325  0.60 27.40 ?  7   SER   A HB3  1 
ATOM   127  H  HB3  B SER   A 1 7   ? 12.051 -5.777  19.965  0.40 29.50 ?  7   SER   A HB3  1 
ATOM   128  H  HG   A SER   A 1 7   ? 10.059 -6.096  20.756  0.60 29.05 ?  7   SER   A HG   1 
ATOM   129  H  HG   B SER   A 1 7   ? 10.424 -6.213  21.371  0.40 30.63 ?  7   SER   A HG   1 
ATOM   130  N  N    A GLY   A 1 8   ? 9.665  -8.188  17.433  0.60 17.00 ?  8   GLY   A N    1 
ATOM   131  N  N    B GLY   A 1 8   ? 10.032 -8.250  17.980  0.40 20.05 ?  8   GLY   A N    1 
ATOM   132  C  CA   A GLY   A 1 8   ? 8.572  -7.977  16.500  0.60 15.83 ?  8   GLY   A CA   1 
ATOM   133  C  CA   B GLY   A 1 8   ? 8.898  -8.027  17.111  0.40 18.47 ?  8   GLY   A CA   1 
ATOM   134  C  C    A GLY   A 1 8   ? 8.793  -8.487  15.092  0.60 14.80 ?  8   GLY   A C    1 
ATOM   135  C  C    B GLY   A 1 8   ? 9.053  -8.506  15.688  0.40 16.79 ?  8   GLY   A C    1 
ATOM   136  O  O    A GLY   A 1 8   ? 8.044  -8.105  14.187  0.60 15.19 ?  8   GLY   A O    1 
ATOM   137  O  O    B GLY   A 1 8   ? 8.221  -8.150  14.847  0.40 16.82 ?  8   GLY   A O    1 
ATOM   138  H  H    A GLY   A 1 8   ? 9.541  -8.843  17.974  0.60 20.44 ?  8   GLY   A H    1 
ATOM   139  H  H    B GLY   A 1 8   ? 9.982  -8.971  18.448  0.40 24.10 ?  8   GLY   A H    1 
ATOM   140  H  HA2  A GLY   A 1 8   ? 7.773  -8.406  16.857  0.60 19.04 ?  8   GLY   A HA2  1 
ATOM   141  H  HA2  B GLY   A 1 8   ? 8.126  -8.475  17.480  0.40 22.20 ?  8   GLY   A HA2  1 
ATOM   142  H  HA3  A GLY   A 1 8   ? 8.388  -7.026  16.441  0.60 19.04 ?  8   GLY   A HA3  1 
ATOM   143  H  HA3  B GLY   A 1 8   ? 8.711  -7.077  17.080  0.40 22.20 ?  8   GLY   A HA3  1 
ATOM   144  N  N    A TYR   A 1 9   ? 9.787  -9.345  14.872  0.60 13.34 ?  9   TYR   A N    1 
ATOM   145  N  N    B TYR   A 1 9   ? 10.078 -9.299  15.385  0.40 15.47 ?  9   TYR   A N    1 
ATOM   146  C  CA   A TYR   A 1 9   ? 10.054 -9.884  13.546  0.60 12.18 ?  9   TYR   A CA   1 
ATOM   147  C  CA   B TYR   A 1 9   ? 10.273 -9.775  14.023  0.40 14.67 ?  9   TYR   A CA   1 
ATOM   148  C  C    A TYR   A 1 9   ? 9.206  -11.121 13.285  0.60 11.83 ?  9   TYR   A C    1 
ATOM   149  C  C    B TYR   A 1 9   ? 9.386  -10.978 13.723  0.40 14.45 ?  9   TYR   A C    1 
ATOM   150  O  O    A TYR   A 1 9   ? 8.973  -11.940 14.181  0.60 13.57 ?  9   TYR   A O    1 
ATOM   151  O  O    B TYR   A 1 9   ? 9.074  -11.789 14.601  0.40 15.30 ?  9   TYR   A O    1 
ATOM   152  C  CB   A TYR   A 1 9   ? 11.530 -10.261 13.383  0.60 12.84 ?  9   TYR   A CB   1 
ATOM   153  C  CB   B TYR   A 1 9   ? 11.744 -10.133 13.777  0.40 14.42 ?  9   TYR   A CB   1 
ATOM   154  C  CG   A TYR   A 1 9   ? 12.454 -9.079  13.242  0.60 13.63 ?  9   TYR   A CG   1 
ATOM   155  C  CG   B TYR   A 1 9   ? 12.608 -8.910  13.555  0.40 14.21 ?  9   TYR   A CG   1 
ATOM   156  C  CD1  A TYR   A 1 9   ? 12.811 -8.327  14.348  0.60 14.36 ?  9   TYR   A CD1  1 
ATOM   157  C  CD1  B TYR   A 1 9   ? 12.890 -8.044  14.600  0.40 14.74 ?  9   TYR   A CD1  1 
ATOM   158  C  CD2  A TYR   A 1 9   ? 12.961 -8.713  12.003  0.60 13.89 ?  9   TYR   A CD2  1 
ATOM   159  C  CD2  B TYR   A 1 9   ? 13.116 -8.609  12.297  0.40 13.84 ?  9   TYR   A CD2  1 
ATOM   160  C  CE1  A TYR   A 1 9   ? 13.645 -7.236  14.229  0.60 15.45 ?  9   TYR   A CE1  1 
ATOM   161  C  CE1  B TYR   A 1 9   ? 13.662 -6.915  14.404  0.40 14.96 ?  9   TYR   A CE1  1 
ATOM   162  C  CE2  A TYR   A 1 9   ? 13.798 -7.626  11.870  0.60 14.42 ?  9   TYR   A CE2  1 
ATOM   163  C  CE2  B TYR   A 1 9   ? 13.891 -7.479  12.090  0.40 14.05 ?  9   TYR   A CE2  1 
ATOM   164  C  CZ   A TYR   A 1 9   ? 14.134 -6.887  12.984  0.60 15.54 ?  9   TYR   A CZ   1 
ATOM   165  C  CZ   B TYR   A 1 9   ? 14.156 -6.637  13.148  0.40 14.74 ?  9   TYR   A CZ   1 
ATOM   166  O  OH   A TYR   A 1 9   ? 14.961 -5.803  12.852  0.60 16.95 ?  9   TYR   A OH   1 
ATOM   167  O  OH   B TYR   A 1 9   ? 14.916 -5.510  12.949  0.40 15.46 ?  9   TYR   A OH   1 
ATOM   168  H  H    A TYR   A 1 9   ? 10.305 -9.645  15.479  0.60 16.05 ?  9   TYR   A H    1 
ATOM   169  H  H    B TYR   A 1 9   ? 10.680 -9.566  15.945  0.40 18.60 ?  9   TYR   A H    1 
ATOM   170  H  HA   A TYR   A 1 9   ? 9.827  -9.223  12.874  0.60 14.66 ?  9   TYR   A HA   1 
ATOM   171  H  HA   B TYR   A 1 9   ? 10.040 -9.060  13.409  0.40 17.65 ?  9   TYR   A HA   1 
ATOM   172  H  HB2  A TYR   A 1 9   ? 11.807 -10.773 14.156  0.60 15.44 ?  9   TYR   A HB2  1 
ATOM   173  H  HB2  B TYR   A 1 9   ? 12.088 -10.618 14.542  0.40 17.34 ?  9   TYR   A HB2  1 
ATOM   174  H  HB3  A TYR   A 1 9   ? 11.611 -10.801 12.581  0.60 15.44 ?  9   TYR   A HB3  1 
ATOM   175  H  HB3  B TYR   A 1 9   ? 11.797 -10.689 12.981  0.40 17.34 ?  9   TYR   A HB3  1 
ATOM   176  H  HD1  A TYR   A 1 9   ? 12.467 -8.560  15.185  0.60 17.28 ?  9   TYR   A HD1  1 
ATOM   177  H  HD1  B TYR   A 1 9   ? 12.552 -8.229  15.447  0.40 17.74 ?  9   TYR   A HD1  1 
ATOM   178  H  HD2  A TYR   A 1 9   ? 12.725 -9.209  11.247  0.60 16.71 ?  9   TYR   A HD2  1 
ATOM   179  H  HD2  B TYR   A 1 9   ? 12.936 -9.178  11.582  0.40 16.65 ?  9   TYR   A HD2  1 
ATOM   180  H  HE1  A TYR   A 1 9   ? 13.872 -6.741  14.982  0.60 18.58 ?  9   TYR   A HE1  1 
ATOM   181  H  HE1  B TYR   A 1 9   ? 13.842 -6.346  15.115  0.40 18.00 ?  9   TYR   A HE1  1 
ATOM   182  H  HE2  A TYR   A 1 9   ? 14.131 -7.392  11.035  0.60 17.35 ?  9   TYR   A HE2  1 
ATOM   183  H  HE2  B TYR   A 1 9   ? 14.230 -7.291  11.243  0.40 16.90 ?  9   TYR   A HE2  1 
ATOM   184  H  HH   A TYR   A 1 9   ? 15.099 -5.456  13.605  0.60 20.38 ?  9   TYR   A HH   1 
ATOM   185  H  HH   B TYR   A 1 9   ? 15.017 -5.097  13.672  0.40 18.60 ?  9   TYR   A HH   1 
ATOM   186  N  N    A LEU   A 1 10  ? 8.778  -11.267 12.037  0.60 11.58 ?  10  LEU   A N    1 
ATOM   187  N  N    B LEU   A 1 10  ? 8.980  -11.079 12.459  0.40 14.49 ?  10  LEU   A N    1 
ATOM   188  C  CA   A LEU   A 1 10  ? 8.203  -12.513 11.560  0.60 11.25 ?  10  LEU   A CA   1 
ATOM   189  C  CA   B LEU   A 1 10  ? 8.235  -12.220 11.945  0.40 14.95 ?  10  LEU   A CA   1 
ATOM   190  C  C    A LEU   A 1 10  ? 9.339  -13.445 11.137  0.60 11.37 ?  10  LEU   A C    1 
ATOM   191  C  C    B LEU   A 1 10  ? 9.250  -13.226 11.413  0.40 13.45 ?  10  LEU   A C    1 
ATOM   192  O  O    A LEU   A 1 10  ? 10.321 -13.001 10.535  0.60 11.72 ?  10  LEU   A O    1 
ATOM   193  O  O    B LEU   A 1 10  ? 10.063 -12.895 10.544  0.40 13.42 ?  10  LEU   A O    1 
ATOM   194  C  CB   A LEU   A 1 10  ? 7.315  -12.200 10.360  0.60 12.06 ?  10  LEU   A CB   1 
ATOM   195  C  CB   B LEU   A 1 10  ? 7.312  -11.746 10.818  0.40 17.19 ?  10  LEU   A CB   1 
ATOM   196  C  CG   A LEU   A 1 10  ? 6.575  -13.361 9.708   0.60 14.12 ?  10  LEU   A CG   1 
ATOM   197  C  CG   B LEU   A 1 10  ? 5.976  -12.429 10.503  0.40 19.98 ?  10  LEU   A CG   1 
ATOM   198  C  CD1  A LEU   A 1 10  ? 5.502  -13.926 10.626  0.60 15.46 ?  10  LEU   A CD1  1 
ATOM   199  C  CD1  B LEU   A 1 10  ? 5.977  -12.978 9.079   0.40 20.89 ?  10  LEU   A CD1  1 
ATOM   200  C  CD2  A LEU   A 1 10  ? 5.976  -12.913 8.378   0.60 15.69 ?  10  LEU   A CD2  1 
ATOM   201  C  CD2  B LEU   A 1 10  ? 5.640  -13.514 11.504  0.40 20.43 ?  10  LEU   A CD2  1 
ATOM   202  H  H    A LEU   A 1 10  ? 8.819  -10.658 11.423  0.60 13.93 ?  10  LEU   A H    1 
ATOM   203  H  H    B LEU   A 1 10  ? 9.135  -10.481 11.863  0.40 17.43 ?  10  LEU   A H    1 
ATOM   204  H  HA   A LEU   A 1 10  ? 7.679  -12.941 12.248  0.60 13.54 ?  10  LEU   A HA   1 
ATOM   205  H  HA   B LEU   A 1 10  ? 7.713  -12.623 12.658  0.40 17.98 ?  10  LEU   A HA   1 
ATOM   206  H  HB2  A LEU   A 1 10  ? 6.642  -11.569 10.640  0.60 14.52 ?  10  LEU   A HB2  1 
ATOM   207  H  HB2  B LEU   A 1 10  ? 7.091  -10.817 10.996  0.40 20.67 ?  10  LEU   A HB2  1 
ATOM   208  H  HB3  A LEU   A 1 10  ? 7.864  -11.804 9.666   0.60 14.52 ?  10  LEU   A HB3  1 
ATOM   209  H  HB3  B LEU   A 1 10  ? 7.825  -11.784 9.997   0.40 20.67 ?  10  LEU   A HB3  1 
ATOM   210  H  HG   A LEU   A 1 10  ? 7.202  -14.078 9.516   0.60 16.99 ?  10  LEU   A HG   1 
ATOM   211  H  HG   B LEU   A 1 10  ? 5.272  -11.761 10.548  0.40 24.02 ?  10  LEU   A HG   1 
ATOM   212  H  HD11 A LEU   A 1 10  ? 5.069  -14.677 10.189  0.60 18.60 ?  10  LEU   A HD11 1 
ATOM   213  H  HD11 B LEU   A 1 10  ? 5.124  -13.411 8.907   0.40 25.11 ?  10  LEU   A HD11 1 
ATOM   214  H  HD12 A LEU   A 1 10  ? 5.916  -14.217 11.452  0.60 18.60 ?  10  LEU   A HD12 1 
ATOM   215  H  HD12 B LEU   A 1 10  ? 6.104  -12.245 8.455   0.40 25.11 ?  10  LEU   A HD12 1 
ATOM   216  H  HD13 A LEU   A 1 10  ? 4.849  -13.231 10.811  0.60 18.60 ?  10  LEU   A HD13 1 
ATOM   217  H  HD13 B LEU   A 1 10  ? 6.697  -13.620 8.987   0.40 25.11 ?  10  LEU   A HD13 1 
ATOM   218  H  HD21 A LEU   A 1 10  ? 5.497  -13.658 7.979   0.60 18.87 ?  10  LEU   A HD21 1 
ATOM   219  H  HD21 B LEU   A 1 10  ? 4.806  -13.932 11.246  0.40 24.56 ?  10  LEU   A HD21 1 
ATOM   220  H  HD22 A LEU   A 1 10  ? 5.365  -12.179 8.542   0.60 18.87 ?  10  LEU   A HD22 1 
ATOM   221  H  HD22 B LEU   A 1 10  ? 6.355  -14.166 11.503  0.40 24.56 ?  10  LEU   A HD22 1 
ATOM   222  H  HD23 A LEU   A 1 10  ? 6.692  -12.628 7.792   0.60 18.87 ?  10  LEU   A HD23 1 
ATOM   223  H  HD23 B LEU   A 1 10  ? 5.553  -13.112 12.383  0.40 24.56 ?  10  LEU   A HD23 1 
ATOM   224  N  N    A LYS   A 1 11  ? 9.209  -14.737 11.458  0.60 11.43 ?  11  LYS   A N    1 
ATOM   225  N  N    B LYS   A 1 11  ? 9.224  -14.439 11.951  0.40 12.53 ?  11  LYS   A N    1 
ATOM   226  C  CA   A LYS   A 1 11  ? 10.222 -15.740 11.142  0.60 11.64 ?  11  LYS   A CA   1 
ATOM   227  C  CA   B LYS   A 1 11  ? 10.164 -15.472 11.535  0.40 11.97 ?  11  LYS   A CA   1 
ATOM   228  C  C    A LYS   A 1 11  ? 9.881  -16.353 9.791   0.60 11.48 ?  11  LYS   A C    1 
ATOM   229  C  C    B LYS   A 1 11  ? 9.770  -16.001 10.160  0.40 10.86 ?  11  LYS   A C    1 
ATOM   230  O  O    A LYS   A 1 11  ? 8.819  -16.963 9.641   0.60 13.02 ?  11  LYS   A O    1 
ATOM   231  O  O    B LYS   A 1 11  ? 8.640  -16.460 9.965   0.40 11.24 ?  11  LYS   A O    1 
ATOM   232  C  CB   A LYS   A 1 11  ? 10.263 -16.811 12.239  0.60 11.53 ?  11  LYS   A CB   1 
ATOM   233  C  CB   B LYS   A 1 11  ? 10.167 -16.598 12.564  0.40 12.40 ?  11  LYS   A CB   1 
ATOM   234  C  CG   A LYS   A 1 11  ? 11.333 -17.898 12.096  0.60 12.01 ?  11  LYS   A CG   1 
ATOM   235  C  CG   B LYS   A 1 11  ? 11.131 -17.726 12.261  0.40 12.54 ?  11  LYS   A CG   1 
ATOM   236  C  CD   A LYS   A 1 11  ? 11.449 -18.707 13.405  0.60 12.42 ?  11  LYS   A CD   1 
ATOM   237  C  CD   B LYS   A 1 11  ? 11.113 -18.747 13.386  0.40 12.91 ?  11  LYS   A CD   1 
ATOM   238  C  CE   A LYS   A 1 11  ? 12.443 -19.869 13.323  0.60 12.64 ?  11  LYS   A CE   1 
ATOM   239  C  CE   B LYS   A 1 11  ? 12.132 -19.853 13.170  0.40 12.68 ?  11  LYS   A CE   1 
ATOM   240  N  NZ   A LYS   A 1 11  ? 13.812 -19.434 12.942  0.60 12.57 ?  11  LYS   A NZ   1 
ATOM   241  N  NZ   B LYS   A 1 11  ? 13.527 -19.330 13.115  0.40 12.75 ?  11  LYS   A NZ   1 
ATOM   242  H  H    A LYS   A 1 11  ? 8.508  -15.073 11.833  0.60 13.76 ?  11  LYS   A H    1 
ATOM   243  H  H    B LYS   A 1 11  ? 8.669  -14.685 12.556  0.40 15.08 ?  11  LYS   A H    1 
ATOM   244  H  HA   A LYS   A 1 11  ? 11.089 -15.326 11.076  0.60 14.00 ?  11  LYS   A HA   1 
ATOM   245  H  HA   B LYS   A 1 11  ? 11.053 -15.093 11.476  0.40 14.41 ?  11  LYS   A HA   1 
ATOM   246  H  HB2  A LYS   A 1 11  ? 10.424 -16.367 13.085  0.60 13.88 ?  11  LYS   A HB2  1 
ATOM   247  H  HB2  B LYS   A 1 11  ? 10.411 -16.220 13.425  0.40 14.93 ?  11  LYS   A HB2  1 
ATOM   248  H  HB3  A LYS   A 1 11  ? 9.406  -17.261 12.268  0.60 13.88 ?  11  LYS   A HB3  1 
ATOM   249  H  HB3  B LYS   A 1 11  ? 9.275  -16.971 12.613  0.40 14.93 ?  11  LYS   A HB3  1 
ATOM   250  H  HG2  A LYS   A 1 11  ? 11.088 -18.508 11.382  0.60 14.45 ?  11  LYS   A HG2  1 
ATOM   251  H  HG2  B LYS   A 1 11  ? 10.866 -18.168 11.439  0.40 15.10 ?  11  LYS   A HG2  1 
ATOM   252  H  HG3  A LYS   A 1 11  ? 12.194 -17.491 11.914  0.60 14.45 ?  11  LYS   A HG3  1 
ATOM   253  H  HG3  B LYS   A 1 11  ? 12.029 -17.369 12.179  0.40 15.10 ?  11  LYS   A HG3  1 
ATOM   254  H  HD2  A LYS   A 1 11  ? 11.739 -18.116 14.116  0.60 14.95 ?  11  LYS   A HD2  1 
ATOM   255  H  HD2  B LYS   A 1 11  ? 11.319 -18.300 14.221  0.40 15.54 ?  11  LYS   A HD2  1 
ATOM   256  H  HD3  A LYS   A 1 11  ? 10.578 -19.079 13.622  0.60 14.95 ?  11  LYS   A HD3  1 
ATOM   257  H  HD3  B LYS   A 1 11  ? 10.231 -19.150 13.430  0.40 15.54 ?  11  LYS   A HD3  1 
ATOM   258  H  HE2  A LYS   A 1 11  ? 12.499 -20.299 14.193  0.60 15.21 ?  11  LYS   A HE2  1 
ATOM   259  H  HE2  B LYS   A 1 11  ? 12.075 -20.484 13.905  0.40 15.26 ?  11  LYS   A HE2  1 
ATOM   260  H  HE3  A LYS   A 1 11  ? 12.135 -20.505 12.660  0.60 15.21 ?  11  LYS   A HE3  1 
ATOM   261  H  HE3  B LYS   A 1 11  ? 11.944 -20.301 12.330  0.40 15.26 ?  11  LYS   A HE3  1 
ATOM   262  H  HZ1  A LYS   A 1 11  ? 14.354 -20.142 12.900  0.60 15.13 ?  11  LYS   A HZ1  1 
ATOM   263  H  HZ1  B LYS   A 1 11  ? 14.086 -19.981 12.884  0.40 15.34 ?  11  LYS   A HZ1  1 
ATOM   264  H  HZ2  A LYS   A 1 11  ? 13.794 -19.039 12.146  0.60 15.13 ?  11  LYS   A HZ2  1 
ATOM   265  H  HZ2  B LYS   A 1 11  ? 13.585 -18.674 12.516  0.40 15.34 ?  11  LYS   A HZ2  1 
ATOM   266  H  HZ3  A LYS   A 1 11  ? 14.131 -18.864 13.545  0.60 15.13 ?  11  LYS   A HZ3  1 
ATOM   267  H  HZ3  B LYS   A 1 11  ? 13.765 -19.015 13.912  0.40 15.34 ?  11  LYS   A HZ3  1 
ATOM   268  N  N    A LEU   A 1 12  ? 10.772 -16.206 8.810   0.60 10.64 ?  12  LEU   A N    1 
ATOM   269  N  N    B LEU   A 1 12  ? 10.688 -15.917 9.197   0.40 10.76 ?  12  LEU   A N    1 
ATOM   270  C  CA   A LEU   A 1 12  ? 10.525 -16.805 7.500   0.60 10.81 ?  12  LEU   A CA   1 
ATOM   271  C  CA   B LEU   A 1 12  ? 10.442 -16.448 7.860   0.40 10.84 ?  12  LEU   A CA   1 
ATOM   272  C  C    A LEU   A 1 12  ? 11.121 -18.201 7.371   0.60 10.91 ?  12  LEU   A C    1 
ATOM   273  C  C    B LEU   A 1 12  ? 11.001 -17.851 7.674   0.40 10.67 ?  12  LEU   A C    1 
ATOM   274  O  O    A LEU   A 1 12  ? 10.501 -19.076 6.759   0.60 11.30 ?  12  LEU   A O    1 
ATOM   275  O  O    B LEU   A 1 12  ? 10.337 -18.718 7.097   0.40 10.34 ?  12  LEU   A O    1 
ATOM   276  C  CB   A LEU   A 1 12  ? 11.076 -15.922 6.376   0.60 11.12 ?  12  LEU   A CB   1 
ATOM   277  C  CB   B LEU   A 1 12  ? 11.035 -15.521 6.794   0.40 11.37 ?  12  LEU   A CB   1 
ATOM   278  C  CG   A LEU   A 1 12  ? 10.417 -14.562 6.160   0.60 12.57 ?  12  LEU   A CG   1 
ATOM   279  C  CG   B LEU   A 1 12  ? 10.346 -14.169 6.638   0.40 11.89 ?  12  LEU   A CG   1 
ATOM   280  C  CD1  A LEU   A 1 12  ? 11.189 -13.793 5.111   0.60 13.07 ?  12  LEU   A CD1  1 
ATOM   281  C  CD1  B LEU   A 1 12  ? 10.955 -13.404 5.479   0.40 12.41 ?  12  LEU   A CD1  1 
ATOM   282  C  CD2  A LEU   A 1 12  ? 8.961  -14.722 5.739   0.60 13.46 ?  12  LEU   A CD2  1 
ATOM   283  C  CD2  B LEU   A 1 12  ? 8.853  -14.363 6.436   0.40 11.86 ?  12  LEU   A CD2  1 
ATOM   284  H  H    A LEU   A 1 12  ? 11.510 -15.762 8.868   0.60 12.81 ?  12  LEU   A H    1 
ATOM   285  H  H    B LEU   A 1 12  ? 11.458 -15.533 9.290   0.40 12.96 ?  12  LEU   A H    1 
ATOM   286  H  HA   A LEU   A 1 12  ? 9.568  -16.886 7.373   0.60 13.01 ?  12  LEU   A HA   1 
ATOM   287  H  HA   B LEU   A 1 12  ? 9.485  -16.497 7.720   0.40 13.05 ?  12  LEU   A HA   1 
ATOM   288  H  HB2  A LEU   A 1 12  ? 12.013 -15.762 6.552   0.60 13.39 ?  12  LEU   A HB2  1 
ATOM   289  H  HB2  B LEU   A 1 12  ? 11.964 -15.349 7.018   0.40 13.69 ?  12  LEU   A HB2  1 
ATOM   290  H  HB3  A LEU   A 1 12  ? 10.990 -16.416 5.541   0.60 13.39 ?  12  LEU   A HB3  1 
ATOM   291  H  HB3  B LEU   A 1 12  ? 10.987 -15.972 5.937   0.40 13.69 ?  12  LEU   A HB3  1 
ATOM   292  H  HG   A LEU   A 1 12  ? 10.439 -14.060 6.989   0.60 15.13 ?  12  LEU   A HG   1 
ATOM   293  H  HG   B LEU   A 1 12  ? 10.477 -13.649 7.447   0.40 14.32 ?  12  LEU   A HG   1 
ATOM   294  H  HD11 A LEU   A 1 12  ? 10.767 -12.934 4.975   0.60 15.73 ?  12  LEU   A HD11 1 
ATOM   295  H  HD11 B LEU   A 1 12  ? 10.512 -12.545 5.399   0.40 14.93 ?  12  LEU   A HD11 1 
ATOM   296  H  HD12 A LEU   A 1 12  ? 12.101 -13.673 5.420   0.60 15.73 ?  12  LEU   A HD12 1 
ATOM   297  H  HD12 B LEU   A 1 12  ? 11.902 -13.273 5.650   0.40 14.93 ?  12  LEU   A HD12 1 
ATOM   298  H  HD13 A LEU   A 1 12  ? 11.186 -14.301 4.283   0.60 15.73 ?  12  LEU   A HD13 1 
ATOM   299  H  HD13 B LEU   A 1 12  ? 10.835 -13.917 4.665   0.40 14.93 ?  12  LEU   A HD13 1 
ATOM   300  H  HD21 A LEU   A 1 12  ? 8.562  -13.847 5.635   0.60 16.19 ?  12  LEU   A HD21 1 
ATOM   301  H  HD21 B LEU   A 1 12  ? 8.477  -13.553 6.065   0.40 14.27 ?  12  LEU   A HD21 1 
ATOM   302  H  HD22 A LEU   A 1 12  ? 8.929  -15.198 4.894   0.60 16.19 ?  12  LEU   A HD22 1 
ATOM   303  H  HD22 B LEU   A 1 12  ? 8.713  -15.106 5.828   0.40 14.27 ?  12  LEU   A HD22 1 
ATOM   304  H  HD23 A LEU   A 1 12  ? 8.480  -15.226 6.417   0.60 16.19 ?  12  LEU   A HD23 1 
ATOM   305  H  HD23 B LEU   A 1 12  ? 8.441  -14.558 7.294   0.40 14.27 ?  12  LEU   A HD23 1 
ATOM   306  N  N    A THR   A 1 13  ? 12.326 -18.403 7.901   0.60 11.27 ?  13  THR   A N    1 
ATOM   307  N  N    B THR   A 1 13  ? 12.231 -18.077 8.120   0.40 10.75 ?  13  THR   A N    1 
ATOM   308  C  CA   A THR   A 1 13  ? 13.036 -19.677 7.832   0.60 11.54 ?  13  THR   A CA   1 
ATOM   309  C  CA   B THR   A 1 13  ? 12.881 -19.371 8.001   0.40 11.34 ?  13  THR   A CA   1 
ATOM   310  C  C    A THR   A 1 13  ? 13.805 -19.868 9.134   0.60 11.68 ?  13  THR   A C    1 
ATOM   311  C  C    B THR   A 1 13  ? 13.653 -19.629 9.288   0.40 11.76 ?  13  THR   A C    1 
ATOM   312  O  O    A THR   A 1 13  ? 13.694 -19.074 10.073  0.60 11.91 ?  13  THR   A O    1 
ATOM   313  O  O    B THR   A 1 13  ? 13.575 -18.867 10.256  0.40 12.22 ?  13  THR   A O    1 
ATOM   314  C  CB   A THR   A 1 13  ? 14.025 -19.727 6.658   0.60 12.23 ?  13  THR   A CB   1 
ATOM   315  C  CB   B THR   A 1 13  ? 13.828 -19.415 6.795   0.40 11.88 ?  13  THR   A CB   1 
ATOM   316  O  OG1  A THR   A 1 13  ? 15.098 -18.816 6.914   0.60 12.44 ?  13  THR   A OG1  1 
ATOM   317  O  OG1  B THR   A 1 13  ? 14.880 -18.468 6.995   0.40 11.74 ?  13  THR   A OG1  1 
ATOM   318  C  CG2  A THR   A 1 13  ? 13.363 -19.372 5.337   0.60 13.33 ?  13  THR   A CG2  1 
ATOM   319  C  CG2  B THR   A 1 13  ? 13.097 -19.110 5.484   0.40 12.44 ?  13  THR   A CG2  1 
ATOM   320  H  H    A THR   A 1 13  ? 12.772 -17.794 8.306   0.60 13.57 ?  13  THR   A H    1 
ATOM   321  H  H    B THR   A 1 13  ? 12.723 -17.474 8.492   0.40 12.94 ?  13  THR   A H    1 
ATOM   322  H  HA   A THR   A 1 13  ? 12.398 -20.406 7.734   0.60 13.89 ?  13  THR   A HA   1 
ATOM   323  H  HA   B THR   A 1 13  ? 12.209 -20.059 7.893   0.40 13.65 ?  13  THR   A HA   1 
ATOM   324  H  HB   A THR   A 1 13  ? 14.383 -20.627 6.581   0.60 14.72 ?  13  THR   A HB   1 
ATOM   325  H  HB   B THR   A 1 13  ? 14.214 -20.301 6.723   0.40 14.29 ?  13  THR   A HB   1 
ATOM   326  H  HG1  A THR   A 1 13  ? 15.646 -18.833 6.273   0.60 14.97 ?  13  THR   A HG1  1 
ATOM   327  H  HG1  B THR   A 1 13  ? 15.404 -18.475 6.335   0.40 14.13 ?  13  THR   A HG1  1 
ATOM   328  H  HG21 A THR   A 1 13  ? 13.987 -19.515 4.607   0.60 16.04 ?  13  THR   A HG21 1 
ATOM   329  H  HG21 B THR   A 1 13  ? 13.711 -19.197 4.733   0.40 14.97 ?  13  THR   A HG21 1 
ATOM   330  H  HG22 A THR   A 1 13  ? 12.584 -19.933 5.195   0.60 16.04 ?  13  THR   A HG22 1 
ATOM   331  H  HG22 B THR   A 1 13  ? 12.365 -19.737 5.358   0.40 14.97 ?  13  THR   A HG22 1 
ATOM   332  H  HG23 A THR   A 1 13  ? 13.089 -18.444 5.342   0.60 16.04 ?  13  THR   A HG23 1 
ATOM   333  H  HG23 B THR   A 1 13  ? 12.744 -18.210 5.497   0.40 14.97 ?  13  THR   A HG23 1 
ATOM   334  N  N    A ASP   A 1 14  ? 14.636 -20.913 9.171   0.60 12.37 ?  14  ASP   A N    1 
ATOM   335  N  N    B ASP   A 1 14  ? 14.422 -20.715 9.276   0.40 12.23 ?  14  ASP   A N    1 
ATOM   336  C  CA   A ASP   A 1 14  ? 15.463 -21.156 10.347  0.60 13.32 ?  14  ASP   A CA   1 
ATOM   337  C  CA   B ASP   A 1 14  ? 15.306 -21.025 10.389  0.40 13.03 ?  14  ASP   A CA   1 
ATOM   338  C  C    A ASP   A 1 14  ? 16.292 -19.937 10.743  0.60 12.66 ?  14  ASP   A C    1 
ATOM   339  C  C    B ASP   A 1 14  ? 16.159 -19.820 10.770  0.40 12.42 ?  14  ASP   A C    1 
ATOM   340  O  O    A ASP   A 1 14  ? 16.576 -19.744 11.931  0.60 13.27 ?  14  ASP   A O    1 
ATOM   341  O  O    B ASP   A 1 14  ? 16.320 -19.514 11.957  0.40 12.84 ?  14  ASP   A O    1 
ATOM   342  C  CB   A ASP   A 1 14  ? 16.398 -22.334 10.092  0.60 16.15 ?  14  ASP   A CB   1 
ATOM   343  C  CB   B ASP   A 1 14  ? 16.195 -22.202 9.992   0.40 14.85 ?  14  ASP   A CB   1 
ATOM   344  C  CG   A ASP   A 1 14  ? 17.345 -22.565 11.245  0.60 20.23 ?  14  ASP   A CG   1 
ATOM   345  C  CG   B ASP   A 1 14  ? 17.100 -22.654 11.114  0.40 17.42 ?  14  ASP   A CG   1 
ATOM   346  O  OD1  A ASP   A 1 14  ? 16.880 -23.034 12.305  0.60 22.03 ?  14  ASP   A OD1  1 
ATOM   347  O  OD1  B ASP   A 1 14  ? 16.573 -23.045 12.178  0.40 18.24 ?  14  ASP   A OD1  1 
ATOM   348  O  OD2  A ASP   A 1 14  ? 18.545 -22.248 11.098  0.60 22.57 -1 14  ASP   A OD2  1 
ATOM   349  O  OD2  B ASP   A 1 14  ? 18.332 -22.642 10.925  0.40 19.13 -1 14  ASP   A OD2  1 
ATOM   350  H  H    A ASP   A 1 14  ? 14.743 -21.486 8.534   0.60 14.89 ?  14  ASP   A H    1 
ATOM   351  H  H    B ASP   A 1 14  ? 14.449 -21.274 8.632   0.40 14.72 ?  14  ASP   A H    1 
ATOM   352  H  HA   A ASP   A 1 14  ? 14.893 -21.388 11.096  0.60 16.03 ?  14  ASP   A HA   1 
ATOM   353  H  HA   B ASP   A 1 14  ? 14.772 -21.284 11.159  0.40 15.68 ?  14  ASP   A HA   1 
ATOM   354  H  HB2  A ASP   A 1 14  ? 15.860 -23.144 9.944   0.60 19.43 ?  14  ASP   A HB2  1 
ATOM   355  H  HB2  B ASP   A 1 14  ? 15.630 -22.956 9.755   0.40 17.86 ?  14  ASP   A HB2  1 
ATOM   356  H  HB3  A ASP   A 1 14  ? 16.938 -22.162 9.310   0.60 19.43 ?  14  ASP   A HB3  1 
ATOM   357  H  HB3  B ASP   A 1 14  ? 16.733 -21.942 9.227   0.40 17.86 ?  14  ASP   A HB3  1 
ATOM   358  N  N    . ASN   A 1 15  ? 16.697 -19.107 9.774   1.00 12.06 ?  15  ASN   A N    1 
ATOM   359  C  CA   . ASN   A 1 15  ? 17.681 -18.059 10.027  1.00 12.59 ?  15  ASN   A CA   1 
ATOM   360  C  C    . ASN   A 1 15  ? 17.312 -16.670 9.521   1.00 12.99 ?  15  ASN   A C    1 
ATOM   361  O  O    . ASN   A 1 15  ? 18.092 -15.739 9.750   1.00 14.40 ?  15  ASN   A O    1 
ATOM   362  C  CB   . ASN   A 1 15  ? 19.053 -18.458 9.452   1.00 12.53 ?  15  ASN   A CB   1 
ATOM   363  C  CG   . ASN   A 1 15  ? 19.045 -18.552 7.946   1.00 12.83 ?  15  ASN   A CG   1 
ATOM   364  O  OD1  . ASN   A 1 15  ? 18.317 -19.364 7.366   1.00 13.84 ?  15  ASN   A OD1  1 
ATOM   365  N  ND2  . ASN   A 1 15  ? 19.844 -17.711 7.297   1.00 12.94 ?  15  ASN   A ND2  1 
ATOM   366  H  H    A ASN   A 1 15  ? 16.397 -19.122 8.972   0.60 14.52 ?  15  ASN   A H    1 
ATOM   367  H  H    B ASN   A 1 15  ? 16.505 -19.215 8.947   0.40 14.52 ?  15  ASN   A H    1 
ATOM   368  H  HA   . ASN   A 1 15  ? 17.802 -17.979 10.986  1.00 15.16 ?  15  ASN   A HA   1 
ATOM   369  H  HB2  . ASN   A 1 15  ? 19.715 -17.789 9.714   1.00 15.08 ?  15  ASN   A HB2  1 
ATOM   370  H  HB3  . ASN   A 1 15  ? 19.312 -19.324 9.805   1.00 15.08 ?  15  ASN   A HB3  1 
ATOM   371  H  HD21 . ASN   A 1 15  ? 19.878 -17.721 6.437   1.00 15.58 ?  15  ASN   A HD21 1 
ATOM   372  H  HD22 . ASN   A 1 15  ? 20.339 -17.150 7.733   1.00 15.58 ?  15  ASN   A HD22 1 
ATOM   373  N  N    A VAL   A 1 16  ? 16.176 -16.494 8.848   0.60 12.50 ?  16  VAL   A N    1 
ATOM   374  N  N    B VAL   A 1 16  ? 16.163 -16.495 8.868   0.40 12.50 ?  16  VAL   A N    1 
ATOM   375  C  CA   A VAL   A 1 16  ? 15.791 -15.208 8.281   0.60 12.22 ?  16  VAL   A CA   1 
ATOM   376  C  CA   B VAL   A 1 16  ? 15.773 -15.226 8.264   0.40 12.12 ?  16  VAL   A CA   1 
ATOM   377  C  C    A VAL   A 1 16  ? 14.513 -14.718 8.950   0.60 12.24 ?  16  VAL   A C    1 
ATOM   378  C  C    B VAL   A 1 16  ? 14.504 -14.716 8.941   0.40 12.01 ?  16  VAL   A C    1 
ATOM   379  O  O    A VAL   A 1 16  ? 13.518 -15.452 9.039   0.60 12.68 ?  16  VAL   A O    1 
ATOM   380  O  O    B VAL   A 1 16  ? 13.503 -15.440 9.034   0.40 12.20 ?  16  VAL   A O    1 
ATOM   381  C  CB   A VAL   A 1 16  ? 15.634 -15.264 6.753   0.60 12.81 ?  16  VAL   A CB   1 
ATOM   382  C  CB   B VAL   A 1 16  ? 15.579 -15.358 6.742   0.40 12.52 ?  16  VAL   A CB   1 
ATOM   383  C  CG1  A VAL   A 1 16  ? 15.250 -13.883 6.211   0.60 13.28 ?  16  VAL   A CG1  1 
ATOM   384  C  CG1  B VAL   A 1 16  ? 15.105 -14.038 6.144   0.40 12.95 ?  16  VAL   A CG1  1 
ATOM   385  C  CG2  A VAL   A 1 16  ? 16.915 -15.762 6.100   0.60 13.82 ?  16  VAL   A CG2  1 
ATOM   386  C  CG2  B VAL   A 1 16  ? 16.871 -15.818 6.072   0.40 13.19 ?  16  VAL   A CG2  1 
ATOM   387  H  H    A VAL   A 1 16  ? 15.602 -17.123 8.712   0.60 15.04 ?  16  VAL   A H    1 
ATOM   388  H  H    B VAL   A 1 16  ? 15.579 -17.120 8.764   0.40 15.04 ?  16  VAL   A H    1 
ATOM   389  H  HA   A VAL   A 1 16  ? 16.491 -14.567 8.478   0.60 14.71 ?  16  VAL   A HA   1 
ATOM   390  H  HA   B VAL   A 1 16  ? 16.480 -14.578 8.417   0.40 14.58 ?  16  VAL   A HA   1 
ATOM   391  H  HB   A VAL   A 1 16  ? 14.924 -15.885 6.533   0.60 15.41 ?  16  VAL   A HB   1 
ATOM   392  H  HB   B VAL   A 1 16  ? 14.902 -16.027 6.568   0.40 15.07 ?  16  VAL   A HB   1 
ATOM   393  H  HG11 A VAL   A 1 16  ? 15.341 -13.892 5.246   0.60 15.98 ?  16  VAL   A HG11 1 
ATOM   394  H  HG11 B VAL   A 1 16  ? 15.194 -14.082 5.179   0.40 15.58 ?  16  VAL   A HG11 1 
ATOM   395  H  HG12 A VAL   A 1 16  ? 14.332 -13.691 6.455   0.60 15.98 ?  16  VAL   A HG12 1 
ATOM   396  H  HG12 B VAL   A 1 16  ? 14.177 -13.898 6.384   0.40 15.58 ?  16  VAL   A HG12 1 
ATOM   397  H  HG13 A VAL   A 1 16  ? 15.844 -13.219 6.594   0.60 15.98 ?  16  VAL   A HG13 1 
ATOM   398  H  HG13 B VAL   A 1 16  ? 15.654 -13.318 6.493   0.40 15.58 ?  16  VAL   A HG13 1 
ATOM   399  H  HG21 A VAL   A 1 16  ? 16.821 -15.701 5.138   0.60 16.62 ?  16  VAL   A HG21 1 
ATOM   400  H  HG21 B VAL   A 1 16  ? 16.733 -15.855 5.113   0.40 15.87 ?  16  VAL   A HG21 1 
ATOM   401  H  HG22 A VAL   A 1 16  ? 17.656 -15.212 6.397   0.60 16.62 ?  16  VAL   A HG22 1 
ATOM   402  H  HG22 B VAL   A 1 16  ? 17.578 -15.186 6.280   0.40 15.87 ?  16  VAL   A HG22 1 
ATOM   403  H  HG23 A VAL   A 1 16  ? 17.064 -16.684 6.361   0.60 16.62 ?  16  VAL   A HG23 1 
ATOM   404  H  HG23 B VAL   A 1 16  ? 17.106 -16.698 6.407   0.40 15.87 ?  16  VAL   A HG23 1 
ATOM   405  N  N    . TYR   A 1 17  ? 14.553 -13.458 9.386   1.00 11.88 ?  17  TYR   A N    1 
ATOM   406  C  CA   . TYR   A 1 17  ? 13.470 -12.775 10.081  1.00 11.86 ?  17  TYR   A CA   1 
ATOM   407  C  C    . TYR   A 1 17  ? 13.206 -11.442 9.383   1.00 12.24 ?  17  TYR   A C    1 
ATOM   408  O  O    . TYR   A 1 17  ? 14.114 -10.882 8.764   1.00 12.84 ?  17  TYR   A O    1 
ATOM   409  C  CB   . TYR   A 1 17  ? 13.909 -12.506 11.522  1.00 12.39 ?  17  TYR   A CB   1 
ATOM   410  C  CG   . TYR   A 1 17  ? 14.104 -13.769 12.332  1.00 13.37 ?  17  TYR   A CG   1 
ATOM   411  C  CD1  . TYR   A 1 17  ? 15.274 -14.520 12.238  1.00 14.19 ?  17  TYR   A CD1  1 
ATOM   412  C  CD2  . TYR   A 1 17  ? 13.106 -14.224 13.181  1.00 13.91 ?  17  TYR   A CD2  1 
ATOM   413  C  CE1  . TYR   A 1 17  ? 15.439 -15.699 12.972  1.00 14.93 ?  17  TYR   A CE1  1 
ATOM   414  C  CE2  . TYR   A 1 17  ? 13.256 -15.403 13.915  1.00 14.71 ?  17  TYR   A CE2  1 
ATOM   415  C  CZ   . TYR   A 1 17  ? 14.425 -16.133 13.813  1.00 14.98 ?  17  TYR   A CZ   1 
ATOM   416  O  OH   . TYR   A 1 17  ? 14.576 -17.287 14.550  1.00 16.09 ?  17  TYR   A OH   1 
ATOM   417  H  H    A TYR   A 1 17  ? 15.244 -12.949 9.274   0.60 14.30 ?  17  TYR   A H    1 
ATOM   418  H  H    B TYR   A 1 17  ? 15.249 -12.954 9.283   0.40 14.30 ?  17  TYR   A H    1 
ATOM   419  H  HA   . TYR   A 1 17  ? 12.666 -13.319 10.070  1.00 14.28 ?  17  TYR   A HA   1 
ATOM   420  H  HB2  . TYR   A 1 17  ? 14.749 -12.029 11.505  1.00 14.91 ?  17  TYR   A HB2  1 
ATOM   421  H  HB3  . TYR   A 1 17  ? 13.231 -11.977 11.957  1.00 14.91 ?  17  TYR   A HB3  1 
ATOM   422  H  HD1  . TYR   A 1 17  ? 15.957 -14.240 11.668  1.00 17.08 ?  17  TYR   A HD1  1 
ATOM   423  H  HD2  . TYR   A 1 17  ? 12.313 -13.742 13.251  1.00 16.74 ?  17  TYR   A HD2  1 
ATOM   424  H  HE1  . TYR   A 1 17  ? 16.231 -16.190 12.900  1.00 17.96 ?  17  TYR   A HE1  1 
ATOM   425  H  HE2  . TYR   A 1 17  ? 12.576 -15.684 14.484  1.00 17.69 ?  17  TYR   A HE2  1 
ATOM   426  H  HH   . TYR   A 1 17  ? 13.851 -17.472 14.933  1.00 19.34 ?  17  TYR   A HH   1 
ATOM   427  N  N    A ILE   A 1 18  ? 11.947 -10.981 9.380   0.60 11.99 ?  18  ILE   A N    1 
ATOM   428  N  N    B ILE   A 1 18  ? 12.017 -10.871 9.614   0.40 11.66 ?  18  ILE   A N    1 
ATOM   429  C  CA   A ILE   A 1 18  ? 11.561 -9.822  8.572   0.60 11.76 ?  18  ILE   A CA   1 
ATOM   430  C  CA   B ILE   A 1 18  ? 11.622 -9.640  8.933   0.40 11.07 ?  18  ILE   A CA   1 
ATOM   431  C  C    A ILE   A 1 18  ? 10.569 -8.938  9.327   0.60 12.13 ?  18  ILE   A C    1 
ATOM   432  C  C    B ILE   A 1 18  ? 10.708 -8.793  9.815   0.40 10.69 ?  18  ILE   A C    1 
ATOM   433  O  O    A ILE   A 1 18  ? 9.723  -9.428  10.081  0.60 12.23 ?  18  ILE   A O    1 
ATOM   434  O  O    B ILE   A 1 18  ? 9.889  -9.312  10.580  0.40 11.04 ?  18  ILE   A O    1 
ATOM   435  C  CB   A ILE   A 1 18  ? 11.027 -10.258 7.181   0.60 11.49 ?  18  ILE   A CB   1 
ATOM   436  C  CB   B ILE   A 1 18  ? 10.966 -9.973  7.576   0.40 10.67 ?  18  ILE   A CB   1 
ATOM   437  C  CG1  A ILE   A 1 18  ? 10.950 -9.069  6.223   0.60 11.44 ?  18  ILE   A CG1  1 
ATOM   438  C  CG1  B ILE   A 1 18  ? 10.897 -8.735  6.687   0.40 11.61 ?  18  ILE   A CG1  1 
ATOM   439  C  CG2  A ILE   A 1 18  ? 9.689  -10.993 7.302   0.60 11.44 ?  18  ILE   A CG2  1 
ATOM   440  C  CG2  B ILE   A 1 18  ? 9.595  -10.610 7.779   0.40 10.82 ?  18  ILE   A CG2  1 
ATOM   441  C  CD1  A ILE   A 1 18  ? 10.747 -9.483  4.793   0.60 12.49 ?  18  ILE   A CD1  1 
ATOM   442  C  CD1  B ILE   A 1 18  ? 10.508 -9.064  5.272   0.40 12.81 ?  18  ILE   A CD1  1 
ATOM   443  H  H    A ILE   A 1 18  ? 11.302 -11.331 9.827   0.60 14.44 ?  18  ILE   A H    1 
ATOM   444  H  H    B ILE   A 1 18  ? 11.431 -11.178 10.167  0.40 14.04 ?  18  ILE   A H    1 
ATOM   445  H  HA   A ILE   A 1 18  ? 12.353 -9.295  8.402   0.60 14.15 ?  18  ILE   A HA   1 
ATOM   446  H  HA   B ILE   A 1 18  ? 12.422 -9.120  8.761   0.40 13.33 ?  18  ILE   A HA   1 
ATOM   447  H  HB   A ILE   A 1 18  ? 11.659 -10.890 6.800   0.60 13.83 ?  18  ILE   A HB   1 
ATOM   448  H  HB   B ILE   A 1 18  ? 11.532 -10.619 7.138   0.40 12.85 ?  18  ILE   A HB   1 
ATOM   449  H  HG12 A ILE   A 1 18  ? 10.209 -8.501  6.475   0.60 13.78 ?  18  ILE   A HG12 1 
ATOM   450  H  HG12 B ILE   A 1 18  ? 10.240 -8.120  7.048   0.40 13.97 ?  18  ILE   A HG12 1 
ATOM   451  H  HG13 A ILE   A 1 18  ? 11.783 -8.574  6.269   0.60 13.78 ?  18  ILE   A HG13 1 
ATOM   452  H  HG13 B ILE   A 1 18  ? 11.772 -8.310  6.670   0.40 13.97 ?  18  ILE   A HG13 1 
ATOM   453  H  HG21 A ILE   A 1 18  ? 9.459  -11.387 6.440   0.60 13.78 ?  18  ILE   A HG21 1 
ATOM   454  H  HG21 B ILE   A 1 18  ? 9.291  -10.972 6.932   0.40 13.02 ?  18  ILE   A HG21 1 
ATOM   455  H  HG22 A ILE   A 1 18  ? 9.772  -11.694 7.966   0.60 13.78 ?  18  ILE   A HG22 1 
ATOM   456  H  HG22 B ILE   A 1 18  ? 9.670  -11.321 8.434   0.40 13.02 ?  18  ILE   A HG22 1 
ATOM   457  H  HG23 A ILE   A 1 18  ? 9.001  -10.364 7.566   0.60 13.78 ?  18  ILE   A HG23 1 
ATOM   458  H  HG23 B ILE   A 1 18  ? 8.971  -9.936  8.093   0.40 13.02 ?  18  ILE   A HG23 1 
ATOM   459  H  HD11 A ILE   A 1 18  ? 10.772 -8.690  4.229   0.60 15.03 ?  18  ILE   A HD11 1 
ATOM   460  H  HD11 B ILE   A 1 18  ? 10.601 -8.270  4.725   0.40 15.42 ?  18  ILE   A HD11 1 
ATOM   461  H  HD12 A ILE   A 1 18  ? 11.453 -10.092 4.534   0.60 15.03 ?  18  ILE   A HD12 1 
ATOM   462  H  HD12 B ILE   A 1 18  ? 11.093 -9.764  4.941   0.40 15.42 ?  18  ILE   A HD12 1 
ATOM   463  H  HD13 A ILE   A 1 18  ? 9.884  -9.917  4.708   0.60 15.03 ?  18  ILE   A HD13 1 
ATOM   464  H  HD13 B ILE   A 1 18  ? 9.588  -9.369  5.262   0.40 15.42 ?  18  ILE   A HD13 1 
ATOM   465  N  N    A LYS   A 1 19  ? 10.661 -7.624  9.103   0.60 11.55 ?  19  LYS   A N    1 
ATOM   466  N  N    B LYS   A 1 19  ? 10.834 -7.469  9.673   0.40 10.44 ?  19  LYS   A N    1 
ATOM   467  C  CA   A LYS   A 1 19  ? 9.836  -6.655  9.817   0.60 12.20 ?  19  LYS   A CA   1 
ATOM   468  C  CA   B LYS   A 1 19  ? 10.045 -6.512  10.439  0.40 11.63 ?  19  LYS   A CA   1 
ATOM   469  C  C    A LYS   A 1 19  ? 9.681  -5.403  8.963   0.60 12.55 ?  19  LYS   A C    1 
ATOM   470  C  C    B LYS   A 1 19  ? 9.820  -5.283  9.576   0.40 11.76 ?  19  LYS   A C    1 
ATOM   471  O  O    A LYS   A 1 19  ? 10.583 -5.048  8.200   0.60 12.26 ?  19  LYS   A O    1 
ATOM   472  O  O    B LYS   A 1 19  ? 10.712 -4.882  8.826   0.40 11.99 ?  19  LYS   A O    1 
ATOM   473  C  CB   A LYS   A 1 19  ? 10.518 -6.286  11.140  0.60 13.14 ?  19  LYS   A CB   1 
ATOM   474  C  CB   B LYS   A 1 19  ? 10.795 -6.111  11.719  0.40 12.72 ?  19  LYS   A CB   1 
ATOM   475  C  CG   A LYS   A 1 19  ? 9.752  -5.335  12.055  0.60 14.32 ?  19  LYS   A CG   1 
ATOM   476  C  CG   B LYS   A 1 19  ? 10.087 -5.158  12.672  0.40 13.65 ?  19  LYS   A CG   1 
ATOM   477  C  CD   A LYS   A 1 19  ? 10.596 -5.028  13.291  0.60 15.68 ?  19  LYS   A CD   1 
ATOM   478  C  CD   B LYS   A 1 19  ? 11.043 -4.821  13.817  0.40 14.64 ?  19  LYS   A CD   1 
ATOM   479  C  CE   A LYS   A 1 19  ? 9.885  -4.103  14.264  0.60 16.44 ?  19  LYS   A CE   1 
ATOM   480  C  CE   B LYS   A 1 19  ? 10.430 -3.945  14.890  0.40 15.45 ?  19  LYS   A CE   1 
ATOM   481  N  NZ   A LYS   A 1 19  ? 10.762 -3.739  15.413  0.60 17.00 ?  19  LYS   A NZ   1 
ATOM   482  N  NZ   B LYS   A 1 19  ? 11.358 -3.845  16.059  0.40 15.87 ?  19  LYS   A NZ   1 
ATOM   483  H  H    A LYS   A 1 19  ? 11.203 -7.273  8.536   0.60 13.90 ?  19  LYS   A H    1 
ATOM   484  H  H    B LYS   A 1 19  ? 11.392 -7.083  9.130   0.40 12.57 ?  19  LYS   A H    1 
ATOM   485  H  HA   A LYS   A 1 19  ? 8.958  -7.041  10.000  0.60 14.69 ?  19  LYS   A HA   1 
ATOM   486  H  HA   B LYS   A 1 19  ? 9.191  -6.888  10.679  0.40 14.00 ?  19  LYS   A HA   1 
ATOM   487  H  HB2  A LYS   A 1 19  ? 10.671 -7.104  11.639  0.60 15.82 ?  19  LYS   A HB2  1 
ATOM   488  H  HB2  B LYS   A 1 19  ? 10.982 -6.914  12.225  0.40 15.31 ?  19  LYS   A HB2  1 
ATOM   489  H  HB3  A LYS   A 1 19  ? 11.366 -5.871  10.932  0.60 15.82 ?  19  LYS   A HB3  1 
ATOM   490  H  HB3  B LYS   A 1 19  ? 11.631 -5.685  11.470  0.40 15.31 ?  19  LYS   A HB3  1 
ATOM   491  H  HG2  A LYS   A 1 19  ? 9.575  -4.505  11.587  0.60 17.22 ?  19  LYS   A HG2  1 
ATOM   492  H  HG2  B LYS   A 1 19  ? 9.854  -4.337  12.213  0.40 16.42 ?  19  LYS   A HG2  1 
ATOM   493  H  HG3  A LYS   A 1 19  ? 8.925  -5.752  12.341  0.60 17.22 ?  19  LYS   A HG3  1 
ATOM   494  H  HG3  B LYS   A 1 19  ? 9.299  -5.584  13.043  0.40 16.42 ?  19  LYS   A HG3  1 
ATOM   495  H  HD2  A LYS   A 1 19  ? 10.796 -5.857  13.755  0.60 18.86 ?  19  LYS   A HD2  1 
ATOM   496  H  HD2  B LYS   A 1 19  ? 11.319 -5.647  14.241  0.40 17.61 ?  19  LYS   A HD2  1 
ATOM   497  H  HD3  A LYS   A 1 19  ? 11.421 -4.597  13.014  0.60 18.86 ?  19  LYS   A HD3  1 
ATOM   498  H  HD3  B LYS   A 1 19  ? 11.816 -4.359  13.456  0.40 17.61 ?  19  LYS   A HD3  1 
ATOM   499  H  HE2  A LYS   A 1 19  ? 9.633  -3.287  13.804  0.60 19.77 ?  19  LYS   A HE2  1 
ATOM   500  H  HE2  B LYS   A 1 19  ? 10.284 -3.053  14.539  0.40 18.58 ?  19  LYS   A HE2  1 
ATOM   501  H  HE3  A LYS   A 1 19  ? 9.097  -4.549  14.612  0.60 19.77 ?  19  LYS   A HE3  1 
ATOM   502  H  HE3  B LYS   A 1 19  ? 9.597  -4.334  15.193  0.40 18.58 ?  19  LYS   A HE3  1 
ATOM   503  H  HZ1  A LYS   A 1 19  ? 10.326 -3.203  15.972  0.60 20.44 ?  19  LYS   A HZ1  1 
ATOM   504  H  HZ1  B LYS   A 1 19  ? 10.997 -3.333  16.692  0.40 19.08 ?  19  LYS   A HZ1  1 
ATOM   505  H  HZ2  A LYS   A 1 19  ? 11.009 -4.474  15.851  0.60 20.44 ?  19  LYS   A HZ2  1 
ATOM   506  H  HZ2  B LYS   A 1 19  ? 11.511 -4.655  16.396  0.40 19.08 ?  19  LYS   A HZ2  1 
ATOM   507  H  HZ3  A LYS   A 1 19  ? 11.491 -3.321  15.119  0.60 20.44 ?  19  LYS   A HZ3  1 
ATOM   508  H  HZ3  B LYS   A 1 19  ? 12.132 -3.487  15.805  0.40 19.08 ?  19  LYS   A HZ3  1 
ATOM   509  N  N    A ASN   A 1 20  ? 8.526  -4.740  9.088   0.60 13.29 ?  20  ASN   A N    1 
ATOM   510  N  N    B ASN   A 1 20  ? 8.628  -4.692  9.673   0.40 12.60 ?  20  ASN   A N    1 
ATOM   511  C  CA   A ASN   A 1 20  ? 8.314  -3.421  8.482   0.60 14.64 ?  20  ASN   A CA   1 
ATOM   512  C  CA   B ASN   A 1 20  ? 8.414  -3.372  9.094   0.40 13.68 ?  20  ASN   A CA   1 
ATOM   513  C  C    A ASN   A 1 20  ? 8.875  -2.368  9.439   0.60 16.18 ?  20  ASN   A C    1 
ATOM   514  C  C    B ASN   A 1 20  ? 9.123  -2.374  9.982   0.40 14.29 ?  20  ASN   A C    1 
ATOM   515  O  O    A ASN   A 1 20  ? 8.242  -2.030  10.442  0.60 17.03 ?  20  ASN   A O    1 
ATOM   516  O  O    B ASN   A 1 20  ? 8.738  -2.171  11.137  0.40 14.04 ?  20  ASN   A O    1 
ATOM   517  C  CB   A ASN   A 1 20  ? 6.825  -3.202  8.204   0.60 14.87 ?  20  ASN   A CB   1 
ATOM   518  C  CB   B ASN   A 1 20  ? 6.930  -3.036  8.980   0.40 14.26 ?  20  ASN   A CB   1 
ATOM   519  C  CG   A ASN   A 1 20  ? 6.498  -1.766  7.801   0.60 15.80 ?  20  ASN   A CG   1 
ATOM   520  C  CG   B ASN   A 1 20  ? 6.678  -1.556  8.698   0.40 15.09 ?  20  ASN   A CG   1 
ATOM   521  O  OD1  A ASN   A 1 20  ? 5.521  -1.180  8.281   0.60 17.62 ?  20  ASN   A OD1  1 
ATOM   522  O  OD1  B ASN   A 1 20  ? 5.848  -0.927  9.353   0.40 16.30 ?  20  ASN   A OD1  1 
ATOM   523  N  ND2  A ASN   A 1 20  ? 7.309  -1.201  6.912   0.60 15.79 ?  20  ASN   A ND2  1 
ATOM   524  N  ND2  B ASN   A 1 20  ? 7.397  -0.995  7.728   0.40 15.05 ?  20  ASN   A ND2  1 
ATOM   525  H  H    A ASN   A 1 20  ? 7.837  -5.049  9.510   0.60 16.00 ?  20  ASN   A H    1 
ATOM   526  H  H    B ASN   A 1 20  ? 7.950  -5.020  10.071  0.40 15.16 ?  20  ASN   A H    1 
ATOM   527  H  HA   A ASN   A 1 20  ? 8.792  -3.380  7.643   0.60 17.61 ?  20  ASN   A HA   1 
ATOM   528  H  HA   B ASN   A 1 20  ? 8.814  -3.327  8.215   0.40 16.46 ?  20  ASN   A HA   1 
ATOM   529  H  HB2  A ASN   A 1 20  ? 6.547  -3.779  7.474   0.60 17.88 ?  20  ASN   A HB2  1 
ATOM   530  H  HB2  B ASN   A 1 20  ? 6.550  -3.545  8.252   0.40 17.15 ?  20  ASN   A HB2  1 
ATOM   531  H  HB3  A ASN   A 1 20  ? 6.318  -3.416  9.003   0.60 17.88 ?  20  ASN   A HB3  1 
ATOM   532  H  HB3  B ASN   A 1 20  ? 6.489  -3.259  9.813   0.40 17.15 ?  20  ASN   A HB3  1 
ATOM   533  H  HD21 A ASN   A 1 20  ? 7.164  -0.392  6.660   0.60 18.99 ?  20  ASN   A HD21 1 
ATOM   534  H  HD21 B ASN   A 1 20  ? 7.281  -0.162  7.535   0.40 18.10 ?  20  ASN   A HD21 1 
ATOM   535  H  HD22 A ASN   A 1 20  ? 7.969  -1.644  6.589   0.60 18.99 ?  20  ASN   A HD22 1 
ATOM   536  H  HD22 B ASN   A 1 20  ? 7.971  -1.460  7.292   0.40 18.10 ?  20  ASN   A HD22 1 
ATOM   537  N  N    A ALA   A 1 21  ? 10.067 -1.840  9.140   0.60 17.08 ?  21  ALA   A N    1 
ATOM   538  N  N    B ALA   A 1 21  ? 10.194 -1.797  9.463   0.40 15.54 ?  21  ALA   A N    1 
ATOM   539  C  CA   A ALA   A 1 21  ? 10.741 -0.952  10.088  0.60 17.74 ?  21  ALA   A CA   1 
ATOM   540  C  CA   B ALA   A 1 21  ? 10.933 -0.803  10.212  0.40 16.03 ?  21  ALA   A CA   1 
ATOM   541  C  C    A ALA   A 1 21  ? 11.752 -0.051  9.383   0.60 17.09 ?  21  ALA   A C    1 
ATOM   542  C  C    B ALA   A 1 21  ? 11.908 -0.142  9.268   0.40 15.86 ?  21  ALA   A C    1 
ATOM   543  O  O    A ALA   A 1 21  ? 12.223 -0.353  8.282   0.60 16.68 ?  21  ALA   A O    1 
ATOM   544  O  O    B ALA   A 1 21  ? 12.423 -0.776  8.345   0.40 16.39 ?  21  ALA   A O    1 
ATOM   545  C  CB   A ALA   A 1 21  ? 11.436 -1.747  11.199  0.60 19.01 ?  21  ALA   A CB   1 
ATOM   546  C  CB   B ALA   A 1 21  ? 11.695 -1.438  11.377  0.40 16.64 ?  21  ALA   A CB   1 
ATOM   547  H  H    A ALA   A 1 21  ? 10.490 -1.977  8.407   0.60 20.54 ?  21  ALA   A H    1 
ATOM   548  H  H    B ALA   A 1 21  ? 10.514 -1.963  8.684   0.40 18.68 ?  21  ALA   A H    1 
ATOM   549  H  HA   A ALA   A 1 21  ? 10.073 -0.385  10.505  0.60 21.33 ?  21  ALA   A HA   1 
ATOM   550  H  HA   B ALA   A 1 21  ? 10.328 -0.127  10.560  0.40 19.28 ?  21  ALA   A HA   1 
ATOM   551  H  HB1  A ALA   A 1 21  ? 11.868 -1.125  11.806  0.60 22.85 ?  21  ALA   A HB1  1 
ATOM   552  H  HB1  B ALA   A 1 21  ? 12.111 -0.731  11.894  0.40 20.01 ?  21  ALA   A HB1  1 
ATOM   553  H  HB2  A ALA   A 1 21  ? 10.770 -2.267  11.680  0.60 22.85 ?  21  ALA   A HB2  1 
ATOM   554  H  HB2  B ALA   A 1 21  ? 11.067 -1.926  11.930  0.40 20.01 ?  21  ALA   A HB2  1 
ATOM   555  H  HB3  A ALA   A 1 21  ? 12.093 -2.337  10.803  0.60 22.85 ?  21  ALA   A HB3  1 
ATOM   556  H  HB3  B ALA   A 1 21  ? 12.366 -2.038  11.022  0.40 20.01 ?  21  ALA   A HB3  1 
ATOM   557  N  N    A ASP   A 1 22  ? 12.085 1.063   10.060  0.60 16.42 ?  22  ASP   A N    1 
ATOM   558  N  N    B ASP   A 1 22  ? 12.095 1.147   9.470   0.40 14.91 ?  22  ASP   A N    1 
ATOM   559  C  CA   A ASP   A 1 22  ? 13.104 2.021   9.621   0.60 16.35 ?  22  ASP   A CA   1 
ATOM   560  C  CA   B ASP   A 1 22  ? 13.252 1.835   8.933   0.40 14.33 ?  22  ASP   A CA   1 
ATOM   561  C  C    A ASP   A 1 22  ? 14.446 1.581   10.200  0.60 15.03 ?  22  ASP   A C    1 
ATOM   562  C  C    B ASP   A 1 22  ? 14.503 1.233   9.565   0.40 13.21 ?  22  ASP   A C    1 
ATOM   563  O  O    A ASP   A 1 22  ? 14.638 1.602   11.420  0.60 15.66 ?  22  ASP   A O    1 
ATOM   564  O  O    B ASP   A 1 22  ? 14.621 1.187   10.793  0.40 13.52 ?  22  ASP   A O    1 
ATOM   565  C  CB   A ASP   A 1 22  ? 12.737 3.428   10.102  0.60 17.91 ?  22  ASP   A CB   1 
ATOM   566  C  CB   B ASP   A 1 22  ? 13.115 3.299   9.329   0.40 15.00 ?  22  ASP   A CB   1 
ATOM   567  C  CG   A ASP   A 1 22  ? 13.758 4.495   9.696   0.60 19.70 ?  22  ASP   A CG   1 
ATOM   568  C  CG   B ASP   A 1 22  ? 14.110 4.185   8.646   0.40 15.04 ?  22  ASP   A CG   1 
ATOM   569  O  OD1  A ASP   A 1 22  ? 14.873 4.155   9.252   0.60 20.06 ?  22  ASP   A OD1  1 
ATOM   570  O  OD1  B ASP   A 1 22  ? 15.192 3.696   8.256   0.40 13.97 ?  22  ASP   A OD1  1 
ATOM   571  O  OD2  A ASP   A 1 22  ? 13.438 5.697   9.833   0.60 21.20 -1 22  ASP   A OD2  1 
ATOM   572  O  OD2  B ASP   A 1 22  ? 13.799 5.385   8.508   0.40 16.16 -1 22  ASP   A OD2  1 
ATOM   573  H  H    A ASP   A 1 22  ? 11.709 1.296   10.801  0.60 19.74 ?  22  ASP   A H    1 
ATOM   574  H  H    B ASP   A 1 22  ? 11.545 1.651   9.905   0.40 17.93 ?  22  ASP   A H    1 
ATOM   575  H  HA   A ASP   A 1 22  ? 13.164 2.025   8.653   0.60 19.66 ?  22  ASP   A HA   1 
ATOM   576  H  HA   B ASP   A 1 22  ? 13.283 1.748   7.961   0.40 17.24 ?  22  ASP   A HA   1 
ATOM   577  H  HB2  A ASP   A 1 22  ? 11.873 3.672   9.735   0.60 21.54 ?  22  ASP   A HB2  1 
ATOM   578  H  HB2  B ASP   A 1 22  ? 12.231 3.615   9.093   0.40 18.04 ?  22  ASP   A HB2  1 
ATOM   579  H  HB3  A ASP   A 1 22  ? 12.694 3.428   11.072  0.60 21.54 ?  22  ASP   A HB3  1 
ATOM   580  H  HB3  B ASP   A 1 22  ? 13.252 3.375   10.286  0.40 18.04 ?  22  ASP   A HB3  1 
ATOM   581  N  N    A ILE   A 1 23  ? 15.376 1.193   9.322   0.60 14.09 ?  23  ILE   A N    1 
ATOM   582  N  N    B ILE   A 1 23  ? 15.433 0.753   8.731   0.40 12.22 ?  23  ILE   A N    1 
ATOM   583  C  CA   A ILE   A 1 23  ? 16.631 0.581   9.759   0.60 12.97 ?  23  ILE   A CA   1 
ATOM   584  C  CA   B ILE   A 1 23  ? 16.657 0.150   9.259   0.40 11.62 ?  23  ILE   A CA   1 
ATOM   585  C  C    A ILE   A 1 23  ? 17.446 1.532   10.626  0.60 12.64 ?  23  ILE   A C    1 
ATOM   586  C  C    B ILE   A 1 23  ? 17.389 1.122   10.172  0.40 12.23 ?  23  ILE   A C    1 
ATOM   587  O  O    A ILE   A 1 23  ? 18.180 1.093   11.520  0.60 13.13 ?  23  ILE   A O    1 
ATOM   588  O  O    B ILE   A 1 23  ? 18.039 0.706   11.139  0.40 12.26 ?  23  ILE   A O    1 
ATOM   589  C  CB   A ILE   A 1 23  ? 17.426 0.062   8.541   0.60 12.34 ?  23  ILE   A CB   1 
ATOM   590  C  CB   B ILE   A 1 23  ? 17.572 -0.393  8.136   0.40 10.92 ?  23  ILE   A CB   1 
ATOM   591  C  CG1  A ILE   A 1 23  ? 18.569 -0.849  8.989   0.60 12.78 ?  23  ILE   A CG1  1 
ATOM   592  C  CG1  B ILE   A 1 23  ? 18.652 -1.306  8.735   0.40 10.93 ?  23  ILE   A CG1  1 
ATOM   593  C  CG2  A ILE   A 1 23  ? 17.936 1.219   7.683   0.60 12.39 ?  23  ILE   A CG2  1 
ATOM   594  C  CG2  B ILE   A 1 23  ? 18.206 0.745   7.341   0.40 10.64 ?  23  ILE   A CG2  1 
ATOM   595  C  CD1  A ILE   A 1 23  ? 19.225 -1.591  7.844   0.60 12.94 ?  23  ILE   A CD1  1 
ATOM   596  C  CD1  B ILE   A 1 23  ? 19.595 -1.924  7.711   0.40 11.03 ?  23  ILE   A CD1  1 
ATOM   597  H  H    A ILE   A 1 23  ? 15.299 1.270   8.472   0.60 16.95 ?  23  ILE   A H    1 
ATOM   598  H  H    B ILE   A 1 23  ? 15.376 0.761   7.884   0.40 14.71 ?  23  ILE   A H    1 
ATOM   599  H  HA   A ILE   A 1 23  ? 16.419 -0.187  10.307  0.60 15.61 ?  23  ILE   A HA   1 
ATOM   600  H  HA   B ILE   A 1 23  ? 16.397 -0.608  9.802   0.40 13.99 ?  23  ILE   A HA   1 
ATOM   601  H  HB   A ILE   A 1 23  ? 16.824 -0.466  7.997   0.60 14.85 ?  23  ILE   A HB   1 
ATOM   602  H  HB   B ILE   A 1 23  ? 17.030 -0.927  7.532   0.40 13.15 ?  23  ILE   A HB   1 
ATOM   603  H  HG12 A ILE   A 1 23  ? 19.252 -0.314  9.422   0.60 15.38 ?  23  ILE   A HG12 1 
ATOM   604  H  HG12 B ILE   A 1 23  ? 19.191 -0.789  9.354   0.40 13.15 ?  23  ILE   A HG12 1 
ATOM   605  H  HG13 A ILE   A 1 23  ? 18.222 -1.509  9.608   0.60 15.38 ?  23  ILE   A HG13 1 
ATOM   606  H  HG13 B ILE   A 1 23  ? 18.219 -2.033  9.212   0.40 13.15 ?  23  ILE   A HG13 1 
ATOM   607  H  HG21 A ILE   A 1 23  ? 18.280 0.867   6.846   0.60 14.91 ?  23  ILE   A HG21 1 
ATOM   608  H  HG21 B ILE   A 1 23  ? 18.603 0.377   6.532   0.40 12.81 ?  23  ILE   A HG21 1 
ATOM   609  H  HG22 A ILE   A 1 23  ? 17.197 1.826   7.501   0.60 14.91 ?  23  ILE   A HG22 1 
ATOM   610  H  HG22 B ILE   A 1 23  ? 17.521 1.386   7.111   0.40 12.81 ?  23  ILE   A HG22 1 
ATOM   611  H  HG23 A ILE   A 1 23  ? 18.636 1.689   8.159   0.60 14.91 ?  23  ILE   A HG23 1 
ATOM   612  H  HG23 B ILE   A 1 23  ? 18.892 1.163   7.882   0.40 12.81 ?  23  ILE   A HG23 1 
ATOM   613  H  HD11 A ILE   A 1 23  ? 19.888 -2.202  8.202   0.60 15.57 ?  23  ILE   A HD11 1 
ATOM   614  H  HD11 B ILE   A 1 23  ? 20.167 -2.571  8.160   0.40 13.27 ?  23  ILE   A HD11 1 
ATOM   615  H  HD12 A ILE   A 1 23  ? 18.545 -2.088  7.361   0.60 15.57 ?  23  ILE   A HD12 1 
ATOM   616  H  HD12 B ILE   A 1 23  ? 19.071 -2.368  7.027   0.40 13.27 ?  23  ILE   A HD12 1 
ATOM   617  H  HD13 A ILE   A 1 23  ? 19.649 -0.951  7.253   0.60 15.57 ?  23  ILE   A HD13 1 
ATOM   618  H  HD13 B ILE   A 1 23  ? 20.136 -1.225  7.316   0.40 13.27 ?  23  ILE   A HD13 1 
ATOM   619  N  N    A VAL   A 1 24  ? 17.328 2.840   10.390  0.60 13.23 ?  24  VAL   A N    1 
ATOM   620  N  N    B VAL   A 1 24  ? 17.291 2.425   9.893   0.40 12.67 ?  24  VAL   A N    1 
ATOM   621  C  CA   A VAL   A 1 24  ? 18.008 3.810   11.244  0.60 14.57 ?  24  VAL   A CA   1 
ATOM   622  C  CA   B VAL   A 1 24  ? 17.923 3.418   10.756  0.40 13.53 ?  24  VAL   A CA   1 
ATOM   623  C  C    A VAL   A 1 24  ? 17.489 3.708   12.671  0.60 15.08 ?  24  VAL   A C    1 
ATOM   624  C  C    B VAL   A 1 24  ? 17.299 3.390   12.144  0.40 14.43 ?  24  VAL   A C    1 
ATOM   625  O  O    A VAL   A 1 24  ? 18.264 3.607   13.632  0.60 15.20 ?  24  VAL   A O    1 
ATOM   626  O  O    B VAL   A 1 24  ? 18.001 3.458   13.159  0.40 14.77 ?  24  VAL   A O    1 
ATOM   627  C  CB   A VAL   A 1 24  ? 17.830 5.232   10.683  0.60 15.17 ?  24  VAL   A CB   1 
ATOM   628  C  CB   B VAL   A 1 24  ? 17.837 4.814   10.113  0.40 13.81 ?  24  VAL   A CB   1 
ATOM   629  C  CG1  A VAL   A 1 24  ? 18.309 6.274   11.692  0.60 15.56 ?  24  VAL   A CG1  1 
ATOM   630  C  CG1  B VAL   A 1 24  ? 18.486 5.853   11.012  0.40 14.77 ?  24  VAL   A CG1  1 
ATOM   631  C  CG2  A VAL   A 1 24  ? 18.567 5.378   9.360   0.60 16.14 ?  24  VAL   A CG2  1 
ATOM   632  C  CG2  B VAL   A 1 24  ? 18.488 4.797   8.743   0.40 13.38 ?  24  VAL   A CG2  1 
ATOM   633  H  H    A VAL   A 1 24  ? 16.868 3.185   9.751   0.60 15.92 ?  24  VAL   A H    1 
ATOM   634  H  H    B VAL   A 1 24  ? 16.865 2.755   9.225   0.40 15.25 ?  24  VAL   A H    1 
ATOM   635  H  HA   A VAL   A 1 24  ? 18.956 3.615   11.255  0.60 17.53 ?  24  VAL   A HA   1 
ATOM   636  H  HA   B VAL   A 1 24  ? 18.860 3.195   10.854  0.40 16.28 ?  24  VAL   A HA   1 
ATOM   637  H  HB   A VAL   A 1 24  ? 16.889 5.393   10.513  0.60 18.25 ?  24  VAL   A HB   1 
ATOM   638  H  HB   B VAL   A 1 24  ? 16.904 5.055   10.000  0.40 16.61 ?  24  VAL   A HB   1 
ATOM   639  H  HG11 A VAL   A 1 24  ? 18.455 7.115   11.229  0.60 18.71 ?  24  VAL   A HG11 1 
ATOM   640  H  HG11 B VAL   A 1 24  ? 18.613 6.671   10.508  0.40 17.76 ?  24  VAL   A HG11 1 
ATOM   641  H  HG12 A VAL   A 1 24  ? 17.632 6.387   12.374  0.60 18.71 ?  24  VAL   A HG12 1 
ATOM   642  H  HG12 B VAL   A 1 24  ? 17.904 6.021   11.770  0.40 17.76 ?  24  VAL   A HG12 1 
ATOM   643  H  HG13 A VAL   A 1 24  ? 19.140 5.969   12.089  0.60 18.71 ?  24  VAL   A HG13 1 
ATOM   644  H  HG13 B VAL   A 1 24  ? 19.342 5.516   11.318  0.40 17.76 ?  24  VAL   A HG13 1 
ATOM   645  H  HG21 A VAL   A 1 24  ? 18.388 6.258   8.990   0.60 19.40 ?  24  VAL   A HG21 1 
ATOM   646  H  HG21 B VAL   A 1 24  ? 18.584 5.708   8.429   0.40 16.10 ?  24  VAL   A HG21 1 
ATOM   647  H  HG22 A VAL   A 1 24  ? 19.520 5.276   9.514   0.60 19.40 ?  24  VAL   A HG22 1 
ATOM   648  H  HG22 B VAL   A 1 24  ? 19.361 4.379   8.817   0.40 16.10 ?  24  VAL   A HG22 1 
ATOM   649  H  HG23 A VAL   A 1 24  ? 18.257 4.694   8.745   0.60 19.40 ?  24  VAL   A HG23 1 
ATOM   650  H  HG23 B VAL   A 1 24  ? 17.930 4.290   8.135   0.40 16.10 ?  24  VAL   A HG23 1 
ATOM   651  N  N    A GLU   A 1 25  ? 16.165 3.750   12.827  0.60 15.80 ?  25  GLU   A N    1 
ATOM   652  N  N    B GLU   A 1 25  ? 15.971 3.274   12.212  0.40 15.30 ?  25  GLU   A N    1 
ATOM   653  C  CA   A GLU   A 1 25  ? 15.573 3.674   14.156  0.60 17.32 ?  25  GLU   A CA   1 
ATOM   654  C  CA   B GLU   A 1 25  ? 15.300 3.222   13.508  0.40 16.57 ?  25  GLU   A CA   1 
ATOM   655  C  C    A GLU   A 1 25  ? 15.807 2.308   14.785  0.60 16.70 ?  25  GLU   A C    1 
ATOM   656  C  C    B GLU   A 1 25  ? 15.580 1.908   14.231  0.40 16.69 ?  25  GLU   A C    1 
ATOM   657  O  O    A GLU   A 1 25  ? 16.037 2.207   15.996  0.60 17.27 ?  25  GLU   A O    1 
ATOM   658  O  O    B GLU   A 1 25  ? 15.769 1.899   15.453  0.40 17.07 ?  25  GLU   A O    1 
ATOM   659  C  CB   A GLU   A 1 25  ? 14.080 4.005   14.076  0.60 19.96 ?  25  GLU   A CB   1 
ATOM   660  C  CB   B GLU   A 1 25  ? 13.799 3.467   13.337  0.40 18.28 ?  25  GLU   A CB   1 
ATOM   661  C  CG   A GLU   A 1 25  ? 13.810 5.455   13.692  0.60 22.76 ?  25  GLU   A CG   1 
ATOM   662  C  CG   B GLU   A 1 25  ? 13.473 4.854   12.796  0.40 20.60 ?  25  GLU   A CG   1 
ATOM   663  C  CD   A GLU   A 1 25  ? 14.599 6.445   14.533  0.60 24.98 ?  25  GLU   A CD   1 
ATOM   664  C  CD   B GLU   A 1 25  ? 14.015 5.965   13.675  0.40 22.78 ?  25  GLU   A CD   1 
ATOM   665  O  OE1  A GLU   A 1 25  ? 14.693 6.242   15.763  0.60 25.60 ?  25  GLU   A OE1  1 
ATOM   666  O  OE1  B GLU   A 1 25  ? 14.042 5.787   14.911  0.40 23.93 ?  25  GLU   A OE1  1 
ATOM   667  O  OE2  A GLU   A 1 25  ? 15.142 7.413   13.961  0.60 26.12 -1 25  GLU   A OE2  1 
ATOM   668  O  OE2  B GLU   A 1 25  ? 14.424 7.010   13.128  0.40 23.61 -1 25  GLU   A OE2  1 
ATOM   669  H  H    A GLU   A 1 25  ? 15.599 3.837   12.187  0.60 19.00 ?  25  GLU   A H    1 
ATOM   670  H  H    B GLU   A 1 25  ? 15.446 3.224   11.533  0.40 18.40 ?  25  GLU   A H    1 
ATOM   671  H  HA   A GLU   A 1 25  ? 15.995 4.328   14.731  0.60 20.82 ?  25  GLU   A HA   1 
ATOM   672  H  HA   B GLU   A 1 25  ? 15.649 3.933   14.062  0.40 19.93 ?  25  GLU   A HA   1 
ATOM   673  H  HB2  A GLU   A 1 25  ? 13.663 3.440   13.401  0.60 24.00 ?  25  GLU   A HB2  1 
ATOM   674  H  HB2  B GLU   A 1 25  ? 13.439 2.815   12.714  0.40 21.98 ?  25  GLU   A HB2  1 
ATOM   675  H  HB3  A GLU   A 1 25  ? 13.667 3.844   14.938  0.60 24.00 ?  25  GLU   A HB3  1 
ATOM   676  H  HB3  B GLU   A 1 25  ? 13.362 3.375   14.199  0.40 21.98 ?  25  GLU   A HB3  1 
ATOM   677  H  HG2  A GLU   A 1 25  ? 14.069 5.591   12.770  0.60 27.36 ?  25  GLU   A HG2  1 
ATOM   678  H  HG2  B GLU   A 1 25  ? 13.878 4.956   11.922  0.40 24.76 ?  25  GLU   A HG2  1 
ATOM   679  H  HG3  A GLU   A 1 25  ? 12.865 5.642   13.807  0.60 27.36 ?  25  GLU   A HG3  1 
ATOM   680  H  HG3  B GLU   A 1 25  ? 12.509 4.950   12.731  0.40 24.76 ?  25  GLU   A HG3  1 
ATOM   681  N  N    A GLU   A 1 26  ? 15.764 1.246   13.978  0.60 16.50 ?  26  GLU   A N    1 
ATOM   682  N  N    B GLU   A 1 26  ? 15.613 0.787   13.503  0.40 16.55 ?  26  GLU   A N    1 
ATOM   683  C  CA   A GLU   A 1 26  ? 16.033 -0.091  14.499  0.60 16.38 ?  26  GLU   A CA   1 
ATOM   684  C  CA   B GLU   A 1 26  ? 16.016 -0.474  14.124  0.40 16.98 ?  26  GLU   A CA   1 
ATOM   685  C  C    A GLU   A 1 26  ? 17.462 -0.194  15.022  0.60 15.95 ?  26  GLU   A C    1 
ATOM   686  C  C    B GLU   A 1 26  ? 17.413 -0.367  14.721  0.40 16.06 ?  26  GLU   A C    1 
ATOM   687  O  O    A GLU   A 1 26  ? 17.700 -0.715  16.117  0.60 16.28 ?  26  GLU   A O    1 
ATOM   688  O  O    B GLU   A 1 26  ? 17.667 -0.861  15.825  0.40 16.25 ?  26  GLU   A O    1 
ATOM   689  C  CB   A GLU   A 1 26  ? 15.782 -1.137  13.410  0.60 17.96 ?  26  GLU   A CB   1 
ATOM   690  C  CB   B GLU   A 1 26  ? 15.991 -1.612  13.101  0.40 18.34 ?  26  GLU   A CB   1 
ATOM   691  C  CG   A GLU   A 1 26  ? 14.353 -1.639  13.312  0.60 21.20 ?  26  GLU   A CG   1 
ATOM   692  C  CG   B GLU   A 1 26  ? 14.617 -2.161  12.776  0.40 18.93 ?  26  GLU   A CG   1 
ATOM   693  C  CD   A GLU   A 1 26  ? 13.933 -2.427  14.540  0.60 23.47 ?  26  GLU   A CD   1 
ATOM   694  C  CD   B GLU   A 1 26  ? 13.882 -2.724  13.989  0.40 19.10 ?  26  GLU   A CD   1 
ATOM   695  O  OE1  A GLU   A 1 26  ? 14.551 -3.474  14.823  0.60 24.00 ?  26  GLU   A OE1  1 
ATOM   696  O  OE1  B GLU   A 1 26  ? 14.275 -3.801  14.499  0.40 19.53 ?  26  GLU   A OE1  1 
ATOM   697  O  OE2  A GLU   A 1 26  ? 12.997 -1.980  15.230  0.60 24.85 -1 26  GLU   A OE2  1 
ATOM   698  O  OE2  B GLU   A 1 26  ? 12.899 -2.089  14.427  0.40 18.63 -1 26  GLU   A OE2  1 
ATOM   699  H  H    A GLU   A 1 26  ? 15.602 1.280   13.135  0.60 19.84 ?  26  GLU   A H    1 
ATOM   700  H  H    B GLU   A 1 26  ? 15.404 0.730   12.671  0.40 19.90 ?  26  GLU   A H    1 
ATOM   701  H  HA   A GLU   A 1 26  ? 15.432 -0.268  15.233  0.60 19.69 ?  26  GLU   A HA   1 
ATOM   702  H  HA   B GLU   A 1 26  ? 15.396 -0.693  14.837  0.40 20.42 ?  26  GLU   A HA   1 
ATOM   703  H  HB2  A GLU   A 1 26  ? 16.015 -0.748  12.549  0.60 21.60 ?  26  GLU   A HB2  1 
ATOM   704  H  HB2  B GLU   A 1 26  ? 16.379 -1.287  12.270  0.40 22.05 ?  26  GLU   A HB2  1 
ATOM   705  H  HB3  A GLU   A 1 26  ? 16.353 -1.901  13.582  0.60 21.60 ?  26  GLU   A HB3  1 
ATOM   706  H  HB3  B GLU   A 1 26  ? 16.527 -2.346  13.440  0.40 22.05 ?  26  GLU   A HB3  1 
ATOM   707  H  HG2  A GLU   A 1 26  ? 13.754 -0.882  13.240  0.60 25.48 ?  26  GLU   A HG2  1 
ATOM   708  H  HG2  B GLU   A 1 26  ? 14.097 -1.444  12.394  0.40 22.76 ?  26  GLU   A HG2  1 
ATOM   709  H  HG3  A GLU   A 1 26  ? 14.270 -2.201  12.521  0.60 25.48 ?  26  GLU   A HG3  1 
ATOM   710  H  HG3  B GLU   A 1 26  ? 14.714 -2.882  12.134  0.40 22.76 ?  26  GLU   A HG3  1 
ATOM   711  N  N    A ALA   A 1 27  ? 18.432 0.305   14.253  0.60 15.21 ?  27  ALA   A N    1 
ATOM   712  N  N    B ALA   A 1 27  ? 18.339 0.264   13.998  0.40 14.78 ?  27  ALA   A N    1 
ATOM   713  C  CA   A ALA   A 1 27  ? 19.824 0.218   14.685  0.60 15.44 ?  27  ALA   A CA   1 
ATOM   714  C  CA   B ALA   A 1 27  ? 19.717 0.341   14.471  0.40 14.59 ?  27  ALA   A CA   1 
ATOM   715  C  C    A ALA   A 1 27  ? 20.051 1.010   15.966  0.60 16.94 ?  27  ALA   A C    1 
ATOM   716  C  C    B ALA   A 1 27  ? 19.816 1.170   15.747  0.40 15.71 ?  27  ALA   A C    1 
ATOM   717  O  O    A ALA   A 1 27  ? 20.721 0.532   16.889  0.60 17.07 ?  27  ALA   A O    1 
ATOM   718  O  O    B ALA   A 1 27  ? 20.471 0.765   16.713  0.40 15.66 ?  27  ALA   A O    1 
ATOM   719  C  CB   A ALA   A 1 27  ? 20.760 0.693   13.569  0.60 14.74 ?  27  ALA   A CB   1 
ATOM   720  C  CB   B ALA   A 1 27  ? 20.613 0.920   13.375  0.40 13.87 ?  27  ALA   A CB   1 
ATOM   721  H  H    A ALA   A 1 27  ? 18.314 0.700   13.500  0.60 18.30 ?  27  ALA   A H    1 
ATOM   722  H  H    B ALA   A 1 27  ? 18.191 0.649   13.245  0.40 17.77 ?  27  ALA   A H    1 
ATOM   723  H  HA   A ALA   A 1 27  ? 20.036 -0.707  14.872  0.60 18.57 ?  27  ALA   A HA   1 
ATOM   724  H  HA   B ALA   A 1 27  ? 20.026 -0.555  14.670  0.40 17.55 ?  27  ALA   A HA   1 
ATOM   725  H  HB1  A ALA   A 1 27  ? 21.680 0.624   13.875  0.60 17.73 ?  27  ALA   A HB1  1 
ATOM   726  H  HB1  B ALA   A 1 27  ? 21.523 0.961   13.704  0.40 16.68 ?  27  ALA   A HB1  1 
ATOM   727  H  HB2  A ALA   A 1 27  ? 20.632 0.129   12.789  0.60 17.73 ?  27  ALA   A HB2  1 
ATOM   728  H  HB2  B ALA   A 1 27  ? 20.567 0.348   12.594  0.40 16.68 ?  27  ALA   A HB2  1 
ATOM   729  H  HB3  A ALA   A 1 27  ? 20.555 1.614   13.349  0.60 17.73 ?  27  ALA   A HB3  1 
ATOM   730  H  HB3  B ALA   A 1 27  ? 20.301 1.812   13.150  0.40 16.68 ?  27  ALA   A HB3  1 
ATOM   731  N  N    A LYS   A 1 28  ? 19.484 2.216   16.052  0.60 19.19 ?  28  LYS   A N    1 
ATOM   732  N  N    B LYS   A 1 28  ? 19.160 2.332   15.774  0.40 17.52 ?  28  LYS   A N    1 
ATOM   733  C  CA   A LYS   A 1 28  ? 19.633 3.016   17.264  0.60 21.93 ?  28  LYS   A CA   1 
ATOM   734  C  CA   B LYS   A 1 28  ? 19.256 3.207   16.939  0.40 19.99 ?  28  LYS   A CA   1 
ATOM   735  C  C    A LYS   A 1 28  ? 19.062 2.294   18.479  0.60 22.77 ?  28  LYS   A C    1 
ATOM   736  C  C    B LYS   A 1 28  ? 18.749 2.531   18.205  0.40 21.24 ?  28  LYS   A C    1 
ATOM   737  O  O    A LYS   A 1 28  ? 19.620 2.382   19.579  0.60 23.93 ?  28  LYS   A O    1 
ATOM   738  O  O    B LYS   A 1 28  ? 19.260 2.801   19.297  0.40 21.80 ?  28  LYS   A O    1 
ATOM   739  C  CB   A LYS   A 1 28  ? 18.989 4.393   17.073  0.60 23.79 ?  28  LYS   A CB   1 
ATOM   740  C  CB   B LYS   A 1 28  ? 18.482 4.500   16.694  0.40 21.47 ?  28  LYS   A CB   1 
ATOM   741  C  CG   A LYS   A 1 28  ? 19.802 5.324   16.181  0.60 25.63 ?  28  LYS   A CG   1 
ATOM   742  C  CG   B LYS   A 1 28  ? 19.132 5.412   15.677  0.40 23.29 ?  28  LYS   A CG   1 
ATOM   743  C  CD   A LYS   A 1 28  ? 19.308 6.763   16.239  0.60 27.68 ?  28  LYS   A CD   1 
ATOM   744  C  CD   B LYS   A 1 28  ? 18.622 6.839   15.794  0.40 25.21 ?  28  LYS   A CD   1 
ATOM   745  C  CE   A LYS   A 1 28  ? 17.990 6.933   15.508  0.60 29.21 ?  28  LYS   A CE   1 
ATOM   746  C  CE   B LYS   A 1 28  ? 17.810 7.247   14.578  0.40 26.64 ?  28  LYS   A CE   1 
ATOM   747  N  NZ   A LYS   A 1 28  ? 17.578 8.364   15.454  0.60 30.09 ?  28  LYS   A NZ   1 
ATOM   748  N  NZ   B LYS   A 1 28  ? 17.691 8.728   14.466  0.40 27.31 ?  28  LYS   A NZ   1 
ATOM   749  H  H    A LYS   A 1 28  ? 19.018 2.583   15.437  0.60 23.07 ?  28  LYS   A H    1 
ATOM   750  H  H    B LYS   A 1 28  ? 18.663 2.629   15.143  0.40 21.07 ?  28  LYS   A H    1 
ATOM   751  H  HA   A LYS   A 1 28  ? 20.573 3.158   17.441  0.60 26.36 ?  28  LYS   A HA   1 
ATOM   752  H  HA   B LYS   A 1 28  ? 20.185 3.439   17.078  0.40 24.03 ?  28  LYS   A HA   1 
ATOM   753  H  HB2  A LYS   A 1 28  ? 18.118 4.284   16.662  0.60 28.59 ?  28  LYS   A HB2  1 
ATOM   754  H  HB2  B LYS   A 1 28  ? 17.594 4.278   16.370  0.40 25.81 ?  28  LYS   A HB2  1 
ATOM   755  H  HB3  A LYS   A 1 28  ? 18.894 4.826   17.935  0.60 28.59 ?  28  LYS   A HB3  1 
ATOM   756  H  HB3  B LYS   A 1 28  ? 18.415 4.984   17.532  0.40 25.81 ?  28  LYS   A HB3  1 
ATOM   757  H  HG2  A LYS   A 1 28  ? 20.727 5.314   16.469  0.60 30.80 ?  28  LYS   A HG2  1 
ATOM   758  H  HG2  B LYS   A 1 28  ? 20.091 5.420   15.822  0.40 27.99 ?  28  LYS   A HG2  1 
ATOM   759  H  HG3  A LYS   A 1 28  ? 19.735 5.023   15.261  0.60 30.80 ?  28  LYS   A HG3  1 
ATOM   760  H  HG3  B LYS   A 1 28  ? 18.932 5.087   14.785  0.40 27.99 ?  28  LYS   A HG3  1 
ATOM   761  H  HD2  A LYS   A 1 28  ? 19.176 7.020   17.165  0.60 33.26 ?  28  LYS   A HD2  1 
ATOM   762  H  HD2  B LYS   A 1 28  ? 18.053 6.916   16.578  0.40 30.30 ?  28  LYS   A HD2  1 
ATOM   763  H  HD3  A LYS   A 1 28  ? 19.964 7.345   15.822  0.60 33.26 ?  28  LYS   A HD3  1 
ATOM   764  H  HD3  B LYS   A 1 28  ? 19.378 7.442   15.871  0.40 30.30 ?  28  LYS   A HD3  1 
ATOM   765  H  HE2  A LYS   A 1 28  ? 18.086 6.611   14.598  0.60 35.09 ?  28  LYS   A HE2  1 
ATOM   766  H  HE2  B LYS   A 1 28  ? 18.246 6.919   13.778  0.40 32.01 ?  28  LYS   A HE2  1 
ATOM   767  H  HE3  A LYS   A 1 28  ? 17.300 6.435   15.971  0.60 35.09 ?  28  LYS   A HE3  1 
ATOM   768  H  HE3  B LYS   A 1 28  ? 16.916 6.873   14.651  0.40 32.01 ?  28  LYS   A HE3  1 
ATOM   769  H  HZ1  A LYS   A 1 28  ? 16.805 8.443   15.021  0.60 36.15 ?  28  LYS   A HZ1  1 
ATOM   770  H  HZ1  B LYS   A 1 28  ? 17.213 8.941   13.747  0.40 32.82 ?  28  LYS   A HZ1  1 
ATOM   771  H  HZ2  A LYS   A 1 28  ? 17.482 8.684   16.279  0.60 36.15 ?  28  LYS   A HZ2  1 
ATOM   772  H  HZ2  B LYS   A 1 28  ? 17.291 9.057   15.189  0.40 32.82 ?  28  LYS   A HZ2  1 
ATOM   773  H  HZ3  A LYS   A 1 28  ? 18.197 8.844   15.029  0.60 36.15 ?  28  LYS   A HZ3  1 
ATOM   774  H  HZ3  B LYS   A 1 28  ? 18.501 9.092   14.393  0.40 32.82 ?  28  LYS   A HZ3  1 
ATOM   775  N  N    A LYS   A 1 29  ? 17.966 1.553   18.298  0.60 23.35 ?  29  LYS   A N    1 
ATOM   776  N  N    B LYS   A 1 29  ? 17.743 1.664   18.084  0.40 22.45 ?  29  LYS   A N    1 
ATOM   777  C  CA   A LYS   A 1 29  ? 17.346 0.850   19.418  0.60 24.77 ?  29  LYS   A CA   1 
ATOM   778  C  CA   B LYS   A 1 29  ? 17.169 1.012   19.256  0.40 24.37 ?  29  LYS   A CA   1 
ATOM   779  C  C    A LYS   A 1 29  ? 18.144 -0.391  19.807  0.60 23.81 ?  29  LYS   A C    1 
ATOM   780  C  C    B LYS   A 1 29  ? 17.976 -0.210  19.680  0.40 23.96 ?  29  LYS   A C    1 
ATOM   781  O  O    A LYS   A 1 29  ? 18.446 -0.602  20.988  0.60 24.92 ?  29  LYS   A O    1 
ATOM   782  O  O    B LYS   A 1 29  ? 18.214 -0.414  20.877  0.40 24.46 ?  29  LYS   A O    1 
ATOM   783  C  CB   A LYS   A 1 29  ? 15.911 0.459   19.055  0.60 27.64 ?  29  LYS   A CB   1 
ATOM   784  C  CB   B LYS   A 1 29  ? 15.725 0.603   18.961  0.40 26.86 ?  29  LYS   A CB   1 
ATOM   785  C  CG   A LYS   A 1 29  ? 15.153 -0.259  20.166  0.60 30.68 ?  29  LYS   A CG   1 
ATOM   786  C  CG   B LYS   A 1 29  ? 15.006 -0.066  20.125  0.40 29.32 ?  29  LYS   A CG   1 
ATOM   787  C  CD   A LYS   A 1 29  ? 14.825 0.681   21.314  0.60 33.54 ?  29  LYS   A CD   1 
ATOM   788  C  CD   B LYS   A 1 29  ? 14.694 0.927   21.231  0.40 31.55 ?  29  LYS   A CD   1 
ATOM   789  C  CE   A LYS   A 1 29  ? 13.939 0.006   22.349  0.60 35.45 ?  29  LYS   A CE   1 
ATOM   790  C  CE   B LYS   A 1 29  ? 13.831 0.296   22.312  0.40 33.11 ?  29  LYS   A CE   1 
ATOM   791  N  NZ   A LYS   A 1 29  ? 13.499 0.959   23.405  0.60 36.59 ?  29  LYS   A NZ   1 
ATOM   792  N  NZ   B LYS   A 1 29  ? 13.479 1.272   23.378  0.40 34.04 ?  29  LYS   A NZ   1 
ATOM   793  H  H    A LYS   A 1 29  ? 17.570 1.437   17.544  0.60 28.07 ?  29  LYS   A H    1 
ATOM   794  H  H    B LYS   A 1 29  ? 17.372 1.447   17.341  0.40 26.99 ?  29  LYS   A H    1 
ATOM   795  H  HA   A LYS   A 1 29  ? 17.309 1.440   20.187  0.60 29.77 ?  29  LYS   A HA   1 
ATOM   796  H  HA   B LYS   A 1 29  ? 17.160 1.636   19.996  0.40 29.28 ?  29  LYS   A HA   1 
ATOM   797  H  HB2  A LYS   A 1 29  ? 15.413 1.262   18.836  0.60 33.21 ?  29  LYS   A HB2  1 
ATOM   798  H  HB2  B LYS   A 1 29  ? 15.222 1.397   18.724  0.40 32.27 ?  29  LYS   A HB2  1 
ATOM   799  H  HB3  A LYS   A 1 29  ? 15.932 -0.132  18.287  0.60 33.21 ?  29  LYS   A HB3  1 
ATOM   800  H  HB3  B LYS   A 1 29  ? 15.724 -0.021  18.218  0.40 32.27 ?  29  LYS   A HB3  1 
ATOM   801  H  HG2  A LYS   A 1 29  ? 14.319 -0.604  19.811  0.60 36.86 ?  29  LYS   A HG2  1 
ATOM   802  H  HG2  B LYS   A 1 29  ? 14.168 -0.437  19.808  0.40 35.23 ?  29  LYS   A HG2  1 
ATOM   803  H  HG3  A LYS   A 1 29  ? 15.692 -0.988  20.513  0.60 36.86 ?  29  LYS   A HG3  1 
ATOM   804  H  HG3  B LYS   A 1 29  ? 15.562 -0.771  20.495  0.40 35.23 ?  29  LYS   A HG3  1 
ATOM   805  H  HD2  A LYS   A 1 29  ? 15.647 0.956   21.750  0.60 40.29 ?  29  LYS   A HD2  1 
ATOM   806  H  HD2  B LYS   A 1 29  ? 15.523 1.225   21.637  0.40 37.91 ?  29  LYS   A HD2  1 
ATOM   807  H  HD3  A LYS   A 1 29  ? 14.353 1.456   20.969  0.60 40.29 ?  29  LYS   A HD3  1 
ATOM   808  H  HD3  B LYS   A 1 29  ? 14.213 1.681   20.857  0.40 37.91 ?  29  LYS   A HD3  1 
ATOM   809  H  HE2  A LYS   A 1 29  ? 13.149 -0.349  21.911  0.60 42.58 ?  29  LYS   A HE2  1 
ATOM   810  H  HE2  B LYS   A 1 29  ? 13.008 -0.029  21.913  0.40 39.78 ?  29  LYS   A HE2  1 
ATOM   811  H  HE3  A LYS   A 1 29  ? 14.435 -0.711  22.775  0.60 42.58 ?  29  LYS   A HE3  1 
ATOM   812  H  HE3  B LYS   A 1 29  ? 14.317 -0.439  22.720  0.40 39.78 ?  29  LYS   A HE3  1 
ATOM   813  H  HZ1  A LYS   A 1 29  ? 12.983 0.540   23.997  0.60 43.95 ?  29  LYS   A HZ1  1 
ATOM   814  H  HZ1  B LYS   A 1 29  ? 12.975 0.877   23.996  0.40 40.89 ?  29  LYS   A HZ1  1 
ATOM   815  H  HZ2  A LYS   A 1 29  ? 14.208 1.295   23.825  0.60 43.95 ?  29  LYS   A HZ2  1 
ATOM   816  H  HZ2  B LYS   A 1 29  ? 14.219 1.581   23.763  0.40 40.89 ?  29  LYS   A HZ2  1 
ATOM   817  H  HZ3  A LYS   A 1 29  ? 13.037 1.626   23.039  0.60 43.95 ?  29  LYS   A HZ3  1 
ATOM   818  H  HZ3  B LYS   A 1 29  ? 13.027 1.954   23.029  0.40 40.89 ?  29  LYS   A HZ3  1 
ATOM   819  N  N    A VAL   A 1 30  ? 18.469 -1.235  18.827  0.60 22.48 ?  30  VAL   A N    1 
ATOM   820  N  N    B VAL   A 1 30  ? 18.391 -1.038  18.721  0.40 23.22 ?  30  VAL   A N    1 
ATOM   821  C  CA   A VAL   A 1 30  ? 19.134 -2.502  19.113  0.60 21.49 ?  30  VAL   A CA   1 
ATOM   822  C  CA   B VAL   A 1 30  ? 19.001 -2.323  19.049  0.40 22.61 ?  30  VAL   A CA   1 
ATOM   823  C  C    A VAL   A 1 30  ? 20.633 -2.319  19.333  0.60 20.17 ?  30  VAL   A C    1 
ATOM   824  C  C    B VAL   A 1 30  ? 20.497 -2.180  19.316  0.40 21.93 ?  30  VAL   A C    1 
ATOM   825  O  O    A VAL   A 1 30  ? 21.241 -3.053  20.121  0.60 20.35 ?  30  VAL   A O    1 
ATOM   826  O  O    B VAL   A 1 30  ? 21.052 -2.873  20.176  0.40 21.94 ?  30  VAL   A O    1 
ATOM   827  C  CB   A VAL   A 1 30  ? 18.850 -3.500  17.977  0.60 22.31 ?  30  VAL   A CB   1 
ATOM   828  C  CB   B VAL   A 1 30  ? 18.710 -3.340  17.930  0.40 22.85 ?  30  VAL   A CB   1 
ATOM   829  C  CG1  A VAL   A 1 30  ? 19.615 -4.801  18.196  0.60 22.79 ?  30  VAL   A CG1  1 
ATOM   830  C  CG1  B VAL   A 1 30  ? 19.429 -4.654  18.196  0.40 23.13 ?  30  VAL   A CG1  1 
ATOM   831  C  CG2  A VAL   A 1 30  ? 17.356 -3.765  17.862  0.60 22.92 ?  30  VAL   A CG2  1 
ATOM   832  C  CG2  B VAL   A 1 30  ? 17.211 -3.569  17.795  0.40 23.04 ?  30  VAL   A CG2  1 
ATOM   833  H  H    A VAL   A 1 30  ? 18.299 -1.105  17.995  0.60 27.01 ?  30  VAL   A H    1 
ATOM   834  H  H    B VAL   A 1 30  ? 18.315 -0.885  17.878  0.40 27.90 ?  30  VAL   A H    1 
ATOM   835  H  HA   A VAL   A 1 30  ? 18.753 -2.871  19.926  0.60 25.83 ?  30  VAL   A HA   1 
ATOM   836  H  HA   B VAL   A 1 30  ? 18.588 -2.660  19.858  0.40 27.17 ?  30  VAL   A HA   1 
ATOM   837  H  HB   A VAL   A 1 30  ? 19.151 -3.119  17.138  0.60 26.81 ?  30  VAL   A HB   1 
ATOM   838  H  HB   B VAL   A 1 30  ? 19.036 -2.988  17.087  0.40 27.46 ?  30  VAL   A HB   1 
ATOM   839  H  HG11 A VAL   A 1 30  ? 19.259 -5.479  17.599  0.60 27.39 ?  30  VAL   A HG11 1 
ATOM   840  H  HG11 B VAL   A 1 30  ? 19.059 -5.339  17.616  0.40 27.80 ?  30  VAL   A HG11 1 
ATOM   841  H  HG12 A VAL   A 1 30  ? 20.554 -4.655  18.006  0.60 27.39 ?  30  VAL   A HG12 1 
ATOM   842  H  HG12 B VAL   A 1 30  ? 20.375 -4.543  18.012  0.40 27.80 ?  30  VAL   A HG12 1 
ATOM   843  H  HG13 A VAL   A 1 30  ? 19.500 -5.083  19.117  0.60 27.39 ?  30  VAL   A HG13 1 
ATOM   844  H  HG13 B VAL   A 1 30  ? 19.297 -4.903  19.124  0.40 27.80 ?  30  VAL   A HG13 1 
ATOM   845  H  HG21 A VAL   A 1 30  ? 17.207 -4.440  17.180  0.60 27.54 ?  30  VAL   A HG21 1 
ATOM   846  H  HG21 B VAL   A 1 30  ? 17.054 -4.244  17.116  0.40 27.69 ?  30  VAL   A HG21 1 
ATOM   847  H  HG22 A VAL   A 1 30  ? 17.026 -4.081  18.718  0.60 27.54 ?  30  VAL   A HG22 1 
ATOM   848  H  HG22 B VAL   A 1 30  ? 16.861 -3.872  18.648  0.40 27.69 ?  30  VAL   A HG22 1 
ATOM   849  H  HG23 A VAL   A 1 30  ? 16.908 -2.942  17.617  0.60 27.54 ?  30  VAL   A HG23 1 
ATOM   850  H  HG23 B VAL   A 1 30  ? 16.786 -2.737  17.538  0.40 27.69 ?  30  VAL   A HG23 1 
ATOM   851  N  N    A LYS   A 1 31  ? 21.249 -1.356  18.656  0.60 19.07 ?  31  LYS   A N    1 
ATOM   852  N  N    B LYS   A 1 31  ? 21.170 -1.290  18.595  0.40 21.36 ?  31  LYS   A N    1 
ATOM   853  C  CA   A LYS   A 1 31  ? 22.700 -1.231  18.602  0.60 19.86 ?  31  LYS   A CA   1 
ATOM   854  C  CA   B LYS   A 1 31  ? 22.626 -1.223  18.575  0.40 21.62 ?  31  LYS   A CA   1 
ATOM   855  C  C    A LYS   A 1 31  ? 23.315 -2.587  18.247  0.60 18.23 ?  31  LYS   A C    1 
ATOM   856  C  C    B LYS   A 1 31  ? 23.215 -2.607  18.284  0.40 19.11 ?  31  LYS   A C    1 
ATOM   857  O  O    A LYS   A 1 31  ? 24.121 -3.131  19.009  0.60 19.17 ?  31  LYS   A O    1 
ATOM   858  O  O    B LYS   A 1 31  ? 23.903 -3.188  19.129  0.40 19.55 ?  31  LYS   A O    1 
ATOM   859  C  CB   A LYS   A 1 31  ? 23.276 -0.695  19.905  0.60 24.43 ?  31  LYS   A CB   1 
ATOM   860  C  CB   B LYS   A 1 31  ? 23.192 -0.644  19.864  0.40 25.03 ?  31  LYS   A CB   1 
ATOM   861  C  CG   A LYS   A 1 31  ? 22.594 0.563   20.418  0.60 29.34 ?  31  LYS   A CG   1 
ATOM   862  C  CG   B LYS   A 1 31  ? 22.555 0.672   20.277  0.40 28.63 ?  31  LYS   A CG   1 
ATOM   863  C  CD   A LYS   A 1 31  ? 23.610 1.628   20.802  0.60 33.00 ?  31  LYS   A CD   1 
ATOM   864  C  CD   B LYS   A 1 31  ? 23.573 1.614   20.899  0.40 31.43 ?  31  LYS   A CD   1 
ATOM   865  C  CE   A LYS   A 1 31  ? 22.997 2.676   21.715  0.60 35.37 ?  31  LYS   A CE   1 
ATOM   866  C  CE   B LYS   A 1 31  ? 22.901 2.665   21.766  0.40 33.29 ?  31  LYS   A CE   1 
ATOM   867  N  NZ   A LYS   A 1 31  ? 21.769 3.281   21.133  0.60 36.60 ?  31  LYS   A NZ   1 
ATOM   868  N  NZ   B LYS   A 1 31  ? 21.785 3.357   21.065  0.40 34.28 ?  31  LYS   A NZ   1 
ATOM   869  H  H    A LYS   A 1 31  ? 20.835 -0.749  18.213  0.60 22.93 ?  31  LYS   A H    1 
ATOM   870  H  H    B LYS   A 1 31  ? 20.794 -0.700  18.100  0.40 25.68 ?  31  LYS   A H    1 
ATOM   871  H  HA   A LYS   A 1 31  ? 22.926 -0.606  17.901  0.60 23.87 ?  31  LYS   A HA   1 
ATOM   872  H  HA   B LYS   A 1 31  ? 22.886 -0.627  17.859  0.40 25.99 ?  31  LYS   A HA   1 
ATOM   873  H  HB2  A LYS   A 1 31  ? 23.193 -1.377  20.587  0.60 29.36 ?  31  LYS   A HB2  1 
ATOM   874  H  HB2  B LYS   A 1 31  ? 23.051 -1.278  20.578  0.40 30.08 ?  31  LYS   A HB2  1 
ATOM   875  H  HB3  A LYS   A 1 31  ? 24.214 -0.485  19.764  0.60 29.36 ?  31  LYS   A HB3  1 
ATOM   876  H  HB3  B LYS   A 1 31  ? 24.144 -0.486  19.745  0.40 30.08 ?  31  LYS   A HB3  1 
ATOM   877  H  HG2  A LYS   A 1 31  ? 22.022 0.925   19.723  0.60 35.25 ?  31  LYS   A HG2  1 
ATOM   878  H  HG2  B LYS   A 1 31  ? 22.178 1.106   19.495  0.40 34.40 ?  31  LYS   A HG2  1 
ATOM   879  H  HG3  A LYS   A 1 31  ? 22.070 0.345   21.205  0.60 35.25 ?  31  LYS   A HG3  1 
ATOM   880  H  HG3  B LYS   A 1 31  ? 21.861 0.500   20.933  0.40 34.40 ?  31  LYS   A HG3  1 
ATOM   881  H  HD2  A LYS   A 1 31  ? 24.351 1.213   21.271  0.60 39.64 ?  31  LYS   A HD2  1 
ATOM   882  H  HD2  B LYS   A 1 31  ? 24.183 1.105   21.455  0.40 37.76 ?  31  LYS   A HD2  1 
ATOM   883  H  HD3  A LYS   A 1 31  ? 23.928 2.073   19.999  0.60 39.64 ?  31  LYS   A HD3  1 
ATOM   884  H  HD3  B LYS   A 1 31  ? 24.062 2.068   20.193  0.40 37.76 ?  31  LYS   A HD3  1 
ATOM   885  H  HE2  A LYS   A 1 31  ? 22.758 2.261   22.558  0.60 42.48 ?  31  LYS   A HE2  1 
ATOM   886  H  HE2  B LYS   A 1 31  ? 22.540 2.237   22.558  0.40 39.98 ?  31  LYS   A HE2  1 
ATOM   887  H  HE3  A LYS   A 1 31  ? 23.642 3.385   21.863  0.60 42.48 ?  31  LYS   A HE3  1 
ATOM   888  H  HE3  B LYS   A 1 31  ? 23.557 3.333   22.019  0.40 39.98 ?  31  LYS   A HE3  1 
ATOM   889  H  HZ1  A LYS   A 1 31  ? 21.454 3.912   21.676  0.60 43.96 ?  31  LYS   A HZ1  1 
ATOM   890  H  HZ1  B LYS   A 1 31  ? 21.449 3.996   21.585  0.40 41.18 ?  31  LYS   A HZ1  1 
ATOM   891  H  HZ2  A LYS   A 1 31  ? 21.955 3.646   20.343  0.60 43.96 ?  31  LYS   A HZ2  1 
ATOM   892  H  HZ2  B LYS   A 1 31  ? 22.080 3.724   20.310  0.40 41.18 ?  31  LYS   A HZ2  1 
ATOM   893  H  HZ3  A LYS   A 1 31  ? 21.145 2.657   21.023  0.60 43.96 ?  31  LYS   A HZ3  1 
ATOM   894  H  HZ3  B LYS   A 1 31  ? 21.140 2.775   20.870  0.40 41.18 ?  31  LYS   A HZ3  1 
ATOM   895  N  N    . PRO   A 1 32  ? 22.953 -3.155  17.101  1.00 16.84 ?  32  PRO   A N    1 
ATOM   896  C  CA   . PRO   A 1 32  ? 23.421 -4.501  16.780  1.00 16.17 ?  32  PRO   A CA   1 
ATOM   897  C  C    . PRO   A 1 32  ? 24.921 -4.525  16.572  1.00 16.01 ?  32  PRO   A C    1 
ATOM   898  O  O    . PRO   A 1 32  ? 25.573 -3.497  16.374  1.00 16.14 ?  32  PRO   A O    1 
ATOM   899  C  CB   . PRO   A 1 32  ? 22.698 -4.806  15.465  1.00 16.32 ?  32  PRO   A CB   1 
ATOM   900  C  CG   . PRO   A 1 32  ? 22.560 -3.455  14.820  1.00 15.35 ?  32  PRO   A CG   1 
ATOM   901  C  CD   . PRO   A 1 32  ? 22.240 -2.540  15.971  1.00 15.58 ?  32  PRO   A CD   1 
ATOM   902  H  HA   . PRO   A 1 32  ? 23.163 -5.136  17.465  1.00 19.45 ?  32  PRO   A HA   1 
ATOM   903  H  HB2  . PRO   A 1 32  ? 23.237 -5.404  14.922  1.00 19.63 ?  32  PRO   A HB2  1 
ATOM   904  H  HB3  . PRO   A 1 32  ? 21.827 -5.197  15.650  1.00 19.63 ?  32  PRO   A HB3  1 
ATOM   905  H  HG2  . PRO   A 1 32  ? 23.396 -3.214  14.394  1.00 18.46 ?  32  PRO   A HG2  1 
ATOM   906  H  HG3  . PRO   A 1 32  ? 21.835 -3.479  14.174  1.00 18.46 ?  32  PRO   A HG3  1 
ATOM   907  H  HD2  . PRO   A 1 32  ? 22.586 -1.654  15.781  1.00 18.74 ?  32  PRO   A HD2  1 
ATOM   908  H  HD3  . PRO   A 1 32  ? 21.288 -2.529  16.127  1.00 18.74 ?  32  PRO   A HD3  1 
ATOM   909  N  N    A THR   A 1 33  ? 25.470 -5.736  16.607  0.60 15.84 ?  33  THR   A N    1 
ATOM   910  N  N    B THR   A 1 33  ? 25.469 -5.738  16.601  0.40 15.79 ?  33  THR   A N    1 
ATOM   911  C  CA   A THR   A 1 33  ? 26.883 -5.902  16.297  0.60 16.06 ?  33  THR   A CA   1 
ATOM   912  C  CA   B THR   A 1 33  ? 26.884 -5.908  16.297  0.40 15.87 ?  33  THR   A CA   1 
ATOM   913  C  C    A THR   A 1 33  ? 27.187 -5.449  14.875  0.60 14.70 ?  33  THR   A C    1 
ATOM   914  C  C    B THR   A 1 33  ? 27.194 -5.463  14.873  0.40 14.55 ?  33  THR   A C    1 
ATOM   915  O  O    A THR   A 1 33  ? 28.214 -4.802  14.628  0.60 14.98 ?  33  THR   A O    1 
ATOM   916  O  O    B THR   A 1 33  ? 28.235 -4.843  14.622  0.40 14.76 ?  33  THR   A O    1 
ATOM   917  C  CB   A THR   A 1 33  ? 27.287 -7.360  16.503  0.60 17.69 ?  33  THR   A CB   1 
ATOM   918  C  CB   B THR   A 1 33  ? 27.282 -7.369  16.500  0.40 17.27 ?  33  THR   A CB   1 
ATOM   919  O  OG1  A THR   A 1 33  ? 27.028 -7.738  17.860  0.60 19.29 ?  33  THR   A OG1  1 
ATOM   920  O  OG1  B THR   A 1 33  ? 26.930 -7.780  17.826  0.40 18.46 ?  33  THR   A OG1  1 
ATOM   921  C  CG2  A THR   A 1 33  ? 28.763 -7.557  16.208  0.60 18.24 ?  33  THR   A CG2  1 
ATOM   922  C  CG2  B THR   A 1 33  ? 28.779 -7.550  16.298  0.40 17.74 ?  33  THR   A CG2  1 
ATOM   923  H  H    A THR   A 1 33  ? 25.052 -6.461  16.804  0.60 19.05 ?  33  THR   A H    1 
ATOM   924  H  H    B THR   A 1 33  ? 25.051 -6.463  16.794  0.40 18.99 ?  33  THR   A H    1 
ATOM   925  H  HA   A THR   A 1 33  ? 27.406 -5.359  16.906  0.60 19.32 ?  33  THR   A HA   1 
ATOM   926  H  HA   B THR   A 1 33  ? 27.407 -5.365  16.907  0.40 19.09 ?  33  THR   A HA   1 
ATOM   927  H  HB   A THR   A 1 33  ? 26.772 -7.931  15.909  0.60 21.28 ?  33  THR   A HB   1 
ATOM   928  H  HB   B THR   A 1 33  ? 26.814 -7.926  15.857  0.40 20.77 ?  33  THR   A HB   1 
ATOM   929  H  HG1  A THR   A 1 33  ? 27.470 -7.256  18.388  0.60 23.19 ?  33  THR   A HG1  1 
ATOM   930  H  HG1  B THR   A 1 33  ? 27.334 -7.306  18.392  0.40 22.20 ?  33  THR   A HG1  1 
ATOM   931  H  HG21 A THR   A 1 33  ? 29.051 -8.428  16.524  0.60 21.93 ?  33  THR   A HG21 1 
ATOM   932  H  HG21 B THR   A 1 33  ? 29.045 -8.440  16.576  0.40 21.33 ?  33  THR   A HG21 1 
ATOM   933  H  HG22 A THR   A 1 33  ? 28.922 -7.500  15.254  0.60 21.93 ?  33  THR   A HG22 1 
ATOM   934  H  HG22 B THR   A 1 33  ? 29.006 -7.432  15.362  0.40 21.33 ?  33  THR   A HG22 1 
ATOM   935  H  HG23 A THR   A 1 33  ? 29.282 -6.873  16.658  0.60 21.93 ?  33  THR   A HG23 1 
ATOM   936  H  HG23 B THR   A 1 33  ? 29.265 -6.897  16.826  0.40 21.33 ?  33  THR   A HG23 1 
ATOM   937  N  N    . VAL   A 1 34  ? 26.306 -5.772  13.929  1.00 13.40 ?  34  VAL   A N    1 
ATOM   938  C  CA   . VAL   A 1 34  ? 26.504 -5.439  12.521  1.00 11.96 ?  34  VAL   A CA   1 
ATOM   939  C  C    . VAL   A 1 34  ? 25.208 -4.881  11.948  1.00 11.10 ?  34  VAL   A C    1 
ATOM   940  O  O    . VAL   A 1 34  ? 24.170 -5.554  11.988  1.00 12.01 ?  34  VAL   A O    1 
ATOM   941  C  CB   . VAL   A 1 34  ? 26.957 -6.648  11.679  1.00 12.46 ?  34  VAL   A CB   1 
ATOM   942  C  CG1  . VAL   A 1 34  ? 27.145 -6.240  10.223  1.00 12.58 ?  34  VAL   A CG1  1 
ATOM   943  C  CG2  . VAL   A 1 34  ? 28.237 -7.264  12.237  1.00 13.94 ?  34  VAL   A CG2  1 
ATOM   944  H  H    A VAL   A 1 34  ? 25.569 -6.191  14.083  0.60 16.12 ?  34  VAL   A H    1 
ATOM   945  H  H    B VAL   A 1 34  ? 25.566 -6.186  14.084  0.40 16.12 ?  34  VAL   A H    1 
ATOM   946  H  HA   . VAL   A 1 34  ? 27.183 -4.748  12.447  1.00 14.40 ?  34  VAL   A HA   1 
ATOM   947  H  HB   . VAL   A 1 34  ? 26.262 -7.323  11.713  1.00 14.99 ?  34  VAL   A HB   1 
ATOM   948  H  HG11 . VAL   A 1 34  ? 27.643 -6.935  9.768   1.00 15.14 ?  34  VAL   A HG11 1 
ATOM   949  H  HG12 . VAL   A 1 34  ? 26.277 -6.127  9.810   1.00 15.14 ?  34  VAL   A HG12 1 
ATOM   950  H  HG13 . VAL   A 1 34  ? 27.641 -5.405  10.193  1.00 15.14 ?  34  VAL   A HG13 1 
ATOM   951  H  HG21 . VAL   A 1 34  ? 28.517 -7.990  11.657  1.00 16.78 ?  34  VAL   A HG21 1 
ATOM   952  H  HG22 . VAL   A 1 34  ? 28.928 -6.585  12.274  1.00 16.78 ?  34  VAL   A HG22 1 
ATOM   953  H  HG23 . VAL   A 1 34  ? 28.063 -7.606  13.130  1.00 16.78 ?  34  VAL   A HG23 1 
ATOM   954  N  N    . VAL   A 1 35  ? 25.277 -3.672  11.387  1.00 10.68 ?  35  VAL   A N    1 
ATOM   955  C  CA   . VAL   A 1 35  ? 24.253 -3.162  10.488  1.00 10.13 ?  35  VAL   A CA   1 
ATOM   956  C  C    . VAL   A 1 35  ? 24.814 -3.177  9.074   1.00 9.80  ?  35  VAL   A C    1 
ATOM   957  O  O    . VAL   A 1 35  ? 25.961 -2.773  8.844   1.00 10.43 ?  35  VAL   A O    1 
ATOM   958  C  CB   . VAL   A 1 35  ? 23.725 -1.765  10.888  1.00 10.84 ?  35  VAL   A CB   1 
ATOM   959  C  CG1  . VAL   A 1 35  ? 24.801 -0.662  10.758  1.00 11.56 ?  35  VAL   A CG1  1 
ATOM   960  C  CG2  . VAL   A 1 35  ? 22.486 -1.415  10.067  1.00 11.56 ?  35  VAL   A CG2  1 
ATOM   961  H  H    . VAL   A 1 35  ? 25.924 -3.121  11.512  1.00 12.85 ?  35  VAL   A H    1 
ATOM   962  H  HA   . VAL   A 1 35  ? 23.494 -3.770  10.508  1.00 12.20 ?  35  VAL   A HA   1 
ATOM   963  H  HB   . VAL   A 1 35  ? 23.445 -1.794  11.813  1.00 13.06 ?  35  VAL   A HB   1 
ATOM   964  H  HG11 . VAL   A 1 35  ? 24.445 0.173   11.107  1.00 13.91 ?  35  VAL   A HG11 1 
ATOM   965  H  HG12 . VAL   A 1 35  ? 25.582 -0.925  11.267  1.00 13.91 ?  35  VAL   A HG12 1 
ATOM   966  H  HG13 . VAL   A 1 35  ? 25.037 -0.551  9.822   1.00 13.91 ?  35  VAL   A HG13 1 
ATOM   967  H  HG21 . VAL   A 1 35  ? 22.134 -0.564  10.366  1.00 13.92 ?  35  VAL   A HG21 1 
ATOM   968  H  HG22 . VAL   A 1 35  ? 22.734 -1.356  9.126   1.00 13.92 ?  35  VAL   A HG22 1 
ATOM   969  H  HG23 . VAL   A 1 35  ? 21.819 -2.110  10.185  1.00 13.92 ?  35  VAL   A HG23 1 
ATOM   970  N  N    . VAL   A 1 36  ? 23.997 -3.631  8.123   1.00 9.44  ?  36  VAL   A N    1 
ATOM   971  C  CA   . VAL   A 1 36  ? 24.376 -3.644  6.719   1.00 9.04  ?  36  VAL   A CA   1 
ATOM   972  C  C    . VAL   A 1 36  ? 23.918 -2.352  6.054   1.00 9.31  ?  36  VAL   A C    1 
ATOM   973  O  O    . VAL   A 1 36  ? 22.752 -1.952  6.183   1.00 10.03 ?  36  VAL   A O    1 
ATOM   974  C  CB   . VAL   A 1 36  ? 23.771 -4.860  5.999   1.00 9.14  ?  36  VAL   A CB   1 
ATOM   975  C  CG1  . VAL   A 1 36  ? 24.033 -4.792  4.518   1.00 9.93  ?  36  VAL   A CG1  1 
ATOM   976  C  CG2  . VAL   A 1 36  ? 24.305 -6.157  6.591   1.00 10.03 ?  36  VAL   A CG2  1 
ATOM   977  H  H    . VAL   A 1 36  ? 23.204 -3.944  8.274   1.00 11.37 ?  36  VAL   A H    1 
ATOM   978  H  HA   . VAL   A 1 36  ? 25.344 -3.703  6.652   1.00 10.89 ?  36  VAL   A HA   1 
ATOM   979  H  HB   . VAL   A 1 36  ? 22.811 -4.849  6.129   1.00 11.01 ?  36  VAL   A HB   1 
ATOM   980  H  HG11 . VAL   A 1 36  ? 23.893 -5.668  4.133   1.00 11.96 ?  36  VAL   A HG11 1 
ATOM   981  H  HG12 . VAL   A 1 36  ? 23.420 -4.153  4.116   1.00 11.96 ?  36  VAL   A HG12 1 
ATOM   982  H  HG13 . VAL   A 1 36  ? 24.949 -4.507  4.372   1.00 11.96 ?  36  VAL   A HG13 1 
ATOM   983  H  HG21 . VAL   A 1 36  ? 23.916 -6.908  6.111   1.00 12.08 ?  36  VAL   A HG21 1 
ATOM   984  H  HG22 . VAL   A 1 36  ? 25.270 -6.174  6.503   1.00 12.08 ?  36  VAL   A HG22 1 
ATOM   985  H  HG23 . VAL   A 1 36  ? 24.057 -6.205  7.529   1.00 12.08 ?  36  VAL   A HG23 1 
ATOM   986  N  N    . ASN   A 1 37  ? 24.837 -1.717  5.322   1.00 9.01  ?  37  ASN   A N    1 
ATOM   987  C  CA   . ASN   A 1 37  ? 24.507 -0.599  4.453   1.00 8.67  ?  37  ASN   A CA   1 
ATOM   988  C  C    . ASN   A 1 37  ? 24.369 -1.074  3.017   1.00 8.56  ?  37  ASN   A C    1 
ATOM   989  O  O    . ASN   A 1 37  ? 25.153 -1.907  2.544   1.00 9.49  ?  37  ASN   A O    1 
ATOM   990  C  CB   . ASN   A 1 37  ? 25.585 0.478   4.531   1.00 9.05  ?  37  ASN   A CB   1 
ATOM   991  C  CG   . ASN   A 1 37  ? 25.265 1.677   3.677   1.00 9.27  ?  37  ASN   A CG   1 
ATOM   992  O  OD1  . ASN   A 1 37  ? 24.090 2.014   3.492   1.00 10.01 ?  37  ASN   A OD1  1 
ATOM   993  N  ND2  . ASN   A 1 37  ? 26.296 2.328   3.157   1.00 9.62  ?  37  ASN   A ND2  1 
ATOM   994  H  H    . ASN   A 1 37  ? 25.675 -1.923  5.319   1.00 10.86 ?  37  ASN   A H    1 
ATOM   995  H  HA   . ASN   A 1 37  ? 23.668 -0.212  4.736   1.00 10.45 ?  37  ASN   A HA   1 
ATOM   996  H  HB2  . ASN   A 1 37  ? 25.669 0.775   5.453   1.00 10.91 ?  37  ASN   A HB2  1 
ATOM   997  H  HB3  . ASN   A 1 37  ? 26.431 0.103   4.229   1.00 10.91 ?  37  ASN   A HB3  1 
ATOM   998  H  HD21 . ASN   A 1 37  ? 26.157 3.018   2.661   1.00 11.59 ?  37  ASN   A HD21 1 
ATOM   999  H  HD22 . ASN   A 1 37  ? 27.091 2.067   3.309   1.00 11.59 ?  37  ASN   A HD22 1 
ATOM   1000 N  N    A ALA   A 1 38  ? 23.345 -0.542  2.342   0.60 8.98  ?  38  ALA   A N    1 
ATOM   1001 N  N    B ALA   A 1 38  ? 23.358 -0.547  2.320   0.40 9.09  ?  38  ALA   A N    1 
ATOM   1002 C  CA   A ALA   A 1 38  ? 23.157 -0.679  0.899   0.60 9.31  ?  38  ALA   A CA   1 
ATOM   1003 C  CA   B ALA   A 1 38  ? 23.196 -0.783  0.883   0.40 9.63  ?  38  ALA   A CA   1 
ATOM   1004 C  C    A ALA   A 1 38  ? 24.077 0.323   0.203   0.60 9.31  ?  38  ALA   A C    1 
ATOM   1005 C  C    B ALA   A 1 38  ? 24.048 0.235   0.123   0.40 9.37  ?  38  ALA   A C    1 
ATOM   1006 O  O    A ALA   A 1 38  ? 23.679 1.431   -0.172  0.60 9.19  ?  38  ALA   A O    1 
ATOM   1007 O  O    B ALA   A 1 38  ? 23.571 1.256   -0.384  0.40 9.37  ?  38  ALA   A O    1 
ATOM   1008 C  CB   A ALA   A 1 38  ? 21.697 -0.427  0.542   0.60 10.38 ?  38  ALA   A CB   1 
ATOM   1009 C  CB   B ALA   A 1 38  ? 21.727 -0.715  0.488   0.40 10.78 ?  38  ALA   A CB   1 
ATOM   1010 H  H    A ALA   A 1 38  ? 22.739 -0.061  2.719   0.60 10.81 ?  38  ALA   A H    1 
ATOM   1011 H  H    B ALA   A 1 38  ? 22.752 -0.042  2.665   0.40 10.95 ?  38  ALA   A H    1 
ATOM   1012 H  HA   A ALA   A 1 38  ? 23.399 -1.572  0.622   0.60 11.21 ?  38  ALA   A HA   1 
ATOM   1013 H  HA   B ALA   A 1 38  ? 23.524 -1.673  0.674   0.40 11.60 ?  38  ALA   A HA   1 
ATOM   1014 H  HB1  A ALA   A 1 38  ? 21.582 -0.524  -0.415  0.60 12.50 ?  38  ALA   A HB1  1 
ATOM   1015 H  HB1  B ALA   A 1 38  ? 21.654 -0.857  -0.467  0.40 12.98 ?  38  ALA   A HB1  1 
ATOM   1016 H  HB2  A ALA   A 1 38  ? 21.141 -1.073  1.010   0.60 12.50 ?  38  ALA   A HB2  1 
ATOM   1017 H  HB2  B ALA   A 1 38  ? 21.235 -1.404  0.964   0.40 12.98 ?  38  ALA   A HB2  1 
ATOM   1018 H  HB3  A ALA   A 1 38  ? 21.452 0.473   0.815   0.60 12.50 ?  38  ALA   A HB3  1 
ATOM   1019 H  HB3  B ALA   A 1 38  ? 21.379 0.159   0.720   0.40 12.98 ?  38  ALA   A HB3  1 
ATOM   1020 N  N    . ALA   A 1 39  ? 25.339 -0.072  0.040   1.00 9.44  ?  39  ALA   A N    1 
ATOM   1021 C  CA   . ALA   A 1 39  ? 26.366 0.825   -0.462  1.00 9.65  ?  39  ALA   A CA   1 
ATOM   1022 C  C    . ALA   A 1 39  ? 26.494 0.763   -1.978  1.00 9.70  ?  39  ALA   A C    1 
ATOM   1023 O  O    . ALA   A 1 39  ? 26.020 -0.166  -2.633  1.00 9.95  ?  39  ALA   A O    1 
ATOM   1024 C  CB   . ALA   A 1 39  ? 27.708 0.445   0.170   1.00 10.72 ?  39  ALA   A CB   1 
ATOM   1025 H  H    A ALA   A 1 39  ? 25.620 -0.868  0.222   0.60 11.37 ?  39  ALA   A H    1 
ATOM   1026 H  H    B ALA   A 1 39  ? 25.651 -0.841  0.278   0.40 11.37 ?  39  ALA   A H    1 
ATOM   1027 H  HA   . ALA   A 1 39  ? 26.147 1.736   -0.205  1.00 11.62 ?  39  ALA   A HA   1 
ATOM   1028 H  HB1  . ALA   A 1 39  ? 28.388 1.050   -0.161  1.00 12.90 ?  39  ALA   A HB1  1 
ATOM   1029 H  HB2  . ALA   A 1 39  ? 27.634 0.531   1.137   1.00 12.90 ?  39  ALA   A HB2  1 
ATOM   1030 H  HB3  . ALA   A 1 39  ? 27.920 -0.466  -0.067  1.00 12.90 ?  39  ALA   A HB3  1 
ATOM   1031 N  N    A ASN   A 1 40  ? 27.220 1.748   -2.516  0.60 10.00 ?  40  ASN   A N    1 
ATOM   1032 N  N    B ASN   A 1 40  ? 27.087 1.805   -2.550  0.40 9.62  ?  40  ASN   A N    1 
ATOM   1033 C  CA   A ASN   A 1 40  ? 27.792 1.703   -3.856  0.60 9.73  ?  40  ASN   A CA   1 
ATOM   1034 C  CA   B ASN   A 1 40  ? 27.537 1.758   -3.934  0.40 9.75  ?  40  ASN   A CA   1 
ATOM   1035 C  C    A ASN   A 1 40  ? 29.315 1.592   -3.765  0.60 8.93  ?  40  ASN   A C    1 
ATOM   1036 C  C    B ASN   A 1 40  ? 29.060 1.653   -3.952  0.40 9.38  ?  40  ASN   A C    1 
ATOM   1037 O  O    A ASN   A 1 40  ? 29.899 1.680   -2.684  0.60 9.11  ?  40  ASN   A O    1 
ATOM   1038 O  O    B ASN   A 1 40  ? 29.720 1.773   -2.919  0.40 9.53  ?  40  ASN   A O    1 
ATOM   1039 C  CB   A ASN   A 1 40  ? 27.337 2.887   -4.727  0.60 10.10 ?  40  ASN   A CB   1 
ATOM   1040 C  CB   B ASN   A 1 40  ? 27.029 2.964   -4.738  0.40 10.52 ?  40  ASN   A CB   1 
ATOM   1041 C  CG   A ASN   A 1 40  ? 27.690 4.240   -4.137  0.60 11.18 ?  40  ASN   A CG   1 
ATOM   1042 C  CG   B ASN   A 1 40  ? 27.454 4.288   -4.146  0.40 11.22 ?  40  ASN   A CG   1 
ATOM   1043 O  OD1  A ASN   A 1 40  ? 28.842 4.487   -3.767  0.60 11.78 ?  40  ASN   A OD1  1 
ATOM   1044 O  OD1  B ASN   A 1 40  ? 28.647 4.576   -4.029  0.40 11.87 ?  40  ASN   A OD1  1 
ATOM   1045 N  ND2  A ASN   A 1 40  ? 26.693 5.129   -4.056  0.60 12.19 ?  40  ASN   A ND2  1 
ATOM   1046 N  ND2  B ASN   A 1 40  ? 26.474 5.117   -3.790  0.40 11.70 ?  40  ASN   A ND2  1 
ATOM   1047 H  H    A ASN   A 1 40  ? 27.416 2.467   -2.094  0.60 12.04 ?  40  ASN   A H    1 
ATOM   1048 H  H    B ASN   A 1 40  ? 27.233 2.553   -2.156  0.40 11.59 ?  40  ASN   A H    1 
ATOM   1049 H  HA   A ASN   A 1 40  ? 27.490 0.895   -4.289  0.60 11.72 ?  40  ASN   A HA   1 
ATOM   1050 H  HA   B ASN   A 1 40  ? 27.171 0.952   -4.351  0.40 11.74 ?  40  ASN   A HA   1 
ATOM   1051 H  HB2  A ASN   A 1 40  ? 27.760 2.815   -5.600  0.60 12.16 ?  40  ASN   A HB2  1 
ATOM   1052 H  HB2  B ASN   A 1 40  ? 27.381 2.906   -5.637  0.40 12.66 ?  40  ASN   A HB2  1 
ATOM   1053 H  HB3  A ASN   A 1 40  ? 26.376 2.846   -4.824  0.60 12.16 ?  40  ASN   A HB3  1 
ATOM   1054 H  HB3  B ASN   A 1 40  ? 26.056 2.938   -4.761  0.40 12.66 ?  40  ASN   A HB3  1 
ATOM   1055 H  HD21 A ASN   A 1 40  ? 26.840 5.918   -3.740  0.60 14.67 ?  40  ASN   A HD21 1 
ATOM   1056 H  HD21 B ASN   A 1 40  ? 26.665 5.883   -3.449  0.40 14.08 ?  40  ASN   A HD21 1 
ATOM   1057 H  HD22 A ASN   A 1 40  ? 25.903 4.913   -4.316  0.60 14.67 ?  40  ASN   A HD22 1 
ATOM   1058 H  HD22 B ASN   A 1 40  ? 25.653 4.887   -3.900  0.40 14.08 ?  40  ASN   A HD22 1 
ATOM   1059 N  N    A VAL   A 1 41  ? 29.954 1.354   -4.916  0.60 8.80  ?  41  VAL   A N    1 
ATOM   1060 N  N    B VAL   A 1 41  ? 29.621 1.397   -5.135  0.40 9.86  ?  41  VAL   A N    1 
ATOM   1061 C  CA   A VAL   A 1 41  ? 31.383 1.037   -4.932  0.60 9.43  ?  41  VAL   A CA   1 
ATOM   1062 C  CA   B VAL   A 1 41  ? 31.050 1.095   -5.218  0.40 10.07 ?  41  VAL   A CA   1 
ATOM   1063 C  C    A VAL   A 1 41  ? 32.229 2.197   -4.439  0.60 9.41  ?  41  VAL   A C    1 
ATOM   1064 C  C    B VAL   A 1 41  ? 31.932 2.239   -4.729  0.40 10.02 ?  41  VAL   A C    1 
ATOM   1065 O  O    A VAL   A 1 41  ? 33.353 1.986   -3.965  0.60 9.65  ?  41  VAL   A O    1 
ATOM   1066 O  O    B VAL   A 1 41  ? 33.103 2.008   -4.403  0.40 9.85  ?  41  VAL   A O    1 
ATOM   1067 C  CB   A VAL   A 1 41  ? 31.869 0.543   -6.314  0.60 9.70  ?  41  VAL   A CB   1 
ATOM   1068 C  CB   B VAL   A 1 41  ? 31.472 0.655   -6.639  0.40 10.97 ?  41  VAL   A CB   1 
ATOM   1069 C  CG1  A VAL   A 1 41  ? 31.165 -0.747  -6.715  0.60 10.44 ?  41  VAL   A CG1  1 
ATOM   1070 C  CG1  B VAL   A 1 41  ? 30.814 -0.668  -7.012  0.40 11.80 ?  41  VAL   A CG1  1 
ATOM   1071 C  CG2  A VAL   A 1 41  ? 31.736 1.622   -7.396  0.60 9.71  ?  41  VAL   A CG2  1 
ATOM   1072 C  CG2  B VAL   A 1 41  ? 31.155 1.735   -7.670  0.40 11.25 ?  41  VAL   A CG2  1 
ATOM   1073 H  H    A VAL   A 1 41  ? 29.590 1.364   -5.690  0.60 10.60 ?  41  VAL   A H    1 
ATOM   1074 H  H    B VAL   A 1 41  ? 29.198 1.385   -5.884  0.40 11.88 ?  41  VAL   A H    1 
ATOM   1075 H  HA   A VAL   A 1 41  ? 31.543 0.316   -4.312  0.60 11.36 ?  41  VAL   A HA   1 
ATOM   1076 H  HA   B VAL   A 1 41  ? 31.217 0.342   -4.631  0.40 12.12 ?  41  VAL   A HA   1 
ATOM   1077 H  HB   A VAL   A 1 41  ? 32.817 0.334   -6.248  0.60 11.68 ?  41  VAL   A HB   1 
ATOM   1078 H  HB   B VAL   A 1 41  ? 32.432 0.515   -6.639  0.40 13.21 ?  41  VAL   A HB   1 
ATOM   1079 H  HG11 A VAL   A 1 41  ? 31.497 -1.044  -7.579  0.60 12.57 ?  41  VAL   A HG11 1 
ATOM   1080 H  HG11 B VAL   A 1 41  ? 31.066 -0.900  -7.919  0.40 14.20 ?  41  VAL   A HG11 1 
ATOM   1081 H  HG12 A VAL   A 1 41  ? 31.340 -1.427  -6.045  0.60 12.57 ?  41  VAL   A HG12 1 
ATOM   1082 H  HG12 B VAL   A 1 41  ? 31.118 -1.358  -6.399  0.40 14.20 ?  41  VAL   A HG12 1 
ATOM   1083 H  HG13 A VAL   A 1 41  ? 30.208 -0.582  -6.773  0.60 12.57 ?  41  VAL   A HG13 1 
ATOM   1084 H  HG13 B VAL   A 1 41  ? 29.852 -0.575  -6.950  0.40 14.20 ?  41  VAL   A HG13 1 
ATOM   1085 H  HG21 A VAL   A 1 41  ? 31.961 1.233   -8.260  0.60 11.70 ?  41  VAL   A HG21 1 
ATOM   1086 H  HG21 B VAL   A 1 41  ? 31.442 1.425   -8.544  0.40 13.54 ?  41  VAL   A HG21 1 
ATOM   1087 H  HG22 A VAL   A 1 41  ? 30.829 1.949   -7.405  0.60 11.70 ?  41  VAL   A HG22 1 
ATOM   1088 H  HG22 B VAL   A 1 41  ? 30.198 1.895   -7.676  0.40 13.54 ?  41  VAL   A HG22 1 
ATOM   1089 H  HG23 A VAL   A 1 41  ? 32.353 2.345   -7.196  0.60 11.70 ?  41  VAL   A HG23 1 
ATOM   1090 H  HG23 B VAL   A 1 41  ? 31.627 2.547   -7.434  0.40 13.54 ?  41  VAL   A HG23 1 
ATOM   1091 N  N    A TYR   A 1 42  ? 31.739 3.429   -4.578  0.60 10.07 ?  42  TYR   A N    1 
ATOM   1092 N  N    B TYR   A 1 42  ? 31.415 3.471   -4.690  0.40 10.24 ?  42  TYR   A N    1 
ATOM   1093 C  CA   A TYR   A 1 42  ? 32.459 4.620   -4.150  0.60 10.17 ?  42  TYR   A CA   1 
ATOM   1094 C  CA   B TYR   A 1 42  ? 32.202 4.634   -4.290  0.40 10.15 ?  42  TYR   A CA   1 
ATOM   1095 C  C    A TYR   A 1 42  ? 32.152 4.985   -2.711  0.60 10.13 ?  42  TYR   A C    1 
ATOM   1096 C  C    B TYR   A 1 42  ? 32.008 5.030   -2.832  0.40 10.15 ?  42  TYR   A C    1 
ATOM   1097 O  O    A TYR   A 1 42  ? 32.729 5.950   -2.189  0.60 10.67 ?  42  TYR   A O    1 
ATOM   1098 O  O    B TYR   A 1 42  ? 32.558 6.052   -2.405  0.40 10.69 ?  42  TYR   A O    1 
ATOM   1099 C  CB   A TYR   A 1 42  ? 32.124 5.806   -5.075  0.60 11.00 ?  42  TYR   A CB   1 
ATOM   1100 C  CB   B TYR   A 1 42  ? 31.876 5.833   -5.191  0.40 10.62 ?  42  TYR   A CB   1 
ATOM   1101 C  CG   A TYR   A 1 42  ? 32.314 5.480   -6.542  0.60 11.54 ?  42  TYR   A CG   1 
ATOM   1102 C  CG   B TYR   A 1 42  ? 32.054 5.540   -6.661  0.40 11.50 ?  42  TYR   A CG   1 
ATOM   1103 C  CD1  A TYR   A 1 42  ? 33.581 5.269   -7.065  0.60 12.42 ?  42  TYR   A CD1  1 
ATOM   1104 C  CD1  B TYR   A 1 42  ? 33.315 5.340   -7.201  0.40 11.76 ?  42  TYR   A CD1  1 
ATOM   1105 C  CD2  A TYR   A 1 42  ? 31.230 5.353   -7.399  0.60 12.54 ?  42  TYR   A CD2  1 
ATOM   1106 C  CD2  B TYR   A 1 42  ? 30.959 5.456   -7.509  0.40 12.91 ?  42  TYR   A CD2  1 
ATOM   1107 C  CE1  A TYR   A 1 42  ? 33.763 4.951   -8.403  0.60 13.05 ?  42  TYR   A CE1  1 
ATOM   1108 C  CE1  B TYR   A 1 42  ? 33.479 5.065   -8.544  0.40 12.29 ?  42  TYR   A CE1  1 
ATOM   1109 C  CE2  A TYR   A 1 42  ? 31.405 5.040   -8.741  0.60 13.71 ?  42  TYR   A CE2  1 
ATOM   1110 C  CE2  B TYR   A 1 42  ? 31.113 5.189   -8.853  0.40 13.77 ?  42  TYR   A CE2  1 
ATOM   1111 C  CZ   A TYR   A 1 42  ? 32.676 4.840   -9.234  0.60 13.38 ?  42  TYR   A CZ   1 
ATOM   1112 C  CZ   B TYR   A 1 42  ? 32.375 4.990   -9.366  0.40 13.34 ?  42  TYR   A CZ   1 
ATOM   1113 O  OH   A TYR   A 1 42  ? 32.858 4.523   -10.560 0.60 14.65 ?  42  TYR   A OH   1 
ATOM   1114 O  OH   B TYR   A 1 42  ? 32.531 4.723   -10.706 0.40 14.36 ?  42  TYR   A OH   1 
ATOM   1115 H  H    A TYR   A 1 42  ? 30.972 3.601   -4.914  0.60 12.13 ?  42  TYR   A H    1 
ATOM   1116 H  H    B TYR   A 1 42  ? 30.599 3.658   -4.911  0.40 12.33 ?  42  TYR   A H    1 
ATOM   1117 H  HA   A TYR   A 1 42  ? 33.415 4.462   -4.215  0.60 12.25 ?  42  TYR   A HA   1 
ATOM   1118 H  HA   B TYR   A 1 42  ? 33.136 4.425   -4.416  0.40 12.22 ?  42  TYR   A HA   1 
ATOM   1119 H  HB2  A TYR   A 1 42  ? 31.199 6.061   -4.940  0.60 13.24 ?  42  TYR   A HB2  1 
ATOM   1120 H  HB2  B TYR   A 1 42  ? 30.953 6.097   -5.050  0.40 12.79 ?  42  TYR   A HB2  1 
ATOM   1121 H  HB3  A TYR   A 1 42  ? 32.707 6.555   -4.858  0.60 13.24 ?  42  TYR   A HB3  1 
ATOM   1122 H  HB3  B TYR   A 1 42  ? 32.467 6.568   -4.960  0.40 12.79 ?  42  TYR   A HB3  1 
ATOM   1123 H  HD1  A TYR   A 1 42  ? 34.326 5.341   -6.509  0.60 14.95 ?  42  TYR   A HD1  1 
ATOM   1124 H  HD1  B TYR   A 1 42  ? 34.063 5.388   -6.646  0.40 14.15 ?  42  TYR   A HD1  1 
ATOM   1125 H  HD2  A TYR   A 1 42  ? 30.370 5.491   -7.068  0.60 15.09 ?  42  TYR   A HD2  1 
ATOM   1126 H  HD2  B TYR   A 1 42  ? 30.106 5.592   -7.163  0.40 15.54 ?  42  TYR   A HD2  1 
ATOM   1127 H  HE1  A TYR   A 1 42  ? 34.622 4.818   -8.741  0.60 15.71 ?  42  TYR   A HE1  1 
ATOM   1128 H  HE1  B TYR   A 1 42  ? 34.334 4.931   -8.890  0.40 14.79 ?  42  TYR   A HE1  1 
ATOM   1129 H  HE2  A TYR   A 1 42  ? 30.664 4.968   -9.304  0.60 16.50 ?  42  TYR   A HE2  1 
ATOM   1130 H  HE2  B TYR   A 1 42  ? 30.370 5.136   -9.408  0.40 16.57 ?  42  TYR   A HE2  1 
ATOM   1131 H  HH   A TYR   A 1 42  ? 33.673 4.412   -10.725 0.60 17.62 ?  42  TYR   A HH   1 
ATOM   1132 H  HH   B TYR   A 1 42  ? 31.786 4.702   -11.083 0.40 17.28 ?  42  TYR   A HH   1 
ATOM   1133 N  N    . LEU   A 1 43  ? 31.251 4.243   -2.066  1.00 10.08 ?  43  LEU   A N    1 
ATOM   1134 C  CA   . LEU   A 1 43  ? 30.813 4.584   -0.716  1.00 9.63  ?  43  LEU   A CA   1 
ATOM   1135 C  C    . LEU   A 1 43  ? 30.330 6.031   -0.624  1.00 9.89  ?  43  LEU   A C    1 
ATOM   1136 O  O    . LEU   A 1 43  ? 30.595 6.734   0.354   1.00 10.83 ?  43  LEU   A O    1 
ATOM   1137 C  CB   . LEU   A 1 43  ? 31.868 4.285   0.346   1.00 10.37 ?  43  LEU   A CB   1 
ATOM   1138 C  CG   . LEU   A 1 43  ? 32.350 2.836   0.450   1.00 10.56 ?  43  LEU   A CG   1 
ATOM   1139 C  CD1  . LEU   A 1 43  ? 33.401 2.735   1.547   1.00 11.52 ?  43  LEU   A CD1  1 
ATOM   1140 C  CD2  . LEU   A 1 43  ? 31.210 1.856   0.702   1.00 11.11 ?  43  LEU   A CD2  1 
ATOM   1141 H  H    A LEU   A 1 43  ? 30.872 3.537   -2.388  0.60 12.14 ?  43  LEU   A H    1 
ATOM   1142 H  H    B LEU   A 1 43  ? 30.960 3.470   -2.319  0.40 12.14 ?  43  LEU   A H    1 
ATOM   1143 H  HA   . LEU   A 1 43  ? 30.049 4.024   -0.504  1.00 11.60 ?  43  LEU   A HA   1 
ATOM   1144 H  HB2  . LEU   A 1 43  ? 32.647 4.834   0.166   1.00 12.48 ?  43  LEU   A HB2  1 
ATOM   1145 H  HB3  . LEU   A 1 43  ? 31.501 4.524   1.213   1.00 12.48 ?  43  LEU   A HB3  1 
ATOM   1146 H  HG   . LEU   A 1 43  ? 32.777 2.585   -0.383  1.00 12.71 ?  43  LEU   A HG   1 
ATOM   1147 H  HD11 . LEU   A 1 43  ? 33.705 1.815   1.613   1.00 13.87 ?  43  LEU   A HD11 1 
ATOM   1148 H  HD12 . LEU   A 1 43  ? 34.145 3.315   1.328   1.00 13.87 ?  43  LEU   A HD12 1 
ATOM   1149 H  HD13 . LEU   A 1 43  ? 33.004 3.010   2.391   1.00 13.87 ?  43  LEU   A HD13 1 
ATOM   1150 H  HD21 . LEU   A 1 43  ? 31.584 0.971   0.850   1.00 13.38 ?  43  LEU   A HD21 1 
ATOM   1151 H  HD22 . LEU   A 1 43  ? 30.718 2.141   1.485   1.00 13.38 ?  43  LEU   A HD22 1 
ATOM   1152 H  HD23 . LEU   A 1 43  ? 30.631 1.844   -0.073  1.00 13.38 ?  43  LEU   A HD23 1 
ATOM   1153 N  N    A LYS   A 1 44  ? 29.600 6.476   -1.649  0.60 9.97  ?  44  LYS   A N    1 
ATOM   1154 N  N    B LYS   A 1 44  ? 29.603 6.468   -1.653  0.40 10.27 ?  44  LYS   A N    1 
ATOM   1155 C  CA   A LYS   A 1 44  ? 28.966 7.796   -1.640  0.60 10.32 ?  44  LYS   A CA   1 
ATOM   1156 C  CA   B LYS   A 1 44  ? 28.945 7.770   -1.660  0.40 10.90 ?  44  LYS   A CA   1 
ATOM   1157 C  C    A LYS   A 1 44  ? 27.535 7.621   -1.151  0.60 9.72  ?  44  LYS   A C    1 
ATOM   1158 C  C    B LYS   A 1 44  ? 27.532 7.569   -1.135  0.40 10.10 ?  44  LYS   A C    1 
ATOM   1159 O  O    A LYS   A 1 44  ? 26.661 7.150   -1.885  0.60 10.94 ?  44  LYS   A O    1 
ATOM   1160 O  O    B LYS   A 1 44  ? 26.672 7.010   -1.826  0.40 10.62 ?  44  LYS   A O    1 
ATOM   1161 C  CB   A LYS   A 1 44  ? 29.022 8.437   -3.019  0.60 12.61 ?  44  LYS   A CB   1 
ATOM   1162 C  CB   B LYS   A 1 44  ? 28.942 8.363   -3.067  0.40 13.11 ?  44  LYS   A CB   1 
ATOM   1163 C  CG   A LYS   A 1 44  ? 30.414 8.873   -3.445  0.60 15.70 ?  44  LYS   A CG   1 
ATOM   1164 C  CG   B LYS   A 1 44  ? 30.294 8.892   -3.525  0.40 16.08 ?  44  LYS   A CG   1 
ATOM   1165 C  CD   A LYS   A 1 44  ? 31.062 9.842   -2.455  0.60 20.43 ?  44  LYS   A CD   1 
ATOM   1166 C  CD   B LYS   A 1 44  ? 31.060 9.530   -2.376  0.40 19.79 ?  44  LYS   A CD   1 
ATOM   1167 C  CE   A LYS   A 1 44  ? 32.437 10.277  -2.937  0.60 23.66 ?  44  LYS   A CE   1 
ATOM   1168 C  CE   B LYS   A 1 44  ? 32.099 10.515  -2.861  0.40 21.99 ?  44  LYS   A CE   1 
ATOM   1169 N  NZ   A LYS   A 1 44  ? 33.231 10.919  -1.856  0.60 25.25 ?  44  LYS   A NZ   1 
ATOM   1170 N  NZ   B LYS   A 1 44  ? 32.982 10.954  -1.748  0.40 23.27 ?  44  LYS   A NZ   1 
ATOM   1171 H  H    A LYS   A 1 44  ? 29.461 6.026   -2.369  0.60 12.00 ?  44  LYS   A H    1 
ATOM   1172 H  H    B LYS   A 1 44  ? 29.468 6.012   -2.370  0.40 12.36 ?  44  LYS   A H    1 
ATOM   1173 H  HA   A LYS   A 1 44  ? 29.422 8.364   -1.003  0.60 12.43 ?  44  LYS   A HA   1 
ATOM   1174 H  HA   B LYS   A 1 44  ? 29.389 8.365   -1.039  0.40 13.12 ?  44  LYS   A HA   1 
ATOM   1175 H  HB2  A LYS   A 1 44  ? 28.699 7.802   -3.673  0.60 15.17 ?  44  LYS   A HB2  1 
ATOM   1176 H  HB2  B LYS   A 1 44  ? 28.671 7.676   -3.697  0.40 15.78 ?  44  LYS   A HB2  1 
ATOM   1177 H  HB3  A LYS   A 1 44  ? 28.455 9.225   -3.015  0.60 15.17 ?  44  LYS   A HB3  1 
ATOM   1178 H  HB3  B LYS   A 1 44  ? 28.315 9.102   -3.100  0.40 15.78 ?  44  LYS   A HB3  1 
ATOM   1179 H  HG2  A LYS   A 1 44  ? 30.986 8.094   -3.518  0.60 18.88 ?  44  LYS   A HG2  1 
ATOM   1180 H  HG2  B LYS   A 1 44  ? 30.825 8.160   -3.878  0.40 19.34 ?  44  LYS   A HG2  1 
ATOM   1181 H  HG3  A LYS   A 1 44  ? 30.358 9.325   -4.304  0.60 18.88 ?  44  LYS   A HG3  1 
ATOM   1182 H  HG3  B LYS   A 1 44  ? 30.162 9.569   -4.211  0.40 19.34 ?  44  LYS   A HG3  1 
ATOM   1183 H  HD2  A LYS   A 1 44  ? 30.499 10.623  -2.357  0.60 24.56 ?  44  LYS   A HD2  1 
ATOM   1184 H  HD2  B LYS   A 1 44  ? 30.437 10.015  -1.811  0.40 23.79 ?  44  LYS   A HD2  1 
ATOM   1185 H  HD3  A LYS   A 1 44  ? 31.175 9.396   -1.599  0.60 24.56 ?  44  LYS   A HD3  1 
ATOM   1186 H  HD3  B LYS   A 1 44  ? 31.504 8.831   -1.863  0.40 23.79 ?  44  LYS   A HD3  1 
ATOM   1187 H  HE2  A LYS   A 1 44  ? 32.925 9.501   -3.250  0.60 28.43 ?  44  LYS   A HE2  1 
ATOM   1188 H  HE2  B LYS   A 1 44  ? 32.646 10.093  -3.540  0.40 26.43 ?  44  LYS   A HE2  1 
ATOM   1189 H  HE3  A LYS   A 1 44  ? 32.329 10.918  -3.656  0.60 28.43 ?  44  LYS   A HE3  1 
ATOM   1190 H  HE3  B LYS   A 1 44  ? 31.651 11.295  -3.223  0.40 26.43 ?  44  LYS   A HE3  1 
ATOM   1191 H  HZ1  A LYS   A 1 44  ? 34.026 11.166  -2.169  0.60 30.34 ?  44  LYS   A HZ1  1 
ATOM   1192 H  HZ1  B LYS   A 1 44  ? 33.586 11.533  -2.051  0.40 27.97 ?  44  LYS   A HZ1  1 
ATOM   1193 H  HZ2  A LYS   A 1 44  ? 32.804 11.641  -1.553  0.60 30.34 ?  44  LYS   A HZ2  1 
ATOM   1194 H  HZ2  B LYS   A 1 44  ? 32.499 11.345  -1.111  0.40 27.97 ?  44  LYS   A HZ2  1 
ATOM   1195 H  HZ3  A LYS   A 1 44  ? 33.347 10.350  -1.183  0.60 30.34 ?  44  LYS   A HZ3  1 
ATOM   1196 H  HZ3  B LYS   A 1 44  ? 33.404 10.251  -1.400  0.40 27.97 ?  44  LYS   A HZ3  1 
ATOM   1197 N  N    . HIS   A 1 45  ? 27.302 7.994   0.104   1.00 9.70  ?  45  HIS   A N    1 
ATOM   1198 C  CA   . HIS   A 1 45  ? 26.063 7.655   0.799   1.00 9.64  ?  45  HIS   A CA   1 
ATOM   1199 C  C    . HIS   A 1 45  ? 25.035 8.777   0.636   1.00 10.22 ?  45  HIS   A C    1 
ATOM   1200 O  O    . HIS   A 1 45  ? 24.760 9.554   1.549   1.00 11.94 ?  45  HIS   A O    1 
ATOM   1201 C  CB   . HIS   A 1 45  ? 26.363 7.404   2.265   1.00 9.51  ?  45  HIS   A CB   1 
ATOM   1202 C  CG   . HIS   A 1 45  ? 27.474 6.435   2.496   1.00 9.32  ?  45  HIS   A CG   1 
ATOM   1203 N  ND1  . HIS   A 1 45  ? 27.465 5.146   1.996   1.00 9.68  ?  45  HIS   A ND1  1 
ATOM   1204 C  CD2  . HIS   A 1 45  ? 28.640 6.587   3.170   1.00 9.53  ?  45  HIS   A CD2  1 
ATOM   1205 C  CE1  . HIS   A 1 45  ? 28.587 4.551   2.367   1.00 9.60  ?  45  HIS   A CE1  1 
ATOM   1206 N  NE2  . HIS   A 1 45  ? 29.313 5.398   3.082   1.00 9.68  ?  45  HIS   A NE2  1 
ATOM   1207 H  H    A HIS   A 1 45  ? 27.844 8.467   0.579   0.60 11.68 ?  45  HIS   A H    1 
ATOM   1208 H  H    B HIS   A 1 45  ? 27.843 8.477   0.570   0.40 11.68 ?  45  HIS   A H    1 
ATOM   1209 H  HA   . HIS   A 1 45  ? 25.689 6.842   0.419   1.00 11.61 ?  45  HIS   A HA   1 
ATOM   1210 H  HB2  . HIS   A 1 45  ? 26.598 8.244   2.685   1.00 11.45 ?  45  HIS   A HB2  1 
ATOM   1211 H  HB3  . HIS   A 1 45  ? 25.559 7.043   2.689   1.00 11.45 ?  45  HIS   A HB3  1 
ATOM   1212 H  HD2  . HIS   A 1 45  ? 28.931 7.355   3.611   1.00 11.48 ?  45  HIS   A HD2  1 
ATOM   1213 H  HE1  . HIS   A 1 45  ? 28.822 3.672   2.172   1.00 11.56 ?  45  HIS   A HE1  1 
ATOM   1214 H  HE2  . HIS   A 1 45  ? 30.085 5.231   3.425   1.00 11.66 ?  45  HIS   A HE2  1 
ATOM   1215 N  N    A GLY   A 1 46  ? 24.472 8.855   -0.565  0.60 11.14 ?  46  GLY   A N    1 
ATOM   1216 N  N    B GLY   A 1 46  ? 24.421 8.825   -0.543  0.40 10.71 ?  46  GLY   A N    1 
ATOM   1217 C  CA   A GLY   A 1 46  ? 23.673 10.010  -0.923  0.60 12.09 ?  46  GLY   A CA   1 
ATOM   1218 C  CA   B GLY   A 1 46  ? 23.575 9.953   -0.892  0.40 11.16 ?  46  GLY   A CA   1 
ATOM   1219 C  C    A GLY   A 1 46  ? 22.183 9.866   -0.707  0.60 12.09 ?  46  GLY   A C    1 
ATOM   1220 C  C    B GLY   A 1 46  ? 22.119 9.858   -0.460  0.40 10.67 ?  46  GLY   A C    1 
ATOM   1221 O  O    A GLY   A 1 46  ? 21.505 10.854  -0.409  0.60 12.98 ?  46  GLY   A O    1 
ATOM   1222 O  O    B GLY   A 1 46  ? 21.525 10.863  -0.056  0.40 11.73 ?  46  GLY   A O    1 
ATOM   1223 H  H    A GLY   A 1 46  ? 24.521 8.254   -1.174  0.60 13.41 ?  46  GLY   A H    1 
ATOM   1224 H  H    B GLY   A 1 46  ? 24.471 8.216   -1.147  0.40 12.89 ?  46  GLY   A H    1 
ATOM   1225 H  HA2  A GLY   A 1 46  ? 23.976 10.777  -0.409  0.60 14.55 ?  46  GLY   A HA2  1 
ATOM   1226 H  HA2  B GLY   A 1 46  ? 23.944 10.752  -0.483  0.40 13.43 ?  46  GLY   A HA2  1 
ATOM   1227 H  HA3  A GLY   A 1 46  ? 23.800 10.204  -1.859  0.60 14.55 ?  46  GLY   A HA3  1 
ATOM   1228 H  HA3  B GLY   A 1 46  ? 23.609 10.075  -1.854  0.40 13.43 ?  46  GLY   A HA3  1 
ATOM   1229 N  N    A GLY   A 1 47  ? 21.653 8.661   -0.894  0.60 11.15 ?  47  GLY   A N    1 
ATOM   1230 N  N    B GLY   A 1 47  ? 21.532 8.670   -0.543  0.40 10.26 ?  47  GLY   A N    1 
ATOM   1231 C  CA   A GLY   A 1 47  ? 20.223 8.438   -0.840  0.60 10.57 ?  47  GLY   A CA   1 
ATOM   1232 C  CA   B GLY   A 1 47  ? 20.108 8.504   -0.331  0.40 10.32 ?  47  GLY   A CA   1 
ATOM   1233 C  C    A GLY   A 1 47  ? 19.919 7.009   -0.444  0.60 10.49 ?  47  GLY   A C    1 
ATOM   1234 C  C    B GLY   A 1 47  ? 19.764 7.061   -0.025  0.40 9.63  ?  47  GLY   A C    1 
ATOM   1235 O  O    A GLY   A 1 47  ? 20.820 6.194   -0.233  0.60 10.70 ?  47  GLY   A O    1 
ATOM   1236 O  O    B GLY   A 1 47  ? 20.645 6.210   0.120   0.40 9.66  ?  47  GLY   A O    1 
ATOM   1237 H  H    A GLY   A 1 47  ? 22.110 7.949   -1.056  0.60 13.43 ?  47  GLY   A H    1 
ATOM   1238 H  H    B GLY   A 1 47  ? 21.948 7.943   -0.706  0.40 12.35 ?  47  GLY   A H    1 
ATOM   1239 H  HA2  A GLY   A 1 47  ? 19.815 9.047   -0.200  0.60 12.73 ?  47  GLY   A HA2  1 
ATOM   1240 H  HA2  B GLY   A 1 47  ? 19.815 9.052   0.414   0.40 12.42 ?  47  GLY   A HA2  1 
ATOM   1241 H  HA3  A GLY   A 1 47  ? 19.835 8.603   -1.716  0.60 12.73 ?  47  GLY   A HA3  1 
ATOM   1242 H  HA3  B GLY   A 1 47  ? 19.618 8.785   -1.126  0.40 12.42 ?  47  GLY   A HA3  1 
ATOM   1243 N  N    A GLY   A 1 48  ? 18.632 6.698   -0.360  0.60 10.46 ?  48  GLY   A N    1 
ATOM   1244 N  N    B GLY   A 1 48  ? 18.462 6.793   0.075   0.40 10.28 ?  48  GLY   A N    1 
ATOM   1245 C  CA   A GLY   A 1 48  ? 18.249 5.371   0.059   0.60 11.09 ?  48  GLY   A CA   1 
ATOM   1246 C  CA   B GLY   A 1 48  ? 18.027 5.454   0.434   0.40 10.02 ?  48  GLY   A CA   1 
ATOM   1247 C  C    A GLY   A 1 48  ? 18.700 5.090   1.486   0.60 10.33 ?  48  GLY   A C    1 
ATOM   1248 C  C    B GLY   A 1 48  ? 18.600 5.040   1.774   0.40 9.89  ?  48  GLY   A C    1 
ATOM   1249 O  O    A GLY   A 1 48  ? 18.890 5.999   2.302   0.60 10.44 ?  48  GLY   A O    1 
ATOM   1250 O  O    B GLY   A 1 48  ? 18.730 5.849   2.703   0.40 9.81  ?  48  GLY   A O    1 
ATOM   1251 H  H    A GLY   A 1 48  ? 17.983 7.229   -0.529  0.60 12.60 ?  48  GLY   A H    1 
ATOM   1252 H  H    B GLY   A 1 48  ? 17.820 7.357   -0.056  0.40 12.38 ?  48  GLY   A H    1 
ATOM   1253 H  HA2  A GLY   A 1 48  ? 17.287 5.273   0.014   0.60 13.35 ?  48  GLY   A HA2  1 
ATOM   1254 H  HA2  B GLY   A 1 48  ? 17.058 5.418   0.483   0.40 12.07 ?  48  GLY   A HA2  1 
ATOM   1255 H  HA3  A GLY   A 1 48  ? 18.659 4.710   -0.518  0.60 13.35 ?  48  GLY   A HA3  1 
ATOM   1256 H  HA3  B GLY   A 1 48  ? 18.324 4.818   -0.241  0.40 12.07 ?  48  GLY   A HA3  1 
ATOM   1257 N  N    A VAL   A 1 49  ? 18.866 3.798   1.782   0.60 10.40 ?  49  VAL   A N    1 
ATOM   1258 N  N    B VAL   A 1 49  ? 18.948 3.757   1.878   0.40 9.85  ?  49  VAL   A N    1 
ATOM   1259 C  CA   A VAL   A 1 49  ? 19.365 3.393   3.095   0.60 10.52 ?  49  VAL   A CA   1 
ATOM   1260 C  CA   B VAL   A 1 49  ? 19.540 3.232   3.106   0.40 9.82  ?  49  VAL   A CA   1 
ATOM   1261 C  C    A VAL   A 1 49  ? 20.676 4.098   3.416   0.60 9.60  ?  49  VAL   A C    1 
ATOM   1262 C  C    B VAL   A 1 49  ? 20.807 3.997   3.463   0.40 9.06  ?  49  VAL   A C    1 
ATOM   1263 O  O    A VAL   A 1 49  ? 20.885 4.558   4.542   0.60 10.21 ?  49  VAL   A O    1 
ATOM   1264 O  O    B VAL   A 1 49  ? 21.014 4.377   4.621   0.40 8.86  ?  49  VAL   A O    1 
ATOM   1265 C  CB   A VAL   A 1 49  ? 19.513 1.858   3.161   0.60 11.17 ?  49  VAL   A CB   1 
ATOM   1266 C  CB   B VAL   A 1 49  ? 19.825 1.726   2.956   0.40 9.58  ?  49  VAL   A CB   1 
ATOM   1267 C  CG1  A VAL   A 1 49  ? 20.302 1.438   4.406   0.60 10.86 ?  49  VAL   A CG1  1 
ATOM   1268 C  CG1  B VAL   A 1 49  ? 20.707 1.243   4.106   0.40 8.86  ?  49  VAL   A CG1  1 
ATOM   1269 C  CG2  A VAL   A 1 49  ? 18.149 1.190   3.142   0.60 13.10 ?  49  VAL   A CG2  1 
ATOM   1270 C  CG2  B VAL   A 1 49  ? 18.532 0.928   2.878   0.40 10.06 ?  49  VAL   A CG2  1 
ATOM   1271 H  H    A VAL   A 1 49  ? 18.699 3.137   1.253   0.60 12.52 ?  49  VAL   A H    1 
ATOM   1272 H  H    B VAL   A 1 49  ? 18.852 3.175   1.257   0.40 11.86 ?  49  VAL   A H    1 
ATOM   1273 H  HA   A VAL   A 1 49  ? 18.720 3.645   3.773   0.60 12.67 ?  49  VAL   A HA   1 
ATOM   1274 H  HA   B VAL   A 1 49  ? 18.911 3.345   3.835   0.40 11.83 ?  49  VAL   A HA   1 
ATOM   1275 H  HB   A VAL   A 1 49  ? 20.014 1.552   2.387   0.60 13.45 ?  49  VAL   A HB   1 
ATOM   1276 H  HB   B VAL   A 1 49  ? 20.311 1.581   2.131   0.40 11.54 ?  49  VAL   A HB   1 
ATOM   1277 H  HG11 A VAL   A 1 49  ? 20.151 0.495   4.574   0.60 13.07 ?  49  VAL   A HG11 1 
ATOM   1278 H  HG11 B VAL   A 1 49  ? 20.634 0.278   4.178   0.40 10.67 ?  49  VAL   A HG11 1 
ATOM   1279 H  HG12 A VAL   A 1 49  ? 21.248 1.599   4.260   0.60 13.07 ?  49  VAL   A HG12 1 
ATOM   1280 H  HG12 B VAL   A 1 49  ? 21.633 1.484   3.924   0.40 10.67 ?  49  VAL   A HG12 1 
ATOM   1281 H  HG13 A VAL   A 1 49  ? 19.992 1.960   5.166   0.60 13.07 ?  49  VAL   A HG13 1 
ATOM   1282 H  HG13 B VAL   A 1 49  ? 20.415 1.657   4.932   0.40 10.67 ?  49  VAL   A HG13 1 
ATOM   1283 H  HG21 A VAL   A 1 49  ? 18.270 0.228   3.184   0.60 15.76 ?  49  VAL   A HG21 1 
ATOM   1284 H  HG21 B VAL   A 1 49  ? 18.742 -0.012  2.779   0.40 12.11 ?  49  VAL   A HG21 1 
ATOM   1285 H  HG22 A VAL   A 1 49  ? 17.643 1.495   3.909   0.60 15.76 ?  49  VAL   A HG22 1 
ATOM   1286 H  HG22 B VAL   A 1 49  ? 18.023 1.069   3.694   0.40 12.11 ?  49  VAL   A HG22 1 
ATOM   1287 H  HG23 A VAL   A 1 49  ? 17.698 1.434   2.322   0.60 15.76 ?  49  VAL   A HG23 1 
ATOM   1288 H  HG23 B VAL   A 1 49  ? 18.017 1.235   2.114   0.40 12.11 ?  49  VAL   A HG23 1 
ATOM   1289 N  N    A ALA   A 1 50  ? 21.592 4.151   2.446   0.60 9.32  ?  50  ALA   A N    1 
ATOM   1290 N  N    B ALA   A 1 50  ? 21.697 4.181   2.485   0.40 8.83  ?  50  ALA   A N    1 
ATOM   1291 C  CA   A ALA   A 1 50  ? 22.917 4.704   2.704   0.60 9.22  ?  50  ALA   A CA   1 
ATOM   1292 C  CA   B ALA   A 1 50  ? 23.003 4.761   2.778   0.40 8.78  ?  50  ALA   A CA   1 
ATOM   1293 C  C    A ALA   A 1 50  ? 22.835 6.162   3.130   0.60 9.44  ?  50  ALA   A C    1 
ATOM   1294 C  C    B ALA   A 1 50  ? 22.877 6.219   3.198   0.40 8.52  ?  50  ALA   A C    1 
ATOM   1295 O  O    A ALA   A 1 50  ? 23.495 6.579   4.088   0.60 10.12 ?  50  ALA   A O    1 
ATOM   1296 O  O    B ALA   A 1 50  ? 23.478 6.645   4.192   0.40 8.32  ?  50  ALA   A O    1 
ATOM   1297 C  CB   A ALA   A 1 50  ? 23.784 4.573   1.456   0.60 9.10  ?  50  ALA   A CB   1 
ATOM   1298 C  CB   B ALA   A 1 50  ? 23.920 4.626   1.564   0.40 8.73  ?  50  ALA   A CB   1 
ATOM   1299 H  H    A ALA   A 1 50  ? 21.469 3.876   1.643   0.60 11.23 ?  50  ALA   A H    1 
ATOM   1300 H  H    B ALA   A 1 50  ? 21.566 3.983   1.658   0.40 10.64 ?  50  ALA   A H    1 
ATOM   1301 H  HA   A ALA   A 1 50  ? 23.338 4.210   3.424   0.60 11.11 ?  50  ALA   A HA   1 
ATOM   1302 H  HA   B ALA   A 1 50  ? 23.404 4.278   3.513   0.40 10.58 ?  50  ALA   A HA   1 
ATOM   1303 H  HB1  A ALA   A 1 50  ? 24.658 4.951   1.644   0.60 10.96 ?  50  ALA   A HB1  1 
ATOM   1304 H  HB1  B ALA   A 1 50  ? 24.781 5.017   1.776   0.40 10.52 ?  50  ALA   A HB1  1 
ATOM   1305 H  HB2  A ALA   A 1 50  ? 23.863 3.640   1.226   0.60 10.96 ?  50  ALA   A HB2  1 
ATOM   1306 H  HB2  B ALA   A 1 50  ? 24.024 3.686   1.351   0.40 10.52 ?  50  ALA   A HB2  1 
ATOM   1307 H  HB3  A ALA   A 1 50  ? 23.362 5.064   0.732   0.60 10.96 ?  50  ALA   A HB3  1 
ATOM   1308 H  HB3  B ALA   A 1 50  ? 23.520 5.094   0.813   0.40 10.52 ?  50  ALA   A HB3  1 
ATOM   1309 N  N    A GLY   A 1 51  ? 22.046 6.963   2.415   0.60 9.59  ?  51  GLY   A N    1 
ATOM   1310 N  N    B GLY   A 1 51  ? 22.101 7.003   2.450   0.40 9.14  ?  51  GLY   A N    1 
ATOM   1311 C  CA   A GLY   A 1 51  ? 21.904 8.356   2.801   0.60 10.01 ?  51  GLY   A CA   1 
ATOM   1312 C  CA   B GLY   A 1 51  ? 21.912 8.392   2.822   0.40 9.68  ?  51  GLY   A CA   1 
ATOM   1313 C  C    A GLY   A 1 51  ? 21.306 8.505   4.186   0.60 9.75  ?  51  GLY   A C    1 
ATOM   1314 C  C    B GLY   A 1 51  ? 21.281 8.535   4.192   0.40 9.72  ?  51  GLY   A C    1 
ATOM   1315 O  O    A GLY   A 1 51  ? 21.701 9.387   4.953   0.60 10.48 ?  51  GLY   A O    1 
ATOM   1316 O  O    B GLY   A 1 51  ? 21.634 9.434   4.959   0.40 10.10 ?  51  GLY   A O    1 
ATOM   1317 H  H    A GLY   A 1 51  ? 21.600 6.728   1.718   0.60 11.55 ?  51  GLY   A H    1 
ATOM   1318 H  H    B GLY   A 1 51  ? 21.683 6.756   1.738   0.40 11.01 ?  51  GLY   A H    1 
ATOM   1319 H  HA2  A GLY   A 1 51  ? 22.772 8.786   2.791   0.60 12.06 ?  51  GLY   A HA2  1 
ATOM   1320 H  HA2  B GLY   A 1 51  ? 22.769 8.845   2.829   0.40 11.66 ?  51  GLY   A HA2  1 
ATOM   1321 H  HA3  A GLY   A 1 51  ? 21.327 8.811   2.166   0.60 12.06 ?  51  GLY   A HA3  1 
ATOM   1322 H  HA3  B GLY   A 1 51  ? 21.337 8.828   2.173   0.40 11.66 ?  51  GLY   A HA3  1 
ATOM   1323 N  N    . ALA   A 1 52  ? 20.334 7.650   4.517   1.00 9.82  ?  52  ALA   A N    1 
ATOM   1324 C  CA   . ALA   A 1 52  ? 19.680 7.713   5.821   1.00 10.52 ?  52  ALA   A CA   1 
ATOM   1325 C  C    . ALA   A 1 52  ? 20.628 7.300   6.948   1.00 9.77  ?  52  ALA   A C    1 
ATOM   1326 O  O    . ALA   A 1 52  ? 20.696 7.966   7.984   1.00 10.73 ?  52  ALA   A O    1 
ATOM   1327 C  CB   . ALA   A 1 52  ? 18.419 6.846   5.802   1.00 12.10 ?  52  ALA   A CB   1 
ATOM   1328 H  H    A ALA   A 1 52  ? 20.044 7.022   4.003   0.60 11.83 ?  52  ALA   A H    1 
ATOM   1329 H  H    B ALA   A 1 52  ? 20.064 7.010   4.007   0.40 11.83 ?  52  ALA   A H    1 
ATOM   1330 H  HA   . ALA   A 1 52  ? 19.406 8.624   5.984   1.00 12.67 ?  52  ALA   A HA   1 
ATOM   1331 H  HB1  . ALA   A 1 52  ? 17.963 6.935   6.653   1.00 14.56 ?  52  ALA   A HB1  1 
ATOM   1332 H  HB2  . ALA   A 1 52  ? 17.839 7.148   5.085   1.00 14.56 ?  52  ALA   A HB2  1 
ATOM   1333 H  HB3  . ALA   A 1 52  ? 18.670 5.920   5.655   1.00 14.56 ?  52  ALA   A HB3  1 
ATOM   1334 N  N    A LEU   A 1 53  ? 21.353 6.190   6.772   0.60 9.59  ?  53  LEU   A N    1 
ATOM   1335 N  N    B LEU   A 1 53  ? 21.363 6.197   6.771   0.40 9.35  ?  53  LEU   A N    1 
ATOM   1336 C  CA   A LEU   A 1 53  ? 22.316 5.779   7.795   0.60 9.94  ?  53  LEU   A CA   1 
ATOM   1337 C  CA   B LEU   A 1 53  ? 22.353 5.814   7.779   0.40 9.27  ?  53  LEU   A CA   1 
ATOM   1338 C  C    A LEU   A 1 53  ? 23.383 6.844   7.986   0.60 9.79  ?  53  LEU   A C    1 
ATOM   1339 C  C    B LEU   A 1 53  ? 23.370 6.931   7.982   0.40 8.88  ?  53  LEU   A C    1 
ATOM   1340 O  O    A LEU   A 1 53  ? 23.763 7.162   9.118   0.60 10.70 ?  53  LEU   A O    1 
ATOM   1341 O  O    B LEU   A 1 53  ? 23.625 7.360   9.113   0.40 9.32  ?  53  LEU   A O    1 
ATOM   1342 C  CB   A LEU   A 1 53  ? 22.968 4.441   7.427   0.60 10.34 ?  53  LEU   A CB   1 
ATOM   1343 C  CB   B LEU   A 1 53  ? 23.062 4.510   7.388   0.40 9.68  ?  53  LEU   A CB   1 
ATOM   1344 C  CG   A LEU   A 1 53  ? 22.066 3.201   7.476   0.60 10.64 ?  53  LEU   A CG   1 
ATOM   1345 C  CG   B LEU   A 1 53  ? 22.303 3.175   7.464   0.40 10.31 ?  53  LEU   A CG   1 
ATOM   1346 C  CD1  A LEU   A 1 53  ? 22.786 2.002   6.885   0.60 10.97 ?  53  LEU   A CD1  1 
ATOM   1347 C  CD1  B LEU   A 1 53  ? 23.154 2.053   6.881   0.40 10.56 ?  53  LEU   A CD1  1 
ATOM   1348 C  CD2  A LEU   A 1 53  ? 21.623 2.902   8.901   0.60 11.99 ?  53  LEU   A CD2  1 
ATOM   1349 C  CD2  B LEU   A 1 53  ? 21.892 2.831   8.890   0.40 11.23 ?  53  LEU   A CD2  1 
ATOM   1350 H  H    A LEU   A 1 53  ? 21.306 5.666   6.089   0.60 11.55 ?  53  LEU   A H    1 
ATOM   1351 H  H    B LEU   A 1 53  ? 21.307 5.661   6.098   0.40 11.26 ?  53  LEU   A H    1 
ATOM   1352 H  HA   A LEU   A 1 53  ? 21.853 5.660   8.638   0.60 11.97 ?  53  LEU   A HA   1 
ATOM   1353 H  HA   B LEU   A 1 53  ? 21.899 5.665   8.624   0.40 11.17 ?  53  LEU   A HA   1 
ATOM   1354 H  HB2  A LEU   A 1 53  ? 23.315 4.508   6.522   0.60 12.45 ?  53  LEU   A HB2  1 
ATOM   1355 H  HB2  B LEU   A 1 53  ? 23.360 4.603   6.471   0.40 11.66 ?  53  LEU   A HB2  1 
ATOM   1356 H  HB3  A LEU   A 1 53  ? 23.707 4.282   8.038   0.60 12.45 ?  53  LEU   A HB3  1 
ATOM   1357 H  HB3  B LEU   A 1 53  ? 23.839 4.417   7.962   0.40 11.66 ?  53  LEU   A HB3  1 
ATOM   1358 H  HG   A LEU   A 1 53  ? 21.273 3.369   6.943   0.60 12.81 ?  53  LEU   A HG   1 
ATOM   1359 H  HG   B LEU   A 1 53  ? 21.498 3.239   6.931   0.40 12.41 ?  53  LEU   A HG   1 
ATOM   1360 H  HD11 A LEU   A 1 53  ? 22.200 1.233   6.926   0.60 13.21 ?  53  LEU   A HD11 1 
ATOM   1361 H  HD11 B LEU   A 1 53  ? 22.660 1.218   6.940   0.40 12.71 ?  53  LEU   A HD11 1 
ATOM   1362 H  HD12 A LEU   A 1 53  ? 23.018 2.197   5.964   0.60 13.21 ?  53  LEU   A HD12 1 
ATOM   1363 H  HD12 B LEU   A 1 53  ? 23.351 2.255   5.954   0.40 12.71 ?  53  LEU   A HD12 1 
ATOM   1364 H  HD13 A LEU   A 1 53  ? 23.592 1.835   7.401   0.60 13.21 ?  53  LEU   A HD13 1 
ATOM   1365 H  HD13 B LEU   A 1 53  ? 23.978 1.983   7.389   0.40 12.71 ?  53  LEU   A HD13 1 
ATOM   1366 H  HD21 A LEU   A 1 53  ? 21.124 2.074   8.908   0.60 14.43 ?  53  LEU   A HD21 1 
ATOM   1367 H  HD21 B LEU   A 1 53  ? 21.335 2.035   8.877   0.40 13.51 ?  53  LEU   A HD21 1 
ATOM   1368 H  HD22 A LEU   A 1 53  ? 22.412 2.819   9.462   0.60 14.43 ?  53  LEU   A HD22 1 
ATOM   1369 H  HD22 B LEU   A 1 53  ? 22.685 2.670   9.422   0.40 13.51 ?  53  LEU   A HD22 1 
ATOM   1370 H  HD23 A LEU   A 1 53  ? 21.068 3.630   9.220   0.60 14.43 ?  53  LEU   A HD23 1 
ATOM   1371 H  HD23 B LEU   A 1 53  ? 21.390 3.574   9.264   0.40 13.51 ?  53  LEU   A HD23 1 
ATOM   1372 N  N    A ASN   A 1 54  ? 23.881 7.407   6.890   0.60 9.61  ?  54  ASN   A N    1 
ATOM   1373 N  N    B ASN   A 1 54  ? 23.954 7.424   6.889   0.40 8.94  ?  54  ASN   A N    1 
ATOM   1374 C  CA   A ASN   A 1 54  ? 24.940 8.395   7.020   0.60 9.68  ?  54  ASN   A CA   1 
ATOM   1375 C  CA   B ASN   A 1 54  ? 24.985 8.447   7.016   0.40 9.15  ?  54  ASN   A CA   1 
ATOM   1376 C  C    A ASN   A 1 54  ? 24.440 9.646   7.738   0.60 9.98  ?  54  ASN   A C    1 
ATOM   1377 C  C    B ASN   A 1 54  ? 24.453 9.683   7.731   0.40 9.76  ?  54  ASN   A C    1 
ATOM   1378 O  O    A ASN   A 1 54  ? 25.134 10.192  8.606   0.60 10.60 ?  54  ASN   A O    1 
ATOM   1379 O  O    B ASN   A 1 54  ? 25.138 10.259  8.586   0.40 10.16 ?  54  ASN   A O    1 
ATOM   1380 C  CB   A ASN   A 1 54  ? 25.507 8.744   5.652   0.60 9.65  ?  54  ASN   A CB   1 
ATOM   1381 C  CB   B ASN   A 1 54  ? 25.548 8.823   5.649   0.40 9.12  ?  54  ASN   A CB   1 
ATOM   1382 C  CG   A ASN   A 1 54  ? 26.565 9.808   5.751   0.60 9.54  ?  54  ASN   A CG   1 
ATOM   1383 C  CG   B ASN   A 1 54  ? 26.517 9.978   5.743   0.40 9.06  ?  54  ASN   A CG   1 
ATOM   1384 O  OD1  A ASN   A 1 54  ? 27.524 9.672   6.526   0.60 9.06  ?  54  ASN   A OD1  1 
ATOM   1385 O  OD1  B ASN   A 1 54  ? 27.581 9.852   6.355   0.40 9.82  ?  54  ASN   A OD1  1 
ATOM   1386 N  ND2  A ASN   A 1 54  ? 26.382 10.902  5.024   0.60 10.50 ?  54  ASN   A ND2  1 
ATOM   1387 N  ND2  B ASN   A 1 54  ? 26.151 11.118  5.174   0.40 8.96  ?  54  ASN   A ND2  1 
ATOM   1388 H  H    A ASN   A 1 54  ? 23.631 7.231   6.086   0.60 11.57 ?  54  ASN   A H    1 
ATOM   1389 H  H    B ASN   A 1 54  ? 23.775 7.180   6.085   0.40 10.77 ?  54  ASN   A H    1 
ATOM   1390 H  HA   A ASN   A 1 54  ? 25.656 8.015   7.548   0.60 11.66 ?  54  ASN   A HA   1 
ATOM   1391 H  HA   B ASN   A 1 54  ? 25.709 8.090   7.549   0.40 11.02 ?  54  ASN   A HA   1 
ATOM   1392 H  HB2  A ASN   A 1 54  ? 25.902 7.944   5.258   0.60 11.63 ?  54  ASN   A HB2  1 
ATOM   1393 H  HB2  B ASN   A 1 54  ? 26.019 8.059   5.283   0.40 10.99 ?  54  ASN   A HB2  1 
ATOM   1394 H  HB3  A ASN   A 1 54  ? 24.792 9.072   5.082   0.60 11.63 ?  54  ASN   A HB3  1 
ATOM   1395 H  HB3  B ASN   A 1 54  ? 24.818 9.080   5.066   0.40 10.99 ?  54  ASN   A HB3  1 
ATOM   1396 H  HD21 A ASN   A 1 54  ? 26.961 11.532  5.053   0.60 12.64 ?  54  ASN   A HD21 1 
ATOM   1397 H  HD21 B ASN   A 1 54  ? 26.671 11.802  5.212   0.40 10.79 ?  54  ASN   A HD21 1 
ATOM   1398 H  HD22 A ASN   A 1 54  ? 25.694 10.965  4.512   0.60 12.64 ?  54  ASN   A HD22 1 
ATOM   1399 H  HD22 B ASN   A 1 54  ? 25.403 11.169  4.755   0.40 10.79 ?  54  ASN   A HD22 1 
ATOM   1400 N  N    . LYS   A 1 55  ? 23.232 10.108  7.394   1.00 10.22 ?  55  LYS   A N    1 
ATOM   1401 C  CA   . LYS   A 1 55  ? 22.651 11.268  8.059   1.00 10.76 ?  55  LYS   A CA   1 
ATOM   1402 C  C    . LYS   A 1 55  ? 22.560 11.039  9.561   1.00 10.95 ?  55  LYS   A C    1 
ATOM   1403 O  O    . LYS   A 1 55  ? 22.842 11.944  10.356  1.00 11.55 ?  55  LYS   A O    1 
ATOM   1404 C  CB   . LYS   A 1 55  ? 21.280 11.572  7.447   1.00 11.59 ?  55  LYS   A CB   1 
ATOM   1405 C  CG   . LYS   A 1 55  ? 20.534 12.737  8.080   1.00 13.09 ?  55  LYS   A CG   1 
ATOM   1406 C  CD   . LYS   A 1 55  ? 19.213 12.976  7.343   1.00 14.78 ?  55  LYS   A CD   1 
ATOM   1407 C  CE   . LYS   A 1 55  ? 18.320 13.995  8.038   1.00 16.89 ?  55  LYS   A CE   1 
ATOM   1408 N  NZ   . LYS   A 1 55  ? 16.984 14.119  7.375   1.00 17.39 ?  55  LYS   A NZ   1 
ATOM   1409 H  H    A LYS   A 1 55  ? 22.726 9.759   6.786   0.60 12.30 ?  55  LYS   A H    1 
ATOM   1410 H  H    B LYS   A 1 55  ? 22.721 9.738   6.802   0.40 12.30 ?  55  LYS   A H    1 
ATOM   1411 H  HA   . LYS   A 1 55  ? 23.221 12.032  7.908   1.00 12.96 ?  55  LYS   A HA   1 
ATOM   1412 H  HB2  . LYS   A 1 55  ? 21.401 11.781  6.508   1.00 13.95 ?  55  LYS   A HB2  1 
ATOM   1413 H  HB3  . LYS   A 1 55  ? 20.718 10.785  7.534   1.00 13.95 ?  55  LYS   A HB3  1 
ATOM   1414 H  HG2  . LYS   A 1 55  ? 20.332 12.528  9.006   1.00 15.75 ?  55  LYS   A HG2  1 
ATOM   1415 H  HG3  . LYS   A 1 55  ? 21.072 13.538  8.019   1.00 15.75 ?  55  LYS   A HG3  1 
ATOM   1416 H  HD2  . LYS   A 1 55  ? 19.411 13.305  6.451   1.00 17.78 ?  55  LYS   A HD2  1 
ATOM   1417 H  HD3  . LYS   A 1 55  ? 18.730 12.137  7.285   1.00 17.78 ?  55  LYS   A HD3  1 
ATOM   1418 H  HE2  . LYS   A 1 55  ? 18.178 13.714  8.955   1.00 20.31 ?  55  LYS   A HE2  1 
ATOM   1419 H  HE3  . LYS   A 1 55  ? 18.753 14.861  8.015   1.00 20.31 ?  55  LYS   A HE3  1 
ATOM   1420 H  HZ1  . LYS   A 1 55  ? 16.386 14.433  7.953   1.00 20.91 ?  55  LYS   A HZ1  1 
ATOM   1421 H  HZ2  . LYS   A 1 55  ? 17.036 14.677  6.683   1.00 20.91 ?  55  LYS   A HZ2  1 
ATOM   1422 H  HZ3  . LYS   A 1 55  ? 16.710 13.322  7.084   1.00 20.91 ?  55  LYS   A HZ3  1 
ATOM   1423 N  N    . ALA   A 1 56  ? 22.178 9.827   9.969   1.00 11.08 ?  56  ALA   A N    1 
ATOM   1424 C  CA   . ALA   A 1 56  ? 22.052 9.516   11.387  1.00 11.77 ?  56  ALA   A CA   1 
ATOM   1425 C  C    . ALA   A 1 56  ? 23.393 9.538   12.110  1.00 11.59 ?  56  ALA   A C    1 
ATOM   1426 O  O    . ALA   A 1 56  ? 23.418 9.736   13.327  1.00 13.29 ?  56  ALA   A O    1 
ATOM   1427 C  CB   . ALA   A 1 56  ? 21.349 8.169   11.583  1.00 12.83 ?  56  ALA   A CB   1 
ATOM   1428 H  H    . ALA   A 1 56  ? 21.994 9.174   9.444   1.00 13.34 ?  56  ALA   A H    1 
ATOM   1429 H  HA   . ALA   A 1 56  ? 21.498 10.187  11.800  1.00 14.16 ?  56  ALA   A HA   1 
ATOM   1430 H  HB1  . ALA   A 1 56  ? 21.273 7.987   12.538  1.00 15.44 ?  56  ALA   A HB1  1 
ATOM   1431 H  HB2  . ALA   A 1 56  ? 20.461 8.217   11.192  1.00 15.44 ?  56  ALA   A HB2  1 
ATOM   1432 H  HB3  . ALA   A 1 56  ? 21.862 7.469   11.156  1.00 15.44 ?  56  ALA   A HB3  1 
ATOM   1433 N  N    . THR   A 1 57  ? 24.504 9.344   11.392  1.00 10.87 ?  57  THR   A N    1 
ATOM   1434 C  CA   . THR   A 1 57  ? 25.846 9.475   11.964  1.00 10.98 ?  57  THR   A CA   1 
ATOM   1435 C  C    . THR   A 1 57  ? 26.396 10.895  11.881  1.00 11.51 ?  57  THR   A C    1 
ATOM   1436 O  O    . THR   A 1 57  ? 27.581 11.105  12.176  1.00 12.08 ?  57  THR   A O    1 
ATOM   1437 C  CB   . THR   A 1 57  ? 26.860 8.531   11.290  1.00 11.11 ?  57  THR   A CB   1 
ATOM   1438 O  OG1  . THR   A 1 57  ? 27.243 9.030   9.992   1.00 10.54 ?  57  THR   A OG1  1 
ATOM   1439 C  CG2  . THR   A 1 57  ? 26.325 7.108   11.193  1.00 11.07 ?  57  THR   A CG2  1 
ATOM   1440 H  H    . THR   A 1 57  ? 24.508 9.105   10.565  1.00 13.09 ?  57  THR   A H    1 
ATOM   1441 H  HA   . THR   A 1 57  ? 25.805 9.222   12.906  1.00 13.22 ?  57  THR   A HA   1 
ATOM   1442 H  HB   . THR   A 1 57  ? 27.657 8.489   11.851  1.00 13.38 ?  57  THR   A HB   1 
ATOM   1443 H  HG1  . THR   A 1 57  ? 26.562 9.089   9.506   1.00 12.69 ?  57  THR   A HG1  1 
ATOM   1444 H  HG21 . THR   A 1 57  ? 27.004 6.516   10.828  1.00 13.33 ?  57  THR   A HG21 1 
ATOM   1445 H  HG22 . THR   A 1 57  ? 26.068 6.780   12.072  1.00 13.33 ?  57  THR   A HG22 1 
ATOM   1446 H  HG23 . THR   A 1 57  ? 25.548 7.081   10.614  1.00 13.33 ?  57  THR   A HG23 1 
ATOM   1447 N  N    . ASN   A 1 58  ? 25.581 11.870  11.480  1.00 11.67 ?  58  ASN   A N    1 
ATOM   1448 C  CA   . ASN   A 1 58  ? 26.051 13.250  11.375  1.00 12.72 ?  58  ASN   A CA   1 
ATOM   1449 C  C    . ASN   A 1 58  ? 27.202 13.366  10.368  1.00 11.54 ?  58  ASN   A C    1 
ATOM   1450 O  O    . ASN   A 1 58  ? 28.097 14.202  10.521  1.00 12.27 ?  58  ASN   A O    1 
ATOM   1451 C  CB   . ASN   A 1 58  ? 26.423 13.791  12.768  1.00 15.85 ?  58  ASN   A CB   1 
ATOM   1452 C  CG   . ASN   A 1 58  ? 26.808 15.252  12.764  1.00 19.81 ?  58  ASN   A CG   1 
ATOM   1453 O  OD1  . ASN   A 1 58  ? 26.178 16.062  12.098  1.00 21.55 ?  58  ASN   A OD1  1 
ATOM   1454 N  ND2  . ASN   A 1 58  ? 27.846 15.599  13.520  1.00 21.59 ?  58  ASN   A ND2  1 
ATOM   1455 H  H    . ASN   A 1 58  ? 24.755 11.750  11.254  1.00 14.05 ?  58  ASN   A H    1 
ATOM   1456 H  HA   . ASN   A 1 58  ? 25.316 13.785  11.041  1.00 15.30 ?  58  ASN   A HA   1 
ATOM   1457 H  HB2  . ASN   A 1 58  ? 25.655 13.679  13.361  1.00 19.06 ?  58  ASN   A HB2  1 
ATOM   1458 H  HB3  . ASN   A 1 58  ? 27.175 13.293  13.113  1.00 19.06 ?  58  ASN   A HB3  1 
ATOM   1459 H  HD21 . ASN   A 1 58  ? 28.089 16.424  13.554  1.00 25.95 ?  58  ASN   A HD21 1 
ATOM   1460 H  HD22 . ASN   A 1 58  ? 28.254 15.005  13.975  1.00 25.95 ?  58  ASN   A HD22 1 
ATOM   1461 N  N    . ASN   A 1 59  ? 27.180 12.541  9.318   1.00 10.48 ?  59  ASN   A N    1 
ATOM   1462 C  CA   . ASN   A 1 59  ? 28.160 12.520  8.223   1.00 10.51 ?  59  ASN   A CA   1 
ATOM   1463 C  C    . ASN   A 1 59  ? 29.475 11.839  8.611   1.00 10.26 ?  59  ASN   A C    1 
ATOM   1464 O  O    . ASN   A 1 59  ? 30.394 11.798  7.783   1.00 10.62 ?  59  ASN   A O    1 
ATOM   1465 C  CB   . ASN   A 1 59  ? 28.447 13.906  7.614   1.00 10.94 ?  59  ASN   A CB   1 
ATOM   1466 C  CG   . ASN   A 1 59  ? 28.809 13.835  6.145   1.00 11.06 ?  59  ASN   A CG   1 
ATOM   1467 O  OD1  . ASN   A 1 59  ? 28.100 13.213  5.346   1.00 11.33 ?  59  ASN   A OD1  1 
ATOM   1468 N  ND2  . ASN   A 1 59  ? 29.897 14.502  5.768   1.00 11.60 ?  59  ASN   A ND2  1 
ATOM   1469 H  H    . ASN   A 1 59  ? 26.571 11.947  9.208   1.00 12.62 ?  59  ASN   A H    1 
ATOM   1470 H  HA   . ASN   A 1 59  ? 27.780 11.989  7.512   1.00 12.66 ?  59  ASN   A HA   1 
ATOM   1471 H  HB2  . ASN   A 1 59  ? 27.657 14.462  7.694   1.00 13.17 ?  59  ASN   A HB2  1 
ATOM   1472 H  HB3  . ASN   A 1 59  ? 29.191 14.316  8.081   1.00 13.17 ?  59  ASN   A HB3  1 
ATOM   1473 H  HD21 . ASN   A 1 59  ? 30.148 14.495  4.944   1.00 13.96 ?  59  ASN   A HD21 1 
ATOM   1474 H  HD22 . ASN   A 1 59  ? 30.370 14.929  6.351   1.00 13.96 ?  59  ASN   A HD22 1 
ATOM   1475 N  N    . ALA   A 1 60  ? 29.599 11.291  9.821   1.00 10.37 ?  60  ALA   A N    1 
ATOM   1476 C  CA   . ALA   A 1 60  ? 30.835 10.606  10.180  1.00 10.49 ?  60  ALA   A CA   1 
ATOM   1477 C  C    . ALA   A 1 60  ? 31.060 9.367   9.320   1.00 10.39 ?  60  ALA   A C    1 
ATOM   1478 O  O    . ALA   A 1 60  ? 32.204 9.041   8.984   1.00 10.91 ?  60  ALA   A O    1 
ATOM   1479 C  CB   . ALA   A 1 60  ? 30.822 10.241  11.661  1.00 11.39 ?  60  ALA   A CB   1 
ATOM   1480 H  H    . ALA   A 1 60  ? 29.000 11.300  10.435  1.00 12.49 ?  60  ALA   A H    1 
ATOM   1481 H  HA   . ALA   A 1 60  ? 31.583 11.210  10.029  1.00 12.63 ?  60  ALA   A HA   1 
ATOM   1482 H  HB1  . ALA   A 1 60  ? 31.650 9.792   11.884  1.00 13.71 ?  60  ALA   A HB1  1 
ATOM   1483 H  HB2  . ALA   A 1 60  ? 30.739 11.058  12.183  1.00 13.71 ?  60  ALA   A HB2  1 
ATOM   1484 H  HB3  . ALA   A 1 60  ? 30.067 9.661   11.835  1.00 13.71 ?  60  ALA   A HB3  1 
ATOM   1485 N  N    . MET   A 1 61  ? 29.988 8.674   8.937   1.00 9.94  ?  61  MET   A N    1 
ATOM   1486 C  CA   . MET   A 1 61  ? 30.129 7.536   8.035   1.00 9.78  ?  61  MET   A CA   1 
ATOM   1487 C  C    . MET   A 1 61  ? 30.757 7.956   6.708   1.00 9.75  ?  61  MET   A C    1 
ATOM   1488 O  O    . MET   A 1 61  ? 31.652 7.275   6.192   1.00 10.24 ?  61  MET   A O    1 
ATOM   1489 C  CB   . MET   A 1 61  ? 28.769 6.871   7.823   1.00 9.67  ?  61  MET   A CB   1 
ATOM   1490 C  CG   . MET   A 1 61  ? 28.784 5.701   6.853   1.00 10.55 ?  61  MET   A CG   1 
ATOM   1491 S  SD   . MET   A 1 61  ? 27.151 4.955   6.639   1.00 11.21 ?  61  MET   A SD   1 
ATOM   1492 C  CE   . MET   A 1 61  ? 27.010 4.062   8.192   1.00 12.68 ?  61  MET   A CE   1 
ATOM   1493 H  H    . MET   A 1 61  ? 29.179 8.845   9.174   1.00 11.98 ?  61  MET   A H    1 
ATOM   1494 H  HA   . MET   A 1 61  ? 30.708 6.883   8.453   1.00 11.77 ?  61  MET   A HA   1 
ATOM   1495 H  HB2  . MET   A 1 61  ? 28.450 6.538   8.675   1.00 11.64 ?  61  MET   A HB2  1 
ATOM   1496 H  HB3  . MET   A 1 61  ? 28.148 7.528   7.475   1.00 11.64 ?  61  MET   A HB3  1 
ATOM   1497 H  HG2  . MET   A 1 61  ? 29.076 6.004   5.981   1.00 12.71 ?  61  MET   A HG2  1 
ATOM   1498 H  HG3  . MET   A 1 61  ? 29.379 5.013   7.187   1.00 12.71 ?  61  MET   A HG3  1 
ATOM   1499 H  HE1  . MET   A 1 61  ? 26.164 3.585   8.208   1.00 15.26 ?  61  MET   A HE1  1 
ATOM   1500 H  HE2  . MET   A 1 61  ? 27.744 3.434   8.263   1.00 15.26 ?  61  MET   A HE2  1 
ATOM   1501 H  HE3  . MET   A 1 61  ? 27.043 4.696   8.928   1.00 15.26 ?  61  MET   A HE3  1 
ATOM   1502 N  N    . GLN   A 1 62  ? 30.318 9.088   6.151   1.00 9.83  ?  62  GLN   A N    1 
ATOM   1503 C  CA   . GLN   A 1 62  ? 30.880 9.560   4.888   1.00 9.85  ?  62  GLN   A CA   1 
ATOM   1504 C  C    . GLN   A 1 62  ? 32.348 9.939   5.035   1.00 9.84  ?  62  GLN   A C    1 
ATOM   1505 O  O    . GLN   A 1 62  ? 33.160 9.627   4.156   1.00 10.26 ?  62  GLN   A O    1 
ATOM   1506 C  CB   . GLN   A 1 62  ? 30.073 10.738  4.349   1.00 10.00 ?  62  GLN   A CB   1 
ATOM   1507 C  CG   . GLN   A 1 62  ? 30.461 11.101  2.925   1.00 10.05 ?  62  GLN   A CG   1 
ATOM   1508 C  CD   . GLN   A 1 62  ? 30.131 9.975   1.977   1.00 10.00 ?  62  GLN   A CD   1 
ATOM   1509 O  OE1  . GLN   A 1 62  ? 28.953 9.665   1.768   1.00 10.63 ?  62  GLN   A OE1  1 
ATOM   1510 N  NE2  . GLN   A 1 62  ? 31.153 9.301   1.456   1.00 10.91 ?  62  GLN   A NE2  1 
ATOM   1511 H  H    . GLN   A 1 62  ? 29.698 9.584   6.477   1.00 11.84 ?  62  GLN   A H    1 
ATOM   1512 H  HA   . GLN   A 1 62  ? 30.829 8.839   4.241   1.00 11.87 ?  62  GLN   A HA   1 
ATOM   1513 H  HB2  . GLN   A 1 62  ? 29.132 10.513  4.358   1.00 12.04 ?  62  GLN   A HB2  1 
ATOM   1514 H  HB3  . GLN   A 1 62  ? 30.236 11.517  4.909   1.00 12.04 ?  62  GLN   A HB3  1 
ATOM   1515 H  HG2  . GLN   A 1 62  ? 29.963 11.883  2.644   1.00 12.10 ?  62  GLN   A HG2  1 
ATOM   1516 H  HG3  . GLN   A 1 62  ? 31.414 11.272  2.878   1.00 12.10 ?  62  GLN   A HG3  1 
ATOM   1517 H  HE21 . GLN   A 1 62  ? 31.962 9.534   1.642   1.00 13.14 ?  62  GLN   A HE21 1 
ATOM   1518 H  HE22 . GLN   A 1 62  ? 31.009 8.645   0.920   1.00 13.14 ?  62  GLN   A HE22 1 
ATOM   1519 N  N    . VAL   A 1 63  ? 32.707 10.629  6.121   1.00 10.36 ?  63  VAL   A N    1 
ATOM   1520 C  CA   . VAL   A 1 63  ? 34.101 11.015  6.338   1.00 11.18 ?  63  VAL   A CA   1 
ATOM   1521 C  C    . VAL   A 1 63  ? 34.998 9.779   6.398   1.00 10.64 ?  63  VAL   A C    1 
ATOM   1522 O  O    . VAL   A 1 63  ? 36.051 9.714   5.746   1.00 11.30 ?  63  VAL   A O    1 
ATOM   1523 C  CB   . VAL   A 1 63  ? 34.213 11.883  7.605   1.00 12.65 ?  63  VAL   A CB   1 
ATOM   1524 C  CG1  . VAL   A 1 63  ? 35.661 12.119  7.963   1.00 14.35 ?  63  VAL   A CG1  1 
ATOM   1525 C  CG2  . VAL   A 1 63  ? 33.485 13.210  7.396   1.00 13.37 ?  63  VAL   A CG2  1 
ATOM   1526 H  H    . VAL   A 1 63  ? 32.160 10.888  6.740   1.00 12.47 ?  63  VAL   A H    1 
ATOM   1527 H  HA   . VAL   A 1 63  ? 34.387 11.557  5.588   1.00 13.46 ?  63  VAL   A HA   1 
ATOM   1528 H  HB   . VAL   A 1 63  ? 33.792 11.423  8.347   1.00 15.23 ?  63  VAL   A HB   1 
ATOM   1529 H  HG11 . VAL   A 1 63  ? 35.714 12.853  8.596   1.00 17.26 ?  63  VAL   A HG11 1 
ATOM   1530 H  HG12 . VAL   A 1 63  ? 36.028 11.315  8.357   1.00 17.26 ?  63  VAL   A HG12 1 
ATOM   1531 H  HG13 . VAL   A 1 63  ? 36.152 12.349  7.155   1.00 17.26 ?  63  VAL   A HG13 1 
ATOM   1532 H  HG21 . VAL   A 1 63  ? 33.579 13.754  8.197   1.00 16.09 ?  63  VAL   A HG21 1 
ATOM   1533 H  HG22 . VAL   A 1 63  ? 33.877 13.674  6.639   1.00 16.09 ?  63  VAL   A HG22 1 
ATOM   1534 H  HG23 . VAL   A 1 63  ? 32.546 13.036  7.227   1.00 16.09 ?  63  VAL   A HG23 1 
ATOM   1535 N  N    . GLU   A 1 64  ? 34.582 8.774   7.171   1.00 10.65 ?  64  GLU   A N    1 
ATOM   1536 C  CA   . GLU   A 1 64  ? 35.339 7.534   7.268   1.00 10.50 ?  64  GLU   A CA   1 
ATOM   1537 C  C    . GLU   A 1 64  ? 35.421 6.841   5.915   1.00 10.07 ?  64  GLU   A C    1 
ATOM   1538 O  O    . GLU   A 1 64  ? 36.471 6.299   5.536   1.00 10.81 ?  64  GLU   A O    1 
ATOM   1539 C  CB   . GLU   A 1 64  ? 34.646 6.623   8.282   1.00 11.03 ?  64  GLU   A CB   1 
ATOM   1540 C  CG   . GLU   A 1 64  ? 35.292 5.269   8.428   1.00 11.84 ?  64  GLU   A CG   1 
ATOM   1541 C  CD   . GLU   A 1 64  ? 34.408 4.279   9.166   1.00 12.35 ?  64  GLU   A CD   1 
ATOM   1542 O  OE1  . GLU   A 1 64  ? 33.169 4.373   9.030   1.00 13.21 ?  64  GLU   A OE1  1 
ATOM   1543 O  OE2  . GLU   A 1 64  ? 34.951 3.389   9.863   1.00 12.63 -1 64  GLU   A OE2  1 
ATOM   1544 H  H    . GLU   A 1 64  ? 33.854 8.782   7.628   1.00 12.83 ?  64  GLU   A H    1 
ATOM   1545 H  HA   . GLU   A 1 64  ? 36.237 7.729   7.585   1.00 12.65 ?  64  GLU   A HA   1 
ATOM   1546 H  HB2  . GLU   A 1 64  ? 34.666 7.057   9.155   1.00 13.27 ?  64  GLU   A HB2  1 
ATOM   1547 H  HB3  . GLU   A 1 64  ? 33.726 6.496   8.005   1.00 13.27 ?  64  GLU   A HB3  1 
ATOM   1548 H  HG2  . GLU   A 1 64  ? 35.478 4.899   7.546   1.00 14.25 ?  64  GLU   A HG2  1 
ATOM   1549 H  HG3  . GLU   A 1 64  ? 36.117 5.365   8.923   1.00 14.25 ?  64  GLU   A HG3  1 
ATOM   1550 N  N    . SER   A 1 65  ? 34.305 6.835   5.181   1.00 9.98  ?  65  SER   A N    1 
ATOM   1551 C  CA   . SER   A 1 65  ? 34.257 6.174   3.880   1.00 10.15 ?  65  SER   A CA   1 
ATOM   1552 C  C    . SER   A 1 65  ? 35.180 6.841   2.866   1.00 10.30 ?  65  SER   A C    1 
ATOM   1553 O  O    . SER   A 1 65  ? 35.820 6.158   2.057   1.00 11.22 ?  65  SER   A O    1 
ATOM   1554 C  CB   . SER   A 1 65  ? 32.825 6.179   3.348   1.00 10.02 ?  65  SER   A CB   1 
ATOM   1555 O  OG   . SER   A 1 65  ? 31.978 5.366   4.150   1.00 10.63 ?  65  SER   A OG   1 
ATOM   1556 H  H    . SER   A 1 65  ? 33.574 7.219   5.412   1.00 12.02 ?  65  SER   A H    1 
ATOM   1557 H  HA   . SER   A 1 65  ? 34.541 5.256   3.981   1.00 12.22 ?  65  SER   A HA   1 
ATOM   1558 H  HB2  . SER   A 1 65  ? 32.484 7.086   3.358   1.00 12.07 ?  65  SER   A HB2  1 
ATOM   1559 H  HB3  . SER   A 1 65  ? 32.823 5.832   2.444   1.00 12.07 ?  65  SER   A HB3  1 
ATOM   1560 H  HG   . SER   A 1 65  ? 31.974 5.652   4.947   1.00 12.79 ?  65  SER   A HG   1 
ATOM   1561 N  N    . ASP   A 1 66  ? 35.255 8.176   2.879   1.00 10.19 ?  66  ASP   A N    1 
ATOM   1562 C  CA   . ASP   A 1 66  ? 36.120 8.869   1.928   1.00 11.25 ?  66  ASP   A CA   1 
ATOM   1563 C  C    . ASP   A 1 66  ? 37.583 8.514   2.168   1.00 11.04 ?  66  ASP   A C    1 
ATOM   1564 O  O    . ASP   A 1 66  ? 38.356 8.337   1.218   1.00 12.17 ?  66  ASP   A O    1 
ATOM   1565 C  CB   . ASP   A 1 66  ? 35.903 10.378  2.033   1.00 12.51 ?  66  ASP   A CB   1 
ATOM   1566 C  CG   . ASP   A 1 66  ? 34.561 10.835  1.447   1.00 14.05 ?  66  ASP   A CG   1 
ATOM   1567 O  OD1  . ASP   A 1 66  ? 33.846 10.035  0.803   1.00 14.30 ?  66  ASP   A OD1  1 
ATOM   1568 O  OD2  . ASP   A 1 66  ? 34.261 12.037  1.602   1.00 17.24 -1 66  ASP   A OD2  1 
ATOM   1569 H  H    . ASP   A 1 66  ? 34.812 8.693   3.408   1.00 12.28 ?  66  ASP   A H    1 
ATOM   1570 H  HA   . ASP   A 1 66  ? 35.884 8.597   1.027   1.00 13.55 ?  66  ASP   A HA   1 
ATOM   1571 H  HB2  . ASP   A 1 66  ? 35.917 10.637  2.966   1.00 15.06 ?  66  ASP   A HB2  1 
ATOM   1572 H  HB3  . ASP   A 1 66  ? 36.617 10.832  1.553   1.00 15.06 ?  66  ASP   A HB3  1 
ATOM   1573 N  N    . ASP   A 1 67  ? 37.978 8.387   3.435   1.00 11.49 ?  67  ASP   A N    1 
ATOM   1574 C  CA   . ASP   A 1 67  ? 39.333 7.938   3.742   1.00 12.20 ?  67  ASP   A CA   1 
ATOM   1575 C  C    . ASP   A 1 67  ? 39.554 6.502   3.278   1.00 12.21 ?  67  ASP   A C    1 
ATOM   1576 O  O    . ASP   A 1 67  ? 40.612 6.175   2.729   1.00 12.85 ?  67  ASP   A O    1 
ATOM   1577 C  CB   . ASP   A 1 67  ? 39.599 8.073   5.240   1.00 13.65 ?  67  ASP   A CB   1 
ATOM   1578 C  CG   . ASP   A 1 67  ? 40.894 7.419   5.661   1.00 14.85 ?  67  ASP   A CG   1 
ATOM   1579 O  OD1  . ASP   A 1 67  ? 41.966 8.043   5.500   1.00 17.78 ?  67  ASP   A OD1  1 
ATOM   1580 O  OD2  . ASP   A 1 67  ? 40.849 6.264   6.138   1.00 14.62 -1 67  ASP   A OD2  1 
ATOM   1581 H  H    . ASP   A 1 67  ? 37.491 8.548   4.122   1.00 13.83 ?  67  ASP   A H    1 
ATOM   1582 H  HA   . ASP   A 1 67  ? 39.966 8.500   3.271   1.00 14.68 ?  67  ASP   A HA   1 
ATOM   1583 H  HB2  . ASP   A 1 67  ? 39.647 9.007   5.465   1.00 16.43 ?  67  ASP   A HB2  1 
ATOM   1584 H  HB3  . ASP   A 1 67  ? 38.875 7.643   5.725   1.00 16.43 ?  67  ASP   A HB3  1 
ATOM   1585 N  N    . TYR   A 1 68  ? 38.558 5.630   3.470   1.00 11.70 ?  68  TYR   A N    1 
ATOM   1586 C  CA   . TYR   A 1 68  ? 38.676 4.250   2.995   1.00 11.62 ?  68  TYR   A CA   1 
ATOM   1587 C  C    . TYR   A 1 68  ? 38.918 4.200   1.487   1.00 11.50 ?  68  TYR   A C    1 
ATOM   1588 O  O    . TYR   A 1 68  ? 39.795 3.466   1.015   1.00 12.32 ?  68  TYR   A O    1 
ATOM   1589 C  CB   . TYR   A 1 68  ? 37.428 3.423   3.384   1.00 11.99 ?  68  TYR   A CB   1 
ATOM   1590 C  CG   . TYR   A 1 68  ? 37.449 2.035   2.755   1.00 13.47 ?  68  TYR   A CG   1 
ATOM   1591 C  CD1  . TYR   A 1 68  ? 36.988 1.845   1.456   1.00 14.70 ?  68  TYR   A CD1  1 
ATOM   1592 C  CD2  . TYR   A 1 68  ? 37.985 0.944   3.422   1.00 15.35 ?  68  TYR   A CD2  1 
ATOM   1593 C  CE1  . TYR   A 1 68  ? 37.051 0.632   0.833   1.00 15.94 ?  68  TYR   A CE1  1 
ATOM   1594 C  CE2  . TYR   A 1 68  ? 38.042 -0.313  2.799   1.00 16.03 ?  68  TYR   A CE2  1 
ATOM   1595 C  CZ   . TYR   A 1 68  ? 37.575 -0.444  1.504   1.00 16.28 ?  68  TYR   A CZ   1 
ATOM   1596 O  OH   . TYR   A 1 68  ? 37.649 -1.656  0.869   1.00 17.33 ?  68  TYR   A OH   1 
ATOM   1597 H  H    . TYR   A 1 68  ? 37.811 5.809   3.860   1.00 14.08 ?  68  TYR   A H    1 
ATOM   1598 H  HA   . TYR   A 1 68  ? 39.437 3.841   3.425   1.00 13.98 ?  68  TYR   A HA   1 
ATOM   1599 H  HB2  . TYR   A 1 68  ? 37.405 3.317   4.347   1.00 14.43 ?  68  TYR   A HB2  1 
ATOM   1600 H  HB3  . TYR   A 1 68  ? 36.630 3.883   3.077   1.00 14.43 ?  68  TYR   A HB3  1 
ATOM   1601 H  HD1  . TYR   A 1 68  ? 36.642 2.578   0.993   1.00 17.68 ?  68  TYR   A HD1  1 
ATOM   1602 H  HD2  . TYR   A 1 68  ? 38.319 1.049   4.280   1.00 18.47 ?  68  TYR   A HD2  1 
ATOM   1603 H  HE1  . TYR   A 1 68  ? 36.725 0.537   -0.032  1.00 19.17 ?  68  TYR   A HE1  1 
ATOM   1604 H  HE2  . TYR   A 1 68  ? 38.406 -1.046  3.235   1.00 19.28 ?  68  TYR   A HE2  1 
ATOM   1605 H  HH   . TYR   A 1 68  ? 37.979 -2.227  1.393   1.00 20.84 ?  68  TYR   A HH   1 
ATOM   1606 N  N    . ILE   A 1 69  ? 38.130 4.955   0.709   1.00 11.09 ?  69  ILE   A N    1 
ATOM   1607 C  CA   . ILE   A 1 69  ? 38.267 4.933   -0.747  1.00 11.14 ?  69  ILE   A CA   1 
ATOM   1608 C  C    . ILE   A 1 69  ? 39.601 5.542   -1.176  1.00 11.05 ?  69  ILE   A C    1 
ATOM   1609 O  O    . ILE   A 1 69  ? 40.248 5.062   -2.113  1.00 11.64 ?  69  ILE   A O    1 
ATOM   1610 C  CB   . ILE   A 1 69  ? 37.070 5.643   -1.412  1.00 12.13 ?  69  ILE   A CB   1 
ATOM   1611 C  CG1  . ILE   A 1 69  ? 35.757 4.920   -1.122  1.00 12.29 ?  69  ILE   A CG1  1 
ATOM   1612 C  CG2  . ILE   A 1 69  ? 37.301 5.818   -2.918  1.00 13.61 ?  69  ILE   A CG2  1 
ATOM   1613 C  CD1  . ILE   A 1 69  ? 35.586 3.630   -1.884  1.00 13.25 ?  69  ILE   A CD1  1 
ATOM   1614 H  H    . ILE   A 1 69  ? 37.517 5.482   0.999   1.00 13.35 ?  69  ILE   A H    1 
ATOM   1615 H  HA   . ILE   A 1 69  ? 38.264 4.009   -1.044  1.00 13.41 ?  69  ILE   A HA   1 
ATOM   1616 H  HB   . ILE   A 1 69  ? 37.008 6.527   -1.028  1.00 14.60 ?  69  ILE   A HB   1 
ATOM   1617 H  HG12 . ILE   A 1 69  ? 35.720 4.712   -0.174  1.00 14.79 ?  69  ILE   A HG12 1 
ATOM   1618 H  HG13 . ILE   A 1 69  ? 35.022 5.506   -1.356  1.00 14.79 ?  69  ILE   A HG13 1 
ATOM   1619 H  HG21 . ILE   A 1 69  ? 36.454 6.032   -3.344  1.00 16.37 ?  69  ILE   A HG21 1 
ATOM   1620 H  HG22 . ILE   A 1 69  ? 37.930 6.546   -3.063  1.00 16.37 ?  69  ILE   A HG22 1 
ATOM   1621 H  HG23 . ILE   A 1 69  ? 37.655 4.996   -3.287  1.00 16.37 ?  69  ILE   A HG23 1 
ATOM   1622 H  HD11 . ILE   A 1 69  ? 34.798 3.176   -1.551  1.00 15.94 ?  69  ILE   A HD11 1 
ATOM   1623 H  HD12 . ILE   A 1 69  ? 35.476 3.835   -2.826  1.00 15.94 ?  69  ILE   A HD12 1 
ATOM   1624 H  HD13 . ILE   A 1 69  ? 36.370 3.078   -1.753  1.00 15.94 ?  69  ILE   A HD13 1 
ATOM   1625 N  N    . ALA   A 1 70  ? 40.019 6.624   -0.520  1.00 11.64 ?  70  ALA   A N    1 
ATOM   1626 C  CA   . ALA   A 1 70  ? 41.298 7.233   -0.875  1.00 12.47 ?  70  ALA   A CA   1 
ATOM   1627 C  C    . ALA   A 1 70  ? 42.448 6.252   -0.701  1.00 12.78 ?  70  ALA   A C    1 
ATOM   1628 O  O    . ALA   A 1 70  ? 43.414 6.284   -1.468  1.00 14.52 ?  70  ALA   A O    1 
ATOM   1629 C  CB   . ALA   A 1 70  ? 41.541 8.488   -0.035  1.00 13.17 ?  70  ALA   A CB   1 
ATOM   1630 H  H    . ALA   A 1 70  ? 39.591 7.019   0.107   1.00 14.01 ?  70  ALA   A H    1 
ATOM   1631 H  HA   . ALA   A 1 70  ? 41.275 7.503   -1.809  1.00 15.00 ?  70  ALA   A HA   1 
ATOM   1632 H  HB1  . ALA   A 1 70  ? 42.399 8.872   -0.286  1.00 15.85 ?  70  ALA   A HB1  1 
ATOM   1633 H  HB2  . ALA   A 1 70  ? 40.833 9.124   -0.200  1.00 15.85 ?  70  ALA   A HB2  1 
ATOM   1634 H  HB3  . ALA   A 1 70  ? 41.556 8.239   0.903   1.00 15.85 ?  70  ALA   A HB3  1 
ATOM   1635 N  N    . THR   A 1 71  ? 42.342 5.352   0.275   1.00 12.14 ?  71  THR   A N    1 
ATOM   1636 C  CA   . THR   A 1 71  ? 43.395 4.371   0.521   1.00 13.75 ?  71  THR   A CA   1 
ATOM   1637 C  C    . THR   A 1 71  ? 43.270 3.147   -0.375  1.00 13.74 ?  71  THR   A C    1 
ATOM   1638 O  O    . THR   A 1 71  ? 44.282 2.634   -0.875  1.00 15.76 ?  71  THR   A O    1 
ATOM   1639 C  CB   . THR   A 1 71  ? 43.329 3.917   1.975   1.00 15.96 ?  71  THR   A CB   1 
ATOM   1640 O  OG1  . THR   A 1 71  ? 43.569 5.041   2.826   1.00 17.40 ?  71  THR   A OG1  1 
ATOM   1641 C  CG2  . THR   A 1 71  ? 44.348 2.816   2.257   1.00 17.48 ?  71  THR   A CG2  1 
ATOM   1642 H  H    . THR   A 1 71  ? 41.666 5.278   0.802   1.00 14.61 ?  71  THR   A H    1 
ATOM   1643 H  HA   . THR   A 1 71  ? 44.259 4.775   0.359   1.00 16.54 ?  71  THR   A HA   1 
ATOM   1644 H  HB   . THR   A 1 71  ? 42.444 3.553   2.152   1.00 19.20 ?  71  THR   A HB   1 
ATOM   1645 H  HG1  . THR   A 1 71  ? 43.530 4.792   3.627   1.00 20.93 ?  71  THR   A HG1  1 
ATOM   1646 H  HG21 . THR   A 1 71  ? 44.486 2.732   3.213   1.00 21.02 ?  71  THR   A HG21 1 
ATOM   1647 H  HG22 . THR   A 1 71  ? 44.040 1.965   1.908   1.00 21.02 ?  71  THR   A HG22 1 
ATOM   1648 H  HG23 . THR   A 1 71  ? 45.199 3.037   1.839   1.00 21.02 ?  71  THR   A HG23 1 
ATOM   1649 N  N    . ASN   A 1 72  ? 42.044 2.643   -0.559  1.00 12.71 ?  72  ASN   A N    1 
ATOM   1650 C  CA   . ASN   A 1 72  ? 41.825 1.315   -1.117  1.00 13.14 ?  72  ASN   A CA   1 
ATOM   1651 C  C    . ASN   A 1 72  ? 41.199 1.298   -2.499  1.00 13.35 ?  72  ASN   A C    1 
ATOM   1652 O  O    . ASN   A 1 72  ? 41.201 0.241   -3.141  1.00 14.67 ?  72  ASN   A O    1 
ATOM   1653 C  CB   . ASN   A 1 72  ? 40.943 0.491   -0.172  1.00 14.19 ?  72  ASN   A CB   1 
ATOM   1654 C  CG   . ASN   A 1 72  ? 41.559 0.342   1.193   1.00 15.35 ?  72  ASN   A CG   1 
ATOM   1655 O  OD1  . ASN   A 1 72  ? 41.103 0.939   2.167   1.00 16.89 ?  72  ASN   A OD1  1 
ATOM   1656 N  ND2  . ASN   A 1 72  ? 42.618 -0.437  1.269   1.00 15.62 ?  72  ASN   A ND2  1 
ATOM   1657 H  H    . ASN   A 1 72  ? 41.313 3.065   -0.374  1.00 15.29 ?  72  ASN   A H    1 
ATOM   1658 H  HA   . ASN   A 1 72  ? 42.680 0.869   -1.189  1.00 15.82 ?  72  ASN   A HA   1 
ATOM   1659 H  HB2  . ASN   A 1 72  ? 40.086 0.928   -0.075  1.00 17.07 ?  72  ASN   A HB2  1 
ATOM   1660 H  HB3  . ASN   A 1 72  ? 40.825 -0.397  -0.550  1.00 17.07 ?  72  ASN   A HB3  1 
ATOM   1661 H  HD21 . ASN   A 1 72  ? 43.014 -0.550  2.024   1.00 18.79 ?  72  ASN   A HD21 1 
ATOM   1662 H  HD22 . ASN   A 1 72  ? 42.919 -0.829  0.564   1.00 18.79 ?  72  ASN   A HD22 1 
ATOM   1663 N  N    . GLY   A 1 73  ? 40.655 2.413   -2.968  1.00 12.74 ?  73  GLY   A N    1 
ATOM   1664 C  CA   . GLY   A 1 73  ? 39.915 2.424   -4.204  1.00 12.50 ?  73  GLY   A CA   1 
ATOM   1665 C  C    . GLY   A 1 73  ? 38.523 1.849   -4.030  1.00 12.11 ?  73  GLY   A C    1 
ATOM   1666 O  O    . GLY   A 1 73  ? 38.138 1.397   -2.944  1.00 12.66 ?  73  GLY   A O    1 
ATOM   1667 H  H    . GLY   A 1 73  ? 40.708 3.190   -2.590  1.00 15.33 ?  73  GLY   A H    1 
ATOM   1668 H  HA2  . GLY   A 1 73  ? 39.835 3.339   -4.526  1.00 15.04 ?  73  GLY   A HA2  1 
ATOM   1669 H  HA3  . GLY   A 1 73  ? 40.389 1.905   -4.874  1.00 15.04 ?  73  GLY   A HA3  1 
ATOM   1670 N  N    . PRO   A 1 74  ? 37.746 1.860   -5.112  1.00 12.64 ?  74  PRO   A N    1 
ATOM   1671 C  CA   . PRO   A 1 74  ? 36.347 1.431   -5.032  1.00 12.67 ?  74  PRO   A CA   1 
ATOM   1672 C  C    . PRO   A 1 74  ? 36.197 -0.052  -4.718  1.00 11.96 ?  74  PRO   A C    1 
ATOM   1673 O  O    . PRO   A 1 74  ? 37.070 -0.880  -4.998  1.00 12.90 ?  74  PRO   A O    1 
ATOM   1674 C  CB   . PRO   A 1 74  ? 35.801 1.742   -6.432  1.00 14.32 ?  74  PRO   A CB   1 
ATOM   1675 C  CG   . PRO   A 1 74  ? 36.758 2.714   -7.037  1.00 17.17 ?  74  PRO   A CG   1 
ATOM   1676 C  CD   . PRO   A 1 74  ? 38.092 2.388   -6.442  1.00 14.74 ?  74  PRO   A CD   1 
ATOM   1677 H  HA   . PRO   A 1 74  ? 35.864 1.956   -4.369  1.00 15.25 ?  74  PRO   A HA   1 
ATOM   1678 H  HB2  . PRO   A 1 74  ? 35.758 0.925   -6.951  1.00 17.23 ?  74  PRO   A HB2  1 
ATOM   1679 H  HB3  . PRO   A 1 74  ? 34.914 2.140   -6.352  1.00 17.23 ?  74  PRO   A HB3  1 
ATOM   1680 H  HG2  . PRO   A 1 74  ? 36.778 2.595   -7.999  1.00 20.64 ?  74  PRO   A HG2  1 
ATOM   1681 H  HG3  . PRO   A 1 74  ? 36.497 3.618   -6.808  1.00 20.64 ?  74  PRO   A HG3  1 
ATOM   1682 H  HD2  . PRO   A 1 74  ? 38.547 1.709   -6.968  1.00 17.74 ?  74  PRO   A HD2  1 
ATOM   1683 H  HD3  . PRO   A 1 74  ? 38.630 3.196   -6.370  1.00 17.74 ?  74  PRO   A HD3  1 
ATOM   1684 N  N    . LEU   A 1 75  ? 35.051 -0.377  -4.126  1.00 11.22 ?  75  LEU   A N    1 
ATOM   1685 C  CA   . LEU   A 1 75  ? 34.652 -1.766  -3.970  1.00 11.03 ?  75  LEU   A CA   1 
ATOM   1686 C  C    . LEU   A 1 75  ? 34.264 -2.349  -5.327  1.00 11.56 ?  75  LEU   A C    1 
ATOM   1687 O  O    . LEU   A 1 75  ? 34.140 -1.638  -6.329  1.00 13.02 ?  75  LEU   A O    1 
ATOM   1688 C  CB   . LEU   A 1 75  ? 33.468 -1.888  -3.011  1.00 11.31 ?  75  LEU   A CB   1 
ATOM   1689 C  CG   . LEU   A 1 75  ? 33.685 -1.466  -1.558  1.00 12.49 ?  75  LEU   A CG   1 
ATOM   1690 C  CD1  . LEU   A 1 75  ? 32.399 -1.645  -0.763  1.00 14.61 ?  75  LEU   A CD1  1 
ATOM   1691 C  CD2  . LEU   A 1 75  ? 34.813 -2.193  -0.895  1.00 15.84 ?  75  LEU   A CD2  1 
ATOM   1692 H  H    . LEU   A 1 75  ? 34.487 0.193   -3.811  1.00 13.51 ?  75  LEU   A H    1 
ATOM   1693 H  HA   . LEU   A 1 75  ? 35.394 -2.275  -3.620  1.00 13.27 ?  75  LEU   A HA   1 
ATOM   1694 H  HB2  . LEU   A 1 75  ? 32.742 -1.349  -3.358  1.00 13.61 ?  75  LEU   A HB2  1 
ATOM   1695 H  HB3  . LEU   A 1 75  ? 33.193 -2.820  -2.999  1.00 13.61 ?  75  LEU   A HB3  1 
ATOM   1696 H  HG   . LEU   A 1 75  ? 33.910 -0.523  -1.546  1.00 15.03 ?  75  LEU   A HG   1 
ATOM   1697 H  HD11 . LEU   A 1 75  ? 32.556 -1.368  0.154   1.00 17.58 ?  75  LEU   A HD11 1 
ATOM   1698 H  HD12 . LEU   A 1 75  ? 31.709 -1.091  -1.161  1.00 17.58 ?  75  LEU   A HD12 1 
ATOM   1699 H  HD13 . LEU   A 1 75  ? 32.137 -2.575  -0.791  1.00 17.58 ?  75  LEU   A HD13 1 
ATOM   1700 H  HD21 . LEU   A 1 75  ? 34.874 -1.912  0.032   1.00 19.05 ?  75  LEU   A HD21 1 
ATOM   1701 H  HD22 . LEU   A 1 75  ? 34.652 -3.148  -0.941  1.00 19.05 ?  75  LEU   A HD22 1 
ATOM   1702 H  HD23 . LEU   A 1 75  ? 35.647 -1.980  -1.354  1.00 19.05 ?  75  LEU   A HD23 1 
ATOM   1703 N  N    . LYS   A 1 76  ? 34.083 -3.668  -5.344  1.00 11.72 ?  76  LYS   A N    1 
ATOM   1704 C  CA   . LYS   A 1 76  ? 33.490 -4.388  -6.464  1.00 12.38 ?  76  LYS   A CA   1 
ATOM   1705 C  C    . LYS   A 1 76  ? 31.978 -4.470  -6.275  1.00 11.04 ?  76  LYS   A C    1 
ATOM   1706 O  O    . LYS   A 1 76  ? 31.494 -4.583  -5.151  1.00 11.11 ?  76  LYS   A O    1 
ATOM   1707 C  CB   . LYS   A 1 76  ? 34.039 -5.826  -6.513  1.00 13.94 ?  76  LYS   A CB   1 
ATOM   1708 C  CG   . LYS   A 1 76  ? 35.548 -5.937  -6.713  1.00 15.32 ?  76  LYS   A CG   1 
ATOM   1709 C  CD   . LYS   A 1 76  ? 36.073 -7.341  -6.499  1.00 16.68 ?  76  LYS   A CD   1 
ATOM   1710 C  CE   . LYS   A 1 76  ? 37.574 -7.398  -6.687  1.00 19.12 ?  76  LYS   A CE   1 
ATOM   1711 N  NZ   . LYS   A 1 76  ? 38.114 -8.760  -6.499  1.00 20.13 ?  76  LYS   A NZ   1 
ATOM   1712 H  H    . LYS   A 1 76  ? 34.306 -4.184  -4.690  1.00 14.11 ?  76  LYS   A H    1 
ATOM   1713 H  HA   . LYS   A 1 76  ? 33.693 -3.937  -7.300  1.00 14.90 ?  76  LYS   A HA   1 
ATOM   1714 H  HB2  . LYS   A 1 76  ? 33.820 -6.265  -5.677  1.00 16.77 ?  76  LYS   A HB2  1 
ATOM   1715 H  HB3  . LYS   A 1 76  ? 33.610 -6.291  -7.248  1.00 16.77 ?  76  LYS   A HB3  1 
ATOM   1716 H  HG2  . LYS   A 1 76  ? 35.766 -5.670  -7.620  1.00 18.42 ?  76  LYS   A HG2  1 
ATOM   1717 H  HG3  . LYS   A 1 76  ? 35.995 -5.352  -6.080  1.00 18.42 ?  76  LYS   A HG3  1 
ATOM   1718 H  HD2  . LYS   A 1 76  ? 35.865 -7.629  -5.595  1.00 20.05 ?  76  LYS   A HD2  1 
ATOM   1719 H  HD3  . LYS   A 1 76  ? 35.661 -7.940  -7.144  1.00 20.05 ?  76  LYS   A HD3  1 
ATOM   1720 H  HE2  . LYS   A 1 76  ? 37.791 -7.107  -7.585  1.00 22.99 ?  76  LYS   A HE2  1 
ATOM   1721 H  HE3  . LYS   A 1 76  ? 37.994 -6.816  -6.035  1.00 22.99 ?  76  LYS   A HE3  1 
ATOM   1722 H  HZ1  . LYS   A 1 76  ? 38.995 -8.762  -6.617  1.00 24.19 ?  76  LYS   A HZ1  1 
ATOM   1723 H  HZ2  . LYS   A 1 76  ? 37.931 -9.056  -5.678  1.00 24.19 ?  76  LYS   A HZ2  1 
ATOM   1724 H  HZ3  . LYS   A 1 76  ? 37.745 -9.321  -7.091  1.00 24.19 ?  76  LYS   A HZ3  1 
ATOM   1725 N  N    . VAL   A 1 77  ? 31.228 -4.435  -7.383  1.00 11.49 ?  77  VAL   A N    1 
ATOM   1726 C  CA   . VAL   A 1 77  ? 29.821 -4.823  -7.302  1.00 11.31 ?  77  VAL   A CA   1 
ATOM   1727 C  C    . VAL   A 1 77  ? 29.758 -6.276  -6.851  1.00 10.97 ?  77  VAL   A C    1 
ATOM   1728 O  O    . VAL   A 1 77  ? 30.418 -7.147  -7.427  1.00 11.42 ?  77  VAL   A O    1 
ATOM   1729 C  CB   . VAL   A 1 77  ? 29.097 -4.611  -8.640  1.00 12.41 ?  77  VAL   A CB   1 
ATOM   1730 C  CG1  . VAL   A 1 77  ? 27.637 -5.039  -8.518  1.00 13.39 ?  77  VAL   A CG1  1 
ATOM   1731 C  CG2  . VAL   A 1 77  ? 29.186 -3.155  -9.072  1.00 13.81 ?  77  VAL   A CG2  1 
ATOM   1732 H  H    . VAL   A 1 77  ? 31.509 -4.198  -8.162  1.00 13.83 ?  77  VAL   A H    1 
ATOM   1733 H  HA   . VAL   A 1 77  ? 29.386 -4.281  -6.631  1.00 13.61 ?  77  VAL   A HA   1 
ATOM   1734 H  HB   . VAL   A 1 77  ? 29.520 -5.155  -9.323  1.00 14.93 ?  77  VAL   A HB   1 
ATOM   1735 H  HG11 . VAL   A 1 77  ? 27.163 -4.761  -9.317  1.00 16.12 ?  77  VAL   A HG11 1 
ATOM   1736 H  HG12 . VAL   A 1 77  ? 27.593 -6.002  -8.426  1.00 16.12 ?  77  VAL   A HG12 1 
ATOM   1737 H  HG13 . VAL   A 1 77  ? 27.249 -4.612  -7.739  1.00 16.12 ?  77  VAL   A HG13 1 
ATOM   1738 H  HG21 . VAL   A 1 77  ? 28.676 -3.040  -9.888  1.00 16.62 ?  77  VAL   A HG21 1 
ATOM   1739 H  HG22 . VAL   A 1 77  ? 28.816 -2.598  -8.368  1.00 16.62 ?  77  VAL   A HG22 1 
ATOM   1740 H  HG23 . VAL   A 1 77  ? 30.115 -2.926  -9.223  1.00 16.62 ?  77  VAL   A HG23 1 
ATOM   1741 N  N    . GLY   A 1 78  ? 28.972 -6.543  -5.803  1.00 10.69 ?  78  GLY   A N    1 
ATOM   1742 C  CA   . GLY   A 1 78  ? 28.949 -7.833  -5.142  1.00 10.96 ?  78  GLY   A CA   1 
ATOM   1743 C  C    . GLY   A 1 78  ? 29.865 -7.925  -3.942  1.00 10.54 ?  78  GLY   A C    1 
ATOM   1744 O  O    . GLY   A 1 78  ? 29.805 -8.925  -3.210  1.00 11.01 ?  78  GLY   A O    1 
ATOM   1745 H  H    . GLY   A 1 78  ? 28.425 -5.970  -5.462  1.00 12.87 ?  78  GLY   A H    1 
ATOM   1746 H  HA2  . GLY   A 1 78  ? 28.046 -8.019  -4.851  1.00 13.19 ?  78  GLY   A HA2  1 
ATOM   1747 H  HA3  . GLY   A 1 78  ? 29.212 -8.515  -5.778  1.00 13.19 ?  78  GLY   A HA3  1 
ATOM   1748 N  N    . GLY   A 1 79  ? 30.722 -6.921  -3.725  1.00 10.47 ?  79  GLY   A N    1 
ATOM   1749 C  CA   . GLY   A 1 79  ? 31.683 -6.933  -2.647  1.00 10.74 ?  79  GLY   A CA   1 
ATOM   1750 C  C    . GLY   A 1 79  ? 31.235 -6.139  -1.431  1.00 10.14 ?  79  GLY   A C    1 
ATOM   1751 O  O    . GLY   A 1 79  ? 30.117 -5.631  -1.354  1.00 10.73 ?  79  GLY   A O    1 
ATOM   1752 H  H    . GLY   A 1 79  ? 30.765 -6.207  -4.208  1.00 12.60 ?  79  GLY   A H    1 
ATOM   1753 H  HA2  . GLY   A 1 79  ? 31.840 -7.857  -2.373  1.00 12.93 ?  79  GLY   A HA2  1 
ATOM   1754 H  HA3  . GLY   A 1 79  ? 32.525 -6.570  -2.961  1.00 12.93 ?  79  GLY   A HA3  1 
ATOM   1755 N  N    . SER   A 1 80  ? 32.145 -6.047  -0.461  1.00 11.06 ?  80  SER   A N    1 
ATOM   1756 C  CA   . SER   A 1 80  ? 31.831 -5.414  0.809   1.00 10.45 ?  80  SER   A CA   1 
ATOM   1757 C  C    . SER   A 1 80  ? 33.101 -4.961  1.512   1.00 10.28 ?  80  SER   A C    1 
ATOM   1758 O  O    . SER   A 1 80  ? 34.214 -5.394  1.187   1.00 11.88 ?  80  SER   A O    1 
ATOM   1759 C  CB   . SER   A 1 80  ? 31.071 -6.377  1.733   1.00 11.40 ?  80  SER   A CB   1 
ATOM   1760 O  OG   . SER   A 1 80  ? 31.906 -7.419  2.211   1.00 12.92 ?  80  SER   A OG   1 
ATOM   1761 H  H    . SER   A 1 80  ? 32.958 -6.332  -0.522  1.00 13.32 ?  80  SER   A H    1 
ATOM   1762 H  HA   . SER   A 1 80  ? 31.279 -4.633  0.633   1.00 12.58 ?  80  SER   A HA   1 
ATOM   1763 H  HB2  . SER   A 1 80  ? 30.728 -5.875  2.486   1.00 13.72 ?  80  SER   A HB2  1 
ATOM   1764 H  HB3  . SER   A 1 80  ? 30.334 -6.764  1.231   1.00 13.72 ?  80  SER   A HB3  1 
ATOM   1765 H  HG   . SER   A 1 80  ? 32.209 -7.859  1.558   1.00 15.54 ?  80  SER   A HG   1 
ATOM   1766 N  N    . CYS   A 1 81  ? 32.908 -4.106  2.514   1.00 10.04 ?  81  CYS   A N    1 
ATOM   1767 C  CA   . CYS   A 1 81  ? 33.961 -3.824  3.476   1.00 10.36 ?  81  CYS   A CA   1 
ATOM   1768 C  C    . CYS   A 1 81  ? 33.318 -3.583  4.834   1.00 10.10 ?  81  CYS   A C    1 
ATOM   1769 O  O    . CYS   A 1 81  ? 32.152 -3.180  4.920   1.00 11.23 ?  81  CYS   A O    1 
ATOM   1770 C  CB   . CYS   A 1 81  ? 34.836 -2.636  3.055   1.00 10.98 ?  81  CYS   A CB   1 
ATOM   1771 S  SG   . CYS   A 1 81  ? 33.941 -1.057  3.073   1.00 10.94 ?  81  CYS   A SG   1 
ATOM   1772 H  H    . CYS   A 1 81  ? 32.172 -3.680  2.660   1.00 12.09 ?  81  CYS   A H    1 
ATOM   1773 H  HA   . CYS   A 1 81  ? 34.535 -4.603  3.548   1.00 12.48 ?  81  CYS   A HA   1 
ATOM   1774 H  HB2  . CYS   A 1 81  ? 35.588 -2.566  3.665   1.00 13.22 ?  81  CYS   A HB2  1 
ATOM   1775 H  HB3  . CYS   A 1 81  ? 35.163 -2.790  2.150   1.00 13.22 ?  81  CYS   A HB3  1 
ATOM   1776 H  HG   . CYS   A 1 81  ? 34.686 -0.180  2.731   1.00 13.17 ?  81  CYS   A HG   1 
ATOM   1777 N  N    . VAL   A 1 82  ? 34.085 -3.846  5.893   1.00 10.48 ?  82  VAL   A N    1 
ATOM   1778 C  CA   . VAL   A 1 82  ? 33.661 -3.592  7.264   1.00 11.03 ?  82  VAL   A CA   1 
ATOM   1779 C  C    . VAL   A 1 82  ? 34.264 -2.280  7.736   1.00 10.97 ?  82  VAL   A C    1 
ATOM   1780 O  O    . VAL   A 1 82  ? 35.488 -2.109  7.721   1.00 11.73 ?  82  VAL   A O    1 
ATOM   1781 C  CB   . VAL   A 1 82  ? 34.078 -4.730  8.208   1.00 12.53 ?  82  VAL   A CB   1 
ATOM   1782 C  CG1  . VAL   A 1 82  ? 33.625 -4.425  9.629   1.00 13.95 ?  82  VAL   A CG1  1 
ATOM   1783 C  CG2  . VAL   A 1 82  ? 33.516 -6.061  7.742   1.00 13.50 ?  82  VAL   A CG2  1 
ATOM   1784 H  H    . VAL   A 1 82  ? 34.880 -4.185  5.837   1.00 12.61 ?  82  VAL   A H    1 
ATOM   1785 H  HA   . VAL   A 1 82  ? 32.694 -3.510  7.287   1.00 13.28 ?  82  VAL   A HA   1 
ATOM   1786 H  HB   . VAL   A 1 82  ? 35.042 -4.793  8.213   1.00 15.07 ?  82  VAL   A HB   1 
ATOM   1787 H  HG11 . VAL   A 1 82  ? 33.700 -5.230  10.163  1.00 16.78 ?  82  VAL   A HG11 1 
ATOM   1788 H  HG12 . VAL   A 1 82  ? 34.186 -3.727  10.004  1.00 16.78 ?  82  VAL   A HG12 1 
ATOM   1789 H  HG13 . VAL   A 1 82  ? 32.698 -4.128  9.612   1.00 16.78 ?  82  VAL   A HG13 1 
ATOM   1790 H  HG21 . VAL   A 1 82  ? 33.763 -6.747  8.381   1.00 16.25 ?  82  VAL   A HG21 1 
ATOM   1791 H  HG22 . VAL   A 1 82  ? 32.549 -5.994  7.685   1.00 16.25 ?  82  VAL   A HG22 1 
ATOM   1792 H  HG23 . VAL   A 1 82  ? 33.884 -6.270  6.870   1.00 16.25 ?  82  VAL   A HG23 1 
ATOM   1793 N  N    . LEU   A 1 83  ? 33.408 -1.356  8.161   1.00 10.61 ?  83  LEU   A N    1 
ATOM   1794 C  CA   . LEU   A 1 83  ? 33.825 -0.088  8.732   1.00 10.48 ?  83  LEU   A CA   1 
ATOM   1795 C  C    . LEU   A 1 83  ? 33.107 0.095   10.064  1.00 10.69 ?  83  LEU   A C    1 
ATOM   1796 O  O    . LEU   A 1 83  ? 32.385 -0.794  10.528  1.00 11.39 ?  83  LEU   A O    1 
ATOM   1797 C  CB   . LEU   A 1 83  ? 33.577 1.066   7.749   1.00 11.15 ?  83  LEU   A CB   1 
ATOM   1798 C  CG   . LEU   A 1 83  ? 34.476 1.058   6.512   1.00 11.63 ?  83  LEU   A CG   1 
ATOM   1799 C  CD1  . LEU   A 1 83  ? 34.035 2.101   5.508   1.00 12.45 ?  83  LEU   A CD1  1 
ATOM   1800 C  CD2  . LEU   A 1 83  ? 35.950 1.273   6.892   1.00 12.44 ?  83  LEU   A CD2  1 
ATOM   1801 H  H    . LEU   A 1 83  ? 32.553 -1.448  8.121   1.00 12.78 ?  83  LEU   A H    1 
ATOM   1802 H  HA   . LEU   A 1 83  ? 34.773 -0.117  8.912   1.00 12.62 ?  83  LEU   A HA   1 
ATOM   1803 H  HB2  . LEU   A 1 83  ? 32.659 1.026   7.435   1.00 13.42 ?  83  LEU   A HB2  1 
ATOM   1804 H  HB3  . LEU   A 1 83  ? 33.723 1.910   8.206   1.00 13.42 ?  83  LEU   A HB3  1 
ATOM   1805 H  HG   . LEU   A 1 83  ? 34.412 0.190   6.085   1.00 14.00 ?  83  LEU   A HG   1 
ATOM   1806 H  HD11 . LEU   A 1 83  ? 34.626 2.063   4.738   1.00 14.98 ?  83  LEU   A HD11 1 
ATOM   1807 H  HD12 . LEU   A 1 83  ? 33.126 1.905   5.239   1.00 14.98 ?  83  LEU   A HD12 1 
ATOM   1808 H  HD13 . LEU   A 1 83  ? 34.084 2.974   5.922   1.00 14.98 ?  83  LEU   A HD13 1 
ATOM   1809 H  HD21 . LEU   A 1 83  ? 36.473 1.418   6.085   1.00 14.97 ?  83  LEU   A HD21 1 
ATOM   1810 H  HD22 . LEU   A 1 83  ? 36.021 2.052   7.469   1.00 14.97 ?  83  LEU   A HD22 1 
ATOM   1811 H  HD23 . LEU   A 1 83  ? 36.281 0.489   7.359   1.00 14.97 ?  83  LEU   A HD23 1 
ATOM   1812 N  N    . SER   A 1 84  ? 33.320 1.246   10.695  1.00 11.50 ?  84  SER   A N    1 
ATOM   1813 C  CA   . SER   A 1 84  ? 32.676 1.505   11.973  1.00 11.51 ?  84  SER   A CA   1 
ATOM   1814 C  C    . SER   A 1 84  ? 31.158 1.586   11.824  1.00 11.37 ?  84  SER   A C    1 
ATOM   1815 O  O    . SER   A 1 84  ? 30.630 2.053   10.814  1.00 11.52 ?  84  SER   A O    1 
ATOM   1816 C  CB   . SER   A 1 84  ? 33.172 2.828   12.543  1.00 12.68 ?  84  SER   A CB   1 
ATOM   1817 O  OG   . SER   A 1 84  ? 32.535 3.107   13.775  1.00 13.30 ?  84  SER   A OG   1 
ATOM   1818 H  H    . SER   A 1 84  ? 33.822 1.887   10.401  1.00 13.84 ?  84  SER   A H    1 
ATOM   1819 H  HA   . SER   A 1 84  ? 32.898 0.794   12.589  1.00 13.86 ?  84  SER   A HA   1 
ATOM   1820 H  HB2  . SER   A 1 84  ? 34.130 2.775   12.680  1.00 15.26 ?  84  SER   A HB2  1 
ATOM   1821 H  HB3  . SER   A 1 84  ? 32.967 3.540   11.914  1.00 15.26 ?  84  SER   A HB3  1 
ATOM   1822 H  HG   . SER   A 1 84  ? 32.817 3.835   14.085  1.00 16.01 ?  84  SER   A HG   1 
ATOM   1823 N  N    . GLY   A 1 85  ? 30.452 1.173   12.874  1.00 12.20 ?  85  GLY   A N    1 
ATOM   1824 C  CA   . GLY   A 1 85  ? 29.028 1.407   12.973  1.00 12.85 ?  85  GLY   A CA   1 
ATOM   1825 C  C    . GLY   A 1 85  ? 28.657 2.729   13.609  1.00 12.39 ?  85  GLY   A C    1 
ATOM   1826 O  O    . GLY   A 1 85  ? 27.465 3.040   13.720  1.00 12.88 ?  85  GLY   A O    1 
ATOM   1827 H  H    . GLY   A 1 85  ? 30.790 0.748   13.545  1.00 14.68 ?  85  GLY   A H    1 
ATOM   1828 H  HA2  . GLY   A 1 85  ? 28.644 1.379   12.085  1.00 15.46 ?  85  GLY   A HA2  1 
ATOM   1829 H  HA3  . GLY   A 1 85  ? 28.630 0.700   13.499  1.00 15.46 ?  85  GLY   A HA3  1 
ATOM   1830 N  N    . HIS   A 1 86  ? 29.640 3.514   14.041  1.00 11.92 ?  86  HIS   A N    1 
ATOM   1831 C  CA   . HIS   A 1 86  ? 29.412 4.848   14.605  1.00 12.51 ?  86  HIS   A CA   1 
ATOM   1832 C  C    . HIS   A 1 86  ? 28.425 4.727   15.760  1.00 13.20 ?  86  HIS   A C    1 
ATOM   1833 O  O    . HIS   A 1 86  ? 28.604 3.850   16.616  1.00 14.69 ?  86  HIS   A O    1 
ATOM   1834 C  CB   . HIS   A 1 86  ? 29.028 5.813   13.491  1.00 12.56 ?  86  HIS   A CB   1 
ATOM   1835 C  CG   . HIS   A 1 86  ? 30.087 5.919   12.454  1.00 12.29 ?  86  HIS   A CG   1 
ATOM   1836 N  ND1  . HIS   A 1 86  ? 31.177 6.753   12.592  1.00 13.65 ?  86  HIS   A ND1  1 
ATOM   1837 C  CD2  . HIS   A 1 86  ? 30.276 5.228   11.308  1.00 12.26 ?  86  HIS   A CD2  1 
ATOM   1838 C  CE1  . HIS   A 1 86  ? 31.973 6.590   11.551  1.00 13.33 ?  86  HIS   A CE1  1 
ATOM   1839 N  NE2  . HIS   A 1 86  ? 31.458 5.663   10.765  1.00 12.54 ?  86  HIS   A NE2  1 
ATOM   1840 H  H    . HIS   A 1 86  ? 30.466 3.295   14.025  1.00 14.34 ?  86  HIS   A H    1 
ATOM   1841 H  HA   . HIS   A 1 86  ? 30.247 5.169   14.975  1.00 15.05 ?  86  HIS   A HA   1 
ATOM   1842 H  HB2  . HIS   A 1 86  ? 28.211 5.507   13.062  1.00 15.12 ?  86  HIS   A HB2  1 
ATOM   1843 H  HB3  . HIS   A 1 86  ? 28.889 6.702   13.864  1.00 15.12 ?  86  HIS   A HB3  1 
ATOM   1844 H  HD2  . HIS   A 1 86  ? 29.714 4.567   10.954  1.00 14.75 ?  86  HIS   A HD2  1 
ATOM   1845 H  HE1  . HIS   A 1 86  ? 32.763 7.049   11.387  1.00 16.04 ?  86  HIS   A HE1  1 
ATOM   1846 H  HE2  . HIS   A 1 86  ? 31.794 5.388   10.014  1.00 15.09 ?  86  HIS   A HE2  1 
ATOM   1847 N  N    . ASN   A 1 87  ? 27.409 5.576   15.825  1.00 14.17 ?  87  ASN   A N    1 
ATOM   1848 C  CA   . ASN   A 1 87  ? 26.422 5.568   16.889  1.00 15.19 ?  87  ASN   A CA   1 
ATOM   1849 C  C    . ASN   A 1 87  ? 25.295 4.580   16.643  1.00 16.66 ?  87  ASN   A C    1 
ATOM   1850 O  O    . ASN   A 1 87  ? 24.359 4.530   17.445  1.00 18.97 ?  87  ASN   A O    1 
ATOM   1851 C  CB   . ASN   A 1 87  ? 25.834 6.976   17.054  1.00 16.11 ?  87  ASN   A CB   1 
ATOM   1852 C  CG   . ASN   A 1 87  ? 25.327 7.562   15.742  1.00 17.06 ?  87  ASN   A CG   1 
ATOM   1853 O  OD1  . ASN   A 1 87  ? 25.959 7.426   14.698  1.00 17.73 ?  87  ASN   A OD1  1 
ATOM   1854 N  ND2  . ASN   A 1 87  ? 24.185 8.224   15.796  1.00 18.24 ?  87  ASN   A ND2  1 
ATOM   1855 H  H    . ASN   A 1 87  ? 27.264 6.185   15.243  1.00 17.05 ?  87  ASN   A H    1 
ATOM   1856 H  HA   . ASN   A 1 87  ? 26.851 5.324   17.726  1.00 18.27 ?  87  ASN   A HA   1 
ATOM   1857 H  HB2  . ASN   A 1 87  ? 25.085 6.935   17.677  1.00 19.37 ?  87  ASN   A HB2  1 
ATOM   1858 H  HB3  . ASN   A 1 87  ? 26.519 7.564   17.405  1.00 19.37 ?  87  ASN   A HB3  1 
ATOM   1859 H  HD21 . ASN   A 1 87  ? 23.860 8.572   15.080  1.00 21.94 ?  87  ASN   A HD21 1 
ATOM   1860 H  HD22 . ASN   A 1 87  ? 23.770 8.309   16.544  1.00 21.94 ?  87  ASN   A HD22 1 
ATOM   1861 N  N    . LEU   A 1 88  ? 25.362 3.786   15.580  1.00 15.19 ?  88  LEU   A N    1 
ATOM   1862 C  CA   . LEU   A 1 88  ? 24.252 2.925   15.186  1.00 15.01 ?  88  LEU   A CA   1 
ATOM   1863 C  C    . LEU   A 1 88  ? 24.461 1.448   15.487  1.00 14.48 ?  88  LEU   A C    1 
ATOM   1864 O  O    . LEU   A 1 88  ? 23.479 0.720   15.647  1.00 15.73 ?  88  LEU   A O    1 
ATOM   1865 C  CB   . LEU   A 1 88  ? 23.998 3.080   13.685  1.00 15.56 ?  88  LEU   A CB   1 
ATOM   1866 C  CG   . LEU   A 1 88  ? 23.725 4.505   13.200  1.00 17.39 ?  88  LEU   A CG   1 
ATOM   1867 C  CD1  . LEU   A 1 88  ? 23.549 4.514   11.694  1.00 18.00 ?  88  LEU   A CD1  1 
ATOM   1868 C  CD2  . LEU   A 1 88  ? 22.498 5.093   13.888  1.00 19.39 ?  88  LEU   A CD2  1 
ATOM   1869 H  H    . LEU   A 1 88  ? 26.055 3.720   15.072  1.00 18.27 ?  88  LEU   A H    1 
ATOM   1870 H  HA   . LEU   A 1 88  ? 23.454 3.213   15.656  1.00 18.06 ?  88  LEU   A HA   1 
ATOM   1871 H  HB2  . LEU   A 1 88  ? 24.773 2.757   13.205  1.00 18.72 ?  88  LEU   A HB2  1 
ATOM   1872 H  HB3  . LEU   A 1 88  ? 23.223 2.545   13.450  1.00 18.72 ?  88  LEU   A HB3  1 
ATOM   1873 H  HG   . LEU   A 1 88  ? 24.486 5.065   13.414  1.00 20.91 ?  88  LEU   A HG   1 
ATOM   1874 H  HD11 . LEU   A 1 88  ? 23.392 5.425   11.396  1.00 21.64 ?  88  LEU   A HD11 1 
ATOM   1875 H  HD12 . LEU   A 1 88  ? 24.354 4.166   11.278  1.00 21.64 ?  88  LEU   A HD12 1 
ATOM   1876 H  HD13 . LEU   A 1 88  ? 22.789 3.956   11.459  1.00 21.64 ?  88  LEU   A HD13 1 
ATOM   1877 H  HD21 . LEU   A 1 88  ? 22.288 5.947   13.478  1.00 23.31 ?  88  LEU   A HD21 1 
ATOM   1878 H  HD22 . LEU   A 1 88  ? 21.755 4.482   13.779  1.00 23.31 ?  88  LEU   A HD22 1 
ATOM   1879 H  HD23 . LEU   A 1 88  ? 22.695 5.216   14.828  1.00 23.31 ?  88  LEU   A HD23 1 
ATOM   1880 N  N    . ALA   A 1 89  ? 25.707 0.996   15.546  1.00 14.04 ?  89  ALA   A N    1 
ATOM   1881 C  CA   . ALA   A 1 89  ? 26.047 -0.416  15.644  1.00 13.62 ?  89  ALA   A CA   1 
ATOM   1882 C  C    . ALA   A 1 89  ? 27.531 -0.486  15.961  1.00 14.02 ?  89  ALA   A C    1 
ATOM   1883 O  O    . ALA   A 1 89  ? 28.247 0.510   15.847  1.00 14.85 ?  89  ALA   A O    1 
ATOM   1884 C  CB   . ALA   A 1 89  ? 25.768 -1.131  14.322  1.00 13.54 ?  89  ALA   A CB   1 
ATOM   1885 H  H    . ALA   A 1 89  ? 26.396 1.508   15.514  1.00 16.89 ?  89  ALA   A H    1 
ATOM   1886 H  HA   . ALA   A 1 89  ? 25.538 -0.836  16.357  1.00 16.39 ?  89  ALA   A HA   1 
ATOM   1887 H  HB1  . ALA   A 1 89  ? 26.012 -2.068  14.412  1.00 16.29 ?  89  ALA   A HB1  1 
ATOM   1888 H  HB2  . ALA   A 1 89  ? 24.820 -1.061  14.113  1.00 16.29 ?  89  ALA   A HB2  1 
ATOM   1889 H  HB3  . ALA   A 1 89  ? 26.292 -0.720  13.620  1.00 16.29 ?  89  ALA   A HB3  1 
ATOM   1890 N  N    . LYS   A 1 90  ? 28.004 -1.667  16.348  1.00 14.47 ?  90  LYS   A N    1 
ATOM   1891 C  CA   . LYS   A 1 90  ? 29.449 -1.816  16.499  1.00 15.26 ?  90  LYS   A CA   1 
ATOM   1892 C  C    . LYS   A 1 90  ? 30.153 -1.630  15.156  1.00 14.21 ?  90  LYS   A C    1 
ATOM   1893 O  O    . LYS   A 1 90  ? 31.086 -0.820  15.029  1.00 15.74 ?  90  LYS   A O    1 
ATOM   1894 C  CB   . LYS   A 1 90  ? 29.787 -3.168  17.128  1.00 17.77 ?  90  LYS   A CB   1 
ATOM   1895 C  CG   . LYS   A 1 90  ? 31.266 -3.322  17.452  1.00 22.56 ?  90  LYS   A CG   1 
ATOM   1896 C  CD   . LYS   A 1 90  ? 31.521 -4.566  18.286  1.00 27.29 ?  90  LYS   A CD   1 
ATOM   1897 C  CE   . LYS   A 1 90  ? 32.916 -4.563  18.894  1.00 31.53 ?  90  LYS   A CE   1 
ATOM   1898 N  NZ   . LYS   A 1 90  ? 33.986 -4.811  17.889  1.00 33.91 ?  90  LYS   A NZ   1 
ATOM   1899 H  H    . LYS   A 1 90  ? 27.530 -2.357  16.531  1.00 17.40 ?  90  LYS   A H    1 
ATOM   1900 H  HA   . LYS   A 1 90  ? 29.770 -1.124  17.095  1.00 18.36 ?  90  LYS   A HA   1 
ATOM   1901 H  HB2  . LYS   A 1 90  ? 29.285 -3.262  17.956  1.00 21.37 ?  90  LYS   A HB2  1 
ATOM   1902 H  HB3  . LYS   A 1 90  ? 29.537 -3.873  16.512  1.00 21.37 ?  90  LYS   A HB3  1 
ATOM   1903 H  HG2  . LYS   A 1 90  ? 31.769 -3.399  16.626  1.00 27.12 ?  90  LYS   A HG2  1 
ATOM   1904 H  HG3  . LYS   A 1 90  ? 31.566 -2.549  17.957  1.00 27.12 ?  90  LYS   A HG3  1 
ATOM   1905 H  HD2  . LYS   A 1 90  ? 30.874 -4.606  19.009  1.00 32.79 ?  90  LYS   A HD2  1 
ATOM   1906 H  HD3  . LYS   A 1 90  ? 31.438 -5.352  17.721  1.00 32.79 ?  90  LYS   A HD3  1 
ATOM   1907 H  HE2  . LYS   A 1 90  ? 33.082 -3.698  19.301  1.00 37.88 ?  90  LYS   A HE2  1 
ATOM   1908 H  HE3  . LYS   A 1 90  ? 32.970 -5.260  19.567  1.00 37.88 ?  90  LYS   A HE3  1 
ATOM   1909 H  HZ1  . LYS   A 1 90  ? 34.784 -4.803  18.286  1.00 40.73 ?  90  LYS   A HZ1  1 
ATOM   1910 H  HZ2  . LYS   A 1 90  ? 33.864 -5.604  17.504  1.00 40.73 ?  90  LYS   A HZ2  1 
ATOM   1911 H  HZ3  . LYS   A 1 90  ? 33.969 -4.179  17.264  1.00 40.73 ?  90  LYS   A HZ3  1 
ATOM   1912 N  N    . HIS   A 1 91  ? 29.685 -2.345  14.133  1.00 12.61 ?  91  HIS   A N    1 
ATOM   1913 C  CA   . HIS   A 1 91  ? 30.270 -2.326  12.806  1.00 12.11 ?  91  HIS   A CA   1 
ATOM   1914 C  C    . HIS   A 1 91  ? 29.190 -2.055  11.777  1.00 10.90 ?  91  HIS   A C    1 
ATOM   1915 O  O    . HIS   A 1 91  ? 28.027 -2.424  11.964  1.00 11.73 ?  91  HIS   A O    1 
ATOM   1916 C  CB   . HIS   A 1 91  ? 30.871 -3.695  12.448  1.00 14.58 ?  91  HIS   A CB   1 
ATOM   1917 C  CG   . HIS   A 1 91  ? 31.835 -4.225  13.461  1.00 18.63 ?  91  HIS   A CG   1 
ATOM   1918 N  ND1  . HIS   A 1 91  ? 33.126 -3.758  13.574  1.00 20.67 ?  91  HIS   A ND1  1 
ATOM   1919 C  CD2  . HIS   A 1 91  ? 31.702 -5.193  14.398  1.00 20.48 ?  91  HIS   A CD2  1 
ATOM   1920 C  CE1  . HIS   A 1 91  ? 33.747 -4.412  14.541  1.00 21.55 ?  91  HIS   A CE1  1 
ATOM   1921 N  NE2  . HIS   A 1 91  ? 32.904 -5.290  15.057  1.00 21.70 ?  91  HIS   A NE2  1 
ATOM   1922 H  H    . HIS   A 1 91  ? 29.001 -2.881  14.196  1.00 15.17 ?  91  HIS   A H    1 
ATOM   1923 H  HA   . HIS   A 1 91  ? 30.957 -1.650  12.751  1.00 14.58 ?  91  HIS   A HA   1 
ATOM   1924 H  HB2  . HIS   A 1 91  ? 30.153 -4.344  12.362  1.00 17.54 ?  91  HIS   A HB2  1 
ATOM   1925 H  HB3  . HIS   A 1 91  ? 31.343 -3.618  11.604  1.00 17.54 ?  91  HIS   A HB3  1 
ATOM   1926 H  HD1  . HIS   A 1 91  ? 33.477 -3.138  13.087  1.00 24.85 ?  91  HIS   A HD1  1 
ATOM   1927 H  HD2  . HIS   A 1 91  ? 30.945 -5.698  14.568  1.00 24.62 ?  91  HIS   A HD2  1 
ATOM   1928 H  HE1  . HIS   A 1 91  ? 34.630 -4.273  14.810  1.00 25.90 ?  91  HIS   A HE1  1 
ATOM   1929 N  N    . CYS   A 1 92  ? 29.603 -1.468  10.658  1.00 10.54 ?  92  CYS   A N    1 
ATOM   1930 C  CA   . CYS   A 1 92  ? 28.768 -1.382  9.470   1.00 10.39 ?  92  CYS   A CA   1 
ATOM   1931 C  C    . CYS   A 1 92  ? 29.414 -2.205  8.362   1.00 9.91  ?  92  CYS   A C    1 
ATOM   1932 O  O    . CYS   A 1 92  ? 30.578 -1.965  7.998   1.00 10.69 ?  92  CYS   A O    1 
ATOM   1933 C  CB   . CYS   A 1 92  ? 28.564 0.063   9.013   1.00 10.71 ?  92  CYS   A CB   1 
ATOM   1934 S  SG   . CYS   A 1 92  ? 27.542 0.165   7.500   1.00 10.24 ?  92  CYS   A SG   1 
ATOM   1935 H  H    . CYS   A 1 92  ? 30.384 -1.107  10.562  1.00 12.69 ?  92  CYS   A H    1 
ATOM   1936 H  HA   . CYS   A 1 92  ? 27.902 -1.764  9.666   1.00 12.51 ?  92  CYS   A HA   1 
ATOM   1937 H  HB2  . CYS   A 1 92  ? 28.110 0.561   9.713   1.00 12.90 ?  92  CYS   A HB2  1 
ATOM   1938 H  HB3  . CYS   A 1 92  ? 29.422 0.467   8.819   1.00 12.90 ?  92  CYS   A HB3  1 
ATOM   1939 H  HG   . CYS   A 1 92  ? 27.402 1.313   7.201   1.00 12.33 ?  92  CYS   A HG   1 
ATOM   1940 N  N    . LEU   A 1 93  ? 28.674 -3.189  7.860   1.00 9.63  ?  93  LEU   A N    1 
ATOM   1941 C  CA   . LEU   A 1 93  ? 29.081 -3.954  6.688   1.00 9.70  ?  93  LEU   A CA   1 
ATOM   1942 C  C    . LEU   A 1 93  ? 28.488 -3.262  5.463   1.00 9.29  ?  93  LEU   A C    1 
ATOM   1943 O  O    . LEU   A 1 93  ? 27.271 -3.316  5.235   1.00 9.37  ?  93  LEU   A O    1 
ATOM   1944 C  CB   . LEU   A 1 93  ? 28.589 -5.396  6.798   1.00 9.82  ?  93  LEU   A CB   1 
ATOM   1945 C  CG   . LEU   A 1 93  ? 28.986 -6.299  5.629   1.00 10.43 ?  93  LEU   A CG   1 
ATOM   1946 C  CD1  . LEU   A 1 93  ? 30.489 -6.553  5.625   1.00 11.66 ?  93  LEU   A CD1  1 
ATOM   1947 C  CD2  . LEU   A 1 93  ? 28.214 -7.622  5.664   1.00 10.93 ?  93  LEU   A CD2  1 
ATOM   1948 H  H    . LEU   A 1 93  ? 27.916 -3.434  8.194   1.00 11.59 ?  93  LEU   A H    1 
ATOM   1949 H  HA   . LEU   A 1 93  ? 30.043 -3.950  6.617   1.00 11.68 ?  93  LEU   A HA   1 
ATOM   1950 H  HB2  . LEU   A 1 93  ? 28.954 -5.785  7.612   1.00 11.83 ?  93  LEU   A HB2  1 
ATOM   1951 H  HB3  . LEU   A 1 93  ? 27.620 -5.394  6.849   1.00 11.83 ?  93  LEU   A HB3  1 
ATOM   1952 H  HG   . LEU   A 1 93  ? 28.768 -5.859  4.803   1.00 12.56 ?  93  LEU   A HG   1 
ATOM   1953 H  HD11 . LEU   A 1 93  ? 30.707 -7.179  4.918   1.00 14.04 ?  93  LEU   A HD11 1 
ATOM   1954 H  HD12 . LEU   A 1 93  ? 30.955 -5.715  5.483   1.00 14.04 ?  93  LEU   A HD12 1 
ATOM   1955 H  HD13 . LEU   A 1 93  ? 30.753 -6.931  6.486   1.00 14.04 ?  93  LEU   A HD13 1 
ATOM   1956 H  HD21 . LEU   A 1 93  ? 28.494 -8.176  4.914   1.00 13.16 ?  93  LEU   A HD21 1 
ATOM   1957 H  HD22 . LEU   A 1 93  ? 28.405 -8.087  6.498   1.00 13.16 ?  93  LEU   A HD22 1 
ATOM   1958 H  HD23 . LEU   A 1 93  ? 27.265 -7.440  5.601   1.00 13.16 ?  93  LEU   A HD23 1 
ATOM   1959 N  N    . HIS   A 1 94  ? 29.343 -2.573  4.701   1.00 9.02  ?  94  HIS   A N    1 
ATOM   1960 C  CA   . HIS   A 1 94  ? 28.917 -1.903  3.476   1.00 9.20  ?  94  HIS   A CA   1 
ATOM   1961 C  C    . HIS   A 1 94  ? 28.924 -2.936  2.365   1.00 9.14  ?  94  HIS   A C    1 
ATOM   1962 O  O    . HIS   A 1 94  ? 29.991 -3.448  2.017   1.00 10.66 ?  94  HIS   A O    1 
ATOM   1963 C  CB   . HIS   A 1 94  ? 29.870 -0.755  3.142   1.00 9.40  ?  94  HIS   A CB   1 
ATOM   1964 C  CG   . HIS   A 1 94  ? 29.855 0.342   4.155   1.00 9.14  ?  94  HIS   A CG   1 
ATOM   1965 N  ND1  . HIS   A 1 94  ? 28.986 1.412   4.091   1.00 9.34  ?  94  HIS   A ND1  1 
ATOM   1966 C  CD2  . HIS   A 1 94  ? 30.593 0.510   5.277   1.00 10.07 ?  94  HIS   A CD2  1 
ATOM   1967 C  CE1  . HIS   A 1 94  ? 29.202 2.192   5.136   1.00 9.63  ?  94  HIS   A CE1  1 
ATOM   1968 N  NE2  . HIS   A 1 94  ? 30.169 1.667   5.871   1.00 10.08 ?  94  HIS   A NE2  1 
ATOM   1969 H  H    . HIS   A 1 94  ? 30.182 -2.486  4.874   1.00 10.86 ?  94  HIS   A H    1 
ATOM   1970 H  HA   . HIS   A 1 94  ? 28.016 -1.556  3.583   1.00 11.08 ?  94  HIS   A HA   1 
ATOM   1971 H  HB2  . HIS   A 1 94  ? 30.767 -1.097  3.088   1.00 11.32 ?  94  HIS   A HB2  1 
ATOM   1972 H  HB3  . HIS   A 1 94  ? 29.603 -0.370  2.290   1.00 11.32 ?  94  HIS   A HB3  1 
ATOM   1973 H  HD2  . HIS   A 1 94  ? 31.263 -0.047  5.589   1.00 12.13 ?  94  HIS   A HD2  1 
ATOM   1974 H  HE1  . HIS   A 1 94  ? 28.735 2.982   5.319   1.00 11.60 ?  94  HIS   A HE1  1 
ATOM   1975 H  HE2  . HIS   A 1 94  ? 30.479 2.016   6.593   1.00 12.14 ?  94  HIS   A HE2  1 
ATOM   1976 N  N    . VAL   A 1 95  ? 27.754 -3.262  1.820   1.00 8.64  ?  95  VAL   A N    1 
ATOM   1977 C  CA   . VAL   A 1 95  ? 27.613 -4.298  0.800   1.00 8.95  ?  95  VAL   A CA   1 
ATOM   1978 C  C    . VAL   A 1 95  ? 27.067 -3.660  -0.464  1.00 8.67  ?  95  VAL   A C    1 
ATOM   1979 O  O    . VAL   A 1 95  ? 26.060 -2.940  -0.410  1.00 9.61  ?  95  VAL   A O    1 
ATOM   1980 C  CB   . VAL   A 1 95  ? 26.677 -5.436  1.251   1.00 9.52  ?  95  VAL   A CB   1 
ATOM   1981 C  CG1  . VAL   A 1 95  ? 26.565 -6.484  0.147   1.00 10.08 ?  95  VAL   A CG1  1 
ATOM   1982 C  CG2  . VAL   A 1 95  ? 27.179 -6.060  2.539   1.00 9.77  ?  95  VAL   A CG2  1 
ATOM   1983 H  H    . VAL   A 1 95  ? 27.002 -2.894  2.034   1.00 10.41 ?  95  VAL   A H    1 
ATOM   1984 H  HA   . VAL   A 1 95  ? 28.476 -4.678  0.597   1.00 10.78 ?  95  VAL   A HA   1 
ATOM   1985 H  HB   . VAL   A 1 95  ? 25.792 -5.084  1.415   1.00 11.47 ?  95  VAL   A HB   1 
ATOM   1986 H  HG11 . VAL   A 1 95  ? 26.171 -7.296  0.512   1.00 12.14 ?  95  VAL   A HG11 1 
ATOM   1987 H  HG12 . VAL   A 1 95  ? 26.002 -6.144  -0.567  1.00 12.14 ?  95  VAL   A HG12 1 
ATOM   1988 H  HG13 . VAL   A 1 95  ? 27.452 -6.684  -0.199  1.00 12.14 ?  95  VAL   A HG13 1 
ATOM   1989 H  HG21 . VAL   A 1 95  ? 26.613 -6.817  2.763   1.00 11.77 ?  95  VAL   A HG21 1 
ATOM   1990 H  HG22 . VAL   A 1 95  ? 28.092 -6.356  2.411   1.00 11.77 ?  95  VAL   A HG22 1 
ATOM   1991 H  HG23 . VAL   A 1 95  ? 27.138 -5.396  3.242   1.00 11.77 ?  95  VAL   A HG23 1 
ATOM   1992 N  N    . VAL   A 1 96  ? 27.696 -3.951  -1.603  1.00 8.78  ?  96  VAL   A N    1 
ATOM   1993 C  CA   . VAL   A 1 96  ? 27.284 -3.405  -2.891  1.00 9.64  ?  96  VAL   A CA   1 
ATOM   1994 C  C    . VAL   A 1 96  ? 26.477 -4.453  -3.650  1.00 9.83  ?  96  VAL   A C    1 
ATOM   1995 O  O    . VAL   A 1 96  ? 27.033 -5.399  -4.213  1.00 10.70 ?  96  VAL   A O    1 
ATOM   1996 C  CB   . VAL   A 1 96  ? 28.476 -2.931  -3.720  1.00 10.02 ?  96  VAL   A CB   1 
ATOM   1997 C  CG1  . VAL   A 1 96  ? 27.976 -2.298  -4.999  1.00 10.31 ?  96  VAL   A CG1  1 
ATOM   1998 C  CG2  . VAL   A 1 96  ? 29.331 -1.949  -2.931  1.00 10.79 ?  96  VAL   A CG2  1 
ATOM   1999 H  H    . VAL   A 1 96  ? 28.391 -4.460  -1.653  1.00 10.58 ?  96  VAL   A H    1 
ATOM   2000 H  HA   . VAL   A 1 96  ? 26.713 -2.639  -2.740  1.00 11.61 ?  96  VAL   A HA   1 
ATOM   2001 H  HB   . VAL   A 1 96  ? 29.032 -3.687  -3.956  1.00 12.07 ?  96  VAL   A HB   1 
ATOM   2002 H  HG11 . VAL   A 1 96  ? 28.712 -1.820  -5.418  1.00 12.41 ?  96  VAL   A HG11 1 
ATOM   2003 H  HG12 . VAL   A 1 96  ? 27.655 -2.991  -5.590  1.00 12.41 ?  96  VAL   A HG12 1 
ATOM   2004 H  HG13 . VAL   A 1 96  ? 27.263 -1.678  -4.785  1.00 12.41 ?  96  VAL   A HG13 1 
ATOM   2005 H  HG21 . VAL   A 1 96  ? 30.034 -1.600  -3.500  1.00 12.99 ?  96  VAL   A HG21 1 
ATOM   2006 H  HG22 . VAL   A 1 96  ? 28.769 -1.215  -2.620  1.00 12.99 ?  96  VAL   A HG22 1 
ATOM   2007 H  HG23 . VAL   A 1 96  ? 29.720 -2.404  -2.167  1.00 12.99 ?  96  VAL   A HG23 1 
ATOM   2008 N  N    A GLY   A 1 97  ? 25.160 -4.296  -3.673  0.60 10.12 ?  97  GLY   A N    1 
ATOM   2009 N  N    B GLY   A 1 97  ? 25.160 -4.287  -3.684  0.40 10.24 ?  97  GLY   A N    1 
ATOM   2010 C  CA   A GLY   A 1 97  ? 24.342 -5.050  -4.586  0.60 10.53 ?  97  GLY   A CA   1 
ATOM   2011 C  CA   B GLY   A 1 97  ? 24.335 -5.055  -4.581  0.40 10.71 ?  97  GLY   A CA   1 
ATOM   2012 C  C    A GLY   A 1 97  ? 24.380 -4.410  -5.961  0.60 10.64 ?  97  GLY   A C    1 
ATOM   2013 C  C    B GLY   A 1 97  ? 24.280 -4.390  -5.944  0.40 10.91 ?  97  GLY   A C    1 
ATOM   2014 O  O    A GLY   A 1 97  ? 24.733 -3.233  -6.110  0.60 11.24 ?  97  GLY   A O    1 
ATOM   2015 O  O    B GLY   A 1 97  ? 24.462 -3.173  -6.068  0.40 11.15 ?  97  GLY   A O    1 
ATOM   2016 H  H    A GLY   A 1 97  ? 24.725 -3.752  -3.162  0.60 12.18 ?  97  GLY   A H    1 
ATOM   2017 H  H    B GLY   A 1 97  ? 24.726 -3.730  -3.187  0.40 12.33 ?  97  GLY   A H    1 
ATOM   2018 H  HA2  A GLY   A 1 97  ? 24.677 -5.957  -4.641  0.60 12.68 ?  97  GLY   A HA2  1 
ATOM   2019 H  HA2  B GLY   A 1 97  ? 24.704 -5.948  -4.669  0.40 12.89 ?  97  GLY   A HA2  1 
ATOM   2020 H  HA3  A GLY   A 1 97  ? 23.426 -5.072  -4.261  0.60 12.68 ?  97  GLY   A HA3  1 
ATOM   2021 H  HA3  B GLY   A 1 97  ? 23.436 -5.123  -4.221  0.40 12.89 ?  97  GLY   A HA3  1 
ATOM   2022 N  N    . PRO   A 1 98  ? 24.014 -5.167  -6.994  1.00 10.88 ?  98  PRO   A N    1 
ATOM   2023 C  CA   . PRO   A 1 98  ? 23.925 -4.574  -8.332  1.00 12.15 ?  98  PRO   A CA   1 
ATOM   2024 C  C    . PRO   A 1 98  ? 22.809 -3.538  -8.408  1.00 12.55 ?  98  PRO   A C    1 
ATOM   2025 O  O    . PRO   A 1 98  ? 21.728 -3.700  -7.832  1.00 12.60 ?  98  PRO   A O    1 
ATOM   2026 C  CB   . PRO   A 1 98  ? 23.641 -5.780  -9.234  1.00 12.74 ?  98  PRO   A CB   1 
ATOM   2027 C  CG   . PRO   A 1 98  ? 22.977 -6.782  -8.327  1.00 12.59 ?  98  PRO   A CG   1 
ATOM   2028 C  CD   . PRO   A 1 98  ? 23.689 -6.609  -6.999  1.00 11.44 ?  98  PRO   A CD   1 
ATOM   2029 H  HA   . PRO   A 1 98  ? 24.771 -4.171  -8.577  1.00 14.62 ?  98  PRO   A HA   1 
ATOM   2030 H  HB2  . PRO   A 1 98  ? 23.042 -5.515  -9.950  1.00 15.33 ?  98  PRO   A HB2  1 
ATOM   2031 H  HB3  . PRO   A 1 98  ? 24.471 -6.130  -9.587  1.00 15.33 ?  98  PRO   A HB3  1 
ATOM   2032 H  HG2  . PRO   A 1 98  ? 22.034 -6.575  -8.246  1.00 15.15 ?  98  PRO   A HG2  1 
ATOM   2033 H  HG3  . PRO   A 1 98  ? 23.108 -7.675  -8.678  1.00 15.15 ?  98  PRO   A HG3  1 
ATOM   2034 H  HD2  . PRO   A 1 98  ? 23.091 -6.834  -6.264  1.00 13.77 ?  98  PRO   A HD2  1 
ATOM   2035 H  HD3  . PRO   A 1 98  ? 24.499 -7.142  -6.971  1.00 13.77 ?  98  PRO   A HD3  1 
ATOM   2036 N  N    A ASN   A 1 99  ? 23.090 -2.427  -9.091  0.60 13.77 ?  99  ASN   A N    1 
ATOM   2037 N  N    B ASN   A 1 99  ? 23.090 -2.486  -9.160  0.40 13.93 ?  99  ASN   A N    1 
ATOM   2038 C  CA   A ASN   A 1 99  ? 22.117 -1.346  -9.277  0.60 14.53 ?  99  ASN   A CA   1 
ATOM   2039 C  CA   B ASN   A 1 99  ? 22.118 -1.461  -9.501  0.40 15.10 ?  99  ASN   A CA   1 
ATOM   2040 C  C    A ASN   A 1 99  ? 21.563 -1.466  -10.694 0.60 15.59 ?  99  ASN   A C    1 
ATOM   2041 C  C    B ASN   A 1 99  ? 21.541 -1.805  -10.870 0.40 15.90 ?  99  ASN   A C    1 
ATOM   2042 O  O    A ASN   A 1 99  ? 22.231 -1.112  -11.670 0.60 16.21 ?  99  ASN   A O    1 
ATOM   2043 O  O    B ASN   A 1 99  ? 22.252 -1.767  -11.880 0.40 15.38 ?  99  ASN   A O    1 
ATOM   2044 C  CB   A ASN   A 1 99  ? 22.742 0.026   -9.019  0.60 14.32 ?  99  ASN   A CB   1 
ATOM   2045 C  CB   B ASN   A 1 99  ? 22.819 -0.109  -9.531  0.40 16.13 ?  99  ASN   A CB   1 
ATOM   2046 C  CG   A ASN   A 1 99  ? 21.705 1.160   -8.994  0.60 14.25 ?  99  ASN   A CG   1 
ATOM   2047 C  CG   B ASN   A 1 99  ? 21.862 1.037   -9.735  0.40 17.14 ?  99  ASN   A CG   1 
ATOM   2048 O  OD1  A ASN   A 1 99  ? 20.694 1.106   -9.697  0.60 14.56 ?  99  ASN   A OD1  1 
ATOM   2049 O  OD1  B ASN   A 1 99  ? 20.879 0.915   -10.460 0.40 17.33 ?  99  ASN   A OD1  1 
ATOM   2050 N  ND2  A ASN   A 1 99  ? 21.965 2.195   -8.192  0.60 14.29 ?  99  ASN   A ND2  1 
ATOM   2051 N  ND2  B ASN   A 1 99  ? 22.143 2.163   -9.089  0.40 17.83 ?  99  ASN   A ND2  1 
ATOM   2052 H  H    A ASN   A 1 99  ? 23.854 -2.268  -9.455  0.60 16.57 ?  99  ASN   A H    1 
ATOM   2053 H  H    B ASN   A 1 99  ? 23.878 -2.332  -9.479  0.40 16.76 ?  99  ASN   A H    1 
ATOM   2054 H  HA   A ASN   A 1 99  ? 21.384 -1.467  -8.652  0.60 17.48 ?  99  ASN   A HA   1 
ATOM   2055 H  HA   B ASN   A 1 99  ? 21.406 -1.450  -8.837  0.40 18.16 ?  99  ASN   A HA   1 
ATOM   2056 H  HB2  A ASN   A 1 99  ? 23.190 0.021   -8.162  0.60 17.23 ?  99  ASN   A HB2  1 
ATOM   2057 H  HB2  B ASN   A 1 99  ? 23.287 0.026   -8.691  0.40 19.40 ?  99  ASN   A HB2  1 
ATOM   2058 H  HB3  A ASN   A 1 99  ? 23.383 0.220   -9.725  0.60 17.23 ?  99  ASN   A HB3  1 
ATOM   2059 H  HB3  B ASN   A 1 99  ? 23.447 -0.111  -10.267 0.40 19.40 ?  99  ASN   A HB3  1 
ATOM   2060 H  HD21 A ASN   A 1 99  ? 21.420 2.863   -8.150  0.60 17.19 ?  99  ASN   A HD21 1 
ATOM   2061 H  HD21 B ASN   A 1 99  ? 21.628 2.844   -9.169  0.40 21.44 ?  99  ASN   A HD21 1 
ATOM   2062 H  HD22 A ASN   A 1 99  ? 22.680 2.199   -7.716  0.60 17.19 ?  99  ASN   A HD22 1 
ATOM   2063 H  HD22 B ASN   A 1 99  ? 22.843 2.208   -8.590  0.40 21.44 ?  99  ASN   A HD22 1 
ATOM   2064 N  N    A VAL   A 1 100 ? 20.335 -1.985  -10.794 0.60 16.62 ?  100 VAL   A N    1 
ATOM   2065 N  N    B VAL   A 1 100 ? 20.252 -2.144  -10.898 0.40 17.47 ?  100 VAL   A N    1 
ATOM   2066 C  CA   A VAL   A 1 100 ? 19.695 -2.180  -12.092 0.60 18.24 ?  100 VAL   A CA   1 
ATOM   2067 C  CA   B VAL   A 1 100 ? 19.605 -2.527  -12.149 0.40 19.41 ?  100 VAL   A CA   1 
ATOM   2068 C  C    A VAL   A 1 100 ? 19.569 -0.860  -12.843 0.60 18.32 ?  100 VAL   A C    1 
ATOM   2069 C  C    B VAL   A 1 100 ? 19.613 -1.374  -13.137 0.40 20.14 ?  100 VAL   A C    1 
ATOM   2070 O  O    A VAL   A 1 100 ? 19.655 -0.827  -14.076 0.60 18.79 ?  100 VAL   A O    1 
ATOM   2071 O  O    B VAL   A 1 100 ? 19.686 -1.589  -14.354 0.40 20.60 ?  100 VAL   A O    1 
ATOM   2072 C  CB   A VAL   A 1 100 ? 18.338 -2.898  -11.914 0.60 19.88 ?  100 VAL   A CB   1 
ATOM   2073 C  CB   B VAL   A 1 100 ? 18.172 -3.015  -11.876 0.40 20.57 ?  100 VAL   A CB   1 
ATOM   2074 C  CG1  A VAL   A 1 100 ? 17.582 -2.985  -13.235 0.60 20.57 ?  100 VAL   A CG1  1 
ATOM   2075 C  CG1  B VAL   A 1 100 ? 17.529 -3.517  -13.160 0.40 20.93 ?  100 VAL   A CG1  1 
ATOM   2076 C  CG2  A VAL   A 1 100 ? 18.553 -4.295  -11.339 0.60 20.27 ?  100 VAL   A CG2  1 
ATOM   2077 C  CG2  B VAL   A 1 100 ? 18.188 -4.094  -10.821 0.40 21.05 ?  100 VAL   A CG2  1 
ATOM   2078 H  H    A VAL   A 1 100 ? 19.854 -2.238  -10.122 0.60 19.98 ?  100 VAL   A H    1 
ATOM   2079 H  H    B VAL   A 1 100 ? 19.736 -2.153  -10.212 0.40 21.00 ?  100 VAL   A H    1 
ATOM   2080 H  HA   A VAL   A 1 100 ? 20.253 -2.766  -12.624 0.60 21.92 ?  100 VAL   A HA   1 
ATOM   2081 H  HA   B VAL   A 1 100 ? 20.102 -3.255  -12.548 0.40 23.33 ?  100 VAL   A HA   1 
ATOM   2082 H  HB   A VAL   A 1 100 ? 17.788 -2.402  -11.288 0.60 23.90 ?  100 VAL   A HB   1 
ATOM   2083 H  HB   B VAL   A 1 100 ? 17.645 -2.268  -11.548 0.40 24.72 ?  100 VAL   A HB   1 
ATOM   2084 H  HG11 A VAL   A 1 100 ? 16.847 -3.615  -13.140 0.60 24.73 ?  100 VAL   A HG11 1 
ATOM   2085 H  HG11 B VAL   A 1 100 ? 16.676 -3.921  -12.943 0.40 25.16 ?  100 VAL   A HG11 1 
ATOM   2086 H  HG12 A VAL   A 1 100 ? 17.237 -2.110  -13.463 0.60 24.73 ?  100 VAL   A HG12 1 
ATOM   2087 H  HG12 B VAL   A 1 100 ? 17.396 -2.769  -13.766 0.40 25.16 ?  100 VAL   A HG12 1 
ATOM   2088 H  HG13 A VAL   A 1 100 ? 18.189 -3.296  -13.926 0.60 24.73 ?  100 VAL   A HG13 1 
ATOM   2089 H  HG13 B VAL   A 1 100 ? 18.114 -4.173  -13.569 0.40 25.16 ?  100 VAL   A HG13 1 
ATOM   2090 H  HG21 A VAL   A 1 100 ? 17.695 -4.746  -11.263 0.60 24.36 ?  100 VAL   A HG21 1 
ATOM   2091 H  HG21 B VAL   A 1 100 ? 17.327 -4.531  -10.812 0.40 25.30 ?  100 VAL   A HG21 1 
ATOM   2092 H  HG22 A VAL   A 1 100 ? 19.134 -4.796  -11.933 0.60 24.36 ?  100 VAL   A HG22 1 
ATOM   2093 H  HG22 B VAL   A 1 100 ? 18.887 -4.731  -11.040 0.40 25.30 ?  100 VAL   A HG22 1 
ATOM   2094 H  HG23 A VAL   A 1 100 ? 18.962 -4.218  -10.464 0.60 24.36 ?  100 VAL   A HG23 1 
ATOM   2095 H  HG23 B VAL   A 1 100 ? 18.368 -3.688  -9.959  0.40 25.30 ?  100 VAL   A HG23 1 
ATOM   2096 N  N    A ASN   A 1 101 ? 19.368 0.244   -12.129 0.60 19.31 ?  101 ASN   A N    1 
ATOM   2097 N  N    B ASN   A 1 101 ? 19.513 -0.140  -12.639 0.40 20.77 ?  101 ASN   A N    1 
ATOM   2098 C  CA   A ASN   A 1 101 ? 19.295 1.535   -12.806 0.60 20.21 ?  101 ASN   A CA   1 
ATOM   2099 C  CA   B ASN   A 1 101 ? 19.495 1.022   -13.516 0.40 21.53 ?  101 ASN   A CA   1 
ATOM   2100 C  C    A ASN   A 1 101 ? 20.643 1.987   -13.368 0.60 22.34 ?  101 ASN   A C    1 
ATOM   2101 C  C    B ASN   A 1 101 ? 20.862 1.305   -14.121 0.40 22.54 ?  101 ASN   A C    1 
ATOM   2102 O  O    A ASN   A 1 101 ? 20.704 3.042   -14.015 0.60 23.78 ?  101 ASN   A O    1 
ATOM   2103 O  O    B ASN   A 1 101 ? 20.937 1.984   -15.152 0.40 22.72 ?  101 ASN   A O    1 
ATOM   2104 C  CB   A ASN   A 1 101 ? 18.681 2.577   -11.871 0.60 19.40 ?  101 ASN   A CB   1 
ATOM   2105 C  CB   B ASN   A 1 101 ? 18.970 2.236   -12.746 0.40 21.44 ?  101 ASN   A CB   1 
ATOM   2106 C  CG   A ASN   A 1 101 ? 17.292 2.177   -11.394 0.60 18.68 ?  101 ASN   A CG   1 
ATOM   2107 C  CG   B ASN   A 1 101 ? 17.726 1.916   -11.934 0.40 21.76 ?  101 ASN   A CG   1 
ATOM   2108 O  OD1  A ASN   A 1 101 ? 16.461 1.717   -12.178 0.60 19.13 ?  101 ASN   A OD1  1 
ATOM   2109 O  OD1  B ASN   A 1 101 ? 16.798 1.268   -12.422 0.40 22.31 ?  101 ASN   A OD1  1 
ATOM   2110 N  ND2  A ASN   A 1 101 ? 17.041 2.336   -10.102 0.60 18.28 ?  101 ASN   A ND2  1 
ATOM   2111 N  ND2  B ASN   A 1 101 ? 17.709 2.355   -10.682 0.40 21.80 ?  101 ASN   A ND2  1 
ATOM   2112 H  H    A ASN   A 1 101 ? 19.262 0.268   -11.277 0.60 23.21 ?  101 ASN   A H    1 
ATOM   2113 H  H    B ASN   A 1 101 ? 19.452 0.051   -11.800 0.40 24.97 ?  101 ASN   A H    1 
ATOM   2114 H  HA   A ASN   A 1 101 ? 18.693 1.439   -13.558 0.60 24.30 ?  101 ASN   A HA   1 
ATOM   2115 H  HA   B ASN   A 1 101 ? 18.890 0.859   -14.249 0.40 25.88 ?  101 ASN   A HA   1 
ATOM   2116 H  HB2  A ASN   A 1 101 ? 19.246 2.683   -11.094 0.60 23.33 ?  101 ASN   A HB2  1 
ATOM   2117 H  HB2  B ASN   A 1 101 ? 19.656 2.544   -12.136 0.40 25.77 ?  101 ASN   A HB2  1 
ATOM   2118 H  HB3  A ASN   A 1 101 ? 18.604 3.419   -12.349 0.60 23.33 ?  101 ASN   A HB3  1 
ATOM   2119 H  HB3  B ASN   A 1 101 ? 18.742 2.943   -13.374 0.40 25.77 ?  101 ASN   A HB3  1 
ATOM   2120 H  HD21 A ASN   A 1 101 ? 16.272 2.122   -9.785  0.60 21.98 ?  101 ASN   A HD21 1 
ATOM   2121 H  HD21 B ASN   A 1 101 ? 17.027 2.197   -10.182 0.40 26.20 ?  101 ASN   A HD21 1 
ATOM   2122 H  HD22 A ASN   A 1 101 ? 17.643 2.657   -9.586  0.60 21.98 ?  101 ASN   A HD22 1 
ATOM   2123 H  HD22 B ASN   A 1 101 ? 18.375 2.803   -10.374 0.40 26.20 ?  101 ASN   A HD22 1 
ATOM   2124 N  N    A LYS   A 1 102 ? 21.710 1.211   -13.152 0.60 24.20 ?  102 LYS   A N    1 
ATOM   2125 N  N    B LYS   A 1 102 ? 21.935 0.799   -13.514 0.40 23.82 ?  102 LYS   A N    1 
ATOM   2126 C  CA   A LYS   A 1 102 ? 22.987 1.409   -13.823 0.60 25.65 ?  102 LYS   A CA   1 
ATOM   2127 C  CA   B LYS   A 1 102 ? 23.270 0.868   -14.094 0.40 24.47 ?  102 LYS   A CA   1 
ATOM   2128 C  C    A LYS   A 1 102 ? 23.295 0.313   -14.834 0.60 25.83 ?  102 LYS   A C    1 
ATOM   2129 C  C    B LYS   A 1 102 ? 23.547 -0.294  -15.039 0.40 24.13 ?  102 LYS   A C    1 
ATOM   2130 O  O    A LYS   A 1 102 ? 24.364 0.346   -15.453 0.60 26.42 ?  102 LYS   A O    1 
ATOM   2131 O  O    B LYS   A 1 102 ? 24.673 -0.421  -15.531 0.40 23.80 ?  102 LYS   A O    1 
ATOM   2132 C  CB   A LYS   A 1 102 ? 24.127 1.485   -12.799 0.60 27.25 ?  102 LYS   A CB   1 
ATOM   2133 C  CB   B LYS   A 1 102 ? 24.337 0.864   -12.989 0.40 25.54 ?  102 LYS   A CB   1 
ATOM   2134 C  CG   A LYS   A 1 102 ? 23.993 2.603   -11.784 0.60 28.49 ?  102 LYS   A CG   1 
ATOM   2135 C  CG   B LYS   A 1 102 ? 24.322 2.074   -12.064 0.40 26.27 ?  102 LYS   A CG   1 
ATOM   2136 C  CD   A LYS   A 1 102 ? 25.168 2.591   -10.817 0.60 29.72 ?  102 LYS   A CD   1 
ATOM   2137 C  CD   B LYS   A 1 102 ? 25.359 1.922   -10.949 0.40 26.95 ?  102 LYS   A CD   1 
ATOM   2138 C  CE   A LYS   A 1 102 ? 25.056 3.692   -9.776  0.60 30.67 ?  102 LYS   A CE   1 
ATOM   2139 C  CE   B LYS   A 1 102 ? 25.238 3.028   -9.910  0.40 27.60 ?  102 LYS   A CE   1 
ATOM   2140 N  NZ   A LYS   A 1 102 ? 26.157 3.610   -8.772  0.60 31.08 ?  102 LYS   A NZ   1 
ATOM   2141 N  NZ   B LYS   A 1 102 ? 25.305 2.495   -8.515  0.40 27.84 ?  102 LYS   A NZ   1 
ATOM   2142 H  H    A LYS   A 1 102 ? 21.716 0.540   -12.608 0.60 29.08 ?  102 LYS   A H    1 
ATOM   2143 H  H    B LYS   A 1 102 ? 21.911 0.392   -12.755 0.40 28.63 ?  102 LYS   A H    1 
ATOM   2144 H  HA   A LYS   A 1 102 ? 22.965 2.241   -14.306 0.60 30.82 ?  102 LYS   A HA   1 
ATOM   2145 H  HA   B LYS   A 1 102 ? 23.357 1.703   -14.583 0.40 29.41 ?  102 LYS   A HA   1 
ATOM   2146 H  HB2  A LYS   A 1 102 ? 24.163 0.649   -12.308 0.60 32.74 ?  102 LYS   A HB2  1 
ATOM   2147 H  HB2  B LYS   A 1 102 ? 24.209 0.076   -12.439 0.40 30.69 ?  102 LYS   A HB2  1 
ATOM   2148 H  HB3  A LYS   A 1 102 ? 24.962 1.620   -13.273 0.60 32.74 ?  102 LYS   A HB3  1 
ATOM   2149 H  HB3  B LYS   A 1 102 ? 25.213 0.829   -13.407 0.40 30.69 ?  102 LYS   A HB3  1 
ATOM   2150 H  HG2  A LYS   A 1 102 ? 23.982 3.457   -12.245 0.60 34.23 ?  102 LYS   A HG2  1 
ATOM   2151 H  HG2  B LYS   A 1 102 ? 24.539 2.872   -12.571 0.40 31.57 ?  102 LYS   A HG2  1 
ATOM   2152 H  HG3  A LYS   A 1 102 ? 23.175 2.482   -11.276 0.60 34.23 ?  102 LYS   A HG3  1 
ATOM   2153 H  HG3  B LYS   A 1 102 ? 23.447 2.160   -11.657 0.40 31.57 ?  102 LYS   A HG3  1 
ATOM   2154 H  HD2  A LYS   A 1 102 ? 25.192 1.737   -10.357 0.60 35.71 ?  102 LYS   A HD2  1 
ATOM   2155 H  HD2  B LYS   A 1 102 ? 25.236 1.070   -10.503 0.40 32.38 ?  102 LYS   A HD2  1 
ATOM   2156 H  HD3  A LYS   A 1 102 ? 25.990 2.725   -11.315 0.60 35.71 ?  102 LYS   A HD3  1 
ATOM   2157 H  HD3  B LYS   A 1 102 ? 26.249 1.967   -11.335 0.40 32.38 ?  102 LYS   A HD3  1 
ATOM   2158 H  HE2  A LYS   A 1 102 ? 25.108 4.555   -10.217 0.60 36.85 ?  102 LYS   A HE2  1 
ATOM   2159 H  HE2  B LYS   A 1 102 ? 25.969 3.656   -10.028 0.40 33.16 ?  102 LYS   A HE2  1 
ATOM   2160 H  HE3  A LYS   A 1 102 ? 24.210 3.605   -9.309  0.60 36.85 ?  102 LYS   A HE3  1 
ATOM   2161 H  HE3  B LYS   A 1 102 ? 24.388 3.480   -10.022 0.40 33.16 ?  102 LYS   A HE3  1 
ATOM   2162 H  HZ1  A LYS   A 1 102 ? 26.072 4.262   -8.174  0.60 37.34 ?  102 LYS   A HZ1  1 
ATOM   2163 H  HZ1  B LYS   A 1 102 ? 25.112 3.140   -7.933  0.40 33.45 ?  102 LYS   A HZ1  1 
ATOM   2164 H  HZ2  A LYS   A 1 102 ? 26.127 2.825   -8.353  0.60 37.34 ?  102 LYS   A HZ2  1 
ATOM   2165 H  HZ2  B LYS   A 1 102 ? 24.720 1.832   -8.415  0.40 33.45 ?  102 LYS   A HZ2  1 
ATOM   2166 H  HZ3  A LYS   A 1 102 ? 26.945 3.690   -9.179  0.60 37.34 ?  102 LYS   A HZ3  1 
ATOM   2167 H  HZ3  B LYS   A 1 102 ? 26.121 2.186   -8.346  0.40 33.45 ?  102 LYS   A HZ3  1 
ATOM   2168 N  N    A GLY   A 1 103 ? 22.398 -0.655  -15.015 0.60 26.64 ?  103 GLY   A N    1 
ATOM   2169 N  N    B GLY   A 1 103 ? 22.562 -1.155  -15.284 0.40 23.88 ?  103 GLY   A N    1 
ATOM   2170 C  CA   A GLY   A 1 103 ? 22.635 -1.746  -15.939 0.60 26.66 ?  103 GLY   A CA   1 
ATOM   2171 C  CA   B GLY   A 1 103 ? 22.779 -2.313  -16.130 0.40 23.12 ?  103 GLY   A CA   1 
ATOM   2172 C  C    A GLY   A 1 103 ? 23.501 -2.862  -15.405 0.60 26.73 ?  103 GLY   A C    1 
ATOM   2173 C  C    B GLY   A 1 103 ? 23.610 -3.414  -15.507 0.40 21.90 ?  103 GLY   A C    1 
ATOM   2174 O  O    A GLY   A 1 103 ? 24.115 -3.580  -16.199 0.60 27.62 ?  103 GLY   A O    1 
ATOM   2175 O  O    B GLY   A 1 103 ? 24.088 -4.300  -16.221 0.40 22.19 ?  103 GLY   A O    1 
ATOM   2176 H  H    A GLY   A 1 103 ? 21.645 -0.705  -14.610 0.60 32.01 ?  103 GLY   A H    1 
ATOM   2177 H  H    B GLY   A 1 103 ? 21.762 -1.083  -14.972 0.40 28.70 ?  103 GLY   A H    1 
ATOM   2178 H  HA2  A GLY   A 1 103 ? 21.781 -2.121  -16.217 0.60 32.04 ?  103 GLY   A HA2  1 
ATOM   2179 H  HA2  B GLY   A 1 103 ? 21.921 -2.693  -16.362 0.40 27.78 ?  103 GLY   A HA2  1 
ATOM   2180 H  HA3  A GLY   A 1 103 ? 23.080 -1.404  -16.728 0.60 32.04 ?  103 GLY   A HA3  1 
ATOM   2181 H  HA3  B GLY   A 1 103 ? 23.208 -2.014  -16.950 0.40 27.78 ?  103 GLY   A HA3  1 
ATOM   2182 N  N    A GLU   A 1 104 ? 23.578 -3.031  -14.088 0.60 25.36 ?  104 GLU   A N    1 
ATOM   2183 N  N    B GLU   A 1 104 ? 23.780 -3.402  -14.189 0.40 20.26 ?  104 GLU   A N    1 
ATOM   2184 C  CA   A GLU   A 1 104 ? 24.453 -4.032  -13.493 0.60 23.88 ?  104 GLU   A CA   1 
ATOM   2185 C  CA   B GLU   A 1 104 ? 24.674 -4.348  -13.536 0.40 18.56 ?  104 GLU   A CA   1 
ATOM   2186 C  C    A GLU   A 1 104 ? 23.764 -5.392  -13.400 0.60 24.08 ?  104 GLU   A C    1 
ATOM   2187 C  C    B GLU   A 1 104 ? 24.005 -5.713  -13.381 0.40 18.78 ?  104 GLU   A C    1 
ATOM   2188 O  O    A GLU   A 1 104 ? 22.537 -5.489  -13.308 0.60 24.58 ?  104 GLU   A O    1 
ATOM   2189 O  O    B GLU   A 1 104 ? 22.795 -5.813  -13.151 0.40 19.15 ?  104 GLU   A O    1 
ATOM   2190 C  CB   A GLU   A 1 104 ? 24.953 -3.551  -12.128 0.60 22.76 ?  104 GLU   A CB   1 
ATOM   2191 C  CB   B GLU   A 1 104 ? 25.135 -3.785  -12.189 0.40 17.89 ?  104 GLU   A CB   1 
ATOM   2192 C  CG   A GLU   A 1 104 ? 25.910 -2.364  -12.282 0.60 22.26 ?  104 GLU   A CG   1 
ATOM   2193 C  CG   B GLU   A 1 104 ? 25.914 -2.476  -12.356 0.40 18.15 ?  104 GLU   A CG   1 
ATOM   2194 C  CD   A GLU   A 1 104 ? 26.203 -1.587  -11.012 0.60 21.29 ?  104 GLU   A CD   1 
ATOM   2195 C  CD   B GLU   A 1 104 ? 26.303 -1.789  -11.055 0.40 17.97 ?  104 GLU   A CD   1 
ATOM   2196 O  OE1  A GLU   A 1 104 ? 25.616 -1.880  -9.952  0.60 19.86 ?  104 GLU   A OE1  1 
ATOM   2197 O  OE1  B GLU   A 1 104 ? 25.754 -2.120  -9.984  0.40 17.22 ?  104 GLU   A OE1  1 
ATOM   2198 O  OE2  A GLU   A 1 104 ? 27.029 -0.650  -11.100 0.60 21.99 -1 104 GLU   A OE2  1 
ATOM   2199 O  OE2  B GLU   A 1 104 ? 27.171 -0.891  -11.119 0.40 18.85 -1 104 GLU   A OE2  1 
ATOM   2200 H  H    A GLU   A 1 104 ? 23.140 -2.565  -13.512 0.60 30.48 ?  104 GLU   A H    1 
ATOM   2201 H  H    B GLU   A 1 104 ? 23.383 -2.856  -13.657 0.40 24.36 ?  104 GLU   A H    1 
ATOM   2202 H  HA   A GLU   A 1 104 ? 25.225 -4.140  -14.067 0.60 28.70 ?  104 GLU   A HA   1 
ATOM   2203 H  HA   B GLU   A 1 104 ? 25.462 -4.460  -14.094 0.40 22.32 ?  104 GLU   A HA   1 
ATOM   2204 H  HB2  A GLU   A 1 104 ? 24.196 -3.272  -11.591 0.60 27.35 ?  104 GLU   A HB2  1 
ATOM   2205 H  HB2  B GLU   A 1 104 ? 24.361 -3.609  -11.635 0.40 21.51 ?  104 GLU   A HB2  1 
ATOM   2206 H  HB3  A GLU   A 1 104 ? 25.429 -4.275  -11.690 0.60 27.35 ?  104 GLU   A HB3  1 
ATOM   2207 H  HB3  B GLU   A 1 104 ? 25.718 -4.430  -11.761 0.40 21.51 ?  104 GLU   A HB3  1 
ATOM   2208 H  HG2  A GLU   A 1 104 ? 26.751 -2.691  -12.630 0.60 26.76 ?  104 GLU   A HG2  1 
ATOM   2209 H  HG2  B GLU   A 1 104 ? 26.733 -2.661  -12.838 0.40 21.82 ?  104 GLU   A HG2  1 
ATOM   2210 H  HG3  A GLU   A 1 104 ? 25.518 -1.733  -12.901 0.60 26.76 ?  104 GLU   A HG3  1 
ATOM   2211 H  HG3  B GLU   A 1 104 ? 25.369 -1.853  -12.863 0.40 21.82 ?  104 GLU   A HG3  1 
ATOM   2212 N  N    A ASP   A 1 105 ? 24.581 -6.445  -13.427 0.60 24.27 ?  105 ASP   A N    1 
ATOM   2213 N  N    B ASP   A 1 105 ? 24.813 -6.764  -13.519 0.40 19.30 ?  105 ASP   A N    1 
ATOM   2214 C  CA   A ASP   A 1 105 ? 24.092 -7.811  -13.576 0.60 24.94 ?  105 ASP   A CA   1 
ATOM   2215 C  CA   B ASP   A 1 105 ? 24.322 -8.139  -13.581 0.40 20.20 ?  105 ASP   A CA   1 
ATOM   2216 C  C    A ASP   A 1 105 ? 23.400 -8.274  -12.297 0.60 22.57 ?  105 ASP   A C    1 
ATOM   2217 C  C    B ASP   A 1 105 ? 23.593 -8.524  -12.299 0.40 19.59 ?  105 ASP   A C    1 
ATOM   2218 O  O    A ASP   A 1 105 ? 24.039 -8.398  -11.248 0.60 20.83 ?  105 ASP   A O    1 
ATOM   2219 O  O    B ASP   A 1 105 ? 24.169 -8.484  -11.208 0.40 18.49 ?  105 ASP   A O    1 
ATOM   2220 C  CB   A ASP   A 1 105 ? 25.272 -8.725  -13.904 0.60 27.91 ?  105 ASP   A CB   1 
ATOM   2221 C  CB   B ASP   A 1 105 ? 25.523 -9.060  -13.803 0.40 21.80 ?  105 ASP   A CB   1 
ATOM   2222 C  CG   A ASP   A 1 105 ? 24.844 -10.141 -14.217 0.60 30.46 ?  105 ASP   A CG   1 
ATOM   2223 C  CG   B ASP   A 1 105 ? 25.155 -10.532 -13.827 0.40 23.09 ?  105 ASP   A CG   1 
ATOM   2224 O  OD1  A ASP   A 1 105 ? 23.623 -10.382 -14.314 0.60 31.10 ?  105 ASP   A OD1  1 
ATOM   2225 O  OD1  B ASP   A 1 105 ? 23.956 -10.862 -13.939 0.40 23.03 ?  105 ASP   A OD1  1 
ATOM   2226 O  OD2  A ASP   A 1 105 ? 25.729 -11.009 -14.376 0.60 31.78 -1 105 ASP   A OD2  1 
ATOM   2227 O  OD2  B ASP   A 1 105 ? 26.086 -11.366 -13.727 0.40 24.19 -1 105 ASP   A OD2  1 
ATOM   2228 H  H    A ASP   A 1 105 ? 25.437 -6.394  -13.357 0.60 29.16 ?  105 ASP   A H    1 
ATOM   2229 H  H    B ASP   A 1 105 ? 25.666 -6.696  -13.585 0.40 23.20 ?  105 ASP   A H    1 
ATOM   2230 H  HA   A ASP   A 1 105 ? 23.458 -7.860  -14.307 0.60 29.97 ?  105 ASP   A HA   1 
ATOM   2231 H  HA   B ASP   A 1 105 ? 23.707 -8.228  -14.328 0.40 24.28 ?  105 ASP   A HA   1 
ATOM   2232 H  HB2  A ASP   A 1 105 ? 25.734 -8.383  -14.687 0.60 33.54 ?  105 ASP   A HB2  1 
ATOM   2233 H  HB2  B ASP   A 1 105 ? 25.941 -8.826  -14.646 0.40 26.21 ?  105 ASP   A HB2  1 
ATOM   2234 H  HB3  A ASP   A 1 105 ? 25.883 -8.743  -13.147 0.60 33.54 ?  105 ASP   A HB3  1 
ATOM   2235 H  HB3  B ASP   A 1 105 ? 26.145 -8.939  -13.074 0.40 26.21 ?  105 ASP   A HB3  1 
ATOM   2236 N  N    A ILE   A 1 106 ? 22.097 -8.553  -12.390 0.60 22.28 ?  106 ILE   A N    1 
ATOM   2237 N  N    B ILE   A 1 106 ? 22.327 -8.926  -12.434 0.40 19.88 ?  106 ILE   A N    1 
ATOM   2238 C  CA   A ILE   A 1 106 ? 21.336 -8.982  -11.222 0.60 21.83 ?  106 ILE   A CA   1 
ATOM   2239 C  CA   B ILE   A 1 106 ? 21.536 -9.283  -11.262 0.40 20.30 ?  106 ILE   A CA   1 
ATOM   2240 C  C    A ILE   A 1 106 ? 21.886 -10.271 -10.631 0.60 20.66 ?  106 ILE   A C    1 
ATOM   2241 C  C    B ILE   A 1 106 ? 22.054 -10.548 -10.591 0.40 19.72 ?  106 ILE   A C    1 
ATOM   2242 O  O    A ILE   A 1 106 ? 21.686 -10.538 -9.442  0.60 19.85 ?  106 ILE   A O    1 
ATOM   2243 O  O    B ILE   A 1 106 ? 21.811 -10.751 -9.396  0.40 19.45 ?  106 ILE   A O    1 
ATOM   2244 C  CB   A ILE   A 1 106 ? 19.831 -9.089  -11.562 0.60 23.18 ?  106 ILE   A CB   1 
ATOM   2245 C  CB   B ILE   A 1 106 ? 20.039 -9.381  -11.623 0.40 21.61 ?  106 ILE   A CB   1 
ATOM   2246 C  CG1  A ILE   A 1 106 ? 18.991 -9.188  -10.285 0.60 23.80 ?  106 ILE   A CG1  1 
ATOM   2247 C  CG1  B ILE   A 1 106 ? 19.172 -9.366  -10.362 0.40 22.30 ?  106 ILE   A CG1  1 
ATOM   2248 C  CG2  A ILE   A 1 106 ? 19.565 -10.293 -12.452 0.60 23.73 ?  106 ILE   A CG2  1 
ATOM   2249 C  CG2  B ILE   A 1 106 ? 19.763 -10.640 -12.421 0.40 21.98 ?  106 ILE   A CG2  1 
ATOM   2250 C  CD1  A ILE   A 1 106 ? 19.142 -8.003  -9.357  0.60 24.09 ?  106 ILE   A CD1  1 
ATOM   2251 C  CD1  B ILE   A 1 106 ? 19.280 -8.091  -9.553  0.40 22.61 ?  106 ILE   A CD1  1 
ATOM   2252 H  H    A ILE   A 1 106 ? 21.640 -8.496  -13.112 0.60 26.78 ?  106 ILE   A H    1 
ATOM   2253 H  H    B ILE   A 1 106 ? 21.914 -8.997  -13.182 0.40 23.90 ?  106 ILE   A H    1 
ATOM   2254 H  HA   A ILE   A 1 106 ? 21.436 -8.305  -10.543 0.60 26.24 ?  106 ILE   A HA   1 
ATOM   2255 H  HA   B ILE   A 1 106 ? 21.632 -8.572  -10.615 0.40 24.41 ?  106 ILE   A HA   1 
ATOM   2256 H  HB   A ILE   A 1 106 ? 19.568 -8.290  -12.043 0.60 27.86 ?  106 ILE   A HB   1 
ATOM   2257 H  HB   B ILE   A 1 106 ? 19.803 -8.613  -12.167 0.40 25.97 ?  106 ILE   A HB   1 
ATOM   2258 H  HG12 A ILE   A 1 106 ? 18.054 -9.248  -10.533 0.60 28.61 ?  106 ILE   A HG12 1 
ATOM   2259 H  HG12 B ILE   A 1 106 ? 18.242 -9.469  -10.621 0.40 26.81 ?  106 ILE   A HG12 1 
ATOM   2260 H  HG13 A ILE   A 1 106 ? 19.252 -9.983  -9.797  0.60 28.61 ?  106 ILE   A HG13 1 
ATOM   2261 H  HG13 B ILE   A 1 106 ? 19.436 -10.101 -9.789  0.40 26.81 ?  106 ILE   A HG13 1 
ATOM   2262 H  HG21 A ILE   A 1 106 ? 18.671 -10.218 -12.820 0.60 28.52 ?  106 ILE   A HG21 1 
ATOM   2263 H  HG21 B ILE   A 1 106 ? 18.884 -10.569 -12.823 0.40 26.42 ?  106 ILE   A HG21 1 
ATOM   2264 H  HG22 A ILE   A 1 106 ? 20.219 -10.303 -13.168 0.60 28.52 ?  106 ILE   A HG22 1 
ATOM   2265 H  HG22 B ILE   A 1 106 ? 20.438 -10.727 -13.110 0.40 26.42 ?  106 ILE   A HG22 1 
ATOM   2266 H  HG23 A ILE   A 1 106 ? 19.639 -11.101 -11.922 0.60 28.52 ?  106 ILE   A HG23 1 
ATOM   2267 H  HG23 B ILE   A 1 106 ? 19.795 -11.404 -11.825 0.40 26.42 ?  106 ILE   A HG23 1 
ATOM   2268 H  HD11 A ILE   A 1 106 ? 18.400 -7.993  -8.736  0.60 28.95 ?  106 ILE   A HD11 1 
ATOM   2269 H  HD11 B ILE   A 1 106 ? 18.532 -8.044  -8.939  0.40 27.17 ?  106 ILE   A HD11 1 
ATOM   2270 H  HD12 A ILE   A 1 106 ? 19.979 -8.087  -8.871  0.60 28.95 ?  106 ILE   A HD12 1 
ATOM   2271 H  HD12 B ILE   A 1 106 ? 20.114 -8.100  -9.056  0.40 27.17 ?  106 ILE   A HD12 1 
ATOM   2272 H  HD13 A ILE   A 1 106 ? 19.145 -7.188  -9.884  0.60 28.95 ?  106 ILE   A HD13 1 
ATOM   2273 H  HD13 B ILE   A 1 106 ? 19.261 -7.332  -10.156 0.40 27.17 ?  106 ILE   A HD13 1 
ATOM   2274 N  N    A GLN   A 1 107 ? 22.594 -11.076 -11.431 0.60 21.41 ?  107 GLN   A N    1 
ATOM   2275 N  N    B GLN   A 1 107 ? 22.774 -11.404 -11.325 0.40 19.76 ?  107 GLN   A N    1 
ATOM   2276 C  CA   A GLN   A 1 107 ? 23.208 -12.294 -10.916 0.60 23.13 ?  107 GLN   A CA   1 
ATOM   2277 C  CA   B GLN   A 1 107 ? 23.398 -12.564 -10.699 0.40 20.75 ?  107 GLN   A CA   1 
ATOM   2278 C  C    A GLN   A 1 107 ? 24.189 -12.002 -9.787  0.60 20.49 ?  107 GLN   A C    1 
ATOM   2279 C  C    B GLN   A 1 107 ? 24.367 -12.157 -9.597  0.40 18.52 ?  107 GLN   A C    1 
ATOM   2280 O  O    A GLN   A 1 107 ? 24.426 -12.873 -8.945  0.60 22.23 ?  107 GLN   A O    1 
ATOM   2281 O  O    B GLN   A 1 107 ? 24.623 -12.946 -8.679  0.40 18.81 ?  107 GLN   A O    1 
ATOM   2282 C  CB   A GLN   A 1 107 ? 23.914 -13.048 -12.053 0.60 27.55 ?  107 GLN   A CB   1 
ATOM   2283 C  CB   B GLN   A 1 107 ? 24.107 -13.412 -11.760 0.40 24.03 ?  107 GLN   A CB   1 
ATOM   2284 C  CG   A GLN   A 1 107 ? 23.039 -13.300 -13.278 0.60 32.01 ?  107 GLN   A CG   1 
ATOM   2285 C  CG   B GLN   A 1 107 ? 23.168 -13.944 -12.831 0.40 27.14 ?  107 GLN   A CG   1 
ATOM   2286 C  CD   A GLN   A 1 107 ? 21.773 -14.064 -12.947 0.60 35.66 ?  107 GLN   A CD   1 
ATOM   2287 C  CD   B GLN   A 1 107 ? 22.000 -14.708 -12.242 0.40 29.86 ?  107 GLN   A CD   1 
ATOM   2288 O  OE1  A GLN   A 1 107 ? 21.818 -15.129 -12.331 0.60 37.10 ?  107 GLN   A OE1  1 
ATOM   2289 O  OE1  B GLN   A 1 107 ? 22.179 -15.570 -11.380 0.40 30.81 ?  107 GLN   A OE1  1 
ATOM   2290 N  NE2  A GLN   A 1 107 ? 20.632 -13.519 -13.352 0.60 36.83 ?  107 GLN   A NE2  1 
ATOM   2291 N  NE2  B GLN   A 1 107 ? 20.792 -14.384 -12.692 0.40 30.69 ?  107 GLN   A NE2  1 
ATOM   2292 H  H    A GLN   A 1 107 ? 22.738 -10.934 -12.265 0.60 25.74 ?  107 GLN   A H    1 
ATOM   2293 H  H    B GLN   A 1 107 ? 22.914 -11.334 -12.174 0.40 23.76 ?  107 GLN   A H    1 
ATOM   2294 H  HA   A GLN   A 1 107 ? 22.521 -12.877 -10.563 0.60 27.80 ?  107 GLN   A HA   1 
ATOM   2295 H  HA   B GLN   A 1 107 ? 22.707 -13.108 -10.299 0.40 24.94 ?  107 GLN   A HA   1 
ATOM   2296 H  HB2  A GLN   A 1 107 ? 24.682 -12.533 -12.346 0.60 33.11 ?  107 GLN   A HB2  1 
ATOM   2297 H  HB2  B GLN   A 1 107 ? 24.782 -12.872 -12.202 0.40 28.88 ?  107 GLN   A HB2  1 
ATOM   2298 H  HB3  A GLN   A 1 107 ? 24.208 -13.913 -11.725 0.60 33.11 ?  107 GLN   A HB3  1 
ATOM   2299 H  HB3  B GLN   A 1 107 ? 24.525 -14.174 -11.330 0.40 28.88 ?  107 GLN   A HB3  1 
ATOM   2300 H  HG2  A GLN   A 1 107 ? 22.780 -12.452 -13.667 0.60 38.45 ?  107 GLN   A HG2  1 
ATOM   2301 H  HG2  B GLN   A 1 107 ? 22.816 -13.198 -13.343 0.40 32.61 ?  107 GLN   A HG2  1 
ATOM   2302 H  HG3  A GLN   A 1 107 ? 23.544 -13.819 -13.926 0.60 38.45 ?  107 GLN   A HG3  1 
ATOM   2303 H  HG3  B GLN   A 1 107 ? 23.656 -14.547 -13.413 0.40 32.61 ?  107 GLN   A HG3  1 
ATOM   2304 H  HE21 A GLN   A 1 107 ? 20.639 -12.774 -13.779 0.60 44.24 ?  107 GLN   A HE21 1 
ATOM   2305 H  HE21 B GLN   A 1 107 ? 20.707 -13.773 -13.292 0.40 36.87 ?  107 GLN   A HE21 1 
ATOM   2306 H  HE22 A GLN   A 1 107 ? 19.887 -13.915 -13.187 0.60 44.24 ?  107 GLN   A HE22 1 
ATOM   2307 H  HE22 B GLN   A 1 107 ? 20.096 -14.783 -12.384 0.40 36.87 ?  107 GLN   A HE22 1 
ATOM   2308 N  N    A LEU   A 1 108 ? 24.741 -10.786 -9.732  0.60 16.26 ?  108 LEU   A N    1 
ATOM   2309 N  N    B LEU   A 1 108 ? 24.893 -10.933 -9.656  0.40 16.26 ?  108 LEU   A N    1 
ATOM   2310 C  CA   A LEU   A 1 108 ? 25.683 -10.426 -8.679  0.60 14.26 ?  108 LEU   A CA   1 
ATOM   2311 C  CA   B LEU   A 1 108 ? 25.753 -10.422 -8.600  0.40 14.82 ?  108 LEU   A CA   1 
ATOM   2312 C  C    A LEU   A 1 108 ? 25.007 -10.260 -7.325  0.60 12.62 ?  108 LEU   A C    1 
ATOM   2313 C  C    B LEU   A 1 108 ? 25.009 -10.213 -7.288  0.40 13.21 ?  108 LEU   A C    1 
ATOM   2314 O  O    A LEU   A 1 108 ? 25.704 -10.138 -6.313  0.60 12.82 ?  108 LEU   A O    1 
ATOM   2315 O  O    B LEU   A 1 108 ? 25.662 -9.995  -6.261  0.40 13.49 ?  108 LEU   A O    1 
ATOM   2316 C  CB   A LEU   A 1 108 ? 26.452 -9.158  -9.068  0.60 14.28 ?  108 LEU   A CB   1 
ATOM   2317 C  CB   B LEU   A 1 108 ? 26.427 -9.122  -9.051  0.40 15.16 ?  108 LEU   A CB   1 
ATOM   2318 C  CG   A LEU   A 1 108 ? 27.423 -9.361  -10.235 0.60 16.00 ?  108 LEU   A CG   1 
ATOM   2319 C  CG   B LEU   A 1 108 ? 27.474 -9.292  -10.154 0.40 16.45 ?  108 LEU   A CG   1 
ATOM   2320 C  CD1  A LEU   A 1 108 ? 27.929 -8.030  -10.771 0.60 16.55 ?  108 LEU   A CD1  1 
ATOM   2321 C  CD1  B LEU   A 1 108 ? 27.832 -7.952  -10.782 0.40 16.85 ?  108 LEU   A CD1  1 
ATOM   2322 C  CD2  A LEU   A 1 108 ? 28.591 -10.245 -9.819  0.60 17.30 ?  108 LEU   A CD2  1 
ATOM   2323 C  CD2  B LEU   A 1 108 ? 28.719 -9.971  -9.606  0.40 17.41 ?  108 LEU   A CD2  1 
ATOM   2324 H  H    A LEU   A 1 108 ? 24.572 -10.158 -10.288 0.60 19.56 ?  108 LEU   A H    1 
ATOM   2325 H  H    B LEU   A 1 108 ? 24.764 -10.386 -10.302 0.40 19.56 ?  108 LEU   A H    1 
ATOM   2326 H  HA   A LEU   A 1 108 ? 26.325 -11.144 -8.587  0.60 17.16 ?  108 LEU   A HA   1 
ATOM   2327 H  HA   B LEU   A 1 108 ? 26.449 -11.072 -8.431  0.40 17.83 ?  108 LEU   A HA   1 
ATOM   2328 H  HB2  A LEU   A 1 108 ? 25.815 -8.475  -9.331  0.60 17.18 ?  108 LEU   A HB2  1 
ATOM   2329 H  HB2  B LEU   A 1 108 ? 25.746 -8.518  -9.385  0.40 18.24 ?  108 LEU   A HB2  1 
ATOM   2330 H  HB3  A LEU   A 1 108 ? 26.964 -8.857  -8.305  0.60 17.18 ?  108 LEU   A HB3  1 
ATOM   2331 H  HB3  B LEU   A 1 108 ? 26.870 -8.724  -8.288  0.40 18.24 ?  108 LEU   A HB3  1 
ATOM   2332 H  HG   A LEU   A 1 108 ? 26.957 -9.811  -10.957 0.60 19.24 ?  108 LEU   A HG   1 
ATOM   2333 H  HG   B LEU   A 1 108 ? 27.110 -9.859  -10.852 0.40 19.78 ?  108 LEU   A HG   1 
ATOM   2334 H  HD11 A LEU   A 1 108 ? 28.536 -8.196  -11.511 0.60 19.90 ?  108 LEU   A HD11 1 
ATOM   2335 H  HD11 B LEU   A 1 108 ? 28.443 -8.103  -11.522 0.40 20.26 ?  108 LEU   A HD11 1 
ATOM   2336 H  HD12 A LEU   A 1 108 ? 27.173 -7.504  -11.077 0.60 19.90 ?  108 LEU   A HD12 1 
ATOM   2337 H  HD12 B LEU   A 1 108 ? 27.022 -7.528  -11.105 0.40 20.26 ?  108 LEU   A HD12 1 
ATOM   2338 H  HD13 A LEU   A 1 108 ? 28.395 -7.559  -10.062 0.60 19.90 ?  108 LEU   A HD13 1 
ATOM   2339 H  HD13 B LEU   A 1 108 ? 28.256 -7.392  -10.113 0.40 20.26 ?  108 LEU   A HD13 1 
ATOM   2340 H  HD21 A LEU   A 1 108 ? 29.265 -10.223 -10.515 0.60 20.80 ?  108 LEU   A HD21 1 
ATOM   2341 H  HD21 B LEU   A 1 108 ? 29.405 -9.975  -10.292 0.40 20.93 ?  108 LEU   A HD21 1 
ATOM   2342 H  HD22 A LEU   A 1 108 ? 28.961 -9.904  -8.989  0.60 20.80 ?  108 LEU   A HD22 1 
ATOM   2343 H  HD22 B LEU   A 1 108 ? 29.030 -9.481  -8.829  0.40 20.93 ?  108 LEU   A HD22 1 
ATOM   2344 H  HD23 A LEU   A 1 108 ? 28.272 -11.151 -9.693  0.60 20.80 ?  108 LEU   A HD23 1 
ATOM   2345 H  HD23 B LEU   A 1 108 ? 28.498 -10.882 -9.356  0.40 20.93 ?  108 LEU   A HD23 1 
ATOM   2346 N  N    . LEU   A 1 109 ? 23.673 -10.288 -7.279  1.00 12.49 ?  109 LEU   A N    1 
ATOM   2347 C  CA   . LEU   A 1 109 ? 22.965 -10.170 -6.011  1.00 11.75 ?  109 LEU   A CA   1 
ATOM   2348 C  C    . LEU   A 1 109 ? 23.308 -11.324 -5.075  1.00 11.20 ?  109 LEU   A C    1 
ATOM   2349 O  O    . LEU   A 1 109 ? 23.442 -11.128 -3.863  1.00 11.68 ?  109 LEU   A O    1 
ATOM   2350 C  CB   . LEU   A 1 109 ? 21.462 -10.089 -6.267  1.00 12.65 ?  109 LEU   A CB   1 
ATOM   2351 C  CG   . LEU   A 1 109 ? 20.569 -9.803  -5.062  1.00 12.83 ?  109 LEU   A CG   1 
ATOM   2352 C  CD1  . LEU   A 1 109 ? 21.021 -8.546  -4.337  1.00 12.99 ?  109 LEU   A CD1  1 
ATOM   2353 C  CD2  . LEU   A 1 109 ? 19.118 -9.663  -5.500  1.00 13.91 ?  109 LEU   A CD2  1 
ATOM   2354 H  H    A LEU   A 1 109 ? 23.158 -10.373 -7.963  0.60 15.03 ?  109 LEU   A H    1 
ATOM   2355 H  H    B LEU   A 1 109 ? 23.170 -10.403 -7.968  0.40 15.03 ?  109 LEU   A H    1 
ATOM   2356 H  HA   . LEU   A 1 109 ? 23.241 -9.342  -5.579  1.00 14.14 ?  109 LEU   A HA   1 
ATOM   2357 H  HB2  . LEU   A 1 109 ? 21.303 -9.383  -6.914  1.00 15.22 ?  109 LEU   A HB2  1 
ATOM   2358 H  HB3  . LEU   A 1 109 ? 21.174 -10.935 -6.639  1.00 15.22 ?  109 LEU   A HB3  1 
ATOM   2359 H  HG   . LEU   A 1 109 ? 20.624 -10.542 -4.441  1.00 15.44 ?  109 LEU   A HG   1 
ATOM   2360 H  HD11 . LEU   A 1 109 ? 20.335 -8.268  -3.716  1.00 15.63 ?  109 LEU   A HD11 1 
ATOM   2361 H  HD12 . LEU   A 1 109 ? 21.847 -8.733  -3.860  1.00 15.63 ?  109 LEU   A HD12 1 
ATOM   2362 H  HD13 . LEU   A 1 109 ? 21.177 -7.839  -4.992  1.00 15.63 ?  109 LEU   A HD13 1 
ATOM   2363 H  HD21 . LEU   A 1 109 ? 18.582 -9.381  -4.740  1.00 16.74 ?  109 LEU   A HD21 1 
ATOM   2364 H  HD22 . LEU   A 1 109 ? 19.059 -9.000  -6.206  1.00 16.74 ?  109 LEU   A HD22 1 
ATOM   2365 H  HD23 . LEU   A 1 109 ? 18.800 -10.521 -5.826  1.00 16.74 ?  109 LEU   A HD23 1 
ATOM   2366 N  N    . LYS   A 1 110 ? 23.461 -12.535 -5.615  1.00 10.91 ?  110 LYS   A N    1 
ATOM   2367 C  CA   . LYS   A 1 110 ? 23.834 -13.658 -4.762  1.00 10.96 ?  110 LYS   A CA   1 
ATOM   2368 C  C    . LYS   A 1 110 ? 25.212 -13.437 -4.150  1.00 10.55 ?  110 LYS   A C    1 
ATOM   2369 O  O    . LYS   A 1 110 ? 25.405 -13.646 -2.949  1.00 10.82 ?  110 LYS   A O    1 
ATOM   2370 C  CB   . LYS   A 1 110 ? 23.761 -14.979 -5.532  1.00 11.78 ?  110 LYS   A CB   1 
ATOM   2371 C  CG   . LYS   A 1 110 ? 23.958 -16.196 -4.621  1.00 12.15 ?  110 LYS   A CG   1 
ATOM   2372 C  CD   . LYS   A 1 110 ? 23.727 -17.523 -5.332  1.00 12.57 ?  110 LYS   A CD   1 
ATOM   2373 C  CE   . LYS   A 1 110 ? 23.835 -18.701 -4.374  1.00 13.66 ?  110 LYS   A CE   1 
ATOM   2374 N  NZ   . LYS   A 1 110 ? 22.648 -18.828 -3.493  1.00 13.82 ?  110 LYS   A NZ   1 
ATOM   2375 H  H    . LYS   A 1 110 ? 23.358 -12.723 -6.445  1.00 13.14 ?  110 LYS   A H    1 
ATOM   2376 H  HA   . LYS   A 1 110 ? 23.194 -13.711 -4.032  1.00 13.19 ?  110 LYS   A HA   1 
ATOM   2377 H  HB2  . LYS   A 1 110 ? 22.889 -15.057 -5.950  1.00 14.18 ?  110 LYS   A HB2  1 
ATOM   2378 H  HB3  . LYS   A 1 110 ? 24.458 -14.995 -6.204  1.00 14.18 ?  110 LYS   A HB3  1 
ATOM   2379 H  HG2  . LYS   A 1 110 ? 24.864 -16.191 -4.278  1.00 14.62 ?  110 LYS   A HG2  1 
ATOM   2380 H  HG3  . LYS   A 1 110 ? 23.327 -16.140 -3.882  1.00 14.62 ?  110 LYS   A HG3  1 
ATOM   2381 H  HD2  . LYS   A 1 110 ? 22.842 -17.531 -5.719  1.00 15.13 ?  110 LYS   A HD2  1 
ATOM   2382 H  HD3  . LYS   A 1 110 ? 24.401 -17.635 -6.021  1.00 15.13 ?  110 LYS   A HD3  1 
ATOM   2383 H  HE2  . LYS   A 1 110 ? 23.921 -19.522 -4.883  1.00 16.43 ?  110 LYS   A HE2  1 
ATOM   2384 H  HE3  . LYS   A 1 110 ? 24.616 -18.581 -3.805  1.00 16.43 ?  110 LYS   A HE3  1 
ATOM   2385 H  HZ1  . LYS   A 1 110 ? 22.738 -19.522 -2.948  1.00 16.63 ?  110 LYS   A HZ1  1 
ATOM   2386 H  HZ2  . LYS   A 1 110 ? 22.548 -18.087 -3.006  1.00 16.63 ?  110 LYS   A HZ2  1 
ATOM   2387 H  HZ3  . LYS   A 1 110 ? 21.914 -18.942 -3.989  1.00 16.63 ?  110 LYS   A HZ3  1 
ATOM   2388 N  N    . SER   A 1 111 ? 26.178 -12.995 -4.962  1.00 10.68 ?  111 SER   A N    1 
ATOM   2389 C  CA   . SER   A 1 111 ? 27.506 -12.689 -4.438  1.00 10.75 ?  111 SER   A CA   1 
ATOM   2390 C  C    . SER   A 1 111 ? 27.438 -11.640 -3.335  1.00 10.14 ?  111 SER   A C    1 
ATOM   2391 O  O    . SER   A 1 111 ? 28.136 -11.740 -2.321  1.00 10.96 ?  111 SER   A O    1 
ATOM   2392 C  CB   . SER   A 1 111 ? 28.406 -12.201 -5.571  1.00 12.01 ?  111 SER   A CB   1 
ATOM   2393 O  OG   . SER   A 1 111 ? 28.484 -13.177 -6.599  1.00 14.06 ?  111 SER   A OG   1 
ATOM   2394 H  H    . SER   A 1 111 ? 26.081 -12.863 -5.807  1.00 12.85 ?  111 SER   A H    1 
ATOM   2395 H  HA   . SER   A 1 111 ? 27.893 -13.502 -4.071  1.00 12.94 ?  111 SER   A HA   1 
ATOM   2396 H  HB2  . SER   A 1 111 ? 28.034 -11.388 -5.943  1.00 14.46 ?  111 SER   A HB2  1 
ATOM   2397 H  HB3  . SER   A 1 111 ? 29.293 -12.031 -5.217  1.00 14.46 ?  111 SER   A HB3  1 
ATOM   2398 H  HG   . SER   A 1 111 ? 29.000 -12.898 -7.214  1.00 16.92 ?  111 SER   A HG   1 
ATOM   2399 N  N    . ALA   A 1 112 ? 26.592 -10.628 -3.516  1.00 10.44 ?  112 ALA   A N    1 
ATOM   2400 C  CA   . ALA   A 1 112 ? 26.448 -9.590  -2.501  1.00 10.57 ?  112 ALA   A CA   1 
ATOM   2401 C  C    . ALA   A 1 112 ? 25.965 -10.186 -1.180  1.00 10.14 ?  112 ALA   A C    1 
ATOM   2402 O  O    . ALA   A 1 112 ? 26.515 -9.898  -0.111  1.00 10.45 ?  112 ALA   A O    1 
ATOM   2403 C  CB   . ALA   A 1 112 ? 25.492 -8.502  -3.000  1.00 11.06 ?  112 ALA   A CB   1 
ATOM   2404 H  H    . ALA   A 1 112 ? 26.093 -10.522 -4.208  1.00 12.57 ?  112 ALA   A H    1 
ATOM   2405 H  HA   . ALA   A 1 112 ? 27.312 -9.176  -2.346  1.00 12.72 ?  112 ALA   A HA   1 
ATOM   2406 H  HB1  . ALA   A 1 112 ? 25.421 -7.806  -2.322  1.00 13.32 ?  112 ALA   A HB1  1 
ATOM   2407 H  HB2  . ALA   A 1 112 ? 25.843 -8.121  -3.821  1.00 13.32 ?  112 ALA   A HB2  1 
ATOM   2408 H  HB3  . ALA   A 1 112 ? 24.620 -8.892  -3.162  1.00 13.32 ?  112 ALA   A HB3  1 
ATOM   2409 N  N    . TYR   A 1 113 ? 24.929 -11.026 -1.231  1.00 10.02 ?  113 TYR   A N    1 
ATOM   2410 C  CA   . TYR   A 1 113 ? 24.419 -11.634 -0.005  1.00 9.99  ?  113 TYR   A CA   1 
ATOM   2411 C  C    . TYR   A 1 113 ? 25.421 -12.589 0.641   1.00 9.72  ?  113 TYR   A C    1 
ATOM   2412 O  O    . TYR   A 1 113 ? 25.376 -12.776 1.860   1.00 10.25 ?  113 TYR   A O    1 
ATOM   2413 C  CB   . TYR   A 1 113 ? 23.101 -12.360 -0.274  1.00 10.51 ?  113 TYR   A CB   1 
ATOM   2414 C  CG   . TYR   A 1 113 ? 21.887 -11.463 -0.194  1.00 10.25 ?  113 TYR   A CG   1 
ATOM   2415 C  CD1  . TYR   A 1 113 ? 21.521 -10.866 1.006   1.00 10.46 ?  113 TYR   A CD1  1 
ATOM   2416 C  CD2  . TYR   A 1 113 ? 21.086 -11.241 -1.308  1.00 10.62 ?  113 TYR   A CD2  1 
ATOM   2417 C  CE1  . TYR   A 1 113 ? 20.394 -10.065 1.095   1.00 10.88 ?  113 TYR   A CE1  1 
ATOM   2418 C  CE2  . TYR   A 1 113 ? 19.937 -10.442 -1.224  1.00 11.12 ?  113 TYR   A CE2  1 
ATOM   2419 C  CZ   . TYR   A 1 113 ? 19.609 -9.859  -0.018  1.00 11.00 ?  113 TYR   A CZ   1 
ATOM   2420 O  OH   . TYR   A 1 113 ? 18.479 -9.065  0.097   1.00 11.64 ?  113 TYR   A OH   1 
ATOM   2421 H  H    . TYR   A 1 113 ? 24.513 -11.250 -1.949  1.00 12.07 ?  113 TYR   A H    1 
ATOM   2422 H  HA   . TYR   A 1 113 ? 24.243 -10.930 0.634   1.00 12.03 ?  113 TYR   A HA   1 
ATOM   2423 H  HB2  . TYR   A 1 113 ? 23.126 -12.737 -1.166  1.00 12.66 ?  113 TYR   A HB2  1 
ATOM   2424 H  HB3  . TYR   A 1 113 ? 22.992 -13.063 0.381   1.00 12.66 ?  113 TYR   A HB3  1 
ATOM   2425 H  HD1  . TYR   A 1 113 ? 22.048 -11.010 1.761   1.00 12.60 ?  113 TYR   A HD1  1 
ATOM   2426 H  HD2  . TYR   A 1 113 ? 21.303 -11.643 -2.118  1.00 12.78 ?  113 TYR   A HD2  1 
ATOM   2427 H  HE1  . TYR   A 1 113 ? 20.168 -9.675  1.908   1.00 13.10 ?  113 TYR   A HE1  1 
ATOM   2428 H  HE2  . TYR   A 1 113 ? 19.402 -10.296 -1.973  1.00 13.38 ?  113 TYR   A HE2  1 
ATOM   2429 H  HH   . TYR   A 1 113 ? 18.089 -9.022  -0.655  1.00 14.01 ?  113 TYR   A HH   1 
ATOM   2430 N  N    . GLU   A 1 114 ? 26.326 -13.202 -0.141  1.00 10.29 ?  114 GLU   A N    1 
ATOM   2431 C  CA   . GLU   A 1 114 ? 27.316 -14.103 0.456   1.00 10.22 ?  114 GLU   A CA   1 
ATOM   2432 C  C    . GLU   A 1 114 ? 28.168 -13.393 1.503   1.00 10.27 ?  114 GLU   A C    1 
ATOM   2433 O  O    . GLU   A 1 114 ? 28.643 -14.027 2.455   1.00 10.44 ?  114 GLU   A O    1 
ATOM   2434 C  CB   . GLU   A 1 114 ? 28.189 -14.745 -0.629  1.00 10.47 ?  114 GLU   A CB   1 
ATOM   2435 C  CG   . GLU   A 1 114 ? 27.422 -15.793 -1.420  1.00 11.03 ?  114 GLU   A CG   1 
ATOM   2436 C  CD   . GLU   A 1 114 ? 28.132 -16.329 -2.657  1.00 11.17 ?  114 GLU   A CD   1 
ATOM   2437 O  OE1  . GLU   A 1 114 ? 29.078 -15.692 -3.169  1.00 11.46 ?  114 GLU   A OE1  1 
ATOM   2438 O  OE2  . GLU   A 1 114 ? 27.696 -17.401 -3.136  1.00 12.54 -1 114 GLU   A OE2  1 
ATOM   2439 H  H    . GLU   A 1 114 ? 26.386 -13.109 -1.003  1.00 12.39 ?  114 GLU   A H    1 
ATOM   2440 H  HA   . GLU   A 1 114 ? 26.842 -14.815 0.900   1.00 12.30 ?  114 GLU   A HA   1 
ATOM   2441 H  HB2  . GLU   A 1 114 ? 28.493 -14.064 -1.251  1.00 12.61 ?  114 GLU   A HB2  1 
ATOM   2442 H  HB3  . GLU   A 1 114 ? 28.950 -15.181 -0.214  1.00 12.61 ?  114 GLU   A HB3  1 
ATOM   2443 H  HG2  . GLU   A 1 114 ? 27.245 -16.549 -0.838  1.00 13.27 ?  114 GLU   A HG2  1 
ATOM   2444 H  HG3  . GLU   A 1 114 ? 26.580 -15.405 -1.710  1.00 13.27 ?  114 GLU   A HG3  1 
ATOM   2445 N  N    . ASN   A 1 115 ? 28.350 -12.074 1.372   1.00 9.98  ?  115 ASN   A N    1 
ATOM   2446 C  CA   . ASN   A 1 115 ? 29.118 -11.346 2.379   1.00 10.38 ?  115 ASN   A CA   1 
ATOM   2447 C  C    . ASN   A 1 115 ? 28.501 -11.480 3.768   1.00 9.98  ?  115 ASN   A C    1 
ATOM   2448 O  O    . ASN   A 1 115 ? 29.218 -11.412 4.777   1.00 10.54 ?  115 ASN   A O    1 
ATOM   2449 C  CB   . ASN   A 1 115 ? 29.225 -9.870  2.002   1.00 10.88 ?  115 ASN   A CB   1 
ATOM   2450 C  CG   . ASN   A 1 115 ? 30.023 -9.650  0.737   1.00 11.40 ?  115 ASN   A CG   1 
ATOM   2451 O  OD1  . ASN   A 1 115 ? 31.243 -9.736  0.752   1.00 14.75 ?  115 ASN   A OD1  1 
ATOM   2452 N  ND2  . ASN   A 1 115 ? 29.344 -9.353  -0.355  1.00 10.96 ?  115 ASN   A ND2  1 
ATOM   2453 H  H    . ASN   A 1 115 ? 28.042 -11.586 0.732   1.00 12.02 ?  115 ASN   A H    1 
ATOM   2454 H  HA   . ASN   A 1 115 ? 30.014 -11.711 2.416   1.00 12.49 ?  115 ASN   A HA   1 
ATOM   2455 H  HB2  . ASN   A 1 115 ? 28.333 -9.512  1.873   1.00 13.10 ?  115 ASN   A HB2  1 
ATOM   2456 H  HB3  . ASN   A 1 115 ? 29.665 -9.393  2.730   1.00 13.10 ?  115 ASN   A HB3  1 
ATOM   2457 H  HD21 . ASN   A 1 115 ? 29.757 -9.216  -1.095  1.00 13.19 ?  115 ASN   A HD21 1 
ATOM   2458 H  HD22 . ASN   A 1 115 ? 28.483 -9.318  -0.330  1.00 13.19 ?  115 ASN   A HD22 1 
ATOM   2459 N  N    . PHE   A 1 116 ? 27.175 -11.645 3.846   1.00 10.22 ?  116 PHE   A N    1 
ATOM   2460 C  CA   . PHE   A 1 116 ? 26.519 -11.742 5.147   1.00 10.08 ?  116 PHE   A CA   1 
ATOM   2461 C  C    . PHE   A 1 116 ? 26.992 -12.972 5.923   1.00 10.28 ?  116 PHE   A C    1 
ATOM   2462 O  O    . PHE   A 1 116 ? 26.920 -12.988 7.152   1.00 10.87 ?  116 PHE   A O    1 
ATOM   2463 C  CB   . PHE   A 1 116 ? 24.993 -11.867 4.997   1.00 10.37 ?  116 PHE   A CB   1 
ATOM   2464 C  CG   . PHE   A 1 116 ? 24.240 -10.616 4.535   1.00 10.17 ?  116 PHE   A CG   1 
ATOM   2465 C  CD1  . PHE   A 1 116 ? 24.810 -9.594  3.780   1.00 10.16 ?  116 PHE   A CD1  1 
ATOM   2466 C  CD2  . PHE   A 1 116 ? 22.891 -10.511 4.858   1.00 10.77 ?  116 PHE   A CD2  1 
ATOM   2467 C  CE1  . PHE   A 1 116 ? 24.044 -8.517  3.364   1.00 10.79 ?  116 PHE   A CE1  1 
ATOM   2468 C  CE2  . PHE   A 1 116 ? 22.125 -9.436  4.449   1.00 11.03 ?  116 PHE   A CE2  1 
ATOM   2469 C  CZ   . PHE   A 1 116 ? 22.695 -8.438  3.703   1.00 10.48 ?  116 PHE   A CZ   1 
ATOM   2470 H  H    . PHE   A 1 116 ? 26.644 -11.697 3.169   1.00 12.31 ?  116 PHE   A H    1 
ATOM   2471 H  HA   . PHE   A 1 116 ? 26.714 -10.949 5.669   1.00 12.14 ?  116 PHE   A HA   1 
ATOM   2472 H  HB2  . PHE   A 1 116 ? 24.812 -12.569 4.349   1.00 12.48 ?  116 PHE   A HB2  1 
ATOM   2473 H  HB3  . PHE   A 1 116 ? 24.629 -12.127 5.857   1.00 12.48 ?  116 PHE   A HB3  1 
ATOM   2474 H  HD1  . PHE   A 1 116 ? 25.702 -9.658  3.542   1.00 12.24 ?  116 PHE   A HD1  1 
ATOM   2475 H  HD2  . PHE   A 1 116 ? 22.486 -11.196 5.356   1.00 12.96 ?  116 PHE   A HD2  1 
ATOM   2476 H  HE1  . PHE   A 1 116 ? 24.436 -7.843  2.864   1.00 12.99 ?  116 PHE   A HE1  1 
ATOM   2477 H  HE2  . PHE   A 1 116 ? 21.224 -9.394  4.684   1.00 13.28 ?  116 PHE   A HE2  1 
ATOM   2478 H  HZ   . PHE   A 1 116 ? 22.186 -7.710  3.439   1.00 12.62 ?  116 PHE   A HZ   1 
ATOM   2479 N  N    . ASN   A 1 117 ? 27.430 -14.025 5.223   1.00 10.48 ?  117 ASN   A N    1 
ATOM   2480 C  CA   . ASN   A 1 117 ? 27.800 -15.267 5.896   1.00 10.60 ?  117 ASN   A CA   1 
ATOM   2481 C  C    . ASN   A 1 117 ? 29.064 -15.146 6.729   1.00 10.95 ?  117 ASN   A C    1 
ATOM   2482 O  O    . ASN   A 1 117 ? 29.360 -16.061 7.505   1.00 12.04 ?  117 ASN   A O    1 
ATOM   2483 C  CB   . ASN   A 1 117 ? 27.916 -16.395 4.874   1.00 10.86 ?  117 ASN   A CB   1 
ATOM   2484 C  CG   . ASN   A 1 117 ? 26.561 -16.783 4.330   1.00 10.86 ?  117 ASN   A CG   1 
ATOM   2485 O  OD1  . ASN   A 1 117 ? 25.589 -16.813 5.074   1.00 11.79 ?  117 ASN   A OD1  1 
ATOM   2486 N  ND2  . ASN   A 1 117 ? 26.478 -17.037 3.041   1.00 10.93 ?  117 ASN   A ND2  1 
ATOM   2487 H  H    . ASN   A 1 117 ? 27.505 -14.048 4.363   1.00 12.62 ?  117 ASN   A H    1 
ATOM   2488 H  HA   . ASN   A 1 117 ? 27.078 -15.503 6.500   1.00 12.77 ?  117 ASN   A HA   1 
ATOM   2489 H  HB2  . ASN   A 1 117 ? 28.470 -16.098 4.133   1.00 13.07 ?  117 ASN   A HB2  1 
ATOM   2490 H  HB3  . ASN   A 1 117 ? 28.307 -17.170 5.299   1.00 13.07 ?  117 ASN   A HB3  1 
ATOM   2491 H  HD21 . ASN   A 1 117 ? 25.722 -17.252 2.702   1.00 13.16 ?  117 ASN   A HD21 1 
ATOM   2492 H  HD22 . ASN   A 1 117 ? 27.180 -16.985 2.548   1.00 13.16 ?  117 ASN   A HD22 1 
ATOM   2493 N  N    . GLN   A 1 118 ? 29.795 -14.037 6.608   1.00 11.09 ?  118 GLN   A N    1 
ATOM   2494 C  CA   . GLN   A 1 118 ? 30.971 -13.799 7.430   1.00 11.73 ?  118 GLN   A CA   1 
ATOM   2495 C  C    . GLN   A 1 118 ? 30.627 -13.223 8.798   1.00 11.67 ?  118 GLN   A C    1 
ATOM   2496 O  O    . GLN   A 1 118 ? 31.541 -12.930 9.580   1.00 13.06 ?  118 GLN   A O    1 
ATOM   2497 C  CB   . GLN   A 1 118 ? 31.965 -12.900 6.691   1.00 12.33 ?  118 GLN   A CB   1 
ATOM   2498 C  CG   . GLN   A 1 118 ? 32.438 -13.485 5.370   1.00 12.08 ?  118 GLN   A CG   1 
ATOM   2499 C  CD   . GLN   A 1 118 ? 33.273 -14.741 5.550   1.00 12.31 ?  118 GLN   A CD   1 
ATOM   2500 O  OE1  . GLN   A 1 118 ? 34.140 -14.803 6.433   1.00 13.32 ?  118 GLN   A OE1  1 
ATOM   2501 N  NE2  . GLN   A 1 118 ? 33.029 -15.742 4.702   1.00 12.54 ?  118 GLN   A NE2  1 
ATOM   2502 H  H    . GLN   A 1 118 ? 29.616 -13.397 6.054   1.00 13.35 ?  118 GLN   A H    1 
ATOM   2503 H  HA   . GLN   A 1 118 ? 31.400 -14.653 7.580   1.00 14.12 ?  118 GLN   A HA   1 
ATOM   2504 H  HB2  . GLN   A 1 118 ? 31.544 -12.050 6.510   1.00 14.84 ?  118 GLN   A HB2  1 
ATOM   2505 H  HB3  . GLN   A 1 118 ? 32.743 -12.774 7.259   1.00 14.84 ?  118 GLN   A HB3  1 
ATOM   2506 H  HG2  . GLN   A 1 118 ? 31.672 -13.708 4.821   1.00 14.53 ?  118 GLN   A HG2  1 
ATOM   2507 H  HG3  . GLN   A 1 118 ? 32.991 -12.827 4.912   1.00 14.53 ?  118 GLN   A HG3  1 
ATOM   2508 H  HE21 . GLN   A 1 118 ? 32.417 -15.657 4.095   1.00 15.09 ?  118 GLN   A HE21 1 
ATOM   2509 H  HE22 . GLN   A 1 118 ? 33.473 -16.475 4.755   1.00 15.09 ?  118 GLN   A HE22 1 
ATOM   2510 N  N    . HIS   A 1 119 ? 29.337 -13.065 9.103   1.00 11.35 ?  119 HIS   A N    1 
ATOM   2511 C  CA   . HIS   A 1 119 ? 28.878 -12.460 10.349  1.00 11.97 ?  119 HIS   A CA   1 
ATOM   2512 C  C    . HIS   A 1 119 ? 27.738 -13.285 10.923  1.00 12.09 ?  119 HIS   A C    1 
ATOM   2513 O  O    . HIS   A 1 119 ? 26.791 -13.620 10.208  1.00 12.63 ?  119 HIS   A O    1 
ATOM   2514 C  CB   . HIS   A 1 119 ? 28.420 -11.028 10.074  1.00 12.27 ?  119 HIS   A CB   1 
ATOM   2515 C  CG   . HIS   A 1 119 ? 29.501 -10.216 9.463   1.00 13.63 ?  119 HIS   A CG   1 
ATOM   2516 N  ND1  . HIS   A 1 119 ? 30.480 -9.613  10.221  1.00 16.42 ?  119 HIS   A ND1  1 
ATOM   2517 C  CD2  . HIS   A 1 119 ? 29.843 -10.022 8.170   1.00 14.94 ?  119 HIS   A CD2  1 
ATOM   2518 C  CE1  . HIS   A 1 119 ? 31.349 -9.030  9.415   1.00 16.69 ?  119 HIS   A CE1  1 
ATOM   2519 N  NE2  . HIS   A 1 119 ? 30.993 -9.271  8.166   1.00 16.26 ?  119 HIS   A NE2  1 
ATOM   2520 H  H    . HIS   A 1 119 ? 28.683 -13.321 8.595   1.00 13.67 ?  119 HIS   A H    1 
ATOM   2521 H  HA   . HIS   A 1 119 ? 29.606 -12.446 10.989  1.00 14.41 ?  119 HIS   A HA   1 
ATOM   2522 H  HB2  . HIS   A 1 119 ? 27.667 -11.052 9.463   1.00 14.77 ?  119 HIS   A HB2  1 
ATOM   2523 H  HB3  . HIS   A 1 119 ? 28.161 -10.617 10.911  1.00 14.77 ?  119 HIS   A HB3  1 
ATOM   2524 H  HD2  . HIS   A 1 119 ? 29.381 -10.333 7.422   1.00 17.97 ?  119 HIS   A HD2  1 
ATOM   2525 H  HE1  . HIS   A 1 119 ? 32.086 -8.530  9.677   1.00 20.07 ?  119 HIS   A HE1  1 
ATOM   2526 H  HE2  . HIS   A 1 119 ? 31.395 -8.980  7.462   1.00 19.55 ?  119 HIS   A HE2  1 
ATOM   2527 N  N    . GLU   A 1 120 ? 27.820 -13.591 12.220  1.00 12.78 ?  120 GLU   A N    1 
ATOM   2528 C  CA   . GLU   A 1 120 ? 26.863 -14.521 12.819  1.00 15.01 ?  120 GLU   A CA   1 
ATOM   2529 C  C    . GLU   A 1 120 ? 25.447 -13.955 12.875  1.00 13.38 ?  120 GLU   A C    1 
ATOM   2530 O  O    . GLU   A 1 120 ? 24.476 -14.721 12.771  1.00 13.61 ?  120 GLU   A O    1 
ATOM   2531 C  CB   . GLU   A 1 120 ? 27.337 -14.923 14.218  1.00 19.79 ?  120 GLU   A CB   1 
ATOM   2532 C  CG   . GLU   A 1 120 ? 28.512 -15.881 14.214  1.00 27.61 ?  120 GLU   A CG   1 
ATOM   2533 C  CD   . GLU   A 1 120 ? 28.714 -16.560 15.551  1.00 35.69 ?  120 GLU   A CD   1 
ATOM   2534 O  OE1  . GLU   A 1 120 ? 28.190 -16.053 16.566  1.00 37.32 ?  120 GLU   A OE1  1 
ATOM   2535 O  OE2  . GLU   A 1 120 ? 29.397 -17.606 15.587  1.00 39.11 -1 120 GLU   A OE2  1 
ATOM   2536 H  H    . GLU   A 1 120 ? 28.418 -13.285 12.764  1.00 15.38 ?  120 GLU   A H    1 
ATOM   2537 H  HA   . GLU   A 1 120 ? 26.842 -15.327 12.285  1.00 18.05 ?  120 GLU   A HA   1 
ATOM   2538 H  HB2  . GLU   A 1 120 ? 27.616 -14.132 14.708  1.00 23.80 ?  120 GLU   A HB2  1 
ATOM   2539 H  HB3  . GLU   A 1 120 ? 26.610 -15.360 14.691  1.00 23.80 ?  120 GLU   A HB3  1 
ATOM   2540 H  HG2  . GLU   A 1 120 ? 28.365 -16.567 13.544  1.00 33.17 ?  120 GLU   A HG2  1 
ATOM   2541 H  HG3  . GLU   A 1 120 ? 29.327 -15.395 14.025  1.00 33.17 ?  120 GLU   A HG3  1 
ATOM   2542 N  N    . VAL   A 1 121 ? 25.314 -12.645 13.090  1.00 12.66 ?  121 VAL   A N    1 
ATOM   2543 C  CA   . VAL   A 1 121 ? 24.019 -11.980 13.208  1.00 12.89 ?  121 VAL   A CA   1 
ATOM   2544 C  C    . VAL   A 1 121 ? 24.129 -10.596 12.576  1.00 11.69 ?  121 VAL   A C    1 
ATOM   2545 O  O    . VAL   A 1 121 ? 25.095 -9.869  12.827  1.00 12.36 ?  121 VAL   A O    1 
ATOM   2546 C  CB   . VAL   A 1 121 ? 23.568 -11.845 14.681  1.00 16.25 ?  121 VAL   A CB   1 
ATOM   2547 C  CG1  . VAL   A 1 121 ? 22.170 -11.247 14.758  1.00 16.79 ?  121 VAL   A CG1  1 
ATOM   2548 C  CG2  . VAL   A 1 121 ? 23.609 -13.172 15.415  1.00 18.39 ?  121 VAL   A CG2  1 
ATOM   2549 H  H    . VAL   A 1 121 ? 25.980 -12.106 13.177  1.00 15.23 ?  121 VAL   A H    1 
ATOM   2550 H  HA   . VAL   A 1 121 ? 23.350 -12.493 12.729  1.00 15.51 ?  121 VAL   A HA   1 
ATOM   2551 H  HB   . VAL   A 1 121 ? 24.168 -11.238 15.138  1.00 19.55 ?  121 VAL   A HB   1 
ATOM   2552 H  HG11 . VAL   A 1 121 ? 21.851 -11.302 15.676  1.00 20.19 ?  121 VAL   A HG11 1 
ATOM   2553 H  HG12 . VAL   A 1 121 ? 22.200 -10.321 14.477  1.00 20.19 ?  121 VAL   A HG12 1 
ATOM   2554 H  HG13 . VAL   A 1 121 ? 21.576 -11.752 14.178  1.00 20.19 ?  121 VAL   A HG13 1 
ATOM   2555 H  HG21 . VAL   A 1 121 ? 23.249 -13.053 16.312  1.00 22.11 ?  121 VAL   A HG21 1 
ATOM   2556 H  HG22 . VAL   A 1 121 ? 23.068 -13.820 14.933  1.00 22.11 ?  121 VAL   A HG22 1 
ATOM   2557 H  HG23 . VAL   A 1 121 ? 24.524 -13.480 15.467  1.00 22.11 ?  121 VAL   A HG23 1 
ATOM   2558 N  N    . LEU   A 1 122 ? 23.120 -10.216 11.783  1.00 11.30 ?  122 LEU   A N    1 
ATOM   2559 C  CA   . LEU   A 1 122 ? 23.121 -8.916  11.112  1.00 11.24 ?  122 LEU   A CA   1 
ATOM   2560 C  C    . LEU   A 1 122 ? 21.722 -8.323  11.079  1.00 10.99 ?  122 LEU   A C    1 
ATOM   2561 O  O    . LEU   A 1 122 ? 20.733 -9.041  10.931  1.00 11.83 ?  122 LEU   A O    1 
ATOM   2562 C  CB   . LEU   A 1 122 ? 23.557 -9.000  9.643   1.00 12.67 ?  122 LEU   A CB   1 
ATOM   2563 C  CG   . LEU   A 1 122 ? 24.763 -9.857  9.286   1.00 12.62 ?  122 LEU   A CG   1 
ATOM   2564 C  CD1  . LEU   A 1 122 ? 24.363 -11.308 9.053   1.00 13.52 ?  122 LEU   A CD1  1 
ATOM   2565 C  CD2  . LEU   A 1 122 ? 25.454 -9.287  8.064   1.00 11.99 ?  122 LEU   A CD2  1 
ATOM   2566 H  H    . LEU   A 1 122 ? 22.421 -10.693 11.614  1.00 13.60 ?  122 LEU   A H    1 
ATOM   2567 H  HA   . LEU   A 1 122 ? 23.712 -8.305  11.581  1.00 13.53 ?  122 LEU   A HA   1 
ATOM   2568 H  HB2  . LEU   A 1 122 ? 22.816 -9.345  9.131   1.00 15.25 ?  122 LEU   A HB2  1 
ATOM   2569 H  HB3  . LEU   A 1 122 ? 23.764 -8.102  9.343   1.00 15.25 ?  122 LEU   A HB3  1 
ATOM   2570 H  HG   . LEU   A 1 122 ? 25.405 -9.844  10.018  1.00 15.19 ?  122 LEU   A HG   1 
ATOM   2571 H  HD11 . LEU   A 1 122 ? 25.141 -11.819 8.777   1.00 16.27 ?  122 LEU   A HD11 1 
ATOM   2572 H  HD12 . LEU   A 1 122 ? 24.006 -11.675 9.878   1.00 16.27 ?  122 LEU   A HD12 1 
ATOM   2573 H  HD13 . LEU   A 1 122 ? 23.686 -11.341 8.358   1.00 16.27 ?  122 LEU   A HD13 1 
ATOM   2574 H  HD21 . LEU   A 1 122 ? 26.198 -9.865  7.812   1.00 14.43 ?  122 LEU   A HD21 1 
ATOM   2575 H  HD22 . LEU   A 1 122 ? 24.820 -9.237  7.333   1.00 14.43 ?  122 LEU   A HD22 1 
ATOM   2576 H  HD23 . LEU   A 1 122 ? 25.791 -8.400  8.272   1.00 14.43 ?  122 LEU   A HD23 1 
ATOM   2577 N  N    . LEU   A 1 123 ? 21.662 -6.993  11.182  1.00 10.66 ?  123 LEU   A N    1 
ATOM   2578 C  CA   . LEU   A 1 123 ? 20.498 -6.189  10.811  1.00 10.61 ?  123 LEU   A CA   1 
ATOM   2579 C  C    . LEU   A 1 123 ? 20.751 -5.670  9.402   1.00 9.94  ?  123 LEU   A C    1 
ATOM   2580 O  O    . LEU   A 1 123 ? 21.802 -5.075  9.155   1.00 10.74 ?  123 LEU   A O    1 
ATOM   2581 C  CB   . LEU   A 1 123 ? 20.380 -5.005  11.773  1.00 10.88 ?  123 LEU   A CB   1 
ATOM   2582 C  CG   . LEU   A 1 123 ? 19.329 -3.945  11.428  1.00 11.81 ?  123 LEU   A CG   1 
ATOM   2583 C  CD1  . LEU   A 1 123 ? 17.931 -4.540  11.437  1.00 12.83 ?  123 LEU   A CD1  1 
ATOM   2584 C  CD2  . LEU   A 1 123 ? 19.424 -2.759  12.386  1.00 12.56 ?  123 LEU   A CD2  1 
ATOM   2585 H  H    . LEU   A 1 123 ? 22.312 -6.512  11.481  1.00 12.84 ?  123 LEU   A H    1 
ATOM   2586 H  HA   . LEU   A 1 123 ? 19.685 -6.719  10.837  1.00 12.78 ?  123 LEU   A HA   1 
ATOM   2587 H  HB2  . LEU   A 1 123 ? 20.148 -5.346  12.656  1.00 13.10 ?  123 LEU   A HB2  1 
ATOM   2588 H  HB3  . LEU   A 1 123 ? 21.230 -4.553  11.818  1.00 13.10 ?  123 LEU   A HB3  1 
ATOM   2589 H  HG   . LEU   A 1 123 ? 19.496 -3.605  10.534  1.00 14.21 ?  123 LEU   A HG   1 
ATOM   2590 H  HD11 . LEU   A 1 123 ? 17.282 -3.844  11.267  1.00 15.44 ?  123 LEU   A HD11 1 
ATOM   2591 H  HD12 . LEU   A 1 123 ? 17.876 -5.223  10.747  1.00 15.44 ?  123 LEU   A HD12 1 
ATOM   2592 H  HD13 . LEU   A 1 123 ? 17.766 -4.943  12.307  1.00 15.44 ?  123 LEU   A HD13 1 
ATOM   2593 H  HD21 . LEU   A 1 123 ? 18.750 -2.103  12.149  1.00 15.11 ?  123 LEU   A HD21 1 
ATOM   2594 H  HD22 . LEU   A 1 123 ? 19.267 -3.077  13.293  1.00 15.11 ?  123 LEU   A HD22 1 
ATOM   2595 H  HD23 . LEU   A 1 123 ? 20.307 -2.371  12.321  1.00 15.11 ?  123 LEU   A HD23 1 
ATOM   2596 N  N    A ALA   A 1 124 ? 19.779 -5.835  8.500   0.60 9.94  ?  124 ALA   A N    1 
ATOM   2597 N  N    B ALA   A 1 124 ? 19.831 -5.927  8.482   0.40 9.82  ?  124 ALA   A N    1 
ATOM   2598 C  CA   A ALA   A 1 124 ? 20.051 -5.541  7.099   0.60 9.66  ?  124 ALA   A CA   1 
ATOM   2599 C  CA   B ALA   A 1 124 ? 20.109 -5.688  7.076   0.40 9.81  ?  124 ALA   A CA   1 
ATOM   2600 C  C    A ALA   A 1 124 ? 18.807 -5.126  6.325   0.60 9.77  ?  124 ALA   A C    1 
ATOM   2601 C  C    B ALA   A 1 124 ? 18.895 -5.124  6.357   0.40 9.64  ?  124 ALA   A C    1 
ATOM   2602 O  O    A ALA   A 1 124 ? 17.688 -5.542  6.660   0.60 9.99  ?  124 ALA   A O    1 
ATOM   2603 O  O    B ALA   A 1 124 ? 17.753 -5.326  6.785   0.40 9.94  ?  124 ALA   A O    1 
ATOM   2604 C  CB   A ALA   A 1 124 ? 20.683 -6.750  6.401   0.60 9.76  ?  124 ALA   A CB   1 
ATOM   2605 C  CB   B ALA   A 1 124 ? 20.554 -6.978  6.375   0.40 10.08 ?  124 ALA   A CB   1 
ATOM   2606 H  H    A ALA   A 1 124 ? 18.977 -6.104  8.675   0.60 11.98 ?  124 ALA   A H    1 
ATOM   2607 H  H    B ALA   A 1 124 ? 19.048 -6.251  8.646   0.40 11.83 ?  124 ALA   A H    1 
ATOM   2608 H  HA   A ALA   A 1 124 ? 20.690 -4.815  7.068   0.60 11.63 ?  124 ALA   A HA   1 
ATOM   2609 H  HA   B ALA   A 1 124 ? 20.830 -5.048  7.014   0.40 11.81 ?  124 ALA   A HA   1 
ATOM   2610 H  HB1  A ALA   A 1 124 ? 20.856 -6.526  5.475   0.60 11.75 ?  124 ALA   A HB1  1 
ATOM   2611 H  HB1  B ALA   A 1 124 ? 20.729 -6.789  5.440   0.40 12.14 ?  124 ALA   A HB1  1 
ATOM   2612 H  HB2  A ALA   A 1 124 ? 21.519 -6.970  6.849   0.60 11.75 ?  124 ALA   A HB2  1 
ATOM   2613 H  HB2  B ALA   A 1 124 ? 21.365 -7.309  6.800   0.40 12.14 ?  124 ALA   A HB2  1 
ATOM   2614 H  HB3  A ALA   A 1 124 ? 20.075 -7.502  6.455   0.60 11.75 ?  124 ALA   A HB3  1 
ATOM   2615 H  HB3  B ALA   A 1 124 ? 19.852 -7.643  6.452   0.40 12.14 ?  124 ALA   A HB3  1 
ATOM   2616 N  N    A PRO   A 1 125 ? 18.985 -4.345  5.261   0.60 9.94  ?  125 PRO   A N    1 
ATOM   2617 N  N    B PRO   A 1 125 ? 19.119 -4.416  5.243   0.40 9.13  ?  125 PRO   A N    1 
ATOM   2618 C  CA   A PRO   A 1 125 ? 17.936 -4.139  4.265   0.60 10.21 ?  125 PRO   A CA   1 
ATOM   2619 C  CA   B PRO   A 1 125 ? 18.024 -4.038  4.353   0.40 9.49  ?  125 PRO   A CA   1 
ATOM   2620 C  C    A PRO   A 1 125 ? 18.009 -5.200  3.172   0.60 9.57  ?  125 PRO   A C    1 
ATOM   2621 C  C    B PRO   A 1 125 ? 17.906 -5.084  3.260   0.40 10.00 ?  125 PRO   A C    1 
ATOM   2622 O  O    A PRO   A 1 125 ? 18.985 -5.947  3.051   0.60 9.90  ?  125 PRO   A O    1 
ATOM   2623 O  O    B PRO   A 1 125 ? 18.747 -5.988  3.183   0.40 10.43 ?  125 PRO   A O    1 
ATOM   2624 C  CB   A PRO   A 1 125 ? 18.332 -2.782  3.671   0.60 10.87 ?  125 PRO   A CB   1 
ATOM   2625 C  CB   B PRO   A 1 125 ? 18.532 -2.716  3.772   0.40 9.27  ?  125 PRO   A CB   1 
ATOM   2626 C  CG   A PRO   A 1 125 ? 19.838 -2.859  3.643   0.60 10.91 ?  125 PRO   A CG   1 
ATOM   2627 C  CG   B PRO   A 1 125 ? 20.013 -3.015  3.551   0.40 8.63  ?  125 PRO   A CG   1 
ATOM   2628 C  CD   A PRO   A 1 125 ? 20.214 -3.599  4.918   0.60 10.44 ?  125 PRO   A CD   1 
ATOM   2629 C  CD   B PRO   A 1 125 ? 20.415 -3.943  4.712   0.40 8.20  ?  125 PRO   A CD   1 
ATOM   2630 H  HA   A PRO   A 1 125 ? 17.054 -4.107  4.665   0.60 12.29 ?  125 PRO   A HA   1 
ATOM   2631 H  HA   B PRO   A 1 125 ? 17.183 -3.912  4.830   0.40 11.43 ?  125 PRO   A HA   1 
ATOM   2632 H  HB2  A PRO   A 1 125 ? 17.964 -2.691  2.775   0.60 13.09 ?  125 PRO   A HB2  1 
ATOM   2633 H  HB2  B PRO   A 1 125 ? 18.084 -2.517  2.935   0.40 11.17 ?  125 PRO   A HB2  1 
ATOM   2634 H  HB3  A PRO   A 1 125 ? 18.025 -2.064  4.248   0.60 13.09 ?  125 PRO   A HB3  1 
ATOM   2635 H  HB3  B PRO   A 1 125 ? 18.413 -1.994  4.413   0.40 11.17 ?  125 PRO   A HB3  1 
ATOM   2636 H  HG2  A PRO   A 1 125 ? 20.126 -3.359  2.861   0.60 13.14 ?  125 PRO   A HG2  1 
ATOM   2637 H  HG2  B PRO   A 1 125 ? 20.129 -3.462  2.694   0.40 10.40 ?  125 PRO   A HG2  1 
ATOM   2638 H  HG3  A PRO   A 1 125 ? 20.212 -1.965  3.634   0.60 13.14 ?  125 PRO   A HG3  1 
ATOM   2639 H  HG3  B PRO   A 1 125 ? 20.522 -2.190  3.573   0.40 10.40 ?  125 PRO   A HG3  1 
ATOM   2640 H  HD2  A PRO   A 1 125 ? 20.952 -4.202  4.757   0.60 12.57 ?  125 PRO   A HD2  1 
ATOM   2641 H  HD2  B PRO   A 1 125 ? 20.947 -4.684  4.375   0.40 9.88  ?  125 PRO   A HD2  1 
ATOM   2642 H  HD3  A PRO   A 1 125 ? 20.426 -2.959  5.624   0.60 12.57 ?  125 PRO   A HD3  1 
ATOM   2643 H  HD3  B PRO   A 1 125 ? 20.894 -3.439  5.386   0.40 9.88  ?  125 PRO   A HD3  1 
ATOM   2644 N  N    A LEU   A 1 126 ? 16.963 -5.228  2.351   0.60 9.63  ?  126 LEU   A N    1 
ATOM   2645 N  N    B LEU   A 1 126 ? 16.901 -4.971  2.397   0.40 10.73 ?  126 LEU   A N    1 
ATOM   2646 C  CA   A LEU   A 1 126 ? 16.983 -6.035  1.139   0.60 10.08 ?  126 LEU   A CA   1 
ATOM   2647 C  CA   B LEU   A 1 126 ? 16.814 -5.837  1.225   0.40 11.69 ?  126 LEU   A CA   1 
ATOM   2648 C  C    A LEU   A 1 126 ? 17.919 -5.403  0.111   0.60 10.38 ?  126 LEU   A C    1 
ATOM   2649 C  C    B LEU   A 1 126 ? 17.758 -5.296  0.154   0.40 11.36 ?  126 LEU   A C    1 
ATOM   2650 O  O    A LEU   A 1 126 ? 17.715 -4.264  -0.325  0.60 11.24 ?  126 LEU   A O    1 
ATOM   2651 O  O    B LEU   A 1 126 ? 17.514 -4.226  -0.414  0.40 12.12 ?  126 LEU   A O    1 
ATOM   2652 C  CB   A LEU   A 1 126 ? 15.572 -6.181  0.580   0.60 10.09 ?  126 LEU   A CB   1 
ATOM   2653 C  CB   B LEU   A 1 126 ? 15.376 -5.854  0.718   0.40 14.19 ?  126 LEU   A CB   1 
ATOM   2654 C  CG   A LEU   A 1 126 ? 14.656 -7.068  1.427   0.60 10.92 ?  126 LEU   A CG   1 
ATOM   2655 C  CG   B LEU   A 1 126 ? 14.747 -7.094  0.085   0.40 16.42 ?  126 LEU   A CG   1 
ATOM   2656 C  CD1  A LEU   A 1 126 ? 13.212 -6.924  0.984   0.60 12.47 ?  126 LEU   A CD1  1 
ATOM   2657 C  CD1  B LEU   A 1 126 ? 15.111 -8.373  0.813   0.40 16.93 ?  126 LEU   A CD1  1 
ATOM   2658 C  CD2  A LEU   A 1 126 ? 15.096 -8.527  1.355   0.60 11.69 ?  126 LEU   A CD2  1 
ATOM   2659 C  CD2  B LEU   A 1 126 ? 13.243 -6.903  0.106   0.40 17.09 ?  126 LEU   A CD2  1 
ATOM   2660 H  H    A LEU   A 1 126 ? 16.238 -4.787  2.467   0.60 11.60 ?  126 LEU   A H    1 
ATOM   2661 H  H    B LEU   A 1 126 ? 16.248 -4.404  2.473   0.40 12.92 ?  126 LEU   A H    1 
ATOM   2662 H  HA   A LEU   A 1 126 ? 17.321 -6.919  1.344   0.60 12.14 ?  126 LEU   A HA   1 
ATOM   2663 H  HA   B LEU   A 1 126 ? 17.089 -6.733  1.471   0.40 14.07 ?  126 LEU   A HA   1 
ATOM   2664 H  HB2  A LEU   A 1 126 ? 15.163 -5.305  0.528   0.60 12.15 ?  126 LEU   A HB2  1 
ATOM   2665 H  HB2  B LEU   A 1 126 ? 14.813 -5.622  1.465   0.40 17.07 ?  126 LEU   A HB2  1 
ATOM   2666 H  HB3  A LEU   A 1 126 ? 15.620 -6.575  -0.304  0.60 12.15 ?  126 LEU   A HB3  1 
ATOM   2667 H  HB3  B LEU   A 1 126 ? 15.313 -5.153  0.051   0.40 17.07 ?  126 LEU   A HB3  1 
ATOM   2668 H  HG   A LEU   A 1 126 ? 14.709 -6.786  2.355   0.60 13.14 ?  126 LEU   A HG   1 
ATOM   2669 H  HG   B LEU   A 1 126 ? 15.035 -7.159  -0.841  0.40 19.74 ?  126 LEU   A HG   1 
ATOM   2670 H  HD11 A LEU   A 1 126 ? 12.653 -7.495  1.534   0.60 15.01 ?  126 LEU   A HD11 1 
ATOM   2671 H  HD11 B LEU   A 1 126 ? 14.557 -9.095  0.478   0.40 20.36 ?  126 LEU   A HD11 1 
ATOM   2672 H  HD12 A LEU   A 1 126 ? 12.942 -5.999  1.084   0.60 15.01 ?  126 LEU   A HD12 1 
ATOM   2673 H  HD12 B LEU   A 1 126 ? 16.046 -8.572  0.657   0.40 20.36 ?  126 LEU   A HD12 1 
ATOM   2674 H  HD13 A LEU   A 1 126 ? 13.142 -7.192  0.053   0.60 15.01 ?  126 LEU   A HD13 1 
ATOM   2675 H  HD13 B LEU   A 1 126 ? 14.950 -8.247  1.761   0.40 20.36 ?  126 LEU   A HD13 1 
ATOM   2676 H  HD21 A LEU   A 1 126 ? 14.423 -9.085  1.777   0.60 14.07 ?  126 LEU   A HD21 1 
ATOM   2677 H  HD21 B LEU   A 1 126 ? 12.815 -7.706  -0.222  0.40 20.55 ?  126 LEU   A HD21 1 
ATOM   2678 H  HD22 A LEU   A 1 126 ? 15.197 -8.781  0.424   0.60 14.07 ?  126 LEU   A HD22 1 
ATOM   2679 H  HD22 B LEU   A 1 126 ? 12.963 -6.735  1.022   0.40 20.55 ?  126 LEU   A HD22 1 
ATOM   2680 H  HD23 A LEU   A 1 126 ? 15.944 -8.627  1.817   0.60 14.07 ?  126 LEU   A HD23 1 
ATOM   2681 H  HD23 B LEU   A 1 126 ? 13.011 -6.145  -0.451  0.40 20.55 ?  126 LEU   A HD23 1 
ATOM   2682 N  N    A LEU   A 1 127 ? 18.959 -6.142  -0.265  0.60 10.37 ?  127 LEU   A N    1 
ATOM   2683 N  N    B LEU   A 1 127 ? 18.834 -6.028  -0.138  0.40 11.21 ?  127 LEU   A N    1 
ATOM   2684 C  CA   A LEU   A 1 127 ? 19.935 -5.646  -1.222  0.60 10.40 ?  127 LEU   A CA   1 
ATOM   2685 C  CA   B LEU   A 1 127 ? 19.844 -5.511  -1.055  0.40 10.93 ?  127 LEU   A CA   1 
ATOM   2686 C  C    A LEU   A 1 127 ? 19.299 -5.470  -2.591  0.60 10.30 ?  127 LEU   A C    1 
ATOM   2687 C  C    B LEU   A 1 127 ? 19.285 -5.373  -2.464  0.40 10.69 ?  127 LEU   A C    1 
ATOM   2688 O  O    A LEU   A 1 127 ? 18.457 -6.263  -3.021  0.60 10.39 ?  127 LEU   A O    1 
ATOM   2689 O  O    B LEU   A 1 127 ? 18.470 -6.183  -2.916  0.40 11.17 ?  127 LEU   A O    1 
ATOM   2690 C  CB   A LEU   A 1 127 ? 21.098 -6.630  -1.325  0.60 11.03 ?  127 LEU   A CB   1 
ATOM   2691 C  CB   B LEU   A 1 127 ? 21.076 -6.417  -1.087  0.40 11.09 ?  127 LEU   A CB   1 
ATOM   2692 C  CG   A LEU   A 1 127 ? 21.871 -6.918  -0.039  0.60 11.51 ?  127 LEU   A CG   1 
ATOM   2693 C  CG   B LEU   A 1 127 ? 21.910 -6.485  0.193   0.40 11.10 ?  127 LEU   A CG   1 
ATOM   2694 C  CD1  A LEU   A 1 127 ? 22.954 -7.931  -0.327  0.60 11.43 ?  127 LEU   A CD1  1 
ATOM   2695 C  CD1  B LEU   A 1 127 ? 23.080 -7.443  0.013   0.40 11.38 ?  127 LEU   A CD1  1 
ATOM   2696 C  CD2  A LEU   A 1 127 ? 22.481 -5.652  0.519   0.60 12.43 ?  127 LEU   A CD2  1 
ATOM   2697 C  CD2  B LEU   A 1 127 ? 22.406 -5.107  0.612   0.40 11.83 ?  127 LEU   A CD2  1 
ATOM   2698 H  H    A LEU   A 1 127 ? 19.124 -6.934  0.033   0.60 12.49 ?  127 LEU   A H    1 
ATOM   2699 H  H    B LEU   A 1 127 ? 19.000 -6.818  0.175   0.40 13.49 ?  127 LEU   A H    1 
ATOM   2700 H  HA   A LEU   A 1 127 ? 20.275 -4.791  -0.924  0.60 12.52 ?  127 LEU   A HA   1 
ATOM   2701 H  HA   B LEU   A 1 127 ? 20.121 -4.635  -0.753  0.40 13.16 ?  127 LEU   A HA   1 
ATOM   2702 H  HB2  A LEU   A 1 127 ? 20.750 -7.477  -1.644  0.60 13.28 ?  127 LEU   A HB2  1 
ATOM   2703 H  HB2  B LEU   A 1 127 ? 20.786 -7.319  -1.294  0.40 13.35 ?  127 LEU   A HB2  1 
ATOM   2704 H  HB3  A LEU   A 1 127 ? 21.734 -6.280  -1.964  0.60 13.28 ?  127 LEU   A HB3  1 
ATOM   2705 H  HB3  B LEU   A 1 127 ? 21.662 -6.100  -1.796  0.40 13.35 ?  127 LEU   A HB3  1 
ATOM   2706 H  HG   A LEU   A 1 127 ? 21.271 -7.299  0.628   0.60 13.85 ?  127 LEU   A HG   1 
ATOM   2707 H  HG   B LEU   A 1 127 ? 21.357 -6.834  0.908   0.40 13.36 ?  127 LEU   A HG   1 
ATOM   2708 H  HD11 A LEU   A 1 127 ? 23.419 -8.147  0.498   0.60 13.76 ?  127 LEU   A HD11 1 
ATOM   2709 H  HD11 B LEU   A 1 127 ? 23.631 -7.423  0.812   0.40 13.70 ?  127 LEU   A HD11 1 
ATOM   2710 H  HD12 A LEU   A 1 127 ? 22.549 -8.737  -0.693  0.60 13.76 ?  127 LEU   A HD12 1 
ATOM   2711 H  HD12 B LEU   A 1 127 ? 22.739 -8.340  -0.130  0.40 13.70 ?  127 LEU   A HD12 1 
ATOM   2712 H  HD13 A LEU   A 1 127 ? 23.575 -7.556  -0.969  0.60 13.76 ?  127 LEU   A HD13 1 
ATOM   2713 H  HD13 B LEU   A 1 127 ? 23.604 -7.162  -0.754  0.40 13.70 ?  127 LEU   A HD13 1 
ATOM   2714 H  HD21 A LEU   A 1 127 ? 23.050 -5.876  1.272   0.60 14.96 ?  127 LEU   A HD21 1 
ATOM   2715 H  HD21 B LEU   A 1 127 ? 23.047 -5.209  1.333   0.40 14.24 ?  127 LEU   A HD21 1 
ATOM   2716 H  HD22 A LEU   A 1 127 ? 23.008 -5.226  -0.177  0.60 14.96 ?  127 LEU   A HD22 1 
ATOM   2717 H  HD22 B LEU   A 1 127 ? 22.828 -4.680  -0.149  0.40 14.24 ?  127 LEU   A HD22 1 
ATOM   2718 H  HD23 A LEU   A 1 127 ? 21.770 -5.059  0.805   0.60 14.96 ?  127 LEU   A HD23 1 
ATOM   2719 H  HD23 B LEU   A 1 127 ? 21.650 -4.581  0.913   0.40 14.24 ?  127 LEU   A HD23 1 
ATOM   2720 N  N    A SER   A 1 128 ? 19.725 -4.423  -3.283  0.60 10.45 ?  128 SER   A N    1 
ATOM   2721 N  N    B SER   A 1 128 ? 19.744 -4.336  -3.158  0.40 10.40 ?  128 SER   A N    1 
ATOM   2722 C  CA   A SER   A 1 128 ? 19.298 -4.065  -4.628  0.60 10.96 ?  128 SER   A CA   1 
ATOM   2723 C  CA   B SER   A 1 128 ? 19.409 -3.993  -4.536  0.40 10.40 ?  128 SER   A CA   1 
ATOM   2724 C  C    A SER   A 1 128 ? 17.835 -3.624  -4.704  0.60 11.48 ?  128 SER   A C    1 
ATOM   2725 C  C    B SER   A 1 128 ? 17.964 -3.543  -4.730  0.40 10.69 ?  128 SER   A C    1 
ATOM   2726 O  O    A SER   A 1 128 ? 17.358 -3.321  -5.802  0.60 13.09 ?  128 SER   A O    1 
ATOM   2727 O  O    B SER   A 1 128 ? 17.594 -3.198  -5.856  0.40 11.05 ?  128 SER   A O    1 
ATOM   2728 C  CB   A SER   A 1 128 ? 19.624 -5.140  -5.677  0.60 11.27 ?  128 SER   A CB   1 
ATOM   2729 C  CB   B SER   A 1 128 ? 19.777 -5.085  -5.552  0.40 10.12 ?  128 SER   A CB   1 
ATOM   2730 O  OG   A SER   A 1 128 ? 21.026 -5.368  -5.745  0.60 11.38 ?  128 SER   A OG   1 
ATOM   2731 O  OG   B SER   A 1 128 ? 21.185 -5.227  -5.636  0.40 10.34 ?  128 SER   A OG   1 
ATOM   2732 H  H    A SER   A 1 128 ? 20.316 -3.879  -2.970  0.60 12.58 ?  128 SER   A H    1 
ATOM   2733 H  H    B SER   A 1 128 ? 20.310 -3.777  -2.823  0.40 12.52 ?  128 SER   A H    1 
ATOM   2734 H  HA   A SER   A 1 128 ? 19.822 -3.295  -4.874  0.60 13.19 ?  128 SER   A HA   1 
ATOM   2735 H  HA   B SER   A 1 128 ? 19.950 -3.227  -4.767  0.40 12.52 ?  128 SER   A HA   1 
ATOM   2736 H  HB2  A SER   A 1 128 ? 19.181 -5.965  -5.440  0.60 13.57 ?  128 SER   A HB2  1 
ATOM   2737 H  HB2  B SER   A 1 128 ? 19.383 -5.923  -5.277  0.40 12.19 ?  128 SER   A HB2  1 
ATOM   2738 H  HB3  A SER   A 1 128 ? 19.319 -4.830  -6.544  0.60 13.57 ?  128 SER   A HB3  1 
ATOM   2739 H  HB3  B SER   A 1 128 ? 19.437 -4.825  -6.427  0.40 12.19 ?  128 SER   A HB3  1 
ATOM   2740 H  HG   A SER   A 1 128 ? 21.429 -4.654  -5.940  0.60 13.70 ?  128 SER   A HG   1 
ATOM   2741 H  HG   B SER   A 1 128 ? 21.532 -4.491  -5.857  0.40 12.45 ?  128 SER   A HG   1 
ATOM   2742 N  N    A ALA   A 1 129 ? 17.121 -3.550  -3.578  0.60 12.07 ?  129 ALA   A N    1 
ATOM   2743 N  N    B ALA   A 1 129 ? 17.150 -3.505  -3.678  0.40 11.49 ?  129 ALA   A N    1 
ATOM   2744 C  CA   A ALA   A 1 129 ? 15.749 -3.058  -3.554  0.60 12.02 ?  129 ALA   A CA   1 
ATOM   2745 C  CA   B ALA   A 1 129 ? 15.794 -2.993  -3.786  0.40 12.07 ?  129 ALA   A CA   1 
ATOM   2746 C  C    A ALA   A 1 129 ? 15.751 -1.528  -3.502  0.60 11.33 ?  129 ALA   A C    1 
ATOM   2747 C  C    B ALA   A 1 129 ? 15.801 -1.464  -3.721  0.40 12.11 ?  129 ALA   A C    1 
ATOM   2748 O  O    A ALA   A 1 129 ? 16.792 -0.871  -3.626  0.60 11.79 ?  129 ALA   A O    1 
ATOM   2749 O  O    B ALA   A 1 129 ? 16.843 -0.818  -3.557  0.40 11.97 ?  129 ALA   A O    1 
ATOM   2750 C  CB   A ALA   A 1 129 ? 14.978 -3.695  -2.397  0.60 13.59 ?  129 ALA   A CB   1 
ATOM   2751 C  CB   B ALA   A 1 129 ? 14.903 -3.616  -2.712  0.40 13.02 ?  129 ALA   A CB   1 
ATOM   2752 H  H    A ALA   A 1 129 ? 17.416 -3.785  -2.802  0.60 14.53 ?  129 ALA   A H    1 
ATOM   2753 H  H    B ALA   A 1 129 ? 17.364 -3.766  -2.883  0.40 13.83 ?  129 ALA   A H    1 
ATOM   2754 H  HA   A ALA   A 1 129 ? 15.315 -3.325  -4.376  0.60 14.47 ?  129 ALA   A HA   1 
ATOM   2755 H  HA   B ALA   A 1 129 ? 15.436 -3.243  -4.646  0.40 14.53 ?  129 ALA   A HA   1 
ATOM   2756 H  HB1  A ALA   A 1 129 ? 14.065 -3.362  -2.405  0.60 16.35 ?  129 ALA   A HB1  1 
ATOM   2757 H  HB1  B ALA   A 1 129 ? 14.028 -3.199  -2.746  0.40 15.66 ?  129 ALA   A HB1  1 
ATOM   2758 H  HB2  A ALA   A 1 129 ? 14.978 -4.657  -2.507  0.60 16.35 ?  129 ALA   A HB2  1 
ATOM   2759 H  HB2  B ALA   A 1 129 ? 14.824 -4.567  -2.881  0.40 15.66 ?  129 ALA   A HB2  1 
ATOM   2760 H  HB3  A ALA   A 1 129 ? 15.406 -3.457  -1.559  0.60 16.35 ?  129 ALA   A HB3  1 
ATOM   2761 H  HB3  B ALA   A 1 129 ? 15.305 -3.469  -1.842  0.40 15.66 ?  129 ALA   A HB3  1 
ATOM   2762 N  N    A GLY   A 1 130 ? 14.565 -0.945  -3.338  0.60 10.73 ?  130 GLY   A N    1 
ATOM   2763 N  N    B GLY   A 1 130 ? 14.619 -0.879  -3.877  0.40 12.13 ?  130 GLY   A N    1 
ATOM   2764 C  CA   A GLY   A 1 130 ? 14.464 0.504   -3.278  0.60 10.97 ?  130 GLY   A CA   1 
ATOM   2765 C  CA   B GLY   A 1 130 ? 14.508 0.569   -3.831  0.40 12.51 ?  130 GLY   A CA   1 
ATOM   2766 C  C    A GLY   A 1 130 ? 15.056 1.137   -4.520  0.60 11.08 ?  130 GLY   A C    1 
ATOM   2767 C  C    B GLY   A 1 130 ? 15.246 1.213   -4.984  0.40 12.73 ?  130 GLY   A C    1 
ATOM   2768 O  O    A GLY   A 1 130 ? 14.799 0.702   -5.649  0.60 11.03 ?  130 GLY   A O    1 
ATOM   2769 O  O    B GLY   A 1 130 ? 15.123 0.797   -6.141  0.40 12.95 ?  130 GLY   A O    1 
ATOM   2770 H  H    A GLY   A 1 130 ? 13.812 -1.362  -3.262  0.60 12.92 ?  130 GLY   A H    1 
ATOM   2771 H  H    B GLY   A 1 130 ? 13.880 -1.296  -4.014  0.40 14.59 ?  130 GLY   A H    1 
ATOM   2772 H  HA2  A GLY   A 1 130 ? 13.527 0.764   -3.201  0.60 13.21 ?  130 GLY   A HA2  1 
ATOM   2773 H  HA2  B GLY   A 1 130 ? 13.574 0.827   -3.880  0.40 15.06 ?  130 GLY   A HA2  1 
ATOM   2774 H  HA3  A GLY   A 1 130 ? 14.940 0.835   -2.505  0.60 13.21 ?  130 GLY   A HA3  1 
ATOM   2775 H  HA3  B GLY   A 1 130 ? 14.883 0.907   -3.008  0.40 15.06 ?  130 GLY   A HA3  1 
ATOM   2776 N  N    A ILE   A 1 131 ? 15.868 2.180   -4.313  0.60 11.76 ?  131 ILE   A N    1 
ATOM   2777 N  N    B ILE   A 1 131 ? 16.034 2.245   -4.666  0.40 12.95 ?  131 ILE   A N    1 
ATOM   2778 C  CA   A ILE   A 1 131 ? 16.410 2.952   -5.427  0.60 12.04 ?  131 ILE   A CA   1 
ATOM   2779 C  CA   B ILE   A 1 131 ? 16.694 3.040   -5.693  0.40 12.81 ?  131 ILE   A CA   1 
ATOM   2780 C  C    A ILE   A 1 131 ? 17.433 2.191   -6.258  0.60 11.87 ?  131 ILE   A C    1 
ATOM   2781 C  C    B ILE   A 1 131 ? 17.692 2.238   -6.515  0.40 12.69 ?  131 ILE   A C    1 
ATOM   2782 O  O    A ILE   A 1 131 ? 17.846 2.700   -7.307  0.60 12.81 ?  131 ILE   A O    1 
ATOM   2783 O  O    B ILE   A 1 131 ? 18.113 2.702   -7.582  0.40 13.21 ?  131 ILE   A O    1 
ATOM   2784 C  CB   A ILE   A 1 131 ? 16.962 4.323   -4.974  0.60 13.09 ?  131 ILE   A CB   1 
ATOM   2785 C  CB   B ILE   A 1 131 ? 17.338 4.315   -5.099  0.40 13.64 ?  131 ILE   A CB   1 
ATOM   2786 C  CG1  A ILE   A 1 131 ? 18.217 4.165   -4.107  0.60 14.19 ?  131 ILE   A CG1  1 
ATOM   2787 C  CG1  B ILE   A 1 131 ? 18.502 3.971   -4.162  0.40 14.58 ?  131 ILE   A CG1  1 
ATOM   2788 C  CG2  A ILE   A 1 131 ? 15.883 5.112   -4.240  0.60 13.80 ?  131 ILE   A CG2  1 
ATOM   2789 C  CG2  B ILE   A 1 131 ? 16.294 5.147   -4.370  0.40 13.83 ?  131 ILE   A CG2  1 
ATOM   2790 C  CD1  A ILE   A 1 131 ? 18.893 5.492   -3.764  0.60 15.12 ?  131 ILE   A CD1  1 
ATOM   2791 C  CD1  B ILE   A 1 131 ? 19.154 5.195   -3.516  0.40 15.26 ?  131 ILE   A CD1  1 
ATOM   2792 H  H    A ILE   A 1 131 ? 16.097 2.464   -3.536  0.60 14.15 ?  131 ILE   A H    1 
ATOM   2793 H  H    B ILE   A 1 131 ? 16.191 2.502   -3.859  0.40 15.58 ?  131 ILE   A H    1 
ATOM   2794 H  HA   A ILE   A 1 131 ? 15.676 3.141   -6.026  0.60 14.49 ?  131 ILE   A HA   1 
ATOM   2795 H  HA   B ILE   A 1 131 ? 16.012 3.340   -6.306  0.40 15.41 ?  131 ILE   A HA   1 
ATOM   2796 H  HB   A ILE   A 1 131 ? 17.206 4.821   -5.766  0.60 15.75 ?  131 ILE   A HB   1 
ATOM   2797 H  HB   B ILE   A 1 131 ? 17.681 4.847   -5.831  0.40 16.41 ?  131 ILE   A HB   1 
ATOM   2798 H  HG12 A ILE   A 1 131 ? 17.972 3.729   -3.275  0.60 17.08 ?  131 ILE   A HG12 1 
ATOM   2799 H  HG12 B ILE   A 1 131 ? 18.175 3.403   -3.450  0.40 17.54 ?  131 ILE   A HG12 1 
ATOM   2800 H  HG13 A ILE   A 1 131 ? 18.865 3.619   -4.582  0.60 17.08 ?  131 ILE   A HG13 1 
ATOM   2801 H  HG13 B ILE   A 1 131 ? 19.188 3.508   -4.667  0.40 17.54 ?  131 ILE   A HG13 1 
ATOM   2802 H  HG21 A ILE   A 1 131 ? 16.220 5.994   -4.032  0.60 16.61 ?  131 ILE   A HG21 1 
ATOM   2803 H  HG21 B ILE   A 1 131 ? 16.657 6.028   -4.193  0.40 16.64 ?  131 ILE   A HG21 1 
ATOM   2804 H  HG22 A ILE   A 1 131 ? 15.104 5.181   -4.814  0.60 16.61 ?  131 ILE   A HG22 1 
ATOM   2805 H  HG22 B ILE   A 1 131 ? 15.507 5.220   -4.930  0.40 16.64 ?  131 ILE   A HG22 1 
ATOM   2806 H  HG23 A ILE   A 1 131 ? 15.649 4.643   -3.422  0.60 16.61 ?  131 ILE   A HG23 1 
ATOM   2807 H  HG23 B ILE   A 1 131 ? 16.067 4.706   -3.536  0.40 16.64 ?  131 ILE   A HG23 1 
ATOM   2808 H  HD11 A ILE   A 1 131 ? 19.745 5.310   -3.333  0.60 18.19 ?  131 ILE   A HD11 1 
ATOM   2809 H  HD11 B ILE   A 1 131 ? 19.970 4.922   -3.068  0.40 18.35 ?  131 ILE   A HD11 1 
ATOM   2810 H  HD12 A ILE   A 1 131 ? 19.039 5.993   -4.582  0.60 18.19 ?  131 ILE   A HD12 1 
ATOM   2811 H  HD12 B ILE   A 1 131 ? 19.361 5.847   -4.206  0.40 18.35 ?  131 ILE   A HD12 1 
ATOM   2812 H  HD13 A ILE   A 1 131 ? 18.321 5.995   -3.165  0.60 18.19 ?  131 ILE   A HD13 1 
ATOM   2813 H  HD13 B ILE   A 1 131 ? 18.539 5.583   -2.872  0.40 18.35 ?  131 ILE   A HD13 1 
ATOM   2814 N  N    A PHE   A 1 132 ? 17.848 0.989   -5.835  0.60 11.52 ?  132 PHE   A N    1 
ATOM   2815 N  N    B PHE   A 1 132 ? 18.083 1.046   -6.051  0.40 12.47 ?  132 PHE   A N    1 
ATOM   2816 C  CA   A PHE   A 1 132 ? 18.713 0.157   -6.669  0.60 11.81 ?  132 PHE   A CA   1 
ATOM   2817 C  CA   B PHE   A 1 132 ? 18.971 0.193   -6.835  0.40 12.72 ?  132 PHE   A CA   1 
ATOM   2818 C  C    A PHE   A 1 132 ? 17.945 -0.603  -7.755  0.60 11.91 ?  132 PHE   A C    1 
ATOM   2819 C  C    B PHE   A 1 132 ? 18.256 -0.550  -7.966  0.40 13.67 ?  132 PHE   A C    1 
ATOM   2820 O  O    A PHE   A 1 132 ? 18.571 -1.236  -8.611  0.60 12.37 ?  132 PHE   A O    1 
ATOM   2821 O  O    B PHE   A 1 132 ? 18.933 -1.142  -8.815  0.40 14.70 ?  132 PHE   A O    1 
ATOM   2822 C  CB   A PHE   A 1 132 ? 19.530 -0.819  -5.807  0.60 11.87 ?  132 PHE   A CB   1 
ATOM   2823 C  CB   B PHE   A 1 132 ? 19.722 -0.790  -5.927  0.40 11.62 ?  132 PHE   A CB   1 
ATOM   2824 C  CG   A PHE   A 1 132 ? 20.785 -0.223  -5.187  0.60 12.07 ?  132 PHE   A CG   1 
ATOM   2825 C  CG   B PHE   A 1 132 ? 20.883 -0.176  -5.169  0.40 11.15 ?  132 PHE   A CG   1 
ATOM   2826 C  CD1  A PHE   A 1 132 ? 20.716 0.850   -4.312  0.60 12.76 ?  132 PHE   A CD1  1 
ATOM   2827 C  CD1  B PHE   A 1 132 ? 20.669 0.743   -4.150  0.40 11.73 ?  132 PHE   A CD1  1 
ATOM   2828 C  CD2  A PHE   A 1 132 ? 22.030 -0.788  -5.440  0.60 12.62 ?  132 PHE   A CD2  1 
ATOM   2829 C  CD2  B PHE   A 1 132 ? 22.186 -0.552  -5.456  0.40 11.20 ?  132 PHE   A CD2  1 
ATOM   2830 C  CE1  A PHE   A 1 132 ? 21.869 1.369   -3.729  0.60 12.78 ?  132 PHE   A CE1  1 
ATOM   2831 C  CE1  B PHE   A 1 132 ? 21.740 1.287   -3.449  0.40 11.45 ?  132 PHE   A CE1  1 
ATOM   2832 C  CE2  A PHE   A 1 132 ? 23.180 -0.278  -4.859  0.60 12.76 ?  132 PHE   A CE2  1 
ATOM   2833 C  CE2  B PHE   A 1 132 ? 23.255 -0.014  -4.759  0.40 11.54 ?  132 PHE   A CE2  1 
ATOM   2834 C  CZ   A PHE   A 1 132 ? 23.098 0.806   -4.003  0.60 12.89 ?  132 PHE   A CZ   1 
ATOM   2835 C  CZ   B PHE   A 1 132 ? 23.030 0.909   -3.755  0.40 11.25 ?  132 PHE   A CZ   1 
ATOM   2836 H  H    A PHE   A 1 132 ? 17.642 0.637   -5.073  0.60 13.87 ?  132 PHE   A H    1 
ATOM   2837 H  H    B PHE   A 1 132 ? 17.862 0.718   -5.279  0.40 15.00 ?  132 PHE   A H    1 
ATOM   2838 H  HA   A PHE   A 1 132 ? 19.347 0.734   -7.114  0.60 14.22 ?  132 PHE   A HA   1 
ATOM   2839 H  HA   B PHE   A 1 132 ? 19.639 0.762   -7.238  0.40 15.31 ?  132 PHE   A HA   1 
ATOM   2840 H  HB2  A PHE   A 1 132 ? 18.973 -1.139  -5.080  0.60 14.28 ?  132 PHE   A HB2  1 
ATOM   2841 H  HB2  B PHE   A 1 132 ? 19.107 -1.147  -5.270  0.40 13.99 ?  132 PHE   A HB2  1 
ATOM   2842 H  HB3  A PHE   A 1 132 ? 19.806 -1.568  -6.360  0.60 14.28 ?  132 PHE   A HB3  1 
ATOM   2843 H  HB3  B PHE   A 1 132 ? 20.078 -1.511  -6.471  0.40 13.99 ?  132 PHE   A HB3  1 
ATOM   2844 H  HD1  A PHE   A 1 132 ? 19.896 1.233   -4.119  0.60 15.36 ?  132 PHE   A HD1  1 
ATOM   2845 H  HD1  B PHE   A 1 132 ? 19.805 1.002   -3.937  0.40 14.12 ?  132 PHE   A HD1  1 
ATOM   2846 H  HD2  A PHE   A 1 132 ? 22.099 -1.520  -6.014  0.60 15.19 ?  132 PHE   A HD2  1 
ATOM   2847 H  HD2  B PHE   A 1 132 ? 22.350 -1.174  -6.129  0.40 13.48 ?  132 PHE   A HD2  1 
ATOM   2848 H  HE1  A PHE   A 1 132 ? 21.814 2.097   -3.150  0.60 15.37 ?  132 PHE   A HE1  1 
ATOM   2849 H  HE1  B PHE   A 1 132 ? 21.587 1.909   -2.772  0.40 13.78 ?  132 PHE   A HE1  1 
ATOM   2850 H  HE2  A PHE   A 1 132 ? 24.010 -0.659  -5.048  0.60 15.35 ?  132 PHE   A HE2  1 
ATOM   2851 H  HE2  B PHE   A 1 132 ? 24.125 -0.271  -4.968  0.40 13.89 ?  132 PHE   A HE2  1 
ATOM   2852 H  HZ   A PHE   A 1 132 ? 23.869 1.156   -3.613  0.60 15.51 ?  132 PHE   A HZ   1 
ATOM   2853 H  HZ   B PHE   A 1 132 ? 23.748 1.273   -3.288  0.40 13.54 ?  132 PHE   A HZ   1 
ATOM   2854 N  N    A GLY   A 1 133 ? 16.614 -0.574  -7.738  0.60 12.37 ?  133 GLY   A N    1 
ATOM   2855 N  N    B GLY   A 1 133 ? 16.919 -0.549  -8.000  0.40 13.59 ?  133 GLY   A N    1 
ATOM   2856 C  CA   A GLY   A 1 133 ? 15.825 -0.944  -8.900  0.60 13.36 ?  133 GLY   A CA   1 
ATOM   2857 C  CA   B GLY   A 1 133 ? 16.168 -0.936  -9.177  0.40 13.63 ?  133 GLY   A CA   1 
ATOM   2858 C  C    A GLY   A 1 133 ? 15.589 -2.420  -9.153  0.60 13.93 ?  133 GLY   A C    1 
ATOM   2859 C  C    B GLY   A 1 133 ? 15.570 -2.333  -9.162  0.40 14.06 ?  133 GLY   A C    1 
ATOM   2860 O  O    A GLY   A 1 133 ? 15.059 -2.757  -10.218 0.60 14.77 ?  133 GLY   A O    1 
ATOM   2861 O  O    B GLY   A 1 133 ? 14.657 -2.599  -9.954  0.40 14.33 ?  133 GLY   A O    1 
ATOM   2862 H  H    A GLY   A 1 133 ? 16.145 -0.339  -7.061  0.60 14.88 ?  133 GLY   A H    1 
ATOM   2863 H  H    B GLY   A 1 133 ? 16.423 -0.317  -7.335  0.40 16.35 ?  133 GLY   A H    1 
ATOM   2864 H  HA2  A GLY   A 1 133 ? 14.957 -0.521  -8.825  0.60 16.08 ?  133 GLY   A HA2  1 
ATOM   2865 H  HA2  B GLY   A 1 133 ? 15.441 -0.310  -9.302  0.40 16.40 ?  133 GLY   A HA2  1 
ATOM   2866 H  HA3  A GLY   A 1 133 ? 16.258 -0.595  -9.691  0.60 16.08 ?  133 GLY   A HA3  1 
ATOM   2867 H  HA3  B GLY   A 1 133 ? 16.750 -0.870  -9.951  0.40 16.40 ?  133 GLY   A HA3  1 
ATOM   2868 N  N    A ALA   A 1 134 ? 15.957 -3.313  -8.237  0.60 13.47 ?  134 ALA   A N    1 
ATOM   2869 N  N    B ALA   A 1 134 ? 16.047 -3.231  -8.301  0.40 14.20 ?  134 ALA   A N    1 
ATOM   2870 C  CA   A ALA   A 1 134 ? 15.663 -4.723  -8.443  0.60 14.35 ?  134 ALA   A CA   1 
ATOM   2871 C  CA   B ALA   A 1 134 ? 15.597 -4.614  -8.371  0.40 14.67 ?  134 ALA   A CA   1 
ATOM   2872 C  C    A ALA   A 1 134 ? 14.301 -5.073  -7.848  0.60 14.77 ?  134 ALA   A C    1 
ATOM   2873 C  C    B ALA   A 1 134 ? 14.283 -4.811  -7.619  0.40 14.76 ?  134 ALA   A C    1 
ATOM   2874 O  O    A ALA   A 1 134 ? 13.705 -4.304  -7.091  0.60 15.90 ?  134 ALA   A O    1 
ATOM   2875 O  O    B ALA   A 1 134 ? 13.885 -4.003  -6.775  0.40 14.76 ?  134 ALA   A O    1 
ATOM   2876 C  CB   A ALA   A 1 134 ? 16.759 -5.607  -7.846  0.60 15.44 ?  134 ALA   A CB   1 
ATOM   2877 C  CB   B ALA   A 1 134 ? 16.652 -5.560  -7.804  0.40 15.43 ?  134 ALA   A CB   1 
ATOM   2878 H  H    A ALA   A 1 134 ? 16.376 -3.131  -7.502  0.60 16.21 ?  134 ALA   A H    1 
ATOM   2879 H  H    B ALA   A 1 134 ? 16.623 -3.064  -7.682  0.40 17.09 ?  134 ALA   A H    1 
ATOM   2880 H  HA   A ALA   A 1 134 ? 15.626 -4.900  -9.395  0.60 17.26 ?  134 ALA   A HA   1 
ATOM   2881 H  HA   B ALA   A 1 134 ? 15.448 -4.845  -9.299  0.40 17.65 ?  134 ALA   A HA   1 
ATOM   2882 H  HB1  A ALA   A 1 134 ? 16.541 -6.535  -8.022  0.60 18.58 ?  134 ALA   A HB1  1 
ATOM   2883 H  HB1  B ALA   A 1 134 ? 16.322 -6.469  -7.874  0.40 18.56 ?  134 ALA   A HB1  1 
ATOM   2884 H  HB2  A ALA   A 1 134 ? 17.605 -5.381  -8.263  0.60 18.58 ?  134 ALA   A HB2  1 
ATOM   2885 H  HB2  B ALA   A 1 134 ? 17.466 -5.459  -8.317  0.40 18.56 ?  134 ALA   A HB2  1 
ATOM   2886 H  HB3  A ALA   A 1 134 ? 16.805 -5.450  -6.892  0.60 18.58 ?  134 ALA   A HB3  1 
ATOM   2887 H  HB3  B ALA   A 1 134 ? 16.810 -5.334  -6.875  0.40 18.56 ?  134 ALA   A HB3  1 
ATOM   2888 N  N    A ASP   A 1 135 ? 13.807 -6.248  -8.212  0.60 15.21 ?  135 ASP   A N    1 
ATOM   2889 N  N    B ASP   A 1 135 ? 13.620 -5.923  -7.926  0.40 15.52 ?  135 ASP   A N    1 
ATOM   2890 C  CA   A ASP   A 1 135 ? 12.546 -6.738  -7.669  0.60 15.97 ?  135 ASP   A CA   1 
ATOM   2891 C  CA   B ASP   A 1 135 ? 12.348 -6.250  -7.301  0.40 16.21 ?  135 ASP   A CA   1 
ATOM   2892 C  C    A ASP   A 1 135 ? 12.768 -7.174  -6.227  0.60 15.64 ?  135 ASP   A C    1 
ATOM   2893 C  C    B ASP   A 1 135 ? 12.588 -6.785  -5.893  0.40 15.30 ?  135 ASP   A C    1 
ATOM   2894 O  O    A ASP   A 1 135 ? 13.584 -8.072  -5.980  0.60 15.47 ?  135 ASP   A O    1 
ATOM   2895 O  O    B ASP   A 1 135 ? 13.310 -7.777  -5.733  0.40 15.13 ?  135 ASP   A O    1 
ATOM   2896 C  CB   A ASP   A 1 135 ? 12.059 -7.918  -8.499  0.60 18.20 ?  135 ASP   A CB   1 
ATOM   2897 C  CB   B ASP   A 1 135 ? 11.604 -7.280  -8.135  0.40 17.90 ?  135 ASP   A CB   1 
ATOM   2898 C  CG   A ASP   A 1 135 ? 10.723 -8.471  -8.020  0.60 20.55 ?  135 ASP   A CG   1 
ATOM   2899 C  CG   B ASP   A 1 135 ? 10.653 -8.115  -7.307  0.40 19.63 ?  135 ASP   A CG   1 
ATOM   2900 O  OD1  A ASP   A 1 135 ? 10.207 -8.015  -6.979  0.60 21.37 ?  135 ASP   A OD1  1 
ATOM   2901 O  OD1  B ASP   A 1 135 ? 9.853  -7.528  -6.545  0.40 19.94 ?  135 ASP   A OD1  1 
ATOM   2902 O  OD2  A ASP   A 1 135 ? 10.177 -9.364  -8.699  0.60 22.56 -1 135 ASP   A OD2  1 
ATOM   2903 O  OD2  B ASP   A 1 135 ? 10.715 -9.357  -7.412  0.40 20.65 -1 135 ASP   A OD2  1 
ATOM   2904 H  H    A ASP   A 1 135 ? 14.177 -6.779  -8.775  0.60 18.30 ?  135 ASP   A H    1 
ATOM   2905 H  H    B ASP   A 1 135 ? 13.888 -6.507  -8.491  0.40 18.66 ?  135 ASP   A H    1 
ATOM   2906 H  HA   A ASP   A 1 135 ? 11.881 -6.033  -7.708  0.60 19.21 ?  135 ASP   A HA   1 
ATOM   2907 H  HA   B ASP   A 1 135 ? 11.800 -5.451  -7.258  0.40 19.49 ?  135 ASP   A HA   1 
ATOM   2908 H  HB2  A ASP   A 1 135 ? 11.945 -7.633  -9.418  0.60 21.89 ?  135 ASP   A HB2  1 
ATOM   2909 H  HB2  B ASP   A 1 135 ? 11.095 -6.817  -8.826  0.40 21.52 ?  135 ASP   A HB2  1 
ATOM   2910 H  HB3  A ASP   A 1 135 ? 12.710 -8.632  -8.448  0.60 21.89 ?  135 ASP   A HB3  1 
ATOM   2911 H  HB3  B ASP   A 1 135 ? 12.246 -7.877  -8.548  0.40 21.52 ?  135 ASP   A HB3  1 
ATOM   2912 N  N    A PRO   A 1 136 ? 12.088 -6.571  -5.251  0.60 15.70 ?  136 PRO   A N    1 
ATOM   2913 N  N    B PRO   A 1 136 ? 12.017 -6.166  -4.856  0.40 14.77 ?  136 PRO   A N    1 
ATOM   2914 C  CA   A PRO   A 1 136 ? 12.319 -6.962  -3.851  0.60 15.62 ?  136 PRO   A CA   1 
ATOM   2915 C  CA   B PRO   A 1 136 ? 12.294 -6.618  -3.482  0.40 14.52 ?  136 PRO   A CA   1 
ATOM   2916 C  C    A PRO   A 1 136 ? 11.898 -8.383  -3.529  0.60 14.65 ?  136 PRO   A C    1 
ATOM   2917 C  C    B PRO   A 1 136 ? 11.875 -8.055  -3.206  0.40 13.51 ?  136 PRO   A C    1 
ATOM   2918 O  O    A PRO   A 1 136 ? 12.502 -9.004  -2.647  0.60 14.11 ?  136 PRO   A O    1 
ATOM   2919 O  O    B PRO   A 1 136 ? 12.469 -8.707  -2.338  0.40 12.63 ?  136 PRO   A O    1 
ATOM   2920 C  CB   A PRO   A 1 136 ? 11.504 -5.931  -3.059  0.60 16.57 ?  136 PRO   A CB   1 
ATOM   2921 C  CB   B PRO   A 1 136 ? 11.525 -5.601  -2.622  0.40 15.19 ?  136 PRO   A CB   1 
ATOM   2922 C  CG   A PRO   A 1 136 ? 10.484 -5.422  -4.032  0.60 17.05 ?  136 PRO   A CG   1 
ATOM   2923 C  CG   B PRO   A 1 136 ? 10.475 -5.045  -3.533  0.40 15.67 ?  136 PRO   A CG   1 
ATOM   2924 C  CD   A PRO   A 1 136 ? 11.121 -5.467  -5.375  0.60 16.58 ?  136 PRO   A CD   1 
ATOM   2925 C  CD   B PRO   A 1 136 ? 11.115 -5.002  -4.881  0.40 15.06 ?  136 PRO   A CD   1 
ATOM   2926 H  HA   A PRO   A 1 136 ? 13.259 -6.862  -3.624  0.60 18.78 ?  136 PRO   A HA   1 
ATOM   2927 H  HA   B PRO   A 1 136 ? 13.239 -6.526  -3.286  0.40 17.47 ?  136 PRO   A HA   1 
ATOM   2928 H  HB2  A PRO   A 1 136 ? 11.075 -6.366  -2.303  0.60 19.93 ?  136 PRO   A HB2  1 
ATOM   2929 H  HB2  B PRO   A 1 136 ? 11.116 -6.042  -1.864  0.40 18.28 ?  136 PRO   A HB2  1 
ATOM   2930 H  HB3  A PRO   A 1 136 ? 12.088 -5.218  -2.758  0.60 19.93 ?  136 PRO   A HB3  1 
ATOM   2931 H  HB3  B PRO   A 1 136 ? 12.123 -4.892  -2.327  0.40 18.28 ?  136 PRO   A HB3  1 
ATOM   2932 H  HG2  A PRO   A 1 136 ? 9.705  -5.993  -4.011  0.60 20.50 ?  136 PRO   A HG2  1 
ATOM   2933 H  HG2  B PRO   A 1 136 ? 9.705  -5.636  -3.544  0.40 18.85 ?  136 PRO   A HG2  1 
ATOM   2934 H  HG3  A PRO   A 1 136 ? 10.251 -4.511  -3.804  0.60 20.50 ?  136 PRO   A HG3  1 
ATOM   2935 H  HG3  B PRO   A 1 136 ? 10.222 -4.155  -3.249  0.40 18.85 ?  136 PRO   A HG3  1 
ATOM   2936 H  HD2  A PRO   A 1 136 ? 10.462 -5.678  -6.055  0.60 19.93 ?  136 PRO   A HD2  1 
ATOM   2937 H  HD2  B PRO   A 1 136 ? 10.445 -5.107  -5.577  0.40 18.12 ?  136 PRO   A HD2  1 
ATOM   2938 H  HD3  A PRO   A 1 136 ? 11.580 -4.635  -5.569  0.60 19.93 ?  136 PRO   A HD3  1 
ATOM   2939 H  HD3  B PRO   A 1 136 ? 11.622 -4.182  -4.996  0.40 18.12 ?  136 PRO   A HD3  1 
ATOM   2940 N  N    A ILE   A 1 137 ? 10.861 -8.910  -4.183  0.60 14.64 ?  137 ILE   A N    1 
ATOM   2941 N  N    B ILE   A 1 137 ? 10.862 -8.567  -3.906  0.40 13.80 ?  137 ILE   A N    1 
ATOM   2942 C  CA   A ILE   A 1 137 ? 10.511 -10.314 -3.988  0.60 14.90 ?  137 ILE   A CA   1 
ATOM   2943 C  CA   B ILE   A 1 137 ? 10.453 -9.958  -3.712  0.40 14.18 ?  137 ILE   A CA   1 
ATOM   2944 C  C    A ILE   A 1 137 ? 11.686 -11.196 -4.383  0.60 14.37 ?  137 ILE   A C    1 
ATOM   2945 C  C    B ILE   A 1 137 ? 11.582 -10.902 -4.112  0.40 13.74 ?  137 ILE   A C    1 
ATOM   2946 O  O    A ILE   A 1 137 ? 12.012 -12.173 -3.698  0.60 14.20 ?  137 ILE   A O    1 
ATOM   2947 O  O    B ILE   A 1 137 ? 11.876 -11.881 -3.414  0.40 13.55 ?  137 ILE   A O    1 
ATOM   2948 C  CB   A ILE   A 1 137 ? 9.223  -10.664 -4.762  0.60 16.20 ?  137 ILE   A CB   1 
ATOM   2949 C  CB   B ILE   A 1 137 ? 9.164  -10.246 -4.504  0.40 15.05 ?  137 ILE   A CB   1 
ATOM   2950 C  CG1  A ILE   A 1 137 ? 8.034  -9.848  -4.233  0.60 17.64 ?  137 ILE   A CG1  1 
ATOM   2951 C  CG1  B ILE   A 1 137 ? 8.052  -9.259  -4.115  0.40 16.36 ?  137 ILE   A CG1  1 
ATOM   2952 C  CG2  A ILE   A 1 137 ? 8.921  -12.158 -4.655  0.60 16.51 ?  137 ILE   A CG2  1 
ATOM   2953 C  CG2  B ILE   A 1 137 ? 8.724  -11.691 -4.290  0.40 15.36 ?  137 ILE   A CG2  1 
ATOM   2954 C  CD1  A ILE   A 1 137 ? 6.749  -10.037 -5.016  0.60 18.40 ?  137 ILE   A CD1  1 
ATOM   2955 C  CD1  B ILE   A 1 137 ? 6.877  -9.252  -5.064  0.40 17.14 ?  137 ILE   A CD1  1 
ATOM   2956 H  H    A ILE   A 1 137 ? 10.355 -8.487  -4.730  0.60 17.61 ?  137 ILE   A H    1 
ATOM   2957 H  H    B ILE   A 1 137 ? 10.396 -8.124  -4.482  0.40 16.60 ?  137 ILE   A H    1 
ATOM   2958 H  HA   A ILE   A 1 137 ? 10.336 -10.473 -3.050  0.60 17.93 ?  137 ILE   A HA   1 
ATOM   2959 H  HA   B ILE   A 1 137 ? 10.258 -10.092 -2.769  0.40 17.06 ?  137 ILE   A HA   1 
ATOM   2960 H  HB   A ILE   A 1 137 ? 9.349  -10.447 -5.696  0.60 19.48 ?  137 ILE   A HB   1 
ATOM   2961 H  HB   B ILE   A 1 137 ? 9.358  -10.123 -5.445  0.40 18.10 ?  137 ILE   A HB   1 
ATOM   2962 H  HG12 A ILE   A 1 137 ? 7.866  -10.105 -3.312  0.60 21.21 ?  137 ILE   A HG12 1 
ATOM   2963 H  HG12 B ILE   A 1 137 ? 7.723  -9.495  -3.236  0.40 19.68 ?  137 ILE   A HG12 1 
ATOM   2964 H  HG13 A ILE   A 1 137 ? 8.270  -8.905  -4.269  0.60 21.21 ?  137 ILE   A HG13 1 
ATOM   2965 H  HG13 B ILE   A 1 137 ? 8.414  -8.357  -4.095  0.40 19.68 ?  137 ILE   A HG13 1 
ATOM   2966 H  HG21 A ILE   A 1 137 ? 8.160  -12.376 -5.215  0.60 19.85 ?  137 ILE   A HG21 1 
ATOM   2967 H  HG21 B ILE   A 1 137 ? 7.839  -11.810 -4.667  0.40 18.48 ?  137 ILE   A HG21 1 
ATOM   2968 H  HG22 A ILE   A 1 137 ? 9.686  -12.666 -4.955  0.60 19.85 ?  137 ILE   A HG22 1 
ATOM   2969 H  HG22 B ILE   A 1 137 ? 9.354  -12.282 -4.733  0.40 18.48 ?  137 ILE   A HG22 1 
ATOM   2970 H  HG23 A ILE   A 1 137 ? 8.721  -12.371 -3.731  0.60 19.85 ?  137 ILE   A HG23 1 
ATOM   2971 H  HG23 B ILE   A 1 137 ? 8.706  -11.878 -3.338  0.40 18.48 ?  137 ILE   A HG23 1 
ATOM   2972 H  HD11 A ILE   A 1 137 ? 6.013  -9.800  -4.441  0.60 22.13 ?  137 ILE   A HD11 1 
ATOM   2973 H  HD11 B ILE   A 1 137 ? 6.661  -8.332  -5.290  0.40 20.61 ?  137 ILE   A HD11 1 
ATOM   2974 H  HD12 A ILE   A 1 137 ? 6.772  -9.458  -5.793  0.60 22.13 ?  137 ILE   A HD12 1 
ATOM   2975 H  HD12 B ILE   A 1 137 ? 7.118  -9.739  -5.868  0.40 20.61 ?  137 ILE   A HD12 1 
ATOM   2976 H  HD13 A ILE   A 1 137 ? 6.661  -10.960 -5.293  0.60 22.13 ?  137 ILE   A HD13 1 
ATOM   2977 H  HD13 B ILE   A 1 137 ? 6.121  -9.676  -4.633  0.40 20.61 ?  137 ILE   A HD13 1 
ATOM   2978 N  N    A HIS   A 1 138 ? 12.342 -10.860 -5.490  0.60 14.69 ?  138 HIS   A N    1 
ATOM   2979 N  N    B HIS   A 1 138 ? 12.222 -10.627 -5.249  0.40 13.93 ?  138 HIS   A N    1 
ATOM   2980 C  CA   A HIS   A 1 138 ? 13.556 -11.570 -5.869  0.60 14.60 ?  138 HIS   A CA   1 
ATOM   2981 C  CA   B HIS   A 1 138 ? 13.331 -11.458 -5.709  0.40 13.98 ?  138 HIS   A CA   1 
ATOM   2982 C  C    A HIS   A 1 138 ? 14.662 -11.387 -4.831  0.60 13.91 ?  138 HIS   A C    1 
ATOM   2983 C  C    B HIS   A 1 138 ? 14.515 -11.376 -4.755  0.40 13.69 ?  138 HIS   A C    1 
ATOM   2984 O  O    A HIS   A 1 138 ? 15.354 -12.353 -4.483  0.60 13.92 ?  138 HIS   A O    1 
ATOM   2985 O  O    B HIS   A 1 138 ? 15.132 -12.395 -4.422  0.40 13.89 ?  138 HIS   A O    1 
ATOM   2986 C  CB   A HIS   A 1 138 ? 14.012 -11.134 -7.259  0.60 15.46 ?  138 HIS   A CB   1 
ATOM   2987 C  CB   B HIS   A 1 138 ? 13.740 -11.018 -7.115  0.40 14.18 ?  138 HIS   A CB   1 
ATOM   2988 C  CG   A HIS   A 1 138 ? 15.251 -11.833 -7.724  0.60 16.50 ?  138 HIS   A CG   1 
ATOM   2989 C  CG   B HIS   A 1 138 ? 15.031 -11.614 -7.583  0.40 14.88 ?  138 HIS   A CG   1 
ATOM   2990 N  ND1  A HIS   A 1 138 ? 15.312 -13.198 -7.913  0.60 17.58 ?  138 HIS   A ND1  1 
ATOM   2991 N  ND1  B HIS   A 1 138 ? 15.148 -12.933 -7.964  0.40 15.98 ?  138 HIS   A ND1  1 
ATOM   2992 C  CD2  A HIS   A 1 138 ? 16.483 -11.357 -8.018  0.60 16.65 ?  138 HIS   A CD2  1 
ATOM   2993 C  CD2  B HIS   A 1 138 ? 16.263 -11.069 -7.730  0.40 14.74 ?  138 HIS   A CD2  1 
ATOM   2994 C  CE1  A HIS   A 1 138 ? 16.524 -13.530 -8.316  0.60 17.96 ?  138 HIS   A CE1  1 
ATOM   2995 C  CE1  B HIS   A 1 138 ? 16.395 -13.175 -8.326  0.40 15.98 ?  138 HIS   A CE1  1 
ATOM   2996 N  NE2  A HIS   A 1 138 ? 17.255 -12.432 -8.386  0.60 17.21 ?  138 HIS   A NE2  1 
ATOM   2997 N  NE2  B HIS   A 1 138 ? 17.093 -12.061 -8.193  0.40 15.21 ?  138 HIS   A NE2  1 
ATOM   2998 H  H    A HIS   A 1 138 ? 12.101 -10.234 -6.035  0.60 17.67 ?  138 HIS   A H    1 
ATOM   2999 H  H    B HIS   A 1 138 ? 12.033 -9.965  -5.767  0.40 16.76 ?  138 HIS   A H    1 
ATOM   3000 H  HA   A HIS   A 1 138 ? 13.354 -12.513 -5.917  0.60 17.56 ?  138 HIS   A HA   1 
ATOM   3001 H  HA   B HIS   A 1 138 ? 13.039 -12.378 -5.748  0.40 16.81 ?  138 HIS   A HA   1 
ATOM   3002 H  HB2  A HIS   A 1 138 ? 13.301 -11.325 -7.898  0.60 18.60 ?  138 HIS   A HB2  1 
ATOM   3003 H  HB2  B HIS   A 1 138 ? 13.044 -11.285 -7.738  0.40 17.06 ?  138 HIS   A HB2  1 
ATOM   3004 H  HB3  A HIS   A 1 138 ? 14.190 -10.179 -7.250  0.60 18.60 ?  138 HIS   A HB3  1 
ATOM   3005 H  HB3  B HIS   A 1 138 ? 13.834 -10.052 -7.127  0.40 17.06 ?  138 HIS   A HB3  1 
ATOM   3006 H  HD1  B HIS   A 1 138 ? 14.506 -13.508 -7.965  0.40 19.21 ?  138 HIS   A HD1  1 
ATOM   3007 H  HD2  A HIS   A 1 138 ? 16.752 -10.467 -7.981  0.60 20.02 ?  138 HIS   A HD2  1 
ATOM   3008 H  HD2  B HIS   A 1 138 ? 16.500 -10.188 -7.551  0.40 17.72 ?  138 HIS   A HD2  1 
ATOM   3009 H  HE1  A HIS   A 1 138 ? 16.809 -14.389 -8.516  0.60 21.60 ?  138 HIS   A HE1  1 
ATOM   3010 H  HE1  B HIS   A 1 138 ? 16.723 -13.993 -8.623  0.40 19.22 ?  138 HIS   A HE1  1 
ATOM   3011 H  HE2  A HIS   A 1 138 ? 18.076 -12.394 -8.623  0.60 20.70 ?  138 HIS   A HE2  1 
ATOM   3012 N  N    . SER   A 1 139 ? 14.848 -10.165 -4.316  1.00 13.46 ?  139 SER   A N    1 
ATOM   3013 C  CA   . SER   A 1 139 ? 15.917 -9.972  -3.346  1.00 13.00 ?  139 SER   A CA   1 
ATOM   3014 C  C    . SER   A 1 139 ? 15.699 -10.817 -2.096  1.00 12.55 ?  139 SER   A C    1 
ATOM   3015 O  O    . SER   A 1 139 ? 16.651 -11.401 -1.564  1.00 12.61 ?  139 SER   A O    1 
ATOM   3016 C  CB   . SER   A 1 139 ? 16.036 -8.492  -2.993  1.00 13.13 ?  139 SER   A CB   1 
ATOM   3017 O  OG   . SER   A 1 139 ? 17.118 -8.313  -2.092  1.00 13.42 ?  139 SER   A OG   1 
ATOM   3018 H  H    A SER   A 1 139 ? 14.385 -9.459  -4.502  0.60 16.20 ?  139 SER   A H    1 
ATOM   3019 H  H    B SER   A 1 139 ? 14.455 -9.434  -4.557  0.40 16.20 ?  139 SER   A H    1 
ATOM   3020 H  HA   . SER   A 1 139 ? 16.756 -10.240 -3.744  1.00 15.64 ?  139 SER   A HA   1 
ATOM   3021 H  HB2  . SER   A 1 139 ? 16.209 -7.975  -3.797  1.00 15.80 ?  139 SER   A HB2  1 
ATOM   3022 H  HB3  . SER   A 1 139 ? 15.208 -8.192  -2.584  1.00 15.80 ?  139 SER   A HB3  1 
ATOM   3023 H  HG   . SER   A 1 139 ? 17.195 -7.491  -1.885  1.00 16.15 ?  139 SER   A HG   1 
ATOM   3024 N  N    . LEU   A 1 140 ? 14.458 -10.886 -1.607  1.00 12.49 ?  140 LEU   A N    1 
ATOM   3025 C  CA   . LEU   A 1 140 ? 14.184 -11.706 -0.431  1.00 12.36 ?  140 LEU   A CA   1 
ATOM   3026 C  C    . LEU   A 1 140 ? 14.456 -13.179 -0.715  1.00 12.48 ?  140 LEU   A C    1 
ATOM   3027 O  O    . LEU   A 1 140 ? 15.011 -13.894 0.130   1.00 12.81 ?  140 LEU   A O    1 
ATOM   3028 C  CB   . LEU   A 1 140 ? 12.739 -11.496 0.018   1.00 12.80 ?  140 LEU   A CB   1 
ATOM   3029 C  CG   . LEU   A 1 140 ? 12.286 -12.352 1.200   1.00 12.97 ?  140 LEU   A CG   1 
ATOM   3030 C  CD1  . LEU   A 1 140 ? 13.180 -12.153 2.409   1.00 13.02 ?  140 LEU   A CD1  1 
ATOM   3031 C  CD2  . LEU   A 1 140 ? 10.826 -12.058 1.555   1.00 13.86 ?  140 LEU   A CD2  1 
ATOM   3032 H  H    . LEU   A 1 140 ? 13.778 -10.463 -1.922  1.00 15.03 ?  140 LEU   A H    1 
ATOM   3033 H  HA   . LEU   A 1 140 ? 14.764 -11.427 0.293   1.00 14.88 ?  140 LEU   A HA   1 
ATOM   3034 H  HB2  . LEU   A 1 140 ? 12.623 -10.573 0.275   1.00 15.40 ?  140 LEU   A HB2  1 
ATOM   3035 H  HB3  . LEU   A 1 140 ? 12.153 -11.706 -0.725  1.00 15.40 ?  140 LEU   A HB3  1 
ATOM   3036 H  HG   . LEU   A 1 140 ? 12.331 -13.289 0.950   1.00 15.60 ?  140 LEU   A HG   1 
ATOM   3037 H  HD11 . LEU   A 1 140 ? 12.797 -12.619 3.168   1.00 15.67 ?  140 LEU   A HD11 1 
ATOM   3038 H  HD12 . LEU   A 1 140 ? 14.058 -12.518 2.208   1.00 15.67 ?  140 LEU   A HD12 1 
ATOM   3039 H  HD13 . LEU   A 1 140 ? 13.249 -11.207 2.598   1.00 15.67 ?  140 LEU   A HD13 1 
ATOM   3040 H  HD21 . LEU   A 1 140 ? 10.561 -12.624 2.305   1.00 16.67 ?  140 LEU   A HD21 1 
ATOM   3041 H  HD22 . LEU   A 1 140 ? 10.739 -11.127 1.803   1.00 16.67 ?  140 LEU   A HD22 1 
ATOM   3042 H  HD23 . LEU   A 1 140 ? 10.264 -12.254 0.789   1.00 16.67 ?  140 LEU   A HD23 1 
ATOM   3043 N  N    . ARG   A 1 141 ? 14.064 -13.653 -1.900  1.00 13.08 ?  141 ARG   A N    1 
ATOM   3044 C  CA   . ARG   A 1 141 ? 14.308 -15.042 -2.266  1.00 13.96 ?  141 ARG   A CA   1 
ATOM   3045 C  C    . ARG   A 1 141 ? 15.803 -15.347 -2.278  1.00 12.98 ?  141 ARG   A C    1 
ATOM   3046 O  O    . ARG   A 1 141 ? 16.248 -16.361 -1.722  1.00 13.20 ?  141 ARG   A O    1 
ATOM   3047 C  CB   . ARG   A 1 141 ? 13.687 -15.308 -3.639  1.00 16.12 ?  141 ARG   A CB   1 
ATOM   3048 C  CG   . ARG   A 1 141 ? 13.694 -16.757 -4.081  1.00 19.13 ?  141 ARG   A CG   1 
ATOM   3049 C  CD   . ARG   A 1 141 ? 12.658 -17.534 -3.334  1.00 21.30 ?  141 ARG   A CD   1 
ATOM   3050 N  NE   . ARG   A 1 141 ? 13.267 -18.340 -2.289  1.00 22.12 ?  141 ARG   A NE   1 
ATOM   3051 C  CZ   . ARG   A 1 141 ? 12.585 -18.922 -1.312  1.00 22.88 ?  141 ARG   A CZ   1 
ATOM   3052 N  NH1  . ARG   A 1 141 ? 11.296 -18.684 -1.130  1.00 22.70 ?  141 ARG   A NH1  1 
ATOM   3053 N  NH2  . ARG   A 1 141 ? 13.215 -19.759 -0.492  1.00 23.35 ?  141 ARG   A NH2  1 
ATOM   3054 H  H    . ARG   A 1 141 ? 13.654 -13.192 -2.501  1.00 15.74 ?  141 ARG   A H    1 
ATOM   3055 H  HA   . ARG   A 1 141 ? 13.885 -15.625 -1.619  1.00 16.80 ?  141 ARG   A HA   1 
ATOM   3056 H  HB2  . ARG   A 1 141 ? 12.767 -15.004 -3.628  1.00 19.38 ?  141 ARG   A HB2  1 
ATOM   3057 H  HB3  . ARG   A 1 141 ? 14.184 -14.800 -4.302  1.00 19.38 ?  141 ARG   A HB3  1 
ATOM   3058 H  HG2  . ARG   A 1 141 ? 13.497 -16.808 -5.031  1.00 23.00 ?  141 ARG   A HG2  1 
ATOM   3059 H  HG3  . ARG   A 1 141 ? 14.566 -17.150 -3.900  1.00 23.00 ?  141 ARG   A HG3  1 
ATOM   3060 H  HD2  . ARG   A 1 141 ? 12.036 -16.923 -2.909  1.00 25.61 ?  141 ARG   A HD2  1 
ATOM   3061 H  HD3  . ARG   A 1 141 ? 12.182 -18.115 -3.954  1.00 25.61 ?  141 ARG   A HD3  1 
ATOM   3062 H  HE   . ARG   A 1 141 ? 14.089 -18.568 -2.388  1.00 26.59 ?  141 ARG   A HE   1 
ATOM   3063 H  HH11 . ARG   A 1 141 ? 10.871 -18.161 -1.664  1.00 27.28 ?  141 ARG   A HH11 1 
ATOM   3064 H  HH12 . ARG   A 1 141 ? 10.872 -19.071 -0.486  1.00 27.28 ?  141 ARG   A HH12 1 
ATOM   3065 H  HH21 . ARG   A 1 141 ? 14.050 -19.924 -0.604  1.00 28.06 ?  141 ARG   A HH21 1 
ATOM   3066 H  HH22 . ARG   A 1 141 ? 12.785 -20.135 0.155   1.00 28.06 ?  141 ARG   A HH22 1 
ATOM   3067 N  N    . VAL   A 1 142 ? 16.598 -14.479 -2.909  1.00 12.51 ?  142 VAL   A N    1 
ATOM   3068 C  CA   . VAL   A 1 142 ? 18.043 -14.693 -2.940  1.00 12.37 ?  142 VAL   A CA   1 
ATOM   3069 C  C    . VAL   A 1 142 ? 18.613 -14.676 -1.529  1.00 11.89 ?  142 VAL   A C    1 
ATOM   3070 O  O    . VAL   A 1 142 ? 19.476 -15.490 -1.182  1.00 12.02 ?  142 VAL   A O    1 
ATOM   3071 C  CB   . VAL   A 1 142 ? 18.734 -13.667 -3.855  1.00 12.48 ?  142 VAL   A CB   1 
ATOM   3072 C  CG1  . VAL   A 1 142 ? 20.247 -13.882 -3.824  1.00 12.67 ?  142 VAL   A CG1  1 
ATOM   3073 C  CG2  . VAL   A 1 142 ? 18.222 -13.794 -5.277  1.00 13.70 ?  142 VAL   A CG2  1 
ATOM   3074 H  H    . VAL   A 1 142 ? 16.330 -13.764 -3.317  1.00 15.05 ?  142 VAL   A H    1 
ATOM   3075 H  HA   . VAL   A 1 142 ? 18.214 -15.565 -3.314  1.00 14.89 ?  142 VAL   A HA   1 
ATOM   3076 H  HB   . VAL   A 1 142 ? 18.555 -12.764 -3.537  1.00 15.02 ?  142 VAL   A HB   1 
ATOM   3077 H  HG11 . VAL   A 1 142 ? 20.655 -13.391 -4.555  1.00 15.25 ?  142 VAL   A HG11 1 
ATOM   3078 H  HG12 . VAL   A 1 142 ? 20.603 -13.561 -2.977  1.00 15.25 ?  142 VAL   A HG12 1 
ATOM   3079 H  HG13 . VAL   A 1 142 ? 20.434 -14.830 -3.920  1.00 15.25 ?  142 VAL   A HG13 1 
ATOM   3080 H  HG21 . VAL   A 1 142 ? 18.690 -13.154 -5.837  1.00 16.48 ?  142 VAL   A HG21 1 
ATOM   3081 H  HG22 . VAL   A 1 142 ? 18.396 -14.695 -5.587  1.00 16.48 ?  142 VAL   A HG22 1 
ATOM   3082 H  HG23 . VAL   A 1 142 ? 17.274 -13.612 -5.282  1.00 16.48 ?  142 VAL   A HG23 1 
ATOM   3083 N  N    . CYS   A 1 143 ? 18.139 -13.755 -0.692  1.00 11.84 ?  143 CYS   A N    1 
ATOM   3084 C  CA   . CYS   A 1 143 ? 18.599 -13.704 0.691   1.00 11.81 ?  143 CYS   A CA   1 
ATOM   3085 C  C    . CYS   A 1 143 ? 18.375 -15.043 1.386   1.00 11.69 ?  143 CYS   A C    1 
ATOM   3086 O  O    . CYS   A 1 143 ? 19.296 -15.623 1.971   1.00 11.47 ?  143 CYS   A O    1 
ATOM   3087 C  CB   . CYS   A 1 143 ? 17.864 -12.587 1.431   1.00 11.95 ?  143 CYS   A CB   1 
ATOM   3088 S  SG   . CYS   A 1 143 ? 18.364 -12.400 3.156   1.00 12.43 ?  143 CYS   A SG   1 
ATOM   3089 H  H    . CYS   A 1 143 ? 17.555 -13.163 -0.897  1.00 14.25 ?  143 CYS   A H    1 
ATOM   3090 H  HA   . CYS   A 1 143 ? 19.546 -13.514 0.707   1.00 14.21 ?  143 CYS   A HA   1 
ATOM   3091 H  HB2  . CYS   A 1 143 ? 18.036 -11.747 0.978   1.00 14.38 ?  143 CYS   A HB2  1 
ATOM   3092 H  HB3  . CYS   A 1 143 ? 16.914 -12.775 1.416   1.00 14.38 ?  143 CYS   A HB3  1 
ATOM   3093 H  HG   . CYS   A 1 143 ? 17.810 -11.450 3.616   1.00 14.96 ?  143 CYS   A HG   1 
ATOM   3094 N  N    . VAL   A 1 144 ? 17.144 -15.547 1.330   1.00 12.23 ?  144 VAL   A N    1 
ATOM   3095 C  CA   . VAL   A 1 144 ? 16.800 -16.781 2.025   1.00 13.17 ?  144 VAL   A CA   1 
ATOM   3096 C  C    . VAL   A 1 144 ? 17.623 -17.948 1.502   1.00 12.52 ?  144 VAL   A C    1 
ATOM   3097 O  O    . VAL   A 1 144 ? 17.995 -18.854 2.261   1.00 13.14 ?  144 VAL   A O    1 
ATOM   3098 C  CB   . VAL   A 1 144 ? 15.285 -17.022 1.884   1.00 15.92 ?  144 VAL   A CB   1 
ATOM   3099 C  CG1  . VAL   A 1 144 ? 14.920 -18.456 2.202   1.00 17.51 ?  144 VAL   A CG1  1 
ATOM   3100 C  CG2  . VAL   A 1 144 ? 14.517 -16.019 2.763   1.00 16.21 ?  144 VAL   A CG2  1 
ATOM   3101 H  H    . VAL   A 1 144 ? 16.489 -15.191 0.892   1.00 14.72 ?  144 VAL   A H    1 
ATOM   3102 H  HA   . VAL   A 1 144 ? 16.992 -16.675 2.964   1.00 15.85 ?  144 VAL   A HA   1 
ATOM   3103 H  HB   . VAL   A 1 144 ? 15.024 -16.851 0.961   1.00 19.15 ?  144 VAL   A HB   1 
ATOM   3104 H  HG11 . VAL   A 1 144 ? 13.965 -18.507 2.380   1.00 21.05 ?  144 VAL   A HG11 1 
ATOM   3105 H  HG12 . VAL   A 1 144 ? 15.140 -19.017 1.442   1.00 21.05 ?  144 VAL   A HG12 1 
ATOM   3106 H  HG13 . VAL   A 1 144 ? 15.414 -18.741 2.984   1.00 21.05 ?  144 VAL   A HG13 1 
ATOM   3107 H  HG21 . VAL   A 1 144 ? 13.563 -16.190 2.694   1.00 19.50 ?  144 VAL   A HG21 1 
ATOM   3108 H  HG22 . VAL   A 1 144 ? 14.802 -16.114 3.684   1.00 19.50 ?  144 VAL   A HG22 1 
ATOM   3109 H  HG23 . VAL   A 1 144 ? 14.705 -15.112 2.456   1.00 19.50 ?  144 VAL   A HG23 1 
ATOM   3110 N  N    . ASP   A 1 145 ? 17.887 -17.968 0.198   1.00 13.00 ?  145 ASP   A N    1 
ATOM   3111 C  CA   . ASP   A 1 145 ? 18.603 -19.069 -0.433  1.00 13.52 ?  145 ASP   A CA   1 
ATOM   3112 C  C    . ASP   A 1 145 ? 20.125 -18.922 -0.383  1.00 13.48 ?  145 ASP   A C    1 
ATOM   3113 O  O    . ASP   A 1 145 ? 20.831 -19.822 -0.856  1.00 15.64 ?  145 ASP   A O    1 
ATOM   3114 C  CB   . ASP   A 1 145 ? 18.153 -19.215 -1.889  1.00 15.35 ?  145 ASP   A CB   1 
ATOM   3115 C  CG   . ASP   A 1 145 ? 16.705 -19.657 -2.016  1.00 17.66 ?  145 ASP   A CG   1 
ATOM   3116 O  OD1  . ASP   A 1 145 ? 16.134 -20.186 -1.036  1.00 18.12 ?  145 ASP   A OD1  1 
ATOM   3117 O  OD2  . ASP   A 1 145 ? 16.136 -19.472 -3.109  1.00 19.01 -1 145 ASP   A OD2  1 
ATOM   3118 H  H    . ASP   A 1 145 ? 17.642 -17.349 -0.352  1.00 15.65 ?  145 ASP   A H    1 
ATOM   3119 H  HA   . ASP   A 1 145 ? 18.369 -19.889 0.025   1.00 16.26 ?  145 ASP   A HA   1 
ATOM   3120 H  HB2  . ASP   A 1 145 ? 18.253 -18.363 -2.342  1.00 18.46 ?  145 ASP   A HB2  1 
ATOM   3121 H  HB3  . ASP   A 1 145 ? 18.696 -19.889 -2.322  1.00 18.46 ?  145 ASP   A HB3  1 
ATOM   3122 N  N    . THR   A 1 146 ? 20.650 -17.829 0.168   1.00 11.85 ?  146 THR   A N    1 
ATOM   3123 C  CA   . THR   A 1 146 ? 22.090 -17.576 0.187   1.00 11.28 ?  146 THR   A CA   1 
ATOM   3124 C  C    . THR   A 1 146 ? 22.639 -17.398 1.592   1.00 11.26 ?  146 THR   A C    1 
ATOM   3125 O  O    . THR   A 1 146 ? 23.722 -17.922 1.906   1.00 12.28 ?  146 THR   A O    1 
ATOM   3126 C  CB   . THR   A 1 146 ? 22.408 -16.323 -0.654  1.00 11.51 ?  146 THR   A CB   1 
ATOM   3127 O  OG1  . THR   A 1 146 ? 21.881 -16.489 -1.971  1.00 12.16 ?  146 THR   A OG1  1 
ATOM   3128 C  CG2  . THR   A 1 146 ? 23.907 -16.097 -0.750  1.00 11.93 ?  146 THR   A CG2  1 
ATOM   3129 H  H    . THR   A 1 146 ? 20.184 -17.201 0.534   1.00 14.27 ?  146 THR   A H    1 
ATOM   3130 H  HA   . THR   A 1 146 ? 22.549 -18.321 -0.217  1.00 13.57 ?  146 THR   A HA   1 
ATOM   3131 H  HB   . THR   A 1 146 ? 22.013 -15.539 -0.240  1.00 13.85 ?  146 THR   A HB   1 
ATOM   3132 H  HG1  . THR   A 1 146 ? 21.044 -16.559 -1.935  1.00 14.64 ?  146 THR   A HG1  1 
ATOM   3133 H  HG21 . THR   A 1 146 ? 24.097 -15.422 -1.418  1.00 14.35 ?  146 THR   A HG21 1 
ATOM   3134 H  HG22 . THR   A 1 146 ? 24.255 -15.802 0.105   1.00 14.35 ?  146 THR   A HG22 1 
ATOM   3135 H  HG23 . THR   A 1 146 ? 24.347 -16.924 -1.004  1.00 14.35 ?  146 THR   A HG23 1 
ATOM   3136 N  N    . VAL   A 1 147 ? 21.960 -16.608 2.421   1.00 11.22 ?  147 VAL   A N    1 
ATOM   3137 C  CA   . VAL   A 1 147 ? 22.444 -16.312 3.760   1.00 11.31 ?  147 VAL   A CA   1 
ATOM   3138 C  C    . VAL   A 1 147 ? 22.125 -17.485 4.674   1.00 11.46 ?  147 VAL   A C    1 
ATOM   3139 O  O    . VAL   A 1 147 ? 20.983 -17.961 4.718   1.00 12.22 ?  147 VAL   A O    1 
ATOM   3140 C  CB   . VAL   A 1 147 ? 21.820 -15.009 4.278   1.00 11.45 ?  147 VAL   A CB   1 
ATOM   3141 C  CG1  . VAL   A 1 147 ? 22.345 -14.692 5.658   1.00 12.54 ?  147 VAL   A CG1  1 
ATOM   3142 C  CG2  . VAL   A 1 147 ? 22.077 -13.861 3.310   1.00 11.21 ?  147 VAL   A CG2  1 
ATOM   3143 H  H    . VAL   A 1 147 ? 21.205 -16.237 2.232   1.00 13.51 ?  147 VAL   A H    1 
ATOM   3144 H  HA   . VAL   A 1 147 ? 23.407 -16.199 3.730   1.00 13.61 ?  147 VAL   A HA   1 
ATOM   3145 H  HB   . VAL   A 1 147 ? 20.860 -15.129 4.346   1.00 13.78 ?  147 VAL   A HB   1 
ATOM   3146 H  HG11 . VAL   A 1 147 ? 22.089 -13.791 5.893   1.00 15.09 ?  147 VAL   A HG11 1 
ATOM   3147 H  HG12 . VAL   A 1 147 ? 21.959 -15.322 6.293   1.00 15.09 ?  147 VAL   A HG12 1 
ATOM   3148 H  HG13 . VAL   A 1 147 ? 23.310 -14.778 5.655   1.00 15.09 ?  147 VAL   A HG13 1 
ATOM   3149 H  HG21 . VAL   A 1 147 ? 21.744 -13.039 3.705   1.00 13.49 ?  147 VAL   A HG21 1 
ATOM   3150 H  HG22 . VAL   A 1 147 ? 23.029 -13.790 3.152   1.00 13.49 ?  147 VAL   A HG22 1 
ATOM   3151 H  HG23 . VAL   A 1 147 ? 21.612 -14.039 2.479   1.00 13.49 ?  147 VAL   A HG23 1 
ATOM   3152 N  N    . ARG   A 1 148 ? 23.147 -17.954 5.393   1.00 11.75 ?  148 ARG   A N    1 
ATOM   3153 C  CA   . ARG   A 1 148 ? 23.013 -19.028 6.361   1.00 11.71 ?  148 ARG   A CA   1 
ATOM   3154 C  C    . ARG   A 1 148 ? 23.129 -18.552 7.798   1.00 12.26 ?  148 ARG   A C    1 
ATOM   3155 O  O    . ARG   A 1 148 ? 22.717 -19.278 8.711   1.00 13.80 ?  148 ARG   A O    1 
ATOM   3156 C  CB   . ARG   A 1 148 ? 24.055 -20.123 6.087   1.00 12.56 ?  148 ARG   A CB   1 
ATOM   3157 C  CG   . ARG   A 1 148 ? 23.884 -20.769 4.726   1.00 13.83 ?  148 ARG   A CG   1 
ATOM   3158 C  CD   . ARG   A 1 148 ? 24.976 -21.801 4.432   1.00 14.83 ?  148 ARG   A CD   1 
ATOM   3159 N  NE   . ARG   A 1 148 ? 26.315 -21.220 4.449   1.00 14.74 ?  148 ARG   A NE   1 
ATOM   3160 C  CZ   . ARG   A 1 148 ? 26.822 -20.489 3.466   1.00 13.99 ?  148 ARG   A CZ   1 
ATOM   3161 N  NH1  . ARG   A 1 148 ? 26.141 -20.258 2.354   1.00 14.29 ?  148 ARG   A NH1  1 
ATOM   3162 N  NH2  . ARG   A 1 148 ? 28.042 -19.965 3.606   1.00 14.27 ?  148 ARG   A NH2  1 
ATOM   3163 H  H    . ARG   A 1 148 ? 23.953 -17.652 5.320   1.00 14.14 ?  148 ARG   A H    1 
ATOM   3164 H  HA   . ARG   A 1 148 ? 22.141 -19.426 6.254   1.00 14.10 ?  148 ARG   A HA   1 
ATOM   3165 H  HB2  . ARG   A 1 148 ? 24.943 -19.744 6.126   1.00 15.11 ?  148 ARG   A HB2  1 
ATOM   3166 H  HB3  . ARG   A 1 148 ? 23.960 -20.823 6.755   1.00 15.11 ?  148 ARG   A HB3  1 
ATOM   3167 H  HG2  . ARG   A 1 148 ? 23.024 -21.214 4.692   1.00 16.64 ?  148 ARG   A HG2  1 
ATOM   3168 H  HG3  . ARG   A 1 148 ? 23.929 -20.078 4.045   1.00 16.64 ?  148 ARG   A HG3  1 
ATOM   3169 H  HD2  . ARG   A 1 148 ? 24.942 -22.499 5.105   1.00 17.84 ?  148 ARG   A HD2  1 
ATOM   3170 H  HD3  . ARG   A 1 148 ? 24.821 -22.184 3.551   1.00 17.84 ?  148 ARG   A HD3  1 
ATOM   3171 H  HE   . ARG   A 1 148 ? 26.804 -21.360 5.137   1.00 17.73 ?  148 ARG   A HE   1 
ATOM   3172 H  HH11 . ARG   A 1 148 ? 25.352 -20.578 2.250   1.00 17.19 ?  148 ARG   A HH11 1 
ATOM   3173 H  HH12 . ARG   A 1 148 ? 26.489 -19.771 1.729   1.00 17.19 ?  148 ARG   A HH12 1 
ATOM   3174 H  HH21 . ARG   A 1 148 ? 28.488 -20.105 4.326   1.00 17.17 ?  148 ARG   A HH21 1 
ATOM   3175 H  HH22 . ARG   A 1 148 ? 28.380 -19.484 2.977   1.00 17.17 ?  148 ARG   A HH22 1 
ATOM   3176 N  N    . THR   A 1 149 ? 23.679 -17.360 8.013   1.00 12.35 ?  149 THR   A N    1 
ATOM   3177 C  CA   . THR   A 1 149 ? 23.759 -16.759 9.329   1.00 12.63 ?  149 THR   A CA   1 
ATOM   3178 C  C    . THR   A 1 149 ? 22.432 -16.064 9.637   1.00 12.20 ?  149 THR   A C    1 
ATOM   3179 O  O    . THR   A 1 149 ? 21.498 -16.060 8.824   1.00 12.74 ?  149 THR   A O    1 
ATOM   3180 C  CB   . THR   A 1 149 ? 24.961 -15.821 9.387   1.00 12.71 ?  149 THR   A CB   1 
ATOM   3181 O  OG1  . THR   A 1 149 ? 24.832 -14.885 8.315   1.00 12.65 ?  149 THR   A OG1  1 
ATOM   3182 C  CG2  . THR   A 1 149 ? 26.274 -16.617 9.265   1.00 13.64 ?  149 THR   A CG2  1 
ATOM   3183 H  H    . THR   A 1 149 ? 24.023 -16.869 7.389   1.00 14.86 ?  149 THR   A H    1 
ATOM   3184 H  HA   . THR   A 1 149 ? 23.886 -17.462 9.985   1.00 15.20 ?  149 THR   A HA   1 
ATOM   3185 H  HB   . THR   A 1 149 ? 24.953 -15.352 10.231  1.00 15.29 ?  149 THR   A HB   1 
ATOM   3186 H  HG1  . THR   A 1 149 ? 25.483 -14.356 8.318   1.00 15.22 ?  149 THR   A HG1  1 
ATOM   3187 H  HG21 . THR   A 1 149 ? 27.032 -16.017 9.316   1.00 16.41 ?  149 THR   A HG21 1 
ATOM   3188 H  HG22 . THR   A 1 149 ? 26.340 -17.268 9.985   1.00 16.41 ?  149 THR   A HG22 1 
ATOM   3189 H  HG23 . THR   A 1 149 ? 26.305 -17.091 8.417   1.00 16.41 ?  149 THR   A HG23 1 
ATOM   3190 N  N    . ASN   A 1 150 ? 22.307 -15.521 10.842  1.00 12.68 ?  150 ASN   A N    1 
ATOM   3191 C  CA   . ASN   A 1 150 ? 21.021 -15.007 11.314  1.00 12.75 ?  150 ASN   A CA   1 
ATOM   3192 C  C    . ASN   A 1 150 ? 20.840 -13.568 10.853  1.00 11.97 ?  150 ASN   A C    1 
ATOM   3193 O  O    . ASN   A 1 150 ? 21.593 -12.675 11.265  1.00 13.46 ?  150 ASN   A O    1 
ATOM   3194 C  CB   . ASN   A 1 150 ? 20.946 -15.111 12.832  1.00 15.32 ?  150 ASN   A CB   1 
ATOM   3195 C  CG   . ASN   A 1 150 ? 20.853 -16.540 13.298  1.00 19.55 ?  150 ASN   A CG   1 
ATOM   3196 O  OD1  . ASN   A 1 150 ? 20.246 -17.376 12.629  1.00 20.65 ?  150 ASN   A OD1  1 
ATOM   3197 N  ND2  . ASN   A 1 150 ? 21.472 -16.842 14.436  1.00 21.96 ?  150 ASN   A ND2  1 
ATOM   3198 H  H    . ASN   A 1 150 ? 22.949 -15.434 11.403  1.00 15.26 ?  150 ASN   A H    1 
ATOM   3199 H  HA   . ASN   A 1 150 ? 20.300 -15.542 10.941  1.00 15.34 ?  150 ASN   A HA   1 
ATOM   3200 H  HB2  . ASN   A 1 150 ? 21.744 -14.721 13.221  1.00 18.43 ?  150 ASN   A HB2  1 
ATOM   3201 H  HB3  . ASN   A 1 150 ? 20.156 -14.650 13.151  1.00 18.43 ?  150 ASN   A HB3  1 
ATOM   3202 H  HD21 . ASN   A 1 150 ? 21.456 -17.650 14.741  1.00 26.40 ?  150 ASN   A HD21 1 
ATOM   3203 H  HD22 . ASN   A 1 150 ? 21.887 -16.230 14.877  1.00 26.40 ?  150 ASN   A HD22 1 
ATOM   3204 N  N    . VAL   A 1 151 ? 19.850 -13.340 9.996   1.00 11.62 ?  151 VAL   A N    1 
ATOM   3205 C  CA   . VAL   A 1 151 ? 19.642 -12.036 9.388   1.00 11.85 ?  151 VAL   A CA   1 
ATOM   3206 C  C    . VAL   A 1 151 ? 18.253 -11.520 9.741   1.00 11.59 ?  151 VAL   A C    1 
ATOM   3207 O  O    . VAL   A 1 151 ? 17.246 -12.229 9.591   1.00 13.14 ?  151 VAL   A O    1 
ATOM   3208 C  CB   . VAL   A 1 151 ? 19.941 -12.039 7.873   1.00 12.95 ?  151 VAL   A CB   1 
ATOM   3209 C  CG1  . VAL   A 1 151 ? 19.115 -13.062 7.122   1.00 13.87 ?  151 VAL   A CG1  1 
ATOM   3210 C  CG2  . VAL   A 1 151 ? 19.767 -10.637 7.286   1.00 13.37 ?  151 VAL   A CG2  1 
ATOM   3211 H  H    . VAL   A 1 151 ? 19.286 -13.935 9.743   1.00 13.99 ?  151 VAL   A H    1 
ATOM   3212 H  HA   . VAL   A 1 151 ? 20.279 -11.419 9.778   1.00 14.26 ?  151 VAL   A HA   1 
ATOM   3213 H  HB   . VAL   A 1 151 ? 20.875 -12.283 7.741   1.00 15.58 ?  151 VAL   A HB   1 
ATOM   3214 H  HG11 . VAL   A 1 151 ? 19.324 -13.019 6.174   1.00 16.69 ?  151 VAL   A HG11 1 
ATOM   3215 H  HG12 . VAL   A 1 151 ? 19.323 -13.951 7.460   1.00 16.69 ?  151 VAL   A HG12 1 
ATOM   3216 H  HG13 . VAL   A 1 151 ? 18.172 -12.875 7.258   1.00 16.69 ?  151 VAL   A HG13 1 
ATOM   3217 H  HG21 . VAL   A 1 151 ? 20.088 -10.637 6.367   1.00 16.08 ?  151 VAL   A HG21 1 
ATOM   3218 H  HG22 . VAL   A 1 151 ? 18.828 -10.402 7.305   1.00 16.08 ?  151 VAL   A HG22 1 
ATOM   3219 H  HG23 . VAL   A 1 151 ? 20.282 -10.010 7.814   1.00 16.08 ?  151 VAL   A HG23 1 
ATOM   3220 N  N    . TYR   A 1 152 ? 18.233 -10.272 10.218  1.00 11.94 ?  152 TYR   A N    1 
ATOM   3221 C  CA   . TYR   A 1 152 ? 17.038 -9.537  10.604  1.00 11.71 ?  152 TYR   A CA   1 
ATOM   3222 C  C    . TYR   A 1 152 ? 16.843 -8.438  9.569   1.00 11.16 ?  152 TYR   A C    1 
ATOM   3223 O  O    . TYR   A 1 152 ? 17.617 -7.474  9.520   1.00 11.49 ?  152 TYR   A O    1 
ATOM   3224 C  CB   . TYR   A 1 152 ? 17.220 -8.990  12.017  1.00 12.48 ?  152 TYR   A CB   1 
ATOM   3225 C  CG   . TYR   A 1 152 ? 17.163 -10.115 13.018  1.00 13.01 ?  152 TYR   A CG   1 
ATOM   3226 C  CD1  . TYR   A 1 152 ? 18.285 -10.883 13.294  1.00 14.26 ?  152 TYR   A CD1  1 
ATOM   3227 C  CD2  . TYR   A 1 152 ? 15.974 -10.451 13.646  1.00 13.29 ?  152 TYR   A CD2  1 
ATOM   3228 C  CE1  . TYR   A 1 152 ? 18.231 -11.941 14.178  1.00 15.56 ?  152 TYR   A CE1  1 
ATOM   3229 C  CE2  . TYR   A 1 152 ? 15.907 -11.517 14.539  1.00 15.07 ?  152 TYR   A CE2  1 
ATOM   3230 C  CZ   . TYR   A 1 152 ? 17.043 -12.255 14.801  1.00 15.82 ?  152 TYR   A CZ   1 
ATOM   3231 O  OH   . TYR   A 1 152 ? 17.001 -13.319 15.682  1.00 18.28 ?  152 TYR   A OH   1 
ATOM   3232 H  H    . TYR   A 1 152 ? 18.954 -9.805  10.323  1.00 14.37 ?  152 TYR   A H    1 
ATOM   3233 H  HA   . TYR   A 1 152 ? 16.271 -10.126 10.591  1.00 14.10 ?  152 TYR   A HA   1 
ATOM   3234 H  HB2  . TYR   A 1 152 ? 18.089 -8.563  12.089  1.00 15.02 ?  152 TYR   A HB2  1 
ATOM   3235 H  HB3  . TYR   A 1 152 ? 16.514 -8.361  12.216  1.00 15.02 ?  152 TYR   A HB3  1 
ATOM   3236 H  HD1  . TYR   A 1 152 ? 19.087 -10.680 12.870  1.00 17.15 ?  152 TYR   A HD1  1 
ATOM   3237 H  HD2  . TYR   A 1 152 ? 15.203 -9.953  13.462  1.00 15.99 ?  152 TYR   A HD2  1 
ATOM   3238 H  HE1  . TYR   A 1 152 ? 18.994 -12.437 14.356  1.00 18.71 ?  152 TYR   A HE1  1 
ATOM   3239 H  HE2  . TYR   A 1 152 ? 15.101 -11.720 14.959  1.00 18.13 ?  152 TYR   A HE2  1 
ATOM   3240 H  HH   . TYR   A 1 152 ? 16.225 -13.394 15.999  1.00 21.98 ?  152 TYR   A HH   1 
ATOM   3241 N  N    A LEU   A 1 153 ? 15.849 -8.634  8.701   0.60 11.49 ?  153 LEU   A N    1 
ATOM   3242 N  N    B LEU   A 1 153 ? 15.795 -8.549  8.769   0.40 11.24 ?  153 LEU   A N    1 
ATOM   3243 C  CA   A LEU   A 1 153 ? 15.581 -7.764  7.562   0.60 11.61 ?  153 LEU   A CA   1 
ATOM   3244 C  CA   B LEU   A 1 153 ? 15.556 -7.604  7.690   0.40 11.04 ?  153 LEU   A CA   1 
ATOM   3245 C  C    A LEU   A 1 153 ? 14.575 -6.685  7.932   0.60 11.75 ?  153 LEU   A C    1 
ATOM   3246 C  C    B LEU   A 1 153 ? 14.591 -6.522  8.155   0.40 11.15 ?  153 LEU   A C    1 
ATOM   3247 O  O    A LEU   A 1 153 ? 13.487 -6.984  8.435   0.60 13.32 ?  153 LEU   A O    1 
ATOM   3248 O  O    B LEU   A 1 153 ? 13.464 -6.819  8.565   0.40 12.11 ?  153 LEU   A O    1 
ATOM   3249 C  CB   A LEU   A 1 153 ? 15.008 -8.587  6.406   0.60 11.51 ?  153 LEU   A CB   1 
ATOM   3250 C  CB   B LEU   A 1 153 ? 15.002 -8.325  6.466   0.40 11.23 ?  153 LEU   A CB   1 
ATOM   3251 C  CG   A LEU   A 1 153 ? 15.971 -9.545  5.709   0.60 11.51 ?  153 LEU   A CG   1 
ATOM   3252 C  CG   B LEU   A 1 153 ? 15.901 -9.410  5.873   0.40 11.67 ?  153 LEU   A CG   1 
ATOM   3253 C  CD1  A LEU   A 1 153 ? 15.201 -10.486 4.791   0.60 11.47 ?  153 LEU   A CD1  1 
ATOM   3254 C  CD1  B LEU   A 1 153 ? 15.147 -10.161 4.782   0.40 12.10 ?  153 LEU   A CD1  1 
ATOM   3255 C  CD2  A LEU   A 1 153 ? 17.001 -8.754  4.921   0.60 10.90 ?  153 LEU   A CD2  1 
ATOM   3256 C  CD2  B LEU   A 1 153 ? 17.205 -8.828  5.333   0.40 11.71 ?  153 LEU   A CD2  1 
ATOM   3257 H  H    A LEU   A 1 153 ? 15.299 -9.301  8.760   0.60 13.83 ?  153 LEU   A H    1 
ATOM   3258 H  H    B LEU   A 1 153 ? 15.192 -9.166  8.843   0.40 13.53 ?  153 LEU   A H    1 
ATOM   3259 H  HA   A LEU   A 1 153 ? 16.400 -7.354  7.274   0.60 13.97 ?  153 LEU   A HA   1 
ATOM   3260 H  HA   B LEU   A 1 153 ? 16.390 -7.180  7.456   0.40 13.29 ?  153 LEU   A HA   1 
ATOM   3261 H  HB2  A LEU   A 1 153 ? 14.265 -9.120  6.742   0.60 13.85 ?  153 LEU   A HB2  1 
ATOM   3262 H  HB2  B LEU   A 1 153 ? 14.165 -8.743  6.718   0.40 13.52 ?  153 LEU   A HB2  1 
ATOM   3263 H  HB3  A LEU   A 1 153 ? 14.675 -7.973  5.731   0.60 13.85 ?  153 LEU   A HB3  1 
ATOM   3264 H  HB3  B LEU   A 1 153 ? 14.844 -7.662  5.781   0.40 13.52 ?  153 LEU   A HB3  1 
ATOM   3265 H  HG   A LEU   A 1 153 ? 16.436 -10.078 6.377   0.60 13.86 ?  153 LEU   A HG   1 
ATOM   3266 H  HG   B LEU   A 1 153 ? 16.129 -10.043 6.572   0.40 14.05 ?  153 LEU   A HG   1 
ATOM   3267 H  HD11 A LEU   A 1 153 ? 15.800 -11.183 4.479   0.60 13.81 ?  153 LEU   A HD11 1 
ATOM   3268 H  HD11 B LEU   A 1 153 ? 15.720 -10.857 4.425   0.40 14.56 ?  153 LEU   A HD11 1 
ATOM   3269 H  HD12 A LEU   A 1 153 ? 14.467 -10.877 5.283   0.60 13.81 ?  153 LEU   A HD12 1 
ATOM   3270 H  HD12 B LEU   A 1 153 ? 14.347 -10.552 5.164   0.40 14.56 ?  153 LEU   A HD12 1 
ATOM   3271 H  HD13 A LEU   A 1 153 ? 14.864 -9.978  4.036   0.60 13.81 ?  153 LEU   A HD13 1 
ATOM   3272 H  HD13 B LEU   A 1 153 ? 14.906 -9.537  4.078   0.40 14.56 ?  153 LEU   A HD13 1 
ATOM   3273 H  HD21 A LEU   A 1 153 ? 17.562 -9.370  4.432   0.60 13.12 ?  153 LEU   A HD21 1 
ATOM   3274 H  HD21 B LEU   A 1 153 ? 17.720 -9.539  4.922   0.40 14.10 ?  153 LEU   A HD21 1 
ATOM   3275 H  HD22 A LEU   A 1 153 ? 16.535 -8.165  4.308   0.60 13.12 ?  153 LEU   A HD22 1 
ATOM   3276 H  HD22 B LEU   A 1 153 ? 16.998 -8.145  4.677   0.40 14.10 ?  153 LEU   A HD22 1 
ATOM   3277 H  HD23 A LEU   A 1 153 ? 17.535 -8.234  5.540   0.60 13.12 ?  153 LEU   A HD23 1 
ATOM   3278 H  HD23 B LEU   A 1 153 ? 17.708 -8.438  6.067   0.40 14.10 ?  153 LEU   A HD23 1 
ATOM   3279 N  N    A ALA   A 1 154 ? 14.926 -5.437  7.640   0.60 10.64 ?  154 ALA   A N    1 
ATOM   3280 N  N    B ALA   A 1 154 ? 15.042 -5.272  8.098   0.40 9.73  ?  154 ALA   A N    1 
ATOM   3281 C  CA   A ALA   A 1 154 ? 14.060 -4.288  7.862   0.60 10.60 ?  154 ALA   A CA   1 
ATOM   3282 C  CA   B ALA   A 1 154 ? 14.196 -4.114  8.341   0.40 10.14 ?  154 ALA   A CA   1 
ATOM   3283 C  C    A ALA   A 1 154 ? 13.599 -3.764  6.510   0.60 9.88  ?  154 ALA   A C    1 
ATOM   3284 C  C    B ALA   A 1 154 ? 13.699 -3.607  6.995   0.40 10.01 ?  154 ALA   A C    1 
ATOM   3285 O  O    A ALA   A 1 154 ? 14.422 -3.362  5.680   0.60 11.03 ?  154 ALA   A O    1 
ATOM   3286 O  O    B ALA   A 1 154 ? 14.501 -3.205  6.145   0.40 9.68  ?  154 ALA   A O    1 
ATOM   3287 C  CB   A ALA   A 1 154 ? 14.805 -3.196  8.624   0.60 11.20 ?  154 ALA   A CB   1 
ATOM   3288 C  CB   B ALA   A 1 154 ? 14.974 -3.023  9.077   0.40 10.55 ?  154 ALA   A CB   1 
ATOM   3289 H  H    A ALA   A 1 154 ? 15.678 -5.235  7.281   0.60 12.81 ?  154 ALA   A H    1 
ATOM   3290 H  H    B ALA   A 1 154 ? 15.859 -5.060  7.915   0.40 11.72 ?  154 ALA   A H    1 
ATOM   3291 H  HA   A ALA   A 1 154 ? 13.280 -4.559  8.376   0.60 12.76 ?  154 ALA   A HA   1 
ATOM   3292 H  HA   B ALA   A 1 154 ? 13.430 -4.363  8.876   0.40 12.21 ?  154 ALA   A HA   1 
ATOM   3293 H  HB1  A ALA   A 1 154 ? 14.208 -2.446  8.759   0.60 13.48 ?  154 ALA   A HB1  1 
ATOM   3294 H  HB1  B ALA   A 1 154 ? 14.390 -2.264  9.232   0.40 12.70 ?  154 ALA   A HB1  1 
ATOM   3295 H  HB2  A ALA   A 1 154 ? 15.095 -3.550  9.478   0.60 13.48 ?  154 ALA   A HB2  1 
ATOM   3296 H  HB2  B ALA   A 1 154 ? 15.285 -3.381  9.923   0.40 12.70 ?  154 ALA   A HB2  1 
ATOM   3297 H  HB3  A ALA   A 1 154 ? 15.574 -2.920  8.100   0.60 13.48 ?  154 ALA   A HB3  1 
ATOM   3298 H  HB3  B ALA   A 1 154 ? 15.731 -2.753  8.534   0.40 12.70 ?  154 ALA   A HB3  1 
ATOM   3299 N  N    A VAL   A 1 155 ? 12.287 -3.781  6.294   0.30 8.08  ?  155 VAL   A N    1 
ATOM   3300 N  N    B VAL   A 1 155 ? 12.384 -3.641  6.798   0.40 10.18 ?  155 VAL   A N    1 
ATOM   3301 C  CA   A VAL   A 1 155 ? 11.653 -3.287  5.077   0.30 10.61 ?  155 VAL   A CA   1 
ATOM   3302 C  CA   B VAL   A 1 155 ? 11.751 -3.211  5.558   0.40 11.51 ?  155 VAL   A CA   1 
ATOM   3303 C  CA   T VAL   A 1 155 ? 11.650 -3.381  5.077   0.30 13.22 ?  155 VAL   A CA   1 
ATOM   3304 C  C    A VAL   A 1 155 ? 10.907 -2.009  5.449   0.30 12.01 ?  155 VAL   A C    1 
ATOM   3305 C  C    B VAL   A 1 155 ? 11.138 -1.839  5.790   0.40 12.86 ?  155 VAL   A C    1 
ATOM   3306 C  C    T VAL   A 1 155 ? 10.940 -2.052  5.348   0.30 13.05 ?  155 VAL   A C    1 
ATOM   3307 O  O    A VAL   A 1 155 ? 9.918  -2.053  6.189   0.30 12.71 ?  155 VAL   A O    1 
ATOM   3308 O  O    B VAL   A 1 155 ? 10.299 -1.668  6.683   0.40 12.33 ?  155 VAL   A O    1 
ATOM   3309 O  O    T VAL   A 1 155 ? 9.991  -1.986  6.125   0.30 13.11 ?  155 VAL   A O    1 
ATOM   3310 C  CB   A VAL   A 1 155 ? 10.714 -4.344  4.478   0.30 11.22 ?  155 VAL   A CB   1 
ATOM   3311 C  CB   B VAL   A 1 155 ? 10.691 -4.219  5.092   0.40 11.43 ?  155 VAL   A CB   1 
ATOM   3312 C  CB   T VAL   A 1 155 ? 10.694 -4.471  4.551   0.30 13.14 ?  155 VAL   A CB   1 
ATOM   3313 C  CG1  A VAL   A 1 155 ? 10.097 -3.854  3.179   0.30 11.64 ?  155 VAL   A CG1  1 
ATOM   3314 C  CG1  B VAL   A 1 155 ? 9.932  -3.669  3.888   0.40 11.69 ?  155 VAL   A CG1  1 
ATOM   3315 C  CG1  T VAL   A 1 155 ? 9.990  -4.000  3.292   0.30 13.15 ?  155 VAL   A CG1  1 
ATOM   3316 C  CG2  A VAL   A 1 155 ? 11.470 -5.650  4.250   0.30 12.25 ?  155 VAL   A CG2  1 
ATOM   3317 C  CG2  B VAL   A 1 155 ? 11.345 -5.550  4.763   0.40 12.34 ?  155 VAL   A CG2  1 
ATOM   3318 C  CG2  T VAL   A 1 155 ? 11.461 -5.762  4.278   0.30 13.78 ?  155 VAL   A CG2  1 
ATOM   3319 H  H    A VAL   A 1 155 ? 11.719 -4.102  6.859   0.30 9.73  ?  155 VAL   A H    1 
ATOM   3320 H  H    B VAL   A 1 155 ? 11.818 -3.899  7.390   0.40 12.26 ?  155 VAL   A H    1 
ATOM   3321 H  HA   A VAL   A 1 155 ? 12.328 -3.072  4.419   0.30 12.77 ?  155 VAL   A HA   1 
ATOM   3322 H  HA   B VAL   A 1 155 ? 12.418 -3.125  4.861   0.40 13.86 ?  155 VAL   A HA   1 
ATOM   3323 H  HB   A VAL   A 1 155 ? 9.991  -4.522  5.103   0.30 13.50 ?  155 VAL   A HB   1 
ATOM   3324 H  HB   B VAL   A 1 155 ? 10.053 -4.363  5.810   0.40 13.76 ?  155 VAL   A HB   1 
ATOM   3325 H  HB   T VAL   A 1 155 ? 10.020 -4.660  5.224   0.30 15.81 ?  155 VAL   A HB   1 
ATOM   3326 H  HG11 A VAL   A 1 155 ? 9.585  -4.579  2.779   0.30 14.01 ?  155 VAL   A HG11 1 
ATOM   3327 H  HG11 B VAL   A 1 155 ? 9.455  -4.394  3.457   0.40 14.07 ?  155 VAL   A HG11 1 
ATOM   3328 H  HG11 T VAL   A 1 155 ? 9.516  -4.748  2.896   0.30 15.82 ?  155 VAL   A HG11 1 
ATOM   3329 H  HG12 A VAL   A 1 155 ? 9.509  -3.106  3.367   0.30 14.01 ?  155 VAL   A HG12 1 
ATOM   3330 H  HG12 B VAL   A 1 155 ? 9.299  -2.995  4.188   0.40 14.07 ?  155 VAL   A HG12 1 
ATOM   3331 H  HG12 T VAL   A 1 155 ? 9.362  -3.298  3.523   0.30 15.82 ?  155 VAL   A HG12 1 
ATOM   3332 H  HG13 A VAL   A 1 155 ? 10.804 -3.581  2.577   0.30 14.01 ?  155 VAL   A HG13 1 
ATOM   3333 H  HG13 B VAL   A 1 155 ? 10.565 -3.275  3.268   0.40 14.07 ?  155 VAL   A HG13 1 
ATOM   3334 H  HG13 T VAL   A 1 155 ? 10.652 -3.662  2.669   0.30 15.82 ?  155 VAL   A HG13 1 
ATOM   3335 H  HG21 A VAL   A 1 155 ? 10.896 -6.271  3.775   0.30 14.74 ?  155 VAL   A HG21 1 
ATOM   3336 H  HG21 B VAL   A 1 155 ? 10.702 -6.111  4.305   0.40 14.85 ?  155 VAL   A HG21 1 
ATOM   3337 H  HG21 T VAL   A 1 155 ? 10.843 -6.433  3.949   0.30 16.58 ?  155 VAL   A HG21 1 
ATOM   3338 H  HG22 A VAL   A 1 155 ? 12.265 -5.465  3.726   0.30 14.74 ?  155 VAL   A HG22 1 
ATOM   3339 H  HG22 B VAL   A 1 155 ? 12.112 -5.389  4.190   0.40 14.85 ?  155 VAL   A HG22 1 
ATOM   3340 H  HG22 T VAL   A 1 155 ? 12.144 -5.586  3.612   0.30 16.58 ?  155 VAL   A HG22 1 
ATOM   3341 H  HG23 A VAL   A 1 155 ? 11.721 -6.024  5.110   0.30 14.74 ?  155 VAL   A HG23 1 
ATOM   3342 H  HG23 B VAL   A 1 155 ? 11.632 -5.973  5.587   0.40 14.85 ?  155 VAL   A HG23 1 
ATOM   3343 H  HG23 T VAL   A 1 155 ? 11.872 -6.066  5.103   0.30 16.58 ?  155 VAL   A HG23 1 
ATOM   3344 N  N    A PHE   A 1 156 ? 11.379 -0.864  4.945   0.30 13.33 ?  156 PHE   A N    1 
ATOM   3345 N  N    B PHE   A 1 156 ? 11.546 -0.871  4.966   0.40 14.45 ?  156 PHE   A N    1 
ATOM   3346 N  N    T PHE   A 1 156 ? 11.418 -0.993  4.690   0.30 13.52 ?  156 PHE   A N    1 
ATOM   3347 C  CA   A PHE   A 1 156 ? 10.807 0.424   5.344   0.30 14.60 ?  156 PHE   A CA   1 
ATOM   3348 C  CA   B PHE   A 1 156 ? 11.151 0.518   5.174   0.40 15.97 ?  156 PHE   A CA   1 
ATOM   3349 C  CA   T PHE   A 1 156 ? 10.947 0.361   4.980   0.30 13.84 ?  156 PHE   A CA   1 
ATOM   3350 C  C    A PHE   A 1 156 ? 9.352  0.565   4.903   0.30 14.64 ?  156 PHE   A C    1 
ATOM   3351 C  C    B PHE   A 1 156 ? 9.648  0.697   5.019   0.40 17.60 ?  156 PHE   A C    1 
ATOM   3352 C  C    T PHE   A 1 156 ? 9.499  0.567   4.549   0.30 13.70 ?  156 PHE   A C    1 
ATOM   3353 O  O    A PHE   A 1 156 ? 8.528  1.126   5.636   0.30 15.26 ?  156 PHE   A O    1 
ATOM   3354 O  O    B PHE   A 1 156 ? 8.973  1.217   5.917   0.40 17.72 ?  156 PHE   A O    1 
ATOM   3355 O  O    T PHE   A 1 156 ? 8.742  1.278   5.221   0.30 14.27 ?  156 PHE   A O    1 
ATOM   3356 C  CB   A PHE   A 1 156 ? 11.662 1.564   4.778   0.30 15.77 ?  156 PHE   A CB   1 
ATOM   3357 C  CB   B PHE   A 1 156 ? 11.894 1.399   4.169   0.40 14.84 ?  156 PHE   A CB   1 
ATOM   3358 C  CB   T PHE   A 1 156 ? 11.863 1.367   4.279   0.30 14.17 ?  156 PHE   A CB   1 
ATOM   3359 C  CG   A PHE   A 1 156 ? 11.159 2.950   5.119   0.30 16.80 ?  156 PHE   A CG   1 
ATOM   3360 C  CG   B PHE   A 1 156 ? 11.595 2.861   4.313   0.40 14.14 ?  156 PHE   A CG   1 
ATOM   3361 C  CG   T PHE   A 1 156 ? 11.509 2.820   4.523   0.30 14.88 ?  156 PHE   A CG   1 
ATOM   3362 C  CD1  A PHE   A 1 156 ? 11.129 3.389   6.432   0.30 17.20 ?  156 PHE   A CD1  1 
ATOM   3363 C  CD1  B PHE   A 1 156 ? 12.131 3.579   5.368   0.40 14.35 ?  156 PHE   A CD1  1 
ATOM   3364 C  CD1  T PHE   A 1 156 ? 11.879 3.457   5.702   0.30 15.49 ?  156 PHE   A CD1  1 
ATOM   3365 C  CD2  A PHE   A 1 156 ? 10.748 3.823   4.120   0.30 17.45 ?  156 PHE   A CD2  1 
ATOM   3366 C  CD2  B PHE   A 1 156 ? 10.792 3.519   3.396   0.40 14.62 ?  156 PHE   A CD2  1 
ATOM   3367 C  CD2  T PHE   A 1 156 ? 10.847 3.560   3.554   0.30 15.83 ?  156 PHE   A CD2  1 
ATOM   3368 C  CE1  A PHE   A 1 156 ? 10.678 4.663   6.745   0.30 17.68 ?  156 PHE   A CE1  1 
ATOM   3369 C  CE1  B PHE   A 1 156 ? 11.868 4.925   5.517   0.40 14.65 ?  156 PHE   A CE1  1 
ATOM   3370 C  CE1  T PHE   A 1 156 ? 11.572 4.795   5.918   0.30 15.92 ?  156 PHE   A CE1  1 
ATOM   3371 C  CE2  A PHE   A 1 156 ? 10.295 5.096   4.427   0.30 17.88 ?  156 PHE   A CE2  1 
ATOM   3372 C  CE2  B PHE   A 1 156 ? 10.525 4.868   3.537   0.40 15.22 ?  156 PHE   A CE2  1 
ATOM   3373 C  CE2  T PHE   A 1 156 ? 10.537 4.896   3.765   0.30 16.39 ?  156 PHE   A CE2  1 
ATOM   3374 C  CZ   A PHE   A 1 156 ? 10.265 5.517   5.740   0.30 17.98 ?  156 PHE   A CZ   1 
ATOM   3375 C  CZ   B PHE   A 1 156 ? 11.064 5.572   4.600   0.40 15.14 ?  156 PHE   A CZ   1 
ATOM   3376 C  CZ   T PHE   A 1 156 ? 10.902 5.514   4.948   0.30 16.29 ?  156 PHE   A CZ   1 
ATOM   3377 H  H    A PHE   A 1 156 ? 12.026 -0.809  4.386   0.30 16.04 ?  156 PHE   A H    1 
ATOM   3378 H  H    B PHE   A 1 156 ? 12.046 -0.993  4.278   0.40 17.39 ?  156 PHE   A H    1 
ATOM   3379 H  H    T PHE   A 1 156 ? 12.022 -1.040  4.086   0.30 16.27 ?  156 PHE   A H    1 
ATOM   3380 H  HA   A PHE   A 1 156 ? 10.832 0.492   6.311   0.30 17.56 ?  156 PHE   A HA   1 
ATOM   3381 H  HA   B PHE   A 1 156 ? 11.410 0.799   6.065   0.40 19.20 ?  156 PHE   A HA   1 
ATOM   3382 H  HA   T PHE   A 1 156 ? 11.003 0.513   5.937   0.30 16.65 ?  156 PHE   A HA   1 
ATOM   3383 H  HB2  A PHE   A 1 156 ? 12.563 1.486   5.134   0.30 18.97 ?  156 PHE   A HB2  1 
ATOM   3384 H  HB2  B PHE   A 1 156 ? 12.842 1.287   4.315   0.40 17.85 ?  156 PHE   A HB2  1 
ATOM   3385 H  HB2  T PHE   A 1 156 ? 12.769 1.229   4.593   0.30 17.04 ?  156 PHE   A HB2  1 
ATOM   3386 H  HB3  A PHE   A 1 156 ? 11.685 1.491   3.813   0.30 18.97 ?  156 PHE   A HB3  1 
ATOM   3387 H  HB3  B PHE   A 1 156 ? 11.665 1.126   3.266   0.40 17.85 ?  156 PHE   A HB3  1 
ATOM   3388 H  HB3  T PHE   A 1 156 ? 11.818 1.211   3.324   0.30 17.04 ?  156 PHE   A HB3  1 
ATOM   3389 H  HD1  A PHE   A 1 156 ? 11.406 2.820   7.114   0.30 20.68 ?  156 PHE   A HD1  1 
ATOM   3390 H  HD1  B PHE   A 1 156 ? 12.676 3.140   5.987   0.40 17.26 ?  156 PHE   A HD1  1 
ATOM   3391 H  HD1  T PHE   A 1 156 ? 12.329 2.980   6.362   0.30 18.63 ?  156 PHE   A HD1  1 
ATOM   3392 H  HD2  A PHE   A 1 156 ? 10.769 3.545   3.233   0.30 20.98 ?  156 PHE   A HD2  1 
ATOM   3393 H  HD2  B PHE   A 1 156 ? 10.430 3.048   2.681   0.40 17.59 ?  156 PHE   A HD2  1 
ATOM   3394 H  HD2  T PHE   A 1 156 ? 10.598 3.152   2.759   0.30 19.04 ?  156 PHE   A HD2  1 
ATOM   3395 H  HE1  A PHE   A 1 156 ? 10.658 4.943   7.633   0.30 21.26 ?  156 PHE   A HE1  1 
ATOM   3396 H  HE1  B PHE   A 1 156 ? 12.232 5.391   6.235   0.40 17.62 ?  156 PHE   A HE1  1 
ATOM   3397 H  HE1  T PHE   A 1 156 ? 11.818 5.208   6.716   0.30 19.15 ?  156 PHE   A HE1  1 
ATOM   3398 H  HE2  A PHE   A 1 156 ? 10.021 5.669   3.747   0.30 21.49 ?  156 PHE   A HE2  1 
ATOM   3399 H  HE2  B PHE   A 1 156 ? 9.981  5.301   2.923   0.40 18.30 ?  156 PHE   A HE2  1 
ATOM   3400 H  HE2  T PHE   A 1 156 ? 10.086 5.380   3.110   0.30 19.71 ?  156 PHE   A HE2  1 
ATOM   3401 H  HZ   A PHE   A 1 156 ? 9.963  6.372   5.951   0.30 21.62 ?  156 PHE   A HZ   1 
ATOM   3402 H  HZ   B PHE   A 1 156 ? 10.883 6.476   4.702   0.40 18.21 ?  156 PHE   A HZ   1 
ATOM   3403 H  HZ   T PHE   A 1 156 ? 10.694 6.412   5.091   0.30 19.59 ?  156 PHE   A HZ   1 
ATOM   3404 N  N    A ASP   A 1 157 ? 9.015  0.064   3.719   0.30 14.40 ?  157 ASP   A N    1 
ATOM   3405 N  N    B ASP   A 1 157 ? 9.108  0.278   3.881   0.40 18.71 ?  157 ASP   A N    1 
ATOM   3406 N  N    T ASP   A 1 157 ? 9.095  -0.030  3.433   0.30 14.11 ?  157 ASP   A N    1 
ATOM   3407 C  CA   A ASP   A 1 157 ? 7.696  0.290   3.134   0.30 14.76 ?  157 ASP   A CA   1 
ATOM   3408 C  CA   B ASP   A 1 157 ? 7.731  0.584   3.517   0.40 20.38 ?  157 ASP   A CA   1 
ATOM   3409 C  CA   T ASP   A 1 157 ? 7.780  0.225   2.858   0.30 14.90 ?  157 ASP   A CA   1 
ATOM   3410 C  C    A ASP   A 1 157 ? 6.718  -0.776  3.621   0.30 14.76 ?  157 ASP   A C    1 
ATOM   3411 C  C    B ASP   A 1 157 ? 6.793  -0.438  4.147   0.40 20.98 ?  157 ASP   A C    1 
ATOM   3412 C  C    T ASP   A 1 157 ? 6.765  -0.769  3.412   0.30 15.28 ?  157 ASP   A C    1 
ATOM   3413 O  O    A ASP   A 1 157 ? 6.944  -1.971  3.412   0.30 14.13 ?  157 ASP   A O    1 
ATOM   3414 O  O    B ASP   A 1 157 ? 6.946  -1.645  3.931   0.40 20.69 ?  157 ASP   A O    1 
ATOM   3415 O  O    T ASP   A 1 157 ? 6.894  -1.977  3.192   0.30 14.92 ?  157 ASP   A O    1 
ATOM   3416 C  CB   A ASP   A 1 157 ? 7.779  0.284   1.608   0.30 15.02 ?  157 ASP   A CB   1 
ATOM   3417 C  CB   B ASP   A 1 157 ? 7.596  0.558   1.997   0.40 21.52 ?  157 ASP   A CB   1 
ATOM   3418 C  CB   T ASP   A 1 157 ? 7.856  0.118   1.338   0.30 15.63 ?  157 ASP   A CB   1 
ATOM   3419 C  CG   A ASP   A 1 157 ? 6.469  0.698   0.951   0.30 15.33 ?  157 ASP   A CG   1 
ATOM   3420 C  CG   B ASP   A 1 157 ? 6.249  1.052   1.522   0.40 22.57 ?  157 ASP   A CG   1 
ATOM   3421 C  CG   T ASP   A 1 157 ? 6.692  0.786   0.651   0.30 16.13 ?  157 ASP   A CG   1 
ATOM   3422 O  OD1  A ASP   A 1 157 ? 6.042  1.857   1.141   0.30 15.30 ?  157 ASP   A OD1  1 
ATOM   3423 O  OD1  B ASP   A 1 157 ? 5.230  0.469   1.937   0.40 22.92 ?  157 ASP   A OD1  1 
ATOM   3424 O  OD1  T ASP   A 1 157 ? 5.596  0.190   0.651   0.30 16.25 ?  157 ASP   A OD1  1 
ATOM   3425 O  OD2  A ASP   A 1 157 ? 5.861  -0.143  0.249   0.30 15.50 -1 157 ASP   A OD2  1 
ATOM   3426 O  OD2  B ASP   A 1 157 ? 6.209  2.025   0.740   0.40 22.99 -1 157 ASP   A OD2  1 
ATOM   3427 O  OD2  T ASP   A 1 157 ? 6.869  1.909   0.131   0.30 16.43 -1 157 ASP   A OD2  1 
ATOM   3428 H  H    A ASP   A 1 157 ? 9.536  -0.423  3.235   0.30 17.32 ?  157 ASP   A H    1 
ATOM   3429 H  H    B ASP   A 1 157 ? 9.529  -0.195  3.303   0.40 22.50 ?  157 ASP   A H    1 
ATOM   3430 H  H    T ASP   A 1 157 ? 9.570  -0.591  2.982   0.30 16.98 ?  157 ASP   A H    1 
ATOM   3431 H  HA   A ASP   A 1 157 ? 7.366  1.151   3.421   0.30 17.76 ?  157 ASP   A HA   1 
ATOM   3432 H  HA   B ASP   A 1 157 ? 7.498  1.472   3.834   0.40 24.50 ?  157 ASP   A HA   1 
ATOM   3433 H  HA   T ASP   A 1 157 ? 7.490  1.113   3.099   0.30 17.93 ?  157 ASP   A HA   1 
ATOM   3434 H  HB2  A ASP   A 1 157 ? 8.507  0.872   1.336   0.30 18.07 ?  157 ASP   A HB2  1 
ATOM   3435 H  HB2  B ASP   A 1 157 ? 8.276  1.117   1.605   0.40 25.87 ?  157 ASP   A HB2  1 
ATOM   3436 H  HB2  T ASP   A 1 157 ? 8.669  0.536   1.041   0.30 18.80 ?  157 ASP   A HB2  1 
ATOM   3437 H  HB3  A ASP   A 1 157 ? 7.950  -0.617  1.302   0.30 18.07 ?  157 ASP   A HB3  1 
ATOM   3438 H  HB3  B ASP   A 1 157 ? 7.704  -0.350  1.684   0.40 25.87 ?  157 ASP   A HB3  1 
ATOM   3439 H  HB3  T ASP   A 1 157 ? 7.851  -0.820  1.090   0.30 18.80 ?  157 ASP   A HB3  1 
ATOM   3440 N  N    A LYS   A 1 158 ? 5.625  -0.339  4.258   0.30 15.50 ?  158 LYS   A N    1 
ATOM   3441 N  N    B LYS   A 1 158 ? 5.814  0.044   4.917   0.40 22.00 ?  158 LYS   A N    1 
ATOM   3442 N  N    T LYS   A 1 158 ? 5.747  -0.259  4.118   0.30 16.56 ?  158 LYS   A N    1 
ATOM   3443 C  CA   A LYS   A 1 158 ? 4.660  -1.273  4.839   0.30 16.01 ?  158 LYS   A CA   1 
ATOM   3444 C  CA   B LYS   A 1 158 ? 4.857  -0.868  5.537   0.40 22.81 ?  158 LYS   A CA   1 
ATOM   3445 C  CA   T LYS   A 1 158 ? 4.759  -1.133  4.750   0.30 17.75 ?  158 LYS   A CA   1 
ATOM   3446 C  C    A LYS   A 1 158 ? 3.949  -2.087  3.760   0.30 15.66 ?  158 LYS   A C    1 
ATOM   3447 C  C    B LYS   A 1 158 ? 4.072  -1.638  4.483   0.40 22.11 ?  158 LYS   A C    1 
ATOM   3448 C  C    T LYS   A 1 158 ? 4.002  -1.950  3.709   0.30 17.84 ?  158 LYS   A C    1 
ATOM   3449 O  O    A LYS   A 1 158 ? 3.767  -3.302  3.905   0.30 15.63 ?  158 LYS   A O    1 
ATOM   3450 O  O    B LYS   A 1 158 ? 3.841  -2.844  4.629   0.40 22.37 ?  158 LYS   A O    1 
ATOM   3451 O  O    T LYS   A 1 158 ? 3.797  -3.157  3.880   0.30 17.73 ?  158 LYS   A O    1 
ATOM   3452 C  CB   A LYS   A 1 158 ? 3.663  -0.498  5.708   0.30 16.96 ?  158 LYS   A CB   1 
ATOM   3453 C  CB   B LYS   A 1 158 ? 3.918  -0.101  6.471   0.40 23.99 ?  158 LYS   A CB   1 
ATOM   3454 C  CB   T LYS   A 1 158 ? 3.796  -0.299  5.605   0.30 19.12 ?  158 LYS   A CB   1 
ATOM   3455 C  CG   A LYS   A 1 158 ? 2.455  -1.293  6.200   0.30 17.95 ?  158 LYS   A CG   1 
ATOM   3456 C  CG   B LYS   A 1 158 ? 2.661  -0.868  6.892   0.40 25.10 ?  158 LYS   A CG   1 
ATOM   3457 C  CG   T LYS   A 1 158 ? 2.577  -1.055  6.133   0.30 20.57 ?  158 LYS   A CG   1 
ATOM   3458 C  CD   A LYS   A 1 158 ? 2.840  -2.473  7.087   0.30 18.69 ?  158 LYS   A CD   1 
ATOM   3459 C  CD   B LYS   A 1 158 ? 2.973  -2.102  7.735   0.40 25.77 ?  158 LYS   A CD   1 
ATOM   3460 C  CD   T LYS   A 1 158 ? 2.962  -2.217  7.039   0.30 21.94 ?  158 LYS   A CD   1 
ATOM   3461 C  CE   A LYS   A 1 158 ? 1.598  -3.133  7.672   0.30 18.96 ?  158 LYS   A CE   1 
ATOM   3462 C  CE   B LYS   A 1 158 ? 1.690  -2.793  8.189   0.40 26.05 ?  158 LYS   A CE   1 
ATOM   3463 C  CE   T LYS   A 1 158 ? 1.727  -2.984  7.497   0.30 22.76 ?  158 LYS   A CE   1 
ATOM   3464 N  NZ   A LYS   A 1 158 ? 1.882  -4.456  8.293   0.30 19.08 ?  158 LYS   A NZ   1 
ATOM   3465 N  NZ   B LYS   A 1 158 ? 1.951  -4.092  8.870   0.40 26.30 ?  158 LYS   A NZ   1 
ATOM   3466 N  NZ   T LYS   A 1 158 ? 2.067  -4.196  8.294   0.30 23.20 ?  158 LYS   A NZ   1 
ATOM   3467 H  H    A LYS   A 1 158 ? 5.433  0.488   4.373   0.30 18.65 ?  158 LYS   A H    1 
ATOM   3468 H  H    B LYS   A 1 158 ? 5.689  0.877   5.086   0.40 26.45 ?  158 LYS   A H    1 
ATOM   3469 H  H    T LYS   A 1 158 ? 5.607  0.577   4.244   0.30 19.92 ?  158 LYS   A H    1 
ATOM   3470 H  HA   A LYS   A 1 158 ? 5.135  -1.894  5.418   0.30 19.26 ?  158 LYS   A HA   1 
ATOM   3471 H  HA   B LYS   A 1 158 ? 5.345  -1.511  6.073   0.40 27.42 ?  158 LYS   A HA   1 
ATOM   3472 H  HA   T LYS   A 1 158 ? 5.213  -1.752  5.349   0.30 21.35 ?  158 LYS   A HA   1 
ATOM   3473 H  HB2  A LYS   A 1 158 ? 4.133  -0.168  6.495   0.30 20.39 ?  158 LYS   A HB2  1 
ATOM   3474 H  HB2  B LYS   A 1 158 ? 4.406  0.127   7.281   0.40 28.83 ?  158 LYS   A HB2  1 
ATOM   3475 H  HB2  T LYS   A 1 158 ? 4.278  0.042   6.380   0.30 22.98 ?  158 LYS   A HB2  1 
ATOM   3476 H  HB3  A LYS   A 1 158 ? 3.331  0.254   5.196   0.30 20.39 ?  158 LYS   A HB3  1 
ATOM   3477 H  HB3  B LYS   A 1 158 ? 3.633  0.712   6.027   0.40 28.83 ?  158 LYS   A HB3  1 
ATOM   3478 H  HB3  T LYS   A 1 158 ? 3.470  0.443   5.076   0.30 22.98 ?  158 LYS   A HB3  1 
ATOM   3479 H  HG2  A LYS   A 1 158 ? 1.888  -0.702  6.720   0.30 21.58 ?  158 LYS   A HG2  1 
ATOM   3480 H  HG2  B LYS   A 1 158 ? 2.107  -0.281  7.425   0.40 30.17 ?  158 LYS   A HG2  1 
ATOM   3481 H  HG2  T LYS   A 1 158 ? 2.028  -0.444  6.652   0.30 24.73 ?  158 LYS   A HG2  1 
ATOM   3482 H  HG3  A LYS   A 1 158 ? 1.964  -1.632  5.437   0.30 21.58 ?  158 LYS   A HG3  1 
ATOM   3483 H  HG3  B LYS   A 1 158 ? 2.168  -1.152  6.105   0.40 30.17 ?  158 LYS   A HG3  1 
ATOM   3484 H  HG3  T LYS   A 1 158 ? 2.061  -1.404  5.390   0.30 24.73 ?  158 LYS   A HG3  1 
ATOM   3485 H  HD2  A LYS   A 1 158 ? 3.319  -3.128  6.558   0.30 22.46 ?  158 LYS   A HD2  1 
ATOM   3486 H  HD2  B LYS   A 1 158 ? 3.490  -2.732  7.210   0.40 30.96 ?  158 LYS   A HD2  1 
ATOM   3487 H  HD2  T LYS   A 1 158 ? 3.536  -2.828  6.554   0.30 26.36 ?  158 LYS   A HD2  1 
ATOM   3488 H  HD3  A LYS   A 1 158 ? 3.395  -2.155  7.817   0.30 22.46 ?  158 LYS   A HD3  1 
ATOM   3489 H  HD3  B LYS   A 1 158 ? 3.470  -1.834  8.525   0.40 30.96 ?  158 LYS   A HD3  1 
ATOM   3490 H  HD3  T LYS   A 1 158 ? 3.417  -1.875  7.825   0.30 26.36 ?  158 LYS   A HD3  1 
ATOM   3491 H  HE2  A LYS   A 1 158 ? 1.216  -2.550  8.345   0.30 22.80 ?  158 LYS   A HE2  1 
ATOM   3492 H  HE2  B LYS   A 1 158 ? 1.222  -2.216  8.813   0.40 31.30 ?  158 LYS   A HE2  1 
ATOM   3493 H  HE2  T LYS   A 1 158 ? 1.175  -2.404  8.045   0.30 27.36 ?  158 LYS   A HE2  1 
ATOM   3494 H  HE3  A LYS   A 1 158 ? 0.959  -3.270  6.961   0.30 22.80 ?  158 LYS   A HE3  1 
ATOM   3495 H  HE3  B LYS   A 1 158 ? 1.132  -2.966  7.414   0.40 31.30 ?  158 LYS   A HE3  1 
ATOM   3496 H  HE3  T LYS   A 1 158 ? 1.228  -3.270  6.717   0.30 27.36 ?  158 LYS   A HE3  1 
ATOM   3497 H  HZ1  A LYS   A 1 158 ? 1.133  -4.803  8.623   0.30 22.94 ?  158 LYS   A HZ1  1 
ATOM   3498 H  HZ1  B LYS   A 1 158 ? 1.182  -4.466  9.119   0.40 31.61 ?  158 LYS   A HZ1  1 
ATOM   3499 H  HZ1  T LYS   A 1 158 ? 1.323  -4.616  8.542   0.30 27.88 ?  158 LYS   A HZ1  1 
ATOM   3500 H  HZ2  A LYS   A 1 158 ? 2.215  -5.012  7.682   0.30 22.94 ?  158 LYS   A HZ2  1 
ATOM   3501 H  HZ2  B LYS   A 1 158 ? 2.375  -4.646  8.317   0.40 31.61 ?  158 LYS   A HZ2  1 
ATOM   3502 H  HZ2  T LYS   A 1 158 ? 2.563  -4.751  7.805   0.30 27.88 ?  158 LYS   A HZ2  1 
ATOM   3503 H  HZ3  A LYS   A 1 158 ? 2.474  -4.365  8.952   0.30 22.94 ?  158 LYS   A HZ3  1 
ATOM   3504 H  HZ3  B LYS   A 1 158 ? 2.456  -3.962  9.591   0.40 31.61 ?  158 LYS   A HZ3  1 
ATOM   3505 H  HZ3  T LYS   A 1 158 ? 2.525  -3.964  9.021   0.30 27.88 ?  158 LYS   A HZ3  1 
ATOM   3506 N  N    A ASN   A 1 159 ? 3.561  -1.442  2.662   0.30 16.45 ?  159 ASN   A N    1 
ATOM   3507 N  N    B ASN   A 1 159 ? 3.647  -0.960  3.415   0.40 21.22 ?  159 ASN   A N    1 
ATOM   3508 N  N    T ASN   A 1 159 ? 3.582  -1.312  2.625   0.30 18.89 ?  159 ASN   A N    1 
ATOM   3509 C  CA   A ASN   A 1 159 ? 2.859  -2.160  1.605   0.30 16.38 ?  159 ASN   A CA   1 
ATOM   3510 C  CA   B ASN   A 1 159 ? 2.937  -1.656  2.346   0.40 20.33 ?  159 ASN   A CA   1 
ATOM   3511 C  CA   T ASN   A 1 159 ? 2.853  -2.002  1.572   0.30 19.45 ?  159 ASN   A CA   1 
ATOM   3512 C  C    A ASN   A 1 159 ? 3.745  -3.256  1.001   0.30 14.72 ?  159 ASN   A C    1 
ATOM   3513 C  C    B ASN   A 1 159 ? 3.822  -2.719  1.703   0.40 19.15 ?  159 ASN   A C    1 
ATOM   3514 C  C    T ASN   A 1 159 ? 3.699  -3.099  0.912   0.30 19.14 ?  159 ASN   A C    1 
ATOM   3515 O  O    A ASN   A 1 159 ? 3.297  -4.394  0.800   0.30 14.81 ?  159 ASN   A O    1 
ATOM   3516 O  O    B ASN   A 1 159 ? 3.364  -3.832  1.422   0.40 18.58 ?  159 ASN   A O    1 
ATOM   3517 O  O    T ASN   A 1 159 ? 3.174  -4.136  0.506   0.30 19.48 ?  159 ASN   A O    1 
ATOM   3518 C  CB   A ASN   A 1 159 ? 2.347  -1.147  0.573   0.30 18.08 ?  159 ASN   A CB   1 
ATOM   3519 C  CB   B ASN   A 1 159 ? 2.440  -0.652  1.303   0.40 21.17 ?  159 ASN   A CB   1 
ATOM   3520 C  CB   T ASN   A 1 159 ? 2.349  -0.991  0.539   0.30 20.45 ?  159 ASN   A CB   1 
ATOM   3521 C  CG   A ASN   A 1 159 ? 1.273  -0.223  1.151   0.30 20.06 ?  159 ASN   A CG   1 
ATOM   3522 C  CG   B ASN   A 1 159 ? 1.568  -1.293  0.239   0.40 22.27 ?  159 ASN   A CG   1 
ATOM   3523 C  CG   T ASN   A 1 159 ? 1.247  -0.097  1.091   0.30 21.55 ?  159 ASN   A CG   1 
ATOM   3524 O  OD1  A ASN   A 1 159 ? 0.445  -0.660  1.945   0.30 20.55 ?  159 ASN   A OD1  1 
ATOM   3525 O  OD1  B ASN   A 1 159 ? 0.350  -1.124  0.241   0.40 23.28 ?  159 ASN   A OD1  1 
ATOM   3526 O  OD1  T ASN   A 1 159 ? 0.458  -0.524  1.931   0.30 21.86 ?  159 ASN   A OD1  1 
ATOM   3527 N  ND2  A ASN   A 1 159 ? 1.294  1.056   0.764   0.30 21.24 ?  159 ASN   A ND2  1 
ATOM   3528 N  ND2  B ASN   A 1 159 ? 2.189  -2.015  -0.689  0.40 22.33 ?  159 ASN   A ND2  1 
ATOM   3529 N  ND2  T ASN   A 1 159 ? 1.192  1.146   0.626   0.30 22.24 ?  159 ASN   A ND2  1 
ATOM   3530 H  H    A ASN   A 1 159 ? 3.708  -0.607  2.509   0.30 19.78 ?  159 ASN   A H    1 
ATOM   3531 H  H    B ASN   A 1 159 ? 3.751  -0.117  3.291   0.40 25.51 ?  159 ASN   A H    1 
ATOM   3532 H  H    T ASN   A 1 159 ? 3.707  -0.478  2.486   0.30 22.72 ?  159 ASN   A H    1 
ATOM   3533 H  HA   A ASN   A 1 159 ? 2.082  -2.586  1.993   0.30 19.70 ?  159 ASN   A HA   1 
ATOM   3534 H  HA   B ASN   A 1 159 ? 2.161  -2.102  2.725   0.40 24.43 ?  159 ASN   A HA   1 
ATOM   3535 H  HA   T ASN   A 1 159 ? 2.081  -2.430  1.968   0.30 23.38 ?  159 ASN   A HA   1 
ATOM   3536 H  HB2  A ASN   A 1 159 ? 3.075  -0.584  0.273   0.30 21.74 ?  159 ASN   A HB2  1 
ATOM   3537 H  HB2  B ASN   A 1 159 ? 1.912  0.030   1.748   0.40 25.45 ?  159 ASN   A HB2  1 
ATOM   3538 H  HB2  T ASN   A 1 159 ? 3.086  -0.425  0.265   0.30 24.59 ?  159 ASN   A HB2  1 
ATOM   3539 H  HB3  A ASN   A 1 159 ? 1.949  -1.613  -0.173  0.30 21.74 ?  159 ASN   A HB3  1 
ATOM   3540 H  HB3  B ASN   A 1 159 ? 3.200  -0.251  0.862   0.40 25.45 ?  159 ASN   A HB3  1 
ATOM   3541 H  HB3  T ASN   A 1 159 ? 1.994  -1.472  -0.222  0.30 24.59 ?  159 ASN   A HB3  1 
ATOM   3542 H  HD21 A ASN   A 1 159 ? 0.708  1.616   1.065   0.30 25.53 ?  159 ASN   A HD21 1 
ATOM   3543 H  HD21 B ASN   A 1 159 ? 1.736  -2.399  -1.312  0.40 26.83 ?  159 ASN   A HD21 1 
ATOM   3544 H  HD21 T ASN   A 1 159 ? 0.587  1.686   0.912   0.30 26.73 ?  159 ASN   A HD21 1 
ATOM   3545 H  HD22 A ASN   A 1 159 ? 1.892  1.330   0.215   0.30 25.53 ?  159 ASN   A HD22 1 
ATOM   3546 H  HD22 B ASN   A 1 159 ? 3.044  -2.107  -0.662  0.40 26.83 ?  159 ASN   A HD22 1 
ATOM   3547 H  HD22 T ASN   A 1 159 ? 1.764  1.411   0.045   0.30 26.73 ?  159 ASN   A HD22 1 
ATOM   3548 N  N    A LEU   A 1 160 ? 5.026  -2.953  0.774   0.30 13.31 ?  160 LEU   A N    1 
ATOM   3549 N  N    B LEU   A 1 160 ? 5.094  -2.398  1.463   0.40 18.19 ?  160 LEU   A N    1 
ATOM   3550 N  N    T LEU   A 1 160 ? 5.007  -2.877  0.819   0.30 18.57 ?  160 LEU   A N    1 
ATOM   3551 C  CA   A LEU   A 1 160 ? 5.937  -3.948  0.217   0.30 12.60 ?  160 LEU   A CA   1 
ATOM   3552 C  CA   B LEU   A 1 160 ? 6.001  -3.387  0.893   0.40 16.99 ?  160 LEU   A CA   1 
ATOM   3553 C  CA   T LEU   A 1 160 ? 5.911  -3.878  0.262   0.30 18.07 ?  160 LEU   A CA   1 
ATOM   3554 C  C    A LEU   A 1 160 ? 6.163  -5.088  1.197   0.30 11.37 ?  160 LEU   A C    1 
ATOM   3555 C  C    B LEU   A 1 160 ? 6.186  -4.566  1.836   0.40 14.80 ?  160 LEU   A C    1 
ATOM   3556 O  O    A LEU   A 1 160 ? 6.193  -6.265  0.808   0.30 11.11 ?  160 LEU   A O    1 
ATOM   3557 O  O    B LEU   A 1 160 ? 6.209  -5.723  1.400   0.40 14.46 ?  160 LEU   A O    1 
ATOM   3558 C  CB   A LEU   A 1 160 ? 7.266  -3.282  -0.125  0.30 12.70 ?  160 LEU   A CB   1 
ATOM   3559 C  CB   B LEU   A 1 160 ? 7.348  -2.740  0.586   0.40 17.97 ?  160 LEU   A CB   1 
ATOM   3560 C  CB   T LEU   A 1 160 ? 7.289  -3.272  -0.012  0.30 17.48 ?  160 LEU   A CB   1 
ATOM   3561 C  CG   A LEU   A 1 160 ? 8.400  -4.245  -0.449  0.30 13.51 ?  160 LEU   A CG   1 
ATOM   3562 C  CG   B LEU   A 1 160 ? 8.479  -3.715  0.268   0.40 19.07 ?  160 LEU   A CG   1 
ATOM   3563 C  CG   T LEU   A 1 160 ? 8.376  -4.265  -0.418  0.30 17.42 ?  160 LEU   A CG   1 
ATOM   3564 C  CD1  A LEU   A 1 160 ? 8.012  -5.084  -1.649  0.30 14.14 ?  160 LEU   A CD1  1 
ATOM   3565 C  CD1  B LEU   A 1 160 ? 8.151  -4.535  -0.967  0.40 19.42 ?  160 LEU   A CD1  1 
ATOM   3566 C  CD1  T LEU   A 1 160 ? 7.948  -5.049  -1.645  0.30 17.58 ?  160 LEU   A CD1  1 
ATOM   3567 C  CD2  A LEU   A 1 160 ? 9.678  -3.475  -0.701  0.30 13.43 ?  160 LEU   A CD2  1 
ATOM   3568 C  CD2  B LEU   A 1 160 ? 9.784  -2.964  0.098   0.40 19.35 ?  160 LEU   A CD2  1 
ATOM   3569 C  CD2  T LEU   A 1 160 ? 9.689  -3.541  -0.667  0.30 17.17 ?  160 LEU   A CD2  1 
ATOM   3570 H  H    A LEU   A 1 160 ? 5.388  -2.196  0.966   0.30 16.01 ?  160 LEU   A H    1 
ATOM   3571 H  H    B LEU   A 1 160 ? 5.443  -1.631  1.621   0.40 21.87 ?  160 LEU   A H    1 
ATOM   3572 H  H    T LEU   A 1 160 ? 5.398  -2.153  1.073   0.30 22.33 ?  160 LEU   A H    1 
ATOM   3573 H  HA   A LEU   A 1 160 ? 5.547  -4.311  -0.590  0.30 15.16 ?  160 LEU   A HA   1 
ATOM   3574 H  HA   B LEU   A 1 160 ? 5.626  -3.720  0.066   0.40 20.44 ?  160 LEU   A HA   1 
ATOM   3575 H  HB2  A LEU   A 1 160 ? 7.127  -2.713  -0.896  0.30 15.28 ?  160 LEU   A HB2  1 
ATOM   3576 H  HB2  B LEU   A 1 160 ? 7.245  -2.121  -0.161  0.40 21.61 ?  160 LEU   A HB2  1 
ATOM   3577 H  HB2  T LEU   A 1 160 ? 7.197  -2.618  -0.725  0.30 21.02 ?  160 LEU   A HB2  1 
ATOM   3578 H  HB3  A LEU   A 1 160 ? 7.539  -2.743  0.634   0.30 15.28 ?  160 LEU   A HB3  1 
ATOM   3579 H  HB3  B LEU   A 1 160 ? 7.621  -2.265  1.379   0.40 21.61 ?  160 LEU   A HB3  1 
ATOM   3580 H  HB3  T LEU   A 1 160 ? 7.599  -2.835  0.795   0.30 21.02 ?  160 LEU   A HB3  1 
ATOM   3581 H  HG   A LEU   A 1 160 ? 8.554  -4.836  0.305   0.30 16.26 ?  160 LEU   A HG   1 
ATOM   3582 H  HG   B LEU   A 1 160 ? 8.593  -4.323  1.015   0.40 22.93 ?  160 LEU   A HG   1 
ATOM   3583 H  HG   T LEU   A 1 160 ? 8.518  -4.892  0.310   0.30 20.94 ?  160 LEU   A HG   1 
ATOM   3584 H  HD11 A LEU   A 1 160 ? 8.767  -5.629  -1.901  0.30 17.02 ?  160 LEU   A HD11 1 
ATOM   3585 H  HD11 B LEU   A 1 160 ? 8.911  -5.096  -1.178  0.40 23.35 ?  160 LEU   A HD11 1 
ATOM   3586 H  HD11 T LEU   A 1 160 ? 8.695  -5.587  -1.948  0.30 21.13 ?  160 LEU   A HD11 1 
ATOM   3587 H  HD12 A LEU   A 1 160 ? 7.258  -5.644  -1.412  0.30 17.02 ?  160 LEU   A HD12 1 
ATOM   3588 H  HD12 B LEU   A 1 160 ? 7.373  -5.085  -0.784  0.40 23.35 ?  160 LEU   A HD12 1 
ATOM   3589 H  HD12 T LEU   A 1 160 ? 7.201  -5.619  -1.409  0.30 21.13 ?  160 LEU   A HD12 1 
ATOM   3590 H  HD13 A LEU   A 1 160 ? 7.768  -4.489  -2.377  0.30 17.02 ?  160 LEU   A HD13 1 
ATOM   3591 H  HD13 B LEU   A 1 160 ? 7.966  -3.933  -1.704  0.40 23.35 ?  160 LEU   A HD13 1 
ATOM   3592 H  HD13 T LEU   A 1 160 ? 7.686  -4.424  -2.339  0.30 21.13 ?  160 LEU   A HD13 1 
ATOM   3593 H  HD21 A LEU   A 1 160 ? 10.387 -4.102  -0.902  0.30 16.16 ?  160 LEU   A HD21 1 
ATOM   3594 H  HD21 B LEU   A 1 160 ? 10.489 -3.603  -0.081  0.40 23.27 ?  160 LEU   A HD21 1 
ATOM   3595 H  HD21 T LEU   A 1 160 ? 10.364 -4.189  -0.920  0.30 20.65 ?  160 LEU   A HD21 1 
ATOM   3596 H  HD22 A LEU   A 1 160 ? 9.541  -2.873  -1.449  0.30 16.16 ?  160 LEU   A HD22 1 
ATOM   3597 H  HD22 B LEU   A 1 160 ? 9.695  -2.346  -0.642  0.40 23.27 ?  160 LEU   A HD22 1 
ATOM   3598 H  HD22 T LEU   A 1 160 ? 9.562  -2.898  -1.383  0.30 20.65 ?  160 LEU   A HD22 1 
ATOM   3599 H  HD23 A LEU   A 1 160 ? 9.902  -2.965  0.096   0.30 16.16 ?  160 LEU   A HD23 1 
ATOM   3600 H  HD23 B LEU   A 1 160 ? 9.977  -2.477  0.916   0.40 23.27 ?  160 LEU   A HD23 1 
ATOM   3601 H  HD23 T LEU   A 1 160 ? 9.958  -3.082  0.145   0.30 20.65 ?  160 LEU   A HD23 1 
ATOM   3602 N  N    A TYR   A 1 161 ? 6.336  -4.751  2.474   0.60 13.06 ?  161 TYR   A N    1 
ATOM   3603 N  N    B TYR   A 1 161 ? 6.334  -4.289  3.132   0.40 13.70 ?  161 TYR   A N    1 
ATOM   3604 C  CA   A TYR   A 1 161 ? 6.463  -5.768  3.507   0.60 12.84 ?  161 TYR   A CA   1 
ATOM   3605 C  CA   B TYR   A 1 161 ? 6.493  -5.353  4.117   0.40 13.10 ?  161 TYR   A CA   1 
ATOM   3606 C  C    A TYR   A 1 161 ? 5.302  -6.755  3.450   0.60 13.17 ?  161 TYR   A C    1 
ATOM   3607 C  C    B TYR   A 1 161 ? 5.324  -6.329  4.066   0.40 13.62 ?  161 TYR   A C    1 
ATOM   3608 O  O    A TYR   A 1 161 ? 5.505  -7.973  3.458   0.60 13.27 ?  161 TYR   A O    1 
ATOM   3609 O  O    B TYR   A 1 161 ? 5.520  -7.549  4.034   0.40 13.49 ?  161 TYR   A O    1 
ATOM   3610 C  CB   A TYR   A 1 161 ? 6.537  -5.093  4.876   0.60 12.78 ?  161 TYR   A CB   1 
ATOM   3611 C  CB   B TYR   A 1 161 ? 6.625  -4.736  5.510   0.40 12.87 ?  161 TYR   A CB   1 
ATOM   3612 C  CG   A TYR   A 1 161 ? 6.394  -6.064  6.012   0.60 12.86 ?  161 TYR   A CG   1 
ATOM   3613 C  CG   B TYR   A 1 161 ? 6.473  -5.716  6.647   0.40 12.29 ?  161 TYR   A CG   1 
ATOM   3614 C  CD1  A TYR   A 1 161 ? 7.473  -6.821  6.439   0.60 12.98 ?  161 TYR   A CD1  1 
ATOM   3615 C  CD1  B TYR   A 1 161 ? 7.541  -6.492  7.072   0.40 12.22 ?  161 TYR   A CD1  1 
ATOM   3616 C  CD2  A TYR   A 1 161 ? 5.174  -6.239  6.657   0.60 13.27 ?  161 TYR   A CD2  1 
ATOM   3617 C  CD2  B TYR   A 1 161 ? 5.262  -5.853  7.307   0.40 12.25 ?  161 TYR   A CD2  1 
ATOM   3618 C  CE1  A TYR   A 1 161 ? 7.344  -7.725  7.467   0.60 13.17 ?  161 TYR   A CE1  1 
ATOM   3619 C  CE1  B TYR   A 1 161 ? 7.401  -7.383  8.118   0.40 12.60 ?  161 TYR   A CE1  1 
ATOM   3620 C  CE2  A TYR   A 1 161 ? 5.038  -7.145  7.692   0.60 13.41 ?  161 TYR   A CE2  1 
ATOM   3621 C  CE2  B TYR   A 1 161 ? 5.113  -6.739  8.352   0.40 12.38 ?  161 TYR   A CE2  1 
ATOM   3622 C  CZ   A TYR   A 1 161 ? 6.130  -7.884  8.093   0.60 13.55 ?  161 TYR   A CZ   1 
ATOM   3623 C  CZ   B TYR   A 1 161 ? 6.184  -7.502  8.753   0.40 12.93 ?  161 TYR   A CZ   1 
ATOM   3624 O  OH   A TYR   A 1 161 ? 6.013  -8.792  9.121   0.60 14.91 ?  161 TYR   A OH   1 
ATOM   3625 O  OH   B TYR   A 1 161 ? 6.031  -8.383  9.799   0.40 14.07 ?  161 TYR   A OH   1 
ATOM   3626 H  H    A TYR   A 1 161 ? 6.367  -3.957  2.776   0.60 15.72 ?  161 TYR   A H    1 
ATOM   3627 H  H    B TYR   A 1 161 ? 6.341  -3.499  3.466   0.40 16.49 ?  161 TYR   A H    1 
ATOM   3628 H  HA   A TYR   A 1 161 ? 7.277  -6.277  3.373   0.60 15.45 ?  161 TYR   A HA   1 
ATOM   3629 H  HA   B TYR   A 1 161 ? 7.303  -5.849  3.931   0.40 15.77 ?  161 TYR   A HA   1 
ATOM   3630 H  HB2  A TYR   A 1 161 ? 7.401  -4.665  4.968   0.60 15.38 ?  161 TYR   A HB2  1 
ATOM   3631 H  HB2  B TYR   A 1 161 ? 7.501  -4.331  5.590   0.40 15.49 ?  161 TYR   A HB2  1 
ATOM   3632 H  HB3  A TYR   A 1 161 ? 5.826  -4.445  4.953   0.60 15.38 ?  161 TYR   A HB3  1 
ATOM   3633 H  HB3  B TYR   A 1 161 ? 5.939  -4.055  5.617   0.40 15.49 ?  161 TYR   A HB3  1 
ATOM   3634 H  HD1  A TYR   A 1 161 ? 8.294  -6.724  6.020   0.60 15.62 ?  161 TYR   A HD1  1 
ATOM   3635 H  HD1  B TYR   A 1 161 ? 8.362  -6.411  6.648   0.40 14.71 ?  161 TYR   A HD1  1 
ATOM   3636 H  HD2  A TYR   A 1 161 ? 4.432  -5.746  6.389   0.60 15.96 ?  161 TYR   A HD2  1 
ATOM   3637 H  HD2  B TYR   A 1 161 ? 4.532  -5.341  7.044   0.40 14.74 ?  161 TYR   A HD2  1 
ATOM   3638 H  HE1  A TYR   A 1 161 ? 8.076  -8.228  7.744   0.60 15.85 ?  161 TYR   A HE1  1 
ATOM   3639 H  HE1  B TYR   A 1 161 ? 8.124  -7.900  8.395   0.40 15.16 ?  161 TYR   A HE1  1 
ATOM   3640 H  HE2  A TYR   A 1 161 ? 4.211  -7.254  8.118   0.60 16.13 ?  161 TYR   A HE2  1 
ATOM   3641 H  HE2  B TYR   A 1 161 ? 4.288  -6.822  8.785   0.40 14.90 ?  161 TYR   A HE2  1 
ATOM   3642 H  HH   A TYR   A 1 161 ? 5.224  -8.790  9.426   0.60 17.94 ?  161 TYR   A HH   1 
ATOM   3643 H  HH   B TYR   A 1 161 ? 6.747  -8.788  9.948   0.40 16.93 ?  161 TYR   A HH   1 
ATOM   3644 N  N    A ASP   A 1 162 ? 4.069  -6.245  3.386   0.60 13.76 ?  162 ASP   A N    1 
ATOM   3645 N  N    B ASP   A 1 162 ? 4.095  -5.810  4.065   0.40 14.17 ?  162 ASP   A N    1 
ATOM   3646 C  CA   A ASP   A 1 162 ? 2.903  -7.128  3.349   0.60 14.34 ?  162 ASP   A CA   1 
ATOM   3647 C  CA   B ASP   A 1 162 ? 2.933  -6.694  4.048   0.40 14.89 ?  162 ASP   A CA   1 
ATOM   3648 C  C    A ASP   A 1 162 ? 2.936  -8.035  2.119   0.60 14.32 ?  162 ASP   A C    1 
ATOM   3649 C  C    B ASP   A 1 162 ? 2.927  -7.564  2.799   0.40 15.19 ?  162 ASP   A C    1 
ATOM   3650 O  O    A ASP   A 1 162 ? 2.555  -9.207  2.190   0.60 14.49 ?  162 ASP   A O    1 
ATOM   3651 O  O    B ASP   A 1 162 ? 2.562  -8.744  2.855   0.40 15.57 ?  162 ASP   A O    1 
ATOM   3652 C  CB   A ASP   A 1 162 ? 1.606  -6.302  3.383   0.60 15.41 ?  162 ASP   A CB   1 
ATOM   3653 C  CB   B ASP   A 1 162 ? 1.639  -5.879  4.135   0.40 15.44 ?  162 ASP   A CB   1 
ATOM   3654 C  CG   A ASP   A 1 162 ? 1.284  -5.739  4.764   0.60 16.76 ?  162 ASP   A CG   1 
ATOM   3655 C  CG   B ASP   A 1 162 ? 1.421  -5.250  5.499   0.40 16.16 ?  162 ASP   A CG   1 
ATOM   3656 O  OD1  A ASP   A 1 162 ? 1.981  -6.070  5.740   0.60 17.43 ?  162 ASP   A OD1  1 
ATOM   3657 O  OD1  B ASP   A 1 162 ? 2.147  -5.595  6.453   0.40 16.37 ?  162 ASP   A OD1  1 
ATOM   3658 O  OD2  A ASP   A 1 162 ? 0.299  -4.969  4.870   0.60 17.54 -1 162 ASP   A OD2  1 
ATOM   3659 O  OD2  B ASP   A 1 162 ? 0.509  -4.404  5.616   0.40 17.16 -1 162 ASP   A OD2  1 
ATOM   3660 H  H    A ASP   A 1 162 ? 3.880  -5.416  3.367   0.60 16.56 ?  162 ASP   A H    1 
ATOM   3661 H  H    B ASP   A 1 162 ? 3.908  -4.971  4.070   0.40 17.05 ?  162 ASP   A H    1 
ATOM   3662 H  HA   A ASP   A 1 162 ? 2.899  -7.702  4.134   0.60 17.25 ?  162 ASP   A HA   1 
ATOM   3663 H  HA   B ASP   A 1 162 ? 2.968  -7.281  4.818   0.40 17.91 ?  162 ASP   A HA   1 
ATOM   3664 H  HB2  A ASP   A 1 162 ? 1.686  -5.555  2.775   0.60 18.54 ?  162 ASP   A HB2  1 
ATOM   3665 H  HB2  B ASP   A 1 162 ? 1.668  -5.157  3.495   0.40 18.57 ?  162 ASP   A HB2  1 
ATOM   3666 H  HB3  A ASP   A 1 162 ? 0.855  -6.862  3.129   0.60 18.54 ?  162 ASP   A HB3  1 
ATOM   3667 H  HB3  B ASP   A 1 162 ? 0.881  -6.459  3.955   0.40 18.57 ?  162 ASP   A HB3  1 
ATOM   3668 N  N    A LYS   A 1 163 ? 3.419  -7.516  0.988   0.60 14.71 ?  163 LYS   A N    1 
ATOM   3669 N  N    B LYS   A 1 163 ? 3.315  -6.999  1.657   0.40 15.68 ?  163 LYS   A N    1 
ATOM   3670 C  CA   A LYS   A 1 163 ? 3.493  -8.305  -0.240  0.60 15.28 ?  163 LYS   A CA   1 
ATOM   3671 C  CA   B LYS   A 1 163 ? 3.359  -7.782  0.429   0.40 16.50 ?  163 LYS   A CA   1 
ATOM   3672 C  C    A LYS   A 1 163 ? 4.565  -9.390  -0.145  0.60 14.61 ?  163 LYS   A C    1 
ATOM   3673 C  C    B LYS   A 1 163 ? 4.483  -8.810  0.462   0.40 15.58 ?  163 LYS   A C    1 
ATOM   3674 O  O    A LYS   A 1 163 ? 4.370  -10.517 -0.620  0.60 15.53 ?  163 LYS   A O    1 
ATOM   3675 O  O    B LYS   A 1 163 ? 4.329  -9.915  -0.066  0.40 15.78 ?  163 LYS   A O    1 
ATOM   3676 C  CB   A LYS   A 1 163 ? 3.783  -7.361  -1.404  0.60 18.15 ?  163 LYS   A CB   1 
ATOM   3677 C  CB   B LYS   A 1 163 ? 3.523  -6.859  -0.771  0.40 19.06 ?  163 LYS   A CB   1 
ATOM   3678 C  CG   A LYS   A 1 163 ? 3.822  -8.004  -2.772  0.60 21.37 ?  163 LYS   A CG   1 
ATOM   3679 C  CG   B LYS   A 1 163 ? 3.647  -7.592  -2.082  0.40 21.45 ?  163 LYS   A CG   1 
ATOM   3680 C  CD   A LYS   A 1 163 ? 4.241  -6.980  -3.813  0.60 24.14 ?  163 LYS   A CD   1 
ATOM   3681 C  CD   B LYS   A 1 163 ? 3.669  -6.611  -3.223  0.40 23.48 ?  163 LYS   A CD   1 
ATOM   3682 C  CE   A LYS   A 1 163 ? 4.178  -7.551  -5.218  0.60 26.34 ?  163 LYS   A CE   1 
ATOM   3683 C  CE   B LYS   A 1 163 ? 3.861  -7.308  -4.550  0.40 25.01 ?  163 LYS   A CE   1 
ATOM   3684 N  NZ   A LYS   A 1 163 ? 4.876  -6.679  -6.199  0.60 27.47 ?  163 LYS   A NZ   1 
ATOM   3685 N  NZ   B LYS   A 1 163 ? 4.136  -6.319  -5.625  0.40 25.74 ?  163 LYS   A NZ   1 
ATOM   3686 H  H    A LYS   A 1 163 ? 3.723  -6.719  0.917   0.60 17.70 ?  163 LYS   A H    1 
ATOM   3687 H  H    B LYS   A 1 163 ? 3.549  -6.180  1.568   0.40 18.85 ?  163 LYS   A H    1 
ATOM   3688 H  HA   A LYS   A 1 163 ? 2.640  -8.735  -0.396  0.60 18.38 ?  163 LYS   A HA   1 
ATOM   3689 H  HA   B LYS   A 1 163 ? 2.522  -8.261  0.325   0.40 19.84 ?  163 LYS   A HA   1 
ATOM   3690 H  HB2  A LYS   A 1 163 ? 3.095  -6.679  -1.420  0.60 21.82 ?  163 LYS   A HB2  1 
ATOM   3691 H  HB2  B LYS   A 1 163 ? 2.748  -6.280  -0.827  0.40 22.92 ?  163 LYS   A HB2  1 
ATOM   3692 H  HB3  A LYS   A 1 163 ? 4.647  -6.945  -1.253  0.60 21.82 ?  163 LYS   A HB3  1 
ATOM   3693 H  HB3  B LYS   A 1 163 ? 4.325  -6.328  -0.649  0.40 22.92 ?  163 LYS   A HB3  1 
ATOM   3694 H  HG2  A LYS   A 1 163 ? 4.467  -8.728  -2.776  0.60 25.68 ?  163 LYS   A HG2  1 
ATOM   3695 H  HG2  B LYS   A 1 163 ? 4.477  -8.096  -2.095  0.40 25.78 ?  163 LYS   A HG2  1 
ATOM   3696 H  HG3  A LYS   A 1 163 ? 2.938  -8.333  -3.000  0.60 25.68 ?  163 LYS   A HG3  1 
ATOM   3697 H  HG3  B LYS   A 1 163 ? 2.888  -8.185  -2.193  0.40 25.78 ?  163 LYS   A HG3  1 
ATOM   3698 H  HD2  A LYS   A 1 163 ? 3.642  -6.215  -3.768  0.60 29.01 ?  163 LYS   A HD2  1 
ATOM   3699 H  HD2  B LYS   A 1 163 ? 2.825  -6.135  -3.246  0.40 28.22 ?  163 LYS   A HD2  1 
ATOM   3700 H  HD3  A LYS   A 1 163 ? 5.153  -6.699  -3.638  0.60 29.01 ?  163 LYS   A HD3  1 
ATOM   3701 H  HD3  B LYS   A 1 163 ? 4.403  -5.990  -3.093  0.40 28.22 ?  163 LYS   A HD3  1 
ATOM   3702 H  HE2  A LYS   A 1 163 ? 4.597  -8.423  -5.230  0.60 31.65 ?  163 LYS   A HE2  1 
ATOM   3703 H  HE2  B LYS   A 1 163 ? 4.614  -7.917  -4.486  0.40 30.06 ?  163 LYS   A HE2  1 
ATOM   3704 H  HE3  A LYS   A 1 163 ? 3.249  -7.625  -5.485  0.60 31.65 ?  163 LYS   A HE3  1 
ATOM   3705 H  HE3  B LYS   A 1 163 ? 3.054  -7.795  -4.778  0.40 30.06 ?  163 LYS   A HE3  1 
ATOM   3706 H  HZ1  A LYS   A 1 163 ? 4.824  -7.036  -7.012  0.60 33.01 ?  163 LYS   A HZ1  1 
ATOM   3707 H  HZ1  B LYS   A 1 163 ? 4.249  -6.737  -6.401  0.40 30.93 ?  163 LYS   A HZ1  1 
ATOM   3708 H  HZ2  A LYS   A 1 163 ? 4.496  -5.873  -6.213  0.60 33.01 ?  163 LYS   A HZ2  1 
ATOM   3709 H  HZ2  B LYS   A 1 163 ? 3.455  -5.752  -5.695  0.40 30.93 ?  163 LYS   A HZ2  1 
ATOM   3710 H  HZ3  A LYS   A 1 163 ? 5.732  -6.591  -5.974  0.60 33.01 ?  163 LYS   A HZ3  1 
ATOM   3711 H  HZ3  B LYS   A 1 163 ? 4.875  -5.860  -5.432  0.40 30.93 ?  163 LYS   A HZ3  1 
ATOM   3712 N  N    A LEU   A 1 164 ? 5.713  -9.055  0.449   0.60 13.83 ?  164 LEU   A N    1 
ATOM   3713 N  N    B LEU   A 1 164 ? 5.628  -8.462  1.052   0.40 14.34 ?  164 LEU   A N    1 
ATOM   3714 C  CA   A LEU   A 1 164 ? 6.790  -10.029 0.613   0.60 13.55 ?  164 LEU   A CA   1 
ATOM   3715 C  CA   B LEU   A 1 164 ? 6.716  -9.428  1.179   0.40 13.65 ?  164 LEU   A CA   1 
ATOM   3716 C  C    A LEU   A 1 164 ? 6.351  -11.184 1.501   0.60 13.80 ?  164 LEU   A C    1 
ATOM   3717 C  C    B LEU   A 1 164 ? 6.292  -10.621 2.021   0.40 13.74 ?  164 LEU   A C    1 
ATOM   3718 O  O    A LEU   A 1 164 ? 6.649  -12.348 1.213   0.60 14.16 ?  164 LEU   A O    1 
ATOM   3719 O  O    B LEU   A 1 164 ? 6.596  -11.772 1.682   0.40 14.17 ?  164 LEU   A O    1 
ATOM   3720 C  CB   A LEU   A 1 164 ? 8.020  -9.353  1.220   0.60 13.39 ?  164 LEU   A CB   1 
ATOM   3721 C  CB   B LEU   A 1 164 ? 7.930  -8.758  1.812   0.40 13.30 ?  164 LEU   A CB   1 
ATOM   3722 C  CG   A LEU   A 1 164 ? 8.709  -8.294  0.363   0.60 13.81 ?  164 LEU   A CG   1 
ATOM   3723 C  CG   B LEU   A 1 164 ? 8.705  -7.823  0.895   0.40 13.77 ?  164 LEU   A CG   1 
ATOM   3724 C  CD1  A LEU   A 1 164 ? 9.591  -7.388  1.215   0.60 13.94 ?  164 LEU   A CD1  1 
ATOM   3725 C  CD1  B LEU   A 1 164 ? 9.712  -7.018  1.697   0.40 13.85 ?  164 LEU   A CD1  1 
ATOM   3726 C  CD2  A LEU   A 1 164 ? 9.523  -8.955  -0.732  0.60 14.39 ?  164 LEU   A CD2  1 
ATOM   3727 C  CD2  B LEU   A 1 164 ? 9.392  -8.633  -0.191  0.40 13.87 ?  164 LEU   A CD2  1 
ATOM   3728 H  H    A LEU   A 1 164 ? 5.893  -8.289  0.770   0.60 16.63 ?  164 LEU   A H    1 
ATOM   3729 H  H    B LEU   A 1 164 ? 5.797  -7.683  1.378   0.40 17.25 ?  164 LEU   A H    1 
ATOM   3730 H  HA   A LEU   A 1 164 ? 7.029  -10.403 -0.247  0.60 16.31 ?  164 LEU   A HA   1 
ATOM   3731 H  HA   B LEU   A 1 164 ? 6.966  -9.751  0.302   0.40 16.42 ?  164 LEU   A HA   1 
ATOM   3732 H  HB2  A LEU   A 1 164 ? 7.750  -8.934  2.048   0.60 16.12 ?  164 LEU   A HB2  1 
ATOM   3733 H  HB2  B LEU   A 1 164 ? 7.631  -8.238  2.576   0.40 16.01 ?  164 LEU   A HB2  1 
ATOM   3734 H  HB3  A LEU   A 1 164 ? 8.676  -10.046 1.411   0.60 16.12 ?  164 LEU   A HB3  1 
ATOM   3735 H  HB3  B LEU   A 1 164 ? 8.542  -9.448  2.112   0.40 16.01 ?  164 LEU   A HB3  1 
ATOM   3736 H  HG   A LEU   A 1 164 ? 8.029  -7.746  -0.056  0.60 16.61 ?  164 LEU   A HG   1 
ATOM   3737 H  HG   B LEU   A 1 164 ? 8.085  -7.206  0.474   0.40 16.57 ?  164 LEU   A HG   1 
ATOM   3738 H  HD11 A LEU   A 1 164 ? 10.012 -6.731  0.643   0.60 16.77 ?  164 LEU   A HD11 1 
ATOM   3739 H  HD11 B LEU   A 1 164 ? 10.193 -6.432  1.097   0.40 16.67 ?  164 LEU   A HD11 1 
ATOM   3740 H  HD12 A LEU   A 1 164 ? 9.037  -6.942  1.879   0.60 16.77 ?  164 LEU   A HD12 1 
ATOM   3741 H  HD12 B LEU   A 1 164 ? 9.238  -6.499  2.365   0.40 16.67 ?  164 LEU   A HD12 1 
ATOM   3742 H  HD13 A LEU   A 1 164 ? 10.264 -7.927  1.659   0.60 16.77 ?  164 LEU   A HD13 1 
ATOM   3743 H  HD13 B LEU   A 1 164 ? 10.327 -7.632  2.131   0.40 16.67 ?  164 LEU   A HD13 1 
ATOM   3744 H  HD21 A LEU   A 1 164 ? 9.949  -8.262  -1.263  0.60 17.30 ?  164 LEU   A HD21 1 
ATOM   3745 H  HD21 B LEU   A 1 164 ? 10.023 -8.064  -0.654  0.40 16.69 ?  164 LEU   A HD21 1 
ATOM   3746 H  HD22 A LEU   A 1 164 ? 10.196 -9.522  -0.327  0.60 17.30 ?  164 LEU   A HD22 1 
ATOM   3747 H  HD22 B LEU   A 1 164 ? 9.856  -9.380  0.219   0.40 16.69 ?  164 LEU   A HD22 1 
ATOM   3748 H  HD23 A LEU   A 1 164 ? 8.933  -9.483  -1.291  0.60 17.30 ?  164 LEU   A HD23 1 
ATOM   3749 H  HD23 B LEU   A 1 164 ? 8.723  -8.962  -0.813  0.40 16.69 ?  164 LEU   A HD23 1 
ATOM   3750 N  N    A VAL   A 1 165 ? 5.651  -10.878 2.592   0.60 13.53 ?  165 VAL   A N    1 
ATOM   3751 N  N    B VAL   A 1 165 ? 5.602  -10.360 3.132   0.40 13.47 ?  165 VAL   A N    1 
ATOM   3752 C  CA   A VAL   A 1 165 ? 5.156  -11.919 3.486   0.60 13.31 ?  165 VAL   A CA   1 
ATOM   3753 C  CA   B VAL   A 1 165 ? 5.128  -11.444 3.984   0.40 13.88 ?  165 VAL   A CA   1 
ATOM   3754 C  C    A VAL   A 1 165 ? 4.122  -12.778 2.773   0.60 13.44 ?  165 VAL   A C    1 
ATOM   3755 C  C    B VAL   A 1 165 ? 4.096  -12.282 3.243   0.40 13.84 ?  165 VAL   A C    1 
ATOM   3756 O  O    A VAL   A 1 165 ? 4.227  -14.010 2.741   0.60 13.10 ?  165 VAL   A O    1 
ATOM   3757 O  O    B VAL   A 1 165 ? 4.177  -13.516 3.211   0.40 13.91 ?  165 VAL   A O    1 
ATOM   3758 C  CB   A VAL   A 1 165 ? 4.573  -11.275 4.759   0.60 13.76 ?  165 VAL   A CB   1 
ATOM   3759 C  CB   B VAL   A 1 165 ? 4.565  -10.885 5.305   0.40 14.43 ?  165 VAL   A CB   1 
ATOM   3760 C  CG1  A VAL   A 1 165 ? 3.805  -12.298 5.593   0.60 14.16 ?  165 VAL   A CG1  1 
ATOM   3761 C  CG1  B VAL   A 1 165 ? 3.834  -11.976 6.073   0.40 14.85 ?  165 VAL   A CG1  1 
ATOM   3762 C  CG2  A VAL   A 1 165 ? 5.673  -10.613 5.571   0.60 14.09 ?  165 VAL   A CG2  1 
ATOM   3763 C  CG2  B VAL   A 1 165 ? 5.675  -10.283 6.160   0.40 14.75 ?  165 VAL   A CG2  1 
ATOM   3764 H  H    A VAL   A 1 165 ? 5.436  -10.095 2.836   0.60 16.28 ?  165 VAL   A H    1 
ATOM   3765 H  H    B VAL   A 1 165 ? 5.396  -9.569  3.409   0.40 16.21 ?  165 VAL   A H    1 
ATOM   3766 H  HA   A VAL   A 1 165 ? 5.885  -12.504 3.759   0.60 16.01 ?  165 VAL   A HA   1 
ATOM   3767 H  HA   B VAL   A 1 165 ? 5.874  -12.017 4.205   0.40 16.69 ?  165 VAL   A HA   1 
ATOM   3768 H  HB   A VAL   A 1 165 ? 3.942  -10.590 4.497   0.60 16.55 ?  165 VAL   A HB   1 
ATOM   3769 H  HB   B VAL   A 1 165 ? 3.927  -10.180 5.110   0.40 17.36 ?  165 VAL   A HB   1 
ATOM   3770 H  HG11 A VAL   A 1 165 ? 3.668  -11.938 6.486   0.60 17.04 ?  165 VAL   A HG11 1 
ATOM   3771 H  HG11 B VAL   A 1 165 ? 3.786  -11.725 7.009   0.40 17.86 ?  165 VAL   A HG11 1 
ATOM   3772 H  HG12 A VAL   A 1 165 ? 2.940  -12.467 5.179   0.60 17.04 ?  165 VAL   A HG12 1 
ATOM   3773 H  HG12 B VAL   A 1 165 ? 2.938  -12.074 5.712   0.40 17.86 ?  165 VAL   A HG12 1 
ATOM   3774 H  HG13 A VAL   A 1 165 ? 4.315  -13.118 5.644   0.60 17.04 ?  165 VAL   A HG13 1 
ATOM   3775 H  HG13 B VAL   A 1 165 ? 4.323  -12.808 5.982   0.40 17.86 ?  165 VAL   A HG13 1 
ATOM   3776 H  HG21 A VAL   A 1 165 ? 5.286  -10.215 6.367   0.60 16.95 ?  165 VAL   A HG21 1 
ATOM   3777 H  HG21 B VAL   A 1 165 ? 5.290  -9.930  6.980   0.40 17.74 ?  165 VAL   A HG21 1 
ATOM   3778 H  HG22 A VAL   A 1 165 ? 6.330  -11.281 5.821   0.60 16.95 ?  165 VAL   A HG22 1 
ATOM   3779 H  HG22 B VAL   A 1 165 ? 6.322  -10.974 6.371   0.40 17.74 ?  165 VAL   A HG22 1 
ATOM   3780 H  HG23 A VAL   A 1 165 ? 6.090  -9.925  5.027   0.60 16.95 ?  165 VAL   A HG23 1 
ATOM   3781 H  HG23 B VAL   A 1 165 ? 6.103  -9.568  5.664   0.40 17.74 ?  165 VAL   A HG23 1 
ATOM   3782 N  N    A SER   A 1 166 ? 3.110  -12.139 2.187   0.60 14.25 ?  166 SER   A N    1 
ATOM   3783 N  N    B SER   A 1 166 ? 3.115  -11.623 2.624   0.40 14.31 ?  166 SER   A N    1 
ATOM   3784 C  CA   A SER   A 1 166 ? 1.983  -12.878 1.631   0.60 15.88 ?  166 SER   A CA   1 
ATOM   3785 C  CA   B SER   A 1 166 ? 1.984  -12.351 2.063   0.40 15.11 ?  166 SER   A CA   1 
ATOM   3786 C  C    A SER   A 1 166 ? 2.407  -13.738 0.454   0.60 16.49 ?  166 SER   A C    1 
ATOM   3787 C  C    B SER   A 1 166 ? 2.391  -13.248 0.905   0.40 16.55 ?  166 SER   A C    1 
ATOM   3788 O  O    A SER   A 1 166 ? 1.832  -14.812 0.233   0.60 18.20 ?  166 SER   A O    1 
ATOM   3789 O  O    B SER   A 1 166 ? 1.668  -14.198 0.588   0.40 17.68 ?  166 SER   A O    1 
ATOM   3790 C  CB   A SER   A 1 166 ? 0.881  -11.904 1.201   0.60 17.57 ?  166 SER   A CB   1 
ATOM   3791 C  CB   B SER   A 1 166 ? 0.910  -11.373 1.588   0.40 15.66 ?  166 SER   A CB   1 
ATOM   3792 O  OG   A SER   A 1 166 ? 0.350  -11.177 2.303   0.60 19.48 ?  166 SER   A OG   1 
ATOM   3793 O  OG   B SER   A 1 166 ? 1.177  -10.930 0.272   0.40 16.75 ?  166 SER   A OG   1 
ATOM   3794 H  H    A SER   A 1 166 ? 3.052  -11.300 2.101   0.60 17.14 ?  166 SER   A H    1 
ATOM   3795 H  H    B SER   A 1 166 ? 3.083  -10.766 2.516   0.40 17.21 ?  166 SER   A H    1 
ATOM   3796 H  HA   A SER   A 1 166 ? 1.608  -13.473 2.305   0.60 19.10 ?  166 SER   A HA   1 
ATOM   3797 H  HA   B SER   A 1 166 ? 1.589  -12.902 2.759   0.40 18.18 ?  166 SER   A HA   1 
ATOM   3798 H  HB2  A SER   A 1 166 ? 1.252  -11.274 0.568   0.60 21.13 ?  166 SER   A HB2  1 
ATOM   3799 H  HB2  B SER   A 1 166 ? 0.045  -11.818 1.593   0.40 18.83 ?  166 SER   A HB2  1 
ATOM   3800 H  HB3  A SER   A 1 166 ? 0.158  -12.403 0.786   0.60 21.13 ?  166 SER   A HB3  1 
ATOM   3801 H  HB3  B SER   A 1 166 ? 0.884  -10.607 2.189   0.40 18.83 ?  166 SER   A HB3  1 
ATOM   3802 H  HG   A SER   A 1 166 ? 0.973  -10.751 2.684   0.60 23.42 ?  166 SER   A HG   1 
ATOM   3803 H  HG   B SER   A 1 166 ? 0.588  -10.381 0.027   0.40 20.14 ?  166 SER   A HG   1 
ATOM   3804 N  N    A SER   A 1 167 ? 3.397  -13.286 -0.309  0.60 16.12 ?  167 SER   A N    1 
ATOM   3805 N  N    B SER   A 1 167 ? 3.523  -12.968 0.268   0.40 17.76 ?  167 SER   A N    1 
ATOM   3806 C  CA   A SER   A 1 167 ? 3.914  -14.031 -1.440  0.60 17.45 ?  167 SER   A CA   1 
ATOM   3807 C  CA   B SER   A 1 167 ? 4.008  -13.744 -0.868  0.40 19.50 ?  167 SER   A CA   1 
ATOM   3808 C  C    A SER   A 1 167 ? 5.088  -14.910 -1.056  0.60 17.24 ?  167 SER   A C    1 
ATOM   3809 C  C    B SER   A 1 167 ? 5.344  -14.373 -0.474  0.40 20.72 ?  167 SER   A C    1 
ATOM   3810 O  O    A SER   A 1 167 ? 5.620  -15.608 -1.924  0.60 17.23 ?  167 SER   A O    1 
ATOM   3811 O  O    B SER   A 1 167 ? 6.404  -13.809 -0.755  0.40 22.07 ?  167 SER   A O    1 
ATOM   3812 C  CB   A SER   A 1 167 ? 4.355  -13.066 -2.548  0.60 18.29 ?  167 SER   A CB   1 
ATOM   3813 C  CB   B SER   A 1 167 ? 4.153  -12.830 -2.093  0.40 20.08 ?  167 SER   A CB   1 
ATOM   3814 O  OG   A SER   A 1 167 ? 5.479  -12.300 -2.141  0.60 18.81 ?  167 SER   A OG   1 
ATOM   3815 O  OG   B SER   A 1 167 ? 5.152  -11.842 -1.880  0.40 20.35 ?  167 SER   A OG   1 
ATOM   3816 H  H    A SER   A 1 167 ? 3.780  -12.530 -0.193  0.60 19.38 ?  167 SER   A H    1 
ATOM   3817 H  H    B SER   A 1 167 ? 4.032  -12.304 0.479   0.40 21.35 ?  167 SER   A H    1 
ATOM   3818 H  HA   A SER   A 1 167 ? 3.218  -14.604 -1.800  0.60 20.98 ?  167 SER   A HA   1 
ATOM   3819 H  HA   B SER   A 1 167 ? 3.379  -14.453 -1.072  0.40 23.44 ?  167 SER   A HA   1 
ATOM   3820 H  HB2  A SER   A 1 167 ? 4.589  -13.579 -3.340  0.60 21.99 ?  167 SER   A HB2  1 
ATOM   3821 H  HB2  B SER   A 1 167 ? 4.394  -13.367 -2.863  0.40 24.14 ?  167 SER   A HB2  1 
ATOM   3822 H  HB3  A SER   A 1 167 ? 3.619  -12.465 -2.752  0.60 21.99 ?  167 SER   A HB3  1 
ATOM   3823 H  HB3  B SER   A 1 167 ? 3.305  -12.382 -2.259  0.40 24.14 ?  167 SER   A HB3  1 
ATOM   3824 H  HG   A SER   A 1 167 ? 5.284  -11.860 -1.453  0.60 22.61 ?  167 SER   A HG   1 
ATOM   3825 H  HG   B SER   A 1 167 ? 5.906  -12.203 -1.799  0.40 24.47 ?  167 SER   A HG   1 
ATOM   3826 N  N    A PHE   A 1 168 ? 5.523  -14.881 0.203   0.60 17.28 ?  168 PHE   A N    1 
ATOM   3827 N  N    B PHE   A 1 168 ? 5.299  -15.541 0.176   0.40 20.05 ?  168 PHE   A N    1 
ATOM   3828 C  CA   A PHE   A 1 168 ? 6.701  -15.651 0.571   0.60 17.70 ?  168 PHE   A CA   1 
ATOM   3829 C  CA   B PHE   A 1 168 ? 6.544  -16.222 0.534   0.40 19.49 ?  168 PHE   A CA   1 
ATOM   3830 C  C    A PHE   A 1 168 ? 6.406  -17.139 0.471   0.60 19.15 ?  168 PHE   A C    1 
ATOM   3831 C  C    B PHE   A 1 168 ? 6.486  -17.747 0.477   0.40 20.61 ?  168 PHE   A C    1 
ATOM   3832 O  O    A PHE   A 1 168 ? 5.433  -17.638 1.049   0.60 20.42 ?  168 PHE   A O    1 
ATOM   3833 O  O    B PHE   A 1 168 ? 7.280  -18.361 -0.245  0.40 20.51 ?  168 PHE   A O    1 
ATOM   3834 C  CB   A PHE   A 1 168 ? 7.193  -15.332 1.981   0.60 17.38 ?  168 PHE   A CB   1 
ATOM   3835 C  CB   B PHE   A 1 168 ? 7.060  -15.784 1.907   0.40 18.66 ?  168 PHE   A CB   1 
ATOM   3836 C  CG   A PHE   A 1 168 ? 8.482  -16.029 2.310   0.60 16.96 ?  168 PHE   A CG   1 
ATOM   3837 C  CG   B PHE   A 1 168 ? 8.362  -16.439 2.290   0.40 17.45 ?  168 PHE   A CG   1 
ATOM   3838 C  CD1  A PHE   A 1 168 ? 9.660  -15.600 1.735   0.60 17.06 ?  168 PHE   A CD1  1 
ATOM   3839 C  CD1  B PHE   A 1 168 ? 9.538  -16.091 1.647   0.40 16.79 ?  168 PHE   A CD1  1 
ATOM   3840 C  CD2  A PHE   A 1 168 ? 8.515  -17.139 3.141   0.60 16.97 ?  168 PHE   A CD2  1 
ATOM   3841 C  CD2  B PHE   A 1 168 ? 8.407  -17.416 3.273   0.40 17.00 ?  168 PHE   A CD2  1 
ATOM   3842 C  CE1  A PHE   A 1 168 ? 10.849 -16.239 2.002   0.60 17.03 ?  168 PHE   A CE1  1 
ATOM   3843 C  CE1  B PHE   A 1 168 ? 10.735 -16.694 1.983   0.40 16.20 ?  168 PHE   A CE1  1 
ATOM   3844 C  CE2  A PHE   A 1 168 ? 9.712  -17.782 3.415   0.60 17.38 ?  168 PHE   A CE2  1 
ATOM   3845 C  CE2  B PHE   A 1 168 ? 9.603  -18.023 3.614   0.40 16.74 ?  168 PHE   A CE2  1 
ATOM   3846 C  CZ   A PHE   A 1 168 ? 10.875 -17.332 2.842   0.60 17.25 ?  168 PHE   A CZ   1 
ATOM   3847 C  CZ   B PHE   A 1 168 ? 10.766 -17.662 2.968   0.40 16.44 ?  168 PHE   A CZ   1 
ATOM   3848 H  H    A PHE   A 1 168 ? 5.170  -14.426 0.840   0.60 20.78 ?  168 PHE   A H    1 
ATOM   3849 H  H    B PHE   A 1 168 ? 4.577  -15.946 0.408   0.40 24.10 ?  168 PHE   A H    1 
ATOM   3850 H  HA   A PHE   A 1 168 ? 7.424  -15.438 -0.049  0.60 21.28 ?  168 PHE   A HA   1 
ATOM   3851 H  HA   B PHE   A 1 168 ? 7.213  -15.959 -0.111  0.40 23.43 ?  168 PHE   A HA   1 
ATOM   3852 H  HB2  A PHE   A 1 168 ? 7.341  -14.378 2.064   0.60 20.90 ?  168 PHE   A HB2  1 
ATOM   3853 H  HB2  B PHE   A 1 168 ? 7.202  -14.826 1.894   0.40 22.43 ?  168 PHE   A HB2  1 
ATOM   3854 H  HB3  A PHE   A 1 168 ? 6.520  -15.619 2.618   0.60 20.90 ?  168 PHE   A HB3  1 
ATOM   3855 H  HB3  B PHE   A 1 168 ? 6.401  -16.013 2.579   0.40 22.43 ?  168 PHE   A HB3  1 
ATOM   3856 H  HD1  A PHE   A 1 168 ? 9.650  -14.861 1.167   0.60 20.51 ?  168 PHE   A HD1  1 
ATOM   3857 H  HD1  B PHE   A 1 168 ? 9.524  -15.443 0.981   0.40 20.19 ?  168 PHE   A HD1  1 
ATOM   3858 H  HD2  A PHE   A 1 168 ? 7.726  -17.444 3.531   0.60 20.41 ?  168 PHE   A HD2  1 
ATOM   3859 H  HD2  B PHE   A 1 168 ? 7.625  -17.664 3.711   0.40 20.44 ?  168 PHE   A HD2  1 
ATOM   3860 H  HE1  A PHE   A 1 168 ? 11.639 -15.931 1.614   0.60 20.48 ?  168 PHE   A HE1  1 
ATOM   3861 H  HE1  B PHE   A 1 168 ? 11.520 -16.450 1.547   0.40 19.49 ?  168 PHE   A HE1  1 
ATOM   3862 H  HE2  A PHE   A 1 168 ? 9.723  -18.519 3.981   0.60 20.89 ?  168 PHE   A HE2  1 
ATOM   3863 H  HE2  B PHE   A 1 168 ? 9.622  -18.674 4.279   0.40 20.14 ?  168 PHE   A HE2  1 
ATOM   3864 H  HZ   A PHE   A 1 168 ? 11.681 -17.761 3.023   0.60 20.74 ?  168 PHE   A HZ   1 
ATOM   3865 H  HZ   B PHE   A 1 168 ? 11.573 -18.068 3.197   0.40 19.78 ?  168 PHE   A HZ   1 
ATOM   3866 N  N    A LEU   A 1 169 ? 7.269  -17.848 -0.249  0.60 20.60 ?  169 LEU   A N    1 
ATOM   3867 N  N    B LEU   A 1 169 ? 5.613  -18.373 1.263   0.40 22.20 ?  169 LEU   A N    1 
ATOM   3868 C  CA   A LEU   A 1 169 ? 7.090  -19.276 -0.431  0.60 22.68 ?  169 LEU   A CA   1 
ATOM   3869 C  CA   B LEU   A 1 169 ? 5.571  -19.839 1.324   0.40 23.75 ?  169 LEU   A CA   1 
ATOM   3870 C  C    A LEU   A 1 169 ? 7.925  -20.030 0.588   0.60 22.64 ?  169 LEU   A C    1 
ATOM   3871 C  C    B LEU   A 1 169 ? 5.005  -20.432 0.039   0.40 24.83 ?  169 LEU   A C    1 
ATOM   3872 O  O    A LEU   A 1 169 ? 7.384  -20.517 1.583   0.60 23.26 ?  169 LEU   A O    1 
ATOM   3873 O  O    B LEU   A 1 169 ? 4.196  -19.809 -0.647  0.40 25.15 ?  169 LEU   A O    1 
ATOM   3874 C  CB   A LEU   A 1 169 ? 7.439  -19.684 -1.868  0.60 23.79 ?  169 LEU   A CB   1 
ATOM   3875 C  CB   B LEU   A 1 169 ? 4.732  -20.316 2.514   0.40 24.18 ?  169 LEU   A CB   1 
ATOM   3876 C  CG   A LEU   A 1 169 ? 7.109  -21.127 -2.262  0.60 24.76 ?  169 LEU   A CG   1 
ATOM   3877 C  CG   B LEU   A 1 169 ? 5.134  -21.611 3.236   0.40 24.52 ?  169 LEU   A CG   1 
ATOM   3878 C  CD1  A LEU   A 1 169 ? 5.682  -21.483 -1.881  0.60 25.14 ?  169 LEU   A CD1  1 
ATOM   3879 C  CD1  B LEU   A 1 169 ? 4.054  -22.020 4.231   0.40 24.45 ?  169 LEU   A CD1  1 
ATOM   3880 C  CD2  A LEU   A 1 169 ? 7.326  -21.341 -3.754  0.60 24.90 ?  169 LEU   A CD2  1 
ATOM   3881 C  CD2  B LEU   A 1 169 ? 5.446  -22.762 2.284   0.40 24.96 ?  169 LEU   A CD2  1 
ATOM   3882 O  OXT  A LEU   A 1 169 ? 9.142  -20.149 0.460   0.60 21.88 -1 169 LEU   A OXT  1 
ATOM   3883 O  OXT  B LEU   A 1 169 ? 5.338  -21.558 -0.335  0.40 25.44 -1 169 LEU   A OXT  1 
ATOM   3884 H  H    A LEU   A 1 169 ? 7.966  -17.523 -0.644  0.60 24.77 ?  169 LEU   A H    1 
ATOM   3885 H  H    B LEU   A 1 169 ? 5.048  -17.979 1.779   0.40 26.68 ?  169 LEU   A H    1 
ATOM   3886 H  HA   A LEU   A 1 169 ? 6.170  -19.503 -0.260  0.60 27.26 ?  169 LEU   A HA   1 
ATOM   3887 H  HA   B LEU   A 1 169 ? 6.475  -20.172 1.431   0.40 28.54 ?  169 LEU   A HA   1 
ATOM   3888 H  HB2  A LEU   A 1 169 ? 6.950  -19.104 -2.475  0.60 28.59 ?  169 LEU   A HB2  1 
ATOM   3889 H  HB2  B LEU   A 1 169 ? 4.743  -19.619 3.181   0.40 29.06 ?  169 LEU   A HB2  1 
ATOM   3890 H  HB3  A LEU   A 1 169 ? 8.390  -19.560 -2.003  0.60 28.59 ?  169 LEU   A HB3  1 
ATOM   3891 H  HB3  B LEU   A 1 169 ? 3.826  -20.442 2.200   0.40 29.06 ?  169 LEU   A HB3  1 
ATOM   3892 H  HG   A LEU   A 1 169 ? 7.704  -21.728 -1.788  0.60 29.75 ?  169 LEU   A HG   1 
ATOM   3893 H  HG   B LEU   A 1 169 ? 5.934  -21.436 3.750   0.40 29.46 ?  169 LEU   A HG   1 
ATOM   3894 H  HD11 A LEU   A 1 169 ? 5.430  -22.306 -2.327  0.60 30.22 ?  169 LEU   A HD11 1 
ATOM   3895 H  HD11 B LEU   A 1 169 ? 4.275  -22.891 4.596   0.40 29.38 ?  169 LEU   A HD11 1 
ATOM   3896 H  HD12 A LEU   A 1 169 ? 5.631  -21.600 -0.919  0.60 30.22 ?  169 LEU   A HD12 1 
ATOM   3897 H  HD12 B LEU   A 1 169 ? 4.019  -21.364 4.944   0.40 29.38 ?  169 LEU   A HD12 1 
ATOM   3898 H  HD13 A LEU   A 1 169 ? 5.092  -20.764 -2.158  0.60 30.22 ?  169 LEU   A HD13 1 
ATOM   3899 H  HD13 B LEU   A 1 169 ? 3.201  -22.060 3.772   0.40 29.38 ?  169 LEU   A HD13 1 
ATOM   3900 H  HD21 A LEU   A 1 169 ? 7.120  -22.263 -3.975  0.60 29.92 ?  169 LEU   A HD21 1 
ATOM   3901 H  HD21 B LEU   A 1 169 ? 5.655  -23.556 2.806   0.40 29.99 ?  169 LEU   A HD21 1 
ATOM   3902 H  HD22 A LEU   A 1 169 ? 6.741  -20.744 -4.247  0.60 29.92 ?  169 LEU   A HD22 1 
ATOM   3903 H  HD22 B LEU   A 1 169 ? 4.673  -22.930 1.726   0.40 29.99 ?  169 LEU   A HD22 1 
ATOM   3904 H  HD23 A LEU   A 1 169 ? 8.252  -21.149 -3.969  0.60 29.92 ?  169 LEU   A HD23 1 
ATOM   3905 H  HD23 B LEU   A 1 169 ? 6.208  -22.520 1.736   0.40 29.99 ?  169 LEU   A HD23 1 
ATOM   3906 N  N    A SER   B 1 1   ? 50.859 -9.272  -23.753 0.60 28.60 ?  1   SER   B N    1 
ATOM   3907 N  N    B SER   B 1 1   ? 50.820 -9.281  -23.756 0.40 26.38 ?  1   SER   B N    1 
ATOM   3908 C  CA   A SER   B 1 1   ? 51.356 -10.322 -22.841 0.60 28.68 ?  1   SER   B CA   1 
ATOM   3909 C  CA   B SER   B 1 1   ? 51.284 -10.272 -22.764 0.40 26.27 ?  1   SER   B CA   1 
ATOM   3910 C  C    A SER   B 1 1   ? 50.284 -11.370 -22.588 0.60 27.53 ?  1   SER   B C    1 
ATOM   3911 C  C    B SER   B 1 1   ? 50.209 -11.322 -22.513 0.40 24.97 ?  1   SER   B C    1 
ATOM   3912 O  O    A SER   B 1 1   ? 49.090 -11.155 -22.839 0.60 27.32 ?  1   SER   B O    1 
ATOM   3913 O  O    B SER   B 1 1   ? 49.033 -11.142 -22.856 0.40 24.53 ?  1   SER   B O    1 
ATOM   3914 C  CB   A SER   B 1 1   ? 51.816 -9.718  -21.517 0.60 29.63 ?  1   SER   B CB   1 
ATOM   3915 C  CB   B SER   B 1 1   ? 51.655 -9.589  -21.451 0.40 27.23 ?  1   SER   B CB   1 
ATOM   3916 O  OG   A SER   B 1 1   ? 50.711 -9.402  -20.693 0.60 31.19 ?  1   SER   B OG   1 
ATOM   3917 O  OG   B SER   B 1 1   ? 50.505 -9.387  -20.651 0.40 28.50 ?  1   SER   B OG   1 
ATOM   3918 H  H1   A SER   B 1 1   ? 50.784 -9.612  -24.570 0.60 34.36 ?  1   SER   B H1   1 
ATOM   3919 H  H1   B SER   B 1 1   ? 51.528 -8.900  -24.134 0.40 31.70 ?  1   SER   B H1   1 
ATOM   3920 H  H2   A SER   B 1 1   ? 50.069 -8.991  -23.467 0.60 34.36 ?  1   SER   B H2   1 
ATOM   3921 H  H2   B SER   B 1 1   ? 50.335 -9.695  -24.372 0.40 31.70 ?  1   SER   B H2   1 
ATOM   3922 H  H3   A SER   B 1 1   ? 51.438 -8.600  -23.757 0.60 34.36 ?  1   SER   B H3   1 
ATOM   3923 H  H3   B SER   B 1 1   ? 50.331 -8.668  -23.344 0.40 31.70 ?  1   SER   B H3   1 
ATOM   3924 H  HA   A SER   B 1 1   ? 52.112 -10.753 -23.260 0.60 34.46 ?  1   SER   B HA   1 
ATOM   3925 H  HA   B SER   B 1 1   ? 52.071 -10.709 -23.117 0.40 31.57 ?  1   SER   B HA   1 
ATOM   3926 H  HB2  A SER   B 1 1   ? 52.376 -10.364 -21.062 0.60 35.59 ?  1   SER   B HB2  1 
ATOM   3927 H  HB2  B SER   B 1 1   ? 52.285 -10.153 -20.978 0.40 32.72 ?  1   SER   B HB2  1 
ATOM   3928 H  HB3  A SER   B 1 1   ? 52.319 -8.909  -21.697 0.60 35.59 ?  1   SER   B HB3  1 
ATOM   3929 H  HB3  B SER   B 1 1   ? 52.058 -8.727  -21.643 0.40 32.72 ?  1   SER   B HB3  1 
ATOM   3930 H  HG   A SER   B 1 1   ? 50.968 -8.933  -20.044 0.60 37.46 ?  1   SER   B HG   1 
ATOM   3931 H  HG   B SER   B 1 1   ? 50.670 -8.813  -20.061 0.40 34.25 ?  1   SER   B HG   1 
ATOM   3932 N  N    A MET   B 1 2   ? 50.731 -12.506 -22.072 0.60 26.37 ?  2   MET   B N    1 
ATOM   3933 N  N    B MET   B 1 2   ? 50.632 -12.418 -21.896 0.40 23.91 ?  2   MET   B N    1 
ATOM   3934 C  CA   A MET   B 1 2   ? 49.903 -13.691 -21.907 0.60 25.95 ?  2   MET   B CA   1 
ATOM   3935 C  CA   B MET   B 1 2   ? 49.809 -13.608 -21.726 0.40 23.33 ?  2   MET   B CA   1 
ATOM   3936 C  C    A MET   B 1 2   ? 49.660 -13.888 -20.418 0.60 23.19 ?  2   MET   B C    1 
ATOM   3937 C  C    B MET   B 1 2   ? 49.537 -13.794 -20.240 0.40 21.61 ?  2   MET   B C    1 
ATOM   3938 O  O    A MET   B 1 2   ? 50.601 -14.120 -19.656 0.60 23.20 ?  2   MET   B O    1 
ATOM   3939 O  O    B MET   B 1 2   ? 50.437 -14.166 -19.480 0.40 22.03 ?  2   MET   B O    1 
ATOM   3940 C  CB   A MET   B 1 2   ? 50.617 -14.891 -22.515 0.60 29.40 ?  2   MET   B CB   1 
ATOM   3941 C  CB   B MET   B 1 2   ? 50.560 -14.803 -22.295 0.40 25.20 ?  2   MET   B CB   1 
ATOM   3942 C  CG   A MET   B 1 2   ? 49.772 -16.148 -22.623 0.60 32.54 ?  2   MET   B CG   1 
ATOM   3943 C  CG   B MET   B 1 2   ? 49.688 -15.966 -22.745 0.40 26.56 ?  2   MET   B CG   1 
ATOM   3944 S  SD   A MET   B 1 2   ? 50.597 -17.406 -23.616 0.60 35.53 ?  2   MET   B SD   1 
ATOM   3945 S  SD   B MET   B 1 2   ? 50.570 -17.032 -23.895 0.40 27.83 ?  2   MET   B SD   1 
ATOM   3946 C  CE   A MET   B 1 2   ? 51.121 -16.389 -24.994 0.60 35.95 ?  2   MET   B CE   1 
ATOM   3947 C  CE   B MET   B 1 2   ? 51.426 -15.811 -24.860 0.40 28.23 ?  2   MET   B CE   1 
ATOM   3948 H  H    A MET   B 1 2   ? 51.539 -12.621 -21.796 0.60 31.69 ?  2   MET   B H    1 
ATOM   3949 H  H    B MET   B 1 2   ? 51.424 -12.507 -21.565 0.40 28.74 ?  2   MET   B H    1 
ATOM   3950 H  HA   A MET   B 1 2   ? 49.061 -13.577 -22.366 0.60 31.19 ?  2   MET   B HA   1 
ATOM   3951 H  HA   B MET   B 1 2   ? 48.980 -13.514 -22.220 0.40 28.04 ?  2   MET   B HA   1 
ATOM   3952 H  HB2  A MET   B 1 2   ? 50.899 -14.618 -23.398 0.60 35.33 ?  2   MET   B HB2  1 
ATOM   3953 H  HB2  B MET   B 1 2   ? 51.078 -14.458 -23.032 0.40 30.28 ?  2   MET   B HB2  1 
ATOM   3954 H  HB3  A MET   B 1 2   ? 51.393 -15.117 -21.982 0.60 35.33 ?  2   MET   B HB3  1 
ATOM   3955 H  HB3  B MET   B 1 2   ? 51.159 -15.162 -21.632 0.40 30.28 ?  2   MET   B HB3  1 
ATOM   3956 H  HG2  A MET   B 1 2   ? 49.621 -16.508 -21.732 0.60 39.09 ?  2   MET   B HG2  1 
ATOM   3957 H  HG2  B MET   B 1 2   ? 49.427 -16.492 -21.965 0.40 31.91 ?  2   MET   B HG2  1 
ATOM   3958 H  HG3  A MET   B 1 2   ? 48.926 -15.936 -23.048 0.60 39.09 ?  2   MET   B HG3  1 
ATOM   3959 H  HG3  B MET   B 1 2   ? 48.902 -15.640 -23.201 0.40 31.91 ?  2   MET   B HG3  1 
ATOM   3960 H  HE1  A MET   B 1 2   ? 51.278 -16.955 -25.752 0.60 43.19 ?  2   MET   B HE1  1 
ATOM   3961 H  HE1  B MET   B 1 2   ? 51.626 -16.213 -25.694 0.40 33.92 ?  2   MET   B HE1  1 
ATOM   3962 H  HE2  A MET   B 1 2   ? 50.414 -15.748 -25.194 0.60 43.19 ?  2   MET   B HE2  1 
ATOM   3963 H  HE2  B MET   B 1 2   ? 50.838 -15.047 -24.989 0.40 33.92 ?  2   MET   B HE2  1 
ATOM   3964 H  HE3  A MET   B 1 2   ? 51.937 -15.910 -24.757 0.60 43.19 ?  2   MET   B HE3  1 
ATOM   3965 H  HE3  B MET   B 1 2   ? 52.245 -15.536 -24.403 0.40 33.92 ?  2   MET   B HE3  1 
ATOM   3966 N  N    A VAL   B 1 3   ? 48.401 -13.766 -20.006 0.60 20.71 ?  3   VAL   B N    1 
ATOM   3967 N  N    B VAL   B 1 3   ? 48.306 -13.520 -19.827 0.40 19.68 ?  3   VAL   B N    1 
ATOM   3968 C  CA   A VAL   B 1 3   ? 47.991 -13.999 -18.629 0.60 19.50 ?  3   VAL   B CA   1 
ATOM   3969 C  CA   B VAL   B 1 3   ? 47.861 -13.783 -18.464 0.40 18.76 ?  3   VAL   B CA   1 
ATOM   3970 C  C    A VAL   B 1 3   ? 46.755 -14.888 -18.645 0.60 17.51 ?  3   VAL   B C    1 
ATOM   3971 C  C    B VAL   B 1 3   ? 46.618 -14.658 -18.511 0.40 17.34 ?  3   VAL   B C    1 
ATOM   3972 O  O    A VAL   B 1 3   ? 46.061 -15.012 -19.657 0.60 17.25 ?  3   VAL   B O    1 
ATOM   3973 O  O    B VAL   B 1 3   ? 45.799 -14.566 -19.430 0.40 17.44 ?  3   VAL   B O    1 
ATOM   3974 C  CB   A VAL   B 1 3   ? 47.702 -12.681 -17.879 0.60 21.05 ?  3   VAL   B CB   1 
ATOM   3975 C  CB   B VAL   B 1 3   ? 47.584 -12.490 -17.667 0.40 19.71 ?  3   VAL   B CB   1 
ATOM   3976 C  CG1  A VAL   B 1 3   ? 48.962 -11.823 -17.791 0.60 21.78 ?  3   VAL   B CG1  1 
ATOM   3977 C  CG1  B VAL   B 1 3   ? 48.855 -11.667 -17.519 0.40 20.21 ?  3   VAL   B CG1  1 
ATOM   3978 C  CG2  A VAL   B 1 3   ? 46.576 -11.918 -18.565 0.60 21.67 ?  3   VAL   B CG2  1 
ATOM   3979 C  CG2  B VAL   B 1 3   ? 46.479 -11.681 -18.330 0.40 19.98 ?  3   VAL   B CG2  1 
ATOM   3980 H  H    A VAL   B 1 3   ? 47.753 -13.544 -20.522 0.60 24.89 ?  3   VAL   B H    1 
ATOM   3981 H  H    B VAL   B 1 3   ? 47.705 -13.174 -20.333 0.40 23.66 ?  3   VAL   B H    1 
ATOM   3982 H  HA   A VAL   B 1 3   ? 48.701 -14.469 -18.158 0.60 23.44 ?  3   VAL   B HA   1 
ATOM   3983 H  HA   B VAL   B 1 3   ? 48.552 -14.275 -18.000 0.40 22.56 ?  3   VAL   B HA   1 
ATOM   3984 H  HB   A VAL   B 1 3   ? 47.418 -12.891 -16.975 0.60 25.31 ?  3   VAL   B HB   1 
ATOM   3985 H  HB   B VAL   B 1 3   ? 47.282 -12.735 -16.780 0.40 23.69 ?  3   VAL   B HB   1 
ATOM   3986 H  HG11 A VAL   B 1 3   ? 48.754 -11.010 -17.305 0.60 26.18 ?  3   VAL   B HG11 1 
ATOM   3987 H  HG11 B VAL   B 1 3   ? 48.653 -10.870 -17.006 0.40 24.29 ?  3   VAL   B HG11 1 
ATOM   3988 H  HG12 A VAL   B 1 3   ? 49.651 -12.322 -17.325 0.60 26.18 ?  3   VAL   B HG12 1 
ATOM   3989 H  HG12 B VAL   B 1 3   ? 49.522 -12.199 -17.058 0.40 24.29 ?  3   VAL   B HG12 1 
ATOM   3990 H  HG13 A VAL   B 1 3   ? 49.258 -11.607 -18.688 0.60 26.18 ?  3   VAL   B HG13 1 
ATOM   3991 H  HG13 B VAL   B 1 3   ? 49.177 -11.423 -18.400 0.40 24.29 ?  3   VAL   B HG13 1 
ATOM   3992 H  HG21 A VAL   B 1 3   ? 46.502 -11.040 -18.164 0.60 26.05 ?  3   VAL   B HG21 1 
ATOM   3993 H  HG21 B VAL   B 1 3   ? 46.416 -10.820 -17.893 0.40 24.02 ?  3   VAL   B HG21 1 
ATOM   3994 H  HG22 A VAL   B 1 3   ? 46.778 -11.835 -19.510 0.60 26.05 ?  3   VAL   B HG22 1 
ATOM   3995 H  HG22 B VAL   B 1 3   ? 46.691 -11.564 -19.268 0.40 24.02 ?  3   VAL   B HG22 1 
ATOM   3996 H  HG23 A VAL   B 1 3   ? 45.744 -12.406 -18.447 0.60 26.05 ?  3   VAL   B HG23 1 
ATOM   3997 H  HG23 B VAL   B 1 3   ? 45.638 -12.160 -18.240 0.40 24.02 ?  3   VAL   B HG23 1 
ATOM   3998 N  N    . ASN   B 1 4   ? 46.485 -15.513 -17.499 1.00 16.21 ?  4   ASN   B N    1 
ATOM   3999 C  CA   . ASN   B 1 4   ? 45.345 -16.426 -17.376 1.00 15.09 ?  4   ASN   B CA   1 
ATOM   4000 C  C    . ASN   B 1 4   ? 45.288 -17.396 -18.554 1.00 15.39 ?  4   ASN   B C    1 
ATOM   4001 O  O    . ASN   B 1 4   ? 44.229 -17.649 -19.122 1.00 16.09 ?  4   ASN   B O    1 
ATOM   4002 C  CB   . ASN   B 1 4   ? 44.023 -15.668 -17.211 1.00 14.42 ?  4   ASN   B CB   1 
ATOM   4003 C  CG   . ASN   B 1 4   ? 43.979 -14.854 -15.931 1.00 13.98 ?  4   ASN   B CG   1 
ATOM   4004 O  OD1  . ASN   B 1 4   ? 44.257 -15.364 -14.848 1.00 13.82 ?  4   ASN   B OD1  1 
ATOM   4005 N  ND2  . ASN   B 1 4   ? 43.642 -13.575 -16.054 1.00 14.61 ?  4   ASN   B ND2  1 
ATOM   4006 H  H    A ASN   B 1 4   ? 46.946 -15.428 -16.779 0.60 19.49 ?  4   ASN   B H    1 
ATOM   4007 H  H    B ASN   B 1 4   ? 47.055 -15.588 -16.860 0.40 19.49 ?  4   ASN   B H    1 
ATOM   4008 H  HA   . ASN   B 1 4   ? 45.475 -16.956 -16.574 1.00 18.15 ?  4   ASN   B HA   1 
ATOM   4009 H  HB2  . ASN   B 1 4   ? 43.905 -15.062 -17.956 1.00 17.35 ?  4   ASN   B HB2  1 
ATOM   4010 H  HB3  . ASN   B 1 4   ? 43.293 -16.309 -17.184 1.00 17.35 ?  4   ASN   B HB3  1 
ATOM   4011 H  HD21 . ASN   B 1 4   ? 43.607 -13.068 -15.357 1.00 17.57 ?  4   ASN   B HD21 1 
ATOM   4012 H  HD22 . ASN   B 1 4   ? 43.461 -13.247 -16.828 1.00 17.57 ?  4   ASN   B HD22 1 
ATOM   4013 N  N    . SER   B 1 5   ? 46.446 -17.932 -18.933 1.00 16.29 ?  5   SER   B N    1 
ATOM   4014 C  CA   . SER   B 1 5   ? 46.545 -18.848 -20.069 1.00 18.44 ?  5   SER   B CA   1 
ATOM   4015 C  C    . SER   B 1 5   ? 46.529 -20.283 -19.552 1.00 19.97 ?  5   SER   B C    1 
ATOM   4016 O  O    . SER   B 1 5   ? 47.535 -20.982 -19.523 1.00 22.56 ?  5   SER   B O    1 
ATOM   4017 C  CB   . SER   B 1 5   ? 47.804 -18.553 -20.882 1.00 19.89 ?  5   SER   B CB   1 
ATOM   4018 O  OG   . SER   B 1 5   ? 48.970 -18.747 -20.100 1.00 22.58 ?  5   SER   B OG   1 
ATOM   4019 H  H    . SER   B 1 5   ? 47.199 -17.782 -18.543 1.00 19.59 ?  5   SER   B H    1 
ATOM   4020 H  HA   . SER   B 1 5   ? 45.777 -18.726 -20.647 1.00 22.17 ?  5   SER   B HA   1 
ATOM   4021 H  HB2  . SER   B 1 5   ? 47.827 -19.145 -21.653 1.00 23.91 ?  5   SER   B HB2  1 
ATOM   4022 H  HB3  . SER   B 1 5   ? 47.765 -17.631 -21.179 1.00 23.91 ?  5   SER   B HB3  1 
ATOM   4023 H  HG   . SER   B 1 5   ? 49.026 -19.552 -19.869 1.00 27.13 ?  5   SER   B HG   1 
ATOM   4024 N  N    . PHE   B 1 6   ? 45.348 -20.696 -19.107 1.00 20.17 ?  6   PHE   B N    1 
ATOM   4025 C  CA   . PHE   B 1 6   ? 45.153 -22.042 -18.589 1.00 19.93 ?  6   PHE   B CA   1 
ATOM   4026 C  C    . PHE   B 1 6   ? 45.071 -23.022 -19.749 1.00 23.06 ?  6   PHE   B C    1 
ATOM   4027 O  O    . PHE   B 1 6   ? 44.400 -22.750 -20.748 1.00 25.29 ?  6   PHE   B O    1 
ATOM   4028 C  CB   . PHE   B 1 6   ? 43.866 -22.099 -17.767 1.00 17.87 ?  6   PHE   B CB   1 
ATOM   4029 C  CG   . PHE   B 1 6   ? 43.888 -21.231 -16.539 1.00 16.11 ?  6   PHE   B CG   1 
ATOM   4030 C  CD1  . PHE   B 1 6   ? 44.392 -21.712 -15.348 1.00 15.08 ?  6   PHE   B CD1  1 
ATOM   4031 C  CD2  . PHE   B 1 6   ? 43.397 -19.935 -16.578 1.00 15.94 ?  6   PHE   B CD2  1 
ATOM   4032 C  CE1  . PHE   B 1 6   ? 44.400 -20.921 -14.211 1.00 14.36 ?  6   PHE   B CE1  1 
ATOM   4033 C  CE2  . PHE   B 1 6   ? 43.409 -19.133 -15.452 1.00 16.39 ?  6   PHE   B CE2  1 
ATOM   4034 C  CZ   . PHE   B 1 6   ? 43.918 -19.618 -14.269 1.00 15.23 ?  6   PHE   B CZ   1 
ATOM   4035 H  H    . PHE   B 1 6   ? 44.638 -20.214 -19.096 1.00 24.25 ?  6   PHE   B H    1 
ATOM   4036 H  HA   . PHE   B 1 6   ? 45.897 -22.293 -18.022 1.00 23.96 ?  6   PHE   B HA   1 
ATOM   4037 H  HB2  . PHE   B 1 6   ? 43.124 -21.808 -18.323 1.00 21.48 ?  6   PHE   B HB2  1 
ATOM   4038 H  HB3  . PHE   B 1 6   ? 43.715 -23.015 -17.480 1.00 21.48 ?  6   PHE   B HB3  1 
ATOM   4039 H  HD1  . PHE   B 1 6   ? 44.728 -22.580 -15.305 1.00 18.14 ?  6   PHE   B HD1  1 
ATOM   4040 H  HD2  . PHE   B 1 6   ? 43.048 -19.605 -17.374 1.00 19.17 ?  6   PHE   B HD2  1 
ATOM   4041 H  HE1  . PHE   B 1 6   ? 44.755 -21.248 -13.413 1.00 17.27 ?  6   PHE   B HE1  1 
ATOM   4042 H  HE2  . PHE   B 1 6   ? 43.071 -18.268 -15.494 1.00 19.71 ?  6   PHE   B HE2  1 
ATOM   4043 H  HZ   . PHE   B 1 6   ? 43.924 -19.084 -13.508 1.00 18.32 ?  6   PHE   B HZ   1 
ATOM   4044 N  N    . SER   B 1 7   ? 45.768 -24.153 -19.621 1.00 24.14 ?  7   SER   B N    1 
ATOM   4045 C  CA   . SER   B 1 7   ? 45.838 -25.143 -20.687 1.00 26.47 ?  7   SER   B CA   1 
ATOM   4046 C  C    . SER   B 1 7   ? 45.773 -26.547 -20.104 1.00 25.87 ?  7   SER   B C    1 
ATOM   4047 O  O    . SER   B 1 7   ? 46.368 -26.827 -19.060 1.00 27.01 ?  7   SER   B O    1 
ATOM   4048 C  CB   . SER   B 1 7   ? 47.133 -24.984 -21.496 1.00 29.35 ?  7   SER   B CB   1 
ATOM   4049 O  OG   . SER   B 1 7   ? 47.096 -25.767 -22.676 1.00 31.37 ?  7   SER   B OG   1 
ATOM   4050 H  H    . SER   B 1 7   ? 46.222 -24.366 -18.917 1.00 29.01 ?  7   SER   B H    1 
ATOM   4051 H  HA   . SER   B 1 7   ? 45.088 -25.028 -21.285 1.00 31.81 ?  7   SER   B HA   1 
ATOM   4052 H  HB2  . SER   B 1 7   ? 47.241 -24.049 -21.738 1.00 35.27 ?  7   SER   B HB2  1 
ATOM   4053 H  HB3  . SER   B 1 7   ? 47.885 -25.270 -20.953 1.00 35.27 ?  7   SER   B HB3  1 
ATOM   4054 H  HG   . SER   B 1 7   ? 47.809 -25.665 -23.111 1.00 37.68 ?  7   SER   B HG   1 
ATOM   4055 N  N    . GLY   B 1 8   ? 45.052 -27.429 -20.795 1.00 25.84 ?  8   GLY   B N    1 
ATOM   4056 C  CA   . GLY   B 1 8   ? 45.012 -28.824 -20.417 1.00 24.90 ?  8   GLY   B CA   1 
ATOM   4057 C  C    . GLY   B 1 8   ? 44.075 -29.152 -19.284 1.00 23.57 ?  8   GLY   B C    1 
ATOM   4058 O  O    . GLY   B 1 8   ? 44.216 -30.217 -18.668 1.00 24.79 ?  8   GLY   B O    1 
ATOM   4059 H  H    . GLY   B 1 8   ? 44.582 -27.232 -21.485 1.00 31.05 ?  8   GLY   B H    1 
ATOM   4060 H  HA2  . GLY   B 1 8   ? 44.745 -29.347 -21.187 1.00 29.93 ?  8   GLY   B HA2  1 
ATOM   4061 H  HA3  . GLY   B 1 8   ? 45.899 -29.104 -20.152 1.00 29.93 ?  8   GLY   B HA3  1 
ATOM   4062 N  N    . TYR   B 1 9   ? 43.102 -28.291 -18.998 1.00 21.79 ?  9   TYR   B N    1 
ATOM   4063 C  CA   . TYR   B 1 9   ? 42.148 -28.567 -17.938 1.00 19.74 ?  9   TYR   B CA   1 
ATOM   4064 C  C    . TYR   B 1 9   ? 40.966 -29.365 -18.456 1.00 19.15 ?  9   TYR   B C    1 
ATOM   4065 O  O    . TYR   B 1 9   ? 40.548 -29.231 -19.610 1.00 21.02 ?  9   TYR   B O    1 
ATOM   4066 C  CB   . TYR   B 1 9   ? 41.638 -27.281 -17.290 1.00 18.96 ?  9   TYR   B CB   1 
ATOM   4067 C  CG   . TYR   B 1 9   ? 42.664 -26.651 -16.379 1.00 18.28 ?  9   TYR   B CG   1 
ATOM   4068 C  CD1  . TYR   B 1 9   ? 43.748 -25.965 -16.904 1.00 18.55 ?  9   TYR   B CD1  1 
ATOM   4069 C  CD2  . TYR   B 1 9   ? 42.566 -26.761 -15.000 1.00 17.35 ?  9   TYR   B CD2  1 
ATOM   4070 C  CE1  . TYR   B 1 9   ? 44.702 -25.402 -16.083 1.00 18.67 ?  9   TYR   B CE1  1 
ATOM   4071 C  CE2  . TYR   B 1 9   ? 43.516 -26.195 -14.167 1.00 17.59 ?  9   TYR   B CE2  1 
ATOM   4072 C  CZ   . TYR   B 1 9   ? 44.584 -25.514 -14.717 1.00 18.52 ?  9   TYR   B CZ   1 
ATOM   4073 O  OH   . TYR   B 1 9   ? 45.540 -24.960 -13.902 1.00 19.19 ?  9   TYR   B OH   1 
ATOM   4074 H  H    . TYR   B 1 9   ? 42.958 -27.553 -19.417 1.00 26.19 ?  9   TYR   B H    1 
ATOM   4075 H  HA   . TYR   B 1 9   ? 42.577 -29.093 -17.252 1.00 23.73 ?  9   TYR   B HA   1 
ATOM   4076 H  HB2  . TYR   B 1 9   ? 41.404 -26.637 -17.979 1.00 22.80 ?  9   TYR   B HB2  1 
ATOM   4077 H  HB3  . TYR   B 1 9   ? 40.862 -27.497 -16.756 1.00 22.80 ?  9   TYR   B HB3  1 
ATOM   4078 H  HD1  . TYR   B 1 9   ? 43.831 -25.885 -17.828 1.00 22.30 ?  9   TYR   B HD1  1 
ATOM   4079 H  HD2  . TYR   B 1 9   ? 41.844 -27.225 -14.629 1.00 20.86 ?  9   TYR   B HD2  1 
ATOM   4080 H  HE1  . TYR   B 1 9   ? 45.415 -24.942 -16.451 1.00 22.45 ?  9   TYR   B HE1  1 
ATOM   4081 H  HE2  . TYR   B 1 9   ? 43.429 -26.282 -13.244 1.00 21.15 ?  9   TYR   B HE2  1 
ATOM   4082 H  HH   . TYR   B 1 9   ? 46.116 -24.574 -14.369 1.00 23.07 ?  9   TYR   B HH   1 
ATOM   4083 N  N    . LEU   B 1 10  ? 40.441 -30.212 -17.579 1.00 17.46 ?  10  LEU   B N    1 
ATOM   4084 C  CA   . LEU   B 1 10  ? 39.233 -30.973 -17.838 1.00 17.28 ?  10  LEU   B CA   1 
ATOM   4085 C  C    . LEU   B 1 10  ? 38.047 -30.201 -17.274 1.00 17.12 ?  10  LEU   B C    1 
ATOM   4086 O  O    . LEU   B 1 10  ? 38.067 -29.779 -16.113 1.00 16.72 ?  10  LEU   B O    1 
ATOM   4087 C  CB   . LEU   B 1 10  ? 39.347 -32.337 -17.158 1.00 18.36 ?  10  LEU   B CB   1 
ATOM   4088 C  CG   . LEU   B 1 10  ? 38.220 -33.311 -17.477 1.00 20.21 ?  10  LEU   B CG   1 
ATOM   4089 C  CD1  . LEU   B 1 10  ? 38.325 -33.792 -18.918 1.00 21.49 ?  10  LEU   B CD1  1 
ATOM   4090 C  CD2  . LEU   B 1 10  ? 38.229 -34.480 -16.508 1.00 21.52 ?  10  LEU   B CD2  1 
ATOM   4091 H  H    . LEU   B 1 10  ? 40.770 -30.358 -16.794 1.00 20.99 ?  10  LEU   B H    1 
ATOM   4092 H  HA   . LEU   B 1 10  ? 39.112 -31.101 -18.789 1.00 20.78 ?  10  LEU   B HA   1 
ATOM   4093 H  HB2  . LEU   B 1 10  ? 40.181 -32.753 -17.433 1.00 22.08 ?  10  LEU   B HB2  1 
ATOM   4094 H  HB3  . LEU   B 1 10  ? 39.356 -32.206 -16.194 1.00 22.08 ?  10  LEU   B HB3  1 
ATOM   4095 H  HG   . LEU   B 1 10  ? 37.373 -32.851 -17.378 1.00 24.30 ?  10  LEU   B HG   1 
ATOM   4096 H  HD11 . LEU   B 1 10  ? 37.651 -34.470 -19.071 1.00 25.83 ?  10  LEU   B HD11 1 
ATOM   4097 H  HD12 . LEU   B 1 10  ? 38.176 -33.038 -19.512 1.00 25.83 ?  10  LEU   B HD12 1 
ATOM   4098 H  HD13 . LEU   B 1 10  ? 39.208 -34.160 -19.064 1.00 25.83 ?  10  LEU   B HD13 1 
ATOM   4099 H  HD21 . LEU   B 1 10  ? 37.505 -35.079 -16.739 1.00 25.87 ?  10  LEU   B HD21 1 
ATOM   4100 H  HD22 . LEU   B 1 10  ? 39.079 -34.936 -16.578 1.00 25.87 ?  10  LEU   B HD22 1 
ATOM   4101 H  HD23 . LEU   B 1 10  ? 38.105 -34.138 -15.609 1.00 25.87 ?  10  LEU   B HD23 1 
ATOM   4102 N  N    . LYS   B 1 11  ? 37.020 -30.019 -18.095 1.00 18.06 ?  11  LYS   B N    1 
ATOM   4103 C  CA   . LYS   B 1 11  ? 35.825 -29.301 -17.678 1.00 20.31 ?  11  LYS   B CA   1 
ATOM   4104 C  C    . LYS   B 1 11  ? 34.945 -30.226 -16.843 1.00 19.54 ?  11  LYS   B C    1 
ATOM   4105 O  O    . LYS   B 1 11  ? 34.557 -31.306 -17.303 1.00 21.24 ?  11  LYS   B O    1 
ATOM   4106 C  CB   . LYS   B 1 11  ? 35.080 -28.821 -18.923 1.00 24.34 ?  11  LYS   B CB   1 
ATOM   4107 C  CG   . LYS   B 1 11  ? 33.961 -27.825 -18.675 1.00 28.10 ?  11  LYS   B CG   1 
ATOM   4108 C  CD   . LYS   B 1 11  ? 33.214 -27.545 -19.976 1.00 31.04 ?  11  LYS   B CD   1 
ATOM   4109 C  CE   . LYS   B 1 11  ? 32.182 -26.443 -19.817 1.00 33.30 ?  11  LYS   B CE   1 
ATOM   4110 N  NZ   . LYS   B 1 11  ? 32.816 -25.102 -19.695 1.00 34.61 ?  11  LYS   B NZ   1 
ATOM   4111 H  H    . LYS   B 1 11  ? 36.985 -30.311 -18.906 1.00 21.71 ?  11  LYS   B H    1 
ATOM   4112 H  HA   . LYS   B 1 11  ? 36.073 -28.532 -17.143 1.00 24.41 ?  11  LYS   B HA   1 
ATOM   4113 H  HB2  . LYS   B 1 11  ? 35.719 -28.395 -19.516 1.00 29.25 ?  11  LYS   B HB2  1 
ATOM   4114 H  HB3  . LYS   B 1 11  ? 34.691 -29.590 -19.365 1.00 29.25 ?  11  LYS   B HB3  1 
ATOM   4115 H  HG2  . LYS   B 1 11  ? 33.334 -28.194 -18.034 1.00 33.76 ?  11  LYS   B HG2  1 
ATOM   4116 H  HG3  . LYS   B 1 11  ? 34.333 -26.991 -18.349 1.00 33.76 ?  11  LYS   B HG3  1 
ATOM   4117 H  HD2  . LYS   B 1 11  ? 33.851 -27.268 -20.655 1.00 37.29 ?  11  LYS   B HD2  1 
ATOM   4118 H  HD3  . LYS   B 1 11  ? 32.755 -28.352 -20.260 1.00 37.29 ?  11  LYS   B HD3  1 
ATOM   4119 H  HE2  . LYS   B 1 11  ? 31.600 -26.433 -20.593 1.00 40.00 ?  11  LYS   B HE2  1 
ATOM   4120 H  HE3  . LYS   B 1 11  ? 31.665 -26.614 -19.015 1.00 40.00 ?  11  LYS   B HE3  1 
ATOM   4121 H  HZ1  . LYS   B 1 11  ? 32.190 -24.476 -19.603 1.00 41.57 ?  11  LYS   B HZ1  1 
ATOM   4122 H  HZ2  . LYS   B 1 11  ? 33.352 -25.082 -18.986 1.00 41.57 ?  11  LYS   B HZ2  1 
ATOM   4123 H  HZ3  . LYS   B 1 11  ? 33.295 -24.926 -20.425 1.00 41.57 ?  11  LYS   B HZ3  1 
ATOM   4124 N  N    . LEU   B 1 12  ? 34.630 -29.808 -15.617 1.00 17.79 ?  12  LEU   B N    1 
ATOM   4125 C  CA   . LEU   B 1 12  ? 33.671 -30.518 -14.776 1.00 17.17 ?  12  LEU   B CA   1 
ATOM   4126 C  C    . LEU   B 1 12  ? 32.279 -29.913 -14.867 1.00 16.79 ?  12  LEU   B C    1 
ATOM   4127 O  O    . LEU   B 1 12  ? 31.292 -30.633 -15.041 1.00 17.61 ?  12  LEU   B O    1 
ATOM   4128 C  CB   . LEU   B 1 12  ? 34.132 -30.538 -13.314 1.00 16.63 ?  12  LEU   B CB   1 
ATOM   4129 C  CG   . LEU   B 1 12  ? 35.478 -31.210 -13.049 1.00 16.73 ?  12  LEU   B CG   1 
ATOM   4130 C  CD1  . LEU   B 1 12  ? 35.834 -31.167 -11.575 1.00 17.08 ?  12  LEU   B CD1  1 
ATOM   4131 C  CD2  . LEU   B 1 12  ? 35.482 -32.645 -13.563 1.00 17.37 ?  12  LEU   B CD2  1 
ATOM   4132 H  H    . LEU   B 1 12  ? 34.959 -29.106 -15.246 1.00 21.38 ?  12  LEU   B H    1 
ATOM   4133 H  HA   . LEU   B 1 12  ? 33.605 -31.436 -15.079 1.00 20.65 ?  12  LEU   B HA   1 
ATOM   4134 H  HB2  . LEU   B 1 12  ? 34.195 -29.624 -13.000 1.00 20.00 ?  12  LEU   B HB2  1 
ATOM   4135 H  HB3  . LEU   B 1 12  ? 33.463 -31.012 -12.789 1.00 20.00 ?  12  LEU   B HB3  1 
ATOM   4136 H  HG   . LEU   B 1 12  ? 36.163 -30.725 -13.531 1.00 20.11 ?  12  LEU   B HG   1 
ATOM   4137 H  HD11 . LEU   B 1 12  ? 36.697 -31.597 -11.446 1.00 20.54 ?  12  LEU   B HD11 1 
ATOM   4138 H  HD12 . LEU   B 1 12  ? 35.884 -30.241 -11.288 1.00 20.54 ?  12  LEU   B HD12 1 
ATOM   4139 H  HD13 . LEU   B 1 12  ? 35.154 -31.635 -11.069 1.00 20.54 ?  12  LEU   B HD13 1 
ATOM   4140 H  HD21 . LEU   B 1 12  ? 36.283 -33.090 -13.249 1.00 20.89 ?  12  LEU   B HD21 1 
ATOM   4141 H  HD22 . LEU   B 1 12  ? 34.694 -33.102 -13.229 1.00 20.89 ?  12  LEU   B HD22 1 
ATOM   4142 H  HD23 . LEU   B 1 12  ? 35.468 -32.632 -14.534 1.00 20.89 ?  12  LEU   B HD23 1 
ATOM   4143 N  N    . THR   B 1 13  ? 32.193 -28.593 -14.749 1.00 16.71 ?  13  THR   B N    1 
ATOM   4144 C  CA   . THR   B 1 13  ? 30.971 -27.840 -14.957 1.00 16.63 ?  13  THR   B CA   1 
ATOM   4145 C  C    . THR   B 1 13  ? 31.313 -26.644 -15.838 1.00 18.48 ?  13  THR   B C    1 
ATOM   4146 O  O    . THR   B 1 13  ? 32.460 -26.456 -16.258 1.00 19.14 ?  13  THR   B O    1 
ATOM   4147 C  CB   . THR   B 1 13  ? 30.369 -27.368 -13.628 1.00 16.18 ?  13  THR   B CB   1 
ATOM   4148 O  OG1  . THR   B 1 13  ? 31.215 -26.353 -13.074 1.00 16.29 ?  13  THR   B OG1  1 
ATOM   4149 C  CG2  . THR   B 1 13  ? 30.239 -28.527 -12.641 1.00 16.66 ?  13  THR   B CG2  1 
ATOM   4150 H  H    . THR   B 1 13  ? 32.858 -28.096 -14.539 1.00 20.09 ?  13  THR   B H    1 
ATOM   4151 H  HA   . THR   B 1 13  ? 30.314 -28.395 -15.409 1.00 20.00 ?  13  THR   B HA   1 
ATOM   4152 H  HB   . THR   B 1 13  ? 29.479 -27.001 -13.785 1.00 19.46 ?  13  THR   B HB   1 
ATOM   4153 H  HG1  . THR   B 1 13  ? 30.930 -25.589 -13.296 1.00 19.60 ?  13  THR   B HG1  1 
ATOM   4154 H  HG21 . THR   B 1 13  ? 29.734 -28.248 -11.861 1.00 20.03 ?  13  THR   B HG21 1 
ATOM   4155 H  HG22 . THR   B 1 13  ? 29.776 -29.270 -13.063 1.00 20.03 ?  13  THR   B HG22 1 
ATOM   4156 H  HG23 . THR   B 1 13  ? 31.117 -28.824 -12.360 1.00 20.03 ?  13  THR   B HG23 1 
ATOM   4157 N  N    A ASP   B 1 14  ? 30.301 -25.822 -16.113 0.60 19.44 ?  14  ASP   B N    1 
ATOM   4158 N  N    B ASP   B 1 14  ? 30.307 -25.811 -16.108 0.40 19.26 ?  14  ASP   B N    1 
ATOM   4159 C  CA   A ASP   B 1 14  ? 30.518 -24.664 -16.969 0.60 20.85 ?  14  ASP   B CA   1 
ATOM   4160 C  CA   B ASP   B 1 14  ? 30.518 -24.660 -16.979 0.40 20.25 ?  14  ASP   B CA   1 
ATOM   4161 C  C    A ASP   B 1 14  ? 31.626 -23.764 -16.434 0.60 19.05 ?  14  ASP   B C    1 
ATOM   4162 C  C    B ASP   B 1 14  ? 31.511 -23.657 -16.410 0.40 18.61 ?  14  ASP   B C    1 
ATOM   4163 O  O    A ASP   B 1 14  ? 32.320 -23.108 -17.220 0.60 19.78 ?  14  ASP   B O    1 
ATOM   4164 O  O    B ASP   B 1 14  ? 31.971 -22.781 -17.151 0.40 18.88 ?  14  ASP   B O    1 
ATOM   4165 C  CB   A ASP   B 1 14  ? 29.215 -23.880 -17.134 0.60 24.66 ?  14  ASP   B CB   1 
ATOM   4166 C  CB   B ASP   B 1 14  ? 29.197 -23.943 -17.250 0.40 23.23 ?  14  ASP   B CB   1 
ATOM   4167 C  CG   A ASP   B 1 14  ? 28.240 -24.554 -18.074 0.60 28.16 ?  14  ASP   B CG   1 
ATOM   4168 C  CG   B ASP   B 1 14  ? 28.312 -24.705 -18.216 0.40 25.92 ?  14  ASP   B CG   1 
ATOM   4169 O  OD1  A ASP   B 1 14  ? 28.587 -25.598 -18.670 0.60 29.29 ?  14  ASP   B OD1  1 
ATOM   4170 O  OD1  B ASP   B 1 14  ? 28.860 -25.403 -19.097 0.40 26.90 ?  14  ASP   B OD1  1 
ATOM   4171 O  OD2  A ASP   B 1 14  ? 27.113 -24.035 -18.213 0.60 29.51 -1 14  ASP   B OD2  1 
ATOM   4172 O  OD2  B ASP   B 1 14  ? 27.073 -24.617 -18.096 0.40 26.74 -1 14  ASP   B OD2  1 
ATOM   4173 H  H    A ASP   B 1 14  ? 29.501 -25.903 -15.809 0.60 23.37 ?  14  ASP   B H    1 
ATOM   4174 H  H    B ASP   B 1 14  ? 29.508 -25.889 -15.804 0.40 23.16 ?  14  ASP   B H    1 
ATOM   4175 H  HA   A ASP   B 1 14  ? 30.795 -24.964 -17.844 0.60 25.06 ?  14  ASP   B HA   1 
ATOM   4176 H  HA   B ASP   B 1 14  ? 30.861 -24.975 -17.830 0.40 24.34 ?  14  ASP   B HA   1 
ATOM   4177 H  HB2  A ASP   B 1 14  ? 28.772 -23.807 -16.277 0.60 29.64 ?  14  ASP   B HB2  1 
ATOM   4178 H  HB2  B ASP   B 1 14  ? 28.718 -23.841 -16.412 0.40 27.92 ?  14  ASP   B HB2  1 
ATOM   4179 H  HB3  A ASP   B 1 14  ? 29.408 -23.002 -17.491 0.60 29.64 ?  14  ASP   B HB3  1 
ATOM   4180 H  HB3  B ASP   B 1 14  ? 29.392 -23.063 -17.623 0.40 27.92 ?  14  ASP   B HB3  1 
ATOM   4181 N  N    . ASN   B 1 15  ? 31.825 -23.732 -15.113 1.00 16.86 ?  15  ASN   B N    1 
ATOM   4182 C  CA   . ASN   B 1 15  ? 32.782 -22.811 -14.505 1.00 14.69 ?  15  ASN   B CA   1 
ATOM   4183 C  C    . ASN   B 1 15  ? 33.872 -23.466 -13.663 1.00 13.41 ?  15  ASN   B C    1 
ATOM   4184 O  O    . ASN   B 1 15  ? 34.720 -22.740 -13.129 1.00 13.81 ?  15  ASN   B O    1 
ATOM   4185 C  CB   . ASN   B 1 15  ? 32.062 -21.761 -13.643 1.00 14.93 ?  15  ASN   B CB   1 
ATOM   4186 C  CG   . ASN   B 1 15  ? 31.453 -22.364 -12.396 1.00 14.52 ?  15  ASN   B CG   1 
ATOM   4187 O  OD1  . ASN   B 1 15  ? 30.511 -23.162 -12.474 1.00 16.33 ?  15  ASN   B OD1  1 
ATOM   4188 N  ND2  . ASN   B 1 15  ? 31.984 -22.003 -11.241 1.00 13.74 ?  15  ASN   B ND2  1 
ATOM   4189 H  H    A ASN   B 1 15  ? 31.420 -24.244 -14.551 0.60 20.27 ?  15  ASN   B H    1 
ATOM   4190 H  H    B ASN   B 1 15  ? 31.465 -24.286 -14.560 0.40 20.27 ?  15  ASN   B H    1 
ATOM   4191 H  HA   . ASN   B 1 15  ? 33.231 -22.328 -15.209 1.00 17.67 ?  15  ASN   B HA   1 
ATOM   4192 H  HB2  . ASN   B 1 15  ? 32.704 -21.078 -13.372 1.00 17.95 ?  15  ASN   B HB2  1 
ATOM   4193 H  HB3  . ASN   B 1 15  ? 31.351 -21.350 -14.162 1.00 17.95 ?  15  ASN   B HB3  1 
ATOM   4194 H  HD21 . ASN   B 1 15  ? 31.671 -22.319 -10.504 1.00 16.54 ?  15  ASN   B HD21 1 
ATOM   4195 H  HD22 . ASN   B 1 15  ? 32.650 -21.452 -11.218 1.00 16.54 ?  15  ASN   B HD22 1 
ATOM   4196 N  N    . VAL   B 1 16  ? 33.881 -24.791 -13.515 1.00 13.50 ?  16  VAL   B N    1 
ATOM   4197 C  CA   . VAL   B 1 16  ? 34.882 -25.483 -12.709 1.00 13.27 ?  16  VAL   B CA   1 
ATOM   4198 C  C    . VAL   B 1 16  ? 35.679 -26.418 -13.604 1.00 13.36 ?  16  VAL   B C    1 
ATOM   4199 O  O    . VAL   B 1 16  ? 35.105 -27.294 -14.267 1.00 14.19 ?  16  VAL   B O    1 
ATOM   4200 C  CB   . VAL   B 1 16  ? 34.255 -26.252 -11.533 1.00 13.57 ?  16  VAL   B CB   1 
ATOM   4201 C  CG1  . VAL   B 1 16  ? 35.338 -26.988 -10.746 1.00 13.78 ?  16  VAL   B CG1  1 
ATOM   4202 C  CG2  . VAL   B 1 16  ? 33.467 -25.299 -10.635 1.00 14.55 ?  16  VAL   B CG2  1 
ATOM   4203 H  H    . VAL   B 1 16  ? 33.301 -25.320 -13.876 1.00 16.25 ?  16  VAL   B H    1 
ATOM   4204 H  HA   . VAL   B 1 16  ? 35.492 -24.827 -12.336 1.00 15.97 ?  16  VAL   B HA   1 
ATOM   4205 H  HB   . VAL   B 1 16  ? 33.638 -26.916 -11.882 1.00 16.32 ?  16  VAL   B HB   1 
ATOM   4206 H  HG11 . VAL   B 1 16  ? 34.966 -27.288 -9.900  1.00 16.58 ?  16  VAL   B HG11 1 
ATOM   4207 H  HG12 . VAL   B 1 16  ? 35.647 -27.751 -11.257 1.00 16.58 ?  16  VAL   B HG12 1 
ATOM   4208 H  HG13 . VAL   B 1 16  ? 36.077 -26.379 -10.579 1.00 16.58 ?  16  VAL   B HG13 1 
ATOM   4209 H  HG21 . VAL   B 1 16  ? 33.126 -25.795 -9.872  1.00 17.50 ?  16  VAL   B HG21 1 
ATOM   4210 H  HG22 . VAL   B 1 16  ? 34.053 -24.591 -10.335 1.00 17.50 ?  16  VAL   B HG22 1 
ATOM   4211 H  HG23 . VAL   B 1 16  ? 32.727 -24.928 -11.142 1.00 17.50 ?  16  VAL   B HG23 1 
ATOM   4212 N  N    . TYR   B 1 17  ? 37.002 -26.250 -13.579 1.00 13.73 ?  17  TYR   B N    1 
ATOM   4213 C  CA   . TYR   B 1 17  ? 37.952 -26.998 -14.390 1.00 14.10 ?  17  TYR   B CA   1 
ATOM   4214 C  C    . TYR   B 1 17  ? 39.004 -27.611 -13.476 1.00 13.29 ?  17  TYR   B C    1 
ATOM   4215 O  O    . TYR   B 1 17  ? 39.280 -27.085 -12.394 1.00 13.59 ?  17  TYR   B O    1 
ATOM   4216 C  CB   . TYR   B 1 17  ? 38.658 -26.070 -15.387 1.00 16.32 ?  17  TYR   B CB   1 
ATOM   4217 C  CG   . TYR   B 1 17  ? 37.730 -25.305 -16.299 1.00 19.25 ?  17  TYR   B CG   1 
ATOM   4218 C  CD1  . TYR   B 1 17  ? 37.148 -24.110 -15.895 1.00 20.93 ?  17  TYR   B CD1  1 
ATOM   4219 C  CD2  . TYR   B 1 17  ? 37.440 -25.778 -17.571 1.00 21.09 ?  17  TYR   B CD2  1 
ATOM   4220 C  CE1  . TYR   B 1 17  ? 36.295 -23.408 -16.734 1.00 22.54 ?  17  TYR   B CE1  1 
ATOM   4221 C  CE2  . TYR   B 1 17  ? 36.594 -25.086 -18.416 1.00 22.65 ?  17  TYR   B CE2  1 
ATOM   4222 C  CZ   . TYR   B 1 17  ? 36.023 -23.902 -17.992 1.00 23.60 ?  17  TYR   B CZ   1 
ATOM   4223 O  OH   . TYR   B 1 17  ? 35.183 -23.209 -18.830 1.00 25.10 ?  17  TYR   B OH   1 
ATOM   4224 H  H    . TYR   B 1 17  ? 37.397 -25.671 -13.070 1.00 16.51 ?  17  TYR   B H    1 
ATOM   4225 H  HA   . TYR   B 1 17  ? 37.491 -27.704 -14.876 1.00 16.96 ?  17  TYR   B HA   1 
ATOM   4226 H  HB2  . TYR   B 1 17  ? 39.190 -25.428 -14.896 1.00 19.63 ?  17  TYR   B HB2  1 
ATOM   4227 H  HB3  . TYR   B 1 17  ? 39.229 -26.609 -15.951 1.00 19.63 ?  17  TYR   B HB3  1 
ATOM   4228 H  HD1  . TYR   B 1 17  ? 37.331 -23.776 -15.048 1.00 25.16 ?  17  TYR   B HD1  1 
ATOM   4229 H  HD2  . TYR   B 1 17  ? 37.815 -26.576 -17.862 1.00 25.35 ?  17  TYR   B HD2  1 
ATOM   4230 H  HE1  . TYR   B 1 17  ? 35.912 -22.607 -16.453 1.00 27.09 ?  17  TYR   B HE1  1 
ATOM   4231 H  HE2  . TYR   B 1 17  ? 36.402 -25.417 -19.267 1.00 27.22 ?  17  TYR   B HE2  1 
ATOM   4232 H  HH   . TYR   B 1 17  ? 35.098 -23.613 -19.562 1.00 30.17 ?  17  TYR   B HH   1 
ATOM   4233 N  N    . ILE   B 1 18  ? 39.616 -28.714 -13.910 1.00 13.33 ?  18  ILE   B N    1 
ATOM   4234 C  CA   . ILE   B 1 18  ? 40.547 -29.434 -13.046 1.00 13.50 ?  18  ILE   B CA   1 
ATOM   4235 C  C    . ILE   B 1 18  ? 41.709 -29.984 -13.865 1.00 13.68 ?  18  ILE   B C    1 
ATOM   4236 O  O    . ILE   B 1 18  ? 41.548 -30.378 -15.026 1.00 15.07 ?  18  ILE   B O    1 
ATOM   4237 C  CB   . ILE   B 1 18  ? 39.798 -30.535 -12.244 1.00 13.97 ?  18  ILE   B CB   1 
ATOM   4238 C  CG1  . ILE   B 1 18  ? 40.652 -31.074 -11.089 1.00 14.15 ?  18  ILE   B CG1  1 
ATOM   4239 C  CG2  . ILE   B 1 18  ? 39.301 -31.659 -13.170 1.00 14.69 ?  18  ILE   B CG2  1 
ATOM   4240 C  CD1  . ILE   B 1 18  ? 39.841 -31.875 -10.073 1.00 15.80 ?  18  ILE   B CD1  1 
ATOM   4241 H  H    . ILE   B 1 18  ? 39.511 -29.062 -14.686 1.00 16.04 ?  18  ILE   B H    1 
ATOM   4242 H  HA   . ILE   B 1 18  ? 40.907 -28.819 -12.393 1.00 16.24 ?  18  ILE   B HA   1 
ATOM   4243 H  HB   . ILE   B 1 18  ? 39.010 -30.134 -11.846 1.00 16.80 ?  18  ILE   B HB   1 
ATOM   4244 H  HG12 . ILE   B 1 18  ? 41.340 -31.652 -11.445 1.00 17.03 ?  18  ILE   B HG12 1 
ATOM   4245 H  HG13 . ILE   B 1 18  ? 41.052 -30.323 -10.623 1.00 17.03 ?  18  ILE   B HG13 1 
ATOM   4246 H  HG21 . ILE   B 1 18  ? 38.715 -32.251 -12.667 1.00 17.68 ?  18  ILE   B HG21 1 
ATOM   4247 H  HG22 . ILE   B 1 18  ? 38.810 -31.261 -13.905 1.00 17.68 ?  18  ILE   B HG22 1 
ATOM   4248 H  HG23 . ILE   B 1 18  ? 40.061 -32.155 -13.506 1.00 17.68 ?  18  ILE   B HG23 1 
ATOM   4249 H  HD11 . ILE   B 1 18  ? 40.425 -32.149 -9.348  1.00 19.00 ?  18  ILE   B HD11 1 
ATOM   4250 H  HD12 . ILE   B 1 18  ? 39.126 -31.317 -9.727  1.00 19.00 ?  18  ILE   B HD12 1 
ATOM   4251 H  HD13 . ILE   B 1 18  ? 39.468 -32.656 -10.511 1.00 19.00 ?  18  ILE   B HD13 1 
ATOM   4252 N  N    . LYS   B 1 19  ? 42.888 -30.031 -13.239 1.00 14.01 ?  19  LYS   B N    1 
ATOM   4253 C  CA   . LYS   B 1 19  ? 44.098 -30.501 -13.897 1.00 15.07 ?  19  LYS   B CA   1 
ATOM   4254 C  C    . LYS   B 1 19  ? 44.994 -31.178 -12.874 1.00 14.91 ?  19  LYS   B C    1 
ATOM   4255 O  O    . LYS   B 1 19  ? 45.076 -30.739 -11.725 1.00 14.28 ?  19  LYS   B O    1 
ATOM   4256 C  CB   . LYS   B 1 19  ? 44.865 -29.331 -14.533 1.00 16.18 ?  19  LYS   B CB   1 
ATOM   4257 C  CG   . LYS   B 1 19  ? 46.046 -29.741 -15.389 1.00 18.22 ?  19  LYS   B CG   1 
ATOM   4258 C  CD   . LYS   B 1 19  ? 46.767 -28.510 -15.922 1.00 19.99 ?  19  LYS   B CD   1 
ATOM   4259 C  CE   . LYS   B 1 19  ? 47.935 -28.877 -16.817 1.00 21.81 ?  19  LYS   B CE   1 
ATOM   4260 N  NZ   . LYS   B 1 19  ? 48.638 -27.673 -17.328 1.00 22.62 ?  19  LYS   B NZ   1 
ATOM   4261 H  H    . LYS   B 1 19  ? 42.999 -29.790 -12.416 1.00 16.86 ?  19  LYS   B H    1 
ATOM   4262 H  HA   . LYS   B 1 19  ? 43.861 -31.138 -14.585 1.00 18.13 ?  19  LYS   B HA   1 
ATOM   4263 H  HB2  . LYS   B 1 19  ? 44.247 -28.836 -15.093 1.00 19.46 ?  19  LYS   B HB2  1 
ATOM   4264 H  HB3  . LYS   B 1 19  ? 45.188 -28.754 -13.819 1.00 19.46 ?  19  LYS   B HB3  1 
ATOM   4265 H  HG2  . LYS   B 1 19  ? 46.662 -30.260 -14.852 1.00 21.91 ?  19  LYS   B HG2  1 
ATOM   4266 H  HG3  . LYS   B 1 19  ? 45.722 -30.266 -16.139 1.00 21.91 ?  19  LYS   B HG3  1 
ATOM   4267 H  HD2  . LYS   B 1 19  ? 46.141 -27.975 -16.438 1.00 24.04 ?  19  LYS   B HD2  1 
ATOM   4268 H  HD3  . LYS   B 1 19  ? 47.105 -27.994 -15.173 1.00 24.04 ?  19  LYS   B HD3  1 
ATOM   4269 H  HE2  . LYS   B 1 19  ? 48.566 -29.411 -16.308 1.00 26.21 ?  19  LYS   B HE2  1 
ATOM   4270 H  HE3  . LYS   B 1 19  ? 47.603 -29.387 -17.575 1.00 26.21 ?  19  LYS   B HE3  1 
ATOM   4271 H  HZ1  . LYS   B 1 19  ? 49.302 -27.917 -17.868 1.00 27.18 ?  19  LYS   B HZ1  1 
ATOM   4272 H  HZ2  . LYS   B 1 19  ? 48.070 -27.161 -17.783 1.00 27.18 ?  19  LYS   B HZ2  1 
ATOM   4273 H  HZ3  . LYS   B 1 19  ? 48.971 -27.205 -16.650 1.00 27.18 ?  19  LYS   B HZ3  1 
ATOM   4274 N  N    . ASN   B 1 20  ? 45.681 -32.232 -13.305 1.00 16.06 ?  20  ASN   B N    1 
ATOM   4275 C  CA   . ASN   B 1 20  ? 46.709 -32.868 -12.489 1.00 17.03 ?  20  ASN   B CA   1 
ATOM   4276 C  C    . ASN   B 1 20  ? 47.982 -32.049 -12.677 1.00 17.59 ?  20  ASN   B C    1 
ATOM   4277 O  O    . ASN   B 1 20  ? 48.626 -32.119 -13.728 1.00 19.58 ?  20  ASN   B O    1 
ATOM   4278 C  CB   . ASN   B 1 20  ? 46.874 -34.320 -12.931 1.00 18.89 ?  20  ASN   B CB   1 
ATOM   4279 C  CG   . ASN   B 1 20  ? 48.030 -35.034 -12.249 1.00 20.30 ?  20  ASN   B CG   1 
ATOM   4280 O  OD1  . ASN   B 1 20  ? 48.652 -35.919 -12.843 1.00 22.75 ?  20  ASN   B OD1  1 
ATOM   4281 N  ND2  . ASN   B 1 20  ? 48.318 -34.673 -11.008 1.00 19.79 ?  20  ASN   B ND2  1 
ATOM   4282 H  H    . ASN   B 1 20  ? 45.568 -32.597 -14.075 1.00 19.31 ?  20  ASN   B H    1 
ATOM   4283 H  HA   . ASN   B 1 20  ? 46.438 -32.851 -11.556 1.00 20.48 ?  20  ASN   B HA   1 
ATOM   4284 H  HB2  . ASN   B 1 20  ? 46.056 -34.806 -12.723 1.00 22.71 ?  20  ASN   B HB2  1 
ATOM   4285 H  HB3  . ASN   B 1 20  ? 47.029 -34.339 -13.886 1.00 22.71 ?  20  ASN   B HB3  1 
ATOM   4286 H  HD21 . ASN   B 1 20  ? 48.967 -35.053 -10.594 1.00 23.79 ?  20  ASN   B HD21 1 
ATOM   4287 H  HD22 . ASN   B 1 20  ? 47.868 -34.050 -10.619 1.00 23.79 ?  20  ASN   B HD22 1 
ATOM   4288 N  N    . ALA   B 1 21  ? 48.335 -31.243 -11.672 1.00 17.06 ?  21  ALA   B N    1 
ATOM   4289 C  CA   . ALA   B 1 21  ? 49.443 -30.312 -11.823 1.00 17.64 ?  21  ALA   B CA   1 
ATOM   4290 C  C    . ALA   B 1 21  ? 49.907 -29.818 -10.461 1.00 16.50 ?  21  ALA   B C    1 
ATOM   4291 O  O    . ALA   B 1 21  ? 49.167 -29.848 -9.475  1.00 16.29 ?  21  ALA   B O    1 
ATOM   4292 C  CB   . ALA   B 1 21  ? 49.046 -29.129 -12.706 1.00 19.03 ?  21  ALA   B CB   1 
ATOM   4293 H  H    . ALA   B 1 21  ? 47.946 -31.225 -10.898 1.00 20.51 ?  21  ALA   B H    1 
ATOM   4294 H  HA   . ALA   B 1 21  ? 50.180 -30.778 -12.243 1.00 21.21 ?  21  ALA   B HA   1 
ATOM   4295 H  HB1  . ALA   B 1 21  ? 49.829 -28.582 -12.847 1.00 22.88 ?  21  ALA   B HB1  1 
ATOM   4296 H  HB2  . ALA   B 1 21  ? 48.717 -29.471 -13.550 1.00 22.88 ?  21  ALA   B HB2  1 
ATOM   4297 H  HB3  . ALA   B 1 21  ? 48.351 -28.623 -12.258 1.00 22.88 ?  21  ALA   B HB3  1 
ATOM   4298 N  N    . ASP   B 1 22  ? 51.163 -29.371 -10.441 1.00 16.00 ?  22  ASP   B N    1 
ATOM   4299 C  CA   . ASP   B 1 22  ? 51.777 -28.678 -9.312  1.00 15.32 ?  22  ASP   B CA   1 
ATOM   4300 C  C    . ASP   B 1 22  ? 51.376 -27.206 -9.393  1.00 13.85 ?  22  ASP   B C    1 
ATOM   4301 O  O    . ASP   B 1 22  ? 51.684 -26.536 -10.383 1.00 14.01 ?  22  ASP   B O    1 
ATOM   4302 C  CB   . ASP   B 1 22  ? 53.294 -28.862 -9.463  1.00 16.49 ?  22  ASP   B CB   1 
ATOM   4303 C  CG   . ASP   B 1 22  ? 54.126 -28.094 -8.441  1.00 18.13 ?  22  ASP   B CG   1 
ATOM   4304 O  OD1  . ASP   B 1 22  ? 53.763 -26.977 -8.050  1.00 18.26 ?  22  ASP   B OD1  1 
ATOM   4305 O  OD2  . ASP   B 1 22  ? 55.200 -28.610 -8.058  1.00 20.57 -1 22  ASP   B OD2  1 
ATOM   4306 H  H    . ASP   B 1 22  ? 51.703 -29.464 -11.106 1.00 19.24 ?  22  ASP   B H    1 
ATOM   4307 H  HA   . ASP   B 1 22  ? 51.480 -29.062 -8.470  1.00 18.43 ?  22  ASP   B HA   1 
ATOM   4308 H  HB2  . ASP   B 1 22  ? 53.509 -29.800 -9.368  1.00 19.83 ?  22  ASP   B HB2  1 
ATOM   4309 H  HB3  . ASP   B 1 22  ? 53.560 -28.547 -10.340 1.00 19.83 ?  22  ASP   B HB3  1 
ATOM   4310 N  N    . ILE   B 1 23  ? 50.665 -26.711 -8.371  1.00 13.07 ?  23  ILE   B N    1 
ATOM   4311 C  CA   . ILE   B 1 23  ? 50.076 -25.370 -8.442  1.00 12.34 ?  23  ILE   B CA   1 
ATOM   4312 C  C    . ILE   B 1 23  ? 51.132 -24.281 -8.588  1.00 12.01 ?  23  ILE   B C    1 
ATOM   4313 O  O    . ILE   B 1 23  ? 50.868 -23.242 -9.201  1.00 11.76 ?  23  ILE   B O    1 
ATOM   4314 C  CB   . ILE   B 1 23  ? 49.139 -25.122 -7.244  1.00 12.56 ?  23  ILE   B CB   1 
ATOM   4315 C  CG1  . ILE   B 1 23  ? 48.314 -23.851 -7.449  1.00 13.23 ?  23  ILE   B CG1  1 
ATOM   4316 C  CG2  . ILE   B 1 23  ? 49.906 -25.083 -5.940  1.00 13.70 ?  23  ILE   B CG2  1 
ATOM   4317 C  CD1  . ILE   B 1 23  ? 47.181 -23.707 -6.445  1.00 13.92 ?  23  ILE   B CD1  1 
ATOM   4318 H  H    . ILE   B 1 23  ? 50.512 -27.133 -7.635  1.00 15.73 ?  23  ILE   B H    1 
ATOM   4319 H  HA   . ILE   B 1 23  ? 49.527 -25.335 -9.239  1.00 14.86 ?  23  ILE   B HA   1 
ATOM   4320 H  HB   . ILE   B 1 23  ? 48.518 -25.863 -7.199  1.00 15.11 ?  23  ILE   B HB   1 
ATOM   4321 H  HG12 . ILE   B 1 23  ? 48.897 -23.076 -7.356  1.00 15.92 ?  23  ILE   B HG12 1 
ATOM   4322 H  HG13 . ILE   B 1 23  ? 47.928 -23.861 -8.341  1.00 15.92 ?  23  ILE   B HG13 1 
ATOM   4323 H  HG21 . ILE   B 1 23  ? 49.278 -25.076 -5.204  1.00 16.48 ?  23  ILE   B HG21 1 
ATOM   4324 H  HG22 . ILE   B 1 23  ? 50.472 -25.868 -5.886  1.00 16.48 ?  23  ILE   B HG22 1 
ATOM   4325 H  HG23 . ILE   B 1 23  ? 50.453 -24.280 -5.919  1.00 16.48 ?  23  ILE   B HG23 1 
ATOM   4326 H  HD11 . ILE   B 1 23  ? 46.649 -22.933 -6.681  1.00 16.75 ?  23  ILE   B HD11 1 
ATOM   4327 H  HD12 . ILE   B 1 23  ? 46.635 -24.508 -6.478  1.00 16.75 ?  23  ILE   B HD12 1 
ATOM   4328 H  HD13 . ILE   B 1 23  ? 47.558 -23.597 -5.561  1.00 16.75 ?  23  ILE   B HD13 1 
ATOM   4329 N  N    . VAL   B 1 24  ? 52.328 -24.484 -8.030  1.00 12.36 ?  24  VAL   B N    1 
ATOM   4330 C  CA   . VAL   B 1 24  ? 53.403 -23.507 -8.201  1.00 12.95 ?  24  VAL   B CA   1 
ATOM   4331 C  C    . VAL   B 1 24  ? 53.854 -23.465 -9.653  1.00 12.93 ?  24  VAL   B C    1 
ATOM   4332 O  O    . VAL   B 1 24  ? 54.000 -22.389 -10.247 1.00 13.71 ?  24  VAL   B O    1 
ATOM   4333 C  CB   . VAL   B 1 24  ? 54.583 -23.824 -7.262  1.00 14.05 ?  24  VAL   B CB   1 
ATOM   4334 C  CG1  . VAL   B 1 24  ? 55.787 -22.943 -7.589  1.00 14.94 ?  24  VAL   B CG1  1 
ATOM   4335 C  CG2  . VAL   B 1 24  ? 54.172 -23.650 -5.820  1.00 14.85 ?  24  VAL   B CG2  1 
ATOM   4336 H  H    . VAL   B 1 24  ? 52.536 -25.168 -7.549  1.00 14.87 ?  24  VAL   B H    1 
ATOM   4337 H  HA   . VAL   B 1 24  ? 53.070 -22.630 -7.969  1.00 15.58 ?  24  VAL   B HA   1 
ATOM   4338 H  HB   . VAL   B 1 24  ? 54.848 -24.753 -7.384  1.00 16.90 ?  24  VAL   B HB   1 
ATOM   4339 H  HG11 . VAL   B 1 24  ? 56.384 -22.933 -6.824  1.00 17.97 ?  24  VAL   B HG11 1 
ATOM   4340 H  HG12 . VAL   B 1 24  ? 56.245 -23.311 -8.360  1.00 17.97 ?  24  VAL   B HG12 1 
ATOM   4341 H  HG13 . VAL   B 1 24  ? 55.475 -22.046 -7.778  1.00 17.97 ?  24  VAL   B HG13 1 
ATOM   4342 H  HG21 . VAL   B 1 24  ? 54.910 -23.907 -5.246  1.00 17.87 ?  24  VAL   B HG21 1 
ATOM   4343 H  HG22 . VAL   B 1 24  ? 53.943 -22.720 -5.671  1.00 17.87 ?  24  VAL   B HG22 1 
ATOM   4344 H  HG23 . VAL   B 1 24  ? 53.402 -24.214 -5.640  1.00 17.87 ?  24  VAL   B HG23 1 
ATOM   4345 N  N    . GLU   B 1 25  ? 54.108 -24.638 -10.239 1.00 13.92 ?  25  GLU   B N    1 
ATOM   4346 C  CA   . GLU   B 1 25  ? 54.509 -24.677 -11.640 1.00 15.42 ?  25  GLU   B CA   1 
ATOM   4347 C  C    . GLU   B 1 25  ? 53.404 -24.133 -12.531 1.00 14.21 ?  25  GLU   B C    1 
ATOM   4348 O  O    . GLU   B 1 25  ? 53.676 -23.423 -13.508 1.00 15.29 ?  25  GLU   B O    1 
ATOM   4349 C  CB   . GLU   B 1 25  ? 54.896 -26.102 -12.036 1.00 19.19 ?  25  GLU   B CB   1 
ATOM   4350 C  CG   . GLU   B 1 25  ? 56.187 -26.562 -11.378 1.00 24.77 ?  25  GLU   B CG   1 
ATOM   4351 C  CD   . GLU   B 1 25  ? 57.308 -25.537 -11.480 1.00 29.74 ?  25  GLU   B CD   1 
ATOM   4352 O  OE1  . GLU   B 1 25  ? 57.673 -25.165 -12.616 1.00 31.99 ?  25  GLU   B OE1  1 
ATOM   4353 O  OE2  . GLU   B 1 25  ? 57.812 -25.082 -10.426 1.00 31.83 -1 25  GLU   B OE2  1 
ATOM   4354 H  H    . GLU   B 1 25  ? 54.061 -25.409 -9.854  1.00 16.74 ?  25  GLU   B H    1 
ATOM   4355 H  HA   . GLU   B 1 25  ? 55.272 -24.097 -11.763 1.00 18.54 ?  25  GLU   B HA   1 
ATOM   4356 H  HB2  . GLU   B 1 25  ? 54.190 -26.711 -11.764 1.00 23.07 ?  25  GLU   B HB2  1 
ATOM   4357 H  HB3  . GLU   B 1 25  ? 55.014 -26.142 -12.999 1.00 23.07 ?  25  GLU   B HB3  1 
ATOM   4358 H  HG2  . GLU   B 1 25  ? 56.030 -26.712 -10.440 1.00 29.76 ?  25  GLU   B HG2  1 
ATOM   4359 H  HG3  . GLU   B 1 25  ? 56.490 -27.374 -11.810 1.00 29.76 ?  25  GLU   B HG3  1 
ATOM   4360 N  N    . GLU   B 1 26  ? 52.149 -24.441 -12.196 1.00 13.47 ?  26  GLU   B N    1 
ATOM   4361 C  CA   . GLU   B 1 26  ? 51.024 -23.913 -12.960 1.00 14.20 ?  26  GLU   B CA   1 
ATOM   4362 C  C    . GLU   B 1 26  ? 50.977 -22.395 -12.886 1.00 13.14 ?  26  GLU   B C    1 
ATOM   4363 O  O    . GLU   B 1 26  ? 50.776 -21.721 -13.901 1.00 14.64 ?  26  GLU   B O    1 
ATOM   4364 C  CB   . GLU   B 1 26  ? 49.709 -24.490 -12.433 1.00 16.09 ?  26  GLU   B CB   1 
ATOM   4365 C  CG   . GLU   B 1 26  ? 49.250 -25.763 -13.113 1.00 19.72 ?  26  GLU   B CG   1 
ATOM   4366 C  CD   . GLU   B 1 26  ? 49.013 -25.609 -14.615 1.00 21.06 ?  26  GLU   B CD   1 
ATOM   4367 O  OE1  . GLU   B 1 26  ? 48.036 -24.956 -15.048 1.00 21.44 ?  26  GLU   B OE1  1 
ATOM   4368 O  OE2  . GLU   B 1 26  ? 49.809 -26.180 -15.367 1.00 23.50 -1 26  GLU   B OE2  1 
ATOM   4369 H  H    . GLU   B 1 26  ? 51.922 -24.950 -11.535 1.00 16.20 ?  26  GLU   B H    1 
ATOM   4370 H  HA   . GLU   B 1 26  ? 51.120 -24.167 -13.887 1.00 17.08 ?  26  GLU   B HA   1 
ATOM   4371 H  HB2  . GLU   B 1 26  ? 49.810 -24.683 -11.485 1.00 19.35 ?  26  GLU   B HB2  1 
ATOM   4372 H  HB3  . GLU   B 1 26  ? 49.008 -23.826 -12.550 1.00 19.35 ?  26  GLU   B HB3  1 
ATOM   4373 H  HG2  . GLU   B 1 26  ? 49.937 -26.430 -12.994 1.00 23.71 ?  26  GLU   B HG2  1 
ATOM   4374 H  HG3  . GLU   B 1 26  ? 48.421 -26.053 -12.702 1.00 23.71 ?  26  GLU   B HG3  1 
ATOM   4375 N  N    . ALA   B 1 27  ? 51.120 -21.840 -11.683 1.00 12.54 ?  27  ALA   B N    1 
ATOM   4376 C  CA   . ALA   B 1 27  ? 51.083 -20.390 -11.539 1.00 12.71 ?  27  ALA   B CA   1 
ATOM   4377 C  C    . ALA   B 1 27  ? 52.155 -19.731 -12.397 1.00 13.63 ?  27  ALA   B C    1 
ATOM   4378 O  O    . ALA   B 1 27  ? 51.898 -18.724 -13.076 1.00 14.38 ?  27  ALA   B O    1 
ATOM   4379 C  CB   . ALA   B 1 27  ? 51.251 -20.006 -10.069 1.00 12.84 ?  27  ALA   B CB   1 
ATOM   4380 H  H    . ALA   B 1 27  ? 51.228 -22.274 -10.946 1.00 15.09 ?  27  ALA   B H    1 
ATOM   4381 H  HA   . ALA   B 1 27  ? 50.223 -20.062 -11.834 1.00 15.29 ?  27  ALA   B HA   1 
ATOM   4382 H  HB1  . ALA   B 1 27  ? 51.219 -19.040 -9.987  1.00 15.45 ?  27  ALA   B HB1  1 
ATOM   4383 H  HB2  . ALA   B 1 27  ? 50.527 -20.403 -9.556  1.00 15.45 ?  27  ALA   B HB2  1 
ATOM   4384 H  HB3  . ALA   B 1 27  ? 52.102 -20.338 -9.747  1.00 15.45 ?  27  ALA   B HB3  1 
ATOM   4385 N  N    . LYS   B 1 28  ? 53.370 -20.282 -12.383 1.00 14.96 ?  28  LYS   B N    1 
ATOM   4386 C  CA   . LYS   B 1 28  ? 54.445 -19.664 -13.148 1.00 17.14 ?  28  LYS   B CA   1 
ATOM   4387 C  C    . LYS   B 1 28  ? 54.183 -19.743 -14.644 1.00 18.35 ?  28  LYS   B C    1 
ATOM   4388 O  O    . LYS   B 1 28  ? 54.596 -18.844 -15.389 1.00 19.40 ?  28  LYS   B O    1 
ATOM   4389 C  CB   . LYS   B 1 28  ? 55.803 -20.263 -12.761 1.00 20.02 ?  28  LYS   B CB   1 
ATOM   4390 C  CG   . LYS   B 1 28  ? 56.198 -19.934 -11.326 1.00 22.95 ?  28  LYS   B CG   1 
ATOM   4391 C  CD   . LYS   B 1 28  ? 57.616 -20.358 -10.981 1.00 27.04 ?  28  LYS   B CD   1 
ATOM   4392 C  CE   . LYS   B 1 28  ? 57.714 -21.845 -10.732 1.00 30.99 ?  28  LYS   B CE   1 
ATOM   4393 N  NZ   . LYS   B 1 28  ? 59.063 -22.222 -10.218 1.00 32.49 ?  28  LYS   B NZ   1 
ATOM   4394 H  H    . LYS   B 1 28  ? 53.596 -20.988 -11.949 1.00 17.99 ?  28  LYS   B H    1 
ATOM   4395 H  HA   . LYS   B 1 28  ? 54.479 -18.722 -12.924 1.00 20.61 ?  28  LYS   B HA   1 
ATOM   4396 H  HB2  . LYS   B 1 28  ? 55.766 -21.225 -12.846 1.00 24.06 ?  28  LYS   B HB2  1 
ATOM   4397 H  HB3  . LYS   B 1 28  ? 56.491 -19.902 -13.347 1.00 24.06 ?  28  LYS   B HB3  1 
ATOM   4398 H  HG2  . LYS   B 1 28  ? 56.130 -18.972 -11.198 1.00 27.58 ?  28  LYS   B HG2  1 
ATOM   4399 H  HG3  . LYS   B 1 28  ? 55.591 -20.390 -10.725 1.00 27.58 ?  28  LYS   B HG3  1 
ATOM   4400 H  HD2  . LYS   B 1 28  ? 58.202 -20.131 -11.721 1.00 32.49 ?  28  LYS   B HD2  1 
ATOM   4401 H  HD3  . LYS   B 1 28  ? 57.896 -19.892 -10.178 1.00 32.49 ?  28  LYS   B HD3  1 
ATOM   4402 H  HE2  . LYS   B 1 28  ? 57.052 -22.103 -10.071 1.00 37.23 ?  28  LYS   B HE2  1 
ATOM   4403 H  HE3  . LYS   B 1 28  ? 57.560 -22.321 -11.563 1.00 37.23 ?  28  LYS   B HE3  1 
ATOM   4404 H  HZ1  . LYS   B 1 28  ? 59.100 -23.100 -10.077 1.00 39.03 ?  28  LYS   B HZ1  1 
ATOM   4405 H  HZ2  . LYS   B 1 28  ? 59.688 -21.997 -10.811 1.00 39.03 ?  28  LYS   B HZ2  1 
ATOM   4406 H  HZ3  . LYS   B 1 28  ? 59.225 -21.799 -9.452  1.00 39.03 ?  28  LYS   B HZ3  1 
ATOM   4407 N  N    A LYS   B 1 29  ? 53.484 -20.784 -15.102 0.60 19.37 ?  29  LYS   B N    1 
ATOM   4408 N  N    B LYS   B 1 29  ? 53.478 -20.779 -15.100 0.40 19.67 ?  29  LYS   B N    1 
ATOM   4409 C  CA   A LYS   B 1 29  ? 53.207 -20.933 -16.527 0.60 21.91 ?  29  LYS   B CA   1 
ATOM   4410 C  CA   B LYS   B 1 29  ? 53.204 -20.932 -16.524 0.40 21.88 ?  29  LYS   B CA   1 
ATOM   4411 C  C    A LYS   B 1 29  ? 51.949 -20.188 -16.964 0.60 20.81 ?  29  LYS   B C    1 
ATOM   4412 C  C    B LYS   B 1 29  ? 51.951 -20.181 -16.960 0.40 20.80 ?  29  LYS   B C    1 
ATOM   4413 O  O    A LYS   B 1 29  ? 51.940 -19.570 -18.035 0.60 21.71 ?  29  LYS   B O    1 
ATOM   4414 O  O    B LYS   B 1 29  ? 51.948 -19.547 -18.022 0.40 21.49 ?  29  LYS   B O    1 
ATOM   4415 C  CB   A LYS   B 1 29  ? 53.092 -22.415 -16.895 0.60 26.12 ?  29  LYS   B CB   1 
ATOM   4416 C  CB   B LYS   B 1 29  ? 53.076 -22.416 -16.880 0.40 25.49 ?  29  LYS   B CB   1 
ATOM   4417 C  CG   A LYS   B 1 29  ? 52.836 -22.665 -18.373 0.60 29.89 ?  29  LYS   B CG   1 
ATOM   4418 C  CG   B LYS   B 1 29  ? 53.013 -22.697 -18.372 0.40 28.71 ?  29  LYS   B CG   1 
ATOM   4419 C  CD   A LYS   B 1 29  ? 53.039 -24.131 -18.732 0.60 32.75 ?  29  LYS   B CD   1 
ATOM   4420 C  CD   B LYS   B 1 29  ? 53.256 -24.172 -18.670 0.40 31.16 ?  29  LYS   B CD   1 
ATOM   4421 C  CE   A LYS   B 1 29  ? 51.965 -25.017 -18.122 0.60 34.69 ?  29  LYS   B CE   1 
ATOM   4422 C  CE   B LYS   B 1 29  ? 52.132 -25.050 -18.140 0.40 32.82 ?  29  LYS   B CE   1 
ATOM   4423 N  NZ   A LYS   B 1 29  ? 52.178 -26.453 -18.466 0.60 35.76 ?  29  LYS   B NZ   1 
ATOM   4424 N  NZ   B LYS   B 1 29  ? 52.355 -26.489 -18.460 0.40 33.72 ?  29  LYS   B NZ   1 
ATOM   4425 H  H    A LYS   B 1 29  ? 53.153 -21.412 -14.607 0.60 23.29 ?  29  LYS   B H    1 
ATOM   4426 H  H    B LYS   B 1 29  ? 53.140 -21.403 -14.602 0.40 23.64 ?  29  LYS   B H    1 
ATOM   4427 H  HA   A LYS   B 1 29  ? 53.950 -20.566 -17.021 0.60 26.33 ?  29  LYS   B HA   1 
ATOM   4428 H  HA   B LYS   B 1 29  ? 53.950 -20.572 -17.020 0.40 26.30 ?  29  LYS   B HA   1 
ATOM   4429 H  HB2  A LYS   B 1 29  ? 53.925 -22.860 -16.665 0.60 31.38 ?  29  LYS   B HB2  1 
ATOM   4430 H  HB2  B LYS   B 1 29  ? 53.846 -22.888 -16.528 0.40 30.63 ?  29  LYS   B HB2  1 
ATOM   4431 H  HB3  A LYS   B 1 29  ? 52.361 -22.810 -16.400 0.60 31.38 ?  29  LYS   B HB3  1 
ATOM   4432 H  HB3  B LYS   B 1 29  ? 52.265 -22.767 -16.484 0.40 30.63 ?  29  LYS   B HB3  1 
ATOM   4433 H  HG2  A LYS   B 1 29  ? 51.920 -22.424 -18.585 0.60 35.91 ?  29  LYS   B HG2  1 
ATOM   4434 H  HG2  B LYS   B 1 29  ? 52.134 -22.459 -18.707 0.40 34.49 ?  29  LYS   B HG2  1 
ATOM   4435 H  HG3  A LYS   B 1 29  ? 53.453 -22.133 -18.901 0.60 35.91 ?  29  LYS   B HG3  1 
ATOM   4436 H  HG3  B LYS   B 1 29  ? 53.696 -22.178 -18.826 0.40 34.49 ?  29  LYS   B HG3  1 
ATOM   4437 H  HD2  A LYS   B 1 29  ? 53.004 -24.233 -19.696 0.60 39.35 ?  29  LYS   B HD2  1 
ATOM   4438 H  HD2  B LYS   B 1 29  ? 53.313 -24.299 -19.629 0.40 37.44 ?  29  LYS   B HD2  1 
ATOM   4439 H  HD3  A LYS   B 1 29  ? 53.901 -24.426 -18.396 0.60 39.35 ?  29  LYS   B HD3  1 
ATOM   4440 H  HD3  B LYS   B 1 29  ? 54.083 -24.451 -18.245 0.40 37.44 ?  29  LYS   B HD3  1 
ATOM   4441 H  HE2  A LYS   B 1 29  ? 51.988 -24.932 -17.156 0.60 41.67 ?  29  LYS   B HE2  1 
ATOM   4442 H  HE2  B LYS   B 1 29  ? 52.080 -24.960 -17.176 0.40 39.43 ?  29  LYS   B HE2  1 
ATOM   4443 H  HE3  A LYS   B 1 29  ? 51.097 -24.748 -18.462 0.60 41.67 ?  29  LYS   B HE3  1 
ATOM   4444 H  HE3  B LYS   B 1 29  ? 51.294 -24.776 -18.546 0.40 39.43 ?  29  LYS   B HE3  1 
ATOM   4445 H  HZ1  A LYS   B 1 29  ? 51.539 -26.952 -18.100 0.60 42.95 ?  29  LYS   B HZ1  1 
ATOM   4446 H  HZ1  B LYS   B 1 29  ? 51.685 -26.980 -18.140 0.40 40.51 ?  29  LYS   B HZ1  1 
ATOM   4447 H  HZ2  A LYS   B 1 29  ? 52.157 -26.560 -19.350 0.60 42.95 ?  29  LYS   B HZ2  1 
ATOM   4448 H  HZ2  B LYS   B 1 29  ? 52.400 -26.602 -19.342 0.40 40.51 ?  29  LYS   B HZ2  1 
ATOM   4449 H  HZ3  A LYS   B 1 29  ? 52.968 -26.725 -18.161 0.60 42.95 ?  29  LYS   B HZ3  1 
ATOM   4450 H  HZ3  B LYS   B 1 29  ? 53.117 -26.768 -18.093 0.40 40.51 ?  29  LYS   B HZ3  1 
ATOM   4451 N  N    . VAL   B 1 30  ? 50.888 -20.241 -16.155 1.00 19.46 ?  30  VAL   B N    1 
ATOM   4452 C  CA   . VAL   B 1 30  ? 49.602 -19.639 -16.529 1.00 19.15 ?  30  VAL   B CA   1 
ATOM   4453 C  C    . VAL   B 1 30  ? 49.604 -18.123 -16.390 1.00 18.13 ?  30  VAL   B C    1 
ATOM   4454 O  O    . VAL   B 1 30  ? 48.856 -17.424 -17.094 1.00 19.27 ?  30  VAL   B O    1 
ATOM   4455 C  CB   . VAL   B 1 30  ? 48.498 -20.255 -15.644 1.00 20.38 ?  30  VAL   B CB   1 
ATOM   4456 C  CG1  . VAL   B 1 30  ? 47.210 -19.445 -15.712 1.00 20.71 ?  30  VAL   B CG1  1 
ATOM   4457 C  CG2  . VAL   B 1 30  ? 48.252 -21.706 -16.030 1.00 21.33 ?  30  VAL   B CG2  1 
ATOM   4458 H  H    A VAL   B 1 30  ? 50.879 -20.638 -15.385 0.60 23.40 ?  30  VAL   B H    1 
ATOM   4459 H  H    B VAL   B 1 30  ? 50.877 -20.647 -15.389 0.40 23.40 ?  30  VAL   B H    1 
ATOM   4460 H  HA   . VAL   B 1 30  ? 49.403 -19.868 -17.447 1.00 23.02 ?  30  VAL   B HA   1 
ATOM   4461 H  HB   . VAL   B 1 30  ? 48.794 -20.257 -14.721 1.00 24.50 ?  30  VAL   B HB   1 
ATOM   4462 H  HG11 . VAL   B 1 30  ? 46.470 -20.023 -15.463 1.00 24.89 ?  30  VAL   B HG11 1 
ATOM   4463 H  HG12 . VAL   B 1 30  ? 47.267 -18.705 -15.093 1.00 24.89 ?  30  VAL   B HG12 1 
ATOM   4464 H  HG13 . VAL   B 1 30  ? 47.080 -19.130 -16.615 1.00 24.89 ?  30  VAL   B HG13 1 
ATOM   4465 H  HG21 . VAL   B 1 30  ? 47.560 -22.079 -15.453 1.00 25.63 ?  30  VAL   B HG21 1 
ATOM   4466 H  HG22 . VAL   B 1 30  ? 47.957 -21.744 -16.955 1.00 25.63 ?  30  VAL   B HG22 1 
ATOM   4467 H  HG23 . VAL   B 1 30  ? 49.072 -22.209 -15.923 1.00 25.63 ?  30  VAL   B HG23 1 
ATOM   4468 N  N    . LYS   B 1 31  ? 50.382 -17.610 -15.452 1.00 17.70 ?  31  LYS   B N    1 
ATOM   4469 C  CA   . LYS   B 1 31  ? 50.404 -16.199 -15.096 1.00 18.37 ?  31  LYS   B CA   1 
ATOM   4470 C  C    . LYS   B 1 31  ? 49.007 -15.715 -14.697 1.00 16.25 ?  31  LYS   B C    1 
ATOM   4471 O  O    . LYS   B 1 31  ? 48.470 -14.784 -15.311 1.00 17.30 ?  31  LYS   B O    1 
ATOM   4472 C  CB   . LYS   B 1 31  ? 51.040 -15.393 -16.235 1.00 21.81 ?  31  LYS   B CB   1 
ATOM   4473 C  CG   . LYS   B 1 31  ? 52.477 -15.828 -16.540 1.00 25.33 ?  31  LYS   B CG   1 
ATOM   4474 C  CD   . LYS   B 1 31  ? 53.068 -15.057 -17.703 1.00 29.30 ?  31  LYS   B CD   1 
ATOM   4475 C  CE   . LYS   B 1 31  ? 54.558 -15.290 -17.824 1.00 32.12 ?  31  LYS   B CE   1 
ATOM   4476 N  NZ   . LYS   B 1 31  ? 55.256 -14.871 -16.580 1.00 34.12 ?  31  LYS   B NZ   1 
ATOM   4477 H  H    . LYS   B 1 31  ? 50.928 -18.092 -14.998 1.00 21.29 ?  31  LYS   B H    1 
ATOM   4478 H  HA   . LYS   B 1 31  ? 50.966 -16.112 -14.327 1.00 22.09 ?  31  LYS   B HA   1 
ATOM   4479 H  HB2  . LYS   B 1 31  ? 50.520 -15.511 -17.047 1.00 26.21 ?  31  LYS   B HB2  1 
ATOM   4480 H  HB3  . LYS   B 1 31  ? 51.060 -14.463 -15.981 1.00 26.21 ?  31  LYS   B HB3  1 
ATOM   4481 H  HG2  . LYS   B 1 31  ? 53.021 -15.676 -15.752 1.00 30.44 ?  31  LYS   B HG2  1 
ATOM   4482 H  HG3  . LYS   B 1 31  ? 52.482 -16.774 -16.768 1.00 30.44 ?  31  LYS   B HG3  1 
ATOM   4483 H  HD2  . LYS   B 1 31  ? 52.645 -15.350 -18.523 1.00 35.21 ?  31  LYS   B HD2  1 
ATOM   4484 H  HD3  . LYS   B 1 31  ? 52.917 -14.112 -17.561 1.00 35.21 ?  31  LYS   B HD3  1 
ATOM   4485 H  HE2  . LYS   B 1 31  ? 54.730 -16.234 -17.970 1.00 38.58 ?  31  LYS   B HE2  1 
ATOM   4486 H  HE3  . LYS   B 1 31  ? 54.906 -14.765 -18.563 1.00 38.58 ?  31  LYS   B HE3  1 
ATOM   4487 H  HZ1  . LYS   B 1 31  ? 56.134 -14.855 -16.714 1.00 40.98 ?  31  LYS   B HZ1  1 
ATOM   4488 H  HZ2  . LYS   B 1 31  ? 54.983 -14.058 -16.340 1.00 40.98 ?  31  LYS   B HZ2  1 
ATOM   4489 H  HZ3  . LYS   B 1 31  ? 55.072 -15.442 -15.922 1.00 40.98 ?  31  LYS   B HZ3  1 
ATOM   4490 N  N    . PRO   B 1 32  ? 48.395 -16.312 -13.666 1.00 13.63 ?  32  PRO   B N    1 
ATOM   4491 C  CA   . PRO   B 1 32  ? 47.019 -15.949 -13.308 1.00 12.68 ?  32  PRO   B CA   1 
ATOM   4492 C  C    . PRO   B 1 32  ? 46.942 -14.605 -12.602 1.00 12.95 ?  32  PRO   B C    1 
ATOM   4493 O  O    . PRO   B 1 32  ? 47.867 -14.182 -11.902 1.00 14.43 ?  32  PRO   B O    1 
ATOM   4494 C  CB   . PRO   B 1 32  ? 46.614 -17.066 -12.339 1.00 12.73 ?  32  PRO   B CB   1 
ATOM   4495 C  CG   . PRO   B 1 32  ? 47.911 -17.415 -11.659 1.00 13.21 ?  32  PRO   B CG   1 
ATOM   4496 C  CD   . PRO   B 1 32  ? 48.966 -17.290 -12.717 1.00 13.63 ?  32  PRO   B CD   1 
ATOM   4497 H  HA   . PRO   B 1 32  ? 46.438 -15.960 -14.091 1.00 15.26 ?  32  PRO   B HA   1 
ATOM   4498 H  HB2  . PRO   B 1 32  ? 45.962 -16.732 -11.704 1.00 15.32 ?  32  PRO   B HB2  1 
ATOM   4499 H  HB3  . PRO   B 1 32  ? 46.264 -17.826 -12.833 1.00 15.32 ?  32  PRO   B HB3  1 
ATOM   4500 H  HG2  . PRO   B 1 32  ? 48.076 -16.788 -10.934 1.00 15.90 ?  32  PRO   B HG2  1 
ATOM   4501 H  HG3  . PRO   B 1 32  ? 47.871 -18.323 -11.322 1.00 15.90 ?  32  PRO   B HG3  1 
ATOM   4502 H  HD2  . PRO   B 1 32  ? 49.783 -16.939 -12.337 1.00 16.40 ?  32  PRO   B HD2  1 
ATOM   4503 H  HD3  . PRO   B 1 32  ? 49.105 -18.140 -13.153 1.00 16.40 ?  32  PRO   B HD3  1 
ATOM   4504 N  N    . THR   B 1 33  ? 45.791 -13.951 -12.769 1.00 12.29 ?  33  THR   B N    1 
ATOM   4505 C  CA   . THR   B 1 33  ? 45.497 -12.773 -11.962 1.00 12.52 ?  33  THR   B CA   1 
ATOM   4506 C  C    . THR   B 1 33  ? 45.452 -13.122 -10.479 1.00 12.33 ?  33  THR   B C    1 
ATOM   4507 O  O    . THR   B 1 33  ? 45.930 -12.345 -9.639  1.00 13.37 ?  33  THR   B O    1 
ATOM   4508 C  CB   . THR   B 1 33  ? 44.180 -12.137 -12.412 1.00 13.27 ?  33  THR   B CB   1 
ATOM   4509 O  OG1  . THR   B 1 33  ? 44.228 -11.881 -13.817 1.00 13.43 ?  33  THR   B OG1  1 
ATOM   4510 C  CG2  . THR   B 1 33  ? 43.925 -10.838 -11.659 1.00 14.75 ?  33  THR   B CG2  1 
ATOM   4511 H  H    . THR   B 1 33  ? 45.172 -14.168 -13.333 1.00 14.79 ?  33  THR   B H    1 
ATOM   4512 H  HA   . THR   B 1 33  ? 46.198 -12.121 -12.093 1.00 15.07 ?  33  THR   B HA   1 
ATOM   4513 H  HB   . THR   B 1 33  ? 43.445 -12.747 -12.224 1.00 15.96 ?  33  THR   B HB   1 
ATOM   4514 H  HG1  . THR   B 1 33  ? 43.507 -11.514 -14.069 1.00 16.16 ?  33  THR   B HG1  1 
ATOM   4515 H  HG21 . THR   B 1 33  ? 43.170 -10.374 -12.048 1.00 17.75 ?  33  THR   B HG21 1 
ATOM   4516 H  HG22 . THR   B 1 33  ? 43.736 -11.026 -10.726 1.00 17.75 ?  33  THR   B HG22 1 
ATOM   4517 H  HG23 . THR   B 1 33  ? 44.709 -10.269 -11.714 1.00 17.75 ?  33  THR   B HG23 1 
ATOM   4518 N  N    . VAL   B 1 34  ? 44.898 -14.290 -10.137 1.00 11.61 ?  34  VAL   B N    1 
ATOM   4519 C  CA   . VAL   B 1 34  ? 44.709 -14.691 -8.746  1.00 10.94 ?  34  VAL   B CA   1 
ATOM   4520 C  C    . VAL   B 1 34  ? 45.133 -16.143 -8.578  1.00 10.23 ?  34  VAL   B C    1 
ATOM   4521 O  O    . VAL   B 1 34  ? 44.606 -17.030 -9.261  1.00 11.03 ?  34  VAL   B O    1 
ATOM   4522 C  CB   . VAL   B 1 34  ? 43.238 -14.553 -8.298  1.00 12.23 ?  34  VAL   B CB   1 
ATOM   4523 C  CG1  . VAL   B 1 34  ? 43.071 -15.013 -6.854  1.00 12.43 ?  34  VAL   B CG1  1 
ATOM   4524 C  CG2  . VAL   B 1 34  ? 42.725 -13.130 -8.489  1.00 13.31 ?  34  VAL   B CG2  1 
ATOM   4525 H  H    . VAL   B 1 34  ? 44.630 -14.882 -10.705 1.00 13.97 ?  34  VAL   B H    1 
ATOM   4526 H  HA   . VAL   B 1 34  ? 45.264 -14.141 -8.169  1.00 13.17 ?  34  VAL   B HA   1 
ATOM   4527 H  HB   . VAL   B 1 34  ? 42.697 -15.134 -8.856  1.00 14.72 ?  34  VAL   B HB   1 
ATOM   4528 H  HG11 . VAL   B 1 34  ? 42.218 -14.696 -6.520  1.00 14.95 ?  34  VAL   B HG11 1 
ATOM   4529 H  HG12 . VAL   B 1 34  ? 43.095 -15.984 -6.824  1.00 14.95 ?  34  VAL   B HG12 1 
ATOM   4530 H  HG13 . VAL   B 1 34  ? 43.792 -14.647 -6.319  1.00 14.95 ?  34  VAL   B HG13 1 
ATOM   4531 H  HG21 . VAL   B 1 34  ? 41.805 -13.083 -8.182  1.00 16.02 ?  34  VAL   B HG21 1 
ATOM   4532 H  HG22 . VAL   B 1 34  ? 43.277 -12.521 -7.978  1.00 16.02 ?  34  VAL   B HG22 1 
ATOM   4533 H  HG23 . VAL   B 1 34  ? 42.767 -12.901 -9.434  1.00 16.02 ?  34  VAL   B HG23 1 
ATOM   4534 N  N    . VAL   B 1 35  ? 46.038 -16.394 -7.632  1.00 9.93  ?  35  VAL   B N    1 
ATOM   4535 C  CA   . VAL   B 1 35  ? 46.269 -17.737 -7.113  1.00 9.75  ?  35  VAL   B CA   1 
ATOM   4536 C  C    . VAL   B 1 35  ? 45.730 -17.791 -5.692  1.00 9.35  ?  35  VAL   B C    1 
ATOM   4537 O  O    . VAL   B 1 35  ? 45.948 -16.869 -4.899  1.00 9.97  ?  35  VAL   B O    1 
ATOM   4538 C  CB   . VAL   B 1 35  ? 47.753 -18.165 -7.196  1.00 10.35 ?  35  VAL   B CB   1 
ATOM   4539 C  CG1  . VAL   B 1 35  ? 48.661 -17.314 -6.292  1.00 11.01 ?  35  VAL   B CG1  1 
ATOM   4540 C  CG2  . VAL   B 1 35  ? 47.896 -19.653 -6.873  1.00 10.92 ?  35  VAL   B CG2  1 
ATOM   4541 H  H    . VAL   B 1 35  ? 46.544 -15.793 -7.277  1.00 11.96 ?  35  VAL   B H    1 
ATOM   4542 H  HA   . VAL   B 1 35  ? 45.757 -18.367 -7.638  1.00 11.75 ?  35  VAL   B HA   1 
ATOM   4543 H  HB   . VAL   B 1 35  ? 48.056 -18.043 -8.112  1.00 12.47 ?  35  VAL   B HB   1 
ATOM   4544 H  HG11 . VAL   B 1 35  ? 49.583 -17.553 -6.463  1.00 13.25 ?  35  VAL   B HG11 1 
ATOM   4545 H  HG12 . VAL   B 1 35  ? 48.509 -16.383 -6.488  1.00 13.25 ?  35  VAL   B HG12 1 
ATOM   4546 H  HG13 . VAL   B 1 35  ? 48.437 -17.503 -5.364  1.00 13.25 ?  35  VAL   B HG13 1 
ATOM   4547 H  HG21 . VAL   B 1 35  ? 48.818 -19.922 -6.984  1.00 13.15 ?  35  VAL   B HG21 1 
ATOM   4548 H  HG22 . VAL   B 1 35  ? 47.613 -19.810 -5.955  1.00 13.15 ?  35  VAL   B HG22 1 
ATOM   4549 H  HG23 . VAL   B 1 35  ? 47.328 -20.169 -7.476  1.00 13.15 ?  35  VAL   B HG23 1 
ATOM   4550 N  N    . VAL   B 1 36  ? 45.008 -18.867 -5.375  1.00 9.33  ?  36  VAL   B N    1 
ATOM   4551 C  CA   . VAL   B 1 36  ? 44.465 -19.072 -4.042  1.00 9.20  ?  36  VAL   B CA   1 
ATOM   4552 C  C    . VAL   B 1 36  ? 45.477 -19.831 -3.190  1.00 8.87  ?  36  VAL   B C    1 
ATOM   4553 O  O    . VAL   B 1 36  ? 46.018 -20.863 -3.613  1.00 10.02 ?  36  VAL   B O    1 
ATOM   4554 C  CB   . VAL   B 1 36  ? 43.131 -19.834 -4.113  1.00 9.58  ?  36  VAL   B CB   1 
ATOM   4555 C  CG1  . VAL   B 1 36  ? 42.628 -20.201 -2.727  1.00 10.06 ?  36  VAL   B CG1  1 
ATOM   4556 C  CG2  . VAL   B 1 36  ? 42.095 -19.000 -4.857  1.00 10.40 ?  36  VAL   B CG2  1 
ATOM   4557 H  H    . VAL   B 1 36  ? 44.824 -19.503 -5.925  1.00 11.24 ?  36  VAL   B H    1 
ATOM   4558 H  HA   . VAL   B 1 36  ? 44.298 -18.212 -3.625  1.00 11.08 ?  36  VAL   B HA   1 
ATOM   4559 H  HB   . VAL   B 1 36  ? 43.259 -20.654 -4.612  1.00 11.53 ?  36  VAL   B HB   1 
ATOM   4560 H  HG11 . VAL   B 1 36  ? 41.687 -20.440 -2.782  1.00 12.11 ?  36  VAL   B HG11 1 
ATOM   4561 H  HG12 . VAL   B 1 36  ? 43.138 -20.951 -2.389  1.00 12.11 ?  36  VAL   B HG12 1 
ATOM   4562 H  HG13 . VAL   B 1 36  ? 42.732 -19.434 -2.138  1.00 12.11 ?  36  VAL   B HG13 1 
ATOM   4563 H  HG21 . VAL   B 1 36  ? 41.252 -19.480 -4.878  1.00 12.52 ?  36  VAL   B HG21 1 
ATOM   4564 H  HG22 . VAL   B 1 36  ? 41.979 -18.151 -4.399  1.00 12.52 ?  36  VAL   B HG22 1 
ATOM   4565 H  HG23 . VAL   B 1 36  ? 42.405 -18.841 -5.765  1.00 12.52 ?  36  VAL   B HG23 1 
ATOM   4566 N  N    . ASN   B 1 37  ? 45.696 -19.338 -1.973  1.00 9.23  ?  37  ASN   B N    1 
ATOM   4567 C  CA   . ASN   B 1 37  ? 46.445 -20.062 -0.960  1.00 9.65  ?  37  ASN   B CA   1 
ATOM   4568 C  C    . ASN   B 1 37  ? 45.499 -20.734 0.026   1.00 9.48  ?  37  ASN   B C    1 
ATOM   4569 O  O    . ASN   B 1 37  ? 44.485 -20.157 0.436   1.00 10.13 ?  37  ASN   B O    1 
ATOM   4570 C  CB   . ASN   B 1 37  ? 47.375 -19.118 -0.199  1.00 9.84  ?  37  ASN   B CB   1 
ATOM   4571 C  CG   . ASN   B 1 37  ? 48.235 -19.833 0.812   1.00 9.89  ?  37  ASN   B CG   1 
ATOM   4572 O  OD1  . ASN   B 1 37  ? 48.573 -21.013 0.638   1.00 10.75 ?  37  ASN   B OD1  1 
ATOM   4573 N  ND2  . ASN   B 1 37  ? 48.583 -19.129 1.888   1.00 10.14 ?  37  ASN   B ND2  1 
ATOM   4574 H  H    . ASN   B 1 37  ? 45.414 -18.567 -1.704  1.00 11.12 ?  37  ASN   B H    1 
ATOM   4575 H  HA   . ASN   B 1 37  ? 46.977 -20.755 -1.379  1.00 11.62 ?  37  ASN   B HA   1 
ATOM   4576 H  HB2  . ASN   B 1 37  ? 47.962 -18.686 -0.834  1.00 11.86 ?  37  ASN   B HB2  1 
ATOM   4577 H  HB3  . ASN   B 1 37  ? 46.844 -18.462 0.272   1.00 11.86 ?  37  ASN   B HB3  1 
ATOM   4578 H  HD21 . ASN   B 1 37  ? 49.075 -19.487 2.496   1.00 12.21 ?  37  ASN   B HD21 1 
ATOM   4579 H  HD22 . ASN   B 1 37  ? 48.325 -18.318 1.975   1.00 12.21 ?  37  ASN   B HD22 1 
ATOM   4580 N  N    . ALA   B 1 38  ? 45.849 -21.965 0.400   1.00 9.72  ?  38  ALA   B N    1 
ATOM   4581 C  CA   . ALA   B 1 38  ? 45.200 -22.712 1.478   1.00 10.41 ?  38  ALA   B CA   1 
ATOM   4582 C  C    . ALA   B 1 38  ? 45.785 -22.228 2.804   1.00 9.96  ?  38  ALA   B C    1 
ATOM   4583 O  O    . ALA   B 1 38  ? 46.691 -22.835 3.387   1.00 10.80 ?  38  ALA   B O    1 
ATOM   4584 C  CB   . ALA   B 1 38  ? 45.426 -24.204 1.280   1.00 11.02 ?  38  ALA   B CB   1 
ATOM   4585 H  H    . ALA   B 1 38  ? 46.502 -22.398 0.048   1.00 11.70 ?  38  ALA   B H    1 
ATOM   4586 H  HA   . ALA   B 1 38  ? 44.246 -22.534 1.475   1.00 12.53 ?  38  ALA   B HA   1 
ATOM   4587 H  HB1  . ALA   B 1 38  ? 44.980 -24.689 2.000   1.00 13.27 ?  38  ALA   B HB1  1 
ATOM   4588 H  HB2  . ALA   B 1 38  ? 45.043 -24.470 0.427   1.00 13.27 ?  38  ALA   B HB2  1 
ATOM   4589 H  HB3  . ALA   B 1 38  ? 46.372 -24.390 1.295   1.00 13.27 ?  38  ALA   B HB3  1 
ATOM   4590 N  N    . ALA   B 1 39  ? 45.264 -21.088 3.265   1.00 9.81  ?  39  ALA   B N    1 
ATOM   4591 C  CA   . ALA   B 1 39  ? 45.811 -20.345 4.390   1.00 10.31 ?  39  ALA   B CA   1 
ATOM   4592 C  C    . ALA   B 1 39  ? 45.195 -20.789 5.714   1.00 10.21 ?  39  ALA   B C    1 
ATOM   4593 O  O    . ALA   B 1 39  ? 44.169 -21.468 5.765   1.00 11.17 ?  39  ALA   B O    1 
ATOM   4594 C  CB   . ALA   B 1 39  ? 45.568 -18.845 4.187   1.00 10.88 ?  39  ALA   B CB   1 
ATOM   4595 H  H    . ALA   B 1 39  ? 44.565 -20.722 2.926   1.00 11.82 ?  39  ALA   B H    1 
ATOM   4596 H  HA   . ALA   B 1 39  ? 46.764 -20.494 4.435   1.00 12.41 ?  39  ALA   B HA   1 
ATOM   4597 H  HB1  . ALA   B 1 39  ? 45.936 -18.361 4.942   1.00 13.10 ?  39  ALA   B HB1  1 
ATOM   4598 H  HB2  . ALA   B 1 39  ? 46.007 -18.563 3.368   1.00 13.10 ?  39  ALA   B HB2  1 
ATOM   4599 H  HB3  . ALA   B 1 39  ? 44.614 -18.682 4.123   1.00 13.10 ?  39  ALA   B HB3  1 
ATOM   4600 N  N    . ASN   B 1 40  ? 45.842 -20.373 6.800   1.00 10.92 ?  40  ASN   B N    1 
ATOM   4601 C  CA   . ASN   B 1 40  ? 45.278 -20.413 8.142   1.00 11.72 ?  40  ASN   B CA   1 
ATOM   4602 C  C    . ASN   B 1 40  ? 45.096 -18.985 8.664   1.00 11.38 ?  40  ASN   B C    1 
ATOM   4603 O  O    . ASN   B 1 40  ? 45.506 -18.007 8.034   1.00 11.35 ?  40  ASN   B O    1 
ATOM   4604 C  CB   . ASN   B 1 40  ? 46.126 -21.283 9.086   1.00 12.54 ?  40  ASN   B CB   1 
ATOM   4605 C  CG   . ASN   B 1 40  ? 47.576 -20.878 9.118   1.00 13.54 ?  40  ASN   B CG   1 
ATOM   4606 O  OD1  . ASN   B 1 40  ? 47.895 -19.697 9.179   1.00 15.85 ?  40  ASN   B OD1  1 
ATOM   4607 N  ND2  . ASN   B 1 40  ? 48.468 -21.857 9.084   1.00 13.50 ?  40  ASN   B ND2  1 
ATOM   4608 H  H    . ASN   B 1 40  ? 46.643 -20.060 6.781   1.00 13.15 ?  40  ASN   B H    1 
ATOM   4609 H  HA   . ASN   B 1 40  ? 44.396 -20.808 8.096   1.00 14.11 ?  40  ASN   B HA   1 
ATOM   4610 H  HB2  . ASN   B 1 40  ? 45.772 -21.205 9.987   1.00 15.09 ?  40  ASN   B HB2  1 
ATOM   4611 H  HB3  . ASN   B 1 40  ? 46.074 -22.204 8.789   1.00 15.09 ?  40  ASN   B HB3  1 
ATOM   4612 H  HD21 . ASN   B 1 40  ? 49.310 -21.677 9.102   1.00 16.25 ?  40  ASN   B HD21 1 
ATOM   4613 H  HD22 . ASN   B 1 40  ? 48.206 -22.676 9.042   1.00 16.25 ?  40  ASN   B HD22 1 
ATOM   4614 N  N    . VAL   B 1 41  ? 44.438 -18.860 9.819   1.00 11.99 ?  41  VAL   B N    1 
ATOM   4615 C  CA   . VAL   B 1 41  ? 43.981 -17.540 10.265  1.00 12.34 ?  41  VAL   B CA   1 
ATOM   4616 C  C    . VAL   B 1 41  ? 45.132 -16.590 10.567  1.00 12.21 ?  41  VAL   B C    1 
ATOM   4617 O  O    . VAL   B 1 41  ? 44.952 -15.371 10.487  1.00 12.52 ?  41  VAL   B O    1 
ATOM   4618 C  CB   . VAL   B 1 41  ? 43.003 -17.607 11.452  1.00 14.06 ?  41  VAL   B CB   1 
ATOM   4619 C  CG1  . VAL   B 1 41  ? 41.702 -18.286 11.050  1.00 14.53 ?  41  VAL   B CG1  1 
ATOM   4620 C  CG2  . VAL   B 1 41  ? 43.652 -18.287 12.647  1.00 14.92 ?  41  VAL   B CG2  1 
ATOM   4621 H  H    . VAL   B 1 41  ? 44.244 -19.503 10.348  1.00 14.43 ?  41  VAL   B H    1 
ATOM   4622 H  HA   . VAL   B 1 41  ? 43.489 -17.139 9.532   1.00 14.85 ?  41  VAL   B HA   1 
ATOM   4623 H  HB   . VAL   B 1 41  ? 42.782 -16.700 11.721  1.00 16.92 ?  41  VAL   B HB   1 
ATOM   4624 H  HG11 . VAL   B 1 41  ? 41.097 -18.286 11.810  1.00 17.47 ?  41  VAL   B HG11 1 
ATOM   4625 H  HG12 . VAL   B 1 41  ? 41.303 -17.795 10.313  1.00 17.47 ?  41  VAL   B HG12 1 
ATOM   4626 H  HG13 . VAL   B 1 41  ? 41.891 -19.196 10.778  1.00 17.47 ?  41  VAL   B HG13 1 
ATOM   4627 H  HG21 . VAL   B 1 41  ? 43.012 -18.329 13.371  1.00 17.95 ?  41  VAL   B HG21 1 
ATOM   4628 H  HG22 . VAL   B 1 41  ? 43.922 -19.183 12.389  1.00 17.95 ?  41  VAL   B HG22 1 
ATOM   4629 H  HG23 . VAL   B 1 41  ? 44.429 -17.773 12.918  1.00 17.95 ?  41  VAL   B HG23 1 
ATOM   4630 N  N    . TYR   B 1 42  ? 46.302 -17.106 10.944  1.00 12.45 ?  42  TYR   B N    1 
ATOM   4631 C  CA   . TYR   B 1 42  ? 47.458 -16.261 11.219  1.00 12.98 ?  42  TYR   B CA   1 
ATOM   4632 C  C    . TYR   B 1 42  ? 48.425 -16.183 10.039  1.00 12.27 ?  42  TYR   B C    1 
ATOM   4633 O  O    . TYR   B 1 42  ? 49.515 -15.615 10.178  1.00 13.38 ?  42  TYR   B O    1 
ATOM   4634 C  CB   . TYR   B 1 42  ? 48.152 -16.674 12.523  1.00 14.56 ?  42  TYR   B CB   1 
ATOM   4635 C  CG   . TYR   B 1 42  ? 47.556 -15.984 13.749  1.00 14.89 ?  42  TYR   B CG   1 
ATOM   4636 C  CD1  . TYR   B 1 42  ? 47.779 -14.630 13.978  1.00 14.12 ?  42  TYR   B CD1  1 
ATOM   4637 C  CD2  . TYR   B 1 42  ? 46.771 -16.675 14.660  1.00 16.90 ?  42  TYR   B CD2  1 
ATOM   4638 C  CE1  . TYR   B 1 42  ? 47.242 -13.985 15.076  1.00 15.11 ?  42  TYR   B CE1  1 
ATOM   4639 C  CE2  . TYR   B 1 42  ? 46.232 -16.036 15.769  1.00 17.32 ?  42  TYR   B CE2  1 
ATOM   4640 C  CZ   . TYR   B 1 42  ? 46.470 -14.688 15.971  1.00 17.41 ?  42  TYR   B CZ   1 
ATOM   4641 O  OH   . TYR   B 1 42  ? 45.943 -14.037 17.070  1.00 20.23 ?  42  TYR   B OH   1 
ATOM   4642 H  H    . TYR   B 1 42  ? 46.451 -17.952 11.040  1.00 14.98 ?  42  TYR   B H    1 
ATOM   4643 H  HA   . TYR   B 1 42  ? 47.131 -15.363 11.357  1.00 15.62 ?  42  TYR   B HA   1 
ATOM   4644 H  HB2  . TYR   B 1 42  ? 48.060 -17.631 12.641  1.00 17.51 ?  42  TYR   B HB2  1 
ATOM   4645 H  HB3  . TYR   B 1 42  ? 49.090 -16.434 12.468  1.00 17.51 ?  42  TYR   B HB3  1 
ATOM   4646 H  HD1  . TYR   B 1 42  ? 48.304 -14.148 13.369  1.00 16.99 ?  42  TYR   B HD1  1 
ATOM   4647 H  HD2  . TYR   B 1 42  ? 46.605 -17.583 14.523  1.00 20.32 ?  42  TYR   B HD2  1 
ATOM   4648 H  HE1  . TYR   B 1 42  ? 47.408 -13.078 15.208  1.00 18.18 ?  42  TYR   B HE1  1 
ATOM   4649 H  HE2  . TYR   B 1 42  ? 45.706 -16.515 16.367  1.00 20.82 ?  42  TYR   B HE2  1 
ATOM   4650 H  HH   . TYR   B 1 42  ? 46.170 -13.232 17.052  1.00 24.32 ?  42  TYR   B HH   1 
ATOM   4651 N  N    . LEU   B 1 43  ? 48.028 -16.698 8.876   1.00 11.22 ?  43  LEU   B N    1 
ATOM   4652 C  CA   . LEU   B 1 43  ? 48.844 -16.629 7.666   1.00 11.24 ?  43  LEU   B CA   1 
ATOM   4653 C  C    . LEU   B 1 43  ? 50.257 -17.137 7.921   1.00 11.38 ?  43  LEU   B C    1 
ATOM   4654 O  O    . LEU   B 1 43  ? 51.240 -16.545 7.472   1.00 12.16 ?  43  LEU   B O    1 
ATOM   4655 C  CB   . LEU   B 1 43  ? 48.857 -15.225 7.058   1.00 11.43 ?  43  LEU   B CB   1 
ATOM   4656 C  CG   . LEU   B 1 43  ? 47.502 -14.614 6.680   1.00 11.51 ?  43  LEU   B CG   1 
ATOM   4657 C  CD1  . LEU   B 1 43  ? 47.711 -13.220 6.112   1.00 12.88 ?  43  LEU   B CD1  1 
ATOM   4658 C  CD2  . LEU   B 1 43  ? 46.753 -15.503 5.694   1.00 11.73 ?  43  LEU   B CD2  1 
ATOM   4659 H  H    . LEU   B 1 43  ? 47.283 -17.110 8.758   1.00 13.50 ?  43  LEU   B H    1 
ATOM   4660 H  HA   . LEU   B 1 43  ? 48.450 -17.221 7.003   1.00 13.53 ?  43  LEU   B HA   1 
ATOM   4661 H  HB2  . LEU   B 1 43  ? 49.277 -14.628 7.693   1.00 13.76 ?  43  LEU   B HB2  1 
ATOM   4662 H  HB3  . LEU   B 1 43  ? 49.389 -15.257 6.247   1.00 13.76 ?  43  LEU   B HB3  1 
ATOM   4663 H  HG   . LEU   B 1 43  ? 46.963 -14.531 7.481   1.00 13.85 ?  43  LEU   B HG   1 
ATOM   4664 H  HD11 . LEU   B 1 43  ? 46.848 -12.841 5.880   1.00 15.50 ?  43  LEU   B HD11 1 
ATOM   4665 H  HD12 . LEU   B 1 43  ? 48.143 -12.665 6.783   1.00 15.50 ?  43  LEU   B HD12 1 
ATOM   4666 H  HD13 . LEU   B 1 43  ? 48.270 -13.278 5.323   1.00 15.50 ?  43  LEU   B HD13 1 
ATOM   4667 H  HD21 . LEU   B 1 43  ? 45.954 -15.042 5.400   1.00 14.12 ?  43  LEU   B HD21 1 
ATOM   4668 H  HD22 . LEU   B 1 43  ? 47.330 -15.687 4.936   1.00 14.12 ?  43  LEU   B HD22 1 
ATOM   4669 H  HD23 . LEU   B 1 43  ? 46.515 -16.332 6.137   1.00 14.12 ?  43  LEU   B HD23 1 
ATOM   4670 N  N    . LYS   B 1 44  ? 50.358 -18.262 8.635   1.00 11.54 ?  44  LYS   B N    1 
ATOM   4671 C  CA   . LYS   B 1 44  ? 51.628 -18.934 8.874   1.00 12.19 ?  44  LYS   B CA   1 
ATOM   4672 C  C    . LYS   B 1 44  ? 51.748 -20.056 7.850   1.00 11.65 ?  44  LYS   B C    1 
ATOM   4673 O  O    . LYS   B 1 44  ? 51.048 -21.073 7.939   1.00 13.00 ?  44  LYS   B O    1 
ATOM   4674 C  CB   . LYS   B 1 44  ? 51.689 -19.446 10.311  1.00 13.81 ?  44  LYS   B CB   1 
ATOM   4675 C  CG   . LYS   B 1 44  ? 51.865 -18.337 11.335  1.00 16.49 ?  44  LYS   B CG   1 
ATOM   4676 C  CD   . LYS   B 1 44  ? 53.064 -17.466 10.948  1.00 19.78 ?  44  LYS   B CD   1 
ATOM   4677 C  CE   . LYS   B 1 44  ? 53.554 -16.580 12.063  1.00 22.80 ?  44  LYS   B CE   1 
ATOM   4678 N  NZ   . LYS   B 1 44  ? 54.733 -15.773 11.660  1.00 24.25 ?  44  LYS   B NZ   1 
ATOM   4679 H  H    . LYS   B 1 44  ? 49.686 -18.653 9.002   1.00 13.89 ?  44  LYS   B H    1 
ATOM   4680 H  HA   . LYS   B 1 44  ? 52.356 -18.315 8.713   1.00 14.67 ?  44  LYS   B HA   1 
ATOM   4681 H  HB2  . LYS   B 1 44  ? 50.855 -19.904 10.517  1.00 16.62 ?  44  LYS   B HB2  1 
ATOM   4682 H  HB3  . LYS   B 1 44  ? 52.432 -20.055 10.400  1.00 16.62 ?  44  LYS   B HB3  1 
ATOM   4683 H  HG2  . LYS   B 1 44  ? 51.071 -17.785 11.362  1.00 19.83 ?  44  LYS   B HG2  1 
ATOM   4684 H  HG3  . LYS   B 1 44  ? 52.039 -18.730 12.209  1.00 19.83 ?  44  LYS   B HG3  1 
ATOM   4685 H  HD2  . LYS   B 1 44  ? 53.792 -18.048 10.663  1.00 23.78 ?  44  LYS   B HD2  1 
ATOM   4686 H  HD3  . LYS   B 1 44  ? 52.800 -16.890 10.212  1.00 23.78 ?  44  LYS   B HD3  1 
ATOM   4687 H  HE2  . LYS   B 1 44  ? 52.853 -15.959 12.279  1.00 27.41 ?  44  LYS   B HE2  1 
ATOM   4688 H  HE3  . LYS   B 1 44  ? 53.791 -17.125 12.832  1.00 27.41 ?  44  LYS   B HE3  1 
ATOM   4689 H  HZ1  . LYS   B 1 44  ? 54.991 -15.256 12.337  1.00 29.14 ?  44  LYS   B HZ1  1 
ATOM   4690 H  HZ2  . LYS   B 1 44  ? 55.406 -16.304 11.426  1.00 29.14 ?  44  LYS   B HZ2  1 
ATOM   4691 H  HZ3  . LYS   B 1 44  ? 54.521 -15.253 10.967  1.00 29.14 ?  44  LYS   B HZ3  1 
ATOM   4692 N  N    . HIS   B 1 45  ? 52.604 -19.843 6.852   1.00 11.76 ?  45  HIS   B N    1 
ATOM   4693 C  CA   . HIS   B 1 45  ? 52.620 -20.673 5.649   1.00 11.60 ?  45  HIS   B CA   1 
ATOM   4694 C  C    . HIS   B 1 45  ? 53.634 -21.801 5.808   1.00 13.72 ?  45  HIS   B C    1 
ATOM   4695 O  O    . HIS   B 1 45  ? 54.696 -21.820 5.194   1.00 16.07 ?  45  HIS   B O    1 
ATOM   4696 C  CB   . HIS   B 1 45  ? 52.941 -19.815 4.438   1.00 11.52 ?  45  HIS   B CB   1 
ATOM   4697 C  CG   . HIS   B 1 45  ? 52.066 -18.615 4.320   1.00 11.39 ?  45  HIS   B CG   1 
ATOM   4698 N  ND1  . HIS   B 1 45  ? 50.688 -18.698 4.283   1.00 11.57 ?  45  HIS   B ND1  1 
ATOM   4699 C  CD2  . HIS   B 1 45  ? 52.379 -17.300 4.249   1.00 12.07 ?  45  HIS   B CD2  1 
ATOM   4700 C  CE1  . HIS   B 1 45  ? 50.200 -17.475 4.176   1.00 11.30 ?  45  HIS   B CE1  1 
ATOM   4701 N  NE2  . HIS   B 1 45  ? 51.200 -16.610 4.151   1.00 11.55 ?  45  HIS   B NE2  1 
ATOM   4702 H  H    . HIS   B 1 45  ? 53.174 -19.199 6.840   1.00 14.15 ?  45  HIS   B H    1 
ATOM   4703 H  HA   . HIS   B 1 45  ? 51.739 -21.063 5.518   1.00 13.96 ?  45  HIS   B HA   1 
ATOM   4704 H  HB2  . HIS   B 1 45  ? 53.858 -19.514 4.498   1.00 13.87 ?  45  HIS   B HB2  1 
ATOM   4705 H  HB3  . HIS   B 1 45  ? 52.823 -20.353 3.634   1.00 13.87 ?  45  HIS   B HB3  1 
ATOM   4706 H  HD2  . HIS   B 1 45  ? 53.235 -16.934 4.256   1.00 14.53 ?  45  HIS   B HD2  1 
ATOM   4707 H  HE1  . HIS   B 1 45  ? 49.296 -17.258 4.121   1.00 13.60 ?  45  HIS   B HE1  1 
ATOM   4708 H  HE2  . HIS   B 1 45  ? 51.121 -15.756 4.096   1.00 13.90 ?  45  HIS   B HE2  1 
ATOM   4709 N  N    A GLY   B 1 46  ? 53.260 -22.775 6.635   0.60 14.89 ?  46  GLY   B N    1 
ATOM   4710 N  N    B GLY   B 1 46  ? 53.275 -22.758 6.655   0.40 14.58 ?  46  GLY   B N    1 
ATOM   4711 C  CA   A GLY   B 1 46  ? 54.183 -23.824 7.031   0.60 16.88 ?  46  GLY   B CA   1 
ATOM   4712 C  CA   B GLY   B 1 46  ? 54.196 -23.823 6.993   0.40 16.00 ?  46  GLY   B CA   1 
ATOM   4713 C  C    A GLY   B 1 46  ? 54.243 -25.063 6.159   0.60 18.36 ?  46  GLY   B C    1 
ATOM   4714 C  C    B GLY   B 1 46  ? 54.229 -24.967 5.999   0.40 17.31 ?  46  GLY   B C    1 
ATOM   4715 O  O    A GLY   B 1 46  ? 55.334 -25.534 5.821   0.60 20.85 ?  46  GLY   B O    1 
ATOM   4716 O  O    B GLY   B 1 46  ? 55.265 -25.244 5.385   0.40 18.35 ?  46  GLY   B O    1 
ATOM   4717 H  H    A GLY   B 1 46  ? 52.478 -22.831 6.998   0.60 17.91 ?  46  GLY   B H    1 
ATOM   4718 H  H    B GLY   B 1 46  ? 52.508 -22.801 7.052   0.40 17.54 ?  46  GLY   B H    1 
ATOM   4719 H  HA2  A GLY   B 1 46  ? 55.074 -23.446 7.072   0.60 20.30 ?  46  GLY   B HA2  1 
ATOM   4720 H  HA2  B GLY   B 1 46  ? 55.089 -23.453 7.058   0.40 19.24 ?  46  GLY   B HA2  1 
ATOM   4721 H  HA3  A GLY   B 1 46  ? 53.945 -24.120 7.922   0.60 20.30 ?  46  GLY   B HA3  1 
ATOM   4722 H  HA3  B GLY   B 1 46  ? 53.954 -24.177 7.864   0.40 19.24 ?  46  GLY   B HA3  1 
ATOM   4723 N  N    . GLY   B 1 47  ? 53.089 -25.627 5.810   1.00 17.59 ?  47  GLY   B N    1 
ATOM   4724 C  CA   . GLY   B 1 47  ? 53.036 -26.900 5.122   1.00 15.34 ?  47  GLY   B CA   1 
ATOM   4725 C  C    . GLY   B 1 47  ? 52.120 -26.889 3.914   1.00 13.24 ?  47  GLY   B C    1 
ATOM   4726 O  O    . GLY   B 1 47  ? 51.463 -25.892 3.619   1.00 13.32 ?  47  GLY   B O    1 
ATOM   4727 H  H    A GLY   B 1 47  ? 52.313 -25.297 5.987   0.60 21.15 ?  47  GLY   B H    1 
ATOM   4728 H  H    B GLY   B 1 47  ? 52.318 -25.346 6.076   0.40 21.15 ?  47  GLY   B H    1 
ATOM   4729 H  HA2  . GLY   B 1 47  ? 53.924 -27.148 4.822   1.00 18.45 ?  47  GLY   B HA2  1 
ATOM   4730 H  HA3  . GLY   B 1 47  ? 52.723 -27.583 5.738   1.00 18.45 ?  47  GLY   B HA3  1 
ATOM   4731 N  N    . GLY   B 1 48  ? 52.084 -28.027 3.223   1.00 12.55 ?  48  GLY   B N    1 
ATOM   4732 C  CA   . GLY   B 1 48  ? 51.149 -28.171 2.123   1.00 12.48 ?  48  GLY   B CA   1 
ATOM   4733 C  C    . GLY   B 1 48  ? 51.284 -27.062 1.103   1.00 11.96 ?  48  GLY   B C    1 
ATOM   4734 O  O    . GLY   B 1 48  ? 52.385 -26.599 0.784   1.00 12.42 ?  48  GLY   B O    1 
ATOM   4735 H  H    . GLY   B 1 48  ? 52.588 -28.705 3.363   1.00 15.10 ?  48  GLY   B H    1 
ATOM   4736 H  HA2  . GLY   B 1 48  ? 51.301 -29.022 1.677   1.00 15.02 ?  48  GLY   B HA2  1 
ATOM   4737 H  HA3  . GLY   B 1 48  ? 50.240 -28.164 2.463   1.00 15.02 ?  48  GLY   B HA3  1 
ATOM   4738 N  N    . VAL   B 1 49  ? 50.137 -26.633 0.574   1.00 11.75 ?  49  VAL   B N    1 
ATOM   4739 C  CA   . VAL   B 1 49  ? 50.112 -25.608 -0.466  1.00 11.62 ?  49  VAL   B CA   1 
ATOM   4740 C  C    . VAL   B 1 49  ? 50.772 -24.320 0.019   1.00 10.90 ?  49  VAL   B C    1 
ATOM   4741 O  O    . VAL   B 1 49  ? 51.558 -23.701 -0.705  1.00 11.58 ?  49  VAL   B O    1 
ATOM   4742 C  CB   . VAL   B 1 49  ? 48.666 -25.359 -0.937  1.00 12.85 ?  49  VAL   B CB   1 
ATOM   4743 C  CG1  . VAL   B 1 49  ? 48.587 -24.112 -1.810  1.00 13.16 ?  49  VAL   B CG1  1 
ATOM   4744 C  CG2  . VAL   B 1 49  ? 48.122 -26.572 -1.687  1.00 14.30 ?  49  VAL   B CG2  1 
ATOM   4745 H  H    . VAL   B 1 49  ? 49.354 -26.919 0.799   1.00 14.14 ?  49  VAL   B H    1 
ATOM   4746 H  HA   . VAL   B 1 49  ? 50.614 -25.924 -1.231  1.00 13.99 ?  49  VAL   B HA   1 
ATOM   4747 H  HB   . VAL   B 1 49  ? 48.101 -25.213 -0.163  1.00 15.46 ?  49  VAL   B HB   1 
ATOM   4748 H  HG11 . VAL   B 1 49  ? 47.755 -24.128 -2.310  1.00 15.83 ?  49  VAL   B HG11 1 
ATOM   4749 H  HG12 . VAL   B 1 49  ? 48.613 -23.324 -1.243  1.00 15.83 ?  49  VAL   B HG12 1 
ATOM   4750 H  HG13 . VAL   B 1 49  ? 49.338 -24.107 -2.423  1.00 15.83 ?  49  VAL   B HG13 1 
ATOM   4751 H  HG21 . VAL   B 1 49  ? 47.209 -26.389 -1.967  1.00 17.20 ?  49  VAL   B HG21 1 
ATOM   4752 H  HG22 . VAL   B 1 49  ? 48.677 -26.738 -2.466  1.00 17.20 ?  49  VAL   B HG22 1 
ATOM   4753 H  HG23 . VAL   B 1 49  ? 48.138 -27.341 -1.098  1.00 17.20 ?  49  VAL   B HG23 1 
ATOM   4754 N  N    . ALA   B 1 50  ? 50.427 -23.868 1.231   1.00 10.65 ?  50  ALA   B N    1 
ATOM   4755 C  CA   . ALA   B 1 50  ? 50.948 -22.591 1.707   1.00 10.48 ?  50  ALA   B CA   1 
ATOM   4756 C  C    . ALA   B 1 50  ? 52.468 -22.624 1.811   1.00 10.74 ?  50  ALA   B C    1 
ATOM   4757 O  O    . ALA   B 1 50  ? 53.152 -21.657 1.447   1.00 10.97 ?  50  ALA   B O    1 
ATOM   4758 C  CB   . ALA   B 1 50  ? 50.320 -22.233 3.053   1.00 10.82 ?  50  ALA   B CB   1 
ATOM   4759 H  H    . ALA   B 1 50  ? 49.907 -24.274 1.784   1.00 12.82 ?  50  ALA   B H    1 
ATOM   4760 H  HA   . ALA   B 1 50  ? 50.717 -21.898 1.077   1.00 12.62 ?  50  ALA   B HA   1 
ATOM   4761 H  HB1  . ALA   B 1 50  ? 50.678 -21.382 3.355   1.00 13.02 ?  50  ALA   B HB1  1 
ATOM   4762 H  HB2  . ALA   B 1 50  ? 49.358 -22.165 2.943   1.00 13.02 ?  50  ALA   B HB2  1 
ATOM   4763 H  HB3  . ALA   B 1 50  ? 50.530 -22.926 3.699   1.00 13.02 ?  50  ALA   B HB3  1 
ATOM   4764 N  N    . GLY   B 1 51  ? 53.018 -23.716 2.331   1.00 11.36 ?  51  GLY   B N    1 
ATOM   4765 C  CA   . GLY   B 1 51  ? 54.462 -23.820 2.400   1.00 11.93 ?  51  GLY   B CA   1 
ATOM   4766 C  C    . GLY   B 1 51  ? 55.108 -23.770 1.032   1.00 11.77 ?  51  GLY   B C    1 
ATOM   4767 O  O    . GLY   B 1 51  ? 56.152 -23.138 0.851   1.00 12.73 ?  51  GLY   B O    1 
ATOM   4768 H  H    . GLY   B 1 51  ? 52.593 -24.392 2.647   1.00 13.67 ?  51  GLY   B H    1 
ATOM   4769 H  HA2  . GLY   B 1 51  ? 54.822 -23.090 2.932   1.00 14.36 ?  51  GLY   B HA2  1 
ATOM   4770 H  HA3  . GLY   B 1 51  ? 54.713 -24.657 2.826   1.00 14.36 ?  51  GLY   B HA3  1 
ATOM   4771 N  N    . ALA   B 1 52  ? 54.501 -24.433 0.049   1.00 11.36 ?  52  ALA   B N    1 
ATOM   4772 C  CA   . ALA   B 1 52  ? 55.066 -24.445 -1.293  1.00 12.03 ?  52  ALA   B CA   1 
ATOM   4773 C  C    . ALA   B 1 52  ? 54.983 -23.069 -1.947  1.00 11.55 ?  52  ALA   B C    1 
ATOM   4774 O  O    . ALA   B 1 52  ? 55.952 -22.623 -2.584  1.00 12.18 ?  52  ALA   B O    1 
ATOM   4775 C  CB   . ALA   B 1 52  ? 54.368 -25.496 -2.150  1.00 12.83 ?  52  ALA   B CB   1 
ATOM   4776 H  H    . ALA   B 1 52  ? 53.764 -24.875 0.134   1.00 13.68 ?  52  ALA   B H    1 
ATOM   4777 H  HA   . ALA   B 1 52  ? 56.002 -24.685 -1.231  1.00 14.47 ?  52  ALA   B HA   1 
ATOM   4778 H  HB1  . ALA   B 1 52  ? 54.764 -25.487 -3.039  1.00 15.44 ?  52  ALA   B HB1  1 
ATOM   4779 H  HB2  . ALA   B 1 52  ? 54.497 -26.368 -1.744  1.00 15.44 ?  52  ALA   B HB2  1 
ATOM   4780 H  HB3  . ALA   B 1 52  ? 53.426 -25.289 -2.205  1.00 15.44 ?  52  ALA   B HB3  1 
ATOM   4781 N  N    . LEU   B 1 53  ? 53.839 -22.387 -1.821  1.00 11.02 ?  53  LEU   B N    1 
ATOM   4782 C  CA   . LEU   B 1 53  ? 53.733 -21.049 -2.396  1.00 11.13 ?  53  LEU   B CA   1 
ATOM   4783 C  C    . LEU   B 1 53  ? 54.741 -20.110 -1.748  1.00 11.14 ?  53  LEU   B C    1 
ATOM   4784 O  O    . LEU   B 1 53  ? 55.443 -19.356 -2.435  1.00 11.81 ?  53  LEU   B O    1 
ATOM   4785 C  CB   . LEU   B 1 53  ? 52.312 -20.505 -2.231  1.00 11.50 ?  53  LEU   B CB   1 
ATOM   4786 C  CG   . LEU   B 1 53  ? 51.175 -21.227 -2.961  1.00 11.85 ?  53  LEU   B CG   1 
ATOM   4787 C  CD1  . LEU   B 1 53  ? 49.834 -20.621 -2.594  1.00 13.27 ?  53  LEU   B CD1  1 
ATOM   4788 C  CD2  . LEU   B 1 53  ? 51.373 -21.216 -4.472  1.00 13.58 ?  53  LEU   B CD2  1 
ATOM   4789 H  H    . LEU   B 1 53  ? 53.135 -22.667 -1.417  1.00 13.27 ?  53  LEU   B H    1 
ATOM   4790 H  HA   . LEU   B 1 53  ? 53.937 -21.098 -3.347  1.00 13.40 ?  53  LEU   B HA   1 
ATOM   4791 H  HB2  . LEU   B 1 53  ? 52.099 -20.525 -1.291  1.00 13.84 ?  53  LEU   B HB2  1 
ATOM   4792 H  HB3  . LEU   B 1 53  ? 52.310 -19.592 -2.547  1.00 13.84 ?  53  LEU   B HB3  1 
ATOM   4793 H  HG   . LEU   B 1 53  ? 51.160 -22.154 -2.678  1.00 14.27 ?  53  LEU   B HG   1 
ATOM   4794 H  HD11 . LEU   B 1 53  ? 49.130 -21.101 -3.064  1.00 15.97 ?  53  LEU   B HD11 1 
ATOM   4795 H  HD12 . LEU   B 1 53  ? 49.702 -20.711 -1.634  1.00 15.97 ?  53  LEU   B HD12 1 
ATOM   4796 H  HD13 . LEU   B 1 53  ? 49.825 -19.690 -2.844  1.00 15.97 ?  53  LEU   B HD13 1 
ATOM   4797 H  HD21 . LEU   B 1 53  ? 50.674 -21.749 -4.887  1.00 16.34 ?  53  LEU   B HD21 1 
ATOM   4798 H  HD22 . LEU   B 1 53  ? 51.317 -20.302 -4.791  1.00 16.34 ?  53  LEU   B HD22 1 
ATOM   4799 H  HD23 . LEU   B 1 53  ? 52.239 -21.592 -4.684  1.00 16.34 ?  53  LEU   B HD23 1 
ATOM   4800 N  N    . ASN   B 1 54  ? 54.832 -20.143 -0.420  1.00 10.79 ?  54  ASN   B N    1 
ATOM   4801 C  CA   . ASN   B 1 54  ? 55.743 -19.229 0.251   1.00 11.62 ?  54  ASN   B CA   1 
ATOM   4802 C  C    . ASN   B 1 54  ? 57.186 -19.507 -0.146  1.00 12.05 ?  54  ASN   B C    1 
ATOM   4803 O  O    . ASN   B 1 54  ? 57.962 -18.572 -0.383  1.00 12.28 ?  54  ASN   B O    1 
ATOM   4804 C  CB   . ASN   B 1 54  ? 55.583 -19.302 1.762   1.00 12.31 ?  54  ASN   B CB   1 
ATOM   4805 C  CG   . ASN   B 1 54  ? 56.561 -18.386 2.468   1.00 12.39 ?  54  ASN   B CG   1 
ATOM   4806 O  OD1  . ASN   B 1 54  ? 56.573 -17.178 2.222   1.00 12.38 ?  54  ASN   B OD1  1 
ATOM   4807 N  ND2  . ASN   B 1 54  ? 57.409 -18.954 3.318   1.00 14.06 ?  54  ASN   B ND2  1 
ATOM   4808 H  H    . ASN   B 1 54  ? 54.389 -20.669 0.098   1.00 12.99 ?  54  ASN   B H    1 
ATOM   4809 H  HA   . ASN   B 1 54  ? 55.531 -18.325 -0.025  1.00 13.98 ?  54  ASN   B HA   1 
ATOM   4810 H  HB2  . ASN   B 1 54  ? 54.683 -19.025 2.001   1.00 14.81 ?  54  ASN   B HB2  1 
ATOM   4811 H  HB3  . ASN   B 1 54  ? 55.747 -20.207 2.061   1.00 14.81 ?  54  ASN   B HB3  1 
ATOM   4812 H  HD21 . ASN   B 1 54  ? 57.988 -18.471 3.735   1.00 16.91 ?  54  ASN   B HD21 1 
ATOM   4813 H  HD22 . ASN   B 1 54  ? 57.380 -19.801 3.455   1.00 16.91 ?  54  ASN   B HD22 1 
ATOM   4814 N  N    . LYS   B 1 55  ? 57.569 -20.785 -0.215  1.00 12.46 ?  55  LYS   B N    1 
ATOM   4815 C  CA   . LYS   B 1 55  ? 58.924 -21.125 -0.636  1.00 13.38 ?  55  LYS   B CA   1 
ATOM   4816 C  C    . LYS   B 1 55  ? 59.222 -20.584 -2.028  1.00 12.98 ?  55  LYS   B C    1 
ATOM   4817 O  O    . LYS   B 1 55  ? 60.326 -20.090 -2.284  1.00 13.76 ?  55  LYS   B O    1 
ATOM   4818 C  CB   . LYS   B 1 55  ? 59.120 -22.641 -0.587  1.00 15.22 ?  55  LYS   B CB   1 
ATOM   4819 C  CG   . LYS   B 1 55  ? 60.501 -23.106 -1.009  1.00 19.28 ?  55  LYS   B CG   1 
ATOM   4820 C  CD   . LYS   B 1 55  ? 60.670 -24.604 -0.804  1.00 22.76 ?  55  LYS   B CD   1 
ATOM   4821 C  CE   . LYS   B 1 55  ? 60.783 -24.963 0.678   1.00 25.73 ?  55  LYS   B CE   1 
ATOM   4822 N  NZ   . LYS   B 1 55  ? 61.148 -26.385 0.886   1.00 27.07 ?  55  LYS   B NZ   1 
ATOM   4823 H  H    . LYS   B 1 55  ? 57.068 -21.459 -0.033  1.00 14.99 ?  55  LYS   B H    1 
ATOM   4824 H  HA   . LYS   B 1 55  ? 59.553 -20.720 -0.023  1.00 16.10 ?  55  LYS   B HA   1 
ATOM   4825 H  HB2  . LYS   B 1 55  ? 58.972 -22.938 0.322   1.00 18.31 ?  55  LYS   B HB2  1 
ATOM   4826 H  HB3  . LYS   B 1 55  ? 58.478 -23.057 -1.180  1.00 18.31 ?  55  LYS   B HB3  1 
ATOM   4827 H  HG2  . LYS   B 1 55  ? 60.635 -22.913 -1.951  1.00 23.18 ?  55  LYS   B HG2  1 
ATOM   4828 H  HG3  . LYS   B 1 55  ? 61.172 -22.648 -0.476  1.00 23.18 ?  55  LYS   B HG3  1 
ATOM   4829 H  HD2  . LYS   B 1 55  ? 59.899 -25.068 -1.168  1.00 27.35 ?  55  LYS   B HD2  1 
ATOM   4830 H  HD3  . LYS   B 1 55  ? 61.480 -24.903 -1.247  1.00 27.35 ?  55  LYS   B HD3  1 
ATOM   4831 H  HE2  . LYS   B 1 55  ? 61.466 -24.404 1.084   1.00 30.92 ?  55  LYS   B HE2  1 
ATOM   4832 H  HE3  . LYS   B 1 55  ? 59.925 -24.799 1.107   1.00 30.92 ?  55  LYS   B HE3  1 
ATOM   4833 H  HZ1  . LYS   B 1 55  ? 61.170 -26.566 1.757   1.00 32.53 ?  55  LYS   B HZ1  1 
ATOM   4834 H  HZ2  . LYS   B 1 55  ? 60.545 -26.909 0.495   1.00 32.53 ?  55  LYS   B HZ2  1 
ATOM   4835 H  HZ3  . LYS   B 1 55  ? 61.947 -26.545 0.533   1.00 32.53 ?  55  LYS   B HZ3  1 
ATOM   4836 N  N    . ALA   B 1 56  ? 58.253 -20.667 -2.944  1.00 12.67 ?  56  ALA   B N    1 
ATOM   4837 C  CA   . ALA   B 1 56  ? 58.476 -20.170 -4.295  1.00 13.25 ?  56  ALA   B CA   1 
ATOM   4838 C  C    . ALA   B 1 56  ? 58.749 -18.675 -4.296  1.00 13.24 ?  56  ALA   B C    1 
ATOM   4839 O  O    . ALA   B 1 56  ? 59.478 -18.179 -5.166  1.00 14.39 ?  56  ALA   B O    1 
ATOM   4840 C  CB   . ALA   B 1 56  ? 57.280 -20.501 -5.186  1.00 14.38 ?  56  ALA   B CB   1 
ATOM   4841 H  H    . ALA   B 1 56  ? 57.466 -20.989 -2.810  1.00 15.24 ?  56  ALA   B H    1 
ATOM   4842 H  HA   . ALA   B 1 56  ? 59.255 -20.609 -4.668  1.00 15.94 ?  56  ALA   B HA   1 
ATOM   4843 H  HB1  . ALA   B 1 56  ? 57.453 -20.168 -6.085  1.00 17.30 ?  56  ALA   B HB1  1 
ATOM   4844 H  HB2  . ALA   B 1 56  ? 57.163 -21.462 -5.210  1.00 17.30 ?  56  ALA   B HB2  1 
ATOM   4845 H  HB3  . ALA   B 1 56  ? 56.488 -20.077 -4.826  1.00 17.30 ?  56  ALA   B HB3  1 
ATOM   4846 N  N    . THR   B 1 57  ? 58.189 -17.943 -3.330  1.00 12.97 ?  57  THR   B N    1 
ATOM   4847 C  CA   . THR   B 1 57  ? 58.427 -16.508 -3.207  1.00 13.05 ?  57  THR   B CA   1 
ATOM   4848 C  C    . THR   B 1 57  ? 59.679 -16.180 -2.399  1.00 13.76 ?  57  THR   B C    1 
ATOM   4849 O  O    . THR   B 1 57  ? 59.917 -15.004 -2.095  1.00 14.16 ?  57  THR   B O    1 
ATOM   4850 C  CB   . THR   B 1 57  ? 57.224 -15.778 -2.573  1.00 12.34 ?  57  THR   B CB   1 
ATOM   4851 O  OG1  . THR   B 1 57  ? 57.206 -15.981 -1.152  1.00 12.66 ?  57  THR   B OG1  1 
ATOM   4852 C  CG2  . THR   B 1 57  ? 55.902 -16.187 -3.211  1.00 12.46 ?  57  THR   B CG2  1 
ATOM   4853 H  H    . THR   B 1 57  ? 57.650 -18.260 -2.739  1.00 15.61 ?  57  THR   B H    1 
ATOM   4854 H  HA   . THR   B 1 57  ? 58.546 -16.142 -4.097  1.00 15.70 ?  57  THR   B HA   1 
ATOM   4855 H  HB   . THR   B 1 57  ? 57.330 -14.829 -2.743  1.00 14.85 ?  57  THR   B HB   1 
ATOM   4856 H  HG1  . THR   B 1 57  ? 57.136 -16.801 -0.984  1.00 15.24 ?  57  THR   B HG1  1 
ATOM   4857 H  HG21 . THR   B 1 57  ? 55.173 -15.676 -2.827  1.00 14.99 ?  57  THR   B HG21 1 
ATOM   4858 H  HG22 . THR   B 1 57  ? 55.926 -16.027 -4.169  1.00 14.99 ?  57  THR   B HG22 1 
ATOM   4859 H  HG23 . THR   B 1 57  ? 55.734 -17.131 -3.060  1.00 14.99 ?  57  THR   B HG23 1 
ATOM   4860 N  N    . ASN   B 1 58  ? 60.473 -17.184 -2.036  1.00 14.48 ?  58  ASN   B N    1 
ATOM   4861 C  CA   . ASN   B 1 58  ? 61.670 -16.969 -1.227  1.00 17.41 ?  58  ASN   B CA   1 
ATOM   4862 C  C    . ASN   B 1 58  ? 61.329 -16.252 0.081   1.00 15.14 ?  58  ASN   B C    1 
ATOM   4863 O  O    . ASN   B 1 58  ? 62.063 -15.373 0.541   1.00 15.66 ?  58  ASN   B O    1 
ATOM   4864 C  CB   . ASN   B 1 58  ? 62.758 -16.224 -2.008  1.00 25.32 ?  58  ASN   B CB   1 
ATOM   4865 C  CG   . ASN   B 1 58  ? 64.129 -16.374 -1.380  1.00 34.71 ?  58  ASN   B CG   1 
ATOM   4866 O  OD1  . ASN   B 1 58  ? 64.432 -17.393 -0.758  1.00 37.22 ?  58  ASN   B OD1  1 
ATOM   4867 N  ND2  . ASN   B 1 58  ? 64.967 -15.356 -1.537  1.00 38.66 ?  58  ASN   B ND2  1 
ATOM   4868 H  H    . ASN   B 1 58  ? 60.334 -18.012 -2.244  1.00 17.42 ?  58  ASN   B H    1 
ATOM   4869 H  HA   . ASN   B 1 58  ? 62.030 -17.840 -0.997  1.00 20.94 ?  58  ASN   B HA   1 
ATOM   4870 H  HB2  . ASN   B 1 58  ? 62.798 -16.578 -2.914  1.00 30.42 ?  58  ASN   B HB2  1 
ATOM   4871 H  HB3  . ASN   B 1 58  ? 62.542 -15.281 -2.033  1.00 30.42 ?  58  ASN   B HB3  1 
ATOM   4872 H  HD21 . ASN   B 1 58  ? 65.758 -15.394 -1.202  1.00 46.44 ?  58  ASN   B HD21 1 
ATOM   4873 H  HD22 . ASN   B 1 58  ? 64.718 -14.660 -1.975  1.00 46.44 ?  58  ASN   B HD22 1 
ATOM   4874 N  N    . ASN   B 1 59  ? 60.202 -16.633 0.686   1.00 14.11 ?  59  ASN   B N    1 
ATOM   4875 C  CA   . ASN   B 1 59  ? 59.730 -16.160 1.988   1.00 13.82 ?  59  ASN   B CA   1 
ATOM   4876 C  C    . ASN   B 1 59  ? 59.137 -14.754 1.931   1.00 13.03 ?  59  ASN   B C    1 
ATOM   4877 O  O    . ASN   B 1 59  ? 58.706 -14.247 2.976   1.00 13.47 ?  59  ASN   B O    1 
ATOM   4878 C  CB   . ASN   B 1 59  ? 60.805 -16.218 3.090   1.00 15.01 ?  59  ASN   B CB   1 
ATOM   4879 C  CG   . ASN   B 1 59  ? 60.219 -16.390 4.474   1.00 16.13 ?  59  ASN   B CG   1 
ATOM   4880 O  OD1  . ASN   B 1 59  ? 59.383 -17.272 4.704   1.00 16.15 ?  59  ASN   B OD1  1 
ATOM   4881 N  ND2  . ASN   B 1 59  ? 60.646 -15.548 5.406   1.00 16.78 ?  59  ASN   B ND2  1 
ATOM   4882 H  H    . ASN   B 1 59  ? 59.662 -17.212 0.341   1.00 16.97 ?  59  ASN   B H    1 
ATOM   4883 H  HA   . ASN   B 1 59  ? 59.020 -16.753 2.272   1.00 16.63 ?  59  ASN   B HA   1 
ATOM   4884 H  HB2  . ASN   B 1 59  ? 61.393 -16.972 2.926   1.00 18.06 ?  59  ASN   B HB2  1 
ATOM   4885 H  HB3  . ASN   B 1 59  ? 61.311 -15.393 3.088   1.00 18.06 ?  59  ASN   B HB3  1 
ATOM   4886 H  HD21 . ASN   B 1 59  ? 60.345 -15.606 6.212   1.00 20.18 ?  59  ASN   B HD21 1 
ATOM   4887 H  HD22 . ASN   B 1 59  ? 61.228 -14.947 5.209   1.00 20.18 ?  59  ASN   B HD22 1 
ATOM   4888 N  N    . ALA   B 1 60  ? 59.077 -14.112 0.759   1.00 13.01 ?  60  ALA   B N    1 
ATOM   4889 C  CA   . ALA   B 1 60  ? 58.483 -12.780 0.688   1.00 13.10 ?  60  ALA   B CA   1 
ATOM   4890 C  C    . ALA   B 1 60  ? 57.014 -12.803 1.081   1.00 12.20 ?  60  ALA   B C    1 
ATOM   4891 O  O    . ALA   B 1 60  ? 56.515 -11.848 1.694   1.00 12.87 ?  60  ALA   B O    1 
ATOM   4892 C  CB   . ALA   B 1 60  ? 58.648 -12.192 -0.714  1.00 14.22 ?  60  ALA   B CB   1 
ATOM   4893 H  H    . ALA   B 1 60  ? 59.371 -14.423 0.012   1.00 15.65 ?  60  ALA   B H    1 
ATOM   4894 H  HA   . ALA   B 1 60  ? 58.947 -12.201 1.310   1.00 15.76 ?  60  ALA   B HA   1 
ATOM   4895 H  HB1  . ALA   B 1 60  ? 58.250 -11.309 -0.733  1.00 17.10 ?  60  ALA   B HB1  1 
ATOM   4896 H  HB2  . ALA   B 1 60  ? 59.598 -12.130 -0.920  1.00 17.10 ?  60  ALA   B HB2  1 
ATOM   4897 H  HB3  . ALA   B 1 60  ? 58.211 -12.771 -1.355  1.00 17.10 ?  60  ALA   B HB3  1 
ATOM   4898 N  N    . MET   B 1 61  ? 56.308 -13.881 0.741   1.00 11.65 ?  61  MET   B N    1 
ATOM   4899 C  CA   . MET   B 1 61  ? 54.913 -14.003 1.135   1.00 11.31 ?  61  MET   B CA   1 
ATOM   4900 C  C    . MET   B 1 61  ? 54.771 -14.007 2.659   1.00 11.61 ?  61  MET   B C    1 
ATOM   4901 O  O    . MET   B 1 61  ? 53.864 -13.362 3.207   1.00 11.35 ?  61  MET   B O    1 
ATOM   4902 C  CB   . MET   B 1 61  ? 54.325 -15.268 0.499   1.00 11.19 ?  61  MET   B CB   1 
ATOM   4903 C  CG   . MET   B 1 61  ? 52.883 -15.557 0.916   1.00 10.97 ?  61  MET   B CG   1 
ATOM   4904 S  SD   . MET   B 1 61  ? 52.237 -17.064 0.160   1.00 11.80 ?  61  MET   B SD   1 
ATOM   4905 C  CE   . MET   B 1 61  ? 51.965 -16.475 -1.509  1.00 13.12 ?  61  MET   B CE   1 
ATOM   4906 H  H    . MET   B 1 61  ? 56.612 -14.554 0.290   1.00 14.02 ?  61  MET   B H    1 
ATOM   4907 H  HA   . MET   B 1 61  ? 54.422 -13.248 0.772   1.00 13.61 ?  61  MET   B HA   1 
ATOM   4908 H  HB2  . MET   B 1 61  ? 54.336 -15.171 -0.470  1.00 13.47 ?  61  MET   B HB2  1 
ATOM   4909 H  HB3  . MET   B 1 61  ? 54.867 -16.031 0.754   1.00 13.47 ?  61  MET   B HB3  1 
ATOM   4910 H  HG2  . MET   B 1 61  ? 52.851 -15.671 1.880   1.00 13.21 ?  61  MET   B HG2  1 
ATOM   4911 H  HG3  . MET   B 1 61  ? 52.323 -14.816 0.648   1.00 13.21 ?  61  MET   B HG3  1 
ATOM   4912 H  HE1  . MET   B 1 61  ? 51.577 -17.190 -2.034  1.00 15.79 ?  61  MET   B HE1  1 
ATOM   4913 H  HE2  . MET   B 1 61  ? 51.353 -15.717 -1.482  1.00 15.79 ?  61  MET   B HE2  1 
ATOM   4914 H  HE3  . MET   B 1 61  ? 52.811 -16.200 -1.890  1.00 15.79 ?  61  MET   B HE3  1 
ATOM   4915 N  N    . GLN   B 1 62  ? 55.647 -14.730 3.363   1.00 11.65 ?  62  GLN   B N    1 
ATOM   4916 C  CA   . GLN   B 1 62  ? 55.542 -14.783 4.819   1.00 11.91 ?  62  GLN   B CA   1 
ATOM   4917 C  C    . GLN   B 1 62  ? 55.825 -13.426 5.451   1.00 12.06 ?  62  GLN   B C    1 
ATOM   4918 O  O    . GLN   B 1 62  ? 55.140 -13.025 6.399   1.00 12.41 ?  62  GLN   B O    1 
ATOM   4919 C  CB   . GLN   B 1 62  ? 56.491 -15.839 5.387   1.00 12.06 ?  62  GLN   B CB   1 
ATOM   4920 C  CG   . GLN   B 1 62  ? 56.267 -16.108 6.867   1.00 12.22 ?  62  GLN   B CG   1 
ATOM   4921 C  CD   . GLN   B 1 62  ? 54.893 -16.699 7.112   1.00 12.05 ?  62  GLN   B CD   1 
ATOM   4922 O  OE1  . GLN   B 1 62  ? 54.636 -17.851 6.756   1.00 12.41 ?  62  GLN   B OE1  1 
ATOM   4923 N  NE2  . GLN   B 1 62  ? 53.983 -15.902 7.662   1.00 12.66 ?  62  GLN   B NE2  1 
ATOM   4924 H  H    . GLN   B 1 62  ? 56.293 -15.185 3.020   1.00 14.02 ?  62  GLN   B H    1 
ATOM   4925 H  HA   . GLN   B 1 62  ? 54.636 -15.038 5.048   1.00 14.34 ?  62  GLN   B HA   1 
ATOM   4926 H  HB2  . GLN   B 1 62  ? 56.362 -16.672 4.906   1.00 14.52 ?  62  GLN   B HB2  1 
ATOM   4927 H  HB3  . GLN   B 1 62  ? 57.406 -15.532 5.268   1.00 14.52 ?  62  GLN   B HB3  1 
ATOM   4928 H  HG2  . GLN   B 1 62  ? 56.938 -16.741 7.175   1.00 14.70 ?  62  GLN   B HG2  1 
ATOM   4929 H  HG3  . GLN   B 1 62  ? 56.341 -15.276 7.358   1.00 14.70 ?  62  GLN   B HG3  1 
ATOM   4930 H  HE21 . GLN   B 1 62  ? 54.197 -15.101 7.884   1.00 15.23 ?  62  GLN   B HE21 1 
ATOM   4931 H  HE22 . GLN   B 1 62  ? 53.194 -16.199 7.812   1.00 15.23 ?  62  GLN   B HE22 1 
ATOM   4932 N  N    . VAL   B 1 63  ? 56.839 -12.709 4.957   1.00 12.44 ?  63  VAL   B N    1 
ATOM   4933 C  CA   . VAL   B 1 63  ? 57.147 -11.393 5.513   1.00 13.50 ?  63  VAL   B CA   1 
ATOM   4934 C  C    . VAL   B 1 63  ? 55.957 -10.459 5.335   1.00 12.94 ?  63  VAL   B C    1 
ATOM   4935 O  O    . VAL   B 1 63  ? 55.547 -9.751  6.267   1.00 13.56 ?  63  VAL   B O    1 
ATOM   4936 C  CB   . VAL   B 1 63  ? 58.435 -10.833 4.883   1.00 14.81 ?  63  VAL   B CB   1 
ATOM   4937 C  CG1  . VAL   B 1 63  ? 58.669 -9.395  5.337   1.00 15.53 ?  63  VAL   B CG1  1 
ATOM   4938 C  CG2  . VAL   B 1 63  ? 59.620 -11.712 5.257   1.00 15.55 ?  63  VAL   B CG2  1 
ATOM   4939 H  H    . VAL   B 1 63  ? 57.347 -12.958 4.304   1.00 14.97 ?  63  VAL   B H    1 
ATOM   4940 H  HA   . VAL   B 1 63  ? 57.307 -11.493 6.460   1.00 16.24 ?  63  VAL   B HA   1 
ATOM   4941 H  HB   . VAL   B 1 63  ? 58.354 -10.838 3.917   1.00 17.81 ?  63  VAL   B HB   1 
ATOM   4942 H  HG11 . VAL   B 1 63  ? 59.584 -9.147  5.141   1.00 18.68 ?  63  VAL   B HG11 1 
ATOM   4943 H  HG12 . VAL   B 1 63  ? 58.058 -8.811  4.865   1.00 18.68 ?  63  VAL   B HG12 1 
ATOM   4944 H  HG13 . VAL   B 1 63  ? 58.510 -9.340  6.294   1.00 18.68 ?  63  VAL   B HG13 1 
ATOM   4945 H  HG21 . VAL   B 1 63  ? 60.429 -11.334 4.878   1.00 18.70 ?  63  VAL   B HG21 1 
ATOM   4946 H  HG22 . VAL   B 1 63  ? 59.695 -11.743 6.227   1.00 18.70 ?  63  VAL   B HG22 1 
ATOM   4947 H  HG23 . VAL   B 1 63  ? 59.476 -12.605 4.910   1.00 18.70 ?  63  VAL   B HG23 1 
ATOM   4948 N  N    . GLU   B 1 64  ? 55.385 -10.446 4.130   1.00 12.60 ?  64  GLU   B N    1 
ATOM   4949 C  CA   . GLU   B 1 64  ? 54.218 -9.612  3.857   1.00 11.98 ?  64  GLU   B CA   1 
ATOM   4950 C  C    . GLU   B 1 64  ? 53.036 -10.013 4.734   1.00 11.66 ?  64  GLU   B C    1 
ATOM   4951 O  O    . GLU   B 1 64  ? 52.290 -9.154  5.233   1.00 12.14 ?  64  GLU   B O    1 
ATOM   4952 C  CB   . GLU   B 1 64  ? 53.861 -9.758  2.376   1.00 12.18 ?  64  GLU   B CB   1 
ATOM   4953 C  CG   . GLU   B 1 64  ? 52.603 -9.019  1.934   1.00 12.75 ?  64  GLU   B CG   1 
ATOM   4954 C  CD   . GLU   B 1 64  ? 52.059 -9.524  0.600   1.00 13.14 ?  64  GLU   B CD   1 
ATOM   4955 O  OE1  . GLU   B 1 64  ? 52.237 -10.732 0.280   1.00 13.94 ?  64  GLU   B OE1  1 
ATOM   4956 O  OE2  . GLU   B 1 64  ? 51.436 -8.708  -0.121  1.00 13.79 -1 64  GLU   B OE2  1 
ATOM   4957 H  H    . GLU   B 1 64  ? 55.656 -10.906 3.452   1.00 15.16 ?  64  GLU   B H    1 
ATOM   4958 H  HA   . GLU   B 1 64  ? 54.430 -8.683  4.031   1.00 14.42 ?  64  GLU   B HA   1 
ATOM   4959 H  HB2  . GLU   B 1 64  ? 54.596 -9.411  1.841   1.00 14.66 ?  64  GLU   B HB2  1 
ATOM   4960 H  HB3  . GLU   B 1 64  ? 53.730 -10.696 2.177   1.00 14.66 ?  64  GLU   B HB3  1 
ATOM   4961 H  HG2  . GLU   B 1 64  ? 51.903 -9.137  2.598   1.00 15.34 ?  64  GLU   B HG2  1 
ATOM   4962 H  HG3  . GLU   B 1 64  ? 52.806 -8.074  1.840   1.00 15.34 ?  64  GLU   B HG3  1 
ATOM   4963 N  N    . SER   B 1 65  ? 52.852 -11.322 4.921   1.00 11.61 ?  65  SER   B N    1 
ATOM   4964 C  CA   . SER   B 1 65  ? 51.743 -11.827 5.720   1.00 11.39 ?  65  SER   B CA   1 
ATOM   4965 C  C    . SER   B 1 65  ? 51.877 -11.431 7.184   1.00 11.61 ?  65  SER   B C    1 
ATOM   4966 O  O    . SER   B 1 65  ? 50.879 -11.063 7.819   1.00 11.86 ?  65  SER   B O    1 
ATOM   4967 C  CB   . SER   B 1 65  ? 51.664 -13.347 5.592   1.00 11.60 ?  65  SER   B CB   1 
ATOM   4968 O  OG   . SER   B 1 65  ? 51.312 -13.752 4.276   1.00 11.91 ?  65  SER   B OG   1 
ATOM   4969 H  H    . SER   B 1 65  ? 53.359 -11.944 4.598   1.00 13.98 ?  65  SER   B H    1 
ATOM   4970 H  HA   . SER   B 1 65  ? 50.911 -11.457 5.382   1.00 13.71 ?  65  SER   B HA   1 
ATOM   4971 H  HB2  . SER   B 1 65  ? 52.526 -13.728 5.811   1.00 13.96 ?  65  SER   B HB2  1 
ATOM   4972 H  HB3  . SER   B 1 65  ? 50.991 -13.680 6.211   1.00 13.96 ?  65  SER   B HB3  1 
ATOM   4973 H  HG   . SER   B 1 65  ? 51.878 -13.459 3.724   1.00 14.33 ?  65  SER   B HG   1 
ATOM   4974 N  N    . ASP   B 1 66  ? 53.086 -11.532 7.749   1.00 12.25 ?  66  ASP   B N    1 
ATOM   4975 C  CA   . ASP   B 1 66  ? 53.279 -11.135 9.142   1.00 12.42 ?  66  ASP   B CA   1 
ATOM   4976 C  C    . ASP   B 1 66  ? 52.964 -9.655  9.338   1.00 12.93 ?  66  ASP   B C    1 
ATOM   4977 O  O    . ASP   B 1 66  ? 52.384 -9.263  10.358  1.00 13.24 ?  66  ASP   B O    1 
ATOM   4978 C  CB   . ASP   B 1 66  ? 54.708 -11.447 9.595   1.00 13.55 ?  66  ASP   B CB   1 
ATOM   4979 C  CG   . ASP   B 1 66  ? 54.975 -12.940 9.751   1.00 15.51 ?  66  ASP   B CG   1 
ATOM   4980 O  OD1  . ASP   B 1 66  ? 54.019 -13.748 9.675   1.00 16.00 ?  66  ASP   B OD1  1 
ATOM   4981 O  OD2  . ASP   B 1 66  ? 56.157 -13.305 9.966   1.00 18.09 -1 66  ASP   B OD2  1 
ATOM   4982 H  H    . ASP   B 1 66  ? 53.786 -11.830 7.356   1.00 14.74 ?  66  ASP   B H    1 
ATOM   4983 H  HA   . ASP   B 1 66  ? 52.670 -11.636 9.703   1.00 14.94 ?  66  ASP   B HA   1 
ATOM   4984 H  HB2  . ASP   B 1 66  ? 55.328 -11.101 8.939   1.00 16.30 ?  66  ASP   B HB2  1 
ATOM   4985 H  HB3  . ASP   B 1 66  ? 54.862 -11.021 10.456  1.00 16.30 ?  66  ASP   B HB3  1 
ATOM   4986 N  N    . ASP   B 1 67  ? 53.336 -8.812  8.374   1.00 12.41 ?  67  ASP   B N    1 
ATOM   4987 C  CA   . ASP   B 1 67  ? 52.988 -7.401  8.462   1.00 12.88 ?  67  ASP   B CA   1 
ATOM   4988 C  C    . ASP   B 1 67  ? 51.476 -7.197  8.384   1.00 13.18 ?  67  ASP   B C    1 
ATOM   4989 O  O    . ASP   B 1 67  ? 50.916 -6.382  9.129   1.00 13.39 ?  67  ASP   B O    1 
ATOM   4990 C  CB   . ASP   B 1 67  ? 53.697 -6.630  7.354   1.00 14.14 ?  67  ASP   B CB   1 
ATOM   4991 C  CG   . ASP   B 1 67  ? 53.273 -5.187  7.314   1.00 15.55 ?  67  ASP   B CG   1 
ATOM   4992 O  OD1  . ASP   B 1 67  ? 53.771 -4.375  8.131   1.00 16.81 ?  67  ASP   B OD1  1 
ATOM   4993 O  OD2  . ASP   B 1 67  ? 52.404 -4.882  6.483   1.00 16.57 -1 67  ASP   B OD2  1 
ATOM   4994 H  H    . ASP   B 1 67  ? 53.792 -9.028  7.674   1.00 14.93 ?  67  ASP   B H    1 
ATOM   4995 H  HA   . ASP   B 1 67  ? 53.296 -7.048  9.309   1.00 15.50 ?  67  ASP   B HA   1 
ATOM   4996 H  HB2  . ASP   B 1 67  ? 54.657 -6.658  7.504   1.00 17.01 ?  67  ASP   B HB2  1 
ATOM   4997 H  HB3  . ASP   B 1 67  ? 53.491 -7.042  6.493   1.00 17.01 ?  67  ASP   B HB3  1 
ATOM   4998 N  N    . TYR   B 1 68  ? 50.799 -7.932  7.494   1.00 12.62 ?  68  TYR   B N    1 
ATOM   4999 C  CA   . TYR   B 1 68  ? 49.342 -7.858  7.419   1.00 13.35 ?  68  TYR   B CA   1 
ATOM   5000 C  C    . TYR   B 1 68  ? 48.708 -8.190  8.767   1.00 12.92 ?  68  TYR   B C    1 
ATOM   5001 O  O    . TYR   B 1 68  ? 47.778 -7.507  9.216   1.00 13.35 ?  68  TYR   B O    1 
ATOM   5002 C  CB   . TYR   B 1 68  ? 48.806 -8.788  6.318   1.00 14.04 ?  68  TYR   B CB   1 
ATOM   5003 C  CG   . TYR   B 1 68  ? 47.298 -8.936  6.375   1.00 14.96 ?  68  TYR   B CG   1 
ATOM   5004 C  CD1  . TYR   B 1 68  ? 46.711 -9.887  7.202   1.00 15.93 ?  68  TYR   B CD1  1 
ATOM   5005 C  CD2  . TYR   B 1 68  ? 46.467 -8.105  5.638   1.00 16.14 ?  68  TYR   B CD2  1 
ATOM   5006 C  CE1  . TYR   B 1 68  ? 45.347 -10.008 7.296   1.00 17.00 ?  68  TYR   B CE1  1 
ATOM   5007 C  CE2  . TYR   B 1 68  ? 45.081 -8.231  5.718   1.00 16.35 ?  68  TYR   B CE2  1 
ATOM   5008 C  CZ   . TYR   B 1 68  ? 44.543 -9.183  6.551   1.00 16.81 ?  68  TYR   B CZ   1 
ATOM   5009 O  OH   . TYR   B 1 68  ? 43.178 -9.304  6.652   1.00 17.67 ?  68  TYR   B OH   1 
ATOM   5010 H  H    . TYR   B 1 68  ? 51.160 -8.477  6.927   1.00 15.19 ?  68  TYR   B H    1 
ATOM   5011 H  HA   . TYR   B 1 68  ? 49.091 -6.953  7.190   1.00 16.06 ?  68  TYR   B HA   1 
ATOM   5012 H  HB2  . TYR   B 1 68  ? 49.035 -8.420  5.452   1.00 16.89 ?  68  TYR   B HB2  1 
ATOM   5013 H  HB3  . TYR   B 1 68  ? 49.196 -9.668  6.424   1.00 16.89 ?  68  TYR   B HB3  1 
ATOM   5014 H  HD1  . TYR   B 1 68  ? 47.253 -10.449 7.711   1.00 19.15 ?  68  TYR   B HD1  1 
ATOM   5015 H  HD2  . TYR   B 1 68  ? 46.839 -7.455  5.091   1.00 19.41 ?  68  TYR   B HD2  1 
ATOM   5016 H  HE1  . TYR   B 1 68  ? 44.968 -10.662 7.844   1.00 20.45 ?  68  TYR   B HE1  1 
ATOM   5017 H  HE2  . TYR   B 1 68  ? 44.526 -7.672  5.226   1.00 19.67 ?  68  TYR   B HE2  1 
ATOM   5018 H  HH   . TYR   B 1 68  ? 42.787 -8.758  6.137   1.00 21.25 ?  68  TYR   B HH   1 
ATOM   5019 N  N    . ILE   B 1 69  ? 49.185 -9.258  9.414   1.00 12.78 ?  69  ILE   B N    1 
ATOM   5020 C  CA   . ILE   B 1 69  ? 48.630 -9.679  10.697  1.00 13.25 ?  69  ILE   B CA   1 
ATOM   5021 C  C    . ILE   B 1 69  ? 48.886 -8.631  11.773  1.00 13.00 ?  69  ILE   B C    1 
ATOM   5022 O  O    . ILE   B 1 69  ? 48.020 -8.360  12.611  1.00 13.22 ?  69  ILE   B O    1 
ATOM   5023 C  CB   . ILE   B 1 69  ? 49.208 -11.053 11.089  1.00 13.98 ?  69  ILE   B CB   1 
ATOM   5024 C  CG1  . ILE   B 1 69  ? 48.674 -12.158 10.168  1.00 14.49 ?  69  ILE   B CG1  1 
ATOM   5025 C  CG2  . ILE   B 1 69  ? 48.933 -11.369 12.556  1.00 14.55 ?  69  ILE   B CG2  1 
ATOM   5026 C  CD1  . ILE   B 1 69  ? 47.196 -12.462 10.331  1.00 14.69 ?  69  ILE   B CD1  1 
ATOM   5027 H  H    . ILE   B 1 69  ? 49.829 -9.751  9.135   1.00 15.37 ?  69  ILE   B H    1 
ATOM   5028 H  HA   . ILE   B 1 69  ? 47.671 -9.777  10.608  1.00 15.95 ?  69  ILE   B HA   1 
ATOM   5029 H  HB   . ILE   B 1 69  ? 50.172 -11.013 10.977  1.00 16.82 ?  69  ILE   B HB   1 
ATOM   5030 H  HG12 . ILE   B 1 69  ? 48.822 -11.886 9.249   1.00 17.43 ?  69  ILE   B HG12 1 
ATOM   5031 H  HG13 . ILE   B 1 69  ? 49.166 -12.974 10.349  1.00 17.43 ?  69  ILE   B HG13 1 
ATOM   5032 H  HG21 . ILE   B 1 69  ? 49.072 -12.319 12.703  1.00 17.50 ?  69  ILE   B HG21 1 
ATOM   5033 H  HG22 . ILE   B 1 69  ? 49.542 -10.861 13.114  1.00 17.50 ?  69  ILE   B HG22 1 
ATOM   5034 H  HG23 . ILE   B 1 69  ? 48.016 -11.136 12.763  1.00 17.50 ?  69  ILE   B HG23 1 
ATOM   5035 H  HD11 . ILE   B 1 69  ? 46.961 -13.184 9.733   1.00 17.67 ?  69  ILE   B HD11 1 
ATOM   5036 H  HD12 . ILE   B 1 69  ? 47.026 -12.722 11.249  1.00 17.67 ?  69  ILE   B HD12 1 
ATOM   5037 H  HD13 . ILE   B 1 69  ? 46.684 -11.668 10.110  1.00 17.67 ?  69  ILE   B HD13 1 
ATOM   5038 N  N    . ALA   B 1 70  ? 50.081 -8.039  11.790  1.00 13.11 ?  70  ALA   B N    1 
ATOM   5039 C  CA   . ALA   B 1 70  ? 50.368 -7.006  12.777  1.00 12.89 ?  70  ALA   B CA   1 
ATOM   5040 C  C    . ALA   B 1 70  ? 49.374 -5.859  12.666  1.00 13.32 ?  70  ALA   B C    1 
ATOM   5041 O  O    . ALA   B 1 70  ? 48.935 -5.307  13.679  1.00 13.53 ?  70  ALA   B O    1 
ATOM   5042 C  CB   . ALA   B 1 70  ? 51.799 -6.501  12.602  1.00 13.53 ?  70  ALA   B CB   1 
ATOM   5043 H  H    . ALA   B 1 70  ? 50.721 -8.221  11.256  1.00 15.78 ?  70  ALA   B H    1 
ATOM   5044 H  HA   . ALA   B 1 70  ? 50.293 -7.384  13.669  1.00 15.51 ?  70  ALA   B HA   1 
ATOM   5045 H  HB1  . ALA   B 1 70  ? 51.989 -5.836  13.282  1.00 16.28 ?  70  ALA   B HB1  1 
ATOM   5046 H  HB2  . ALA   B 1 70  ? 52.414 -7.249  12.695  1.00 16.28 ?  70  ALA   B HB2  1 
ATOM   5047 H  HB3  . ALA   B 1 70  ? 51.893 -6.110  11.719  1.00 16.28 ?  70  ALA   B HB3  1 
ATOM   5048 N  N    . THR   B 1 71  ? 48.994 -5.499  11.442  1.00 13.74 ?  71  THR   B N    1 
ATOM   5049 C  CA   . THR   B 1 71  ? 48.100 -4.364  11.233  1.00 14.69 ?  71  THR   B CA   1 
ATOM   5050 C  C    . THR   B 1 71  ? 46.631 -4.730  11.436  1.00 15.23 ?  71  THR   B C    1 
ATOM   5051 O  O    . THR   B 1 71  ? 45.847 -3.913  11.941  1.00 16.77 ?  71  THR   B O    1 
ATOM   5052 C  CB   . THR   B 1 71  ? 48.326 -3.791  9.831   1.00 16.44 ?  71  THR   B CB   1 
ATOM   5053 O  OG1  . THR   B 1 71  ? 49.649 -3.252  9.744   1.00 18.57 ?  71  THR   B OG1  1 
ATOM   5054 C  CG2  . THR   B 1 71  ? 47.304 -2.708  9.503   1.00 17.65 ?  71  THR   B CG2  1 
ATOM   5055 H  H    . THR   B 1 71  ? 49.241 -5.896  10.721  1.00 16.53 ?  71  THR   B H    1 
ATOM   5056 H  HA   . THR   B 1 71  ? 48.323 -3.671  11.871  1.00 17.67 ?  71  THR   B HA   1 
ATOM   5057 H  HB   . THR   B 1 71  ? 48.241 -4.498  9.173   1.00 19.77 ?  71  THR   B HB   1 
ATOM   5058 H  HG1  . THR   B 1 71  ? 49.784 -2.917  8.981   1.00 22.33 ?  71  THR   B HG1  1 
ATOM   5059 H  HG21 . THR   B 1 71  ? 47.610 -2.180  8.747   1.00 21.22 ?  71  THR   B HG21 1 
ATOM   5060 H  HG22 . THR   B 1 71  ? 46.451 -3.109  9.280   1.00 21.22 ?  71  THR   B HG22 1 
ATOM   5061 H  HG23 . THR   B 1 71  ? 47.189 -2.119  10.267  1.00 21.22 ?  71  THR   B HG23 1 
ATOM   5062 N  N    . ASN   B 1 72  ? 46.239 -5.947  11.043  1.00 14.90 ?  72  ASN   B N    1 
ATOM   5063 C  CA   . ASN   B 1 72  ? 44.837 -6.309  10.913  1.00 15.31 ?  72  ASN   B CA   1 
ATOM   5064 C  C    . ASN   B 1 72  ? 44.364 -7.405  11.859  1.00 15.95 ?  72  ASN   B C    1 
ATOM   5065 O  O    . ASN   B 1 72  ? 43.148 -7.559  12.028  1.00 17.27 ?  72  ASN   B O    1 
ATOM   5066 C  CB   . ASN   B 1 72  ? 44.538 -6.739  9.468   1.00 16.03 ?  72  ASN   B CB   1 
ATOM   5067 C  CG   . ASN   B 1 72  ? 44.812 -5.636  8.472   1.00 17.03 ?  72  ASN   B CG   1 
ATOM   5068 O  OD1  . ASN   B 1 72  ? 45.829 -5.643  7.770   1.00 18.21 ?  72  ASN   B OD1  1 
ATOM   5069 N  ND2  . ASN   B 1 72  ? 43.930 -4.658  8.433   1.00 18.79 ?  72  ASN   B ND2  1 
ATOM   5070 H  H    . ASN   B 1 72  ? 46.783 -6.592  10.840  1.00 17.92 ?  72  ASN   B H    1 
ATOM   5071 H  HA   . ASN   B 1 72  ? 44.305 -5.523  11.094  1.00 18.42 ?  72  ASN   B HA   1 
ATOM   5072 H  HB2  . ASN   B 1 72  ? 45.102 -7.497  9.236   1.00 19.28 ?  72  ASN   B HB2  1 
ATOM   5073 H  HB3  . ASN   B 1 72  ? 43.605 -6.984  9.394   1.00 19.28 ?  72  ASN   B HB3  1 
ATOM   5074 H  HD21 . ASN   B 1 72  ? 44.033 -4.001  7.887   1.00 22.60 ?  72  ASN   B HD21 1 
ATOM   5075 H  HD22 . ASN   B 1 72  ? 43.233 -4.685  8.940   1.00 22.60 ?  72  ASN   B HD22 1 
ATOM   5076 N  N    . GLY   B 1 73  ? 45.268 -8.157  12.480  1.00 15.44 ?  73  GLY   B N    1 
ATOM   5077 C  CA   . GLY   B 1 73  ? 44.876 -9.302  13.268  1.00 14.96 ?  73  GLY   B CA   1 
ATOM   5078 C  C    . GLY   B 1 73  ? 44.506 -10.483 12.400  1.00 13.77 ?  73  GLY   B C    1 
ATOM   5079 O  O    . GLY   B 1 73  ? 44.495 -10.399 11.169  1.00 13.37 ?  73  GLY   B O    1 
ATOM   5080 H  H    . GLY   B 1 73  ? 46.120 -8.021  12.457  1.00 18.57 ?  73  GLY   B H    1 
ATOM   5081 H  HA2  . GLY   B 1 73  ? 45.609 -9.559  13.851  1.00 18.00 ?  73  GLY   B HA2  1 
ATOM   5082 H  HA3  . GLY   B 1 73  ? 44.112 -9.068  13.819  1.00 18.00 ?  73  GLY   B HA3  1 
ATOM   5083 N  N    . PRO   B 1 74  ? 44.199 -11.609 13.038  1.00 13.83 ?  74  PRO   B N    1 
ATOM   5084 C  CA   . PRO   B 1 74  ? 43.945 -12.841 12.291  1.00 13.18 ?  74  PRO   B CA   1 
ATOM   5085 C  C    . PRO   B 1 74  ? 42.644 -12.784 11.502  1.00 12.58 ?  74  PRO   B C    1 
ATOM   5086 O  O    . PRO   B 1 74  ? 41.698 -12.056 11.826  1.00 13.77 ?  74  PRO   B O    1 
ATOM   5087 C  CB   . PRO   B 1 74  ? 43.871 -13.903 13.392  1.00 14.46 ?  74  PRO   B CB   1 
ATOM   5088 C  CG   . PRO   B 1 74  ? 43.425 -13.154 14.603  1.00 15.77 ?  74  PRO   B CG   1 
ATOM   5089 C  CD   . PRO   B 1 74  ? 44.091 -11.812 14.493  1.00 15.41 ?  74  PRO   B CD   1 
ATOM   5090 H  HA   . PRO   B 1 74  ? 44.688 -13.032 11.692  1.00 15.86 ?  74  PRO   B HA   1 
ATOM   5091 H  HB2  . PRO   B 1 74  ? 43.226 -14.583 13.144  1.00 17.40 ?  74  PRO   B HB2  1 
ATOM   5092 H  HB3  . PRO   B 1 74  ? 44.750 -14.292 13.528  1.00 17.40 ?  74  PRO   B HB3  1 
ATOM   5093 H  HG2  . PRO   B 1 74  ? 42.459 -13.063 14.588  1.00 18.97 ?  74  PRO   B HG2  1 
ATOM   5094 H  HG3  . PRO   B 1 74  ? 43.717 -13.621 15.398  1.00 18.97 ?  74  PRO   B HG3  1 
ATOM   5095 H  HD2  . PRO   B 1 74  ? 43.534 -11.125 14.896  1.00 18.54 ?  74  PRO   B HD2  1 
ATOM   5096 H  HD3  . PRO   B 1 74  ? 44.973 -11.836 14.894  1.00 18.54 ?  74  PRO   B HD3  1 
ATOM   5097 N  N    . LEU   B 1 75  ? 42.611 -13.601 10.451  1.00 11.91 ?  75  LEU   B N    1 
ATOM   5098 C  CA   . LEU   B 1 75  ? 41.397 -13.816 9.683   1.00 11.88 ?  75  LEU   B CA   1 
ATOM   5099 C  C    . LEU   B 1 75  ? 40.424 -14.676 10.484  1.00 12.69 ?  75  LEU   B C    1 
ATOM   5100 O  O    . LEU   B 1 75  ? 40.768 -15.245 11.522  1.00 13.64 ?  75  LEU   B O    1 
ATOM   5101 C  CB   . LEU   B 1 75  ? 41.722 -14.530 8.369   1.00 12.29 ?  75  LEU   B CB   1 
ATOM   5102 C  CG   . LEU   B 1 75  ? 42.575 -13.785 7.337   1.00 13.73 ?  75  LEU   B CG   1 
ATOM   5103 C  CD1  . LEU   B 1 75  ? 42.790 -14.637 6.082   1.00 15.31 ?  75  LEU   B CD1  1 
ATOM   5104 C  CD2  . LEU   B 1 75  ? 41.976 -12.457 6.969   1.00 17.25 ?  75  LEU   B CD2  1 
ATOM   5105 H  H    . LEU   B 1 75  ? 43.285 -14.054 10.160  1.00 14.34 ?  75  LEU   B H    1 
ATOM   5106 H  HA   . LEU   B 1 75  ? 40.975 -12.971 9.481   1.00 14.30 ?  75  LEU   B HA   1 
ATOM   5107 H  HB2  . LEU   B 1 75  ? 42.195 -15.356 8.584   1.00 14.79 ?  75  LEU   B HB2  1 
ATOM   5108 H  HB3  . LEU   B 1 75  ? 40.885 -14.759 7.933   1.00 14.79 ?  75  LEU   B HB3  1 
ATOM   5109 H  HG   . LEU   B 1 75  ? 43.449 -13.619 7.721   1.00 16.52 ?  75  LEU   B HG   1 
ATOM   5110 H  HD11 . LEU   B 1 75  ? 43.338 -14.138 5.450   1.00 18.41 ?  75  LEU   B HD11 1 
ATOM   5111 H  HD12 . LEU   B 1 75  ? 43.246 -15.459 6.327   1.00 18.41 ?  75  LEU   B HD12 1 
ATOM   5112 H  HD13 . LEU   B 1 75  ? 41.932 -14.841 5.682   1.00 18.41 ?  75  LEU   B HD13 1 
ATOM   5113 H  HD21 . LEU   B 1 75  ? 42.500 -12.061 6.257   1.00 20.74 ?  75  LEU   B HD21 1 
ATOM   5114 H  HD22 . LEU   B 1 75  ? 41.063 -12.595 6.676   1.00 20.74 ?  75  LEU   B HD22 1 
ATOM   5115 H  HD23 . LEU   B 1 75  ? 41.991 -11.882 7.751   1.00 20.74 ?  75  LEU   B HD23 1 
ATOM   5116 N  N    . LYS   B 1 76  ? 39.193 -14.769 9.983   1.00 13.77 ?  76  LYS   B N    1 
ATOM   5117 C  CA   . LYS   B 1 76  ? 38.211 -15.732 10.462  1.00 14.97 ?  76  LYS   B CA   1 
ATOM   5118 C  C    . LYS   B 1 76  ? 38.303 -17.005 9.624   1.00 13.47 ?  76  LYS   B C    1 
ATOM   5119 O  O    . LYS   B 1 76  ? 38.575 -16.945 8.426   1.00 12.99 ?  76  LYS   B O    1 
ATOM   5120 C  CB   . LYS   B 1 76  ? 36.791 -15.166 10.287  1.00 17.25 ?  76  LYS   B CB   1 
ATOM   5121 C  CG   . LYS   B 1 76  ? 36.515 -13.764 10.876  1.00 19.21 ?  76  LYS   B CG   1 
ATOM   5122 C  CD   . LYS   B 1 76  ? 35.104 -13.244 10.518  1.00 20.37 ?  76  LYS   B CD   1 
ATOM   5123 C  CE   . LYS   B 1 76  ? 34.828 -11.883 11.140  1.00 22.26 ?  76  LYS   B CE   1 
ATOM   5124 N  NZ   . LYS   B 1 76  ? 33.524 -11.310 10.716  1.00 22.79 ?  76  LYS   B NZ   1 
ATOM   5125 H  H    . LYS   B 1 76  ? 38.900 -14.277 9.344   1.00 16.57 ?  76  LYS   B H    1 
ATOM   5126 H  HA   . LYS   B 1 76  ? 38.363 -15.949 11.397  1.00 18.01 ?  76  LYS   B HA   1 
ATOM   5127 H  HB2  . LYS   B 1 76  ? 36.600 -15.119 9.337   1.00 20.75 ?  76  LYS   B HB2  1 
ATOM   5128 H  HB3  . LYS   B 1 76  ? 36.165 -15.778 10.707  1.00 20.75 ?  76  LYS   B HB3  1 
ATOM   5129 H  HG2  . LYS   B 1 76  ? 36.588 -13.807 11.842  1.00 23.09 ?  76  LYS   B HG2  1 
ATOM   5130 H  HG3  . LYS   B 1 76  ? 37.170 -13.139 10.520  1.00 23.09 ?  76  LYS   B HG3  1 
ATOM   5131 H  HD2  . LYS   B 1 76  ? 35.034 -13.158 9.552   1.00 24.49 ?  76  LYS   B HD2  1 
ATOM   5132 H  HD3  . LYS   B 1 76  ? 34.442 -13.870 10.846  1.00 24.49 ?  76  LYS   B HD3  1 
ATOM   5133 H  HE2  . LYS   B 1 76  ? 34.820 -11.976 12.104  1.00 26.76 ?  76  LYS   B HE2  1 
ATOM   5134 H  HE3  . LYS   B 1 76  ? 35.530 -11.268 10.871  1.00 26.76 ?  76  LYS   B HE3  1 
ATOM   5135 H  HZ1  . LYS   B 1 76  ? 33.400 -10.516 11.100  1.00 27.40 ?  76  LYS   B HZ1  1 
ATOM   5136 H  HZ2  . LYS   B 1 76  ? 33.506 -11.207 9.831   1.00 27.40 ?  76  LYS   B HZ2  1 
ATOM   5137 H  HZ3  . LYS   B 1 76  ? 32.859 -11.852 10.955  1.00 27.40 ?  76  LYS   B HZ3  1 
ATOM   5138 N  N    . VAL   B 1 77  ? 38.060 -18.163 10.251  1.00 14.13 ?  77  VAL   B N    1 
ATOM   5139 C  CA   . VAL   B 1 77  ? 37.852 -19.376 9.463   1.00 14.25 ?  77  VAL   B CA   1 
ATOM   5140 C  C    . VAL   B 1 77  ? 36.655 -19.144 8.554   1.00 13.29 ?  77  VAL   B C    1 
ATOM   5141 O  O    . VAL   B 1 77  ? 35.595 -18.692 9.005   1.00 13.16 ?  77  VAL   B O    1 
ATOM   5142 C  CB   . VAL   B 1 77  ? 37.658 -20.602 10.369  1.00 15.78 ?  77  VAL   B CB   1 
ATOM   5143 C  CG1  . VAL   B 1 77  ? 37.360 -21.830 9.521   1.00 16.47 ?  77  VAL   B CG1  1 
ATOM   5144 C  CG2  . VAL   B 1 77  ? 38.900 -20.844 11.232  1.00 16.76 ?  77  VAL   B CG2  1 
ATOM   5145 H  H    . VAL   B 1 77  ? 38.021 -18.270 11.099  1.00 17.00 ?  77  VAL   B H    1 
ATOM   5146 H  HA   . VAL   B 1 77  ? 38.625 -19.532 8.902   1.00 17.15 ?  77  VAL   B HA   1 
ATOM   5147 H  HB   . VAL   B 1 77  ? 36.900 -20.450 10.957  1.00 18.98 ?  77  VAL   B HB   1 
ATOM   5148 H  HG11 . VAL   B 1 77  ? 37.423 -22.620 10.080  1.00 19.81 ?  77  VAL   B HG11 1 
ATOM   5149 H  HG12 . VAL   B 1 77  ? 36.461 -21.758 9.158   1.00 19.81 ?  77  VAL   B HG12 1 
ATOM   5150 H  HG13 . VAL   B 1 77  ? 38.005 -21.881 8.801   1.00 19.81 ?  77  VAL   B HG13 1 
ATOM   5151 H  HG21 . VAL   B 1 77  ? 38.757 -21.637 11.768  1.00 20.16 ?  77  VAL   B HG21 1 
ATOM   5152 H  HG22 . VAL   B 1 77  ? 39.664 -20.965 10.649  1.00 20.16 ?  77  VAL   B HG22 1 
ATOM   5153 H  HG23 . VAL   B 1 77  ? 39.035 -20.073 11.803  1.00 20.16 ?  77  VAL   B HG23 1 
ATOM   5154 N  N    . GLY   B 1 78  ? 36.832 -19.412 7.261   1.00 12.53 ?  78  GLY   B N    1 
ATOM   5155 C  CA   . GLY   B 1 78  ? 35.852 -19.092 6.249   1.00 12.37 ?  78  GLY   B CA   1 
ATOM   5156 C  C    . GLY   B 1 78  ? 36.094 -17.773 5.551   1.00 11.54 ?  78  GLY   B C    1 
ATOM   5157 O  O    . GLY   B 1 78  ? 35.410 -17.488 4.564   1.00 11.89 ?  78  GLY   B O    1 
ATOM   5158 H  H    . GLY   B 1 78  ? 37.535 -19.794 6.942   1.00 15.08 ?  78  GLY   B H    1 
ATOM   5159 H  HA2  . GLY   B 1 78  ? 35.846 -19.787 5.577   1.00 14.89 ?  78  GLY   B HA2  1 
ATOM   5160 H  HA3  . GLY   B 1 78  ? 34.974 -19.052 6.658   1.00 14.89 ?  78  GLY   B HA3  1 
ATOM   5161 N  N    . GLY   B 1 79  ? 37.047 -16.969 6.036   1.00 11.71 ?  79  GLY   B N    1 
ATOM   5162 C  CA   . GLY   B 1 79  ? 37.349 -15.675 5.459   1.00 11.44 ?  79  GLY   B CA   1 
ATOM   5163 C  C    . GLY   B 1 79  ? 38.585 -15.691 4.569   1.00 10.65 ?  79  GLY   B C    1 
ATOM   5164 O  O    . GLY   B 1 79  ? 39.199 -16.724 4.316   1.00 11.27 ?  79  GLY   B O    1 
ATOM   5165 H  H    . GLY   B 1 79  ? 37.544 -17.161 6.709   1.00 14.10 ?  79  GLY   B H    1 
ATOM   5166 H  HA2  . GLY   B 1 79  ? 36.597 -15.372 4.926   1.00 13.78 ?  79  GLY   B HA2  1 
ATOM   5167 H  HA3  . GLY   B 1 79  ? 37.498 -15.031 6.168   1.00 13.78 ?  79  GLY   B HA3  1 
ATOM   5168 N  N    . SER   B 1 80  ? 38.950 -14.497 4.095   1.00 10.79 ?  80  SER   B N    1 
ATOM   5169 C  CA   . SER   B 1 80  ? 40.057 -14.364 3.158   1.00 10.66 ?  80  SER   B CA   1 
ATOM   5170 C  C    . SER   B 1 80  ? 40.634 -12.956 3.210   1.00 10.70 ?  80  SER   B C    1 
ATOM   5171 O  O    . SER   B 1 80  ? 40.016 -12.024 3.725   1.00 12.00 ?  80  SER   B O    1 
ATOM   5172 C  CB   . SER   B 1 80  ? 39.619 -14.659 1.719   1.00 11.04 ?  80  SER   B CB   1 
ATOM   5173 O  OG   . SER   B 1 80  ? 38.783 -13.636 1.209   1.00 12.16 ?  80  SER   B OG   1 
ATOM   5174 H  H    . SER   B 1 80  ? 38.573 -13.753 4.302   1.00 12.99 ?  80  SER   B H    1 
ATOM   5175 H  HA   . SER   B 1 80  ? 40.751 -14.990 3.403   1.00 12.84 ?  80  SER   B HA   1 
ATOM   5176 H  HB2  . SER   B 1 80  ? 40.404 -14.723 1.153   1.00 13.29 ?  80  SER   B HB2  1 
ATOM   5177 H  HB3  . SER   B 1 80  ? 39.134 -15.500 1.702   1.00 13.29 ?  80  SER   B HB3  1 
ATOM   5178 H  HG   . SER   B 1 80  ? 38.081 -13.572 1.678   1.00 14.63 ?  80  SER   B HG   1 
ATOM   5179 N  N    . CYS   B 1 81  ? 41.823 -12.812 2.626   1.00 10.48 ?  81  CYS   B N    1 
ATOM   5180 C  CA   . CYS   B 1 81  ? 42.376 -11.500 2.313   1.00 10.78 ?  81  CYS   B CA   1 
ATOM   5181 C  C    . CYS   B 1 81  ? 43.145 -11.590 1.004   1.00 9.93  ?  81  CYS   B C    1 
ATOM   5182 O  O    . CYS   B 1 81  ? 43.657 -12.655 0.638   1.00 11.16 ?  81  CYS   B O    1 
ATOM   5183 C  CB   . CYS   B 1 81  ? 43.271 -10.945 3.434   1.00 11.44 ?  81  CYS   B CB   1 
ATOM   5184 S  SG   . CYS   B 1 81  ? 44.786 -11.884 3.688   1.00 11.80 ?  81  CYS   B SG   1 
ATOM   5185 H  H    . CYS   B 1 81  ? 42.333 -13.467 2.389   1.00 12.62 ?  81  CYS   B H    1 
ATOM   5186 H  HA   . CYS   B 1 81  ? 41.645 -10.875 2.182   1.00 12.97 ?  81  CYS   B HA   1 
ATOM   5187 H  HB2  . CYS   B 1 81  ? 43.522 -10.032 3.216   1.00 13.78 ?  81  CYS   B HB2  1 
ATOM   5188 H  HB3  . CYS   B 1 81  ? 42.768 -10.951 4.268   1.00 13.78 ?  81  CYS   B HB3  1 
ATOM   5189 H  HG   . CYS   B 1 81  ? 45.410 -11.385 4.585   1.00 14.20 ?  81  CYS   B HG   1 
ATOM   5190 N  N    . VAL   B 1 82  ? 43.244 -10.448 0.325   1.00 10.49 ?  82  VAL   B N    1 
ATOM   5191 C  CA   . VAL   B 1 82  ? 44.013 -10.322 -0.911  1.00 10.58 ?  82  VAL   B CA   1 
ATOM   5192 C  C    . VAL   B 1 82  ? 45.354 -9.681  -0.588  1.00 10.98 ?  82  VAL   B C    1 
ATOM   5193 O  O    . VAL   B 1 82  ? 45.407 -8.565  -0.054  1.00 11.95 ?  82  VAL   B O    1 
ATOM   5194 C  CB   . VAL   B 1 82  ? 43.266 -9.477  -1.953  1.00 11.96 ?  82  VAL   B CB   1 
ATOM   5195 C  CG1  . VAL   B 1 82  ? 44.112 -9.319  -3.209  1.00 13.16 ?  82  VAL   B CG1  1 
ATOM   5196 C  CG2  . VAL   B 1 82  ? 41.905 -10.073 -2.270  1.00 12.80 ?  82  VAL   B CG2  1 
ATOM   5197 H  H    . VAL   B 1 82  ? 42.858 -9.711  0.562   1.00 12.63 ?  82  VAL   B H    1 
ATOM   5198 H  HA   . VAL   B 1 82  ? 44.171 -11.199 -1.286  1.00 12.74 ?  82  VAL   B HA   1 
ATOM   5199 H  HB   . VAL   B 1 82  ? 43.115 -8.592  -1.592  1.00 14.40 ?  82  VAL   B HB   1 
ATOM   5200 H  HG11 . VAL   B 1 82  ? 43.550 -9.005  -3.936  1.00 15.84 ?  82  VAL   B HG11 1 
ATOM   5201 H  HG12 . VAL   B 1 82  ? 44.815 -8.669  -3.039  1.00 15.84 ?  82  VAL   B HG12 1 
ATOM   5202 H  HG13 . VAL   B 1 82  ? 44.502 -10.175 -3.441  1.00 15.84 ?  82  VAL   B HG13 1 
ATOM   5203 H  HG21 . VAL   B 1 82  ? 41.475 -9.544  -2.962  1.00 15.41 ?  82  VAL   B HG21 1 
ATOM   5204 H  HG22 . VAL   B 1 82  ? 42.020 -10.987 -2.580  1.00 15.41 ?  82  VAL   B HG22 1 
ATOM   5205 H  HG23 . VAL   B 1 82  ? 41.360 -10.066 -1.466  1.00 15.41 ?  82  VAL   B HG23 1 
ATOM   5206 N  N    . LEU   B 1 83  ? 46.435 -10.371 -0.946  1.00 10.58 ?  83  LEU   B N    1 
ATOM   5207 C  CA   . LEU   B 1 83  ? 47.793 -9.853  -0.828  1.00 10.51 ?  83  LEU   B CA   1 
ATOM   5208 C  C    . LEU   B 1 83  ? 48.493 -9.996  -2.182  1.00 10.42 ?  83  LEU   B C    1 
ATOM   5209 O  O    . LEU   B 1 83  ? 47.892 -10.413 -3.178  1.00 10.63 ?  83  LEU   B O    1 
ATOM   5210 C  CB   . LEU   B 1 83  ? 48.543 -10.530 0.330   1.00 11.27 ?  83  LEU   B CB   1 
ATOM   5211 C  CG   . LEU   B 1 83  ? 48.029 -10.169 1.730   1.00 12.13 ?  83  LEU   B CG   1 
ATOM   5212 C  CD1  . LEU   B 1 83  ? 48.661 -11.035 2.800   1.00 12.80 ?  83  LEU   B CD1  1 
ATOM   5213 C  CD2  . LEU   B 1 83  ? 48.235 -8.684  2.051   1.00 13.45 ?  83  LEU   B CD2  1 
ATOM   5214 H  H    . LEU   B 1 83  ? 46.401 -11.166 -1.269  1.00 12.74 ?  83  LEU   B H    1 
ATOM   5215 H  HA   . LEU   B 1 83  ? 47.741 -8.905  -0.632  1.00 12.65 ?  83  LEU   B HA   1 
ATOM   5216 H  HB2  . LEU   B 1 83  ? 48.468 -11.488 0.228   1.00 13.57 ?  83  LEU   B HB2  1 
ATOM   5217 H  HB3  . LEU   B 1 83  ? 49.476 -10.266 0.284   1.00 13.57 ?  83  LEU   B HB3  1 
ATOM   5218 H  HG   . LEU   B 1 83  ? 47.075 -10.333 1.752   1.00 14.60 ?  83  LEU   B HG   1 
ATOM   5219 H  HD11 . LEU   B 1 83  ? 48.303 -10.781 3.667   1.00 15.41 ?  83  LEU   B HD11 1 
ATOM   5220 H  HD12 . LEU   B 1 83  ? 48.446 -11.966 2.618   1.00 15.41 ?  83  LEU   B HD12 1 
ATOM   5221 H  HD13 . LEU   B 1 83  ? 49.620 -10.910 2.789   1.00 15.41 ?  83  LEU   B HD13 1 
ATOM   5222 H  HD21 . LEU   B 1 83  ? 48.025 -8.532  2.985   1.00 16.18 ?  83  LEU   B HD21 1 
ATOM   5223 H  HD22 . LEU   B 1 83  ? 49.157 -8.447  1.874   1.00 16.18 ?  83  LEU   B HD22 1 
ATOM   5224 H  HD23 . LEU   B 1 83  ? 47.644 -8.155  1.490   1.00 16.18 ?  83  LEU   B HD23 1 
ATOM   5225 N  N    . SER   B 1 84  ? 49.768 -9.623  -2.237  1.00 11.39 ?  84  SER   B N    1 
ATOM   5226 C  CA   . SER   B 1 84  ? 50.502 -9.740  -3.488  1.00 11.74 ?  84  SER   B CA   1 
ATOM   5227 C  C    . SER   B 1 84  ? 50.654 -11.199 -3.905  1.00 10.94 ?  84  SER   B C    1 
ATOM   5228 O  O    . SER   B 1 84  ? 50.779 -12.099 -3.074  1.00 10.93 ?  84  SER   B O    1 
ATOM   5229 C  CB   . SER   B 1 84  ? 51.899 -9.144  -3.342  1.00 13.45 ?  84  SER   B CB   1 
ATOM   5230 O  OG   . SER   B 1 84  ? 52.640 -9.351  -4.533  1.00 15.08 ?  84  SER   B OG   1 
ATOM   5231 H  H    . SER   B 1 84  ? 50.219 -9.296  -1.579  1.00 13.71 ?  84  SER   B H    1 
ATOM   5232 H  HA   . SER   B 1 84  ? 50.034 -9.264  -4.189  1.00 14.13 ?  84  SER   B HA   1 
ATOM   5233 H  HB2  . SER   B 1 84  ? 51.822 -8.187  -3.173  1.00 16.19 ?  84  SER   B HB2  1 
ATOM   5234 H  HB3  . SER   B 1 84  ? 52.359 -9.573  -2.605  1.00 16.19 ?  84  SER   B HB3  1 
ATOM   5235 H  HG   . SER   B 1 84  ? 53.409 -9.012  -4.458  1.00 18.14 ?  84  SER   B HG   1 
ATOM   5236 N  N    . GLY   B 1 85  ? 50.714 -11.416 -5.213  1.00 12.10 ?  85  GLY   B N    1 
ATOM   5237 C  CA   . GLY   B 1 85  ? 51.066 -12.706 -5.753  1.00 12.83 ?  85  GLY   B CA   1 
ATOM   5238 C  C    . GLY   B 1 85  ? 52.535 -12.901 -6.054  1.00 11.77 ?  85  GLY   B C    1 
ATOM   5239 O  O    . GLY   B 1 85  ? 52.910 -13.976 -6.524  1.00 12.39 ?  85  GLY   B O    1 
ATOM   5240 H  H    . GLY   B 1 85  ? 50.565 -10.821 -5.809  1.00 14.56 ?  85  GLY   B H    1 
ATOM   5241 H  HA2  . GLY   B 1 85  ? 50.802 -13.396 -5.125  1.00 15.43 ?  85  GLY   B HA2  1 
ATOM   5242 H  HA3  . GLY   B 1 85  ? 50.579 -12.847 -6.575  1.00 15.43 ?  85  GLY   B HA3  1 
ATOM   5243 N  N    . HIS   B 1 86  ? 53.388 -11.908 -5.825  1.00 11.76 ?  86  HIS   B N    1 
ATOM   5244 C  CA   . HIS   B 1 86  ? 54.851 -12.079 -5.914  1.00 12.05 ?  86  HIS   B CA   1 
ATOM   5245 C  C    . HIS   B 1 86  ? 55.226 -12.588 -7.305  1.00 12.23 ?  86  HIS   B C    1 
ATOM   5246 O  O    . HIS   B 1 86  ? 54.843 -11.965 -8.308  1.00 12.95 ?  86  HIS   B O    1 
ATOM   5247 C  CB   . HIS   B 1 86  ? 55.348 -12.921 -4.740  1.00 12.36 ?  86  HIS   B CB   1 
ATOM   5248 C  CG   . HIS   B 1 86  ? 55.039 -12.314 -3.415  1.00 12.59 ?  86  HIS   B CG   1 
ATOM   5249 N  ND1  . HIS   B 1 86  ? 55.868 -11.398 -2.804  1.00 13.54 ?  86  HIS   B ND1  1 
ATOM   5250 C  CD2  . HIS   B 1 86  ? 53.965 -12.458 -2.604  1.00 12.92 ?  86  HIS   B CD2  1 
ATOM   5251 C  CE1  . HIS   B 1 86  ? 55.311 -11.001 -1.674  1.00 13.59 ?  86  HIS   B CE1  1 
ATOM   5252 N  NE2  . HIS   B 1 86  ? 54.158 -11.630 -1.527  1.00 13.03 ?  86  HIS   B NE2  1 
ATOM   5253 H  H    . HIS   B 1 86  ? 53.151 -11.112 -5.612  1.00 14.15 ?  86  HIS   B H    1 
ATOM   5254 H  HA   . HIS   B 1 86  ? 55.260 -11.206 -5.822  1.00 14.50 ?  86  HIS   B HA   1 
ATOM   5255 H  HB2  . HIS   B 1 86  ? 54.929 -13.793 -4.776  1.00 14.88 ?  86  HIS   B HB2  1 
ATOM   5256 H  HB3  . HIS   B 1 86  ? 56.313 -13.015 -4.805  1.00 14.88 ?  86  HIS   B HB3  1 
ATOM   5257 H  HD2  . HIS   B 1 86  ? 53.226 -13.003 -2.756  1.00 15.54 ?  86  HIS   B HD2  1 
ATOM   5258 H  HE1  . HIS   B 1 86  ? 55.680 -10.399 -1.068  1.00 16.35 ?  86  HIS   B HE1  1 
ATOM   5259 H  HE2  . HIS   B 1 86  ? 53.622 -11.547 -0.859  1.00 15.68 ?  86  HIS   B HE2  1 
ATOM   5260 N  N    . ASN   B 1 87  ? 55.988 -13.673 -7.415  1.00 12.73 ?  87  ASN   B N    1 
ATOM   5261 C  CA   . ASN   B 1 87  ? 56.386 -14.241 -8.693  1.00 13.36 ?  87  ASN   B CA   1 
ATOM   5262 C  C    . ASN   B 1 87  ? 55.409 -15.288 -9.196  1.00 12.94 ?  87  ASN   B C    1 
ATOM   5263 O  O    . ASN   B 1 87  ? 55.725 -15.995 -10.159 1.00 14.65 ?  87  ASN   B O    1 
ATOM   5264 C  CB   . ASN   B 1 87  ? 57.785 -14.860 -8.575  1.00 15.09 ?  87  ASN   B CB   1 
ATOM   5265 C  CG   . ASN   B 1 87  ? 57.848 -15.973 -7.536  1.00 16.20 ?  87  ASN   B CG   1 
ATOM   5266 O  OD1  . ASN   B 1 87  ? 57.206 -15.898 -6.483  1.00 15.06 ?  87  ASN   B OD1  1 
ATOM   5267 N  ND2  . ASN   B 1 87  ? 58.601 -17.033 -7.846  1.00 18.32 ?  87  ASN   B ND2  1 
ATOM   5268 H  H    . ASN   B 1 87  ? 56.289 -14.115 -6.743  1.00 15.32 ?  87  ASN   B H    1 
ATOM   5269 H  HA   . ASN   B 1 87  ? 56.426 -13.533 -9.354  1.00 16.07 ?  87  ASN   B HA   1 
ATOM   5270 H  HB2  . ASN   B 1 87  ? 58.039 -15.233 -9.436  1.00 18.15 ?  87  ASN   B HB2  1 
ATOM   5271 H  HB3  . ASN   B 1 87  ? 58.414 -14.169 -8.317  1.00 18.15 ?  87  ASN   B HB3  1 
ATOM   5272 H  HD21 . ASN   B 1 87  ? 58.672 -17.686 -7.295  1.00 22.02 ?  87  ASN   B HD21 1 
ATOM   5273 H  HD22 . ASN   B 1 87  ? 59.032 -17.053 -8.594  1.00 22.02 ?  87  ASN   B HD22 1 
ATOM   5274 N  N    . LEU   B 1 88  ? 54.229 -15.393 -8.577  1.00 11.83 ?  88  LEU   B N    1 
ATOM   5275 C  CA   . LEU   B 1 88  ? 53.252 -16.424 -8.907  1.00 12.12 ?  88  LEU   B CA   1 
ATOM   5276 C  C    . LEU   B 1 88  ? 52.016 -15.908 -9.625  1.00 11.97 ?  88  LEU   B C    1 
ATOM   5277 O  O    . LEU   B 1 88  ? 51.410 -16.660 -10.400 1.00 13.67 ?  88  LEU   B O    1 
ATOM   5278 C  CB   . LEU   B 1 88  ? 52.789 -17.120 -7.624  1.00 13.34 ?  88  LEU   B CB   1 
ATOM   5279 C  CG   . LEU   B 1 88  ? 53.916 -17.770 -6.831  1.00 15.75 ?  88  LEU   B CG   1 
ATOM   5280 C  CD1  . LEU   B 1 88  ? 53.423 -18.170 -5.451  1.00 17.35 ?  88  LEU   B CD1  1 
ATOM   5281 C  CD2  . LEU   B 1 88  ? 54.444 -18.968 -7.594  1.00 18.83 ?  88  LEU   B CD2  1 
ATOM   5282 H  H    . LEU   B 1 88  ? 53.973 -14.865 -7.942  1.00 14.24 ?  88  LEU   B H    1 
ATOM   5283 H  HA   . LEU   B 1 88  ? 53.670 -17.081 -9.473  1.00 14.59 ?  88  LEU   B HA   1 
ATOM   5284 H  HB2  . LEU   B 1 88  ? 52.361 -16.470 -7.045  1.00 16.05 ?  88  LEU   B HB2  1 
ATOM   5285 H  HB3  . LEU   B 1 88  ? 52.156 -17.817 -7.859  1.00 16.05 ?  88  LEU   B HB3  1 
ATOM   5286 H  HG   . LEU   B 1 88  ? 54.641 -17.134 -6.724  1.00 18.94 ?  88  LEU   B HG   1 
ATOM   5287 H  HD11 . LEU   B 1 88  ? 54.115 -18.681 -5.005  1.00 20.87 ?  88  LEU   B HD11 1 
ATOM   5288 H  HD12 . LEU   B 1 88  ? 53.220 -17.369 -4.944  1.00 20.87 ?  88  LEU   B HD12 1 
ATOM   5289 H  HD13 . LEU   B 1 88  ? 52.623 -18.710 -5.551  1.00 20.87 ?  88  LEU   B HD13 1 
ATOM   5290 H  HD21 . LEU   B 1 88  ? 55.079 -19.440 -7.034  1.00 22.64 ?  88  LEU   B HD21 1 
ATOM   5291 H  HD22 . LEU   B 1 88  ? 53.701 -19.551 -7.816  1.00 22.64 ?  88  LEU   B HD22 1 
ATOM   5292 H  HD23 . LEU   B 1 88  ? 54.879 -18.662 -8.404  1.00 22.64 ?  88  LEU   B HD23 1 
ATOM   5293 N  N    . ALA   B 1 89  ? 51.610 -14.671 -9.360  1.00 11.49 ?  89  ALA   B N    1 
ATOM   5294 C  CA   . ALA   B 1 89  ? 50.316 -14.173 -9.800  1.00 11.15 ?  89  ALA   B CA   1 
ATOM   5295 C  C    . ALA   B 1 89  ? 50.287 -12.680 -9.520  1.00 11.48 ?  89  ALA   B C    1 
ATOM   5296 O  O    . ALA   B 1 89  ? 51.124 -12.160 -8.781  1.00 12.31 ?  89  ALA   B O    1 
ATOM   5297 C  CB   . ALA   B 1 89  ? 49.183 -14.850 -9.033  1.00 11.20 ?  89  ALA   B CB   1 
ATOM   5298 H  H    . ALA   B 1 89  ? 52.065 -14.089 -8.917  1.00 13.83 ?  89  ALA   B H    1 
ATOM   5299 H  HA   . ALA   B 1 89  ? 50.195 -14.323 -10.753 1.00 13.42 ?  89  ALA   B HA   1 
ATOM   5300 H  HB1  . ALA   B 1 89  ? 48.331 -14.513 -9.358  1.00 13.48 ?  89  ALA   B HB1  1 
ATOM   5301 H  HB2  . ALA   B 1 89  ? 49.231 -15.810 -9.183  1.00 13.48 ?  89  ALA   B HB2  1 
ATOM   5302 H  HB3  . ALA   B 1 89  ? 49.278 -14.658 -8.091  1.00 13.48 ?  89  ALA   B HB3  1 
ATOM   5303 N  N    . LYS   B 1 90  ? 49.293 -11.990 -10.080 1.00 12.25 ?  90  LYS   B N    1 
ATOM   5304 C  CA   . LYS   B 1 90  ? 49.109 -10.601 -9.677  1.00 12.59 ?  90  LYS   B CA   1 
ATOM   5305 C  C    . LYS   B 1 90  ? 48.791 -10.524 -8.190  1.00 12.28 ?  90  LYS   B C    1 
ATOM   5306 O  O    . LYS   B 1 90  ? 49.442 -9.782  -7.440  1.00 13.41 ?  90  LYS   B O    1 
ATOM   5307 C  CB   . LYS   B 1 90  ? 48.032 -9.933  -10.531 1.00 13.91 ?  90  LYS   B CB   1 
ATOM   5308 C  CG   . LYS   B 1 90  ? 47.743 -8.491  -10.147 1.00 14.37 ?  90  LYS   B CG   1 
ATOM   5309 C  CD   . LYS   B 1 90  ? 48.958 -7.596  -10.229 1.00 17.03 ?  90  LYS   B CD   1 
ATOM   5310 C  CE   . LYS   B 1 90  ? 48.523 -6.175  -9.983  1.00 19.17 ?  90  LYS   B CE   1 
ATOM   5311 N  NZ   . LYS   B 1 90  ? 49.673 -5.250  -9.854  1.00 19.07 ?  90  LYS   B NZ   1 
ATOM   5312 H  H    . LYS   B 1 90  ? 48.735 -12.292 -10.660 1.00 14.74 ?  90  LYS   B H    1 
ATOM   5313 H  HA   . LYS   B 1 90  ? 49.938 -10.127 -9.826  1.00 15.15 ?  90  LYS   B HA   1 
ATOM   5314 H  HB2  . LYS   B 1 90  ? 48.321 -9.938  -11.458 1.00 16.73 ?  90  LYS   B HB2  1 
ATOM   5315 H  HB3  . LYS   B 1 90  ? 47.205 -10.433 -10.446 1.00 16.73 ?  90  LYS   B HB3  1 
ATOM   5316 H  HG2  . LYS   B 1 90  ? 47.071 -8.134  -10.747 1.00 17.29 ?  90  LYS   B HG2  1 
ATOM   5317 H  HG3  . LYS   B 1 90  ? 47.412 -8.465  -9.233  1.00 17.29 ?  90  LYS   B HG3  1 
ATOM   5318 H  HD2  . LYS   B 1 90  ? 49.601 -7.847  -9.546  1.00 20.47 ?  90  LYS   B HD2  1 
ATOM   5319 H  HD3  . LYS   B 1 90  ? 49.353 -7.657  -11.112 1.00 20.47 ?  90  LYS   B HD3  1 
ATOM   5320 H  HE2  . LYS   B 1 90  ? 47.980 -5.868  -10.730 1.00 23.05 ?  90  LYS   B HE2  1 
ATOM   5321 H  HE3  . LYS   B 1 90  ? 48.011 -6.127  -9.161  1.00 23.05 ?  90  LYS   B HE3  1 
ATOM   5322 H  HZ1  . LYS   B 1 90  ? 49.388 -4.417  -9.713  1.00 22.93 ?  90  LYS   B HZ1  1 
ATOM   5323 H  HZ2  . LYS   B 1 90  ? 50.189 -5.496  -9.172  1.00 22.93 ?  90  LYS   B HZ2  1 
ATOM   5324 H  HZ3  . LYS   B 1 90  ? 50.161 -5.261  -10.601 1.00 22.93 ?  90  LYS   B HZ3  1 
ATOM   5325 N  N    . HIS   B 1 91  ? 47.830 -11.334 -7.740  1.00 10.77 ?  91  HIS   B N    1 
ATOM   5326 C  CA   . HIS   B 1 91  ? 47.367 -11.361 -6.366  1.00 10.80 ?  91  HIS   B CA   1 
ATOM   5327 C  C    . HIS   B 1 91  ? 47.365 -12.790 -5.847  1.00 10.06 ?  91  HIS   B C    1 
ATOM   5328 O  O    . HIS   B 1 91  ? 47.136 -13.740 -6.602  1.00 10.62 ?  91  HIS   B O    1 
ATOM   5329 C  CB   . HIS   B 1 91  ? 45.915 -10.883 -6.257  1.00 12.32 ?  91  HIS   B CB   1 
ATOM   5330 C  CG   . HIS   B 1 91  ? 45.702 -9.477  -6.701  1.00 15.75 ?  91  HIS   B CG   1 
ATOM   5331 N  ND1  . HIS   B 1 91  ? 46.308 -8.399  -6.092  1.00 18.20 ?  91  HIS   B ND1  1 
ATOM   5332 C  CD2  . HIS   B 1 91  ? 44.908 -8.965  -7.667  1.00 17.95 ?  91  HIS   B CD2  1 
ATOM   5333 C  CE1  . HIS   B 1 91  ? 45.922 -7.283  -6.686  1.00 19.20 ?  91  HIS   B CE1  1 
ATOM   5334 N  NE2  . HIS   B 1 91  ? 45.064 -7.600  -7.641  1.00 19.45 ?  91  HIS   B NE2  1 
ATOM   5335 H  H    . HIS   B 1 91  ? 47.413 -11.897 -8.238  1.00 12.96 ?  91  HIS   B H    1 
ATOM   5336 H  HA   . HIS   B 1 91  ? 47.936 -10.803 -5.799  1.00 13.00 ?  91  HIS   B HA   1 
ATOM   5337 H  HB2  . HIS   B 1 91  ? 45.358 -11.454 -6.807  1.00 14.82 ?  91  HIS   B HB2  1 
ATOM   5338 H  HB3  . HIS   B 1 91  ? 45.631 -10.947 -5.328  1.00 14.82 ?  91  HIS   B HB3  1 
ATOM   5339 H  HD1  . HIS   B 1 91  ? 46.866 -8.447  -5.436  1.00 21.88 ?  91  HIS   B HD1  1 
ATOM   5340 H  HD2  . HIS   B 1 91  ? 44.368 -9.442  -8.252  1.00 21.58 ?  91  HIS   B HD2  1 
ATOM   5341 H  HE1  . HIS   B 1 91  ? 46.201 -6.424  -6.460  1.00 23.08 ?  91  HIS   B HE1  1 
ATOM   5342 N  N    . CYS   B 1 92  ? 47.563 -12.929 -4.540  1.00 9.96  ?  92  CYS   B N    1 
ATOM   5343 C  CA   . CYS   B 1 92  ? 47.257 -14.162 -3.829  1.00 9.92  ?  92  CYS   B CA   1 
ATOM   5344 C  C    . CYS   B 1 92  ? 46.036 -13.924 -2.947  1.00 9.43  ?  92  CYS   B C    1 
ATOM   5345 O  O    . CYS   B 1 92  ? 46.033 -13.012 -2.106  1.00 10.39 ?  92  CYS   B O    1 
ATOM   5346 C  CB   . CYS   B 1 92  ? 48.436 -14.623 -2.975  1.00 10.21 ?  92  CYS   B CB   1 
ATOM   5347 S  SG   . CYS   B 1 92  ? 48.081 -16.153 -2.076  1.00 10.22 ?  92  CYS   B SG   1 
ATOM   5348 H  H    . CYS   B 1 92  ? 47.892 -12.309 -4.031  1.00 11.99 ?  92  CYS   B H    1 
ATOM   5349 H  HA   . CYS   B 1 92  ? 47.054 -14.857 -4.476  1.00 11.95 ?  92  CYS   B HA   1 
ATOM   5350 H  HB2  . CYS   B 1 92  ? 49.199 -14.776 -3.545  1.00 12.30 ?  92  CYS   B HB2  1 
ATOM   5351 H  HB3  . CYS   B 1 92  ? 48.632 -13.934 -2.322  1.00 12.30 ?  92  CYS   B HB3  1 
ATOM   5352 H  HG   . CYS   B 1 92  ? 49.051 -16.466 -1.447  1.00 12.31 ?  92  CYS   B HG   1 
ATOM   5353 N  N    . LEU   B 1 93  ? 45.000 -14.735 -3.158  1.00 9.39  ?  93  LEU   B N    1 
ATOM   5354 C  CA   . LEU   B 1 93  ? 43.825 -14.746 -2.299  1.00 9.50  ?  93  LEU   B CA   1 
ATOM   5355 C  C    . LEU   B 1 93  ? 44.051 -15.807 -1.231  1.00 9.00  ?  93  LEU   B C    1 
ATOM   5356 O  O    . LEU   B 1 93  ? 44.003 -17.008 -1.520  1.00 9.60  ?  93  LEU   B O    1 
ATOM   5357 C  CB   . LEU   B 1 93  ? 42.564 -15.037 -3.110  1.00 9.80  ?  93  LEU   B CB   1 
ATOM   5358 C  CG   . LEU   B 1 93  ? 41.268 -15.054 -2.295  1.00 10.55 ?  93  LEU   B CG   1 
ATOM   5359 C  CD1  . LEU   B 1 93  ? 40.913 -13.668 -1.807  1.00 10.69 ?  93  LEU   B CD1  1 
ATOM   5360 C  CD2  . LEU   B 1 93  ? 40.138 -15.648 -3.119  1.00 10.81 ?  93  LEU   B CD2  1 
ATOM   5361 H  H    . LEU   B 1 93  ? 44.958 -15.308 -3.813  1.00 11.31 ?  93  LEU   B H    1 
ATOM   5362 H  HA   . LEU   B 1 93  ? 43.732 -13.883 -1.875  1.00 11.45 ?  93  LEU   B HA   1 
ATOM   5363 H  HB2  . LEU   B 1 93  ? 42.469 -14.349 -3.792  1.00 11.80 ?  93  LEU   B HB2  1 
ATOM   5364 H  HB3  . LEU   B 1 93  ? 42.655 -15.901 -3.533  1.00 11.80 ?  93  LEU   B HB3  1 
ATOM   5365 H  HG   . LEU   B 1 93  ? 41.393 -15.616 -1.518  1.00 12.71 ?  93  LEU   B HG   1 
ATOM   5366 H  HD11 . LEU   B 1 93  ? 40.060 -13.702 -1.352  1.00 12.87 ?  93  LEU   B HD11 1 
ATOM   5367 H  HD12 . LEU   B 1 93  ? 41.603 -13.359 -1.201  1.00 12.87 ?  93  LEU   B HD12 1 
ATOM   5368 H  HD13 . LEU   B 1 93  ? 40.855 -13.069 -2.573  1.00 12.87 ?  93  LEU   B HD13 1 
ATOM   5369 H  HD21 . LEU   B 1 93  ? 39.327 -15.647 -2.588  1.00 13.01 ?  93  LEU   B HD21 1 
ATOM   5370 H  HD22 . LEU   B 1 93  ? 40.013 -15.111 -3.917  1.00 13.01 ?  93  LEU   B HD22 1 
ATOM   5371 H  HD23 . LEU   B 1 93  ? 40.373 -16.557 -3.364  1.00 13.01 ?  93  LEU   B HD23 1 
ATOM   5372 N  N    . HIS   B 1 94  ? 44.325 -15.370 -0.009  1.00 9.13  ?  94  HIS   B N    1 
ATOM   5373 C  CA   . HIS   B 1 94  ? 44.549 -16.275 1.114   1.00 9.32  ?  94  HIS   B CA   1 
ATOM   5374 C  C    . HIS   B 1 94  ? 43.190 -16.634 1.697   1.00 9.69  ?  94  HIS   B C    1 
ATOM   5375 O  O    . HIS   B 1 94  ? 42.516 -15.759 2.245   1.00 11.05 ?  94  HIS   B O    1 
ATOM   5376 C  CB   . HIS   B 1 94  ? 45.419 -15.599 2.173   1.00 9.79  ?  94  HIS   B CB   1 
ATOM   5377 C  CG   . HIS   B 1 94  ? 46.801 -15.297 1.703   1.00 9.79  ?  94  HIS   B CG   1 
ATOM   5378 N  ND1  . HIS   B 1 94  ? 47.828 -16.212 1.791   1.00 10.09 ?  94  HIS   B ND1  1 
ATOM   5379 C  CD2  . HIS   B 1 94  ? 47.311 -14.192 1.106   1.00 10.25 ?  94  HIS   B CD2  1 
ATOM   5380 C  CE1  . HIS   B 1 94  ? 48.917 -15.664 1.282   1.00 9.92  ?  94  HIS   B CE1  1 
ATOM   5381 N  NE2  . HIS   B 1 94  ? 48.633 -14.443 0.857   1.00 10.21 ?  94  HIS   B NE2  1 
ATOM   5382 H  H    . HIS   B 1 94  ? 44.391 -14.531 0.195   1.00 10.99 ?  94  HIS   B H    1 
ATOM   5383 H  HA   . HIS   B 1 94  ? 44.986 -17.080 0.800   1.00 11.23 ?  94  HIS   B HA   1 
ATOM   5384 H  HB2  . HIS   B 1 94  ? 45.003 -14.765 2.431   1.00 11.80 ?  94  HIS   B HB2  1 
ATOM   5385 H  HB3  . HIS   B 1 94  ? 45.486 -16.191 2.935   1.00 11.80 ?  94  HIS   B HB3  1 
ATOM   5386 H  HD2  . HIS   B 1 94  ? 46.855 -13.411 0.904   1.00 12.35 ?  94  HIS   B HD2  1 
ATOM   5387 H  HE1  . HIS   B 1 94  ? 49.748 -16.085 1.233   1.00 11.95 ?  94  HIS   B HE1  1 
ATOM   5388 H  HE2  . HIS   B 1 94  ? 49.193 -13.907 0.492   1.00 12.30 ?  94  HIS   B HE2  1 
ATOM   5389 N  N    . VAL   B 1 95  ? 42.755 -17.888 1.545   1.00 9.43  ?  95  VAL   B N    1 
ATOM   5390 C  CA   . VAL   B 1 95  ? 41.427 -18.324 1.976   1.00 9.70  ?  95  VAL   B CA   1 
ATOM   5391 C  C    . VAL   B 1 95  ? 41.593 -19.359 3.073   1.00 9.85  ?  95  VAL   B C    1 
ATOM   5392 O  O    . VAL   B 1 95  ? 42.363 -20.313 2.917   1.00 10.43 ?  95  VAL   B O    1 
ATOM   5393 C  CB   . VAL   B 1 95  ? 40.605 -18.926 0.820   1.00 9.95  ?  95  VAL   B CB   1 
ATOM   5394 C  CG1  . VAL   B 1 95  ? 39.232 -19.366 1.309   1.00 11.07 ?  95  VAL   B CG1  1 
ATOM   5395 C  CG2  . VAL   B 1 95  ? 40.486 -17.953 -0.317  1.00 10.36 ?  95  VAL   B CG2  1 
ATOM   5396 H  H    . VAL   B 1 95  ? 43.222 -18.516 1.186   1.00 11.36 ?  95  VAL   B H    1 
ATOM   5397 H  HA   . VAL   B 1 95  ? 40.938 -17.569 2.340   1.00 11.68 ?  95  VAL   B HA   1 
ATOM   5398 H  HB   . VAL   B 1 95  ? 41.065 -19.712 0.490   1.00 11.98 ?  95  VAL   B HB   1 
ATOM   5399 H  HG11 . VAL   B 1 95  ? 38.667 -19.557 0.539   1.00 13.32 ?  95  VAL   B HG11 1 
ATOM   5400 H  HG12 . VAL   B 1 95  ? 39.320 -20.163 1.854   1.00 13.32 ?  95  VAL   B HG12 1 
ATOM   5401 H  HG13 . VAL   B 1 95  ? 38.833 -18.650 1.832   1.00 13.32 ?  95  VAL   B HG13 1 
ATOM   5402 H  HG21 . VAL   B 1 95  ? 39.915 -18.343 -0.998  1.00 12.48 ?  95  VAL   B HG21 1 
ATOM   5403 H  HG22 . VAL   B 1 95  ? 40.092 -17.133 0.016   1.00 12.48 ?  95  VAL   B HG22 1 
ATOM   5404 H  HG23 . VAL   B 1 95  ? 41.366 -17.783 -0.675  1.00 12.48 ?  95  VAL   B HG23 1 
ATOM   5405 N  N    . VAL   B 1 96  ? 40.859 -19.187 4.167   1.00 10.28 ?  96  VAL   B N    1 
ATOM   5406 C  CA   . VAL   B 1 96  ? 40.937 -20.101 5.305   1.00 10.51 ?  96  VAL   B CA   1 
ATOM   5407 C  C    . VAL   B 1 96  ? 39.746 -21.060 5.261   1.00 10.90 ?  96  VAL   B C    1 
ATOM   5408 O  O    . VAL   B 1 96  ? 38.628 -20.705 5.645   1.00 11.74 ?  96  VAL   B O    1 
ATOM   5409 C  CB   . VAL   B 1 96  ? 40.990 -19.354 6.641   1.00 11.24 ?  96  VAL   B CB   1 
ATOM   5410 C  CG1  . VAL   B 1 96  ? 41.159 -20.353 7.786   1.00 12.05 ?  96  VAL   B CG1  1 
ATOM   5411 C  CG2  . VAL   B 1 96  ? 42.101 -18.315 6.656   1.00 12.12 ?  96  VAL   B CG2  1 
ATOM   5412 H  H    . VAL   B 1 96  ? 40.297 -18.546 4.278   1.00 12.38 ?  96  VAL   B H    1 
ATOM   5413 H  HA   . VAL   B 1 96  ? 41.749 -20.630 5.233   1.00 12.66 ?  96  VAL   B HA   1 
ATOM   5414 H  HB   . VAL   B 1 96  ? 40.149 -18.893 6.778   1.00 13.53 ?  96  VAL   B HB   1 
ATOM   5415 H  HG11 . VAL   B 1 96  ? 41.353 -19.866 8.608   1.00 14.50 ?  96  VAL   B HG11 1 
ATOM   5416 H  HG12 . VAL   B 1 96  ? 40.339 -20.860 7.897   1.00 14.50 ?  96  VAL   B HG12 1 
ATOM   5417 H  HG13 . VAL   B 1 96  ? 41.895 -20.951 7.584   1.00 14.50 ?  96  VAL   B HG13 1 
ATOM   5418 H  HG21 . VAL   B 1 96  ? 42.144 -17.903 7.538   1.00 14.59 ?  96  VAL   B HG21 1 
ATOM   5419 H  HG22 . VAL   B 1 96  ? 42.946 -18.743 6.454   1.00 14.59 ?  96  VAL   B HG22 1 
ATOM   5420 H  HG23 . VAL   B 1 96  ? 41.909 -17.633 5.990   1.00 14.59 ?  96  VAL   B HG23 1 
ATOM   5421 N  N    . GLY   B 1 97  ? 39.980 -22.292 4.820   1.00 11.07 ?  97  GLY   B N    1 
ATOM   5422 C  CA   . GLY   B 1 97  ? 39.012 -23.355 4.986   1.00 11.67 ?  97  GLY   B CA   1 
ATOM   5423 C  C    . GLY   B 1 97  ? 39.139 -23.962 6.366   1.00 12.86 ?  97  GLY   B C    1 
ATOM   5424 O  O    . GLY   B 1 97  ? 40.182 -23.834 7.022   1.00 13.24 ?  97  GLY   B O    1 
ATOM   5425 H  H    . GLY   B 1 97  ? 40.705 -22.532 4.418   1.00 13.32 ?  97  GLY   B H    1 
ATOM   5426 H  HA2  . GLY   B 1 97  ? 38.117 -22.992 4.868   1.00 14.05 ?  97  GLY   B HA2  1 
ATOM   5427 H  HA3  . GLY   B 1 97  ? 39.160 -24.039 4.314   1.00 14.05 ?  97  GLY   B HA3  1 
ATOM   5428 N  N    . PRO   B 1 98  ? 38.093 -24.648 6.831   1.00 13.50 ?  98  PRO   B N    1 
ATOM   5429 C  CA   . PRO   B 1 98  ? 38.189 -25.349 8.114   1.00 14.54 ?  98  PRO   B CA   1 
ATOM   5430 C  C    . PRO   B 1 98  ? 39.220 -26.464 8.065   1.00 14.10 ?  98  PRO   B C    1 
ATOM   5431 O  O    . PRO   B 1 98  ? 39.323 -27.200 7.085   1.00 14.38 ?  98  PRO   B O    1 
ATOM   5432 C  CB   . PRO   B 1 98  ? 36.774 -25.903 8.319   1.00 15.08 ?  98  PRO   B CB   1 
ATOM   5433 C  CG   . PRO   B 1 98  ? 36.205 -26.026 6.949   1.00 14.51 ?  98  PRO   B CG   1 
ATOM   5434 C  CD   . PRO   B 1 98  ? 36.778 -24.843 6.193   1.00 13.50 ?  98  PRO   B CD   1 
ATOM   5435 H  HA   . PRO   B 1 98  ? 38.410 -24.730 8.818   1.00 17.49 ?  98  PRO   B HA   1 
ATOM   5436 H  HB2  . PRO   B 1 98  ? 36.825 -26.775 8.750   1.00 18.14 ?  98  PRO   B HB2  1 
ATOM   5437 H  HB3  . PRO   B 1 98  ? 36.257 -25.286 8.853   1.00 18.14 ?  98  PRO   B HB3  1 
ATOM   5438 H  HG2  . PRO   B 1 98  ? 36.490 -26.865 6.550   1.00 17.46 ?  98  PRO   B HG2  1 
ATOM   5439 H  HG3  . PRO   B 1 98  ? 35.238 -25.978 6.993   1.00 17.46 ?  98  PRO   B HG3  1 
ATOM   5440 H  HD2  . PRO   B 1 98  ? 36.872 -25.063 5.249   1.00 16.24 ?  98  PRO   B HD2  1 
ATOM   5441 H  HD3  . PRO   B 1 98  ? 36.224 -24.059 6.322   1.00 16.24 ?  98  PRO   B HD3  1 
ATOM   5442 N  N    . ASN   B 1 99  ? 39.974 -26.590 9.149   1.00 15.47 ?  99  ASN   B N    1 
ATOM   5443 C  CA   . ASN   B 1 99  ? 40.951 -27.663 9.308   1.00 16.41 ?  99  ASN   B CA   1 
ATOM   5444 C  C    . ASN   B 1 99  ? 40.319 -28.745 10.183  1.00 19.00 ?  99  ASN   B C    1 
ATOM   5445 O  O    . ASN   B 1 99  ? 40.237 -28.599 11.405  1.00 19.47 ?  99  ASN   B O    1 
ATOM   5446 C  CB   . ASN   B 1 99  ? 42.227 -27.108 9.927   1.00 16.73 ?  99  ASN   B CB   1 
ATOM   5447 C  CG   . ASN   B 1 99  ? 43.359 -28.112 9.928   1.00 17.46 ?  99  ASN   B CG   1 
ATOM   5448 O  OD1  . ASN   B 1 99  ? 43.135 -29.301 10.105  1.00 18.11 ?  99  ASN   B OD1  1 
ATOM   5449 N  ND2  . ASN   B 1 99  ? 44.578 -27.638 9.724   1.00 17.64 ?  99  ASN   B ND2  1 
ATOM   5450 H  H    . ASN   B 1 99  ? 39.943 -26.050 9.813   1.00 18.61 ?  99  ASN   B H    1 
ATOM   5451 H  HA   . ASN   B 1 99  ? 41.161 -28.052 8.444   1.00 19.73 ?  99  ASN   B HA   1 
ATOM   5452 H  HB2  . ASN   B 1 99  ? 42.508 -26.336 9.425   1.00 20.11 ?  99  ASN   B HB2  1 
ATOM   5453 H  HB3  . ASN   B 1 99  ? 42.043 -26.865 10.849  1.00 20.11 ?  99  ASN   B HB3  1 
ATOM   5454 H  HD21 . ASN   B 1 99  ? 45.250 -28.171 9.711   1.00 21.22 ?  99  ASN   B HD21 1 
ATOM   5455 H  HD22 . ASN   B 1 99  ? 44.689 -26.795 9.605   1.00 21.22 ?  99  ASN   B HD22 1 
ATOM   5456 N  N    A VAL   B 1 100 ? 39.849 -29.824 9.550   0.60 21.30 ?  100 VAL   B N    1 
ATOM   5457 N  N    B VAL   B 1 100 ? 39.855 -29.822 9.542   0.40 21.31 ?  100 VAL   B N    1 
ATOM   5458 C  CA   A VAL   B 1 100 ? 39.234 -30.916 10.302  0.60 23.97 ?  100 VAL   B CA   1 
ATOM   5459 C  CA   B VAL   B 1 100 ? 39.237 -30.931 10.266  0.40 23.73 ?  100 VAL   B CA   1 
ATOM   5460 C  C    A VAL   B 1 100 ? 40.247 -31.570 11.231  0.60 24.22 ?  100 VAL   B C    1 
ATOM   5461 C  C    B VAL   B 1 100 ? 40.238 -31.597 11.203  0.40 24.18 ?  100 VAL   B C    1 
ATOM   5462 O  O    A VAL   B 1 100 ? 39.889 -32.056 12.311  0.60 24.81 ?  100 VAL   B O    1 
ATOM   5463 O  O    B VAL   B 1 100 ? 39.861 -32.116 12.261  0.40 24.47 ?  100 VAL   B O    1 
ATOM   5464 C  CB   A VAL   B 1 100 ? 38.586 -31.933 9.341   0.60 26.48 ?  100 VAL   B CB   1 
ATOM   5465 C  CB   B VAL   B 1 100 ? 38.617 -31.930 9.266   0.40 25.69 ?  100 VAL   B CB   1 
ATOM   5466 C  CG1  A VAL   B 1 100 ? 38.119 -33.166 10.103  0.60 27.43 ?  100 VAL   B CG1  1 
ATOM   5467 C  CG1  B VAL   B 1 100 ? 38.148 -33.189 9.978   0.40 26.42 ?  100 VAL   B CG1  1 
ATOM   5468 C  CG2  A VAL   B 1 100 ? 37.422 -31.292 8.604   0.60 27.12 ?  100 VAL   B CG2  1 
ATOM   5469 C  CG2  B VAL   B 1 100 ? 37.461 -31.279 8.519   0.40 26.24 ?  100 VAL   B CG2  1 
ATOM   5470 H  H    A VAL   B 1 100 ? 39.865 -29.940 8.695   0.60 25.61 ?  100 VAL   B H    1 
ATOM   5471 H  H    B VAL   B 1 100 ? 39.875 -29.927 8.685   0.40 25.62 ?  100 VAL   B H    1 
ATOM   5472 H  HA   A VAL   B 1 100 ? 38.520 -30.548 10.848  0.60 28.81 ?  100 VAL   B HA   1 
ATOM   5473 H  HA   B VAL   B 1 100 ? 38.511 -30.580 10.806  0.40 28.52 ?  100 VAL   B HA   1 
ATOM   5474 H  HB   A VAL   B 1 100 ? 39.241 -32.216 8.685   0.60 31.82 ?  100 VAL   B HB   1 
ATOM   5475 H  HB   B VAL   B 1 100 ? 39.287 -32.188 8.614   0.40 30.87 ?  100 VAL   B HB   1 
ATOM   5476 H  HG11 A VAL   B 1 100 ? 37.517 -33.677 9.537   0.60 32.96 ?  100 VAL   B HG11 1 
ATOM   5477 H  HG11 B VAL   B 1 100 ? 37.566 -33.690 9.383   0.40 31.74 ?  100 VAL   B HG11 1 
ATOM   5478 H  HG12 A VAL   B 1 100 ? 38.888 -33.709 10.337  0.60 32.96 ?  100 VAL   B HG12 1 
ATOM   5479 H  HG12 B VAL   B 1 100 ? 38.919 -33.729 10.213  0.40 31.74 ?  100 VAL   B HG12 1 
ATOM   5480 H  HG13 A VAL   B 1 100 ? 37.653 -32.885 10.906  0.60 32.96 ?  100 VAL   B HG13 1 
ATOM   5481 H  HG13 B VAL   B 1 100 ? 37.661 -32.937 10.778  0.40 31.74 ?  100 VAL   B HG13 1 
ATOM   5482 H  HG21 A VAL   B 1 100 ? 37.051 -31.935 7.980   0.60 32.59 ?  100 VAL   B HG21 1 
ATOM   5483 H  HG21 B VAL   B 1 100 ? 37.095 -31.915 7.884   0.40 31.54 ?  100 VAL   B HG21 1 
ATOM   5484 H  HG22 A VAL   B 1 100 ? 36.745 -31.031 9.250   0.60 32.59 ?  100 VAL   B HG22 1 
ATOM   5485 H  HG22 B VAL   B 1 100 ? 36.778 -31.020 9.158   0.40 31.54 ?  100 VAL   B HG22 1 
ATOM   5486 H  HG23 A VAL   B 1 100 ? 37.742 -30.513 8.126   0.60 32.59 ?  100 VAL   B HG23 1 
ATOM   5487 H  HG23 B VAL   B 1 100 ? 37.789 -30.496 8.050   0.40 31.54 ?  100 VAL   B HG23 1 
ATOM   5488 N  N    . ASN   B 1 101 ? 41.520 -31.613 10.828  1.00 24.91 ?  101 ASN   B N    1 
ATOM   5489 C  CA   . ASN   B 1 101 ? 42.557 -32.148 11.709  1.00 26.58 ?  101 ASN   B CA   1 
ATOM   5490 C  C    . ASN   B 1 101 ? 42.741 -31.307 12.969  1.00 28.89 ?  101 ASN   B C    1 
ATOM   5491 O  O    . ASN   B 1 101 ? 43.360 -31.782 13.932  1.00 29.99 ?  101 ASN   B O    1 
ATOM   5492 C  CB   . ASN   B 1 101 ? 43.882 -32.289 10.954  1.00 26.42 ?  101 ASN   B CB   1 
ATOM   5493 C  CG   . ASN   B 1 101 ? 43.869 -33.445 9.968   1.00 25.87 ?  101 ASN   B CG   1 
ATOM   5494 O  OD1  . ASN   B 1 101 ? 43.186 -34.441 10.178  1.00 26.52 ?  101 ASN   B OD1  1 
ATOM   5495 N  ND2  . ASN   B 1 101 ? 44.619 -33.310 8.884   1.00 25.47 ?  101 ASN   B ND2  1 
ATOM   5496 H  H    A ASN   B 1 101 ? 41.793 -31.361 10.052  0.60 29.93 ?  101 ASN   B H    1 
ATOM   5497 H  H    B ASN   B 1 101 ? 41.804 -31.335 10.066  0.40 29.93 ?  101 ASN   B H    1 
ATOM   5498 H  HA   . ASN   B 1 101 ? 42.289 -33.030 11.992  1.00 31.94 ?  101 ASN   B HA   1 
ATOM   5499 H  HB2  . ASN   B 1 101 ? 44.059 -31.476 10.454  1.00 31.74 ?  101 ASN   B HB2  1 
ATOM   5500 H  HB3  . ASN   B 1 101 ? 44.594 -32.446 11.593  1.00 31.74 ?  101 ASN   B HB3  1 
ATOM   5501 H  HD21 . ASN   B 1 101 ? 44.644 -33.942 8.300   1.00 30.61 ?  101 ASN   B HD21 1 
ATOM   5502 H  HD22 . ASN   B 1 101 ? 45.080 -32.596 8.765   1.00 30.61 ?  101 ASN   B HD22 1 
ATOM   5503 N  N    A LYS   B 1 102 ? 42.226 -30.076 12.982  0.60 30.50 ?  102 LYS   B N    1 
ATOM   5504 N  N    B LYS   B 1 102 ? 42.224 -30.077 12.985  0.40 30.60 ?  102 LYS   B N    1 
ATOM   5505 C  CA   A LYS   B 1 102 ? 42.211 -29.232 14.170  0.60 32.50 ?  102 LYS   B CA   1 
ATOM   5506 C  CA   B LYS   B 1 102 ? 42.213 -29.240 14.177  0.40 32.42 ?  102 LYS   B CA   1 
ATOM   5507 C  C    A LYS   B 1 102 ? 40.842 -29.192 14.838  0.60 31.85 ?  102 LYS   B C    1 
ATOM   5508 C  C    B LYS   B 1 102 ? 40.843 -29.195 14.841  0.40 31.89 ?  102 LYS   B C    1 
ATOM   5509 O  O    A LYS   B 1 102 ? 40.639 -28.402 15.764  0.60 32.38 ?  102 LYS   B O    1 
ATOM   5510 O  O    B LYS   B 1 102 ? 40.641 -28.407 15.770  0.40 32.29 ?  102 LYS   B O    1 
ATOM   5511 C  CB   A LYS   B 1 102 ? 42.632 -27.803 13.821  0.60 35.19 ?  102 LYS   B CB   1 
ATOM   5512 C  CB   B LYS   B 1 102 ? 42.662 -27.816 13.841  0.40 34.76 ?  102 LYS   B CB   1 
ATOM   5513 C  CG   A LYS   B 1 102 ? 44.096 -27.615 13.469  0.60 37.70 ?  102 LYS   B CG   1 
ATOM   5514 C  CG   B LYS   B 1 102 ? 44.126 -27.673 13.466  0.40 36.87 ?  102 LYS   B CG   1 
ATOM   5515 C  CD   A LYS   B 1 102 ? 44.353 -26.159 13.108  0.60 40.04 ?  102 LYS   B CD   1 
ATOM   5516 C  CD   B LYS   B 1 102 ? 44.415 -26.253 13.004  0.40 38.79 ?  102 LYS   B CD   1 
ATOM   5517 C  CE   A LYS   B 1 102 ? 45.814 -25.886 12.803  0.60 41.77 ?  102 LYS   B CE   1 
ATOM   5518 C  CE   B LYS   B 1 102 ? 45.900 -26.005 12.810  0.40 40.20 ?  102 LYS   B CE   1 
ATOM   5519 N  NZ   A LYS   B 1 102 ? 46.026 -24.462 12.406  0.60 42.75 ?  102 LYS   B NZ   1 
ATOM   5520 N  NZ   B LYS   B 1 102 ? 46.156 -24.614 12.336  0.40 41.00 ?  102 LYS   B NZ   1 
ATOM   5521 H  H    A LYS   B 1 102 ? 41.866 -29.699 12.295  0.60 36.64 ?  102 LYS   B H    1 
ATOM   5522 H  H    B LYS   B 1 102 ? 41.861 -29.697 12.301  0.40 36.76 ?  102 LYS   B H    1 
ATOM   5523 H  HA   A LYS   B 1 102 ? 42.849 -29.580 14.809  0.60 39.04 ?  102 LYS   B HA   1 
ATOM   5524 H  HA   B LYS   B 1 102 ? 42.844 -29.602 14.817  0.40 38.95 ?  102 LYS   B HA   1 
ATOM   5525 H  HB2  A LYS   B 1 102 ? 42.111 -27.505 13.061  0.60 42.27 ?  102 LYS   B HB2  1 
ATOM   5526 H  HB2  B LYS   B 1 102 ? 42.137 -27.493 13.094  0.40 41.75 ?  102 LYS   B HB2  1 
ATOM   5527 H  HB3  A LYS   B 1 102 ? 42.445 -27.233 14.584  0.60 42.27 ?  102 LYS   B HB3  1 
ATOM   5528 H  HB3  B LYS   B 1 102 ? 42.505 -27.252 14.616  0.40 41.75 ?  102 LYS   B HB3  1 
ATOM   5529 H  HG2  A LYS   B 1 102 ? 44.649 -27.847 14.232  0.60 45.28 ?  102 LYS   B HG2  1 
ATOM   5530 H  HG2  B LYS   B 1 102 ? 44.680 -27.863 14.240  0.40 44.29 ?  102 LYS   B HG2  1 
ATOM   5531 H  HG3  A LYS   B 1 102 ? 44.321 -28.168 12.704  0.60 45.28 ?  102 LYS   B HG3  1 
ATOM   5532 H  HG3  B LYS   B 1 102 ? 44.336 -28.282 12.740  0.40 44.29 ?  102 LYS   B HG3  1 
ATOM   5533 H  HD2  A LYS   B 1 102 ? 43.834 -25.930 12.321  0.60 48.10 ?  102 LYS   B HD2  1 
ATOM   5534 H  HD2  B LYS   B 1 102 ? 43.970 -26.097 12.155  0.40 46.59 ?  102 LYS   B HD2  1 
ATOM   5535 H  HD3  A LYS   B 1 102 ? 44.091 -25.596 13.854  0.60 48.10 ?  102 LYS   B HD3  1 
ATOM   5536 H  HD3  B LYS   B 1 102 ? 44.089 -25.628 13.670  0.40 46.59 ?  102 LYS   B HD3  1 
ATOM   5537 H  HE2  A LYS   B 1 102 ? 46.346 -26.065 13.594  0.60 50.16 ?  102 LYS   B HE2  1 
ATOM   5538 H  HE2  B LYS   B 1 102 ? 46.359 -26.128 13.656  0.40 48.28 ?  102 LYS   B HE2  1 
ATOM   5539 H  HE3  A LYS   B 1 102 ? 46.100 -26.453 12.070  0.60 50.16 ?  102 LYS   B HE3  1 
ATOM   5540 H  HE3  B LYS   B 1 102 ? 46.245 -26.622 12.146  0.40 48.28 ?  102 LYS   B HE3  1 
ATOM   5541 H  HZ1  A LYS   B 1 102 ? 46.887 -24.320 12.231  0.60 51.35 ?  102 LYS   B HZ1  1 
ATOM   5542 H  HZ1  B LYS   B 1 102 ? 47.029 -24.485 12.228  0.40 49.25 ?  102 LYS   B HZ1  1 
ATOM   5543 H  HZ2  A LYS   B 1 102 ? 45.548 -24.275 11.679  0.60 51.35 ?  102 LYS   B HZ2  1 
ATOM   5544 H  HZ2  B LYS   B 1 102 ? 45.744 -24.478 11.558  0.40 49.25 ?  102 LYS   B HZ2  1 
ATOM   5545 H  HZ3  A LYS   B 1 102 ? 45.772 -23.921 13.066  0.60 51.35 ?  102 LYS   B HZ3  1 
ATOM   5546 H  HZ3  B LYS   B 1 102 ? 45.848 -24.029 12.932  0.40 49.25 ?  102 LYS   B HZ3  1 
ATOM   5547 N  N    . GLY   B 1 103 ? 39.895 -30.006 14.377  1.00 31.21 ?  103 GLY   B N    1 
ATOM   5548 C  CA   . GLY   B 1 103 ? 38.573 -30.045 14.967  1.00 30.49 ?  103 GLY   B CA   1 
ATOM   5549 C  C    . GLY   B 1 103 ? 37.619 -28.971 14.498  1.00 29.33 ?  103 GLY   B C    1 
ATOM   5550 O  O    . GLY   B 1 103 ? 36.535 -28.834 15.078  1.00 29.90 ?  103 GLY   B O    1 
ATOM   5551 H  H    A GLY   B 1 103 ? 39.998 -30.546 13.718  0.60 37.50 ?  103 GLY   B H    1 
ATOM   5552 H  H    B GLY   B 1 103 ? 39.998 -30.545 13.717  0.40 37.50 ?  103 GLY   B H    1 
ATOM   5553 H  HA2  . GLY   B 1 103 ? 38.168 -30.902 14.771  1.00 36.63 ?  103 GLY   B HA2  1 
ATOM   5554 H  HA3  . GLY   B 1 103 ? 38.657 -29.967 15.931  1.00 36.63 ?  103 GLY   B HA3  1 
ATOM   5555 N  N    A GLU   B 1 104 ? 37.989 -28.198 13.481  0.60 28.32 ?  104 GLU   B N    1 
ATOM   5556 N  N    B GLU   B 1 104 ? 37.968 -28.219 13.459  0.40 28.57 ?  104 GLU   B N    1 
ATOM   5557 C  CA   A GLU   B 1 104 ? 37.152 -27.098 13.027  0.60 27.17 ?  104 GLU   B CA   1 
ATOM   5558 C  CA   B GLU   B 1 104 ? 37.107 -27.144 12.989  0.40 27.61 ?  104 GLU   B CA   1 
ATOM   5559 C  C    A GLU   B 1 104 ? 35.972 -27.619 12.212  0.60 27.63 ?  104 GLU   B C    1 
ATOM   5560 C  C    B GLU   B 1 104 ? 35.950 -27.694 12.158  0.40 27.70 ?  104 GLU   B C    1 
ATOM   5561 O  O    A GLU   B 1 104 ? 36.021 -28.703 11.622  0.60 28.59 ?  104 GLU   B O    1 
ATOM   5562 O  O    B GLU   B 1 104 ? 36.039 -28.769 11.558  0.40 28.22 ?  104 GLU   B O    1 
ATOM   5563 C  CB   A GLU   B 1 104 ? 37.987 -26.094 12.227  0.60 26.17 ?  104 GLU   B CB   1 
ATOM   5564 C  CB   B GLU   B 1 104 ? 37.925 -26.124 12.196  0.40 26.79 ?  104 GLU   B CB   1 
ATOM   5565 C  CG   A GLU   B 1 104 ? 39.098 -25.468 13.063  0.60 24.99 ?  104 GLU   B CG   1 
ATOM   5566 C  CG   B GLU   B 1 104 ? 39.011 -25.480 13.048  0.40 25.93 ?  104 GLU   B CG   1 
ATOM   5567 C  CD   A GLU   B 1 104 ? 40.033 -24.580 12.271  0.60 23.87 ?  104 GLU   B CD   1 
ATOM   5568 C  CD   B GLU   B 1 104 ? 39.979 -24.628 12.255  0.40 25.20 ?  104 GLU   B CD   1 
ATOM   5569 O  OE1  A GLU   B 1 104 ? 40.029 -24.638 11.023  0.60 22.18 ?  104 GLU   B OE1  1 
ATOM   5570 O  OE1  B GLU   B 1 104 ? 39.926 -24.647 11.007  0.40 24.49 ?  104 GLU   B OE1  1 
ATOM   5571 O  OE2  A GLU   B 1 104 ? 40.782 -23.817 12.914  0.60 24.03 -1 104 GLU   B OE2  1 
ATOM   5572 O  OE2  B GLU   B 1 104 ? 40.800 -23.937 12.892  0.40 25.09 -1 104 GLU   B OE2  1 
ATOM   5573 H  H    A GLU   B 1 104 ? 38.725 -28.286 13.042  0.60 34.02 ?  104 GLU   B H    1 
ATOM   5574 H  H    B GLU   B 1 104 ? 38.701 -28.305 13.016  0.40 34.33 ?  104 GLU   B H    1 
ATOM   5575 H  HA   A GLU   B 1 104 ? 36.801 -26.632 13.802  0.60 32.65 ?  104 GLU   B HA   1 
ATOM   5576 H  HA   B GLU   B 1 104 ? 36.731 -26.686 13.756  0.40 33.17 ?  104 GLU   B HA   1 
ATOM   5577 H  HB2  A GLU   B 1 104 ? 38.398 -26.545 11.475  0.60 31.45 ?  104 GLU   B HB2  1 
ATOM   5578 H  HB2  B GLU   B 1 104 ? 38.352 -26.567 11.447  0.40 32.20 ?  104 GLU   B HB2  1 
ATOM   5579 H  HB3  A GLU   B 1 104 ? 37.412 -25.377 11.915  0.60 31.45 ?  104 GLU   B HB3  1 
ATOM   5580 H  HB3  B GLU   B 1 104 ? 37.337 -25.421 11.877  0.40 32.20 ?  104 GLU   B HB3  1 
ATOM   5581 H  HG2  A GLU   B 1 104 ? 38.704 -24.920 13.760  0.60 30.03 ?  104 GLU   B HG2  1 
ATOM   5582 H  HG2  B GLU   B 1 104 ? 38.593 -24.910 13.713  0.40 31.16 ?  104 GLU   B HG2  1 
ATOM   5583 H  HG3  A GLU   B 1 104 ? 39.634 -26.170 13.462  0.60 30.03 ?  104 GLU   B HG3  1 
ATOM   5584 H  HG3  B GLU   B 1 104 ? 39.522 -26.177 13.489  0.40 31.16 ?  104 GLU   B HG3  1 
ATOM   5585 N  N    A ASP   B 1 105 ? 34.899 -26.830 12.195  0.60 27.13 ?  105 ASP   B N    1 
ATOM   5586 N  N    B ASP   B 1 105 ? 34.854 -26.937 12.136  0.40 27.13 ?  105 ASP   B N    1 
ATOM   5587 C  CA   A ASP   B 1 105 ? 33.622 -27.281 11.653  0.60 27.70 ?  105 ASP   B CA   1 
ATOM   5588 C  CA   B ASP   B 1 105 ? 33.595 -27.416 11.576  0.40 27.06 ?  105 ASP   B CA   1 
ATOM   5589 C  C    A ASP   B 1 105 ? 33.674 -27.331 10.130  0.60 25.73 ?  105 ASP   B C    1 
ATOM   5590 C  C    B ASP   B 1 105 ? 33.660 -27.422 10.053  0.40 25.95 ?  105 ASP   B C    1 
ATOM   5591 O  O    A ASP   B 1 105 ? 33.826 -26.298 9.472   0.60 25.00 ?  105 ASP   B O    1 
ATOM   5592 O  O    B ASP   B 1 105 ? 33.839 -26.373 9.425   0.40 25.44 ?  105 ASP   B O    1 
ATOM   5593 C  CB   A ASP   B 1 105 ? 32.514 -26.335 12.111  0.60 30.80 ?  105 ASP   B CB   1 
ATOM   5594 C  CB   B ASP   B 1 105 ? 32.447 -26.529 12.058  0.40 28.29 ?  105 ASP   B CB   1 
ATOM   5595 C  CG   A ASP   B 1 105 ? 31.136 -26.791 11.674  0.60 33.48 ?  105 ASP   B CG   1 
ATOM   5596 C  CG   B ASP   B 1 105 ? 31.084 -27.123 11.751  0.40 29.35 ?  105 ASP   B CG   1 
ATOM   5597 O  OD1  A ASP   B 1 105 ? 31.017 -27.905 11.122  0.60 33.90 ?  105 ASP   B OD1  1 
ATOM   5598 O  OD1  B ASP   B 1 105 ? 31.014 -28.091 10.964  0.40 29.58 ?  105 ASP   B OD1  1 
ATOM   5599 O  OD2  A ASP   B 1 105 ? 30.168 -26.027 11.878  0.60 34.89 -1 105 ASP   B OD2  1 
ATOM   5600 O  OD2  B ASP   B 1 105 ? 30.079 -26.629 12.308  0.40 29.54 -1 105 ASP   B OD2  1 
ATOM   5601 H  H    A ASP   B 1 105 ? 34.891 -26.025 12.493  0.60 32.60 ?  105 ASP   B H    1 
ATOM   5602 H  H    B ASP   B 1 105 ? 34.816 -26.137 12.437  0.40 32.60 ?  105 ASP   B H    1 
ATOM   5603 H  HA   A ASP   B 1 105 ? 33.426 -28.171 11.983  0.60 33.29 ?  105 ASP   B HA   1 
ATOM   5604 H  HA   B ASP   B 1 105 ? 33.424 -28.320 11.879  0.40 32.52 ?  105 ASP   B HA   1 
ATOM   5605 H  HB2  A ASP   B 1 105 ? 32.534 -26.269 13.081  0.60 37.01 ?  105 ASP   B HB2  1 
ATOM   5606 H  HB2  B ASP   B 1 105 ? 32.512 -26.416 13.021  0.40 34.00 ?  105 ASP   B HB2  1 
ATOM   5607 H  HB3  A ASP   B 1 105 ? 32.659 -25.461 11.718  0.60 37.01 ?  105 ASP   B HB3  1 
ATOM   5608 H  HB3  B ASP   B 1 105 ? 32.509 -25.660 11.622  0.40 34.00 ?  105 ASP   B HB3  1 
ATOM   5609 N  N    A ILE   B 1 106 ? 33.511 -28.535 9.574   0.60 25.20 ?  106 ILE   B N    1 
ATOM   5610 N  N    B ILE   B 1 106 ? 33.493 -28.609 9.461   0.40 25.51 ?  106 ILE   B N    1 
ATOM   5611 C  CA   A ILE   B 1 106 ? 33.510 -28.719 8.127   0.60 24.21 ?  106 ILE   B CA   1 
ATOM   5612 C  CA   B ILE   B 1 106 ? 33.500 -28.754 8.011   0.40 25.10 ?  106 ILE   B CA   1 
ATOM   5613 C  C    A ILE   B 1 106 ? 32.412 -27.905 7.451   0.60 23.15 ?  106 ILE   B C    1 
ATOM   5614 C  C    B ILE   B 1 106 ? 32.401 -27.928 7.354   0.40 24.47 ?  106 ILE   B C    1 
ATOM   5615 O  O    A ILE   B 1 106 ? 32.517 -27.594 6.261   0.60 22.36 ?  106 ILE   B O    1 
ATOM   5616 O  O    B ILE   B 1 106 ? 32.485 -27.624 6.160   0.40 24.15 ?  106 ILE   B O    1 
ATOM   5617 C  CB   A ILE   B 1 106 ? 33.406 -30.226 7.797   0.60 24.88 ?  106 ILE   B CB   1 
ATOM   5618 C  CB   B ILE   B 1 106 ? 33.401 -30.253 7.643   0.40 25.52 ?  106 ILE   B CB   1 
ATOM   5619 C  CG1  A ILE   B 1 106 ? 33.647 -30.480 6.309   0.60 25.11 ?  106 ILE   B CG1  1 
ATOM   5620 C  CG1  B ILE   B 1 106 ? 33.661 -30.474 6.151   0.40 25.68 ?  106 ILE   B CG1  1 
ATOM   5621 C  CG2  A ILE   B 1 106 ? 32.049 -30.779 8.220   0.60 25.30 ?  106 ILE   B CG2  1 
ATOM   5622 C  CG2  B ILE   B 1 106 ? 32.039 -30.813 8.032   0.40 25.87 ?  106 ILE   B CG2  1 
ATOM   5623 C  CD1  A ILE   B 1 106 ? 35.006 -30.028 5.832   0.60 25.16 ?  106 ILE   B CD1  1 
ATOM   5624 C  CD1  B ILE   B 1 106 ? 35.023 -30.006 5.698   0.40 25.75 ?  106 ILE   B CD1  1 
ATOM   5625 H  H    A ILE   B 1 106 ? 33.400 -29.259 10.020  0.60 30.29 ?  106 ILE   B H    1 
ATOM   5626 H  H    B ILE   B 1 106 ? 33.379 -29.345 9.885   0.40 30.65 ?  106 ILE   B H    1 
ATOM   5627 H  HA   A ILE   B 1 106 ? 34.357 -28.401 7.786   0.60 29.09 ?  106 ILE   B HA   1 
ATOM   5628 H  HA   B ILE   B 1 106 ? 34.344 -28.422 7.677   0.40 30.16 ?  106 ILE   B HA   1 
ATOM   5629 H  HB   A ILE   B 1 106 ? 34.090 -30.695 8.299   0.60 29.90 ?  106 ILE   B HB   1 
ATOM   5630 H  HB   B ILE   B 1 106 ? 34.078 -30.734 8.143   0.40 30.67 ?  106 ILE   B HB   1 
ATOM   5631 H  HG12 A ILE   B 1 106 ? 33.581 -31.435 6.140   0.60 30.18 ?  106 ILE   B HG12 1 
ATOM   5632 H  HG12 B ILE   B 1 106 ? 33.599 -31.425 5.962   0.40 30.86 ?  106 ILE   B HG12 1 
ATOM   5633 H  HG13 A ILE   B 1 106 ? 32.978 -30.009 5.793   0.60 30.18 ?  106 ILE   B HG13 1 
ATOM   5634 H  HG13 B ILE   B 1 106 ? 32.994 -29.995 5.639   0.40 30.86 ?  106 ILE   B HG13 1 
ATOM   5635 H  HG21 A ILE   B 1 106 ? 32.059 -31.744 8.128   0.60 30.41 ?  106 ILE   B HG21 1 
ATOM   5636 H  HG21 B ILE   B 1 106 ? 32.055 -31.778 7.934   0.40 31.09 ?  106 ILE   B HG21 1 
ATOM   5637 H  HG22 A ILE   B 1 106 ? 31.885 -30.538 9.146   0.60 30.41 ?  106 ILE   B HG22 1 
ATOM   5638 H  HG22 B ILE   B 1 106 ? 31.853 -30.578 8.955   0.40 31.09 ?  106 ILE   B HG22 1 
ATOM   5639 H  HG23 A ILE   B 1 106 ? 31.360 -30.400 7.653   0.60 30.41 ?  106 ILE   B HG23 1 
ATOM   5640 H  HG23 B ILE   B 1 106 ? 31.361 -30.434 7.451   0.40 31.09 ?  106 ILE   B HG23 1 
ATOM   5641 H  HD11 A ILE   B 1 106 ? 35.188 -30.432 4.970   0.60 30.24 ?  106 ILE   B HD11 1 
ATOM   5642 H  HD11 B ILE   B 1 106 ? 35.215 -30.394 4.831   0.40 30.94 ?  106 ILE   B HD11 1 
ATOM   5643 H  HD12 A ILE   B 1 106 ? 35.007 -29.061 5.749   0.60 30.24 ?  106 ILE   B HD12 1 
ATOM   5644 H  HD12 B ILE   B 1 106 ? 35.019 -29.038 5.634   0.40 30.94 ?  106 ILE   B HD12 1 
ATOM   5645 H  HD13 A ILE   B 1 106 ? 35.677 -30.306 6.475   0.60 30.24 ?  106 ILE   B HD13 1 
ATOM   5646 H  HD13 B ILE   B 1 106 ? 35.687 -30.295 6.344   0.40 30.94 ?  106 ILE   B HD13 1 
ATOM   5647 N  N    A GLN   B 1 107 ? 31.358 -27.540 8.183   0.60 23.82 ?  107 GLN   B N    1 
ATOM   5648 N  N    B GLN   B 1 107 ? 31.367 -27.551 8.110   0.40 24.70 ?  107 GLN   B N    1 
ATOM   5649 C  CA   A GLN   B 1 107 ? 30.287 -26.738 7.600   0.60 24.38 ?  107 GLN   B CA   1 
ATOM   5650 C  CA   B GLN   B 1 107 ? 30.290 -26.741 7.553   0.40 24.91 ?  107 GLN   B CA   1 
ATOM   5651 C  C    A GLN   B 1 107 ? 30.781 -25.390 7.088   0.60 22.33 ?  107 GLN   B C    1 
ATOM   5652 C  C    B GLN   B 1 107 ? 30.772 -25.369 7.093   0.40 22.69 ?  107 GLN   B C    1 
ATOM   5653 O  O    A GLN   B 1 107 ? 30.141 -24.807 6.210   0.60 23.02 ?  107 GLN   B O    1 
ATOM   5654 O  O    B GLN   B 1 107 ? 30.106 -24.744 6.262   0.40 23.17 ?  107 GLN   B O    1 
ATOM   5655 C  CB   A GLN   B 1 107 ? 29.174 -26.529 8.630   0.60 28.10 ?  107 GLN   B CB   1 
ATOM   5656 C  CB   B GLN   B 1 107 ? 29.168 -26.590 8.584   0.40 27.78 ?  107 GLN   B CB   1 
ATOM   5657 C  CG   A GLN   B 1 107 ? 27.854 -26.015 8.057   0.60 31.73 ?  107 GLN   B CG   1 
ATOM   5658 C  CG   B GLN   B 1 107 ? 27.857 -26.041 8.029   0.40 30.54 ?  107 GLN   B CG   1 
ATOM   5659 C  CD   A GLN   B 1 107 ? 27.798 -24.500 7.956   0.60 34.56 ?  107 GLN   B CD   1 
ATOM   5660 C  CD   B GLN   B 1 107 ? 27.776 -24.526 8.092   0.40 32.73 ?  107 GLN   B CD   1 
ATOM   5661 O  OE1  A GLN   B 1 107 ? 28.634 -23.794 8.523   0.60 35.62 ?  107 GLN   B OE1  1 
ATOM   5662 O  OE1  B GLN   B 1 107 ? 28.627 -23.870 8.695   0.40 33.49 ?  107 GLN   B OE1  1 
ATOM   5663 N  NE2  A GLN   B 1 107 ? 26.803 -23.991 7.231   0.60 35.47 ?  107 GLN   B NE2  1 
ATOM   5664 N  NE2  B GLN   B 1 107 ? 26.744 -23.963 7.471   0.40 33.49 ?  107 GLN   B NE2  1 
ATOM   5665 H  H    A GLN   B 1 107 ? 31.245 -27.733 9.005   0.60 28.63 ?  107 GLN   B H    1 
ATOM   5666 H  H    B GLN   B 1 107 ? 31.265 -27.750 8.937   0.40 29.69 ?  107 GLN   B H    1 
ATOM   5667 H  HA   A GLN   B 1 107 ? 29.910 -27.218 6.845   0.60 29.30 ?  107 GLN   B HA   1 
ATOM   5668 H  HA   B GLN   B 1 107 ? 29.920 -27.200 6.781   0.40 29.93 ?  107 GLN   B HA   1 
ATOM   5669 H  HB2  A GLN   B 1 107 ? 28.995 -27.376 9.058   0.60 33.76 ?  107 GLN   B HB2  1 
ATOM   5670 H  HB2  B GLN   B 1 107 ? 28.980 -27.460 8.961   0.40 33.37 ?  107 GLN   B HB2  1 
ATOM   5671 H  HB3  A GLN   B 1 107 ? 29.480 -25.887 9.289   0.60 33.76 ?  107 GLN   B HB3  1 
ATOM   5672 H  HB3  B GLN   B 1 107 ? 29.468 -25.990 9.285   0.40 33.37 ?  107 GLN   B HB3  1 
ATOM   5673 H  HG2  A GLN   B 1 107 ? 27.731 -26.376 7.166   0.60 38.12 ?  107 GLN   B HG2  1 
ATOM   5674 H  HG2  B GLN   B 1 107 ? 27.769 -26.305 7.100   0.40 36.69 ?  107 GLN   B HG2  1 
ATOM   5675 H  HG3  A GLN   B 1 107 ? 27.127 -26.306 8.634   0.60 38.12 ?  107 GLN   B HG3  1 
ATOM   5676 H  HG3  B GLN   B 1 107 ? 27.118 -26.405 8.547   0.40 36.69 ?  107 GLN   B HG3  1 
ATOM   5677 H  HE21 A GLN   B 1 107 ? 26.237 -24.514 6.847   0.60 42.61 ?  107 GLN   B HE21 1 
ATOM   5678 H  HE21 B GLN   B 1 107 ? 26.168 -24.453 7.059   0.40 40.23 ?  107 GLN   B HE21 1 
ATOM   5679 H  HE22 A GLN   B 1 107 ? 26.723 -23.138 7.146   0.60 42.61 ?  107 GLN   B HE22 1 
ATOM   5680 H  HE22 B GLN   B 1 107 ? 26.650 -23.108 7.481   0.40 40.23 ?  107 GLN   B HE22 1 
ATOM   5681 N  N    . LEU   B 1 108 ? 31.911 -24.890 7.599   1.00 20.57 ?  108 LEU   B N    1 
ATOM   5682 C  CA   . LEU   B 1 108 ? 32.447 -23.588 7.194   1.00 18.01 ?  108 LEU   B CA   1 
ATOM   5683 C  C    . LEU   B 1 108 ? 33.096 -23.604 5.819   1.00 15.47 ?  108 LEU   B C    1 
ATOM   5684 O  O    . LEU   B 1 108 ? 33.520 -22.543 5.333   1.00 14.80 ?  108 LEU   B O    1 
ATOM   5685 C  CB   . LEU   B 1 108 ? 33.449 -23.088 8.233   1.00 18.56 ?  108 LEU   B CB   1 
ATOM   5686 C  CG   . LEU   B 1 108 ? 32.826 -22.600 9.539   1.00 19.95 ?  108 LEU   B CG   1 
ATOM   5687 C  CD1  . LEU   B 1 108 ? 33.843 -22.611 10.664  1.00 20.01 ?  108 LEU   B CD1  1 
ATOM   5688 C  CD2  . LEU   B 1 108 ? 32.268 -21.199 9.347   1.00 20.91 ?  108 LEU   B CD2  1 
ATOM   5689 H  H    A LEU   B 1 108 ? 32.382 -25.291 8.193   0.60 24.73 ?  108 LEU   B H    1 
ATOM   5690 H  H    B LEU   B 1 108 ? 32.385 -25.299 8.185   0.40 24.73 ?  108 LEU   B H    1 
ATOM   5691 H  HA   . LEU   B 1 108 ? 31.714 -22.954 7.163   1.00 21.65 ?  108 LEU   B HA   1 
ATOM   5692 H  HB2  . LEU   B 1 108 ? 34.052 -23.813 8.453   1.00 22.32 ?  108 LEU   B HB2  1 
ATOM   5693 H  HB3  . LEU   B 1 108 ? 33.945 -22.350 7.853   1.00 22.32 ?  108 LEU   B HB3  1 
ATOM   5694 H  HG   . LEU   B 1 108 ? 32.091 -23.186 9.788   1.00 23.98 ?  108 LEU   B HG   1 
ATOM   5695 H  HD11 . LEU   B 1 108 ? 33.410 -22.321 11.484  1.00 24.05 ?  108 LEU   B HD11 1 
ATOM   5696 H  HD12 . LEU   B 1 108 ? 34.186 -23.510 10.771  1.00 24.05 ?  108 LEU   B HD12 1 
ATOM   5697 H  HD13 . LEU   B 1 108 ? 34.565 -22.002 10.441  1.00 24.05 ?  108 LEU   B HD13 1 
ATOM   5698 H  HD21 . LEU   B 1 108 ? 31.886 -20.891 10.185  1.00 25.14 ?  108 LEU   B HD21 1 
ATOM   5699 H  HD22 . LEU   B 1 108 ? 32.987 -20.608 9.075   1.00 25.14 ?  108 LEU   B HD22 1 
ATOM   5700 H  HD23 . LEU   B 1 108 ? 31.581 -21.222 8.661   1.00 25.14 ?  108 LEU   B HD23 1 
ATOM   5701 N  N    . LEU   B 1 109 ? 33.158 -24.771 5.183   1.00 14.39 ?  109 LEU   B N    1 
ATOM   5702 C  CA   . LEU   B 1 109 ? 33.785 -24.884 3.875   1.00 13.60 ?  109 LEU   B CA   1 
ATOM   5703 C  C    . LEU   B 1 109 ? 33.019 -24.099 2.818   1.00 13.02 ?  109 LEU   B C    1 
ATOM   5704 O  O    . LEU   B 1 109 ? 33.634 -23.503 1.924   1.00 12.45 ?  109 LEU   B O    1 
ATOM   5705 C  CB   . LEU   B 1 109 ? 33.890 -26.361 3.498   1.00 13.65 ?  109 LEU   B CB   1 
ATOM   5706 C  CG   . LEU   B 1 109 ? 34.676 -26.699 2.237   1.00 13.56 ?  109 LEU   B CG   1 
ATOM   5707 C  CD1  . LEU   B 1 109 ? 36.054 -26.051 2.256   1.00 13.24 ?  109 LEU   B CD1  1 
ATOM   5708 C  CD2  . LEU   B 1 109 ? 34.799 -28.208 2.087   1.00 14.13 ?  109 LEU   B CD2  1 
ATOM   5709 H  H    . LEU   B 1 109 ? 32.847 -25.509 5.485   1.00 17.31 ?  109 LEU   B H    1 
ATOM   5710 H  HA   . LEU   B 1 109 ? 34.681 -24.522 3.921   1.00 16.36 ?  109 LEU   B HA   1 
ATOM   5711 H  HB2  . LEU   B 1 109 ? 34.318 -26.831 4.232   1.00 16.43 ?  109 LEU   B HB2  1 
ATOM   5712 H  HB3  . LEU   B 1 109 ? 32.995 -26.712 3.374   1.00 16.43 ?  109 LEU   B HB3  1 
ATOM   5713 H  HG   . LEU   B 1 109 ? 34.200 -26.369 1.460   1.00 16.32 ?  109 LEU   B HG   1 
ATOM   5714 H  HD11 . LEU   B 1 109 ? 36.592 -26.424 1.537   1.00 15.94 ?  109 LEU   B HD11 1 
ATOM   5715 H  HD12 . LEU   B 1 109 ? 35.952 -25.096 2.127   1.00 15.94 ?  109 LEU   B HD12 1 
ATOM   5716 H  HD13 . LEU   B 1 109 ? 36.476 -26.231 3.109   1.00 15.94 ?  109 LEU   B HD13 1 
ATOM   5717 H  HD21 . LEU   B 1 109 ? 35.367 -28.411 1.323   1.00 17.00 ?  109 LEU   B HD21 1 
ATOM   5718 H  HD22 . LEU   B 1 109 ? 35.190 -28.579 2.893   1.00 17.00 ?  109 LEU   B HD22 1 
ATOM   5719 H  HD23 . LEU   B 1 109 ? 33.915 -28.587 1.945   1.00 17.00 ?  109 LEU   B HD23 1 
ATOM   5720 N  N    . LYS   B 1 110 ? 31.685 -24.067 2.901   1.00 12.71 ?  110 LYS   B N    1 
ATOM   5721 C  CA   . LYS   B 1 110 ? 30.926 -23.305 1.914   1.00 12.24 ?  110 LYS   B CA   1 
ATOM   5722 C  C    . LYS   B 1 110 ? 31.269 -21.817 1.998   1.00 11.99 ?  110 LYS   B C    1 
ATOM   5723 O  O    . LYS   B 1 110 ? 31.527 -21.168 0.978   1.00 11.97 ?  110 LYS   B O    1 
ATOM   5724 C  CB   . LYS   B 1 110 ? 29.419 -23.557 2.060   1.00 13.03 ?  110 LYS   B CB   1 
ATOM   5725 C  CG   . LYS   B 1 110 ? 28.611 -22.922 0.930   1.00 13.29 ?  110 LYS   B CG   1 
ATOM   5726 C  CD   . LYS   B 1 110 ? 27.151 -23.352 0.943   1.00 13.60 ?  110 LYS   B CD   1 
ATOM   5727 C  CE   . LYS   B 1 110 ? 26.387 -22.824 -0.278  1.00 14.48 ?  110 LYS   B CE   1 
ATOM   5728 N  NZ   . LYS   B 1 110 ? 26.724 -23.545 -1.539  1.00 14.56 ?  110 LYS   B NZ   1 
ATOM   5729 H  H    . LYS   B 1 110 ? 31.215 -24.470 3.495   1.00 15.29 ?  110 LYS   B H    1 
ATOM   5730 H  HA   . LYS   B 1 110 ? 31.185 -23.607 1.028   1.00 14.74 ?  110 LYS   B HA   1 
ATOM   5731 H  HB2  . LYS   B 1 110 ? 29.258 -24.516 2.043   1.00 15.67 ?  110 LYS   B HB2  1 
ATOM   5732 H  HB3  . LYS   B 1 110 ? 29.114 -23.184 2.898   1.00 15.67 ?  110 LYS   B HB3  1 
ATOM   5733 H  HG2  . LYS   B 1 110 ? 28.634 -21.959 1.022   1.00 16.00 ?  110 LYS   B HG2  1 
ATOM   5734 H  HG3  . LYS   B 1 110 ? 28.987 -23.187 0.077   1.00 16.00 ?  110 LYS   B HG3  1 
ATOM   5735 H  HD2  . LYS   B 1 110 ? 27.098 -24.326 0.937   1.00 16.36 ?  110 LYS   B HD2  1 
ATOM   5736 H  HD3  . LYS   B 1 110 ? 26.717 -23.007 1.744   1.00 16.36 ?  110 LYS   B HD3  1 
ATOM   5737 H  HE2  . LYS   B 1 110 ? 25.437 -22.921 -0.126  1.00 17.42 ?  110 LYS   B HE2  1 
ATOM   5738 H  HE3  . LYS   B 1 110 ? 26.612 -21.889 -0.401  1.00 17.42 ?  110 LYS   B HE3  1 
ATOM   5739 H  HZ1  . LYS   B 1 110 ? 26.266 -23.201 -2.217  1.00 17.51 ?  110 LYS   B HZ1  1 
ATOM   5740 H  HZ2  . LYS   B 1 110 ? 27.597 -23.466 -1.710  1.00 17.51 ?  110 LYS   B HZ2  1 
ATOM   5741 H  HZ3  . LYS   B 1 110 ? 26.525 -24.408 -1.458  1.00 17.51 ?  110 LYS   B HZ3  1 
ATOM   5742 N  N    . SER   B 1 111 ? 31.288 -21.259 3.217   1.00 12.58 ?  111 SER   B N    1 
ATOM   5743 C  CA   . SER   B 1 111 ? 31.681 -19.860 3.388   1.00 12.35 ?  111 SER   B CA   1 
ATOM   5744 C  C    . SER   B 1 111 ? 33.060 -19.604 2.798   1.00 11.67 ?  111 SER   B C    1 
ATOM   5745 O  O    . SER   B 1 111 ? 33.286 -18.572 2.149   1.00 12.15 ?  111 SER   B O    1 
ATOM   5746 C  CB   . SER   B 1 111 ? 31.672 -19.492 4.869   1.00 13.52 ?  111 SER   B CB   1 
ATOM   5747 O  OG   . SER   B 1 111 ? 30.363 -19.499 5.390   1.00 15.03 ?  111 SER   B OG   1 
ATOM   5748 H  H    . SER   B 1 111 ? 31.085 -21.671 3.945   1.00 15.13 ?  111 SER   B H    1 
ATOM   5749 H  HA   . SER   B 1 111 ? 31.048 -19.295 2.927   1.00 14.86 ?  111 SER   B HA   1 
ATOM   5750 H  HB2  . SER   B 1 111 ? 32.206 -20.136 5.360   1.00 16.27 ?  111 SER   B HB2  1 
ATOM   5751 H  HB3  . SER   B 1 111 ? 32.037 -18.605 4.976   1.00 16.27 ?  111 SER   B HB3  1 
ATOM   5752 H  HG   . SER   B 1 111 ? 30.370 -19.301 6.213   1.00 18.07 ?  111 SER   B HG   1 
ATOM   5753 N  N    . ALA   B 1 112 ? 34.001 -20.522 3.026   1.00 11.77 ?  112 ALA   B N    1 
ATOM   5754 C  CA   . ALA   B 1 112 ? 35.346 -20.355 2.484   1.00 11.58 ?  112 ALA   B CA   1 
ATOM   5755 C  C    . ALA   B 1 112 ? 35.312 -20.260 0.962   1.00 10.88 ?  112 ALA   B C    1 
ATOM   5756 O  O    . ALA   B 1 112 ? 35.936 -19.370 0.371   1.00 11.24 ?  112 ALA   B O    1 
ATOM   5757 C  CB   . ALA   B 1 112 ? 36.250 -21.498 2.958   1.00 12.25 ?  112 ALA   B CB   1 
ATOM   5758 H  H    . ALA   B 1 112 ? 33.888 -21.247 3.485   1.00 14.17 ?  112 ALA   B H    1 
ATOM   5759 H  HA   . ALA   B 1 112 ? 35.715 -19.527 2.825   1.00 13.94 ?  112 ALA   B HA   1 
ATOM   5760 H  HB1  . ALA   B 1 112 ? 37.142 -21.363 2.596   1.00 14.74 ?  112 ALA   B HB1  1 
ATOM   5761 H  HB2  . ALA   B 1 112 ? 36.289 -21.486 3.930   1.00 14.74 ?  112 ALA   B HB2  1 
ATOM   5762 H  HB3  . ALA   B 1 112 ? 35.889 -22.339 2.651   1.00 14.74 ?  112 ALA   B HB3  1 
ATOM   5763 N  N    . TYR   B 1 113 ? 34.581 -21.165 0.304   1.00 11.07 ?  113 TYR   B N    1 
ATOM   5764 C  CA   . TYR   B 1 113 ? 34.502 -21.115 -1.152  1.00 10.74 ?  113 TYR   B CA   1 
ATOM   5765 C  C    . TYR   B 1 113 ? 33.795 -19.865 -1.669  1.00 10.47 ?  113 TYR   B C    1 
ATOM   5766 O  O    . TYR   B 1 113 ? 34.069 -19.434 -2.794  1.00 10.45 ?  113 TYR   B O    1 
ATOM   5767 C  CB   . TYR   B 1 113 ? 33.832 -22.376 -1.695  1.00 11.05 ?  113 TYR   B CB   1 
ATOM   5768 C  CG   . TYR   B 1 113 ? 34.797 -23.521 -1.957  1.00 11.28 ?  113 TYR   B CG   1 
ATOM   5769 C  CD1  . TYR   B 1 113 ? 35.794 -23.421 -2.924  1.00 11.73 ?  113 TYR   B CD1  1 
ATOM   5770 C  CD2  . TYR   B 1 113 ? 34.696 -24.714 -1.257  1.00 11.51 ?  113 TYR   B CD2  1 
ATOM   5771 C  CE1  . TYR   B 1 113 ? 36.666 -24.456 -3.173  1.00 11.83 ?  113 TYR   B CE1  1 
ATOM   5772 C  CE2  . TYR   B 1 113 ? 35.567 -25.768 -1.502  1.00 11.69 ?  113 TYR   B CE2  1 
ATOM   5773 C  CZ   . TYR   B 1 113 ? 36.543 -25.636 -2.467  1.00 11.97 ?  113 TYR   B CZ   1 
ATOM   5774 O  OH   . TYR   B 1 113 ? 37.424 -26.652 -2.739  1.00 12.66 ?  113 TYR   B OH   1 
ATOM   5775 H  H    . TYR   B 1 113 ? 34.127 -21.797 0.676   1.00 13.33 ?  113 TYR   B H    1 
ATOM   5776 H  HA   . TYR   B 1 113 ? 35.403 -21.097 -1.493  1.00 12.93 ?  113 TYR   B HA   1 
ATOM   5777 H  HB2  . TYR   B 1 113 ? 33.174 -22.691 -1.051  1.00 13.30 ?  113 TYR   B HB2  1 
ATOM   5778 H  HB3  . TYR   B 1 113 ? 33.391 -22.162 -2.531  1.00 13.30 ?  113 TYR   B HB3  1 
ATOM   5779 H  HD1  . TYR   B 1 113 ? 35.880 -22.626 -3.407  1.00 14.12 ?  113 TYR   B HD1  1 
ATOM   5780 H  HD2  . TYR   B 1 113 ? 34.026 -24.812 -0.619  1.00 13.85 ?  113 TYR   B HD2  1 
ATOM   5781 H  HE1  . TYR   B 1 113 ? 37.327 -24.362 -3.831  1.00 14.24 ?  113 TYR   B HE1  1 
ATOM   5782 H  HE2  . TYR   B 1 113 ? 35.475 -26.567 -1.035  1.00 14.07 ?  113 TYR   B HE2  1 
ATOM   5783 H  HH   . TYR   B 1 113 ? 37.244 -27.323 -2.266  1.00 15.24 ?  113 TYR   B HH   1 
ATOM   5784 N  N    . GLU   B 1 114 ? 32.867 -19.287 -0.897  1.00 10.76 ?  114 GLU   B N    1 
ATOM   5785 C  CA   . GLU   B 1 114 ? 32.185 -18.076 -1.353  1.00 10.53 ?  114 GLU   B CA   1 
ATOM   5786 C  C    . GLU   B 1 114 ? 33.173 -16.955 -1.650  1.00 10.42 ?  114 GLU   B C    1 
ATOM   5787 O  O    . GLU   B 1 114 ? 32.901 -16.098 -2.493  1.00 10.61 ?  114 GLU   B O    1 
ATOM   5788 C  CB   . GLU   B 1 114 ? 31.124 -17.651 -0.329  1.00 11.09 ?  114 GLU   B CB   1 
ATOM   5789 C  CG   . GLU   B 1 114 ? 29.911 -18.568 -0.391  1.00 11.13 ?  114 GLU   B CG   1 
ATOM   5790 C  CD   . GLU   B 1 114 ? 28.891 -18.379 0.718   1.00 11.42 ?  114 GLU   B CD   1 
ATOM   5791 O  OE1  . GLU   B 1 114 ? 29.180 -17.761 1.764   1.00 11.54 ?  114 GLU   B OE1  1 
ATOM   5792 O  OE2  . GLU   B 1 114 ? 27.772 -18.919 0.552   1.00 12.50 -1 114 GLU   B OE2  1 
ATOM   5793 H  H    . GLU   B 1 114 ? 32.612 -19.580 -0.125  1.00 12.95 ?  114 GLU   B H    1 
ATOM   5794 H  HA   . GLU   B 1 114 ? 31.726 -18.277 -2.176  1.00 12.68 ?  114 GLU   B HA   1 
ATOM   5795 H  HB2  . GLU   B 1 114 ? 31.502 -17.701 0.567   1.00 13.35 ?  114 GLU   B HB2  1 
ATOM   5796 H  HB3  . GLU   B 1 114 ? 30.838 -16.747 -0.522  1.00 13.35 ?  114 GLU   B HB3  1 
ATOM   5797 H  HG2  . GLU   B 1 114 ? 29.461 -18.416 -1.234  1.00 13.39 ?  114 GLU   B HG2  1 
ATOM   5798 H  HG3  . GLU   B 1 114 ? 30.223 -19.487 -0.350  1.00 13.39 ?  114 GLU   B HG3  1 
ATOM   5799 N  N    . ASN   B 1 115 ? 34.339 -16.954 -0.997  1.00 10.49 ?  115 ASN   B N    1 
ATOM   5800 C  CA   . ASN   B 1 115 ? 35.333 -15.921 -1.293  1.00 10.11 ?  115 ASN   B CA   1 
ATOM   5801 C  C    . ASN   B 1 115 ? 35.748 -15.943 -2.758  1.00 10.13 ?  115 ASN   B C    1 
ATOM   5802 O  O    . ASN   B 1 115 ? 36.127 -14.902 -3.312  1.00 10.72 ?  115 ASN   B O    1 
ATOM   5803 C  CB   . ASN   B 1 115 ? 36.572 -16.090 -0.405  1.00 10.84 ?  115 ASN   B CB   1 
ATOM   5804 C  CG   . ASN   B 1 115 ? 36.302 -15.828 1.055   1.00 11.07 ?  115 ASN   B CG   1 
ATOM   5805 O  OD1  . ASN   B 1 115 ? 36.295 -14.684 1.496   1.00 13.31 ?  115 ASN   B OD1  1 
ATOM   5806 N  ND2  . ASN   B 1 115 ? 36.143 -16.895 1.834   1.00 11.23 ?  115 ASN   B ND2  1 
ATOM   5807 H  H    . ASN   B 1 115 ? 34.579 -17.523 -0.390  1.00 12.63 ?  115 ASN   B H    1 
ATOM   5808 H  HA   . ASN   B 1 115 ? 34.951 -15.051 -1.106  1.00 12.17 ?  115 ASN   B HA   1 
ATOM   5809 H  HB2  . ASN   B 1 115 ? 36.902 -16.996 -0.494  1.00 13.05 ?  115 ASN   B HB2  1 
ATOM   5810 H  HB3  . ASN   B 1 115 ? 37.252 -15.460 -0.695  1.00 13.05 ?  115 ASN   B HB3  1 
ATOM   5811 H  HD21 . ASN   B 1 115 ? 36.000 -16.796 2.677   1.00 13.52 ?  115 ASN   B HD21 1 
ATOM   5812 H  HD22 . ASN   B 1 115 ? 36.171 -17.686 1.495   1.00 13.52 ?  115 ASN   B HD22 1 
ATOM   5813 N  N    . PHE   B 1 116 ? 35.715 -17.118 -3.398  1.00 9.95  ?  116 PHE   B N    1 
ATOM   5814 C  CA   . PHE   B 1 116 ? 36.146 -17.215 -4.789  1.00 10.38 ?  116 PHE   B CA   1 
ATOM   5815 C  C    . PHE   B 1 116 ? 35.245 -16.393 -5.705  1.00 9.82  ?  116 PHE   B C    1 
ATOM   5816 O  O    . PHE   B 1 116 ? 35.679 -15.962 -6.778  1.00 10.52 ?  116 PHE   B O    1 
ATOM   5817 C  CB   . PHE   B 1 116 ? 36.104 -18.664 -5.301  1.00 10.21 ?  116 PHE   B CB   1 
ATOM   5818 C  CG   . PHE   B 1 116 ? 37.178 -19.617 -4.757  1.00 10.16 ?  116 PHE   B CG   1 
ATOM   5819 C  CD1  . PHE   B 1 116 ? 37.828 -19.434 -3.546  1.00 10.98 ?  116 PHE   B CD1  1 
ATOM   5820 C  CD2  . PHE   B 1 116 ? 37.482 -20.749 -5.492  1.00 10.44 ?  116 PHE   B CD2  1 
ATOM   5821 C  CE1  . PHE   B 1 116 ? 38.761 -20.369 -3.091  1.00 10.83 ?  116 PHE   B CE1  1 
ATOM   5822 C  CE2  . PHE   B 1 116 ? 38.413 -21.681 -5.046  1.00 10.42 ?  116 PHE   B CE2  1 
ATOM   5823 C  CZ   . PHE   B 1 116 ? 39.046 -21.493 -3.848  1.00 10.50 ?  116 PHE   B CZ   1 
ATOM   5824 H  H    . PHE   B 1 116 ? 35.452 -17.866 -3.054  1.00 11.99 ?  116 PHE   B H    1 
ATOM   5825 H  HA   . PHE   B 1 116 ? 37.056 -16.889 -4.873  1.00 12.50 ?  116 PHE   B HA   1 
ATOM   5826 H  HB2  . PHE   B 1 116 ? 35.234 -19.040 -5.068  1.00 12.30 ?  116 PHE   B HB2  1 
ATOM   5827 H  HB3  . PHE   B 1 116 ? 36.189 -18.649 -6.268  1.00 12.30 ?  116 PHE   B HB3  1 
ATOM   5828 H  HD1  . PHE   B 1 116 ? 37.623 -18.687 -3.025  1.00 13.22 ?  116 PHE   B HD1  1 
ATOM   5829 H  HD2  . PHE   B 1 116 ? 37.048 -20.897 -6.301  1.00 12.57 ?  116 PHE   B HD2  1 
ATOM   5830 H  HE1  . PHE   B 1 116 ? 39.196 -20.231 -2.279  1.00 13.03 ?  116 PHE   B HE1  1 
ATOM   5831 H  HE2  . PHE   B 1 116 ? 38.608 -22.428 -5.561  1.00 12.55 ?  116 PHE   B HE2  1 
ATOM   5832 H  HZ   . PHE   B 1 116 ? 39.684 -22.101 -3.553  1.00 12.64 ?  116 PHE   B HZ   1 
ATOM   5833 N  N    . ASN   B 1 117 ? 33.981 -16.182 -5.317  1.00 10.34 ?  117 ASN   B N    1 
ATOM   5834 C  CA   . ASN   B 1 117 ? 33.035 -15.486 -6.186  1.00 10.40 ?  117 ASN   B CA   1 
ATOM   5835 C  C    . ASN   B 1 117 ? 33.343 -14.007 -6.329  1.00 10.91 ?  117 ASN   B C    1 
ATOM   5836 O  O    . ASN   B 1 117 ? 32.748 -13.354 -7.187  1.00 11.81 ?  117 ASN   B O    1 
ATOM   5837 C  CB   . ASN   B 1 117 ? 31.611 -15.699 -5.693  1.00 10.90 ?  117 ASN   B CB   1 
ATOM   5838 C  CG   . ASN   B 1 117 ? 31.154 -17.112 -5.931  1.00 11.31 ?  117 ASN   B CG   1 
ATOM   5839 O  OD1  . ASN   B 1 117 ? 31.500 -17.709 -6.950  1.00 12.02 ?  117 ASN   B OD1  1 
ATOM   5840 N  ND2  . ASN   B 1 117 ? 30.415 -17.677 -4.987  1.00 11.20 ?  117 ASN   B ND2  1 
ATOM   5841 H  H    . ASN   B 1 117 ? 33.659 -16.428 -4.553  1.00 12.46 ?  117 ASN   B H    1 
ATOM   5842 H  HA   . ASN   B 1 117 ? 33.099 -15.882 -7.063  1.00 12.52 ?  117 ASN   B HA   1 
ATOM   5843 H  HB2  . ASN   B 1 117 ? 31.572 -15.518 -4.737  1.00 13.13 ?  117 ASN   B HB2  1 
ATOM   5844 H  HB3  . ASN   B 1 117 ? 31.020 -15.094 -6.168  1.00 13.13 ?  117 ASN   B HB3  1 
ATOM   5845 H  HD21 . ASN   B 1 117 ? 30.131 -18.481 -5.085  1.00 13.48 ?  117 ASN   B HD21 1 
ATOM   5846 H  HD22 . ASN   B 1 117 ? 30.196 -17.227 -4.285  1.00 13.48 ?  117 ASN   B HD22 1 
ATOM   5847 N  N    . GLN   B 1 118 ? 34.276 -13.478 -5.544  1.00 10.60 ?  118 GLN   B N    1 
ATOM   5848 C  CA   . GLN   B 1 118 ? 34.711 -12.093 -5.685  1.00 11.25 ?  118 GLN   B CA   1 
ATOM   5849 C  C    . GLN   B 1 118 ? 35.774 -11.905 -6.763  1.00 11.17 ?  118 GLN   B C    1 
ATOM   5850 O  O    . GLN   B 1 118 ? 36.245 -10.776 -6.950  1.00 12.72 ?  118 GLN   B O    1 
ATOM   5851 C  CB   . GLN   B 1 118 ? 35.194 -11.559 -4.332  1.00 11.86 ?  118 GLN   B CB   1 
ATOM   5852 C  CG   . GLN   B 1 118 ? 34.106 -11.597 -3.269  1.00 12.01 ?  118 GLN   B CG   1 
ATOM   5853 C  CD   . GLN   B 1 118 ? 32.931 -10.689 -3.608  1.00 11.85 ?  118 GLN   B CD   1 
ATOM   5854 O  OE1  . GLN   B 1 118 ? 33.121 -9.551  -4.044  1.00 12.63 ?  118 GLN   B OE1  1 
ATOM   5855 N  NE2  . GLN   B 1 118 ? 31.715 -11.180 -3.412  1.00 12.04 ?  118 GLN   B NE2  1 
ATOM   5856 H  H    . GLN   B 1 118 ? 34.695 -13.902 -4.919  1.00 12.76 ?  118 GLN   B H    1 
ATOM   5857 H  HA   . GLN   B 1 118 ? 33.945 -11.561 -5.950  1.00 13.54 ?  118 GLN   B HA   1 
ATOM   5858 H  HB2  . GLN   B 1 118 ? 35.936 -12.095 -4.021  1.00 14.27 ?  118 GLN   B HB2  1 
ATOM   5859 H  HB3  . GLN   B 1 118 ? 35.475 -10.632 -4.436  1.00 14.27 ?  118 GLN   B HB3  1 
ATOM   5860 H  HG2  . GLN   B 1 118 ? 33.770 -12.502 -3.187  1.00 14.45 ?  118 GLN   B HG2  1 
ATOM   5861 H  HG3  . GLN   B 1 118 ? 34.478 -11.303 -2.420  1.00 14.45 ?  118 GLN   B HG3  1 
ATOM   5862 H  HE21 . GLN   B 1 118 ? 31.621 -11.976 -3.104  1.00 14.49 ?  118 GLN   B HE21 1 
ATOM   5863 H  HE22 . GLN   B 1 118 ? 31.028 -10.699 -3.591  1.00 14.49 ?  118 GLN   B HE22 1 
ATOM   5864 N  N    . HIS   B 1 119 ? 36.129 -12.964 -7.495  1.00 10.75 ?  119 HIS   B N    1 
ATOM   5865 C  CA   . HIS   B 1 119 ? 37.168 -12.918 -8.516  1.00 11.08 ?  119 HIS   B CA   1 
ATOM   5866 C  C    . HIS   B 1 119 ? 36.692 -13.649 -9.757  1.00 11.13 ?  119 HIS   B C    1 
ATOM   5867 O  O    . HIS   B 1 119 ? 36.183 -14.765 -9.659  1.00 11.84 ?  119 HIS   B O    1 
ATOM   5868 C  CB   . HIS   B 1 119 ? 38.450 -13.545 -7.970  1.00 11.66 ?  119 HIS   B CB   1 
ATOM   5869 C  CG   . HIS   B 1 119 ? 38.933 -12.844 -6.748  1.00 12.76 ?  119 HIS   B CG   1 
ATOM   5870 N  ND1  . HIS   B 1 119 ? 39.737 -11.726 -6.809  1.00 14.64 ?  119 HIS   B ND1  1 
ATOM   5871 C  CD2  . HIS   B 1 119 ? 38.645 -13.036 -5.441  1.00 13.80 ?  119 HIS   B CD2  1 
ATOM   5872 C  CE1  . HIS   B 1 119 ? 39.952 -11.283 -5.585  1.00 15.81 ?  119 HIS   B CE1  1 
ATOM   5873 N  NE2  . HIS   B 1 119 ? 39.292 -12.052 -4.737  1.00 15.36 ?  119 HIS   B NE2  1 
ATOM   5874 H  H    . HIS   B 1 119 ? 35.765 -13.744 -7.417  1.00 12.94 ?  119 HIS   B H    1 
ATOM   5875 H  HA   . HIS   B 1 119 ? 37.348 -11.994 -8.752  1.00 13.34 ?  119 HIS   B HA   1 
ATOM   5876 H  HB2  . HIS   B 1 119 ? 38.281 -14.471 -7.747  1.00 14.04 ?  119 HIS   B HB2  1 
ATOM   5877 H  HB3  . HIS   B 1 119 ? 39.143 -13.485 -8.649  1.00 14.04 ?  119 HIS   B HB3  1 
ATOM   5878 H  HD2  . HIS   B 1 119 ? 38.107 -13.710 -5.088  1.00 16.60 ?  119 HIS   B HD2  1 
ATOM   5879 H  HE1  . HIS   B 1 119 ? 40.485 -10.557 -5.355  1.00 19.02 ?  119 HIS   B HE1  1 
ATOM   5880 H  HE2  . HIS   B 1 119 ? 39.297 -11.973 -3.880  1.00 18.48 ?  119 HIS   B HE2  1 
ATOM   5881 N  N    . GLU   B 1 120 ? 36.844 -13.028 -10.926 1.00 11.75 ?  120 GLU   B N    1 
ATOM   5882 C  CA   . GLU   B 1 120 ? 36.251 -13.614 -12.126 1.00 13.14 ?  120 GLU   B CA   1 
ATOM   5883 C  C    . GLU   B 1 120 ? 36.926 -14.917 -12.543 1.00 12.33 ?  120 GLU   B C    1 
ATOM   5884 O  O    . GLU   B 1 120 ? 36.263 -15.794 -13.111 1.00 12.46 ?  120 GLU   B O    1 
ATOM   5885 C  CB   . GLU   B 1 120 ? 36.257 -12.610 -13.274 1.00 17.27 ?  120 GLU   B CB   1 
ATOM   5886 C  CG   . GLU   B 1 120 ? 35.264 -11.481 -13.076 1.00 23.39 ?  120 GLU   B CG   1 
ATOM   5887 C  CD   . GLU   B 1 120 ? 35.126 -10.584 -14.290 1.00 29.31 ?  120 GLU   B CD   1 
ATOM   5888 O  OE1  . GLU   B 1 120 ? 36.131 -10.386 -15.005 1.00 32.05 ?  120 GLU   B OE1  1 
ATOM   5889 O  OE2  . GLU   B 1 120 ? 34.009 -10.077 -14.525 1.00 32.50 -1 120 GLU   B OE2  1 
ATOM   5890 H  H    . GLU   B 1 120 ? 37.264 -12.287 -11.050 1.00 14.15 ?  120 GLU   B H    1 
ATOM   5891 H  HA   . GLU   B 1 120 ? 35.326 -13.822 -11.933 1.00 15.81 ?  120 GLU   B HA   1 
ATOM   5892 H  HB2  . GLU   B 1 120 ? 37.139 -12.220 -13.351 1.00 20.77 ?  120 GLU   B HB2  1 
ATOM   5893 H  HB3  . GLU   B 1 120 ? 36.023 -13.070 -14.097 1.00 20.77 ?  120 GLU   B HB3  1 
ATOM   5894 H  HG2  . GLU   B 1 120 ? 34.387 -11.856 -12.896 1.00 28.11 ?  120 GLU   B HG2  1 
ATOM   5895 H  HG3  . GLU   B 1 120 ? 35.550 -10.933 -12.331 1.00 28.11 ?  120 GLU   B HG3  1 
ATOM   5896 N  N    . VAL   B 1 121 ? 38.225 -15.060 -12.284 1.00 11.81 ?  121 VAL   B N    1 
ATOM   5897 C  CA   . VAL   B 1 121 ? 38.971 -16.270 -12.625 1.00 11.41 ?  121 VAL   B CA   1 
ATOM   5898 C  C    . VAL   B 1 121 ? 40.085 -16.472 -11.604 1.00 10.89 ?  121 VAL   B C    1 
ATOM   5899 O  O    . VAL   B 1 121 ? 40.761 -15.514 -11.215 1.00 11.67 ?  121 VAL   B O    1 
ATOM   5900 C  CB   . VAL   B 1 121 ? 39.491 -16.225 -14.081 1.00 13.32 ?  121 VAL   B CB   1 
ATOM   5901 C  CG1  . VAL   B 1 121 ? 40.356 -14.996 -14.337 1.00 14.79 ?  121 VAL   B CG1  1 
ATOM   5902 C  CG2  . VAL   B 1 121 ? 40.232 -17.507 -14.431 1.00 14.38 ?  121 VAL   B CG2  1 
ATOM   5903 H  H    . VAL   B 1 121 ? 38.708 -14.457 -11.907 1.00 14.22 ?  121 VAL   B H    1 
ATOM   5904 H  HA   . VAL   B 1 121 ? 38.368 -17.025 -12.557 1.00 13.74 ?  121 VAL   B HA   1 
ATOM   5905 H  HB   . VAL   B 1 121 ? 38.722 -16.166 -14.676 1.00 16.03 ?  121 VAL   B HB   1 
ATOM   5906 H  HG11 . VAL   B 1 121 ? 40.663 -15.011 -15.256 1.00 17.79 ?  121 VAL   B HG11 1 
ATOM   5907 H  HG12 . VAL   B 1 121 ? 39.824 -14.198 -14.180 1.00 17.79 ?  121 VAL   B HG12 1 
ATOM   5908 H  HG13 . VAL   B 1 121 ? 41.113 -15.012 -13.733 1.00 17.79 ?  121 VAL   B HG13 1 
ATOM   5909 H  HG21 . VAL   B 1 121 ? 40.431 -17.507 -15.382 1.00 17.30 ?  121 VAL   B HG21 1 
ATOM   5910 H  HG22 . VAL   B 1 121 ? 41.056 -17.546 -13.923 1.00 17.30 ?  121 VAL   B HG22 1 
ATOM   5911 H  HG23 . VAL   B 1 121 ? 39.670 -18.268 -14.214 1.00 17.30 ?  121 VAL   B HG23 1 
ATOM   5912 N  N    . LEU   B 1 122 ? 40.276 -17.726 -11.173 1.00 10.56 ?  122 LEU   B N    1 
ATOM   5913 C  CA   . LEU   B 1 122 ? 41.262 -18.075 -10.151 1.00 10.18 ?  122 LEU   B CA   1 
ATOM   5914 C  C    . LEU   B 1 122 ? 41.914 -19.408 -10.477 1.00 10.21 ?  122 LEU   B C    1 
ATOM   5915 O  O    . LEU   B 1 122 ? 41.251 -20.331 -10.966 1.00 11.35 ?  122 LEU   B O    1 
ATOM   5916 C  CB   . LEU   B 1 122 ? 40.611 -18.305 -8.772  1.00 12.13 ?  122 LEU   B CB   1 
ATOM   5917 C  CG   . LEU   B 1 122 ? 39.574 -17.287 -8.284  1.00 11.96 ?  122 LEU   B CG   1 
ATOM   5918 C  CD1  . LEU   B 1 122 ? 38.177 -17.646 -8.754  1.00 12.77 ?  122 LEU   B CD1  1 
ATOM   5919 C  CD2  . LEU   B 1 122 ? 39.624 -17.174 -6.773  1.00 11.35 ?  122 LEU   B CD2  1 
ATOM   5920 H  H    . LEU   B 1 122 ? 39.837 -18.407 -11.464 1.00 12.71 ?  122 LEU   B H    1 
ATOM   5921 H  HA   . LEU   B 1 122 ? 41.942 -17.385 -10.077 1.00 12.26 ?  122 LEU   B HA   1 
ATOM   5922 H  HB2  . LEU   B 1 122 ? 40.172 -19.169 -8.791  1.00 14.60 ?  122 LEU   B HB2  1 
ATOM   5923 H  HB3  . LEU   B 1 122 ? 41.317 -18.324 -8.107  1.00 14.60 ?  122 LEU   B HB3  1 
ATOM   5924 H  HG   . LEU   B 1 122 ? 39.793 -16.420 -8.651  1.00 14.39 ?  122 LEU   B HG   1 
ATOM   5925 H  HD11 . LEU   B 1 122 ? 37.549 -17.001 -8.389  1.00 15.36 ?  122 LEU   B HD11 1 
ATOM   5926 H  HD12 . LEU   B 1 122 ? 38.153 -17.612 -9.725  1.00 15.36 ?  122 LEU   B HD12 1 
ATOM   5927 H  HD13 . LEU   B 1 122 ? 37.956 -18.536 -8.447  1.00 15.36 ?  122 LEU   B HD13 1 
ATOM   5928 H  HD21 . LEU   B 1 122 ? 38.940 -16.553 -6.477  1.00 13.66 ?  122 LEU   B HD21 1 
ATOM   5929 H  HD22 . LEU   B 1 122 ? 39.468 -18.049 -6.381  1.00 13.66 ?  122 LEU   B HD22 1 
ATOM   5930 H  HD23 . LEU   B 1 122 ? 40.501 -16.848 -6.509  1.00 13.66 ?  122 LEU   B HD23 1 
ATOM   5931 N  N    . LEU   B 1 123 ? 43.201 -19.517 -10.123 1.00 10.13 ?  123 LEU   B N    1 
ATOM   5932 C  CA   . LEU   B 1 123 ? 43.915 -20.786 -9.996  1.00 10.20 ?  123 LEU   B CA   1 
ATOM   5933 C  C    . LEU   B 1 123 ? 43.883 -21.180 -8.523  1.00 10.07 ?  123 LEU   B C    1 
ATOM   5934 O  O    . LEU   B 1 123 ? 44.234 -20.352 -7.671  1.00 10.36 ?  123 LEU   B O    1 
ATOM   5935 C  CB   . LEU   B 1 123 ? 45.365 -20.601 -10.455 1.00 10.59 ?  123 LEU   B CB   1 
ATOM   5936 C  CG   . LEU   B 1 123 ? 46.311 -21.785 -10.218 1.00 10.89 ?  123 LEU   B CG   1 
ATOM   5937 C  CD1  . LEU   B 1 123 ? 45.889 -23.029 -10.994 1.00 11.73 ?  123 LEU   B CD1  1 
ATOM   5938 C  CD2  . LEU   B 1 123 ? 47.724 -21.390 -10.597 1.00 11.83 ?  123 LEU   B CD2  1 
ATOM   5939 H  H    . LEU   B 1 123 ? 43.701 -18.838 -9.934  1.00 12.20 ?  123 LEU   B H    1 
ATOM   5940 H  HA   . LEU   B 1 123 ? 43.483 -21.475 -10.527 1.00 12.28 ?  123 LEU   B HA   1 
ATOM   5941 H  HB2  . LEU   B 1 123 ? 45.359 -20.423 -11.409 1.00 12.75 ?  123 LEU   B HB2  1 
ATOM   5942 H  HB3  . LEU   B 1 123 ? 45.736 -19.838 -9.988  1.00 12.75 ?  123 LEU   B HB3  1 
ATOM   5943 H  HG   . LEU   B 1 123 ? 46.313 -22.009 -9.276  1.00 13.11 ?  123 LEU   B HG   1 
ATOM   5944 H  HD11 . LEU   B 1 123 ? 46.527 -23.737 -10.823 1.00 14.12 ?  123 LEU   B HD11 1 
ATOM   5945 H  HD12 . LEU   B 1 123 ? 45.006 -23.298 -10.694 1.00 14.12 ?  123 LEU   B HD12 1 
ATOM   5946 H  HD13 . LEU   B 1 123 ? 45.868 -22.818 -11.939 1.00 14.12 ?  123 LEU   B HD13 1 
ATOM   5947 H  HD21 . LEU   B 1 123 ? 48.316 -22.143 -10.447 1.00 14.24 ?  123 LEU   B HD21 1 
ATOM   5948 H  HD22 . LEU   B 1 123 ? 47.742 -21.138 -11.536 1.00 14.24 ?  123 LEU   B HD22 1 
ATOM   5949 H  HD23 . LEU   B 1 123 ? 47.999 -20.638 -10.050 1.00 14.24 ?  123 LEU   B HD23 1 
ATOM   5950 N  N    . ALA   B 1 124 ? 43.450 -22.409 -8.209  1.00 9.88  ?  124 ALA   B N    1 
ATOM   5951 C  CA   . ALA   B 1 124 ? 43.196 -22.720 -6.810  1.00 10.04 ?  124 ALA   B CA   1 
ATOM   5952 C  C    . ALA   B 1 124 ? 43.473 -24.178 -6.485  1.00 9.80  ?  124 ALA   B C    1 
ATOM   5953 O  O    . ALA   B 1 124 ? 43.332 -25.056 -7.348  1.00 10.46 ?  124 ALA   B O    1 
ATOM   5954 C  CB   . ALA   B 1 124 ? 41.745 -22.407 -6.437  1.00 10.34 ?  124 ALA   B CB   1 
ATOM   5955 H  H    . ALA   B 1 124 ? 43.282 -23.047 -8.770  1.00 11.90 ?  124 ALA   B H    1 
ATOM   5956 H  HA   . ALA   B 1 124 ? 43.776 -22.169 -6.270  1.00 12.09 ?  124 ALA   B HA   1 
ATOM   5957 H  HB1  . ALA   B 1 124 ? 41.605 -22.622 -5.504  1.00 12.45 ?  124 ALA   B HB1  1 
ATOM   5958 H  HB2  . ALA   B 1 124 ? 41.583 -21.460 -6.588  1.00 12.45 ?  124 ALA   B HB2  1 
ATOM   5959 H  HB3  . ALA   B 1 124 ? 41.154 -22.935 -6.995  1.00 12.45 ?  124 ALA   B HB3  1 
ATOM   5960 N  N    . PRO   B 1 125 ? 43.769 -24.472 -5.221  1.00 10.17 ?  125 PRO   B N    1 
ATOM   5961 C  CA   . PRO   B 1 125 ? 43.702 -25.836 -4.700  1.00 10.89 ?  125 PRO   B CA   1 
ATOM   5962 C  C    . PRO   B 1 125 ? 42.302 -26.113 -4.154  1.00 10.83 ?  125 PRO   B C    1 
ATOM   5963 O  O    . PRO   B 1 125 ? 41.505 -25.199 -3.941  1.00 11.32 ?  125 PRO   B O    1 
ATOM   5964 C  CB   . PRO   B 1 125 ? 44.693 -25.764 -3.535  1.00 11.67 ?  125 PRO   B CB   1 
ATOM   5965 C  CG   . PRO   B 1 125 ? 44.439 -24.381 -2.954  1.00 11.62 ?  125 PRO   B CG   1 
ATOM   5966 C  CD   . PRO   B 1 125 ? 44.085 -23.502 -4.153  1.00 10.69 ?  125 PRO   B CD   1 
ATOM   5967 H  HA   . PRO   B 1 125 ? 43.972 -26.503 -5.349  1.00 13.10 ?  125 PRO   B HA   1 
ATOM   5968 H  HB2  . PRO   B 1 125 ? 44.497 -26.457 -2.878  1.00 14.05 ?  125 PRO   B HB2  1 
ATOM   5969 H  HB3  . PRO   B 1 125 ? 45.603 -25.845 -3.860  1.00 14.05 ?  125 PRO   B HB3  1 
ATOM   5970 H  HG2  . PRO   B 1 125 ? 43.699 -24.414 -2.326  1.00 13.99 ?  125 PRO   B HG2  1 
ATOM   5971 H  HG3  . PRO   B 1 125 ? 45.242 -24.054 -2.511  1.00 13.99 ?  125 PRO   B HG3  1 
ATOM   5972 H  HD2  . PRO   B 1 125 ? 43.318 -22.947 -3.951  1.00 12.87 ?  125 PRO   B HD2  1 
ATOM   5973 H  HD3  . PRO   B 1 125 ? 44.856 -22.960 -4.406  1.00 12.87 ?  125 PRO   B HD3  1 
ATOM   5974 N  N    . LEU   B 1 126 ? 42.033 -27.391 -3.880  1.00 11.32 ?  126 LEU   B N    1 
ATOM   5975 C  CA   . LEU   B 1 126 ? 40.817 -27.758 -3.159  1.00 11.98 ?  126 LEU   B CA   1 
ATOM   5976 C  C    . LEU   B 1 126 ? 40.934 -27.356 -1.695  1.00 12.24 ?  126 LEU   B C    1 
ATOM   5977 O  O    . LEU   B 1 126 ? 41.819 -27.822 -0.972  1.00 13.66 ?  126 LEU   B O    1 
ATOM   5978 C  CB   . LEU   B 1 126 ? 40.553 -29.254 -3.275  1.00 13.42 ?  126 LEU   B CB   1 
ATOM   5979 C  CG   . LEU   B 1 126 ? 40.022 -29.746 -4.624  1.00 14.14 ?  126 LEU   B CG   1 
ATOM   5980 C  CD1  . LEU   B 1 126 ? 40.063 -31.259 -4.696  1.00 15.91 ?  126 LEU   B CD1  1 
ATOM   5981 C  CD2  . LEU   B 1 126 ? 38.610 -29.254 -4.883  1.00 14.20 ?  126 LEU   B CD2  1 
ATOM   5982 H  H    . LEU   B 1 126 ? 42.535 -28.058 -4.091  1.00 13.62 ?  126 LEU   B H    1 
ATOM   5983 H  HA   . LEU   B 1 126 ? 40.064 -27.283 -3.547  1.00 14.41 ?  126 LEU   B HA   1 
ATOM   5984 H  HB2  . LEU   B 1 126 ? 41.383 -29.721 -3.105  1.00 16.14 ?  126 LEU   B HB2  1 
ATOM   5985 H  HB3  . LEU   B 1 126 ? 39.899 -29.498 -2.605  1.00 16.14 ?  126 LEU   B HB3  1 
ATOM   5986 H  HG   . LEU   B 1 126 ? 40.592 -29.402 -5.332  1.00 17.01 ?  126 LEU   B HG   1 
ATOM   5987 H  HD11 . LEU   B 1 126 ? 39.722 -31.546 -5.559  1.00 19.13 ?  126 LEU   B HD11 1 
ATOM   5988 H  HD12 . LEU   B 1 126 ? 40.976 -31.561 -4.585  1.00 19.13 ?  126 LEU   B HD12 1 
ATOM   5989 H  HD13 . LEU   B 1 126 ? 39.505 -31.624 -3.987  1.00 19.13 ?  126 LEU   B HD13 1 
ATOM   5990 H  HD21 . LEU   B 1 126 ? 38.279 -29.661 -5.700  1.00 17.09 ?  126 LEU   B HD21 1 
ATOM   5991 H  HD22 . LEU   B 1 126 ? 38.048 -29.504 -4.136  1.00 17.09 ?  126 LEU   B HD22 1 
ATOM   5992 H  HD23 . LEU   B 1 126 ? 38.625 -28.288 -4.980  1.00 17.09 ?  126 LEU   B HD23 1 
ATOM   5993 N  N    . LEU   B 1 127 ? 40.005 -26.522 -1.244  1.00 11.96 ?  127 LEU   B N    1 
ATOM   5994 C  CA   . LEU   B 1 127 ? 40.051 -26.033 0.122   1.00 12.30 ?  127 LEU   B CA   1 
ATOM   5995 C  C    . LEU   B 1 127 ? 39.783 -27.157 1.115   1.00 11.98 ?  127 LEU   B C    1 
ATOM   5996 O  O    . LEU   B 1 127 ? 38.958 -28.051 0.885   1.00 12.49 ?  127 LEU   B O    1 
ATOM   5997 C  CB   . LEU   B 1 127 ? 39.031 -24.911 0.328   1.00 12.73 ?  127 LEU   B CB   1 
ATOM   5998 C  CG   . LEU   B 1 127 ? 39.211 -23.640 -0.504  1.00 13.28 ?  127 LEU   B CG   1 
ATOM   5999 C  CD1  . LEU   B 1 127 ? 38.095 -22.661 -0.183  1.00 13.64 ?  127 LEU   B CD1  1 
ATOM   6000 C  CD2  . LEU   B 1 127 ? 40.575 -22.997 -0.265  1.00 14.10 ?  127 LEU   B CD2  1 
ATOM   6001 H  H    . LEU   B 1 127 ? 39.337 -26.224 -1.709  1.00 14.40 ?  127 LEU   B H    1 
ATOM   6002 H  HA   . LEU   B 1 127 ? 40.936 -25.671 0.296   1.00 14.80 ?  127 LEU   B HA   1 
ATOM   6003 H  HB2  . LEU   B 1 127 ? 38.151 -25.258 0.124   1.00 15.32 ?  127 LEU   B HB2  1 
ATOM   6004 H  HB3  . LEU   B 1 127 ? 39.061 -24.641 1.259   1.00 15.32 ?  127 LEU   B HB3  1 
ATOM   6005 H  HG   . LEU   B 1 127 ? 39.139 -23.858 -1.445  1.00 15.97 ?  127 LEU   B HG   1 
ATOM   6006 H  HD11 . LEU   B 1 127 ? 38.222 -21.848 -0.706  1.00 16.41 ?  127 LEU   B HD11 1 
ATOM   6007 H  HD12 . LEU   B 1 127 ? 37.242 -23.061 -0.400  1.00 16.41 ?  127 LEU   B HD12 1 
ATOM   6008 H  HD13 . LEU   B 1 127 ? 38.128 -22.442 0.765   1.00 16.41 ?  127 LEU   B HD13 1 
ATOM   6009 H  HD21 . LEU   B 1 127 ? 40.616 -22.145 -0.728  1.00 16.96 ?  127 LEU   B HD21 1 
ATOM   6010 H  HD22 . LEU   B 1 127 ? 40.701 -22.860 0.688   1.00 16.96 ?  127 LEU   B HD22 1 
ATOM   6011 H  HD23 . LEU   B 1 127 ? 41.265 -23.590 -0.606  1.00 16.96 ?  127 LEU   B HD23 1 
ATOM   6012 N  N    . SER   B 1 128 ? 40.470 -27.075 2.245   1.00 11.93 ?  128 SER   B N    1 
ATOM   6013 C  CA   . SER   B 1 128 ? 40.355 -27.989 3.369   1.00 12.59 ?  128 SER   B CA   1 
ATOM   6014 C  C    . SER   B 1 128 ? 40.852 -29.395 3.049   1.00 13.68 ?  128 SER   B C    1 
ATOM   6015 O  O    . SER   B 1 128 ? 40.762 -30.275 3.902   1.00 14.88 ?  128 SER   B O    1 
ATOM   6016 C  CB   . SER   B 1 128 ? 38.954 -27.994 4.004   1.00 12.97 ?  128 SER   B CB   1 
ATOM   6017 O  OG   . SER   B 1 128 ? 38.642 -26.715 4.550   1.00 13.70 ?  128 SER   B OG   1 
ATOM   6018 H  H    . SER   B 1 128 ? 41.045 -26.449 2.391   1.00 14.36 ?  128 SER   B H    1 
ATOM   6019 H  HA   . SER   B 1 128 ? 40.944 -27.655 4.054   1.00 15.15 ?  128 SER   B HA   1 
ATOM   6020 H  HB2  . SER   B 1 128 ? 38.295 -28.233 3.332   1.00 15.61 ?  128 SER   B HB2  1 
ATOM   6021 H  HB3  . SER   B 1 128 ? 38.938 -28.666 4.721   1.00 15.61 ?  128 SER   B HB3  1 
ATOM   6022 H  HG   . SER   B 1 128 ? 39.211 -26.519 5.136   1.00 16.49 ?  128 SER   B HG   1 
ATOM   6023 N  N    . ALA   B 1 129 ? 41.433 -29.617 1.866   1.00 14.83 ?  129 ALA   B N    1 
ATOM   6024 C  CA   . ALA   B 1 129 ? 41.971 -30.919 1.507   1.00 15.42 ?  129 ALA   B CA   1 
ATOM   6025 C  C    . ALA   B 1 129 ? 43.365 -31.099 2.099   1.00 14.45 ?  129 ALA   B C    1 
ATOM   6026 O  O    . ALA   B 1 129 ? 43.930 -30.200 2.737   1.00 14.30 ?  129 ALA   B O    1 
ATOM   6027 C  CB   . ALA   B 1 129 ? 42.015 -31.075 -0.011  1.00 17.49 ?  129 ALA   B CB   1 
ATOM   6028 H  H    . ALA   B 1 129 ? 41.519 -29.025 1.245   1.00 17.84 ?  129 ALA   B H    1 
ATOM   6029 H  HA   . ALA   B 1 129 ? 41.395 -31.612 1.865   1.00 18.55 ?  129 ALA   B HA   1 
ATOM   6030 H  HB1  . ALA   B 1 129 ? 42.370 -31.954 -0.227  1.00 21.03 ?  129 ALA   B HB1  1 
ATOM   6031 H  HB2  . ALA   B 1 129 ? 41.117 -30.987 -0.364  1.00 21.03 ?  129 ALA   B HB2  1 
ATOM   6032 H  HB3  . ALA   B 1 129 ? 42.588 -30.387 -0.383  1.00 21.03 ?  129 ALA   B HB3  1 
ATOM   6033 N  N    . GLY   B 1 130 ? 43.922 -32.288 1.879   1.00 14.47 ?  130 GLY   B N    1 
ATOM   6034 C  CA   . GLY   B 1 130 ? 45.309 -32.519 2.231   1.00 15.25 ?  130 GLY   B CA   1 
ATOM   6035 C  C    . GLY   B 1 130 ? 45.523 -32.425 3.723   1.00 15.29 ?  130 GLY   B C    1 
ATOM   6036 O  O    . GLY   B 1 130 ? 44.823 -33.069 4.520   1.00 16.17 ?  130 GLY   B O    1 
ATOM   6037 H  H    . GLY   B 1 130 ? 43.520 -32.965 1.531   1.00 17.41 ?  130 GLY   B H    1 
ATOM   6038 H  HA2  . GLY   B 1 130 ? 45.578 -33.405 1.934   1.00 18.34 ?  130 GLY   B HA2  1 
ATOM   6039 H  HA3  . GLY   B 1 130 ? 45.871 -31.863 1.792   1.00 18.34 ?  130 GLY   B HA3  1 
ATOM   6040 N  N    . ILE   B 1 131 ? 46.501 -31.600 4.111   1.00 15.95 ?  131 ILE   B N    1 
ATOM   6041 C  CA   . ILE   B 1 131 ? 46.855 -31.467 5.516   1.00 16.80 ?  131 ILE   B CA   1 
ATOM   6042 C  C    . ILE   B 1 131 ? 45.740 -30.864 6.350   1.00 16.04 ?  131 ILE   B C    1 
ATOM   6043 O  O    . ILE   B 1 131 ? 45.813 -30.933 7.580   1.00 17.26 ?  131 ILE   B O    1 
ATOM   6044 C  CB   . ILE   B 1 131 ? 48.180 -30.697 5.715   1.00 18.64 ?  131 ILE   B CB   1 
ATOM   6045 C  CG1  . ILE   B 1 131 ? 48.028 -29.219 5.326   1.00 19.66 ?  131 ILE   B CG1  1 
ATOM   6046 C  CG2  . ILE   B 1 131 ? 49.294 -31.355 4.913   1.00 19.66 ?  131 ILE   B CG2  1 
ATOM   6047 C  CD1  . ILE   B 1 131 ? 49.236 -28.357 5.661   1.00 20.70 ?  131 ILE   B CD1  1 
ATOM   6048 H  H    . ILE   B 1 131 ? 46.972 -31.109 3.580   1.00 19.18 ?  131 ILE   B H    1 
ATOM   6049 H  HA   . ILE   B 1 131 ? 46.995 -32.356 5.864   1.00 20.21 ?  131 ILE   B HA   1 
ATOM   6050 H  HB   . ILE   B 1 131 ? 48.411 -30.739 6.657   1.00 22.42 ?  131 ILE   B HB   1 
ATOM   6051 H  HG12 . ILE   B 1 131 ? 47.877 -29.166 4.370   1.00 23.64 ?  131 ILE   B HG12 1 
ATOM   6052 H  HG13 . ILE   B 1 131 ? 47.263 -28.842 5.795   1.00 23.64 ?  131 ILE   B HG13 1 
ATOM   6053 H  HG21 . ILE   B 1 131 ? 50.138 -30.956 5.166   1.00 23.64 ?  131 ILE   B HG21 1 
ATOM   6054 H  HG22 . ILE   B 1 131 ? 49.299 -32.303 5.106   1.00 23.64 ?  131 ILE   B HG22 1 
ATOM   6055 H  HG23 . ILE   B 1 131 ? 49.125 -31.210 3.968   1.00 23.64 ?  131 ILE   B HG23 1 
ATOM   6056 H  HD11 . ILE   B 1 131 ? 49.027 -27.433 5.456   1.00 24.88 ?  131 ILE   B HD11 1 
ATOM   6057 H  HD12 . ILE   B 1 131 ? 49.436 -28.451 6.605   1.00 24.88 ?  131 ILE   B HD12 1 
ATOM   6058 H  HD13 . ILE   B 1 131 ? 49.990 -28.654 5.130   1.00 24.88 ?  131 ILE   B HD13 1 
ATOM   6059 N  N    . PHE   B 1 132 ? 44.708 -30.285 5.718   1.00 14.71 ?  132 PHE   B N    1 
ATOM   6060 C  CA   . PHE   B 1 132 ? 43.546 -29.777 6.444   1.00 15.07 ?  132 PHE   B CA   1 
ATOM   6061 C  C    . PHE   B 1 132 ? 42.520 -30.867 6.767   1.00 16.25 ?  132 PHE   B C    1 
ATOM   6062 O  O    . PHE   B 1 132 ? 41.610 -30.617 7.565   1.00 17.86 ?  132 PHE   B O    1 
ATOM   6063 C  CB   . PHE   B 1 132 ? 42.876 -28.637 5.663   1.00 14.14 ?  132 PHE   B CB   1 
ATOM   6064 C  CG   . PHE   B 1 132 ? 43.576 -27.295 5.778   1.00 13.85 ?  132 PHE   B CG   1 
ATOM   6065 C  CD1  . PHE   B 1 132 ? 44.872 -27.116 5.317   1.00 14.98 ?  132 PHE   B CD1  1 
ATOM   6066 C  CD2  . PHE   B 1 132 ? 42.900 -26.197 6.290   1.00 13.47 ?  132 PHE   B CD2  1 
ATOM   6067 C  CE1  . PHE   B 1 132 ? 45.494 -25.877 5.410   1.00 15.47 ?  132 PHE   B CE1  1 
ATOM   6068 C  CE2  . PHE   B 1 132 ? 43.510 -24.955 6.376   1.00 13.95 ?  132 PHE   B CE2  1 
ATOM   6069 C  CZ   . PHE   B 1 132 ? 44.805 -24.796 5.938   1.00 14.80 ?  132 PHE   B CZ   1 
ATOM   6070 H  H    . PHE   B 1 132 ? 44.655 -30.177 4.861   1.00 17.70 ?  132 PHE   B H    1 
ATOM   6071 H  HA   . PHE   B 1 132 ? 43.851 -29.409 7.284   1.00 18.13 ?  132 PHE   B HA   1 
ATOM   6072 H  HB2  . PHE   B 1 132 ? 42.858 -28.876 4.726   1.00 17.02 ?  132 PHE   B HB2  1 
ATOM   6073 H  HB3  . PHE   B 1 132 ? 41.968 -28.527 5.992   1.00 17.02 ?  132 PHE   B HB3  1 
ATOM   6074 H  HD1  . PHE   B 1 132 ? 45.338 -27.844 4.968   1.00 18.02 ?  132 PHE   B HD1  1 
ATOM   6075 H  HD2  . PHE   B 1 132 ? 42.023 -26.299 6.592   1.00 16.21 ?  132 PHE   B HD2  1 
ATOM   6076 H  HE1  . PHE   B 1 132 ? 46.368 -25.775 5.113   1.00 18.60 ?  132 PHE   B HE1  1 
ATOM   6077 H  HE2  . PHE   B 1 132 ? 43.048 -24.229 6.738   1.00 16.78 ?  132 PHE   B HE2  1 
ATOM   6078 H  HZ   . PHE   B 1 132 ? 45.218 -23.963 6.003   1.00 17.80 ?  132 PHE   B HZ   1 
ATOM   6079 N  N    . GLY   B 1 133 ? 42.629 -32.061 6.170   1.00 16.07 ?  133 GLY   B N    1 
ATOM   6080 C  CA   . GLY   B 1 133 ? 41.917 -33.234 6.651   1.00 17.02 ?  133 GLY   B CA   1 
ATOM   6081 C  C    . GLY   B 1 133 ? 40.520 -33.490 6.117   1.00 17.33 ?  133 GLY   B C    1 
ATOM   6082 O  O    . GLY   B 1 133 ? 39.933 -34.515 6.475   1.00 19.25 ?  133 GLY   B O    1 
ATOM   6083 H  H    . GLY   B 1 133 ? 43.126 -32.210 5.483   1.00 19.33 ?  133 GLY   B H    1 
ATOM   6084 H  HA2  . GLY   B 1 133 ? 42.452 -34.014 6.444   1.00 20.46 ?  133 GLY   B HA2  1 
ATOM   6085 H  HA3  . GLY   B 1 133 ? 41.850 -33.170 7.615   1.00 20.46 ?  133 GLY   B HA3  1 
ATOM   6086 N  N    . ALA   B 1 134 ? 39.953 -32.612 5.296   1.00 16.36 ?  134 ALA   B N    1 
ATOM   6087 C  CA   . ALA   B 1 134 ? 38.630 -32.899 4.760   1.00 16.33 ?  134 ALA   B CA   1 
ATOM   6088 C  C    . ALA   B 1 134 ? 38.717 -33.895 3.608   1.00 16.59 ?  134 ALA   B C    1 
ATOM   6089 O  O    . ALA   B 1 134 ? 39.772 -34.088 2.996   1.00 17.47 ?  134 ALA   B O    1 
ATOM   6090 C  CB   . ALA   B 1 134 ? 37.947 -31.619 4.280   1.00 16.76 ?  134 ALA   B CB   1 
ATOM   6091 H  H    . ALA   B 1 134 ? 40.298 -31.856 5.046   1.00 19.68 ?  134 ALA   B H    1 
ATOM   6092 H  HA   . ALA   B 1 134 ? 38.083 -33.283 5.464   1.00 19.63 ?  134 ALA   B HA   1 
ATOM   6093 H  HB1  . ALA   B 1 134 ? 37.063 -31.842 3.943   1.00 20.16 ?  134 ALA   B HB1  1 
ATOM   6094 H  HB2  . ALA   B 1 134 ? 37.868 -31.000 5.024   1.00 20.16 ?  134 ALA   B HB2  1 
ATOM   6095 H  HB3  . ALA   B 1 134 ? 38.478 -31.221 3.574   1.00 20.16 ?  134 ALA   B HB3  1 
ATOM   6096 N  N    . ASP   B 1 135 ? 37.581 -34.518 3.314   1.00 16.82 ?  135 ASP   B N    1 
ATOM   6097 C  CA   . ASP   B 1 135 ? 37.481 -35.415 2.172   1.00 17.63 ?  135 ASP   B CA   1 
ATOM   6098 C  C    . ASP   B 1 135 ? 37.578 -34.583 0.899   1.00 16.32 ?  135 ASP   B C    1 
ATOM   6099 O  O    . ASP   B 1 135 ? 36.723 -33.714 0.672   1.00 16.21 ?  135 ASP   B O    1 
ATOM   6100 C  CB   . ASP   B 1 135 ? 36.140 -36.146 2.235   1.00 19.38 ?  135 ASP   B CB   1 
ATOM   6101 C  CG   . ASP   B 1 135 ? 35.952 -37.142 1.107   1.00 21.30 ?  135 ASP   B CG   1 
ATOM   6102 O  OD1  . ASP   B 1 135 ? 36.807 -37.186 0.197   1.00 20.88 ?  135 ASP   B OD1  1 
ATOM   6103 O  OD2  . ASP   B 1 135 ? 34.959 -37.910 1.149   1.00 23.89 -1 135 ASP   B OD2  1 
ATOM   6104 H  H    . ASP   B 1 135 ? 36.855 -34.437 3.762   1.00 20.23 ?  135 ASP   B H    1 
ATOM   6105 H  HA   . ASP   B 1 135 ? 38.202 -36.068 2.204   1.00 21.20 ?  135 ASP   B HA   1 
ATOM   6106 H  HB2  . ASP   B 1 135 ? 36.091 -36.632 3.069   1.00 23.30 ?  135 ASP   B HB2  1 
ATOM   6107 H  HB3  . ASP   B 1 135 ? 35.431 -35.491 2.181   1.00 23.30 ?  135 ASP   B HB3  1 
ATOM   6108 N  N    . PRO   B 1 136 ? 38.592 -34.791 0.054   1.00 16.48 ?  136 PRO   B N    1 
ATOM   6109 C  CA   . PRO   B 1 136 ? 38.687 -33.973 -1.164  1.00 15.62 ?  136 PRO   B CA   1 
ATOM   6110 C  C    . PRO   B 1 136 ? 37.491 -34.124 -2.083  1.00 15.19 ?  136 PRO   B C    1 
ATOM   6111 O  O    . PRO   B 1 136 ? 37.170 -33.176 -2.808  1.00 14.43 ?  136 PRO   B O    1 
ATOM   6112 C  CB   . PRO   B 1 136 ? 39.993 -34.453 -1.816  1.00 16.85 ?  136 PRO   B CB   1 
ATOM   6113 C  CG   . PRO   B 1 136 ? 40.198 -35.836 -1.271  1.00 17.95 ?  136 PRO   B CG   1 
ATOM   6114 C  CD   . PRO   B 1 136 ? 39.671 -35.790 0.133   1.00 17.47 ?  136 PRO   B CD   1 
ATOM   6115 H  HA   . PRO   B 1 136 ? 38.781 -33.038 -0.933  1.00 18.78 ?  136 PRO   B HA   1 
ATOM   6116 H  HB2  . PRO   B 1 136 ? 39.893 -34.475 -2.784  1.00 20.27 ?  136 PRO   B HB2  1 
ATOM   6117 H  HB3  . PRO   B 1 136 ? 40.722 -33.868 -1.562  1.00 20.27 ?  136 PRO   B HB3  1 
ATOM   6118 H  HG2  . PRO   B 1 136 ? 39.700 -36.479 -1.801  1.00 21.58 ?  136 PRO   B HG2  1 
ATOM   6119 H  HG3  . PRO   B 1 136 ? 41.145 -36.054 -1.273  1.00 21.58 ?  136 PRO   B HG3  1 
ATOM   6120 H  HD2  . PRO   B 1 136 ? 39.315 -36.654 0.391   1.00 21.00 ?  136 PRO   B HD2  1 
ATOM   6121 H  HD3  . PRO   B 1 136 ? 40.361 -35.489 0.748   1.00 21.00 ?  136 PRO   B HD3  1 
ATOM   6122 N  N    . ILE   B 1 137 ? 36.829 -35.289 -2.083  1.00 15.46 ?  137 ILE   B N    1 
ATOM   6123 C  CA   . ILE   B 1 137 ? 35.610 -35.452 -2.871  1.00 15.74 ?  137 ILE   B CA   1 
ATOM   6124 C  C    . ILE   B 1 137 ? 34.538 -34.480 -2.392  1.00 15.32 ?  137 ILE   B C    1 
ATOM   6125 O  O    . ILE   B 1 137 ? 33.819 -33.871 -3.195  1.00 14.91 ?  137 ILE   B O    1 
ATOM   6126 C  CB   . ILE   B 1 137 ? 35.140 -36.922 -2.814  1.00 18.09 ?  137 ILE   B CB   1 
ATOM   6127 C  CG1  . ILE   B 1 137 ? 36.141 -37.818 -3.547  1.00 20.63 ?  137 ILE   B CG1  1 
ATOM   6128 C  CG2  . ILE   B 1 137 ? 33.736 -37.074 -3.407  1.00 18.57 ?  137 ILE   B CG2  1 
ATOM   6129 C  CD1  . ILE   B 1 137 ? 35.869 -39.303 -3.397  1.00 22.95 ?  137 ILE   B CD1  1 
ATOM   6130 H  H    . ILE   B 1 137 ? 37.064 -35.991 -1.646  1.00 18.60 ?  137 ILE   B H    1 
ATOM   6131 H  HA   . ILE   B 1 137 ? 35.801 -35.246 -3.800  1.00 18.93 ?  137 ILE   B HA   1 
ATOM   6132 H  HB   . ILE   B 1 137 ? 35.103 -37.199 -1.889  1.00 21.75 ?  137 ILE   B HB   1 
ATOM   6133 H  HG12 . ILE   B 1 137 ? 36.116 -37.612 -4.495  1.00 24.80 ?  137 ILE   B HG12 1 
ATOM   6134 H  HG13 . ILE   B 1 137 ? 37.027 -37.648 -3.196  1.00 24.80 ?  137 ILE   B HG13 1 
ATOM   6135 H  HG21 . ILE   B 1 137 ? 33.512 -38.017 -3.480  1.00 22.33 ?  137 ILE   B HG21 1 
ATOM   6136 H  HG22 . ILE   B 1 137 ? 33.091 -36.640 -2.825  1.00 22.33 ?  137 ILE   B HG22 1 
ATOM   6137 H  HG23 . ILE   B 1 137 ? 33.714 -36.665 -4.287  1.00 22.33 ?  137 ILE   B HG23 1 
ATOM   6138 H  HD11 . ILE   B 1 137 ? 36.588 -39.791 -3.827  1.00 27.58 ?  137 ILE   B HD11 1 
ATOM   6139 H  HD12 . ILE   B 1 137 ? 35.833 -39.527 -2.454  1.00 27.58 ?  137 ILE   B HD12 1 
ATOM   6140 H  HD13 . ILE   B 1 137 ? 35.026 -39.523 -3.824  1.00 27.58 ?  137 ILE   B HD13 1 
ATOM   6141 N  N    . HIS   B 1 138 ? 34.412 -34.326 -1.077  1.00 15.55 ?  138 HIS   B N    1 
ATOM   6142 C  CA   . HIS   B 1 138 ? 33.465 -33.357 -0.543  1.00 15.74 ?  138 HIS   B CA   1 
ATOM   6143 C  C    . HIS   B 1 138 ? 33.885 -31.928 -0.870  1.00 14.82 ?  138 HIS   B C    1 
ATOM   6144 O  O    . HIS   B 1 138 ? 33.038 -31.082 -1.174  1.00 15.44 ?  138 HIS   B O    1 
ATOM   6145 C  CB   . HIS   B 1 138 ? 33.348 -33.535 0.962   1.00 17.02 ?  138 HIS   B CB   1 
ATOM   6146 C  CG   . HIS   B 1 138 ? 32.409 -32.564 1.595   1.00 18.35 ?  138 HIS   B CG   1 
ATOM   6147 N  ND1  . HIS   B 1 138 ? 31.076 -32.491 1.254   1.00 19.67 ?  138 HIS   B ND1  1 
ATOM   6148 C  CD2  . HIS   B 1 138 ? 32.617 -31.593 2.515   1.00 19.03 ?  138 HIS   B CD2  1 
ATOM   6149 C  CE1  . HIS   B 1 138 ? 30.497 -31.531 1.953   1.00 19.57 ?  138 HIS   B CE1  1 
ATOM   6150 N  NE2  . HIS   B 1 138 ? 31.410 -30.973 2.728   1.00 18.97 ?  138 HIS   B NE2  1 
ATOM   6151 H  H    . HIS   B 1 138 ? 34.864 -34.759 -0.486  1.00 18.71 ?  138 HIS   B H    1 
ATOM   6152 H  HA   . HIS   B 1 138 ? 32.593 -33.525 -0.939  1.00 18.93 ?  138 HIS   B HA   1 
ATOM   6153 H  HB2  . HIS   B 1 138 ? 33.018 -34.427 1.150   1.00 20.47 ?  138 HIS   B HB2  1 
ATOM   6154 H  HB3  . HIS   B 1 138 ? 34.219 -33.410 1.361   1.00 20.47 ?  138 HIS   B HB3  1 
ATOM   6155 H  HD1  . HIS   B 1 138 ? 30.679 -32.998 0.680   1.00 23.64 ?  138 HIS   B HD1  1 
ATOM   6156 H  HD2  . HIS   B 1 138 ? 33.415 -31.390 2.939   1.00 22.88 ?  138 HIS   B HD2  1 
ATOM   6157 H  HE1  . HIS   B 1 138 ? 29.592 -31.299 1.911   1.00 23.52 ?  138 HIS   B HE1  1 
ATOM   6158 N  N    . SER   B 1 139 ? 35.180 -31.630 -0.796  1.00 14.38 ?  139 SER   B N    1 
ATOM   6159 C  CA   . SER   B 1 139 ? 35.625 -30.283 -1.121  1.00 13.90 ?  139 SER   B CA   1 
ATOM   6160 C  C    . SER   B 1 139 ? 35.287 -29.935 -2.560  1.00 13.11 ?  139 SER   B C    1 
ATOM   6161 O  O    . SER   B 1 139 ? 34.835 -28.822 -2.841  1.00 13.14 ?  139 SER   B O    1 
ATOM   6162 C  CB   . SER   B 1 139 ? 37.118 -30.147 -0.851  1.00 14.29 ?  139 SER   B CB   1 
ATOM   6163 O  OG   . SER   B 1 139 ? 37.523 -28.812 -1.096  1.00 14.09 ?  139 SER   B OG   1 
ATOM   6164 H  H    . SER   B 1 139 ? 35.796 -32.177 -0.574  1.00 17.29 ?  139 SER   B H    1 
ATOM   6165 H  HA   . SER   B 1 139 ? 35.152 -29.658 -0.556  1.00 16.73 ?  139 SER   B HA   1 
ATOM   6166 H  HB2  . SER   B 1 139 ? 37.291 -30.371 0.077   1.00 17.19 ?  139 SER   B HB2  1 
ATOM   6167 H  HB3  . SER   B 1 139 ? 37.606 -30.745 -1.438  1.00 17.19 ?  139 SER   B HB3  1 
ATOM   6168 H  HG   . SER   B 1 139 ? 38.349 -28.732 -0.945  1.00 16.95 ?  139 SER   B HG   1 
ATOM   6169 N  N    . LEU   B 1 140 ? 35.476 -30.882 -3.484  1.00 13.01 ?  140 LEU   B N    1 
ATOM   6170 C  CA   . LEU   B 1 140 ? 35.109 -30.633 -4.872  1.00 13.01 ?  140 LEU   B CA   1 
ATOM   6171 C  C    . LEU   B 1 140 ? 33.605 -30.406 -5.003  1.00 13.23 ?  140 LEU   B C    1 
ATOM   6172 O  O    . LEU   B 1 140 ? 33.169 -29.519 -5.741  1.00 13.43 ?  140 LEU   B O    1 
ATOM   6173 C  CB   . LEU   B 1 140 ? 35.578 -31.790 -5.753  1.00 13.21 ?  140 LEU   B CB   1 
ATOM   6174 C  CG   . LEU   B 1 140 ? 35.212 -31.694 -7.228  1.00 13.30 ?  140 LEU   B CG   1 
ATOM   6175 C  CD1  . LEU   B 1 140 ? 35.775 -30.419 -7.831  1.00 14.24 ?  140 LEU   B CD1  1 
ATOM   6176 C  CD2  . LEU   B 1 140 ? 35.686 -32.923 -7.978  1.00 14.55 ?  140 LEU   B CD2  1 
ATOM   6177 H  H    . LEU   B 1 140 ? 35.807 -31.660 -3.339  1.00 15.66 ?  140 LEU   B H    1 
ATOM   6178 H  HA   . LEU   B 1 140 ? 35.564 -29.830 -5.178  1.00 15.65 ?  140 LEU   B HA   1 
ATOM   6179 H  HB2  . LEU   B 1 140 ? 36.547 -31.849 -5.703  1.00 15.89 ?  140 LEU   B HB2  1 
ATOM   6180 H  HB3  . LEU   B 1 140 ? 35.189 -32.613 -5.418  1.00 15.89 ?  140 LEU   B HB3  1 
ATOM   6181 H  HG   . LEU   B 1 140 ? 34.248 -31.651 -7.306  1.00 16.00 ?  140 LEU   B HG   1 
ATOM   6182 H  HD11 . LEU   B 1 140 ? 35.651 -30.445 -8.792  1.00 17.13 ?  140 LEU   B HD11 1 
ATOM   6183 H  HD12 . LEU   B 1 140 ? 35.302 -29.656 -7.458  1.00 17.13 ?  140 LEU   B HD12 1 
ATOM   6184 H  HD13 . LEU   B 1 140 ? 36.719 -30.359 -7.620  1.00 17.13 ?  140 LEU   B HD13 1 
ATOM   6185 H  HD21 . LEU   B 1 140 ? 35.433 -32.831 -8.912  1.00 17.51 ?  140 LEU   B HD21 1 
ATOM   6186 H  HD22 . LEU   B 1 140 ? 36.643 -32.995 -7.895  1.00 17.51 ?  140 LEU   B HD22 1 
ATOM   6187 H  HD23 . LEU   B 1 140 ? 35.252 -33.703 -7.596  1.00 17.51 ?  140 LEU   B HD23 1 
ATOM   6188 N  N    . ARG   B 1 141 ? 32.803 -31.199 -4.291  1.00 13.50 ?  141 ARG   B N    1 
ATOM   6189 C  CA   . ARG   B 1 141 ? 31.353 -31.021 -4.279  1.00 14.54 ?  141 ARG   B CA   1 
ATOM   6190 C  C    . ARG   B 1 141 ? 30.974 -29.610 -3.846  1.00 13.83 ?  141 ARG   B C    1 
ATOM   6191 O  O    . ARG   B 1 141 ? 30.168 -28.934 -4.502  1.00 14.03 ?  141 ARG   B O    1 
ATOM   6192 C  CB   . ARG   B 1 141 ? 30.766 -32.056 -3.314  1.00 15.94 ?  141 ARG   B CB   1 
ATOM   6193 C  CG   . ARG   B 1 141 ? 29.305 -31.929 -2.977  1.00 17.85 ?  141 ARG   B CG   1 
ATOM   6194 C  CD   . ARG   B 1 141 ? 28.500 -32.567 -4.036  1.00 19.52 ?  141 ARG   B CD   1 
ATOM   6195 N  NE   . ARG   B 1 141 ? 28.239 -31.660 -5.142  1.00 19.90 ?  141 ARG   B NE   1 
ATOM   6196 C  CZ   . ARG   B 1 141 ? 28.231 -32.012 -6.420  1.00 19.11 ?  141 ARG   B CZ   1 
ATOM   6197 N  NH1  . ARG   B 1 141 ? 28.671 -33.198 -6.817  1.00 19.24 ?  141 ARG   B NH1  1 
ATOM   6198 N  NH2  . ARG   B 1 141 ? 27.769 -31.153 -7.324  1.00 19.91 ?  141 ARG   B NH2  1 
ATOM   6199 H  H    . ARG   B 1 141 ? 33.081 -31.846 -3.803  1.00 16.24 ?  141 ARG   B H    1 
ATOM   6200 H  HA   . ARG   B 1 141 ? 30.997 -31.180 -5.166  1.00 17.48 ?  141 ARG   B HA   1 
ATOM   6201 H  HB2  . ARG   B 1 141 ? 30.909 -32.939 -3.699  1.00 19.17 ?  141 ARG   B HB2  1 
ATOM   6202 H  HB3  . ARG   B 1 141 ? 31.257 -32.000 -2.482  1.00 19.17 ?  141 ARG   B HB3  1 
ATOM   6203 H  HG2  . ARG   B 1 141 ? 29.137 -32.379 -2.138  1.00 21.46 ?  141 ARG   B HG2  1 
ATOM   6204 H  HG3  . ARG   B 1 141 ? 29.056 -30.991 -2.912  1.00 21.46 ?  141 ARG   B HG3  1 
ATOM   6205 H  HD2  . ARG   B 1 141 ? 28.974 -33.348 -4.373  1.00 23.47 ?  141 ARG   B HD2  1 
ATOM   6206 H  HD3  . ARG   B 1 141 ? 27.657 -32.840 -3.658  1.00 23.47 ?  141 ARG   B HD3  1 
ATOM   6207 H  HE   . ARG   B 1 141 ? 28.057 -30.840 -4.951  1.00 23.92 ?  141 ARG   B HE   1 
ATOM   6208 H  HH11 . ARG   B 1 141 ? 28.963 -33.769 -6.245  1.00 23.13 ?  141 ARG   B HH11 1 
ATOM   6209 H  HH12 . ARG   B 1 141 ? 28.665 -33.397 -7.652  1.00 23.13 ?  141 ARG   B HH12 1 
ATOM   6210 H  HH21 . ARG   B 1 141 ? 27.487 -30.378 -7.078  1.00 23.93 ?  141 ARG   B HH21 1 
ATOM   6211 H  HH22 . ARG   B 1 141 ? 27.777 -31.360 -8.159  1.00 23.93 ?  141 ARG   B HH22 1 
ATOM   6212 N  N    . VAL   B 1 142 ? 31.523 -29.162 -2.720  1.00 13.55 ?  142 VAL   B N    1 
ATOM   6213 C  CA   . VAL   B 1 142 ? 31.182 -27.832 -2.231  1.00 13.12 ?  142 VAL   B CA   1 
ATOM   6214 C  C    . VAL   B 1 142 ? 31.658 -26.769 -3.215  1.00 12.93 ?  142 VAL   B C    1 
ATOM   6215 O  O    . VAL   B 1 142 ? 30.965 -25.776 -3.462  1.00 13.46 ?  142 VAL   B O    1 
ATOM   6216 C  CB   . VAL   B 1 142 ? 31.727 -27.603 -0.809  1.00 13.90 ?  142 VAL   B CB   1 
ATOM   6217 C  CG1  . VAL   B 1 142 ? 31.410 -26.178 -0.335  1.00 13.66 ?  142 VAL   B CG1  1 
ATOM   6218 C  CG2  . VAL   B 1 142 ? 31.147 -28.628 0.148   1.00 14.80 ?  142 VAL   B CG2  1 
ATOM   6219 H  H    . VAL   B 1 142 ? 32.085 -29.597 -2.234  1.00 16.30 ?  142 VAL   B H    1 
ATOM   6220 H  HA   . VAL   B 1 142 ? 30.223 -27.764 -2.179  1.00 15.79 ?  142 VAL   B HA   1 
ATOM   6221 H  HB   . VAL   B 1 142 ? 32.694 -27.712 -0.814  1.00 16.72 ?  142 VAL   B HB   1 
ATOM   6222 H  HG11 . VAL   B 1 142 ? 31.586 -26.116 0.615   1.00 16.43 ?  142 VAL   B HG11 1 
ATOM   6223 H  HG12 . VAL   B 1 142 ? 31.975 -25.551 -0.816  1.00 16.43 ?  142 VAL   B HG12 1 
ATOM   6224 H  HG13 . VAL   B 1 142 ? 30.477 -25.989 -0.514  1.00 16.43 ?  142 VAL   B HG13 1 
ATOM   6225 H  HG21 . VAL   B 1 142 ? 31.467 -28.439 1.042   1.00 17.80 ?  142 VAL   B HG21 1 
ATOM   6226 H  HG22 . VAL   B 1 142 ? 30.180 -28.566 0.119   1.00 17.80 ?  142 VAL   B HG22 1 
ATOM   6227 H  HG23 . VAL   B 1 142 ? 31.432 -29.512 -0.129  1.00 17.80 ?  142 VAL   B HG23 1 
ATOM   6228 N  N    . CYS   B 1 143 ? 32.845 -26.961 -3.794  1.00 12.70 ?  143 CYS   B N    1 
ATOM   6229 C  CA   . CYS   B 1 143 ? 33.339 -26.024 -4.798  1.00 12.38 ?  143 CYS   B CA   1 
ATOM   6230 C  C    . CYS   B 1 143 ? 32.335 -25.882 -5.938  1.00 12.41 ?  143 CYS   B C    1 
ATOM   6231 O  O    . CYS   B 1 143 ? 31.934 -24.773 -6.303  1.00 12.57 ?  143 CYS   B O    1 
ATOM   6232 C  CB   . CYS   B 1 143 ? 34.700 -26.505 -5.320  1.00 12.68 ?  143 CYS   B CB   1 
ATOM   6233 S  SG   . CYS   B 1 143 ? 35.447 -25.416 -6.552  1.00 12.92 ?  143 CYS   B SG   1 
ATOM   6234 H  H    . CYS   B 1 143 ? 33.376 -27.614 -3.624  1.00 15.28 ?  143 CYS   B H    1 
ATOM   6235 H  HA   . CYS   B 1 143 ? 33.466 -25.151 -4.391  1.00 14.90 ?  143 CYS   B HA   1 
ATOM   6236 H  HB2  . CYS   B 1 143 ? 35.321 -26.575 -4.575  1.00 15.25 ?  143 CYS   B HB2  1 
ATOM   6237 H  HB3  . CYS   B 1 143 ? 34.589 -27.373 -5.726  1.00 15.25 ?  143 CYS   B HB3  1 
ATOM   6238 H  HG   . CYS   B 1 143 ? 36.523 -25.850 -6.866  1.00 15.54 ?  143 CYS   B HG   1 
ATOM   6239 N  N    . VAL   B 1 144 ? 31.938 -27.004 -6.532  1.00 13.08 ?  144 VAL   B N    1 
ATOM   6240 C  CA   . VAL   B 1 144 ? 31.027 -26.953 -7.672  1.00 14.03 ?  144 VAL   B CA   1 
ATOM   6241 C  C    . VAL   B 1 144 ? 29.686 -26.331 -7.293  1.00 13.83 ?  144 VAL   B C    1 
ATOM   6242 O  O    . VAL   B 1 144 ? 29.070 -25.620 -8.097  1.00 15.07 ?  144 VAL   B O    1 
ATOM   6243 C  CB   . VAL   B 1 144 ? 30.860 -28.366 -8.240  1.00 16.49 ?  144 VAL   B CB   1 
ATOM   6244 C  CG1  . VAL   B 1 144 ? 29.599 -28.478 -9.092  1.00 19.05 ?  144 VAL   B CG1  1 
ATOM   6245 C  CG2  . VAL   B 1 144 ? 32.114 -28.781 -9.007  1.00 16.65 ?  144 VAL   B CG2  1 
ATOM   6246 H  H    . VAL   B 1 144 ? 32.189 -27.795 -6.309  1.00 15.74 ?  144 VAL   B H    1 
ATOM   6247 H  HA   . VAL   B 1 144 ? 31.414 -26.399 -8.366  1.00 16.88 ?  144 VAL   B HA   1 
ATOM   6248 H  HB   . VAL   B 1 144 ? 30.763 -28.984 -7.495  1.00 19.83 ?  144 VAL   B HB   1 
ATOM   6249 H  HG11 . VAL   B 1 144 ? 29.677 -29.269 -9.654  1.00 22.90 ?  144 VAL   B HG11 1 
ATOM   6250 H  HG12 . VAL   B 1 144 ? 28.831 -28.568 -8.509  1.00 22.90 ?  144 VAL   B HG12 1 
ATOM   6251 H  HG13 . VAL   B 1 144 ? 29.519 -27.690 -9.644  1.00 22.90 ?  144 VAL   B HG13 1 
ATOM   6252 H  HG21 . VAL   B 1 144 ? 31.991 -29.681 -9.352  1.00 20.02 ?  144 VAL   B HG21 1 
ATOM   6253 H  HG22 . VAL   B 1 144 ? 32.252 -28.163 -9.742  1.00 20.02 ?  144 VAL   B HG22 1 
ATOM   6254 H  HG23 . VAL   B 1 144 ? 32.875 -28.759 -8.407  1.00 20.02 ?  144 VAL   B HG23 1 
ATOM   6255 N  N    . ASP   B 1 145 ? 29.216 -26.578 -6.075  1.00 13.94 ?  145 ASP   B N    1 
ATOM   6256 C  CA   . ASP   B 1 145 ? 27.903 -26.108 -5.645  1.00 14.55 ?  145 ASP   B CA   1 
ATOM   6257 C  C    . ASP   B 1 145 ? 27.935 -24.684 -5.101  1.00 14.09 ?  145 ASP   B C    1 
ATOM   6258 O  O    . ASP   B 1 145 ? 26.877 -24.137 -4.765  1.00 16.06 ?  145 ASP   B O    1 
ATOM   6259 C  CB   . ASP   B 1 145 ? 27.320 -27.029 -4.561  1.00 16.22 ?  145 ASP   B CB   1 
ATOM   6260 C  CG   . ASP   B 1 145 ? 26.967 -28.409 -5.067  1.00 18.07 ?  145 ASP   B CG   1 
ATOM   6261 O  OD1  . ASP   B 1 145 ? 26.860 -28.605 -6.295  1.00 18.45 ?  145 ASP   B OD1  1 
ATOM   6262 O  OD2  . ASP   B 1 145 ? 26.790 -29.297 -4.210  1.00 19.99 -1 145 ASP   B OD2  1 
ATOM   6263 H  H    . ASP   B 1 145 ? 29.643 -27.005 -5.470  1.00 16.77 ?  145 ASP   B H    1 
ATOM   6264 H  HA   . ASP   B 1 145 ? 27.303 -26.101 -6.405  1.00 17.50 ?  145 ASP   B HA   1 
ATOM   6265 H  HB2  . ASP   B 1 145 ? 27.969 -27.138 -3.860  1.00 19.50 ?  145 ASP   B HB2  1 
ATOM   6266 H  HB3  . ASP   B 1 145 ? 26.509 -26.620 -4.213  1.00 19.50 ?  145 ASP   B HB3  1 
ATOM   6267 N  N    . THR   B 1 146 ? 29.114 -24.071 -5.000  1.00 12.44 ?  146 THR   B N    1 
ATOM   6268 C  CA   . THR   B 1 146 ? 29.249 -22.745 -4.395  1.00 12.18 ?  146 THR   B CA   1 
ATOM   6269 C  C    . THR   B 1 146 ? 29.879 -21.713 -5.314  1.00 12.05 ?  146 THR   B C    1 
ATOM   6270 O  O    . THR   B 1 146 ? 29.431 -20.550 -5.351  1.00 12.25 ?  146 THR   B O    1 
ATOM   6271 C  CB   . THR   B 1 146 ? 30.078 -22.843 -3.105  1.00 12.65 ?  146 THR   B CB   1 
ATOM   6272 O  OG1  . THR   B 1 146 ? 29.508 -23.837 -2.246  1.00 13.02 ?  146 THR   B OG1  1 
ATOM   6273 C  CG2  . THR   B 1 146 ? 30.146 -21.503 -2.381  1.00 12.93 ?  146 THR   B CG2  1 
ATOM   6274 H  H    . THR   B 1 146 ? 29.868 -24.399 -5.273  1.00 14.97 ?  146 THR   B H    1 
ATOM   6275 H  HA   . THR   B 1 146 ? 28.375 -22.418 -4.154  1.00 14.66 ?  146 THR   B HA   1 
ATOM   6276 H  HB   . THR   B 1 146 ? 30.988 -23.100 -3.327  1.00 15.22 ?  146 THR   B HB   1 
ATOM   6277 H  HG1  . THR   B 1 146 ? 29.548 -24.596 -2.623  1.00 15.67 ?  146 THR   B HG1  1 
ATOM   6278 H  HG21 . THR   B 1 146 ? 30.506 -21.624 -1.489  1.00 15.56 ?  146 THR   B HG21 1 
ATOM   6279 H  HG22 . THR   B 1 146 ? 30.720 -20.889 -2.869  1.00 15.56 ?  146 THR   B HG22 1 
ATOM   6280 H  HG23 . THR   B 1 146 ? 29.259 -21.119 -2.314  1.00 15.56 ?  146 THR   B HG23 1 
ATOM   6281 N  N    . VAL   B 1 147 ? 30.948 -22.084 -6.010  1.00 12.13 ?  147 VAL   B N    1 
ATOM   6282 C  CA   . VAL   B 1 147 ? 31.671 -21.146 -6.854  1.00 11.75 ?  147 VAL   B CA   1 
ATOM   6283 C  C    . VAL   B 1 147 ? 30.932 -21.018 -8.172  1.00 11.97 ?  147 VAL   B C    1 
ATOM   6284 O  O    . VAL   B 1 147 ? 30.567 -22.024 -8.797  1.00 13.08 ?  147 VAL   B O    1 
ATOM   6285 C  CB   . VAL   B 1 147 ? 33.123 -21.608 -7.061  1.00 11.97 ?  147 VAL   B CB   1 
ATOM   6286 C  CG1  . VAL   B 1 147 ? 33.883 -20.582 -7.877  1.00 12.09 ?  147 VAL   B CG1  1 
ATOM   6287 C  CG2  . VAL   B 1 147 ? 33.802 -21.820 -5.717  1.00 12.05 ?  147 VAL   B CG2  1 
ATOM   6288 H  H    . VAL   B 1 147 ? 31.276 -22.887 -6.023  1.00 14.60 ?  147 VAL   B H    1 
ATOM   6289 H  HA   . VAL   B 1 147 ? 31.691 -20.278 -6.425  1.00 14.14 ?  147 VAL   B HA   1 
ATOM   6290 H  HB   . VAL   B 1 147 ? 33.134 -22.450 -7.547  1.00 14.41 ?  147 VAL   B HB   1 
ATOM   6291 H  HG11 . VAL   B 1 147 ? 34.826 -20.805 -7.869  1.00 14.55 ?  147 VAL   B HG11 1 
ATOM   6292 H  HG12 . VAL   B 1 147 ? 33.550 -20.586 -8.787  1.00 14.55 ?  147 VAL   B HG12 1 
ATOM   6293 H  HG13 . VAL   B 1 147 ? 33.750 -19.705 -7.479  1.00 14.55 ?  147 VAL   B HG13 1 
ATOM   6294 H  HG21 . VAL   B 1 147 ? 34.743 -22.010 -5.863  1.00 14.50 ?  147 VAL   B HG21 1 
ATOM   6295 H  HG22 . VAL   B 1 147 ? 33.706 -21.014 -5.186  1.00 14.50 ?  147 VAL   B HG22 1 
ATOM   6296 H  HG23 . VAL   B 1 147 ? 33.381 -22.567 -5.264  1.00 14.50 ?  147 VAL   B HG23 1 
ATOM   6297 N  N    . ARG   B 1 148 ? 30.724 -19.771 -8.598  1.00 11.92 ?  148 ARG   B N    1 
ATOM   6298 C  CA   . ARG   B 1 148 ? 30.101 -19.454 -9.872  1.00 12.03 ?  148 ARG   B CA   1 
ATOM   6299 C  C    . ARG   B 1 148 ? 31.059 -18.782 -10.844 1.00 12.30 ?  148 ARG   B C    1 
ATOM   6300 O  O    . ARG   B 1 148 ? 30.774 -18.759 -12.044 1.00 13.50 ?  148 ARG   B O    1 
ATOM   6301 C  CB   . ARG   B 1 148 ? 28.864 -18.561 -9.656  1.00 12.36 ?  148 ARG   B CB   1 
ATOM   6302 C  CG   . ARG   B 1 148 ? 27.792 -19.264 -8.833  1.00 13.26 ?  148 ARG   B CG   1 
ATOM   6303 C  CD   . ARG   B 1 148 ? 26.581 -18.381 -8.519  1.00 14.11 ?  148 ARG   B CD   1 
ATOM   6304 N  NE   . ARG   B 1 148 ? 26.961 -17.177 -7.792  1.00 13.84 ?  148 ARG   B NE   1 
ATOM   6305 C  CZ   . ARG   B 1 148 ? 27.269 -17.141 -6.502  1.00 12.83 ?  148 ARG   B CZ   1 
ATOM   6306 N  NH1  . ARG   B 1 148 ? 27.207 -18.226 -5.743  1.00 12.99 ?  148 ARG   B NH1  1 
ATOM   6307 N  NH2  . ARG   B 1 148 ? 27.659 -15.989 -5.961  1.00 13.04 ?  148 ARG   B NH2  1 
ATOM   6308 H  H    . ARG   B 1 148 ? 30.948 -19.069 -8.145  1.00 14.34 ?  148 ARG   B H    1 
ATOM   6309 H  HA   . ARG   B 1 148 ? 29.802 -20.277 -10.280 1.00 14.48 ?  148 ARG   B HA   1 
ATOM   6310 H  HB2  . ARG   B 1 148 ? 29.129 -17.757 -9.182  1.00 14.87 ?  148 ARG   B HB2  1 
ATOM   6311 H  HB3  . ARG   B 1 148 ? 28.484 -18.332 -10.517 1.00 14.87 ?  148 ARG   B HB3  1 
ATOM   6312 H  HG2  . ARG   B 1 148 ? 27.473 -20.037 -9.329  1.00 15.96 ?  148 ARG   B HG2  1 
ATOM   6313 H  HG3  . ARG   B 1 148 ? 28.175 -19.550 -7.991  1.00 15.96 ?  148 ARG   B HG3  1 
ATOM   6314 H  HD2  . ARG   B 1 148 ? 26.157 -18.113 -9.349  1.00 16.97 ?  148 ARG   B HD2  1 
ATOM   6315 H  HD3  . ARG   B 1 148 ? 25.953 -18.883 -7.972  1.00 16.97 ?  148 ARG   B HD3  1 
ATOM   6316 H  HE   . ARG   B 1 148 ? 26.999 -16.443 -8.231  1.00 16.65 ?  148 ARG   B HE   1 
ATOM   6317 H  HH11 . ARG   B 1 148 ? 26.952 -18.978 -6.076  1.00 15.64 ?  148 ARG   B HH11 1 
ATOM   6318 H  HH12 . ARG   B 1 148 ? 27.405 -18.179 -4.905  1.00 15.64 ?  148 ARG   B HH12 1 
ATOM   6319 H  HH21 . ARG   B 1 148 ? 27.714 -15.285 -6.448  1.00 15.69 ?  148 ARG   B HH21 1 
ATOM   6320 H  HH22 . ARG   B 1 148 ? 27.865 -15.954 -5.127  1.00 15.69 ?  148 ARG   B HH22 1 
ATOM   6321 N  N    . THR   B 1 149 ? 32.164 -18.223 -10.357 1.00 12.02 ?  149 THR   B N    1 
ATOM   6322 C  CA   . THR   B 1 149 ? 33.204 -17.661 -11.209 1.00 12.22 ?  149 THR   B CA   1 
ATOM   6323 C  C    . THR   B 1 149 ? 34.093 -18.800 -11.719 1.00 11.51 ?  149 THR   B C    1 
ATOM   6324 O  O    . THR   B 1 149 ? 33.899 -19.972 -11.382 1.00 12.11 ?  149 THR   B O    1 
ATOM   6325 C  CB   . THR   B 1 149 ? 33.973 -16.603 -10.429 1.00 12.15 ?  149 THR   B CB   1 
ATOM   6326 O  OG1  . THR   B 1 149 ? 34.436 -17.204 -9.217  1.00 12.18 ?  149 THR   B OG1  1 
ATOM   6327 C  CG2  . THR   B 1 149 ? 33.081 -15.395 -10.131 1.00 12.78 ?  149 THR   B CG2  1 
ATOM   6328 H  H    . THR   B 1 149 ? 32.332 -18.152 -9.519  1.00 14.47 ?  149 THR   B H    1 
ATOM   6329 H  HA   . THR   B 1 149 ? 32.794 -17.230 -11.974 1.00 14.71 ?  149 THR   B HA   1 
ATOM   6330 H  HB   . THR   B 1 149 ? 34.735 -16.312 -10.945 1.00 14.62 ?  149 THR   B HB   1 
ATOM   6331 H  HG1  . THR   B 1 149 ? 34.848 -16.629 -8.751  1.00 14.66 ?  149 THR   B HG1  1 
ATOM   6332 H  HG21 . THR   B 1 149 ? 33.585 -14.726 -9.646  1.00 15.37 ?  149 THR   B HG21 1 
ATOM   6333 H  HG22 . THR   B 1 149 ? 32.761 -15.011 -10.963 1.00 15.37 ?  149 THR   B HG22 1 
ATOM   6334 H  HG23 . THR   B 1 149 ? 32.319 -15.668 -9.596  1.00 15.37 ?  149 THR   B HG23 1 
ATOM   6335 N  N    . ASN   B 1 150 ? 35.064 -18.478 -12.564 1.00 11.86 ?  150 ASN   B N    1 
ATOM   6336 C  CA   . ASN   B 1 150 ? 35.824 -19.510 -13.264 1.00 12.28 ?  150 ASN   B CA   1 
ATOM   6337 C  C    . ASN   B 1 150 ? 36.987 -19.960 -12.392 1.00 11.70 ?  150 ASN   B C    1 
ATOM   6338 O  O    . ASN   B 1 150 ? 37.915 -19.185 -12.136 1.00 12.46 ?  150 ASN   B O    1 
ATOM   6339 C  CB   . ASN   B 1 150 ? 36.297 -18.988 -14.612 1.00 13.92 ?  150 ASN   B CB   1 
ATOM   6340 C  CG   . ASN   B 1 150 ? 35.151 -18.758 -15.554 1.00 16.54 ?  150 ASN   B CG   1 
ATOM   6341 O  OD1  . ASN   B 1 150 ? 34.249 -19.584 -15.648 1.00 17.51 ?  150 ASN   B OD1  1 
ATOM   6342 N  ND2  . ASN   B 1 150 ? 35.154 -17.619 -16.230 1.00 18.51 ?  150 ASN   B ND2  1 
ATOM   6343 H  H    . ASN   B 1 150 ? 35.309 -17.670 -12.747 1.00 14.28 ?  150 ASN   B H    1 
ATOM   6344 H  HA   . ASN   B 1 150 ? 35.243 -20.273 -13.422 1.00 14.78 ?  150 ASN   B HA   1 
ATOM   6345 H  HB2  . ASN   B 1 150 ? 36.756 -18.143 -14.486 1.00 16.74 ?  150 ASN   B HB2  1 
ATOM   6346 H  HB3  . ASN   B 1 150 ? 36.889 -19.637 -15.017 1.00 16.74 ?  150 ASN   B HB3  1 
ATOM   6347 H  HD21 . ASN   B 1 150 ? 34.516 -17.437 -16.781 1.00 22.25 ?  150 ASN   B HD21 1 
ATOM   6348 H  HD22 . ASN   B 1 150 ? 35.801 -17.059 -16.131 1.00 22.25 ?  150 ASN   B HD22 1 
ATOM   6349 N  N    . VAL   B 1 151 ? 36.946 -21.209 -11.942 1.00 11.58 ?  151 VAL   B N    1 
ATOM   6350 C  CA   . VAL   B 1 151 ? 37.963 -21.737 -11.049 1.00 11.90 ?  151 VAL   B CA   1 
ATOM   6351 C  C    . VAL   B 1 151 ? 38.669 -22.907 -11.721 1.00 11.75 ?  151 VAL   B C    1 
ATOM   6352 O  O    . VAL   B 1 151 ? 38.028 -23.842 -12.227 1.00 12.84 ?  151 VAL   B O    1 
ATOM   6353 C  CB   . VAL   B 1 151 ? 37.402 -22.070 -9.652  1.00 12.78 ?  151 VAL   B CB   1 
ATOM   6354 C  CG1  . VAL   B 1 151 ? 36.228 -23.058 -9.732  1.00 13.62 ?  151 VAL   B CG1  1 
ATOM   6355 C  CG2  . VAL   B 1 151 ? 38.509 -22.561 -8.733  1.00 13.50 ?  151 VAL   B CG2  1 
ATOM   6356 H  H    . VAL   B 1 151 ? 36.323 -21.773 -12.146 1.00 13.94 ?  151 VAL   B H    1 
ATOM   6357 H  HA   . VAL   B 1 151 ? 38.627 -21.040 -10.920 1.00 14.32 ?  151 VAL   B HA   1 
ATOM   6358 H  HB   . VAL   B 1 151 ? 37.052 -21.250 -9.267  1.00 15.38 ?  151 VAL   B HB   1 
ATOM   6359 H  HG11 . VAL   B 1 151 ? 35.911 -23.251 -8.834  1.00 16.39 ?  151 VAL   B HG11 1 
ATOM   6360 H  HG12 . VAL   B 1 151 ? 35.508 -22.665 -10.255 1.00 16.39 ?  151 VAL   B HG12 1 
ATOM   6361 H  HG13 . VAL   B 1 151 ? 36.528 -23.880 -10.156 1.00 16.39 ?  151 VAL   B HG13 1 
ATOM   6362 H  HG21 . VAL   B 1 151 ? 38.154 -22.640 -7.832  1.00 16.25 ?  151 VAL   B HG21 1 
ATOM   6363 H  HG22 . VAL   B 1 151 ? 38.818 -23.425 -9.042  1.00 16.25 ?  151 VAL   B HG22 1 
ATOM   6364 H  HG23 . VAL   B 1 151 ? 39.236 -21.920 -8.745  1.00 16.25 ?  151 VAL   B HG23 1 
ATOM   6365 N  N    . TYR   B 1 152 ? 39.999 -22.817 -11.739 1.00 11.11 ?  152 TYR   B N    1 
ATOM   6366 C  CA   . TYR   B 1 152 ? 40.904 -23.799 -12.318 1.00 11.54 ?  152 TYR   B CA   1 
ATOM   6367 C  C    . TYR   B 1 152 ? 41.620 -24.474 -11.153 1.00 10.74 ?  152 TYR   B C    1 
ATOM   6368 O  O    . TYR   B 1 152 ? 42.471 -23.858 -10.500 1.00 11.18 ?  152 TYR   B O    1 
ATOM   6369 C  CB   . TYR   B 1 152 ? 41.875 -23.088 -13.265 1.00 12.25 ?  152 TYR   B CB   1 
ATOM   6370 C  CG   . TYR   B 1 152 ? 41.195 -22.626 -14.534 1.00 12.81 ?  152 TYR   B CG   1 
ATOM   6371 C  CD1  . TYR   B 1 152 ? 40.529 -21.402 -14.604 1.00 13.14 ?  152 TYR   B CD1  1 
ATOM   6372 C  CD2  . TYR   B 1 152 ? 41.193 -23.436 -15.658 1.00 13.96 ?  152 TYR   B CD2  1 
ATOM   6373 C  CE1  . TYR   B 1 152 ? 39.885 -21.007 -15.765 1.00 14.26 ?  152 TYR   B CE1  1 
ATOM   6374 C  CE2  . TYR   B 1 152 ? 40.553 -23.052 -16.818 1.00 14.68 ?  152 TYR   B CE2  1 
ATOM   6375 C  CZ   . TYR   B 1 152 ? 39.903 -21.837 -16.871 1.00 14.90 ?  152 TYR   B CZ   1 
ATOM   6376 O  OH   . TYR   B 1 152 ? 39.273 -21.471 -18.036 1.00 17.39 ?  152 TYR   B OH   1 
ATOM   6377 H  H    . TYR   B 1 152 ? 40.429 -22.148 -11.395 1.00 13.38 ?  152 TYR   B H    1 
ATOM   6378 H  HA   . TYR   B 1 152 ? 40.398 -24.463 -12.815 1.00 13.89 ?  152 TYR   B HA   1 
ATOM   6379 H  HB2  . TYR   B 1 152 ? 42.241 -22.311 -12.816 1.00 14.75 ?  152 TYR   B HB2  1 
ATOM   6380 H  HB3  . TYR   B 1 152 ? 42.589 -23.700 -13.506 1.00 14.75 ?  152 TYR   B HB3  1 
ATOM   6381 H  HD1  . TYR   B 1 152 ? 40.512 -20.848 -13.857 1.00 15.81 ?  152 TYR   B HD1  1 
ATOM   6382 H  HD2  . TYR   B 1 152 ? 41.625 -24.262 -15.628 1.00 16.80 ?  152 TYR   B HD2  1 
ATOM   6383 H  HE1  . TYR   B 1 152 ? 39.449 -20.187 -15.802 1.00 17.15 ?  152 TYR   B HE1  1 
ATOM   6384 H  HE2  . TYR   B 1 152 ? 40.570 -23.608 -17.563 1.00 17.66 ?  152 TYR   B HE2  1 
ATOM   6385 H  HH   . TYR   B 1 152 ? 38.923 -20.713 -17.940 1.00 20.91 ?  152 TYR   B HH   1 
ATOM   6386 N  N    . LEU   B 1 153 ? 41.259 -25.732 -10.886 1.00 11.13 ?  153 LEU   B N    1 
ATOM   6387 C  CA   . LEU   B 1 153 ? 41.764 -26.478 -9.744  1.00 10.88 ?  153 LEU   B CA   1 
ATOM   6388 C  C    . LEU   B 1 153 ? 42.998 -27.276 -10.136 1.00 11.17 ?  153 LEU   B C    1 
ATOM   6389 O  O    . LEU   B 1 153 ? 42.984 -28.003 -11.133 1.00 12.27 ?  153 LEU   B O    1 
ATOM   6390 C  CB   . LEU   B 1 153 ? 40.685 -27.438 -9.237  1.00 11.45 ?  153 LEU   B CB   1 
ATOM   6391 C  CG   . LEU   B 1 153 ? 39.430 -26.781 -8.664  1.00 12.20 ?  153 LEU   B CG   1 
ATOM   6392 C  CD1  . LEU   B 1 153 ? 38.327 -27.821 -8.516  1.00 13.37 ?  153 LEU   B CD1  1 
ATOM   6393 C  CD2  . LEU   B 1 153 ? 39.741 -26.113 -7.327  1.00 12.46 ?  153 LEU   B CD2  1 
ATOM   6394 H  H    . LEU   B 1 153 ? 40.696 -26.182 -11.368 1.00 13.40 ?  153 LEU   B H    1 
ATOM   6395 H  HA   . LEU   B 1 153 ? 41.990 -25.862 -9.035  1.00 13.10 ?  153 LEU   B HA   1 
ATOM   6396 H  HB2  . LEU   B 1 153 ? 40.404 -28.005 -9.972  1.00 13.79 ?  153 LEU   B HB2  1 
ATOM   6397 H  HB3  . LEU   B 1 153 ? 41.070 -27.987 -8.535  1.00 13.79 ?  153 LEU   B HB3  1 
ATOM   6398 H  HG   . LEU   B 1 153 ? 39.122 -26.089 -9.276  1.00 14.69 ?  153 LEU   B HG   1 
ATOM   6399 H  HD11 . LEU   B 1 153 ? 37.524 -27.379 -8.190  1.00 16.09 ?  153 LEU   B HD11 1 
ATOM   6400 H  HD12 . LEU   B 1 153 ? 38.156 -28.217 -9.382  1.00 16.09 ?  153 LEU   B HD12 1 
ATOM   6401 H  HD13 . LEU   B 1 153 ? 38.615 -28.493 -7.886  1.00 16.09 ?  153 LEU   B HD13 1 
ATOM   6402 H  HD21 . LEU   B 1 153 ? 38.927 -25.752 -6.953  1.00 14.99 ?  153 LEU   B HD21 1 
ATOM   6403 H  HD22 . LEU   B 1 153 ? 40.119 -26.779 -6.727  1.00 14.99 ?  153 LEU   B HD22 1 
ATOM   6404 H  HD23 . LEU   B 1 153 ? 40.387 -25.401 -7.471  1.00 14.99 ?  153 LEU   B HD23 1 
ATOM   6405 N  N    . ALA   B 1 154 ? 44.046 -27.170 -9.328  1.00 11.25 ?  154 ALA   B N    1 
ATOM   6406 C  CA   . ALA   B 1 154 ? 45.277 -27.928 -9.512  1.00 12.47 ?  154 ALA   B CA   1 
ATOM   6407 C  C    . ALA   B 1 154 ? 45.344 -29.006 -8.439  1.00 12.88 ?  154 ALA   B C    1 
ATOM   6408 O  O    . ALA   B 1 154 ? 45.264 -28.709 -7.240  1.00 13.97 ?  154 ALA   B O    1 
ATOM   6409 C  CB   . ALA   B 1 154 ? 46.495 -27.009 -9.438  1.00 13.57 ?  154 ALA   B CB   1 
ATOM   6410 H  H    . ALA   B 1 154 ? 44.065 -26.643 -8.644  1.00 13.54 ?  154 ALA   B H    1 
ATOM   6411 H  HA   . ALA   B 1 154 ? 45.272 -28.352 -10.379 1.00 15.01 ?  154 ALA   B HA   1 
ATOM   6412 H  HB1  . ALA   B 1 154 ? 47.304 -27.535 -9.560  1.00 16.33 ?  154 ALA   B HB1  1 
ATOM   6413 H  HB2  . ALA   B 1 154 ? 46.436 -26.335 -10.136 1.00 16.33 ?  154 ALA   B HB2  1 
ATOM   6414 H  HB3  . ALA   B 1 154 ? 46.521 -26.573 -8.567  1.00 16.33 ?  154 ALA   B HB3  1 
ATOM   6415 N  N    . VAL   B 1 155 ? 45.468 -30.255 -8.870  1.00 12.26 ?  155 VAL   B N    1 
ATOM   6416 C  CA   . VAL   B 1 155 ? 45.573 -31.404 -7.977  1.00 12.45 ?  155 VAL   B CA   1 
ATOM   6417 C  C    . VAL   B 1 155 ? 46.914 -32.077 -8.256  1.00 12.48 ?  155 VAL   B C    1 
ATOM   6418 O  O    . VAL   B 1 155 ? 47.152 -32.569 -9.368  1.00 14.45 ?  155 VAL   B O    1 
ATOM   6419 C  CB   . VAL   B 1 155 ? 44.418 -32.399 -8.176  1.00 14.12 ?  155 VAL   B CB   1 
ATOM   6420 C  CG1  . VAL   B 1 155 ? 44.607 -33.604 -7.271  1.00 13.71 ?  155 VAL   B CG1  1 
ATOM   6421 C  CG2  . VAL   B 1 155 ? 43.080 -31.711 -7.910  1.00 15.06 ?  155 VAL   B CG2  1 
ATOM   6422 H  H    . VAL   B 1 155 ? 45.508 -30.467 -9.704  1.00 14.76 ?  155 VAL   B H    1 
ATOM   6423 H  HA   . VAL   B 1 155 ? 45.564 -31.102 -7.056  1.00 14.98 ?  155 VAL   B HA   1 
ATOM   6424 H  HB   . VAL   B 1 155 ? 44.419 -32.703 -9.097  1.00 16.98 ?  155 VAL   B HB   1 
ATOM   6425 H  HG11 . VAL   B 1 155 ? 43.778 -34.106 -7.233  1.00 16.49 ?  155 VAL   B HG11 1 
ATOM   6426 H  HG12 . VAL   B 1 155 ? 45.313 -34.168 -7.632  1.00 16.49 ?  155 VAL   B HG12 1 
ATOM   6427 H  HG13 . VAL   B 1 155 ? 44.850 -33.303 -6.381  1.00 16.49 ?  155 VAL   B HG13 1 
ATOM   6428 H  HG21 . VAL   B 1 155 ? 42.368 -32.367 -8.008  1.00 18.12 ?  155 VAL   B HG21 1 
ATOM   6429 H  HG22 . VAL   B 1 155 ? 43.079 -31.359 -7.007  1.00 18.12 ?  155 VAL   B HG22 1 
ATOM   6430 H  HG23 . VAL   B 1 155 ? 42.956 -30.994 -8.549  1.00 18.12 ?  155 VAL   B HG23 1 
ATOM   6431 N  N    . PHE   B 1 156 ? 47.782 -32.117 -7.242  1.00 13.08 ?  156 PHE   B N    1 
ATOM   6432 C  CA   . PHE   B 1 156 ? 49.161 -32.569 -7.443  1.00 14.25 ?  156 PHE   B CA   1 
ATOM   6433 C  C    . PHE   B 1 156 ? 49.259 -34.069 -7.724  1.00 15.43 ?  156 PHE   B C    1 
ATOM   6434 O  O    . PHE   B 1 156 ? 49.984 -34.494 -8.634  1.00 17.21 ?  156 PHE   B O    1 
ATOM   6435 C  CB   . PHE   B 1 156 ? 49.992 -32.196 -6.219  1.00 14.26 ?  156 PHE   B CB   1 
ATOM   6436 C  CG   . PHE   B 1 156 ? 51.419 -32.660 -6.278  1.00 14.82 ?  156 PHE   B CG   1 
ATOM   6437 C  CD1  . PHE   B 1 156 ? 52.300 -32.123 -7.197  1.00 16.55 ?  156 PHE   B CD1  1 
ATOM   6438 C  CD2  . PHE   B 1 156 ? 51.879 -33.616 -5.396  1.00 14.86 ?  156 PHE   B CD2  1 
ATOM   6439 C  CE1  . PHE   B 1 156 ? 53.620 -32.534 -7.242  1.00 17.38 ?  156 PHE   B CE1  1 
ATOM   6440 C  CE2  . PHE   B 1 156 ? 53.200 -34.031 -5.436  1.00 16.45 ?  156 PHE   B CE2  1 
ATOM   6441 C  CZ   . PHE   B 1 156 ? 54.062 -33.494 -6.365  1.00 17.17 ?  156 PHE   B CZ   1 
ATOM   6442 H  H    . PHE   B 1 156 ? 47.596 -31.899 -6.430  1.00 15.74 ?  156 PHE   B H    1 
ATOM   6443 H  HA   . PHE   B 1 156 ? 49.529 -32.104 -8.204  1.00 17.14 ?  156 PHE   B HA   1 
ATOM   6444 H  HB2  . PHE   B 1 156 ? 50.004 -31.227 -6.140  1.00 17.15 ?  156 PHE   B HB2  1 
ATOM   6445 H  HB3  . PHE   B 1 156 ? 49.589 -32.584 -5.430  1.00 17.15 ?  156 PHE   B HB3  1 
ATOM   6446 H  HD1  . PHE   B 1 156 ? 52.008 -31.468 -7.792  1.00 19.91 ?  156 PHE   B HD1  1 
ATOM   6447 H  HD2  . PHE   B 1 156 ? 51.292 -33.985 -4.773  1.00 17.88 ?  156 PHE   B HD2  1 
ATOM   6448 H  HE1  . PHE   B 1 156 ? 54.206 -32.167 -7.867  1.00 20.89 ?  156 PHE   B HE1  1 
ATOM   6449 H  HE2  . PHE   B 1 156 ? 53.496 -34.688 -4.845  1.00 19.78 ?  156 PHE   B HE2  1 
ATOM   6450 H  HZ   . PHE   B 1 156 ? 54.949 -33.777 -6.395  1.00 20.65 ?  156 PHE   B HZ   1 
ATOM   6451 N  N    . ASP   B 1 157 ? 48.593 -34.892 -6.925  1.00 15.66 ?  157 ASP   B N    1 
ATOM   6452 C  CA   . ASP   B 1 157 ? 48.743 -36.339 -7.028  1.00 16.95 ?  157 ASP   B CA   1 
ATOM   6453 C  C    . ASP   B 1 157 ? 47.825 -36.882 -8.119  1.00 17.12 ?  157 ASP   B C    1 
ATOM   6454 O  O    . ASP   B 1 157 ? 46.598 -36.761 -8.018  1.00 16.35 ?  157 ASP   B O    1 
ATOM   6455 C  CB   . ASP   B 1 157 ? 48.380 -36.959 -5.684  1.00 18.41 ?  157 ASP   B CB   1 
ATOM   6456 C  CG   . ASP   B 1 157 ? 48.526 -38.470 -5.672  1.00 20.48 ?  157 ASP   B CG   1 
ATOM   6457 O  OD1  . ASP   B 1 157 ? 48.872 -39.072 -6.717  1.00 21.22 ?  157 ASP   B OD1  1 
ATOM   6458 O  OD2  . ASP   B 1 157 ? 48.306 -39.054 -4.593  1.00 22.50 -1 157 ASP   B OD2  1 
ATOM   6459 H  H    . ASP   B 1 157 ? 48.054 -34.644 -6.312  1.00 18.83 ?  157 ASP   B H    1 
ATOM   6460 H  HA   . ASP   B 1 157 ? 49.663 -36.574 -7.244  1.00 20.38 ?  157 ASP   B HA   1 
ATOM   6461 H  HB2  . ASP   B 1 157 ? 48.956 -36.584 -5.001  1.00 22.13 ?  157 ASP   B HB2  1 
ATOM   6462 H  HB3  . ASP   B 1 157 ? 47.453 -36.751 -5.484  1.00 22.13 ?  157 ASP   B HB3  1 
ATOM   6463 N  N    . LYS   B 1 158 ? 48.417 -37.504 -9.147  1.00 18.46 ?  158 LYS   B N    1 
ATOM   6464 C  CA   . LYS   B 1 158 ? 47.638 -38.109 -10.231 1.00 19.31 ?  158 LYS   B CA   1 
ATOM   6465 C  C    . LYS   B 1 158 ? 46.577 -39.076 -9.707  1.00 18.83 ?  158 LYS   B C    1 
ATOM   6466 O  O    . LYS   B 1 158 ? 45.472 -39.160 -10.258 1.00 18.82 ?  158 LYS   B O    1 
ATOM   6467 C  CB   . LYS   B 1 158 ? 48.586 -38.814 -11.212 1.00 21.01 ?  158 LYS   B CB   1 
ATOM   6468 C  CG   . LYS   B 1 158 ? 47.910 -39.721 -12.231 1.00 22.91 ?  158 LYS   B CG   1 
ATOM   6469 C  CD   . LYS   B 1 158 ? 47.037 -38.952 -13.199 1.00 25.09 ?  158 LYS   B CD   1 
ATOM   6470 C  CE   . LYS   B 1 158 ? 46.448 -39.884 -14.244 1.00 26.49 ?  158 LYS   B CE   1 
ATOM   6471 N  NZ   . LYS   B 1 158 ? 45.371 -39.228 -15.036 1.00 26.65 ?  158 LYS   B NZ   1 
ATOM   6472 H  H    . LYS   B 1 158 ? 49.271 -37.593 -9.240  1.00 22.19 ?  158 LYS   B H    1 
ATOM   6473 H  HA   . LYS   B 1 158 ? 47.185 -37.406 -10.722 1.00 23.22 ?  158 LYS   B HA   1 
ATOM   6474 H  HB2  . LYS   B 1 158 ? 49.076 -38.138 -11.714 1.00 25.26 ?  158 LYS   B HB2  1 
ATOM   6475 H  HB3  . LYS   B 1 158 ? 49.211 -39.357 -10.709 1.00 25.26 ?  158 LYS   B HB3  1 
ATOM   6476 H  HG2  . LYS   B 1 158 ? 48.595 -40.174 -12.749 1.00 27.54 ?  158 LYS   B HG2  1 
ATOM   6477 H  HG3  . LYS   B 1 158 ? 47.361 -40.382 -11.778 1.00 27.54 ?  158 LYS   B HG3  1 
ATOM   6478 H  HD2  . LYS   B 1 158 ? 46.308 -38.533 -12.715 1.00 30.16 ?  158 LYS   B HD2  1 
ATOM   6479 H  HD3  . LYS   B 1 158 ? 47.571 -38.282 -13.654 1.00 30.16 ?  158 LYS   B HD3  1 
ATOM   6480 H  HE2  . LYS   B 1 158 ? 47.145 -40.160 -14.857 1.00 31.83 ?  158 LYS   B HE2  1 
ATOM   6481 H  HE3  . LYS   B 1 158 ? 46.066 -40.660 -13.802 1.00 31.83 ?  158 LYS   B HE3  1 
ATOM   6482 H  HZ1  . LYS   B 1 158 ? 45.044 -39.796 -15.638 1.00 32.02 ?  158 LYS   B HZ1  1 
ATOM   6483 H  HZ2  . LYS   B 1 158 ? 44.711 -38.967 -14.497 1.00 32.02 ?  158 LYS   B HZ2  1 
ATOM   6484 H  HZ3  . LYS   B 1 158 ? 45.696 -38.515 -15.459 1.00 32.02 ?  158 LYS   B HZ3  1 
ATOM   6485 N  N    A ASN   B 1 159 ? 46.900 -39.831 -8.656  0.60 18.93 ?  159 ASN   B N    1 
ATOM   6486 N  N    B ASN   B 1 159 ? 46.893 -39.823 -8.648  0.40 18.71 ?  159 ASN   B N    1 
ATOM   6487 C  CA   A ASN   B 1 159 ? 45.949 -40.813 -8.143  0.60 19.47 ?  159 ASN   B CA   1 
ATOM   6488 C  CA   B ASN   B 1 159 ? 45.943 -40.814 -8.151  0.40 18.89 ?  159 ASN   B CA   1 
ATOM   6489 C  C    A ASN   B 1 159 ? 44.746 -40.136 -7.488  0.60 18.46 ?  159 ASN   B C    1 
ATOM   6490 C  C    B ASN   B 1 159 ? 44.755 -40.162 -7.446  0.40 18.20 ?  159 ASN   B C    1 
ATOM   6491 O  O    A ASN   B 1 159 ? 43.610 -40.612 -7.618  0.60 18.86 ?  159 ASN   B O    1 
ATOM   6492 O  O    B ASN   B 1 159 ? 43.639 -40.693 -7.497  0.40 18.52 ?  159 ASN   B O    1 
ATOM   6493 C  CB   A ASN   B 1 159 ? 46.652 -41.770 -7.182  0.60 21.07 ?  159 ASN   B CB   1 
ATOM   6494 C  CB   B ASN   B 1 159 ? 46.657 -41.813 -7.243  0.40 19.84 ?  159 ASN   B CB   1 
ATOM   6495 C  CG   A ASN   B 1 159 ? 47.673 -42.649 -7.880  0.60 23.00 ?  159 ASN   B CG   1 
ATOM   6496 C  CG   B ASN   B 1 159 ? 47.711 -42.619 -7.980  0.40 21.16 ?  159 ASN   B CG   1 
ATOM   6497 O  OD1  A ASN   B 1 159 ? 47.419 -43.178 -8.969  0.60 23.72 ?  159 ASN   B OD1  1 
ATOM   6498 O  OD1  B ASN   B 1 159 ? 47.503 -43.042 -9.120  0.40 21.78 ?  159 ASN   B OD1  1 
ATOM   6499 N  ND2  A ASN   B 1 159 ? 48.833 -42.820 -7.252  0.60 23.79 ?  159 ASN   B ND2  1 
ATOM   6500 N  ND2  B ASN   B 1 159 ? 48.849 -42.839 -7.331  0.40 21.72 ?  159 ASN   B ND2  1 
ATOM   6501 H  H    A ASN   B 1 159 ? 47.648 -39.788 -8.236  0.60 22.76 ?  159 ASN   B H    1 
ATOM   6502 H  H    B ASN   B 1 159 ? 47.631 -39.771 -8.214  0.40 22.50 ?  159 ASN   B H    1 
ATOM   6503 H  HA   A ASN   B 1 159 ? 45.624 -41.338 -8.893  0.60 23.41 ?  159 ASN   B HA   1 
ATOM   6504 H  HA   B ASN   B 1 159 ? 45.598 -41.309 -8.912  0.40 22.72 ?  159 ASN   B HA   1 
ATOM   6505 H  HB2  A ASN   B 1 159 ? 47.113 -41.255 -6.503  0.60 25.33 ?  159 ASN   B HB2  1 
ATOM   6506 H  HB2  B ASN   B 1 159 ? 47.096 -41.333 -6.526  0.40 23.86 ?  159 ASN   B HB2  1 
ATOM   6507 H  HB3  A ASN   B 1 159 ? 45.992 -42.349 -6.778  0.60 25.33 ?  159 ASN   B HB3  1 
ATOM   6508 H  HB3  B ASN   B 1 159 ? 46.003 -42.431 -6.882  0.40 23.86 ?  159 ASN   B HB3  1 
ATOM   6509 H  HD21 A ASN   B 1 159 ? 49.448 -43.309 -7.606  0.60 28.60 ?  159 ASN   B HD21 1 
ATOM   6510 H  HD21 B ASN   B 1 159 ? 49.477 -43.294 -7.705  0.40 26.11 ?  159 ASN   B HD21 1 
ATOM   6511 H  HD22 A ASN   B 1 159 ? 48.969 -42.450 -6.487  0.60 28.60 ?  159 ASN   B HD22 1 
ATOM   6512 H  HD22 B ASN   B 1 159 ? 48.957 -42.533 -6.535  0.40 26.11 ?  159 ASN   B HD22 1 
ATOM   6513 N  N    . LEU   B 1 160 ? 44.963 -39.014 -6.794  1.00 17.75 ?  160 LEU   B N    1 
ATOM   6514 C  CA   . LEU   B 1 160 ? 43.834 -38.280 -6.237  1.00 16.76 ?  160 LEU   B CA   1 
ATOM   6515 C  C    . LEU   B 1 160 ? 43.040 -37.611 -7.345  1.00 15.90 ?  160 LEU   B C    1 
ATOM   6516 O  O    . LEU   B 1 160 ? 41.803 -37.621 -7.322  1.00 15.48 ?  160 LEU   B O    1 
ATOM   6517 C  CB   . LEU   B 1 160 ? 44.303 -37.248 -5.215  1.00 16.35 ?  160 LEU   B CB   1 
ATOM   6518 C  CG   . LEU   B 1 160 ? 43.177 -36.354 -4.676  1.00 16.22 ?  160 LEU   B CG   1 
ATOM   6519 C  CD1  . LEU   B 1 160 ? 42.052 -37.184 -4.066  1.00 16.89 ?  160 LEU   B CD1  1 
ATOM   6520 C  CD2  . LEU   B 1 160 ? 43.726 -35.368 -3.658  1.00 16.32 ?  160 LEU   B CD2  1 
ATOM   6521 H  H    A LEU   B 1 160 ? 45.735 -38.668 -6.644  0.60 21.35 ?  160 LEU   B H    1 
ATOM   6522 H  H    B LEU   B 1 160 ? 45.732 -38.650 -6.672  0.40 21.35 ?  160 LEU   B H    1 
ATOM   6523 H  HA   . LEU   B 1 160 ? 43.247 -38.907 -5.793  1.00 20.15 ?  160 LEU   B HA   1 
ATOM   6524 H  HB2  . LEU   B 1 160 ? 44.703 -37.721 -4.467  1.00 19.66 ?  160 LEU   B HB2  1 
ATOM   6525 H  HB3  . LEU   B 1 160 ? 44.970 -36.679 -5.635  1.00 19.66 ?  160 LEU   B HB3  1 
ATOM   6526 H  HG   . LEU   B 1 160 ? 42.808 -35.844 -5.411  1.00 19.50 ?  160 LEU   B HG   1 
ATOM   6527 H  HD11 . LEU   B 1 160 ? 41.429 -36.590 -3.627  1.00 20.31 ?  160 LEU   B HD11 1 
ATOM   6528 H  HD12 . LEU   B 1 160 ? 41.600 -37.678 -4.770  1.00 20.31 ?  160 LEU   B HD12 1 
ATOM   6529 H  HD13 . LEU   B 1 160 ? 42.430 -37.805 -3.421  1.00 20.31 ?  160 LEU   B HD13 1 
ATOM   6530 H  HD21 . LEU   B 1 160 ? 43.005 -34.800 -3.357  1.00 19.62 ?  160 LEU   B HD21 1 
ATOM   6531 H  HD22 . LEU   B 1 160 ? 44.098 -35.863 -2.910  1.00 19.62 ?  160 LEU   B HD22 1 
ATOM   6532 H  HD23 . LEU   B 1 160 ? 44.420 -34.835 -4.078  1.00 19.62 ?  160 LEU   B HD23 1 
ATOM   6533 N  N    . TYR   B 1 161 ? 43.736 -37.032 -8.328  1.00 16.24 ?  161 TYR   B N    1 
ATOM   6534 C  CA   . TYR   B 1 161 ? 43.065 -36.469 -9.494  1.00 15.91 ?  161 TYR   B CA   1 
ATOM   6535 C  C    . TYR   B 1 161 ? 42.119 -37.492 -10.111 1.00 15.86 ?  161 TYR   B C    1 
ATOM   6536 O  O    . TYR   B 1 161 ? 40.946 -37.196 -10.362 1.00 15.63 ?  161 TYR   B O    1 
ATOM   6537 C  CB   . TYR   B 1 161 ? 44.108 -36.000 -10.519 1.00 16.59 ?  161 TYR   B CB   1 
ATOM   6538 C  CG   . TYR   B 1 161 ? 43.530 -35.530 -11.836 1.00 17.07 ?  161 TYR   B CG   1 
ATOM   6539 C  CD1  . TYR   B 1 161 ? 43.136 -34.209 -12.006 1.00 17.07 ?  161 TYR   B CD1  1 
ATOM   6540 C  CD2  . TYR   B 1 161 ? 43.363 -36.406 -12.905 1.00 17.75 ?  161 TYR   B CD2  1 
ATOM   6541 C  CE1  . TYR   B 1 161 ? 42.601 -33.772 -13.193 1.00 18.17 ?  161 TYR   B CE1  1 
ATOM   6542 C  CE2  . TYR   B 1 161 ? 42.826 -35.975 -14.100 1.00 18.92 ?  161 TYR   B CE2  1 
ATOM   6543 C  CZ   . TYR   B 1 161 ? 42.448 -34.655 -14.237 1.00 18.96 ?  161 TYR   B CZ   1 
ATOM   6544 O  OH   . TYR   B 1 161 ? 41.907 -34.211 -15.420 1.00 21.02 ?  161 TYR   B OH   1 
ATOM   6545 H  H    . TYR   B 1 161 ? 44.589 -36.958 -8.349  1.00 19.53 ?  161 TYR   B H    1 
ATOM   6546 H  HA   . TYR   B 1 161 ? 42.539 -35.700 -9.229  1.00 19.14 ?  161 TYR   B HA   1 
ATOM   6547 H  HB2  . TYR   B 1 161 ? 44.603 -35.255 -10.141 1.00 19.95 ?  161 TYR   B HB2  1 
ATOM   6548 H  HB3  . TYR   B 1 161 ? 44.711 -36.731 -10.713 1.00 19.95 ?  161 TYR   B HB3  1 
ATOM   6549 H  HD1  . TYR   B 1 161 ? 43.236 -33.603 -11.307 1.00 20.53 ?  161 TYR   B HD1  1 
ATOM   6550 H  HD2  . TYR   B 1 161 ? 43.611 -37.298 -12.818 1.00 21.35 ?  161 TYR   B HD2  1 
ATOM   6551 H  HE1  . TYR   B 1 161 ? 42.343 -32.879 -13.290 1.00 21.85 ?  161 TYR   B HE1  1 
ATOM   6552 H  HE2  . TYR   B 1 161 ? 42.714 -36.569 -14.807 1.00 22.75 ?  161 TYR   B HE2  1 
ATOM   6553 H  HH   . TYR   B 1 161 ? 41.863 -34.845 -15.971 1.00 25.26 ?  161 TYR   B HH   1 
ATOM   6554 N  N    . ASP   B 1 162 ? 42.615 -38.710 -10.348 1.00 16.53 ?  162 ASP   B N    1 
ATOM   6555 C  CA   . ASP   B 1 162 ? 41.789 -39.746 -10.961 1.00 16.98 ?  162 ASP   B CA   1 
ATOM   6556 C  C    . ASP   B 1 162 ? 40.583 -40.083 -10.091 1.00 16.31 ?  162 ASP   B C    1 
ATOM   6557 O  O    . ASP   B 1 162 ? 39.481 -40.310 -10.605 1.00 16.81 ?  162 ASP   B O    1 
ATOM   6558 C  CB   . ASP   B 1 162 ? 42.620 -41.008 -11.213 1.00 18.43 ?  162 ASP   B CB   1 
ATOM   6559 C  CG   . ASP   B 1 162 ? 43.624 -40.847 -12.344 1.00 19.78 ?  162 ASP   B CG   1 
ATOM   6560 O  OD1  . ASP   B 1 162 ? 43.496 -39.902 -13.145 1.00 19.93 ?  162 ASP   B OD1  1 
ATOM   6561 O  OD2  . ASP   B 1 162 ? 44.531 -41.698 -12.449 1.00 21.56 -1 162 ASP   B OD2  1 
ATOM   6562 H  H    . ASP   B 1 162 ? 43.416 -38.952 -10.168 1.00 19.88 ?  162 ASP   B H    1 
ATOM   6563 H  HA   . ASP   B 1 162 ? 41.460 -39.428 -11.814 1.00 20.42 ?  162 ASP   B HA   1 
ATOM   6564 H  HB2  . ASP   B 1 162 ? 43.116 -41.225 -10.409 1.00 22.16 ?  162 ASP   B HB2  1 
ATOM   6565 H  HB3  . ASP   B 1 162 ? 42.026 -41.736 -11.447 1.00 22.16 ?  162 ASP   B HB3  1 
ATOM   6566 N  N    . LYS   B 1 163 ? 40.777 -40.157 -8.773  1.00 15.83 ?  163 LYS   B N    1 
ATOM   6567 C  CA   . LYS   B 1 163 ? 39.655 -40.437 -7.882  1.00 16.50 ?  163 LYS   B CA   1 
ATOM   6568 C  C    . LYS   B 1 163 ? 38.610 -39.328 -7.942  1.00 15.04 ?  163 LYS   B C    1 
ATOM   6569 O  O    . LYS   B 1 163 ? 37.400 -39.599 -7.946  1.00 15.89 ?  163 LYS   B O    1 
ATOM   6570 C  CB   . LYS   B 1 163 ? 40.149 -40.619 -6.450  1.00 19.69 ?  163 LYS   B CB   1 
ATOM   6571 C  CG   . LYS   B 1 163 ? 39.067 -41.123 -5.520  1.00 25.66 ?  163 LYS   B CG   1 
ATOM   6572 C  CD   . LYS   B 1 163 ? 39.549 -41.294 -4.094  1.00 31.74 ?  163 LYS   B CD   1 
ATOM   6573 C  CE   . LYS   B 1 163 ? 38.464 -41.947 -3.248  1.00 36.51 ?  163 LYS   B CE   1 
ATOM   6574 N  NZ   . LYS   B 1 163 ? 38.591 -41.624 -1.800  1.00 39.45 ?  163 LYS   B NZ   1 
ATOM   6575 H  H    . LYS   B 1 163 ? 41.538 -40.057 -8.382  1.00 19.04 ?  163 LYS   B H    1 
ATOM   6576 H  HA   . LYS   B 1 163 ? 39.235 -41.264 -8.163  1.00 19.84 ?  163 LYS   B HA   1 
ATOM   6577 H  HB2  . LYS   B 1 163 ? 40.876 -41.263 -6.445  1.00 23.67 ?  163 LYS   B HB2  1 
ATOM   6578 H  HB3  . LYS   B 1 163 ? 40.461 -39.765 -6.114  1.00 23.67 ?  163 LYS   B HB3  1 
ATOM   6579 H  HG2  . LYS   B 1 163 ? 38.333 -40.491 -5.514  1.00 30.84 ?  163 LYS   B HG2  1 
ATOM   6580 H  HG3  . LYS   B 1 163 ? 38.757 -41.988 -5.839  1.00 30.84 ?  163 LYS   B HG3  1 
ATOM   6581 H  HD2  . LYS   B 1 163 ? 40.333 -41.868 -4.084  1.00 38.13 ?  163 LYS   B HD2  1 
ATOM   6582 H  HD3  . LYS   B 1 163 ? 39.758 -40.427 -3.716  1.00 38.13 ?  163 LYS   B HD3  1 
ATOM   6583 H  HE2  . LYS   B 1 163 ? 37.595 -41.645 -3.554  1.00 43.86 ?  163 LYS   B HE2  1 
ATOM   6584 H  HE3  . LYS   B 1 163 ? 38.528 -42.909 -3.344  1.00 43.86 ?  163 LYS   B HE3  1 
ATOM   6585 H  HZ1  . LYS   B 1 163 ? 37.939 -42.021 -1.343  1.00 47.39 ?  163 LYS   B HZ1  1 
ATOM   6586 H  HZ2  . LYS   B 1 163 ? 39.375 -41.909 -1.494  1.00 47.39 ?  163 LYS   B HZ2  1 
ATOM   6587 H  HZ3  . LYS   B 1 163 ? 38.534 -40.744 -1.679  1.00 47.39 ?  163 LYS   B HZ3  1 
ATOM   6588 N  N    . LEU   B 1 164 ? 39.061 -38.075 -7.991  1.00 14.12 ?  164 LEU   B N    1 
ATOM   6589 C  CA   . LEU   B 1 164 ? 38.148 -36.937 -8.049  1.00 13.82 ?  164 LEU   B CA   1 
ATOM   6590 C  C    . LEU   B 1 164 ? 37.368 -36.920 -9.358  1.00 14.00 ?  164 LEU   B C    1 
ATOM   6591 O  O    . LEU   B 1 164 ? 36.145 -36.723 -9.362  1.00 15.25 ?  164 LEU   B O    1 
ATOM   6592 C  CB   . LEU   B 1 164 ? 38.943 -35.642 -7.891  1.00 13.43 ?  164 LEU   B CB   1 
ATOM   6593 C  CG   . LEU   B 1 164 ? 39.474 -35.362 -6.489  1.00 14.32 ?  164 LEU   B CG   1 
ATOM   6594 C  CD1  . LEU   B 1 164 ? 40.557 -34.290 -6.537  1.00 14.39 ?  164 LEU   B CD1  1 
ATOM   6595 C  CD2  . LEU   B 1 164 ? 38.360 -34.935 -5.562  1.00 15.98 ?  164 LEU   B CD2  1 
ATOM   6596 H  H    . LEU   B 1 164 ? 39.898 -37.858 -7.996  1.00 16.99 ?  164 LEU   B H    1 
ATOM   6597 H  HA   . LEU   B 1 164 ? 37.520 -36.999 -7.322  1.00 16.62 ?  164 LEU   B HA   1 
ATOM   6598 H  HB2  . LEU   B 1 164 ? 39.710 -35.674 -8.492  1.00 16.16 ?  164 LEU   B HB2  1 
ATOM   6599 H  HB3  . LEU   B 1 164 ? 38.375 -34.899 -8.141  1.00 16.16 ?  164 LEU   B HB3  1 
ATOM   6600 H  HG   . LEU   B 1 164 ? 39.877 -36.166 -6.135  1.00 17.23 ?  164 LEU   B HG   1 
ATOM   6601 H  HD11 . LEU   B 1 164 ? 40.880 -34.119 -5.635  1.00 17.31 ?  164 LEU   B HD11 1 
ATOM   6602 H  HD12 . LEU   B 1 164 ? 41.295 -34.600 -7.091  1.00 17.31 ?  164 LEU   B HD12 1 
ATOM   6603 H  HD13 . LEU   B 1 164 ? 40.189 -33.474 -6.912  1.00 17.31 ?  164 LEU   B HD13 1 
ATOM   6604 H  HD21 . LEU   B 1 164 ? 38.735 -34.700 -4.700  1.00 19.22 ?  164 LEU   B HD21 1 
ATOM   6605 H  HD22 . LEU   B 1 164 ? 37.904 -34.169 -5.944  1.00 19.22 ?  164 LEU   B HD22 1 
ATOM   6606 H  HD23 . LEU   B 1 164 ? 37.738 -35.673 -5.462  1.00 19.22 ?  164 LEU   B HD23 1 
ATOM   6607 N  N    . VAL   B 1 165 ? 38.061 -37.092 -10.484 1.00 15.51 ?  165 VAL   B N    1 
ATOM   6608 C  CA   . VAL   B 1 165 ? 37.405 -37.030 -11.786 1.00 16.80 ?  165 VAL   B CA   1 
ATOM   6609 C  C    . VAL   B 1 165 ? 36.483 -38.230 -11.972 1.00 18.56 ?  165 VAL   B C    1 
ATOM   6610 O  O    . VAL   B 1 165 ? 35.325 -38.092 -12.384 1.00 19.76 ?  165 VAL   B O    1 
ATOM   6611 C  CB   . VAL   B 1 165 ? 38.453 -36.948 -12.912 1.00 17.62 ?  165 VAL   B CB   1 
ATOM   6612 C  CG1  . VAL   B 1 165 ? 37.794 -37.064 -14.267 1.00 18.71 ?  165 VAL   B CG1  1 
ATOM   6613 C  CG2  . VAL   B 1 165 ? 39.247 -35.662 -12.811 1.00 17.48 ?  165 VAL   B CG2  1 
ATOM   6614 H  H    . VAL   B 1 165 ? 38.911 -37.243 -10.522 1.00 18.65 ?  165 VAL   B H    1 
ATOM   6615 H  HA   . VAL   B 1 165 ? 36.864 -36.231 -11.828 1.00 20.20 ?  165 VAL   B HA   1 
ATOM   6616 H  HB   . VAL   B 1 165 ? 39.079 -37.683 -12.818 1.00 21.18 ?  165 VAL   B HB   1 
ATOM   6617 H  HG11 . VAL   B 1 165 ? 38.419 -36.770 -14.946 1.00 22.49 ?  165 VAL   B HG11 1 
ATOM   6618 H  HG12 . VAL   B 1 165 ? 37.559 -37.994 -14.420 1.00 22.49 ?  165 VAL   B HG12 1 
ATOM   6619 H  HG13 . VAL   B 1 165 ? 37.001 -36.513 -14.280 1.00 22.49 ?  165 VAL   B HG13 1 
ATOM   6620 H  HG21 . VAL   B 1 165 ? 39.883 -35.619 -13.544 1.00 21.02 ?  165 VAL   B HG21 1 
ATOM   6621 H  HG22 . VAL   B 1 165 ? 38.637 -34.906 -12.863 1.00 21.02 ?  165 VAL   B HG22 1 
ATOM   6622 H  HG23 . VAL   B 1 165 ? 39.721 -35.642 -11.964 1.00 21.02 ?  165 VAL   B HG23 1 
ATOM   6623 N  N    . SER   B 1 166 ? 36.991 -39.431 -11.671 1.00 19.25 ?  166 SER   B N    1 
ATOM   6624 C  CA   . SER   B 1 166 ? 36.240 -40.648 -11.955 1.00 20.41 ?  166 SER   B CA   1 
ATOM   6625 C  C    . SER   B 1 166 ? 34.981 -40.742 -11.110 1.00 20.74 ?  166 SER   B C    1 
ATOM   6626 O  O    . SER   B 1 166 ? 34.016 -41.382 -11.530 1.00 22.21 ?  166 SER   B O    1 
ATOM   6627 C  CB   . SER   B 1 166 ? 37.112 -41.896 -11.771 1.00 21.31 ?  166 SER   B CB   1 
ATOM   6628 O  OG   . SER   B 1 166 ? 37.453 -42.109 -10.411 1.00 21.50 ?  166 SER   B OG   1 
ATOM   6629 H  H    . SER   B 1 166 ? 37.766 -39.563 -11.312 1.00 23.14 ?  166 SER   B H    1 
ATOM   6630 H  HA   . SER   B 1 166 ? 35.970 -40.626 -12.884 1.00 24.53 ?  166 SER   B HA   1 
ATOM   6631 H  HB2  . SER   B 1 166 ? 36.622 -42.669 -12.094 1.00 25.61 ?  166 SER   B HB2  1 
ATOM   6632 H  HB3  . SER   B 1 166 ? 37.928 -41.788 -12.287 1.00 25.61 ?  166 SER   B HB3  1 
ATOM   6633 H  HG   . SER   B 1 166 ? 37.886 -41.451 -10.121 1.00 25.84 ?  166 SER   B HG   1 
ATOM   6634 N  N    . SER   B 1 167 ? 34.959 -40.124 -9.930  1.00 19.47 ?  167 SER   B N    1 
ATOM   6635 C  CA   . SER   B 1 167 ? 33.804 -40.182 -9.042  1.00 19.17 ?  167 SER   B CA   1 
ATOM   6636 C  C    . SER   B 1 167 ? 32.886 -38.961 -9.141  1.00 18.72 ?  167 SER   B C    1 
ATOM   6637 O  O    . SER   B 1 167 ? 31.808 -38.964 -8.533  1.00 19.06 ?  167 SER   B O    1 
ATOM   6638 C  CB   . SER   B 1 167 ? 34.253 -40.374 -7.587  1.00 19.16 ?  167 SER   B CB   1 
ATOM   6639 O  OG   . SER   B 1 167 ? 34.912 -39.212 -7.100  1.00 18.80 ?  167 SER   B OG   1 
ATOM   6640 H  H    . SER   B 1 167 ? 35.615 -39.672 -9.617  1.00 23.41 ?  167 SER   B H    1 
ATOM   6641 H  HA   . SER   B 1 167 ? 33.278 -40.962 -9.281  1.00 23.05 ?  167 SER   B HA   1 
ATOM   6642 H  HB2  . SER   B 1 167 ? 33.472 -40.556 -7.039  1.00 23.03 ?  167 SER   B HB2  1 
ATOM   6643 H  HB3  . SER   B 1 167 ? 34.862 -41.137 -7.545  1.00 23.03 ?  167 SER   B HB3  1 
ATOM   6644 H  HG   . SER   B 1 167 ? 35.594 -39.063 -7.566  1.00 22.60 ?  167 SER   B HG   1 
ATOM   6645 N  N    . PHE   B 1 168 ? 33.261 -37.929 -9.901  1.00 18.12 ?  168 PHE   B N    1 
ATOM   6646 C  CA   . PHE   B 1 168 ? 32.428 -36.726 -9.968  1.00 17.45 ?  168 PHE   B CA   1 
ATOM   6647 C  C    . PHE   B 1 168 ? 31.107 -36.991 -10.683 1.00 15.40 ?  168 PHE   B C    1 
ATOM   6648 O  O    . PHE   B 1 168 ? 30.065 -36.398 -10.335 1.00 16.09 ?  168 PHE   B O    1 
ATOM   6649 C  CB   . PHE   B 1 168 ? 33.183 -35.597 -10.668 1.00 18.13 ?  168 PHE   B CB   1 
ATOM   6650 C  CG   . PHE   B 1 168 ? 32.384 -34.339 -10.786 1.00 17.89 ?  168 PHE   B CG   1 
ATOM   6651 C  CD1  . PHE   B 1 168 ? 32.060 -33.611 -9.649  1.00 18.81 ?  168 PHE   B CD1  1 
ATOM   6652 C  CD2  . PHE   B 1 168 ? 31.924 -33.901 -12.012 1.00 17.19 ?  168 PHE   B CD2  1 
ATOM   6653 C  CE1  . PHE   B 1 168 ? 31.300 -32.460 -9.732  1.00 19.45 ?  168 PHE   B CE1  1 
ATOM   6654 C  CE2  . PHE   B 1 168 ? 31.179 -32.728 -12.108 1.00 18.27 ?  168 PHE   B CE2  1 
ATOM   6655 C  CZ   . PHE   B 1 168 ? 30.860 -32.011 -10.963 1.00 18.84 ?  168 PHE   B CZ   1 
ATOM   6656 H  H    . PHE   B 1 168 ? 33.980 -37.903 -10.373 1.00 21.78 ?  168 PHE   B H    1 
ATOM   6657 H  HA   . PHE   B 1 168 ? 32.223 -36.438 -9.070  1.00 20.98 ?  168 PHE   B HA   1 
ATOM   6658 H  HB2  . PHE   B 1 168 ? 33.982 -35.394 -10.161 1.00 21.79 ?  168 PHE   B HB2  1 
ATOM   6659 H  HB3  . PHE   B 1 168 ? 33.419 -35.883 -11.563 1.00 21.79 ?  168 PHE   B HB3  1 
ATOM   6660 H  HD1  . PHE   B 1 168 ? 32.349 -33.914 -8.819  1.00 22.62 ?  168 PHE   B HD1  1 
ATOM   6661 H  HD2  . PHE   B 1 168 ? 32.135 -34.372 -12.782 1.00 20.67 ?  168 PHE   B HD2  1 
ATOM   6662 H  HE1  . PHE   B 1 168 ? 31.092 -31.984 -8.962  1.00 23.38 ?  168 PHE   B HE1  1 
ATOM   6663 H  HE2  . PHE   B 1 168 ? 30.874 -32.436 -12.940 1.00 21.97 ?  168 PHE   B HE2  1 
ATOM   6664 H  HZ   . PHE   B 1 168 ? 30.349 -31.234 -11.027 1.00 22.66 ?  168 PHE   B HZ   1 
ATOM   6665 N  N    . LEU   B 1 169 ? 31.136 -37.870 -11.680 1.00 15.82 ?  169 LEU   B N    1 
ATOM   6666 C  CA   . LEU   B 1 169 ? 29.962 -38.186 -12.484 1.00 17.93 ?  169 LEU   B CA   1 
ATOM   6667 C  C    . LEU   B 1 169 ? 29.965 -39.622 -12.990 1.00 20.69 ?  169 LEU   B C    1 
ATOM   6668 O  O    . LEU   B 1 169 ? 29.048 -40.052 -13.694 1.00 23.07 ?  169 LEU   B O    1 
ATOM   6669 C  CB   . LEU   B 1 169 ? 29.881 -37.240 -13.679 1.00 19.65 ?  169 LEU   B CB   1 
ATOM   6670 C  CG   . LEU   B 1 169 ? 28.617 -36.390 -13.796 1.00 22.57 ?  169 LEU   B CG   1 
ATOM   6671 C  CD1  . LEU   B 1 169 ? 28.572 -35.753 -15.167 1.00 23.38 ?  169 LEU   B CD1  1 
ATOM   6672 C  CD2  . LEU   B 1 169 ? 27.361 -37.204 -13.538 1.00 22.45 ?  169 LEU   B CD2  1 
ATOM   6673 O  OXT  . LEU   B 1 169 ? 30.893 -40.369 -12.708 1.00 21.35 -1 169 LEU   B OXT  1 
ATOM   6674 H  H    . LEU   B 1 169 ? 31.842 -38.299 -11.927 1.00 19.02 ?  169 LEU   B H    1 
ATOM   6675 H  HA   . LEU   B 1 169 ? 29.175 -38.064 -11.939 1.00 21.56 ?  169 LEU   B HA   1 
ATOM   6676 H  HB2  . LEU   B 1 169 ? 30.631 -36.627 -13.639 1.00 23.62 ?  169 LEU   B HB2  1 
ATOM   6677 H  HB3  . LEU   B 1 169 ? 29.941 -37.765 -14.493 1.00 23.62 ?  169 LEU   B HB3  1 
ATOM   6678 H  HG   . LEU   B 1 169 ? 28.652 -35.675 -13.139 1.00 27.13 ?  169 LEU   B HG   1 
ATOM   6679 H  HD11 . LEU   B 1 169 ? 27.785 -35.189 -15.226 1.00 28.10 ?  169 LEU   B HD11 1 
ATOM   6680 H  HD12 . LEU   B 1 169 ? 29.372 -35.222 -15.293 1.00 28.10 ?  169 LEU   B HD12 1 
ATOM   6681 H  HD13 . LEU   B 1 169 ? 28.528 -36.454 -15.835 1.00 28.10 ?  169 LEU   B HD13 1 
ATOM   6682 H  HD21 . LEU   B 1 169 ? 26.607 -36.773 -13.965 1.00 26.98 ?  169 LEU   B HD21 1 
ATOM   6683 H  HD22 . LEU   B 1 169 ? 27.485 -38.096 -13.903 1.00 26.98 ?  169 LEU   B HD22 1 
ATOM   6684 H  HD23 . LEU   B 1 169 ? 27.215 -37.258 -12.581 1.00 26.98 ?  169 LEU   B HD23 1 
HETATM 6685 C  C1   T TFA   C 2 .   ? 12.191 -1.366  1.561   0.30 12.00 ?  201 TFA   A C1   1 
HETATM 6686 C  C2   T TFA   C 2 .   ? 12.812 -1.758  0.191   0.30 14.37 ?  201 TFA   A C2   1 
HETATM 6687 O  O    T TFA   C 2 .   ? 12.926 -1.580  2.529   0.30 10.43 ?  201 TFA   A O    1 
HETATM 6688 F  F1   T TFA   C 2 .   ? 12.886 -3.098  0.114   0.30 15.16 ?  201 TFA   A F1   1 
HETATM 6689 F  F2   T TFA   C 2 .   ? 12.084 -1.349  -0.864  0.30 14.75 ?  201 TFA   A F2   1 
HETATM 6690 F  F3   T TFA   C 2 .   ? 14.045 -1.278  -0.011  0.30 15.51 ?  201 TFA   A F3   1 
HETATM 6691 O  OXT  T TFA   C 2 .   ? 11.053 -0.905  1.517   0.30 11.58 ?  201 TFA   A OXT  1 
HETATM 6692 N  N2   B A1A94 D 3 .   ? 14.832 -0.252  3.739   0.28 11.78 ?  202 A1A94 A N2   1 
HETATM 6693 C  C3   B A1A94 D 3 .   ? 14.238 -0.170  -0.527  0.28 13.70 ?  202 A1A94 A C3   1 
HETATM 6694 C  C6   B A1A94 D 3 .   ? 10.722 -0.071  -1.960  0.28 14.95 ?  202 A1A94 A C6   1 
HETATM 6695 C  C9   B A1A94 D 3 .   ? 12.423 1.601   -0.495  0.28 14.64 ?  202 A1A94 A C9   1 
HETATM 6696 C  C12  B A1A94 D 3 .   ? 15.343 2.055   5.115   0.28 10.91 ?  202 A1A94 A C12  1 
HETATM 6697 C  C14  B A1A94 D 3 .   ? 15.593 3.502   3.371   0.28 10.93 ?  202 A1A94 A C14  1 
HETATM 6698 C  C1   B A1A94 D 3 .   ? 15.977 -1.311  0.902   0.28 13.71 ?  202 A1A94 A C1   1 
HETATM 6699 C  C10  B A1A94 D 3 .   ? 15.046 0.898   3.028   0.28 11.16 ?  202 A1A94 A C10  1 
HETATM 6700 C  C11  B A1A94 D 3 .   ? 14.890 -0.160  5.102   0.28 11.85 ?  202 A1A94 A C11  1 
HETATM 6701 C  C13  B A1A94 D 3 .   ? 15.316 2.134   3.693   0.28 10.98 ?  202 A1A94 A C13  1 
HETATM 6702 C  C15  B A1A94 D 3 .   ? 15.767 4.202   4.548   0.28 10.73 ?  202 A1A94 A C15  1 
HETATM 6703 C  C2   B A1A94 D 3 .   ? 14.677 -0.451  0.938   0.28 12.40 ?  202 A1A94 A C2   1 
HETATM 6704 C  C4   B A1A94 D 3 .   ? 12.856 0.327   -0.868  0.28 14.36 ?  202 A1A94 A C4   1 
HETATM 6705 C  C5   B A1A94 D 3 .   ? 12.003 -0.503  -1.605  0.28 14.69 ?  202 A1A94 A C5   1 
HETATM 6706 C  C7   B A1A94 D 3 .   ? 10.344 1.186   -1.558  0.28 15.25 ?  202 A1A94 A C7   1 
HETATM 6707 C  C8   B A1A94 D 3 .   ? 11.147 2.031   -0.839  0.28 15.39 ?  202 A1A94 A C8   1 
HETATM 6708 I  I1   B A1A94 D 3 .   ? 8.523  1.800   -2.079  0.28 15.67 ?  202 A1A94 A I1   1 
HETATM 6709 N  N1   B A1A94 D 3 .   ? 14.990 0.818   1.644   0.28 10.99 ?  202 A1A94 A N1   1 
HETATM 6710 N  N3   B A1A94 D 3 .   ? 15.129 0.931   5.849   0.28 11.56 ?  202 A1A94 A N3   1 
HETATM 6711 N  N4   B A1A94 D 3 .   ? 15.620 3.314   5.625   0.28 10.38 ?  202 A1A94 A N4   1 
HETATM 6712 O  O1   B A1A94 D 3 .   ? 15.643 -2.480  0.225   0.28 14.91 ?  202 A1A94 A O1   1 
HETATM 6713 H  H5   B A1A94 D 3 .   ? 14.928 0.577   -0.968  0.28 16.48 ?  202 A1A94 A H5   1 
HETATM 6714 H  H6   B A1A94 D 3 .   ? 14.415 -1.050  -1.173  0.28 16.48 ?  202 A1A94 A H6   1 
HETATM 6715 H  H8   B A1A94 D 3 .   ? 10.025 -0.690  -2.522  0.28 17.98 ?  202 A1A94 A H8   1 
HETATM 6716 H  H10  B A1A94 D 3 .   ? 13.068 2.271   0.078   0.28 17.61 ?  202 A1A94 A H10  1 
HETATM 6717 H  H13  B A1A94 D 3 .   ? 15.653 3.941   2.385   0.28 13.16 ?  202 A1A94 A H13  1 
HETATM 6718 H  H4   B A1A94 D 3 .   ? 16.802 -0.744  0.409   0.28 16.50 ?  202 A1A94 A H4   1 
HETATM 6719 H  H3   B A1A94 D 3 .   ? 16.355 -1.528  1.928   0.28 16.50 ?  202 A1A94 A H3   1 
HETATM 6720 H  H12  B A1A94 D 3 .   ? 14.708 -1.090  5.668   0.28 14.26 ?  202 A1A94 A H12  1 
HETATM 6721 H  H14  B A1A94 D 3 .   ? 15.991 5.252   4.719   0.28 12.92 ?  202 A1A94 A H14  1 
HETATM 6722 H  H1   B A1A94 D 3 .   ? 13.862 -1.016  1.462   0.28 14.93 ?  202 A1A94 A H1   1 
HETATM 6723 H  H7   B A1A94 D 3 .   ? 12.292 -1.501  -1.929  0.28 17.68 ?  202 A1A94 A H7   1 
HETATM 6724 H  H9   B A1A94 D 3 .   ? 10.779 3.019   -0.552  0.28 18.51 ?  202 A1A94 A H9   1 
HETATM 6725 H  H11  B A1A94 D 3 .   ? 15.166 1.649   1.101   0.28 13.24 ?  202 A1A94 A H11  1 
HETATM 6726 H  H15  B A1A94 D 3 .   ? 15.690 3.532   6.610   0.28 12.50 ?  202 A1A94 A H15  1 
HETATM 6727 H  H2   B A1A94 D 3 .   ? 16.465 -2.935  0.040   0.28 17.93 ?  202 A1A94 A H2   1 
HETATM 6728 O  O1   C A1A93 E 4 .   ? 15.868 -2.522  0.280   0.12 13.43 ?  203 A1A93 A O1   1 
HETATM 6729 C  C1   C A1A93 E 4 .   ? 16.156 -1.317  0.940   0.12 12.79 ?  203 A1A93 A C1   1 
HETATM 6730 C  C2   C A1A93 E 4 .   ? 15.034 -0.244  0.611   0.12 12.12 ?  203 A1A93 A C2   1 
HETATM 6731 C  C3   C A1A93 E 4 .   ? 13.576 -0.894  0.701   0.12 12.37 ?  203 A1A93 A C3   1 
HETATM 6732 C  C4   C A1A93 E 4 .   ? 12.434 -0.219  -0.110  0.12 12.56 ?  203 A1A93 A C4   1 
HETATM 6733 C  C5   C A1A93 E 4 .   ? 12.047 1.130   0.062   0.12 12.83 ?  203 A1A93 A C5   1 
HETATM 6734 C  C6   C A1A93 E 4 .   ? 10.998 1.725   -0.683  0.12 12.84 ?  203 A1A93 A C6   1 
HETATM 6735 C  C7   C A1A93 E 4 .   ? 10.317 0.955   -1.615  0.12 13.02 ?  203 A1A93 A C7   1 
HETATM 6736 C  C8   C A1A93 E 4 .   ? 10.649 -0.372  -1.820  0.12 12.90 ?  203 A1A93 A C8   1 
HETATM 6737 C  C10  C A1A93 E 4 .   ? 15.179 1.002   2.900   0.12 11.46 ?  203 A1A93 A C10  1 
HETATM 6738 C  C11  C A1A93 E 4 .   ? 14.918 -0.136  4.983   0.12 11.46 ?  203 A1A93 A C11  1 
HETATM 6739 C  C12  C A1A93 E 4 .   ? 15.361 2.062   5.074   0.12 11.10 ?  203 A1A93 A C12  1 
HETATM 6740 C  C13  C A1A93 E 4 .   ? 15.411 2.210   3.644   0.12 11.31 ?  203 A1A93 A C13  1 
HETATM 6741 C  C14  C A1A93 E 4 .   ? 15.701 3.611   3.417   0.12 11.26 ?  203 A1A93 A C14  1 
HETATM 6742 C  C15  C A1A93 E 4 .   ? 15.806 4.229   4.663   0.12 11.18 ?  203 A1A93 A C15  1 
HETATM 6743 C  C9   C A1A93 E 4 .   ? 11.697 -0.936  -1.065  0.12 12.72 ?  203 A1A93 A C9   1 
HETATM 6744 I  I1   C A1A93 E 4 .   ? 8.791  1.774   -2.719  0.12 13.47 ?  203 A1A93 A I1   1 
HETATM 6745 N  N1   C A1A93 E 4 .   ? 15.194 0.964   1.475   0.12 11.52 ?  203 A1A93 A N1   1 
HETATM 6746 N  N2   C A1A93 E 4 .   ? 14.934 -0.161  3.596   0.12 11.51 ?  203 A1A93 A N2   1 
HETATM 6747 N  N3   C A1A93 E 4 .   ? 15.119 0.922   5.796   0.12 11.28 ?  203 A1A93 A N3   1 
HETATM 6748 N  N4   C A1A93 E 4 .   ? 15.601 3.281   5.637   0.12 10.89 ?  203 A1A93 A N4   1 
HETATM 6749 H  H2   C A1A93 E 4 .   ? 16.555 -3.148  0.503   0.12 16.16 ?  203 A1A93 A H2   1 
HETATM 6750 H  H3   C A1A93 E 4 .   ? 17.147 -0.929  0.618   0.12 15.39 ?  203 A1A93 A H3   1 
HETATM 6751 H  H4   C A1A93 E 4 .   ? 16.263 -1.481  2.035   0.12 15.39 ?  203 A1A93 A H4   1 
HETATM 6752 H  H1   C A1A93 E 4 .   ? 15.148 0.062   -0.456  0.12 14.59 ?  203 A1A93 A H1   1 
HETATM 6753 H  H6   C A1A93 E 4 .   ? 13.634 -1.971  0.413   0.12 14.89 ?  203 A1A93 A H6   1 
HETATM 6754 H  H5   C A1A93 E 4 .   ? 13.291 -0.982  1.761   0.12 14.89 ?  203 A1A93 A H5   1 
HETATM 6755 H  H7   C A1A93 E 4 .   ? 12.585 1.757   0.794   0.12 15.44 ?  203 A1A93 A H7   1 
HETATM 6756 H  H8   C A1A93 E 4 .   ? 10.727 2.785   -0.520  0.12 15.45 ?  203 A1A93 A H8   1 
HETATM 6757 H  H9   C A1A93 E 4 .   ? 10.101 -0.978  -2.553  0.12 15.52 ?  203 A1A93 A H9   1 
HETATM 6758 H  H12  C A1A93 E 4 .   ? 14.721 -1.073  5.546   0.12 13.79 ?  203 A1A93 A H12  1 
HETATM 6759 H  H13  C A1A93 E 4 .   ? 15.826 4.155   2.503   0.12 13.55 ?  203 A1A93 A H13  1 
HETATM 6760 H  H14  C A1A93 E 4 .   ? 16.007 5.242   4.977   0.12 13.46 ?  203 A1A93 A H14  1 
HETATM 6761 H  H10  C A1A93 E 4 .   ? 11.949 -1.988  -1.240  0.12 15.31 ?  203 A1A93 A H10  1 
HETATM 6762 H  H11  C A1A93 E 4 .   ? 15.326 1.837   0.999   0.12 13.86 ?  203 A1A93 A H11  1 
HETATM 6763 H  H15  C A1A93 E 4 .   ? 15.622 3.468   6.673   0.12 13.11 ?  203 A1A93 A H15  1 
HETATM 6764 CL CL   B CL    F 5 .   ? 16.035 2.790   -1.105  0.40 16.07 ?  204 CL    A CL   1 
HETATM 6765 O  O    . HOH   G 6 .   ? 6.915  -7.993  11.878  1.00 19.99 ?  301 HOH   A O    1 
HETATM 6766 O  O    . HOH   G 6 .   ? 14.766 -4.630  20.535  1.00 45.69 ?  302 HOH   A O    1 
HETATM 6767 O  O    . HOH   G 6 .   ? 4.581  3.892   0.631   1.00 24.89 ?  303 HOH   A O    1 
HETATM 6768 O  O    . HOH   G 6 .   ? 34.332 -1.869  12.482  1.00 37.24 ?  304 HOH   A O    1 
HETATM 6769 O  O    . HOH   G 6 .   ? 0.745  -4.640  0.201   1.00 35.12 ?  305 HOH   A O    1 
HETATM 6770 O  O    . HOH   G 6 .   ? 18.642 -2.405  -16.476 1.00 47.91 ?  306 HOH   A O    1 
HETATM 6771 O  O    . HOH   G 6 .   ? 11.715 -10.813 -10.095 1.00 45.88 ?  307 HOH   A O    1 
HETATM 6772 O  O    A HOH   G 6 .   ? 8.021  -12.595 -0.904  0.60 17.78 ?  308 HOH   A O    1 
HETATM 6773 O  O    . HOH   G 6 .   ? 28.210 -6.321  19.604  1.00 42.20 ?  309 HOH   A O    1 
HETATM 6774 O  O    . HOH   G 6 .   ? 9.290  -10.135 19.512  1.00 41.11 ?  310 HOH   A O    1 
HETATM 6775 O  O    A HOH   G 6 .   ? 3.622  -9.454  9.705   0.60 26.91 ?  311 HOH   A O    1 
HETATM 6776 O  O    . HOH   G 6 .   ? 14.278 -4.531  -11.889 1.00 36.62 ?  312 HOH   A O    1 
HETATM 6777 O  O    . HOH   G 6 .   ? 28.940 0.425   -9.707  1.00 20.88 ?  313 HOH   A O    1 
HETATM 6778 O  O    . HOH   G 6 .   ? 13.352 -1.459  -6.725  1.00 17.68 ?  314 HOH   A O    1 
HETATM 6779 O  O    . HOH   G 6 .   ? 14.683 -13.937 16.688  1.00 24.12 ?  315 HOH   A O    1 
HETATM 6780 O  O    . HOH   G 6 .   ? 12.004 0.367   14.701  1.00 34.99 ?  316 HOH   A O    1 
HETATM 6781 O  O    . HOH   G 6 .   ? 42.482 10.575  5.134   1.00 19.43 ?  317 HOH   A O    1 
HETATM 6782 O  O    . HOH   G 6 .   ? 15.055 -12.222 18.680  1.00 41.26 ?  318 HOH   A O    1 
HETATM 6783 O  O    . HOH   G 6 .   ? 28.593 -10.676 -13.985 1.00 41.31 ?  319 HOH   A O    1 
HETATM 6784 O  O    . HOH   G 6 .   ? 7.562  -6.261  -6.601  1.00 40.37 ?  320 HOH   A O    1 
HETATM 6785 O  O    . HOH   G 6 .   ? 9.861  -21.394 5.679   1.00 17.48 ?  321 HOH   A O    1 
HETATM 6786 O  O    A HOH   G 6 .   ? 14.661 -3.652  3.070   0.60 13.63 ?  322 HOH   A O    1 
HETATM 6787 O  O    . HOH   G 6 .   ? 30.269 -13.330 -8.547  1.00 19.53 ?  323 HOH   A O    1 
HETATM 6788 O  O    . HOH   G 6 .   ? 15.106 4.094   17.608  1.00 43.23 ?  324 HOH   A O    1 
HETATM 6789 O  O    . HOH   G 6 .   ? 36.200 -5.092  -0.545  1.00 29.61 ?  325 HOH   A O    1 
HETATM 6790 O  O    B HOH   G 6 .   ? 11.355 6.385   8.798   0.40 24.12 ?  326 HOH   A O    1 
HETATM 6791 O  O    . HOH   G 6 .   ? 11.723 -10.673 16.955  1.00 23.97 ?  327 HOH   A O    1 
HETATM 6792 O  O    . HOH   G 6 .   ? 22.751 12.518  1.623   1.00 13.90 ?  328 HOH   A O    1 
HETATM 6793 O  O    . HOH   G 6 .   ? 20.668 -19.723 -5.025  1.00 27.82 ?  329 HOH   A O    1 
HETATM 6794 O  O    . HOH   G 6 .   ? -0.409 -2.917  3.061   1.00 43.02 ?  330 HOH   A O    1 
HETATM 6795 O  O    B HOH   G 6 .   ? 7.962  3.922   1.377   0.40 17.31 ?  331 HOH   A O    1 
HETATM 6796 O  O    . HOH   G 6 .   ? 26.506 -19.353 -1.773  1.00 13.37 ?  332 HOH   A O    1 
HETATM 6797 O  O    A HOH   G 6 .   ? 17.523 -1.714  0.414   0.60 18.79 ?  333 HOH   A O    1 
HETATM 6798 O  O    . HOH   G 6 .   ? 5.374  2.670   5.025   1.00 30.55 ?  334 HOH   A O    1 
HETATM 6799 O  O    . HOH   G 6 .   ? 22.387 5.445   18.993  1.00 44.20 ?  335 HOH   A O    1 
HETATM 6800 O  O    . HOH   G 6 .   ? 28.379 -0.184  -13.397 1.00 34.00 ?  336 HOH   A O    1 
HETATM 6801 O  O    . HOH   G 6 .   ? 19.947 -12.599 -8.870  1.00 25.03 ?  337 HOH   A O    1 
HETATM 6802 O  O    . HOH   G 6 .   ? 18.667 -19.376 13.564  1.00 33.87 ?  338 HOH   A O    1 
HETATM 6803 O  O    . HOH   G 6 .   ? 30.962 6.235   -12.267 1.00 27.66 ?  339 HOH   A O    1 
HETATM 6804 O  O    . HOH   G 6 .   ? 31.026 -18.143 7.797   1.00 18.77 ?  340 HOH   A O    1 
HETATM 6805 O  O    . HOH   G 6 .   ? 27.395 13.789  2.821   1.00 30.84 ?  341 HOH   A O    1 
HETATM 6806 O  O    . HOH   G 6 .   ? 38.308 10.173  7.126   1.00 39.09 ?  342 HOH   A O    1 
HETATM 6807 O  O    . HOH   G 6 .   ? 17.121 -18.017 15.018  1.00 26.30 ?  343 HOH   A O    1 
HETATM 6808 O  O    B HOH   G 6 .   ? 15.280 6.762   6.736   0.40 21.00 ?  344 HOH   A O    1 
HETATM 6809 O  O    . HOH   G 6 .   ? 21.309 -2.297  -2.362  1.00 16.07 ?  345 HOH   A O    1 
HETATM 6810 O  O    . HOH   G 6 .   ? 27.951 0.809   -7.164  1.00 13.55 ?  346 HOH   A O    1 
HETATM 6811 O  O    . HOH   G 6 .   ? 11.000 1.719   12.438  1.00 24.39 ?  347 HOH   A O    1 
HETATM 6812 O  O    . HOH   G 6 .   ? 34.023 -1.030  -8.958  1.00 24.92 ?  348 HOH   A O    1 
HETATM 6813 O  O    . HOH   G 6 .   ? 37.569 2.789   10.171  1.00 27.55 ?  349 HOH   A O    1 
HETATM 6814 O  O    . HOH   G 6 .   ? 44.359 7.121   6.374   1.00 26.84 ?  350 HOH   A O    1 
HETATM 6815 O  O    . HOH   G 6 .   ? 38.594 5.005   6.962   1.00 14.69 ?  351 HOH   A O    1 
HETATM 6816 O  O    . HOH   G 6 .   ? 18.889 -21.974 6.886   1.00 30.85 ?  352 HOH   A O    1 
HETATM 6817 O  O    B HOH   G 6 .   ? 14.812 -2.964  3.454   0.40 15.17 ?  353 HOH   A O    1 
HETATM 6818 O  O    . HOH   G 6 .   ? 31.714 8.231   14.817  1.00 23.07 ?  354 HOH   A O    1 
HETATM 6819 O  O    . HOH   G 6 .   ? 14.468 -24.659 11.552  1.00 34.62 ?  355 HOH   A O    1 
HETATM 6820 O  O    . HOH   G 6 .   ? 42.617 4.334   5.376   1.00 30.79 ?  356 HOH   A O    1 
HETATM 6821 O  O    . HOH   G 6 .   ? 35.791 -12.674 6.857   1.00 14.99 ?  357 HOH   A O    1 
HETATM 6822 O  O    . HOH   G 6 .   ? 39.787 -1.042  -5.205  1.00 20.23 ?  358 HOH   A O    1 
HETATM 6823 O  O    . HOH   G 6 .   ? 26.870 11.426  1.652   1.00 15.15 ?  359 HOH   A O    1 
HETATM 6824 O  O    A HOH   G 6 .   ? 14.302 0.578   6.770   0.60 17.83 ?  360 HOH   A O    1 
HETATM 6825 O  O    . HOH   G 6 .   ? 37.402 11.953  4.943   1.00 29.47 ?  361 HOH   A O    1 
HETATM 6826 O  O    . HOH   G 6 .   ? 6.426  -5.422  11.124  1.00 19.52 ?  362 HOH   A O    1 
HETATM 6827 O  O    . HOH   G 6 .   ? 13.540 -15.237 -7.474  1.00 27.50 ?  363 HOH   A O    1 
HETATM 6828 O  O    . HOH   G 6 .   ? 22.180 -19.286 11.395  1.00 32.75 ?  364 HOH   A O    1 
HETATM 6829 O  O    . HOH   G 6 .   ? 17.175 -17.820 -5.030  1.00 27.14 ?  365 HOH   A O    1 
HETATM 6830 O  O    . HOH   G 6 .   ? 14.413 -21.246 -4.291  1.00 29.80 ?  366 HOH   A O    1 
HETATM 6831 O  O    . HOH   G 6 .   ? 8.204  -21.507 4.004   1.00 48.92 ?  367 HOH   A O    1 
HETATM 6832 O  O    . HOH   G 6 .   ? 24.055 -2.118  -2.092  1.00 10.18 ?  368 HOH   A O    1 
HETATM 6833 O  O    . HOH   G 6 .   ? 33.664 -7.160  4.316   1.00 15.93 ?  369 HOH   A O    1 
HETATM 6834 O  O    . HOH   G 6 .   ? 43.954 8.433   -3.105  1.00 26.84 ?  370 HOH   A O    1 
HETATM 6835 O  O    . HOH   G 6 .   ? 22.615 -11.906 21.829  1.00 50.33 ?  371 HOH   A O    1 
HETATM 6836 O  O    . HOH   G 6 .   ? 30.825 3.091   8.267   1.00 11.34 ?  372 HOH   A O    1 
HETATM 6837 O  O    . HOH   G 6 .   ? 31.105 -13.950 -2.478  1.00 12.82 ?  373 HOH   A O    1 
HETATM 6838 O  O    . HOH   G 6 .   ? 15.214 -8.079  -9.727  1.00 25.01 ?  374 HOH   A O    1 
HETATM 6839 O  O    . HOH   G 6 .   ? 21.908 -21.910 8.482   1.00 27.39 ?  375 HOH   A O    1 
HETATM 6840 O  O    . HOH   G 6 .   ? 37.300 -2.837  9.677   1.00 42.73 ?  376 HOH   A O    1 
HETATM 6841 O  O    . HOH   G 6 .   ? 16.558 -22.052 0.959   1.00 26.41 ?  377 HOH   A O    1 
HETATM 6842 O  O    . HOH   G 6 .   ? 27.454 -6.122  -14.035 1.00 37.37 ?  378 HOH   A O    1 
HETATM 6843 O  O    . HOH   G 6 .   ? 15.484 11.839  7.838   1.00 43.00 ?  379 HOH   A O    1 
HETATM 6844 O  O    . HOH   G 6 .   ? 31.924 -9.328  -6.628  1.00 21.16 ?  380 HOH   A O    1 
HETATM 6845 O  O    T HOH   G 6 .   ? 15.434 -0.420  2.357   0.30 12.36 ?  381 HOH   A O    1 
HETATM 6846 O  O    . HOH   G 6 .   ? 18.629 9.508   9.010   1.00 20.37 ?  382 HOH   A O    1 
HETATM 6847 O  O    . HOH   G 6 .   ? 27.469 -10.617 14.060  1.00 16.22 ?  383 HOH   A O    1 
HETATM 6848 O  O    . HOH   G 6 .   ? 33.547 -16.966 8.085   1.00 18.82 ?  384 HOH   A O    1 
HETATM 6849 O  O    . HOH   G 6 .   ? 24.439 3.560   -1.814  1.00 14.13 ?  385 HOH   A O    1 
HETATM 6850 O  O    A HOH   G 6 .   ? 11.094 -0.378  1.904   0.70 25.74 ?  386 HOH   A O    1 
HETATM 6851 O  O    . HOH   G 6 .   ? 17.013 -19.292 4.887   1.00 14.14 ?  387 HOH   A O    1 
HETATM 6852 O  O    . HOH   G 6 .   ? 43.402 7.840   2.672   1.00 27.14 ?  388 HOH   A O    1 
HETATM 6853 O  O    . HOH   G 6 .   ? 25.728 -0.823  -7.352  1.00 15.23 ?  389 HOH   A O    1 
HETATM 6854 O  O    . HOH   G 6 .   ? 31.844 -7.309  -9.842  1.00 20.32 ?  390 HOH   A O    1 
HETATM 6855 O  O    . HOH   G 6 .   ? 24.203 -7.749  14.450  1.00 16.03 ?  391 HOH   A O    1 
HETATM 6856 O  O    . HOH   G 6 .   ? 21.217 10.270  15.002  1.00 37.16 ?  392 HOH   A O    1 
HETATM 6857 O  O    . HOH   G 6 .   ? 18.881 -0.747  -1.613  1.00 13.71 ?  393 HOH   A O    1 
HETATM 6858 O  O    A HOH   G 6 .   ? 24.612 2.033   -7.015  0.60 14.87 ?  394 HOH   A O    1 
HETATM 6859 O  O    . HOH   G 6 .   ? 24.701 -17.533 12.711  1.00 22.54 ?  395 HOH   A O    1 
HETATM 6860 O  O    . HOH   G 6 .   ? 21.373 3.059   -0.282  1.00 12.47 ?  396 HOH   A O    1 
HETATM 6861 O  O    . HOH   G 6 .   ? 14.088 -23.083 7.442   1.00 16.86 ?  397 HOH   A O    1 
HETATM 6862 O  O    A HOH   G 6 .   ? 15.827 -0.942  5.242   0.60 17.58 ?  398 HOH   A O    1 
HETATM 6863 O  O    . HOH   G 6 .   ? 37.571 -2.005  5.797   1.00 26.62 ?  399 HOH   A O    1 
HETATM 6864 O  O    . HOH   G 6 .   ? 15.194 -21.546 14.242  1.00 17.27 ?  400 HOH   A O    1 
HETATM 6865 O  O    B HOH   G 6 .   ? 11.976 -1.603  -4.629  0.40 22.74 ?  401 HOH   A O    1 
HETATM 6866 O  O    . HOH   G 6 .   ? 32.804 -9.250  5.974   1.00 19.74 ?  402 HOH   A O    1 
HETATM 6867 O  O    . HOH   G 6 .   ? 23.500 11.400  4.060   1.00 11.65 ?  403 HOH   A O    1 
HETATM 6868 O  O    . HOH   G 6 .   ? 14.577 -0.489  -12.150 1.00 29.84 ?  404 HOH   A O    1 
HETATM 6869 O  O    . HOH   G 6 .   ? 23.979 -15.740 -9.180  1.00 34.83 ?  405 HOH   A O    1 
HETATM 6870 O  O    . HOH   G 6 .   ? 30.680 1.902   16.708  1.00 19.94 ?  406 HOH   A O    1 
HETATM 6871 O  O    . HOH   G 6 .   ? -0.757 -8.549  2.105   1.00 43.29 ?  407 HOH   A O    1 
HETATM 6872 O  O    . HOH   G 6 .   ? 38.122 -1.336  -1.934  1.00 17.99 ?  408 HOH   A O    1 
HETATM 6873 O  O    . HOH   G 6 .   ? 20.567 -20.025 2.780   1.00 17.14 ?  409 HOH   A O    1 
HETATM 6874 O  O    . HOH   G 6 .   ? 27.282 2.336   18.668  1.00 28.65 ?  410 HOH   A O    1 
HETATM 6875 O  O    . HOH   G 6 .   ? 6.779  -3.262  12.933  1.00 32.65 ?  411 HOH   A O    1 
HETATM 6876 O  O    . HOH   G 6 .   ? 13.925 -4.859  17.375  1.00 28.22 ?  412 HOH   A O    1 
HETATM 6877 O  O    . HOH   G 6 .   ? 40.953 -8.331  -6.780  1.00 36.50 ?  413 HOH   A O    1 
HETATM 6878 O  O    . HOH   G 6 .   ? 26.968 4.151   -0.669  1.00 12.20 ?  414 HOH   A O    1 
HETATM 6879 O  O    . HOH   G 6 .   ? 16.040 6.900   2.906   1.00 19.15 ?  415 HOH   A O    1 
HETATM 6880 O  O    . HOH   G 6 .   ? 23.956 -20.283 -1.347  1.00 15.62 ?  416 HOH   A O    1 
HETATM 6881 O  O    . HOH   G 6 .   ? 30.062 -10.109 13.056  1.00 21.20 ?  417 HOH   A O    1 
HETATM 6882 O  O    . HOH   G 6 .   ? 30.335 -12.930 13.528  1.00 19.07 ?  418 HOH   A O    1 
HETATM 6883 O  O    . HOH   G 6 .   ? 16.189 16.640  8.596   1.00 33.80 ?  419 HOH   A O    1 
HETATM 6884 O  O    . HOH   G 6 .   ? 21.800 -13.899 -8.203  1.00 45.95 ?  420 HOH   A O    1 
HETATM 6885 O  O    . HOH   G 6 .   ? 32.709 -4.364  -9.894  1.00 27.07 ?  421 HOH   A O    1 
HETATM 6886 O  O    . HOH   G 6 .   ? 36.749 -4.933  5.392   1.00 22.38 ?  422 HOH   A O    1 
HETATM 6887 O  O    . HOH   G 6 .   ? 35.119 -5.246  -3.110  1.00 17.22 ?  423 HOH   A O    1 
HETATM 6888 O  O    . HOH   G 6 .   ? 10.405 -13.742 -1.692  1.00 17.41 ?  424 HOH   A O    1 
HETATM 6889 O  O    A HOH   G 6 .   ? 20.129 4.536   -7.577  0.60 17.35 ?  425 HOH   A O    1 
HETATM 6890 O  O    . HOH   G 6 .   ? 44.975 -0.571  3.031   1.00 40.70 ?  426 HOH   A O    1 
HETATM 6891 O  O    . HOH   G 6 .   ? 41.656 1.537   5.000   1.00 37.22 ?  427 HOH   A O    1 
HETATM 6892 O  O    . HOH   G 6 .   ? 15.949 2.195   24.703  1.00 46.52 ?  428 HOH   A O    1 
HETATM 6893 O  O    . HOH   G 6 .   ? 10.432 -22.172 -1.260  1.00 49.35 ?  429 HOH   A O    1 
HETATM 6894 O  O    . HOH   G 6 .   ? 32.595 -10.648 3.217   1.00 30.34 ?  430 HOH   A O    1 
HETATM 6895 O  O    . HOH   G 6 .   ? 27.055 -3.161  19.398  1.00 38.17 ?  431 HOH   A O    1 
HETATM 6896 O  O    A HOH   G 6 .   ? 24.121 3.953   -4.945  0.60 18.57 ?  432 HOH   A O    1 
HETATM 6897 O  O    . HOH   G 6 .   ? 16.217 -14.126 20.171  1.00 48.24 ?  433 HOH   A O    1 
HETATM 6898 O  O    A HOH   G 6 .   ? 16.287 2.946   -1.472  0.60 15.43 ?  434 HOH   A O    1 
HETATM 6899 O  O    . HOH   G 6 .   ? 22.697 8.210   18.378  1.00 48.23 ?  435 HOH   A O    1 
HETATM 6900 O  O    . HOH   G 6 .   ? 23.199 7.600   -3.218  1.00 27.08 ?  436 HOH   A O    1 
HETATM 6901 O  O    A HOH   G 6 .   ? 9.028  -12.110 17.165  0.60 42.86 ?  437 HOH   A O    1 
HETATM 6902 O  O    . HOH   G 6 .   ? 19.419 -11.014 24.013  1.00 67.02 ?  438 HOH   A O    1 
HETATM 6903 O  O    . HOH   G 6 .   ? 20.568 -17.692 24.752  1.00 52.60 ?  439 HOH   A O    1 
HETATM 6904 O  O    . HOH   G 6 .   ? 21.328 -9.214  21.314  1.00 57.03 ?  440 HOH   A O    1 
HETATM 6905 O  O    . HOH   G 6 .   ? 23.508 -8.011  17.090  1.00 20.16 ?  441 HOH   A O    1 
HETATM 6906 O  O    . HOH   G 6 .   ? 23.350 -20.949 1.352   1.00 17.67 ?  442 HOH   A O    1 
HETATM 6907 O  O    B HOH   G 6 .   ? 12.921 -3.309  1.348   0.40 20.74 ?  443 HOH   A O    1 
HETATM 6908 O  O    . HOH   G 6 .   ? 37.771 -8.859  -3.458  1.00 22.52 ?  444 HOH   A O    1 
HETATM 6909 O  O    . HOH   G 6 .   ? 18.878 1.943   -0.671  1.00 12.42 ?  445 HOH   A O    1 
HETATM 6910 O  O    . HOH   G 6 .   ? 18.399 -15.999 16.261  1.00 37.26 ?  446 HOH   A O    1 
HETATM 6911 O  O    . HOH   G 6 .   ? 34.446 -8.094  -0.529  1.00 27.36 ?  447 HOH   A O    1 
HETATM 6912 O  O    . HOH   G 6 .   ? 9.458  -16.367 -2.057  1.00 48.58 ?  448 HOH   A O    1 
HETATM 6913 O  O    . HOH   G 6 .   ? 18.528 4.934   -15.161 1.00 48.59 ?  449 HOH   A O    1 
HETATM 6914 O  O    . HOH   G 6 .   ? 30.632 14.781  2.756   1.00 17.80 ?  450 HOH   A O    1 
HETATM 6915 O  O    A HOH   G 6 .   ? 14.054 -0.336  3.433   0.30 26.71 ?  451 HOH   A O    1 
HETATM 6916 O  O    . HOH   G 6 .   ? 31.354 -12.797 0.014   1.00 18.26 ?  452 HOH   A O    1 
HETATM 6917 O  O    . HOH   G 6 .   ? 21.525 -14.666 17.938  1.00 51.91 ?  453 HOH   A O    1 
HETATM 6918 O  O    A HOH   G 6 .   ? -1.404 -4.934  7.615   0.60 38.06 ?  454 HOH   A O    1 
HETATM 6919 O  O    . HOH   G 6 .   ? 27.743 6.976   -6.490  1.00 35.25 ?  455 HOH   A O    1 
HETATM 6920 O  O    . HOH   G 6 .   ? 29.795 -16.028 10.724  1.00 29.68 ?  456 HOH   A O    1 
HETATM 6921 O  O    . HOH   G 6 .   ? 29.790 -1.949  -12.727 1.00 45.44 ?  457 HOH   A O    1 
HETATM 6922 O  O    . HOH   G 6 .   ? 25.430 8.225   -4.793  1.00 26.90 ?  458 HOH   A O    1 
HETATM 6923 O  O    . HOH   G 6 .   ? 32.458 -15.935 10.876  1.00 31.44 ?  459 HOH   A O    1 
HETATM 6924 O  O    . HOH   G 6 .   ? 19.907 -17.335 -5.088  1.00 24.55 ?  460 HOH   A O    1 
HETATM 6925 O  O    . HOH   G 6 .   ? 24.985 5.665   20.728  1.00 50.27 ?  461 HOH   A O    1 
HETATM 6926 O  O    B HOH   G 6 .   ? 7.432  3.892   4.150   0.40 22.93 ?  462 HOH   A O    1 
HETATM 6927 O  O    . HOH   G 6 .   ? 23.182 -22.344 -3.390  1.00 35.06 ?  463 HOH   A O    1 
HETATM 6928 O  O    . HOH   G 6 .   ? 24.674 14.627  7.781   1.00 35.20 ?  464 HOH   A O    1 
HETATM 6929 O  O    . HOH   G 6 .   ? 39.653 -7.070  -3.591  1.00 46.22 ?  465 HOH   A O    1 
HETATM 6930 O  O    . HOH   G 6 .   ? 23.520 13.744  5.470   1.00 18.12 ?  466 HOH   A O    1 
HETATM 6931 O  O    . HOH   G 6 .   ? 15.749 -21.515 3.691   1.00 21.38 ?  467 HOH   A O    1 
HETATM 6932 O  O    . HOH   G 6 .   ? 11.972 -13.431 16.382  1.00 53.88 ?  468 HOH   A O    1 
HETATM 6933 O  O    . HOH   G 6 .   ? 18.799 10.892  11.341  1.00 31.41 ?  469 HOH   A O    1 
HETATM 6934 O  O    . HOH   G 6 .   ? 26.950 11.657  -1.338  1.00 31.34 ?  470 HOH   A O    1 
HETATM 6935 O  O    A HOH   G 6 .   ? 21.995 5.261   -5.867  0.60 23.32 ?  471 HOH   A O    1 
HETATM 6936 O  O    . HOH   G 6 .   ? 18.192 -16.177 -8.819  1.00 39.97 ?  472 HOH   A O    1 
HETATM 6937 O  O    . HOH   G 6 .   ? 27.545 -11.451 16.555  1.00 35.47 ?  473 HOH   A O    1 
HETATM 6938 O  O    . HOH   G 6 .   ? 11.034 -15.143 -6.104  1.00 35.12 ?  474 HOH   A O    1 
HETATM 6939 O  O    . HOH   G 6 .   ? 12.275 1.596   17.290  1.00 38.56 ?  475 HOH   A O    1 
HETATM 6940 O  O    . HOH   G 6 .   ? 25.838 10.802  -3.744  1.00 25.09 ?  476 HOH   A O    1 
HETATM 6941 O  O    B HOH   G 6 .   ? 5.650  -1.161  -2.526  0.40 31.31 ?  477 HOH   A O    1 
HETATM 6942 O  O    . HOH   G 6 .   ? 14.096 -10.366 -10.895 1.00 33.44 ?  478 HOH   A O    1 
HETATM 6943 O  O    . HOH   G 6 .   ? 15.750 -17.144 -6.974  1.00 32.03 ?  479 HOH   A O    1 
HETATM 6944 O  O    . HOH   G 6 .   ? 35.197 7.528   12.244  1.00 42.42 ?  480 HOH   A O    1 
HETATM 6945 O  O    . HOH   G 6 .   ? 28.876 9.046   17.496  1.00 40.00 ?  481 HOH   A O    1 
HETATM 6946 O  O    . HOH   G 6 .   ? 23.158 11.857  -4.064  1.00 18.69 ?  482 HOH   A O    1 
HETATM 6947 O  O    . HOH   G 6 .   ? 30.775 0.726   19.158  1.00 37.79 ?  483 HOH   A O    1 
HETATM 6948 O  O    . HOH   G 6 .   ? 17.404 -18.671 19.779  1.00 54.32 ?  484 HOH   A O    1 
HETATM 6949 O  O    . HOH   G 6 .   ? 40.939 -4.004  -0.362  1.00 37.54 ?  485 HOH   A O    1 
HETATM 6950 O  O    . HOH   G 6 .   ? 16.779 -20.524 16.177  1.00 27.86 ?  486 HOH   A O    1 
HETATM 6951 O  O    . HOH   G 6 .   ? 28.619 -4.711  -12.317 1.00 38.10 ?  487 HOH   A O    1 
HETATM 6952 O  O    B HOH   G 6 .   ? 11.608 8.883   7.430   0.40 37.35 ?  488 HOH   A O    1 
HETATM 6953 O  O    . HOH   G 6 .   ? 20.558 -16.034 -7.417  1.00 29.21 ?  489 HOH   A O    1 
HETATM 6954 O  O    . HOH   G 6 .   ? 23.245 -12.867 19.309  1.00 42.65 ?  490 HOH   A O    1 
HETATM 6955 O  O    . HOH   G 6 .   ? 41.750 9.351   -4.024  1.00 30.50 ?  491 HOH   A O    1 
HETATM 6956 O  O    . HOH   G 6 .   ? 44.553 10.463  -1.606  1.00 28.33 ?  492 HOH   A O    1 
HETATM 6957 O  O    . HOH   G 6 .   ? 16.051 -6.823  -11.887 1.00 43.77 ?  493 HOH   A O    1 
HETATM 6958 O  O    . HOH   G 6 .   ? 13.918 -25.228 8.979   1.00 31.23 ?  494 HOH   A O    1 
HETATM 6959 O  O    . HOH   G 6 .   ? 31.515 -0.597  -10.568 1.00 27.67 ?  495 HOH   A O    1 
HETATM 6960 O  O    . HOH   G 6 .   ? 28.770 -7.956  -15.302 1.00 48.27 ?  496 HOH   A O    1 
HETATM 6961 O  O    . HOH   G 6 .   ? 18.485 -23.228 1.910   1.00 42.98 ?  497 HOH   A O    1 
HETATM 6962 O  O    . HOH   G 6 .   ? 39.213 2.388   7.515   1.00 30.63 ?  498 HOH   A O    1 
HETATM 6963 O  O    . HOH   G 6 .   ? 40.597 -0.223  -7.800  1.00 33.49 ?  499 HOH   A O    1 
HETATM 6964 O  O    . HOH   G 6 .   ? 20.065 -22.360 4.150   1.00 27.39 ?  500 HOH   A O    1 
HETATM 6965 O  O    . HOH   G 6 .   ? 30.776 5.802   -14.752 1.00 35.12 ?  501 HOH   A O    1 
HETATM 6966 O  O    . HOH   G 6 .   ? 16.182 -23.401 5.696   1.00 26.39 ?  502 HOH   A O    1 
HETATM 6967 O  O    . HOH   G 6 .   ? 23.215 -23.799 1.709   1.00 28.94 ?  503 HOH   A O    1 
HETATM 6968 O  O    . HOH   G 6 .   ? 37.396 -6.676  7.556   1.00 24.46 ?  504 HOH   A O    1 
HETATM 6969 O  O    . HOH   G 6 .   ? 30.780 -5.867  -11.918 1.00 44.86 ?  505 HOH   A O    1 
HETATM 6970 O  O    B HOH   G 6 .   ? 14.776 8.163   4.842   0.40 19.85 ?  506 HOH   A O    1 
HETATM 6971 O  O    . HOH   G 6 .   ? 39.558 -0.006  6.570   1.00 32.45 ?  507 HOH   A O    1 
HETATM 6972 O  O    . HOH   G 6 .   ? 29.110 14.494  0.819   1.00 46.77 ?  508 HOH   A O    1 
HETATM 6973 O  O    . HOH   G 6 .   ? 38.084 13.981  6.686   1.00 44.30 ?  509 HOH   A O    1 
HETATM 6974 O  O    B HOH   G 6 .   ? 7.411  5.868   5.894   0.40 25.54 ?  510 HOH   A O    1 
HETATM 6975 O  O    A HOH   G 6 .   ? 8.276  -3.077  -5.700  0.60 37.11 ?  511 HOH   A O    1 
HETATM 6976 O  O    . HOH   G 6 .   ? 22.023 -24.033 4.438   1.00 24.19 ?  512 HOH   A O    1 
HETATM 6977 O  O    . HOH   G 6 .   ? 36.526 -6.535  10.125  1.00 41.90 ?  513 HOH   A O    1 
HETATM 6978 O  O    . HOH   G 6 .   ? 17.427 -6.612  -14.197 1.00 42.16 ?  514 HOH   A O    1 
HETATM 6979 O  O    T HOH   G 6 .   ? 11.950 -2.150  -3.683  0.30 13.66 ?  515 HOH   A O    1 
HETATM 6980 O  O    A HOH   G 6 .   ? 14.879 8.654   4.854   0.60 38.90 ?  516 HOH   A O    1 
HETATM 6981 O  O    B HOH   G 6 .   ? 9.509  0.005   -5.572  0.40 29.12 ?  517 HOH   A O    1 
HETATM 6982 O  O    . HOH   G 6 .   ? 24.073 8.995   -7.259  1.00 36.88 ?  518 HOH   A O    1 
HETATM 6983 O  O    B HOH   G 6 .   ? 8.347  -1.724  -4.250  0.40 25.40 ?  519 HOH   A O    1 
HETATM 6984 O  O    . HOH   G 6 .   ? 15.879 -12.252 27.419  1.00 47.38 ?  520 HOH   A O    1 
HETATM 6985 O  O    . HOH   G 6 .   ? 16.343 -21.109 18.783  1.00 36.90 ?  521 HOH   A O    1 
HETATM 6986 O  O    . HOH   G 6 .   ? 14.756 -22.785 19.771  1.00 35.12 ?  522 HOH   A O    1 
HETATM 6987 O  O    . HOH   H 6 .   ? 29.850 -22.417 5.486   1.00 18.90 ?  201 HOH   B O    1 
HETATM 6988 O  O    . HOH   H 6 .   ? 52.936 -13.447 -20.299 1.00 33.97 ?  202 HOH   B O    1 
HETATM 6989 O  O    . HOH   H 6 .   ? 41.804 -36.036 -17.177 1.00 31.34 ?  203 HOH   B O    1 
HETATM 6990 O  O    . HOH   H 6 .   ? 27.716 -29.174 -1.830  1.00 37.59 ?  204 HOH   B O    1 
HETATM 6991 O  O    . HOH   H 6 .   ? 59.205 -18.715 6.837   1.00 36.74 ?  205 HOH   B O    1 
HETATM 6992 O  O    . HOH   H 6 .   ? 49.433 -22.724 -19.770 1.00 48.44 ?  206 HOH   B O    1 
HETATM 6993 O  O    . HOH   H 6 .   ? 57.743 -24.553 5.024   1.00 36.99 ?  207 HOH   B O    1 
HETATM 6994 O  O    . HOH   H 6 .   ? 47.462 -7.426  -3.973  1.00 39.42 ?  208 HOH   B O    1 
HETATM 6995 O  O    . HOH   H 6 .   ? 48.108 -6.903  15.566  1.00 32.31 ?  209 HOH   B O    1 
HETATM 6996 O  O    . HOH   H 6 .   ? 54.541 -9.413  -8.742  1.00 18.72 ?  210 HOH   B O    1 
HETATM 6997 O  O    . HOH   H 6 .   ? 41.364 -7.826  5.485   1.00 39.44 ?  211 HOH   B O    1 
HETATM 6998 O  O    . HOH   H 6 .   ? 37.935 -39.520 -0.175  1.00 39.76 ?  212 HOH   B O    1 
HETATM 6999 O  O    . HOH   H 6 .   ? 27.890 -41.931 -15.134 1.00 35.29 ?  213 HOH   B O    1 
HETATM 7000 O  O    . HOH   H 6 .   ? 56.402 -19.720 7.364   1.00 31.83 ?  214 HOH   B O    1 
HETATM 7001 O  O    . HOH   H 6 .   ? 44.529 -7.273  2.079   1.00 32.33 ?  215 HOH   B O    1 
HETATM 7002 O  O    . HOH   H 6 .   ? 30.240 -41.049 -8.102  1.00 16.15 ?  216 HOH   B O    1 
HETATM 7003 O  O    . HOH   H 6 .   ? 55.413 -16.554 -14.337 1.00 35.03 ?  217 HOH   B O    1 
HETATM 7004 O  O    . HOH   H 6 .   ? 29.932 -26.310 4.033   1.00 26.40 ?  218 HOH   B O    1 
HETATM 7005 O  O    . HOH   H 6 .   ? 36.027 -43.346 -8.541  1.00 31.24 ?  219 HOH   B O    1 
HETATM 7006 O  O    . HOH   H 6 .   ? 56.778 -30.733 -7.801  1.00 32.70 ?  220 HOH   B O    1 
HETATM 7007 O  O    . HOH   H 6 .   ? 58.291 -12.947 8.418   1.00 29.78 ?  221 HOH   B O    1 
HETATM 7008 O  O    . HOH   H 6 .   ? 50.274 -3.343  7.142   1.00 34.33 ?  222 HOH   B O    1 
HETATM 7009 O  O    . HOH   H 6 .   ? 37.146 -19.845 -18.088 1.00 37.95 ?  223 HOH   B O    1 
HETATM 7010 O  O    . HOH   H 6 .   ? 29.817 -34.185 -0.398  1.00 35.73 ?  224 HOH   B O    1 
HETATM 7011 O  O    . HOH   H 6 .   ? 50.822 -6.112  0.152   1.00 24.87 ?  225 HOH   B O    1 
HETATM 7012 O  O    . HOH   H 6 .   ? 30.914 -28.791 4.315   1.00 25.86 ?  226 HOH   B O    1 
HETATM 7013 O  O    . HOH   H 6 .   ? 57.229 -26.872 -7.659  1.00 42.89 ?  227 HOH   B O    1 
HETATM 7014 O  O    . HOH   H 6 .   ? 57.449 -16.287 -12.224 1.00 18.07 ?  228 HOH   B O    1 
HETATM 7015 O  O    . HOH   H 6 .   ? 41.521 -39.219 -14.871 1.00 21.64 ?  229 HOH   B O    1 
HETATM 7016 O  O    . HOH   H 6 .   ? 45.153 -35.022 6.851   1.00 40.17 ?  230 HOH   B O    1 
HETATM 7017 O  O    . HOH   H 6 .   ? 34.578 -36.403 -7.173  1.00 17.37 ?  231 HOH   B O    1 
HETATM 7018 O  O    . HOH   H 6 .   ? 44.967 -43.587 -10.543 1.00 27.26 ?  232 HOH   B O    1 
HETATM 7019 O  O    . HOH   H 6 .   ? 40.662 -16.093 14.103  1.00 23.26 ?  233 HOH   B O    1 
HETATM 7020 O  O    . HOH   H 6 .   ? 48.577 -36.505 -15.498 1.00 44.57 ?  234 HOH   B O    1 
HETATM 7021 O  O    . HOH   H 6 .   ? 39.355 -10.906 6.117   1.00 23.34 ?  235 HOH   B O    1 
HETATM 7022 O  O    . HOH   H 6 .   ? 34.939 -24.673 13.857  1.00 33.57 ?  236 HOH   B O    1 
HETATM 7023 O  O    . HOH   H 6 .   ? 43.113 -43.278 -8.202  1.00 28.73 ?  237 HOH   B O    1 
HETATM 7024 O  O    . HOH   H 6 .   ? 44.531 -27.736 -0.657  1.00 21.83 ?  238 HOH   B O    1 
HETATM 7025 O  O    . HOH   H 6 .   ? 28.442 -19.706 -13.109 1.00 23.23 ?  239 HOH   B O    1 
HETATM 7026 O  O    . HOH   H 6 .   ? 51.716 -6.504  4.391   1.00 19.63 ?  240 HOH   B O    1 
HETATM 7027 O  O    . HOH   H 6 .   ? 32.850 -43.848 -11.316 1.00 19.59 ?  241 HOH   B O    1 
HETATM 7028 O  O    . HOH   H 6 .   ? 42.607 -25.391 2.621   1.00 14.20 ?  242 HOH   B O    1 
HETATM 7029 O  O    . HOH   H 6 .   ? 41.406 -9.613  13.059  1.00 22.19 ?  243 HOH   B O    1 
HETATM 7030 O  O    . HOH   H 6 .   ? 50.772 -12.992 -0.470  1.00 11.45 ?  244 HOH   B O    1 
HETATM 7031 O  O    . HOH   H 6 .   ? 25.441 -25.973 -1.320  1.00 30.18 ?  245 HOH   B O    1 
HETATM 7032 O  O    . HOH   H 6 .   ? 35.158 -8.009  -3.004  1.00 17.15 ?  246 HOH   B O    1 
HETATM 7033 O  O    . HOH   H 6 .   ? 34.274 -18.550 11.424  1.00 24.27 ?  247 HOH   B O    1 
HETATM 7034 O  O    . HOH   H 6 .   ? 46.448 -1.554  13.242  1.00 27.61 ?  248 HOH   B O    1 
HETATM 7035 O  O    . HOH   H 6 .   ? 42.673 -22.891 3.855   1.00 11.01 ?  249 HOH   B O    1 
HETATM 7036 O  O    . HOH   H 6 .   ? 38.987 -12.015 12.356  1.00 34.54 ?  250 HOH   B O    1 
HETATM 7037 O  O    . HOH   H 6 .   ? 39.534 -11.131 0.316   1.00 15.63 ?  251 HOH   B O    1 
HETATM 7038 O  O    . HOH   H 6 .   ? 51.017 -39.978 -8.207  1.00 33.47 ?  252 HOH   B O    1 
HETATM 7039 O  O    . HOH   H 6 .   ? 57.634 -24.437 -3.823  1.00 21.49 ?  253 HOH   B O    1 
HETATM 7040 O  O    . HOH   H 6 .   ? 51.600 -13.836 11.019  1.00 28.68 ?  254 HOH   B O    1 
HETATM 7041 O  O    . HOH   H 6 .   ? 41.908 -23.547 9.301   1.00 16.67 ?  255 HOH   B O    1 
HETATM 7042 O  O    . HOH   H 6 .   ? 38.522 -11.065 -2.261  1.00 18.41 ?  256 HOH   B O    1 
HETATM 7043 O  O    . HOH   H 6 .   ? 43.217 -32.413 -17.079 1.00 22.94 ?  257 HOH   B O    1 
HETATM 7044 O  O    . HOH   H 6 .   ? 48.045 -24.554 -17.796 1.00 30.28 ?  258 HOH   B O    1 
HETATM 7045 O  O    . HOH   H 6 .   ? 40.377 -12.781 -11.540 1.00 14.43 ?  259 HOH   B O    1 
HETATM 7046 O  O    . HOH   H 6 .   ? 49.786 -0.510  10.190  1.00 30.18 ?  260 HOH   B O    1 
HETATM 7047 O  O    . HOH   H 6 .   ? 29.750 -25.252 -10.803 1.00 15.76 ?  261 HOH   B O    1 
HETATM 7048 O  O    . HOH   H 6 .   ? 48.031 -22.798 5.831   1.00 16.34 ?  262 HOH   B O    1 
HETATM 7049 O  O    . HOH   H 6 .   ? 58.245 -10.657 -4.070  1.00 18.93 ?  263 HOH   B O    1 
HETATM 7050 O  O    . HOH   H 6 .   ? 56.183 -23.562 -14.733 1.00 26.51 ?  264 HOH   B O    1 
HETATM 7051 O  O    . HOH   H 6 .   ? 30.887 -15.742 2.678   1.00 12.69 ?  265 HOH   B O    1 
HETATM 7052 O  O    . HOH   H 6 .   ? 34.982 -33.371 -19.147 1.00 35.54 ?  266 HOH   B O    1 
HETATM 7053 O  O    . HOH   H 6 .   ? 56.997 -8.639  8.402   1.00 18.57 ?  267 HOH   B O    1 
HETATM 7054 O  O    . HOH   H 6 .   ? 28.518 -30.956 -14.722 1.00 31.02 ?  268 HOH   B O    1 
HETATM 7055 O  O    . HOH   H 6 .   ? 27.159 -31.859 -9.976  1.00 19.64 ?  269 HOH   B O    1 
HETATM 7056 O  O    . HOH   H 6 .   ? 31.875 -17.965 -14.508 1.00 30.88 ?  270 HOH   B O    1 
HETATM 7057 O  O    . HOH   H 6 .   ? 46.899 -29.623 9.826   1.00 32.11 ?  271 HOH   B O    1 
HETATM 7058 O  O    . HOH   H 6 .   ? 57.543 -9.236  1.444   1.00 19.64 ?  272 HOH   B O    1 
HETATM 7059 O  O    . HOH   H 6 .   ? 28.296 -34.403 -9.420  1.00 18.91 ?  273 HOH   B O    1 
HETATM 7060 O  O    . HOH   H 6 .   ? 43.400 -15.823 -12.170 1.00 13.76 ?  274 HOH   B O    1 
HETATM 7061 O  O    . HOH   H 6 .   ? 42.381 -9.935  9.354   1.00 19.91 ?  275 HOH   B O    1 
HETATM 7062 O  O    . HOH   H 6 .   ? 46.643 -31.310 -4.786  1.00 18.72 ?  276 HOH   B O    1 
HETATM 7063 O  O    . HOH   H 6 .   ? 42.965 -20.315 -20.717 1.00 35.22 ?  277 HOH   B O    1 
HETATM 7064 O  O    . HOH   H 6 .   ? 49.366 -28.739 -6.882  1.00 14.63 ?  278 HOH   B O    1 
HETATM 7065 O  O    . HOH   H 6 .   ? 34.511 -12.793 2.635   1.00 22.78 ?  279 HOH   B O    1 
HETATM 7066 O  O    . HOH   H 6 .   ? 41.207 -5.555  11.505  1.00 46.28 ?  280 HOH   B O    1 
HETATM 7067 O  O    . HOH   H 6 .   ? 42.431 -34.732 3.785   1.00 27.36 ?  281 HOH   B O    1 
HETATM 7068 O  O    . HOH   H 6 .   ? 27.628 -26.701 -15.658 1.00 33.23 ?  282 HOH   B O    1 
HETATM 7069 O  O    . HOH   H 6 .   ? 48.445 -25.071 3.124   1.00 12.93 ?  283 HOH   B O    1 
HETATM 7070 O  O    . HOH   H 6 .   ? 27.990 -22.925 -7.954  1.00 16.30 ?  284 HOH   B O    1 
HETATM 7071 O  O    . HOH   H 6 .   ? 59.841 -15.304 8.150   1.00 29.71 ?  285 HOH   B O    1 
HETATM 7072 O  O    . HOH   H 6 .   ? 57.082 -12.097 12.401  1.00 36.59 ?  286 HOH   B O    1 
HETATM 7073 O  O    . HOH   H 6 .   ? 47.123 -34.011 -4.620  1.00 16.80 ?  287 HOH   B O    1 
HETATM 7074 O  O    . HOH   H 6 .   ? 33.555 -15.312 -13.939 1.00 20.77 ?  288 HOH   B O    1 
HETATM 7075 O  O    . HOH   H 6 .   ? 42.329 -10.029 -14.923 1.00 35.86 ?  289 HOH   B O    1 
HETATM 7076 O  O    . HOH   H 6 .   ? 48.761 -20.050 5.935   1.00 13.27 ?  290 HOH   B O    1 
HETATM 7077 O  O    . HOH   H 6 .   ? 36.871 -12.786 -1.499  1.00 25.14 ?  291 HOH   B O    1 
HETATM 7078 O  O    . HOH   H 6 .   ? 44.665 -27.493 2.043   1.00 14.64 ?  292 HOH   B O    1 
HETATM 7079 O  O    . HOH   H 6 .   ? 51.277 -37.635 -9.582  1.00 25.11 ?  293 HOH   B O    1 
HETATM 7080 O  O    . HOH   H 6 .   ? 42.763 -12.299 -18.503 1.00 28.93 ?  294 HOH   B O    1 
HETATM 7081 O  O    . HOH   H 6 .   ? 49.961 -24.731 5.812   1.00 31.05 ?  295 HOH   B O    1 
HETATM 7082 O  O    . HOH   H 6 .   ? 52.560 -10.402 13.024  1.00 22.04 ?  296 HOH   B O    1 
HETATM 7083 O  O    . HOH   H 6 .   ? 30.578 -42.292 -10.553 1.00 29.34 ?  297 HOH   B O    1 
HETATM 7084 O  O    . HOH   H 6 .   ? 51.737 -5.978  -7.942  1.00 48.44 ?  298 HOH   B O    1 
HETATM 7085 O  O    . HOH   H 6 .   ? 45.965 -40.471 -3.598  1.00 27.93 ?  299 HOH   B O    1 
HETATM 7086 O  O    . HOH   H 6 .   ? 40.288 -10.856 -9.535  1.00 16.05 ?  300 HOH   B O    1 
HETATM 7087 O  O    . HOH   H 6 .   ? 52.651 -35.672 -8.626  1.00 29.61 ?  301 HOH   B O    1 
HETATM 7088 O  O    . HOH   H 6 .   ? 45.352 -33.420 -15.948 1.00 23.22 ?  302 HOH   B O    1 
HETATM 7089 O  O    . HOH   H 6 .   ? 44.079 -29.400 -4.660  1.00 22.69 ?  303 HOH   B O    1 
HETATM 7090 O  O    . HOH   H 6 .   ? 37.353 -35.644 7.258   1.00 33.90 ?  304 HOH   B O    1 
HETATM 7091 O  O    . HOH   H 6 .   ? 52.552 -29.272 -13.015 1.00 24.44 ?  305 HOH   B O    1 
HETATM 7092 O  O    . HOH   H 6 .   ? 37.514 -18.153 13.134  1.00 29.20 ?  306 HOH   B O    1 
HETATM 7093 O  O    . HOH   H 6 .   ? 25.971 -21.502 -3.506  1.00 15.30 ?  307 HOH   B O    1 
HETATM 7094 O  O    . HOH   H 6 .   ? 53.540 -30.229 4.507   1.00 18.13 ?  308 HOH   B O    1 
HETATM 7095 O  O    . HOH   H 6 .   ? 62.740 -13.594 4.750   1.00 27.48 ?  309 HOH   B O    1 
HETATM 7096 O  O    . HOH   H 6 .   ? 53.148 -16.073 -12.739 1.00 27.08 ?  310 HOH   B O    1 
HETATM 7097 O  O    . HOH   H 6 .   ? 37.882 -10.271 -10.753 1.00 16.25 ?  311 HOH   B O    1 
HETATM 7098 O  O    . HOH   H 6 .   ? 41.789 -8.083  1.326   1.00 22.39 ?  312 HOH   B O    1 
HETATM 7099 O  O    . HOH   H 6 .   ? 32.840 -34.630 -5.886  1.00 16.36 ?  313 HOH   B O    1 
HETATM 7100 O  O    . HOH   H 6 .   ? 35.065 -33.578 4.565   1.00 26.89 ?  314 HOH   B O    1 
HETATM 7101 O  O    . HOH   H 6 .   ? 51.423 -33.011 -10.758 1.00 40.61 ?  315 HOH   B O    1 
HETATM 7102 O  O    . HOH   H 6 .   ? 43.257 -21.435 10.699  1.00 15.66 ?  316 HOH   B O    1 
HETATM 7103 O  O    . HOH   H 6 .   ? 37.136 -30.573 -21.010 1.00 31.07 ?  317 HOH   B O    1 
HETATM 7104 O  O    . HOH   H 6 .   ? 57.698 -22.096 3.186   1.00 27.91 ?  318 HOH   B O    1 
HETATM 7105 O  O    . HOH   H 6 .   ? 26.375 -21.055 -6.229  1.00 15.22 ?  319 HOH   B O    1 
HETATM 7106 O  O    . HOH   H 6 .   ? 38.388 -12.727 7.951   1.00 17.95 ?  320 HOH   B O    1 
HETATM 7107 O  O    . HOH   H 6 .   ? 53.724 -12.598 -22.226 1.00 33.09 ?  321 HOH   B O    1 
HETATM 7108 O  O    . HOH   H 6 .   ? 43.521 -15.414 18.194  1.00 28.85 ?  322 HOH   B O    1 
HETATM 7109 O  O    . HOH   H 6 .   ? 62.931 -20.136 -0.781  1.00 38.54 ?  323 HOH   B O    1 
HETATM 7110 O  O    . HOH   H 6 .   ? 60.024 -17.191 -10.492 1.00 32.82 ?  324 HOH   B O    1 
HETATM 7111 O  O    . HOH   H 6 .   ? 44.657 -24.631 9.585   1.00 19.53 ?  325 HOH   B O    1 
HETATM 7112 O  O    . HOH   H 6 .   ? 41.218 -24.504 15.823  1.00 45.34 ?  326 HOH   B O    1 
HETATM 7113 O  O    . HOH   H 6 .   ? 36.758 -12.427 4.293   1.00 17.23 ?  327 HOH   B O    1 
HETATM 7114 O  O    . HOH   H 6 .   ? 48.112 -32.692 -16.651 1.00 42.80 ?  328 HOH   B O    1 
HETATM 7115 O  O    . HOH   H 6 .   ? 27.876 -14.809 -9.456  1.00 33.82 ?  329 HOH   B O    1 
HETATM 7116 O  O    . HOH   H 6 .   ? 44.206 -1.751  7.576   1.00 46.67 ?  330 HOH   B O    1 
HETATM 7117 O  O    . HOH   H 6 .   ? 43.144 -34.654 0.115   1.00 19.67 ?  331 HOH   B O    1 
HETATM 7118 O  O    . HOH   H 6 .   ? 38.444 -9.373  -13.279 1.00 25.62 ?  332 HOH   B O    1 
HETATM 7119 O  O    . HOH   H 6 .   ? 33.630 -31.221 11.053  1.00 32.78 ?  333 HOH   B O    1 
HETATM 7120 O  O    . HOH   H 6 .   ? 47.210 -24.513 8.171   1.00 27.19 ?  334 HOH   B O    1 
HETATM 7121 O  O    . HOH   H 6 .   ? 42.886 -43.540 -14.311 1.00 42.71 ?  335 HOH   B O    1 
HETATM 7122 O  O    . HOH   H 6 .   ? 39.545 -23.513 -20.348 1.00 35.67 ?  336 HOH   B O    1 
HETATM 7123 O  O    . HOH   H 6 .   ? 48.644 -11.932 -13.889 1.00 26.61 ?  337 HOH   B O    1 
HETATM 7124 O  O    . HOH   H 6 .   ? 47.512 -27.460 2.026   1.00 14.14 ?  338 HOH   B O    1 
HETATM 7125 O  O    . HOH   H 6 .   ? 45.717 -36.312 -16.074 1.00 36.32 ?  339 HOH   B O    1 
HETATM 7126 O  O    . HOH   H 6 .   ? 46.828 -19.902 12.289  1.00 29.57 ?  340 HOH   B O    1 
HETATM 7127 O  O    . HOH   H 6 .   ? 37.048 -15.098 -16.535 1.00 39.62 ?  341 HOH   B O    1 
HETATM 7128 O  O    . HOH   H 6 .   ? 37.106 -45.222 -9.785  1.00 36.79 ?  342 HOH   B O    1 
HETATM 7129 O  O    . HOH   H 6 .   ? 28.896 -42.987 -12.334 1.00 36.24 ?  343 HOH   B O    1 
HETATM 7130 O  O    . HOH   H 6 .   ? 38.510 -12.294 -16.237 1.00 41.73 ?  344 HOH   B O    1 
HETATM 7131 O  O    . HOH   H 6 .   ? 33.034 -14.704 1.064   1.00 17.36 ?  345 HOH   B O    1 
HETATM 7132 O  O    . HOH   H 6 .   ? 39.842 -44.339 -11.190 1.00 38.80 ?  346 HOH   B O    1 
HETATM 7133 O  O    . HOH   H 6 .   ? 27.802 -26.603 -0.575  1.00 29.83 ?  347 HOH   B O    1 
HETATM 7134 O  O    . HOH   H 6 .   ? 38.599 -22.348 15.045  1.00 39.28 ?  348 HOH   B O    1 
HETATM 7135 O  O    . HOH   H 6 .   ? 33.768 -9.435  -8.872  1.00 31.24 ?  349 HOH   B O    1 
HETATM 7136 O  O    . HOH   H 6 .   ? 62.637 -20.101 -4.793  1.00 47.27 ?  350 HOH   B O    1 
HETATM 7137 O  O    . HOH   H 6 .   ? 40.473 -43.544 -9.094  1.00 27.05 ?  351 HOH   B O    1 
HETATM 7138 O  O    . HOH   H 6 .   ? 55.667 -8.257  10.820  1.00 26.12 ?  352 HOH   B O    1 
HETATM 7139 O  O    . HOH   H 6 .   ? 34.640 -10.335 7.562   1.00 23.39 ?  353 HOH   B O    1 
HETATM 7140 O  O    . HOH   H 6 .   ? 56.613 -7.288  3.099   1.00 26.86 ?  354 HOH   B O    1 
HETATM 7141 O  O    . HOH   H 6 .   ? 36.133 -8.583  -9.735  1.00 33.93 ?  355 HOH   B O    1 
HETATM 7142 O  O    . HOH   H 6 .   ? 44.161 -37.329 -17.821 1.00 34.59 ?  356 HOH   B O    1 
HETATM 7143 O  O    . HOH   H 6 .   ? 23.217 -23.706 6.803   1.00 33.57 ?  357 HOH   B O    1 
HETATM 7144 O  O    . HOH   H 6 .   ? 34.124 -7.822  11.418  1.00 40.06 ?  358 HOH   B O    1 
HETATM 7145 O  O    . HOH   H 6 .   ? 43.191 -12.716 -21.183 1.00 38.48 ?  359 HOH   B O    1 
HETATM 7146 O  O    . HOH   H 6 .   ? 61.561 -19.932 1.681   1.00 38.11 ?  360 HOH   B O    1 
HETATM 7147 O  O    . HOH   H 6 .   ? 57.013 -21.561 -16.344 1.00 38.76 ?  361 HOH   B O    1 
HETATM 7148 O  O    . HOH   H 6 .   ? 40.275 -8.834  9.913   1.00 32.93 ?  362 HOH   B O    1 
HETATM 7149 O  O    . HOH   H 6 .   ? 27.195 -25.979 -11.450 1.00 33.88 ?  363 HOH   B O    1 
HETATM 7150 O  O    . HOH   H 6 .   ? 54.230 -5.752  3.046   1.00 34.71 ?  364 HOH   B O    1 
HETATM 7151 O  O    . HOH   H 6 .   ? 32.590 -23.625 14.085  1.00 40.36 ?  365 HOH   B O    1 
HETATM 7152 O  O    . HOH   H 6 .   ? 59.032 -10.529 9.144   1.00 35.67 ?  366 HOH   B O    1 
HETATM 7153 O  O    . HOH   H 6 .   ? 36.207 -8.707  8.988   1.00 38.24 ?  367 HOH   B O    1 
HETATM 7154 O  O    . HOH   H 6 .   ? 40.108 -11.396 -13.999 1.00 30.85 ?  368 HOH   B O    1 
HETATM 7155 O  O    . HOH   H 6 .   ? 48.468 -26.525 8.766   1.00 38.29 ?  369 HOH   B O    1 
HETATM 7156 O  O    . HOH   H 6 .   ? 39.919 -7.014  7.889   1.00 39.46 ?  370 HOH   B O    1 
HETATM 7157 O  O    . HOH   H 6 .   ? 41.877 -10.061 -17.487 1.00 48.91 ?  371 HOH   B O    1 
HETATM 7158 O  O    . HOH   H 6 .   ? 56.093 -7.811  -0.629  1.00 32.35 ?  372 HOH   B O    1 
HETATM 7159 O  O    . HOH   H 6 .   ? 52.097 -12.940 13.362  1.00 28.73 ?  373 HOH   B O    1 
HETATM 7160 O  O    . HOH   H 6 .   ? 62.978 -12.349 6.939   1.00 39.03 ?  374 HOH   B O    1 
HETATM 7161 O  O    . HOH   H 6 .   ? 41.919 -6.814  -4.870  1.00 45.44 ?  375 HOH   B O    1 
HETATM 7162 O  O    . HOH   H 6 .   ? 38.071 -10.578 10.068  1.00 28.54 ?  376 HOH   B O    1 
HETATM 7163 O  O    . HOH   H 6 .   ? 36.564 -22.894 13.291  1.00 24.96 ?  377 HOH   B O    1 
HETATM 7164 O  O    . HOH   H 6 .   ? 42.690 -17.123 -23.197 1.00 44.74 ?  378 HOH   B O    1 
HETATM 7165 O  O    . HOH   H 6 .   ? 40.174 -7.651  3.190   1.00 37.44 ?  379 HOH   B O    1 
HETATM 7166 O  O    . HOH   H 6 .   ? 44.053 -5.628  -3.479  1.00 41.45 ?  380 HOH   B O    1 
HETATM 7167 O  O    . HOH   H 6 .   ? 39.699 -14.059 15.690  1.00 51.92 ?  381 HOH   B O    1 
HETATM 7168 O  O    . HOH   H 6 .   ? 52.906 -29.918 7.199   1.00 22.35 ?  382 HOH   B O    1 
HETATM 7169 O  O    . HOH   H 6 .   ? 60.532 -22.317 2.858   1.00 47.21 ?  383 HOH   B O    1 
HETATM 7170 O  O    . HOH   H 6 .   ? 25.835 -18.935 -11.862 1.00 37.25 ?  384 HOH   B O    1 
HETATM 7171 O  O    . HOH   H 6 .   ? 46.821 -5.332  2.890   1.00 41.99 ?  385 HOH   B O    1 
HETATM 7172 O  O    . HOH   H 6 .   ? 35.488 -33.726 7.394   1.00 40.15 ?  386 HOH   B O    1 
HETATM 7173 O  O    . HOH   H 6 .   ? 35.338 -20.364 13.327  1.00 29.77 ?  387 HOH   B O    1 
HETATM 7174 O  O    . HOH   H 6 .   ? 40.946 -9.773  15.810  1.00 43.32 ?  388 HOH   B O    1 
HETATM 7175 O  O    . HOH   H 6 .   ? 23.986 -20.951 -7.730  1.00 26.31 ?  389 HOH   B O    1 
HETATM 7176 O  O    . HOH   H 6 .   ? 40.780 -6.626  -0.868  1.00 24.25 ?  390 HOH   B O    1 
HETATM 7177 O  O    . HOH   H 6 .   ? 44.067 -31.810 -3.835  1.00 34.56 ?  391 HOH   B O    1 
HETATM 7178 O  O    . HOH   H 6 .   ? 26.672 -28.011 -13.429 1.00 35.79 ?  392 HOH   B O    1 
HETATM 7179 O  O    . HOH   H 6 .   ? 27.939 -27.111 2.187   1.00 29.87 ?  393 HOH   B O    1 
HETATM 7180 O  O    . HOH   H 6 .   ? 34.386 -33.488 9.606   1.00 33.36 ?  394 HOH   B O    1 
HETATM 7181 O  O    . HOH   H 6 .   ? 24.652 -20.649 -10.490 1.00 36.76 ?  395 HOH   B O    1 
HETATM 7182 O  O    . HOH   H 6 .   ? 50.680 -30.853 8.693   1.00 27.74 ?  396 HOH   B O    1 
HETATM 7183 O  O    . HOH   H 6 .   ? 26.859 -30.699 -12.629 1.00 28.31 ?  397 HOH   B O    1 
HETATM 7184 O  O    . HOH   H 6 .   ? 45.723 -20.134 15.187  1.00 50.70 ?  398 HOH   B O    1 
HETATM 7185 O  O    . HOH   H 6 .   ? 57.748 -6.594  -2.363  1.00 34.38 ?  399 HOH   B O    1 
HETATM 7186 O  O    . HOH   H 6 .   ? 40.922 -11.805 -22.320 1.00 41.79 ?  400 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   A VAL   A 3   ? 0.6664 0.6646 0.7245 -0.0092 -0.0382 0.0823  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.6652 0.6639 0.7108 -0.0110 -0.0338 0.0685  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.6633 0.6622 0.7144 -0.0107 -0.0362 0.0820  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.6621 0.6613 0.7027 -0.0124 -0.0326 0.0692  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.6472 0.6482 0.6881 -0.0179 -0.0370 0.0835  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.6466 0.6475 0.6808 -0.0188 -0.0348 0.0764  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.6506 0.6522 0.7023 -0.0165 -0.0398 0.0850  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.6500 0.6511 0.6939 -0.0177 -0.0371 0.0772  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.6734 0.6716 0.7210 -0.0064 -0.0336 0.0799  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.6717 0.6703 0.7079 -0.0085 -0.0295 0.0635  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.6777 0.6748 0.7225 -0.0039 -0.0330 0.0791  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.6758 0.6735 0.7093 -0.0065 -0.0285 0.0615  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.6756 0.6745 0.7236 -0.0056 -0.0327 0.0792  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.6738 0.6729 0.7102 -0.0078 -0.0285 0.0616  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.6243 0.6274 0.6368 -0.0271 -0.0339 0.0820  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.5754 0.5835 0.5376 -0.0455 -0.0279 0.0837  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.5133 0.5379 0.4725 -0.0620 -0.0055 0.0479  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.5154 0.5415 0.4695 -0.0647 -0.0069 0.0508  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.5853 0.5840 0.4939 -0.0471 -0.0424 0.1202  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.5912 0.5831 0.4525 -0.0487 -0.0553 0.1530  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.5948 0.5828 0.4372 -0.0506 -0.0587 0.1646  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.5918 0.5820 0.4380 -0.0475 -0.0614 0.1665  4   ASN   A ND2 
46   N  N   A SER   A 5   ? 0.4767 0.5124 0.4383 -0.0728 0.0110  0.0276  5   SER   A N   
47   N  N   B SER   A 5   ? 0.4834 0.5106 0.4422 -0.0656 0.0025  0.0297  5   SER   A N   
48   C  CA  A SER   A 5   ? 0.4370 0.4847 0.4027 -0.0834 0.0310  0.0082  5   SER   A CA  
49   C  CA  B SER   A 5   ? 0.4507 0.4811 0.4106 -0.0697 0.0130  0.0128  5   SER   A CA  
50   C  C   A SER   A 5   ? 0.3910 0.4451 0.3592 -0.0925 0.0540  -0.0016 5   SER   A C   
51   C  C   B SER   A 5   ? 0.4122 0.4437 0.3667 -0.0718 0.0248  0.0032  5   SER   A C   
52   O  O   A SER   A 5   ? 0.3966 0.4509 0.3617 -0.0844 0.0578  -0.0102 5   SER   A O   
53   O  O   B SER   A 5   ? 0.4148 0.4462 0.3682 -0.0700 0.0252  -0.0022 5   SER   A O   
54   C  CB  A SER   A 5   ? 0.4422 0.4936 0.4160 -0.0850 0.0284  0.0003  5   SER   A CB  
55   C  CB  B SER   A 5   ? 0.4553 0.4871 0.4243 -0.0720 0.0119  0.0066  5   SER   A CB  
56   O  OG  A SER   A 5   ? 0.4449 0.4982 0.4208 -0.0862 0.0275  -0.0030 5   SER   A OG  
57   O  OG  B SER   A 5   ? 0.4575 0.4902 0.4296 -0.0738 0.0109  0.0032  5   SER   A OG  
68   N  N   A PHE   A 6   ? 0.3366 0.3977 0.3022 -0.1086 0.0770  0.0039  6   PHE   A N   
69   N  N   B PHE   A 6   ? 0.3689 0.4023 0.3156 -0.0748 0.0385  0.0025  6   PHE   A N   
70   C  CA  A PHE   A 6   ? 0.2863 0.3469 0.2503 -0.1168 0.0912  0.0185  6   PHE   A CA  
71   C  CA  B PHE   A 6   ? 0.3265 0.3592 0.2706 -0.0743 0.0511  0.0061  6   PHE   A CA  
72   C  C   A PHE   A 6   ? 0.2769 0.3376 0.2509 -0.1163 0.0983  0.0111  6   PHE   A C   
73   C  C   B PHE   A 6   ? 0.3102 0.3458 0.2597 -0.0759 0.0638  0.0041  6   PHE   A C   
74   O  O   A PHE   A 6   ? 0.2838 0.3392 0.2742 -0.1157 0.1082  0.0213  6   PHE   A O   
75   O  O   B PHE   A 6   ? 0.3096 0.3444 0.2514 -0.0823 0.0736  0.0134  6   PHE   A O   
76   C  CB  A PHE   A 6   ? 0.2572 0.3089 0.2170 -0.1105 0.0780  0.0329  6   PHE   A CB  
77   C  CB  B PHE   A 6   ? 0.3046 0.3309 0.2435 -0.0659 0.0438  0.0075  6   PHE   A CB  
78   C  CG  A PHE   A 6   ? 0.2351 0.2801 0.2006 -0.0925 0.0616  0.0347  6   PHE   A CG  
79   C  CG  B PHE   A 6   ? 0.2849 0.3054 0.2272 -0.0567 0.0352  0.0090  6   PHE   A CG  
80   C  CD1 A PHE   A 6   ? 0.2257 0.2676 0.1928 -0.0827 0.0470  0.0348  6   PHE   A CD1 
81   C  CD1 B PHE   A 6   ? 0.2763 0.2951 0.2198 -0.0527 0.0285  0.0104  6   PHE   A CD1 
82   C  CD2 A PHE   A 6   ? 0.2369 0.2728 0.2109 -0.0721 0.0522  0.0321  6   PHE   A CD2 
83   C  CD2 B PHE   A 6   ? 0.2802 0.2944 0.2264 -0.0467 0.0327  0.0089  6   PHE   A CD2 
84   C  CE1 A PHE   A 6   ? 0.2219 0.2624 0.1970 -0.0744 0.0451  0.0368  6   PHE   A CE1 
85   C  CE1 B PHE   A 6   ? 0.2714 0.2885 0.2185 -0.0488 0.0288  0.0124  6   PHE   A CE1 
86   C  CE2 A PHE   A 6   ? 0.2332 0.2669 0.2182 -0.0650 0.0497  0.0313  6   PHE   A CE2 
87   C  CE2 B PHE   A 6   ? 0.2761 0.2880 0.2262 -0.0428 0.0314  0.0106  6   PHE   A CE2 
88   C  CZ  A PHE   A 6   ? 0.2257 0.2608 0.2052 -0.0683 0.0464  0.0335  6   PHE   A CZ  
89   C  CZ  B PHE   A 6   ? 0.2721 0.2852 0.2185 -0.0447 0.0289  0.0111  6   PHE   A CZ  
108  N  N   A SER   A 7   ? 0.2605 0.3245 0.2266 -0.1132 0.0991  -0.0002 7   SER   A N   
109  N  N   B SER   A 7   ? 0.2958 0.3337 0.2624 -0.0686 0.0603  -0.0073 7   SER   A N   
110  C  CA  A SER   A 7   ? 0.2529 0.3148 0.2269 -0.0989 0.0820  -0.0206 7   SER   A CA  
111  C  CA  B SER   A 7   ? 0.2871 0.3266 0.2717 -0.0547 0.0535  -0.0179 7   SER   A CA  
112  C  C   A SER   A 7   ? 0.2284 0.2764 0.1996 -0.0954 0.0750  -0.0282 7   SER   A C   
113  C  C   B SER   A 7   ? 0.2688 0.3067 0.2512 -0.0474 0.0566  -0.0139 7   SER   A C   
114  O  O   A SER   A 7   ? 0.2408 0.2649 0.1885 -0.0999 0.0777  -0.0297 7   SER   A O   
115  O  O   B SER   A 7   ? 0.2729 0.3076 0.2473 -0.0443 0.0534  -0.0134 7   SER   A O   
116  C  CB  A SER   A 7   ? 0.2722 0.3395 0.2547 -0.0852 0.0713  -0.0250 7   SER   A CB  
117  C  CB  B SER   A 7   ? 0.2953 0.3375 0.3000 -0.0499 0.0462  -0.0263 7   SER   A CB  
118  O  OG  A SER   A 7   ? 0.2885 0.3564 0.2735 -0.0736 0.0581  -0.0331 7   SER   A OG  
119  O  OG  B SER   A 7   ? 0.3005 0.3448 0.3232 -0.0456 0.0366  -0.0339 7   SER   A OG  
130  N  N   A GLY   A 8   ? 0.2003 0.2508 0.1948 -0.0818 0.0624  -0.0291 8   GLY   A N   
131  N  N   B GLY   A 8   ? 0.2494 0.2874 0.2250 -0.0429 0.0596  -0.0132 8   GLY   A N   
132  C  CA  A GLY   A 8   ? 0.1832 0.2269 0.1915 -0.0568 0.0539  -0.0251 8   GLY   A CA  
133  C  CA  B GLY   A 8   ? 0.2297 0.2652 0.2067 -0.0393 0.0569  -0.0070 8   GLY   A CA  
134  C  C   A GLY   A 8   ? 0.1637 0.2101 0.1886 -0.0308 0.0390  -0.0151 8   GLY   A C   
135  C  C   B GLY   A 8   ? 0.2103 0.2450 0.1825 -0.0363 0.0541  0.0015  8   GLY   A C   
136  O  O   A GLY   A 8   ? 0.1672 0.2128 0.1971 -0.0064 0.0359  -0.0320 8   GLY   A O   
137  O  O   B GLY   A 8   ? 0.2102 0.2461 0.1828 -0.0279 0.0573  -0.0030 8   GLY   A O   
144  N  N   A TYR   A 9   ? 0.1451 0.1889 0.1729 -0.0244 0.0356  0.0085  9   TYR   A N   
145  N  N   B TYR   A 9   ? 0.1886 0.2227 0.1764 -0.0359 0.0470  0.0099  9   TYR   A N   
146  C  CA  A TYR   A 9   ? 0.1320 0.1673 0.1636 -0.0220 0.0267  0.0111  9   TYR   A CA  
147  C  CA  B TYR   A 9   ? 0.1787 0.2022 0.1764 -0.0322 0.0409  0.0114  9   TYR   A CA  
148  C  C   A TYR   A 9   ? 0.1326 0.1491 0.1678 -0.0116 0.0331  0.0293  9   TYR   A C   
149  C  C   B TYR   A 9   ? 0.1867 0.1866 0.1759 -0.0270 0.0501  0.0149  9   TYR   A C   
150  O  O   A TYR   A 9   ? 0.1596 0.1625 0.1936 -0.0164 0.0244  0.0239  9   TYR   A O   
151  O  O   B TYR   A 9   ? 0.1981 0.1960 0.1870 -0.0302 0.0464  0.0256  9   TYR   A O   
152  C  CB  A TYR   A 9   ? 0.1310 0.1789 0.1778 -0.0173 0.0247  0.0076  9   TYR   A CB  
153  C  CB  B TYR   A 9   ? 0.1666 0.2012 0.1799 -0.0304 0.0343  0.0083  9   TYR   A CB  
154  C  CG  A TYR   A 9   ? 0.1374 0.1850 0.1956 -0.0114 0.0433  -0.0067 9   TYR   A CG  
155  C  CG  B TYR   A 9   ? 0.1577 0.2000 0.1821 -0.0285 0.0410  0.0021  9   TYR   A CG  
156  C  CD1 A TYR   A 9   ? 0.1439 0.1924 0.2094 -0.0197 0.0549  -0.0197 9   TYR   A CD1 
157  C  CD1 B TYR   A 9   ? 0.1615 0.2027 0.1960 -0.0327 0.0489  -0.0077 9   TYR   A CD1 
158  C  CD2 A TYR   A 9   ? 0.1395 0.1833 0.2048 -0.0073 0.0355  0.0022  9   TYR   A CD2 
159  C  CD2 B TYR   A 9   ? 0.1545 0.1975 0.1738 -0.0239 0.0399  0.0020  9   TYR   A CD2 
160  C  CE1 A TYR   A 9   ? 0.1525 0.1984 0.2360 -0.0218 0.0578  -0.0302 9   TYR   A CE1 
161  C  CE1 B TYR   A 9   ? 0.1634 0.2025 0.2027 -0.0317 0.0559  -0.0143 9   TYR   A CE1 
162  C  CE2 A TYR   A 9   ? 0.1433 0.1902 0.2145 -0.0070 0.0484  -0.0097 9   TYR   A CE2 
163  C  CE2 B TYR   A 9   ? 0.1550 0.2005 0.1782 -0.0206 0.0500  -0.0002 9   TYR   A CE2 
164  C  CZ  A TYR   A 9   ? 0.1497 0.1999 0.2408 -0.0252 0.0606  -0.0212 9   TYR   A CZ  
165  C  CZ  B TYR   A 9   ? 0.1577 0.2007 0.2015 -0.0281 0.0662  -0.0058 9   TYR   A CZ  
166  O  OH  A TYR   A 9   ? 0.1648 0.2135 0.2656 -0.0464 0.0633  -0.0211 9   TYR   A OH  
167  O  OH  B TYR   A 9   ? 0.1633 0.2059 0.2182 -0.0343 0.0794  -0.0023 9   TYR   A OH  
186  N  N   A LEU   A 10  ? 0.1247 0.1384 0.1767 -0.0160 0.0273  0.0304  10  LEU   A N   
187  N  N   B LEU   A 10  ? 0.1910 0.1749 0.1845 -0.0220 0.0433  0.0097  10  LEU   A N   
188  C  CA  A LEU   A 10  ? 0.1141 0.1318 0.1816 -0.0158 0.0262  0.0393  10  LEU   A CA  
189  C  CA  B LEU   A 10  ? 0.1949 0.1744 0.1987 -0.0219 0.0434  0.0043  10  LEU   A CA  
190  C  C   A LEU   A 10  ? 0.1135 0.1287 0.1897 -0.0160 0.0236  0.0437  10  LEU   A C   
191  C  C   B LEU   A 10  ? 0.1790 0.1547 0.1773 -0.0242 0.0369  0.0172  10  LEU   A C   
192  O  O   A LEU   A 10  ? 0.1131 0.1274 0.2049 -0.0070 0.0311  0.0409  10  LEU   A O   
193  O  O   B LEU   A 10  ? 0.1767 0.1510 0.1823 -0.0229 0.0424  0.0334  10  LEU   A O   
194  C  CB  A LEU   A 10  ? 0.1183 0.1358 0.2042 -0.0162 0.0097  0.0483  10  LEU   A CB  
195  C  CB  B LEU   A 10  ? 0.2200 0.1948 0.2382 -0.0281 0.0313  -0.0040 10  LEU   A CB  
196  C  CG  A LEU   A 10  ? 0.1428 0.1567 0.2370 -0.0068 -0.0172 0.0679  10  LEU   A CG  
197  C  CG  B LEU   A 10  ? 0.2483 0.2230 0.2878 -0.0298 0.0157  -0.0094 10  LEU   A CG  
198  C  CD1 A LEU   A 10  ? 0.1612 0.1685 0.2578 -0.0160 -0.0077 0.0528  10  LEU   A CD1 
199  C  CD1 B LEU   A 10  ? 0.2596 0.2300 0.3040 -0.0256 0.0185  -0.0103 10  LEU   A CD1 
200  C  CD2 A LEU   A 10  ? 0.1624 0.1828 0.2510 -0.0001 -0.0138 0.0632  10  LEU   A CD2 
201  C  CD2 B LEU   A 10  ? 0.2533 0.2288 0.2942 -0.0349 0.0059  -0.0155 10  LEU   A CD2 
224  N  N   A LYS   A 11  ? 0.1247 0.1336 0.1762 -0.0116 0.0262  0.0340  11  LYS   A N   
225  N  N   B LYS   A 11  ? 0.1721 0.1438 0.1602 -0.0243 0.0260  0.0138  11  LYS   A N   
226  C  CA  A LYS   A 11  ? 0.1282 0.1315 0.1824 -0.0208 0.0208  0.0339  11  LYS   A CA  
227  C  CA  B LYS   A 11  ? 0.1635 0.1361 0.1553 -0.0245 0.0246  0.0138  11  LYS   A CA  
228  C  C   A LYS   A 11  ? 0.1269 0.1318 0.1776 -0.0182 0.0234  0.0188  11  LYS   A C   
229  C  C   B LYS   A 11  ? 0.1415 0.1201 0.1511 -0.0218 0.0203  0.0074  11  LYS   A C   
230  O  O   A LYS   A 11  ? 0.1349 0.1460 0.2137 -0.0375 0.0289  -0.0020 11  LYS   A O   
231  O  O   B LYS   A 11  ? 0.1336 0.1197 0.1737 -0.0205 0.0282  -0.0095 11  LYS   A O   
232  C  CB  A LYS   A 11  ? 0.1320 0.1300 0.1762 -0.0163 0.0159  0.0302  11  LYS   A CB  
233  C  CB  B LYS   A 11  ? 0.1737 0.1373 0.1603 -0.0228 0.0252  0.0176  11  LYS   A CB  
234  C  CG  A LYS   A 11  ? 0.1374 0.1333 0.1855 -0.0123 0.0217  0.0353  11  LYS   A CG  
235  C  CG  B LYS   A 11  ? 0.1787 0.1426 0.1553 -0.0184 0.0293  0.0223  11  LYS   A CG  
236  C  CD  A LYS   A 11  ? 0.1486 0.1367 0.1867 -0.0187 0.0120  0.0350  11  LYS   A CD  
237  C  CD  B LYS   A 11  ? 0.1820 0.1512 0.1576 -0.0173 0.0272  0.0273  11  LYS   A CD  
238  C  CE  A LYS   A 11  ? 0.1609 0.1351 0.1843 -0.0083 0.0091  0.0385  11  LYS   A CE  
239  C  CE  B LYS   A 11  ? 0.1820 0.1527 0.1472 -0.0179 0.0195  0.0310  11  LYS   A CE  
240  N  NZ  A LYS   A 11  ? 0.1560 0.1342 0.1876 0.0049  0.0105  0.0302  11  LYS   A NZ  
241  N  NZ  B LYS   A 11  ? 0.1803 0.1557 0.1484 -0.0093 0.0217  0.0274  11  LYS   A NZ  
268  N  N   A LEU   A 12  ? 0.1223 0.1253 0.1567 -0.0171 0.0199  0.0218  12  LEU   A N   
269  N  N   B LEU   A 12  ? 0.1322 0.1291 0.1475 -0.0098 0.0106  0.0057  12  LEU   A N   
270  C  CA  A LEU   A 12  ? 0.1275 0.1306 0.1525 -0.0123 0.0111  0.0262  12  LEU   A CA  
271  C  CA  B LEU   A 12  ? 0.1253 0.1375 0.1491 -0.0064 0.0130  0.0049  12  LEU   A CA  
272  C  C   A LEU   A 12  ? 0.1288 0.1240 0.1616 -0.0189 0.0117  0.0254  12  LEU   A C   
273  C  C   B LEU   A 12  ? 0.1252 0.1396 0.1406 -0.0030 0.0201  0.0090  12  LEU   A C   
274  O  O   A LEU   A 12  ? 0.1331 0.1247 0.1714 -0.0171 0.0194  0.0020  12  LEU   A O   
275  O  O   B LEU   A 12  ? 0.1299 0.1361 0.1267 0.0067  0.0170  0.0057  12  LEU   A O   
276  C  CB  A LEU   A 12  ? 0.1369 0.1301 0.1555 -0.0102 0.0008  0.0279  12  LEU   A CB  
277  C  CB  B LEU   A 12  ? 0.1250 0.1421 0.1651 -0.0059 0.0123  0.0092  12  LEU   A CB  
278  C  CG  A LEU   A 12  ? 0.1500 0.1439 0.1837 -0.0045 0.0120  0.0227  12  LEU   A CG  
279  C  CG  B LEU   A 12  ? 0.1263 0.1403 0.1853 -0.0047 0.0125  0.0036  12  LEU   A CG  
280  C  CD1 A LEU   A 12  ? 0.1634 0.1431 0.1902 0.0055  0.0214  0.0350  12  LEU   A CD1 
281  C  CD1 B LEU   A 12  ? 0.1267 0.1461 0.1986 0.0021  0.0241  0.0091  12  LEU   A CD1 
282  C  CD2 A LEU   A 12  ? 0.1535 0.1525 0.2053 -0.0055 0.0091  0.0231  12  LEU   A CD2 
283  C  CD2 B LEU   A 12  ? 0.1271 0.1360 0.1875 -0.0022 0.0069  -0.0133 12  LEU   A CD2 
306  N  N   A THR   A 13  ? 0.1253 0.1266 0.1763 -0.0152 0.0127  0.0173  13  THR   A N   
307  N  N   B THR   A 13  ? 0.1210 0.1374 0.1500 -0.0039 0.0182  0.0043  13  THR   A N   
308  C  CA  A THR   A 13  ? 0.1291 0.1301 0.1791 -0.0118 0.0231  0.0158  13  THR   A CA  
309  C  CA  B THR   A 13  ? 0.1263 0.1393 0.1654 -0.0075 0.0237  0.0098  13  THR   A CA  
310  C  C   A THR   A 13  ? 0.1244 0.1273 0.1920 -0.0137 0.0205  0.0368  13  THR   A C   
311  C  C   B THR   A 13  ? 0.1322 0.1480 0.1665 -0.0136 0.0280  0.0192  13  THR   A C   
312  O  O   A THR   A 13  ? 0.1272 0.1289 0.1967 -0.0045 0.0141  0.0366  13  THR   A O   
313  O  O   B THR   A 13  ? 0.1417 0.1541 0.1685 -0.0159 0.0157  0.0206  13  THR   A O   
314  C  CB  A THR   A 13  ? 0.1362 0.1397 0.1889 -0.0091 0.0266  0.0283  13  THR   A CB  
315  C  CB  B THR   A 13  ? 0.1235 0.1466 0.1811 -0.0034 0.0265  0.0189  13  THR   A CB  
316  O  OG1 A THR   A 13  ? 0.1425 0.1313 0.1988 -0.0059 0.0113  0.0328  13  THR   A OG1 
317  O  OG1 B THR   A 13  ? 0.1073 0.1470 0.1916 -0.0069 0.0376  0.0260  13  THR   A OG1 
318  C  CG2 A THR   A 13  ? 0.1416 0.1592 0.2056 -0.0108 0.0284  0.0165  13  THR   A CG2 
319  C  CG2 B THR   A 13  ? 0.1294 0.1541 0.1892 0.0041  0.0239  0.0151  13  THR   A CG2 
334  N  N   A ASP   A 14  ? 0.1267 0.1339 0.2093 -0.0140 0.0131  0.0399  14  ASP   A N   
335  N  N   B ASP   A 14  ? 0.1339 0.1507 0.1802 -0.0165 0.0226  0.0206  14  ASP   A N   
336  C  CA  A ASP   A 14  ? 0.1368 0.1416 0.2277 -0.0098 0.0027  0.0619  14  ASP   A CA  
337  C  CA  B ASP   A 14  ? 0.1395 0.1560 0.1996 -0.0156 0.0131  0.0355  14  ASP   A CA  
338  C  C   A ASP   A 14  ? 0.1361 0.1454 0.1996 -0.0130 -0.0066 0.0534  14  ASP   A C   
339  C  C   B ASP   A 14  ? 0.1322 0.1494 0.1904 -0.0150 0.0011  0.0429  14  ASP   A C   
340  O  O   A ASP   A 14  ? 0.1493 0.1576 0.1972 -0.0186 -0.0104 0.0560  14  ASP   A O   
341  O  O   B ASP   A 14  ? 0.1376 0.1531 0.1974 -0.0203 -0.0048 0.0500  14  ASP   A O   
342  C  CB  A ASP   A 14  ? 0.1563 0.1647 0.2927 -0.0122 0.0068  0.0813  14  ASP   A CB  
343  C  CB  B ASP   A 14  ? 0.1539 0.1715 0.2387 -0.0153 0.0068  0.0437  14  ASP   A CB  
344  C  CG  A ASP   A 14  ? 0.1809 0.2142 0.3735 -0.0141 0.0096  0.0756  14  ASP   A CG  
345  C  CG  B ASP   A 14  ? 0.1643 0.2082 0.2893 -0.0174 0.0006  0.0441  14  ASP   A CG  
346  O  OD1 A ASP   A 14  ? 0.1958 0.2385 0.4029 -0.0029 -0.0038 0.0751  14  ASP   A OD1 
347  O  OD1 B ASP   A 14  ? 0.1702 0.2186 0.3042 -0.0110 -0.0096 0.0480  14  ASP   A OD1 
348  O  OD2 A ASP   A 14  ? 0.1991 0.2397 0.4187 -0.0207 0.0082  0.0586  14  ASP   A OD2 
349  O  OD2 B ASP   A 14  ? 0.1751 0.2304 0.3215 -0.0211 -0.0045 0.0337  14  ASP   A OD2 
358  N  N   . ASN   A 15  ? 0.1314 0.1368 0.1902 -0.0153 0.0041  0.0484  15  ASN   A N   
359  C  CA  . ASN   A 15  ? 0.1309 0.1404 0.2072 -0.0160 -0.0035 0.0363  15  ASN   A CA  
360  C  C   . ASN   A 15  ? 0.1262 0.1404 0.2270 -0.0199 0.0062  0.0395  15  ASN   A C   
361  O  O   . ASN   A 15  ? 0.1355 0.1446 0.2670 -0.0144 -0.0164 0.0407  15  ASN   A O   
362  C  CB  . ASN   A 15  ? 0.1346 0.1454 0.1962 -0.0125 0.0049  0.0384  15  ASN   A CB  
363  C  CG  . ASN   A 15  ? 0.1287 0.1553 0.2036 -0.0092 0.0104  0.0290  15  ASN   A CG  
364  O  OD1 . ASN   A 15  ? 0.1440 0.1603 0.2217 -0.0237 0.0016  0.0281  15  ASN   A OD1 
365  N  ND2 . ASN   A 15  ? 0.1309 0.1631 0.1977 -0.0134 0.0127  0.0277  15  ASN   A ND2 
373  N  N   A VAL   A 16  ? 0.1243 0.1379 0.2126 -0.0181 0.0000  0.0473  16  VAL   A N   
374  N  N   B VAL   A 16  ? 0.1245 0.1411 0.2094 -0.0204 0.0033  0.0431  16  VAL   A N   
375  C  CA  A VAL   A 16  ? 0.1239 0.1373 0.2031 -0.0131 0.0022  0.0476  16  VAL   A CA  
376  C  CA  B VAL   A 16  ? 0.1238 0.1412 0.1953 -0.0198 0.0079  0.0431  16  VAL   A CA  
377  C  C   A VAL   A 16  ? 0.1212 0.1409 0.2029 -0.0154 0.0008  0.0441  16  VAL   A C   
378  C  C   B VAL   A 16  ? 0.1203 0.1413 0.1946 -0.0179 0.0063  0.0419  16  VAL   A C   
379  O  O   A VAL   A 16  ? 0.1163 0.1429 0.2225 -0.0142 0.0147  0.0366  16  VAL   A O   
380  O  O   B VAL   A 16  ? 0.1173 0.1427 0.2037 -0.0169 0.0158  0.0375  16  VAL   A O   
381  C  CB  A VAL   A 16  ? 0.1364 0.1539 0.1963 0.0062  0.0179  0.0440  16  VAL   A CB  
382  C  CB  B VAL   A 16  ? 0.1348 0.1544 0.1866 -0.0106 0.0222  0.0413  16  VAL   A CB  
383  C  CG1 A VAL   A 16  ? 0.1449 0.1619 0.1977 0.0115  0.0232  0.0431  16  VAL   A CG1 
384  C  CG1 B VAL   A 16  ? 0.1413 0.1628 0.1879 -0.0071 0.0254  0.0325  16  VAL   A CG1 
385  C  CG2 A VAL   A 16  ? 0.1445 0.1683 0.2122 0.0137  0.0307  0.0365  16  VAL   A CG2 
386  C  CG2 B VAL   A 16  ? 0.1399 0.1637 0.1976 -0.0078 0.0323  0.0341  16  VAL   A CG2 
405  N  N   . TYR   A 17  ? 0.1168 0.1366 0.1979 -0.0117 0.0154  0.0425  17  TYR   A N   
406  C  CA  . TYR   A 17  ? 0.1209 0.1413 0.1885 -0.0131 0.0184  0.0461  17  TYR   A CA  
407  C  C   . TYR   A 17  ? 0.1253 0.1351 0.2049 -0.0134 0.0133  0.0409  17  TYR   A C   
408  O  O   . TYR   A 17  ? 0.1216 0.1440 0.2223 -0.0134 0.0191  0.0566  17  TYR   A O   
409  C  CB  . TYR   A 17  ? 0.1443 0.1388 0.1877 -0.0176 0.0131  0.0390  17  TYR   A CB  
410  C  CG  . TYR   A 17  ? 0.1683 0.1512 0.1886 -0.0221 -0.0009 0.0371  17  TYR   A CG  
411  C  CD1 . TYR   A 17  ? 0.1837 0.1526 0.2030 -0.0088 -0.0070 0.0340  17  TYR   A CD1 
412  C  CD2 . TYR   A 17  ? 0.1847 0.1618 0.1821 -0.0362 -0.0047 0.0384  17  TYR   A CD2 
413  C  CE1 . TYR   A 17  ? 0.1996 0.1539 0.2139 -0.0171 -0.0167 0.0368  17  TYR   A CE1 
414  C  CE2 . TYR   A 17  ? 0.2047 0.1599 0.1943 -0.0414 -0.0167 0.0284  17  TYR   A CE2 
415  C  CZ  . TYR   A 17  ? 0.2175 0.1561 0.1955 -0.0312 -0.0299 0.0424  17  TYR   A CZ  
416  O  OH  . TYR   A 17  ? 0.2465 0.1566 0.2080 -0.0279 -0.0334 0.0435  17  TYR   A OH  
427  N  N   A ILE   A 18  ? 0.1287 0.1336 0.1934 -0.0144 0.0128  0.0461  18  ILE   A N   
428  N  N   B ILE   A 18  ? 0.1241 0.1354 0.1836 -0.0155 0.0234  0.0374  18  ILE   A N   
429  C  CA  A ILE   A 18  ? 0.1353 0.1282 0.1833 -0.0119 0.0140  0.0339  18  ILE   A CA  
430  C  CA  B ILE   A 18  ? 0.1221 0.1308 0.1678 -0.0088 0.0200  0.0216  18  ILE   A CA  
431  C  C   A ILE   A 18  ? 0.1404 0.1386 0.1818 -0.0168 0.0125  0.0300  18  ILE   A C   
432  C  C   B ILE   A 18  ? 0.1168 0.1401 0.1493 -0.0121 0.0095  0.0190  18  ILE   A C   
433  O  O   A ILE   A 18  ? 0.1336 0.1515 0.1796 -0.0215 0.0163  0.0447  18  ILE   A O   
434  O  O   B ILE   A 18  ? 0.1083 0.1536 0.1575 -0.0223 0.0127  0.0219  18  ILE   A O   
435  C  CB  A ILE   A 18  ? 0.1411 0.1281 0.1673 -0.0005 0.0147  0.0295  18  ILE   A CB  
436  C  CB  B ILE   A 18  ? 0.1307 0.1230 0.1518 0.0007  0.0306  0.0201  18  ILE   A CB  
437  C  CG1 A ILE   A 18  ? 0.1519 0.1301 0.1528 0.0112  0.0085  0.0269  18  ILE   A CG1 
438  C  CG1 B ILE   A 18  ? 0.1504 0.1309 0.1598 -0.0024 0.0421  0.0164  18  ILE   A CG1 
439  C  CG2 A ILE   A 18  ? 0.1381 0.1265 0.1702 0.0080  0.0138  0.0164  18  ILE   A CG2 
440  C  CG2 B ILE   A 18  ? 0.1342 0.1274 0.1495 0.0007  0.0219  0.0199  18  ILE   A CG2 
441  C  CD1 A ILE   A 18  ? 0.1753 0.1423 0.1569 0.0267  0.0132  0.0283  18  ILE   A CD1 
442  C  CD1 B ILE   A 18  ? 0.1686 0.1433 0.1750 0.0046  0.0459  0.0051  18  ILE   A CD1 
465  N  N   A LYS   A 19  ? 0.1427 0.1302 0.1658 -0.0143 0.0185  0.0266  19  LYS   A N   
466  N  N   B LYS   A 19  ? 0.1237 0.1391 0.1338 -0.0044 0.0167  0.0148  19  LYS   A N   
467  C  CA  A LYS   A 19  ? 0.1492 0.1425 0.1719 -0.0122 0.0129  0.0328  19  LYS   A CA  
468  C  CA  B LYS   A 19  ? 0.1410 0.1542 0.1467 0.0043  0.0255  0.0143  19  LYS   A CA  
469  C  C   A LYS   A 19  ? 0.1412 0.1434 0.1923 -0.0088 0.0258  0.0392  19  LYS   A C   
470  C  C   B LYS   A 19  ? 0.1453 0.1510 0.1506 0.0127  0.0365  0.0203  19  LYS   A C   
471  O  O   A LYS   A 19  ? 0.1399 0.1433 0.1825 -0.0041 0.0281  0.0423  19  LYS   A O   
472  O  O   B LYS   A 19  ? 0.1470 0.1511 0.1576 0.0107  0.0249  0.0240  19  LYS   A O   
473  C  CB  A LYS   A 19  ? 0.1605 0.1603 0.1787 -0.0196 0.0045  0.0217  19  LYS   A CB  
474  C  CB  B LYS   A 19  ? 0.1455 0.1752 0.1626 -0.0019 0.0278  0.0002  19  LYS   A CB  
475  C  CG  A LYS   A 19  ? 0.1738 0.1799 0.1903 -0.0229 0.0017  0.0055  19  LYS   A CG  
476  C  CG  B LYS   A 19  ? 0.1687 0.1900 0.1600 -0.0024 0.0259  -0.0025 19  LYS   A CG  
477  C  CD  A LYS   A 19  ? 0.1901 0.2039 0.2020 -0.0260 -0.0053 -0.0027 19  LYS   A CD  
478  C  CD  B LYS   A 19  ? 0.1850 0.2051 0.1662 -0.0109 0.0246  0.0109  19  LYS   A CD  
479  C  CE  A LYS   A 19  ? 0.2062 0.2149 0.2037 -0.0313 -0.0043 0.0041  19  LYS   A CE  
480  C  CE  B LYS   A 19  ? 0.1942 0.2146 0.1780 -0.0190 0.0160  0.0139  19  LYS   A CE  
481  N  NZ  A LYS   A 19  ? 0.2173 0.2285 0.2001 -0.0330 -0.0055 0.0026  19  LYS   A NZ  
482  N  NZ  B LYS   A 19  ? 0.1999 0.2206 0.1823 -0.0242 0.0156  0.0162  19  LYS   A NZ  
509  N  N   A ASN   A 20  ? 0.1428 0.1484 0.2140 -0.0042 0.0346  0.0646  20  ASN   A N   
510  N  N   B ASN   A 20  ? 0.1563 0.1523 0.1701 0.0165  0.0438  0.0248  20  ASN   A N   
511  C  CA  A ASN   A 20  ? 0.1513 0.1644 0.2405 0.0102  0.0497  0.0557  20  ASN   A CA  
512  C  CA  B ASN   A 20  ? 0.1718 0.1614 0.1865 0.0200  0.0410  0.0241  20  ASN   A CA  
513  C  C   A ASN   A 20  ? 0.1673 0.1714 0.2761 0.0007  0.0634  0.0471  20  ASN   A C   
514  C  C   B ASN   A 20  ? 0.1760 0.1593 0.2075 0.0135  0.0468  0.0241  20  ASN   A C   
515  O  O   A ASN   A 20  ? 0.1814 0.1826 0.2833 -0.0121 0.0609  0.0323  20  ASN   A O   
516  O  O   B ASN   A 20  ? 0.1776 0.1569 0.1989 0.0058  0.0376  0.0194  20  ASN   A O   
517  C  CB  A ASN   A 20  ? 0.1527 0.1748 0.2373 0.0231  0.0502  0.0613  20  ASN   A CB  
518  C  CB  B ASN   A 20  ? 0.1859 0.1706 0.1852 0.0306  0.0319  0.0213  20  ASN   A CB  
519  C  CG  A ASN   A 20  ? 0.1618 0.1820 0.2567 0.0373  0.0496  0.0668  20  ASN   A CG  
520  C  CG  B ASN   A 20  ? 0.2005 0.1795 0.1932 0.0339  0.0218  0.0165  20  ASN   A CG  
521  O  OD1 A ASN   A 20  ? 0.1867 0.1918 0.2909 0.0513  0.0617  0.0557  20  ASN   A OD1 
522  O  OD1 B ASN   A 20  ? 0.2143 0.1942 0.2107 0.0371  0.0096  0.0053  20  ASN   A OD1 
523  N  ND2 A ASN   A 20  ? 0.1648 0.1842 0.2509 0.0354  0.0400  0.0831  20  ASN   A ND2 
524  N  ND2 B ASN   A 20  ? 0.2047 0.1778 0.1892 0.0333  0.0137  0.0164  20  ASN   A ND2 
537  N  N   A ALA   A 21  ? 0.1736 0.1752 0.3003 0.0016  0.0628  0.0423  21  ALA   A N   
538  N  N   B ALA   A 21  ? 0.1796 0.1646 0.2460 0.0097  0.0570  0.0228  21  ALA   A N   
539  C  CA  A ALA   A 21  ? 0.1833 0.1776 0.3131 -0.0042 0.0562  0.0515  21  ALA   A CA  
540  C  CA  B ALA   A 21  ? 0.1805 0.1682 0.2603 -0.0021 0.0704  0.0335  21  ALA   A CA  
541  C  C   A ALA   A 21  ? 0.1712 0.1814 0.2967 0.0044  0.0517  0.0710  21  ALA   A C   
542  C  C   B ALA   A 21  ? 0.1723 0.1699 0.2603 0.0029  0.0755  0.0512  21  ALA   A C   
543  O  O   A ALA   A 21  ? 0.1611 0.1822 0.2904 0.0245  0.0400  0.0857  21  ALA   A O   
544  O  O   B ALA   A 21  ? 0.1711 0.1665 0.2851 0.0159  0.0747  0.0500  21  ALA   A O   
545  C  CB  A ALA   A 21  ? 0.2060 0.1846 0.3316 -0.0122 0.0412  0.0415  21  ALA   A CB  
546  C  CB  B ALA   A 21  ? 0.1910 0.1733 0.2681 -0.0205 0.0737  0.0359  21  ALA   A CB  
557  N  N   A ASP   A 22  ? 0.1632 0.1765 0.2840 -0.0065 0.0561  0.0819  22  ASP   A N   
558  N  N   B ASP   A 22  ? 0.1628 0.1668 0.2369 -0.0044 0.0751  0.0702  22  ASP   A N   
559  C  CA  A ASP   A 22  ? 0.1653 0.1911 0.2647 -0.0017 0.0457  0.0627  22  ASP   A CA  
560  C  CA  B ASP   A 22  ? 0.1604 0.1656 0.2183 -0.0037 0.0590  0.0655  22  ASP   A CA  
561  C  C   A ASP   A 22  ? 0.1628 0.1925 0.2156 0.0013  0.0424  0.0448  22  ASP   A C   
562  C  C   B ASP   A 22  ? 0.1487 0.1662 0.1868 -0.0122 0.0532  0.0510  22  ASP   A C   
563  O  O   A ASP   A 22  ? 0.1712 0.2004 0.2233 0.0020  0.0450  0.0368  22  ASP   A O   
564  O  O   B ASP   A 22  ? 0.1482 0.1761 0.1895 -0.0180 0.0562  0.0314  22  ASP   A O   
565  C  CB  A ASP   A 22  ? 0.1783 0.1982 0.3041 -0.0065 0.0361  0.0616  22  ASP   A CB  
566  C  CB  B ASP   A 22  ? 0.1711 0.1645 0.2344 0.0045  0.0568  0.0565  22  ASP   A CB  
567  C  CG  A ASP   A 22  ? 0.1939 0.2102 0.3444 -0.0092 0.0119  0.0712  22  ASP   A CG  
568  C  CG  B ASP   A 22  ? 0.1789 0.1587 0.2338 0.0129  0.0537  0.0486  22  ASP   A CG  
569  O  OD1 A ASP   A 22  ? 0.1909 0.2075 0.3639 -0.0199 0.0045  0.0895  22  ASP   A OD1 
570  O  OD1 B ASP   A 22  ? 0.1738 0.1509 0.2060 0.0053  0.0553  0.0343  22  ASP   A OD1 
571  O  OD2 A ASP   A 22  ? 0.2139 0.2242 0.3673 -0.0052 0.0066  0.0574  22  ASP   A OD2 
572  O  OD2 B ASP   A 22  ? 0.1917 0.1600 0.2623 0.0157  0.0623  0.0468  22  ASP   A OD2 
581  N  N   A ILE   A 23  ? 0.1600 0.1870 0.1884 0.0006  0.0363  0.0291  23  ILE   A N   
582  N  N   B ILE   A 23  ? 0.1418 0.1545 0.1681 -0.0163 0.0417  0.0369  23  ILE   A N   
583  C  CA  A ILE   A 23  ? 0.1562 0.1735 0.1631 -0.0045 0.0262  0.0158  23  ILE   A CA  
584  C  CA  B ILE   A 23  ? 0.1386 0.1502 0.1529 -0.0185 0.0329  0.0226  23  ILE   A CA  
585  C  C   A ILE   A 23  ? 0.1531 0.1744 0.1526 -0.0026 0.0349  0.0169  23  ILE   A C   
586  C  C   B ILE   A 23  ? 0.1490 0.1608 0.1548 -0.0234 0.0315  0.0070  23  ILE   A C   
587  O  O   A ILE   A 23  ? 0.1608 0.1781 0.1601 -0.0056 0.0285  0.0104  23  ILE   A O   
588  O  O   B ILE   A 23  ? 0.1514 0.1581 0.1563 -0.0246 0.0256  0.0010  23  ILE   A O   
589  C  CB  A ILE   A 23  ? 0.1612 0.1642 0.1434 -0.0046 0.0190  0.0077  23  ILE   A CB  
590  C  CB  B ILE   A 23  ? 0.1365 0.1397 0.1389 -0.0134 0.0208  0.0169  23  ILE   A CB  
591  C  CG1 A ILE   A 23  ? 0.1698 0.1666 0.1493 -0.0011 0.0169  0.0039  23  ILE   A CG1 
592  C  CG1 B ILE   A 23  ? 0.1457 0.1394 0.1300 -0.0126 0.0077  0.0093  23  ILE   A CG1 
593  C  CG2 A ILE   A 23  ? 0.1597 0.1645 0.1464 0.0018  0.0160  0.0076  23  ILE   A CG2 
594  C  CG2 B ILE   A 23  ? 0.1331 0.1371 0.1339 -0.0017 0.0238  0.0179  23  ILE   A CG2 
595  C  CD1 A ILE   A 23  ? 0.1691 0.1658 0.1567 0.0007  0.0109  -0.0002 23  ILE   A CD1 
596  C  CD1 B ILE   A 23  ? 0.1470 0.1420 0.1300 -0.0060 -0.0061 0.0047  23  ILE   A CD1 
619  N  N   A VAL   A 24  ? 0.1588 0.1777 0.1661 -0.0062 0.0326  0.0146  24  VAL   A N   
620  N  N   B VAL   A 24  ? 0.1632 0.1683 0.1499 -0.0328 0.0243  0.0040  24  VAL   A N   
621  C  CA  A VAL   A 24  ? 0.1811 0.1880 0.1846 -0.0136 0.0306  -0.0031 24  VAL   A CA  
622  C  CA  B VAL   A 24  ? 0.1843 0.1759 0.1539 -0.0365 0.0193  -0.0035 24  VAL   A CA  
623  C  C   A VAL   A 24  ? 0.1843 0.1990 0.1899 -0.0237 0.0247  -0.0056 24  VAL   A C   
624  C  C   B VAL   A 24  ? 0.1892 0.1911 0.1679 -0.0377 0.0193  -0.0149 24  VAL   A C   
625  O  O   A VAL   A 24  ? 0.1894 0.1996 0.1885 -0.0192 0.0278  -0.0063 24  VAL   A O   
626  O  O   B VAL   A 24  ? 0.1964 0.1900 0.1749 -0.0413 0.0140  -0.0199 24  VAL   A O   
627  C  CB  A VAL   A 24  ? 0.1889 0.1899 0.1976 -0.0127 0.0465  -0.0035 24  VAL   A CB  
628  C  CB  B VAL   A 24  ? 0.1948 0.1745 0.1553 -0.0360 0.0189  -0.0018 24  VAL   A CB  
629  C  CG1 A VAL   A 24  ? 0.1946 0.1975 0.1989 -0.0111 0.0538  -0.0156 24  VAL   A CG1 
630  C  CG1 B VAL   A 24  ? 0.2043 0.1819 0.1749 -0.0277 0.0133  -0.0036 24  VAL   A CG1 
631  C  CG2 A VAL   A 24  ? 0.2014 0.1934 0.2183 -0.0099 0.0534  0.0069  24  VAL   A CG2 
632  C  CG2 B VAL   A 24  ? 0.1997 0.1711 0.1376 -0.0459 0.0194  -0.0063 24  VAL   A CG2 
651  N  N   A GLU   A 25  ? 0.1904 0.2234 0.1865 -0.0307 0.0395  -0.0094 25  GLU   A N   
652  N  N   B GLU   A 25  ? 0.1903 0.2108 0.1802 -0.0342 0.0318  -0.0179 25  GLU   A N   
653  C  CA  A GLU   A 25  ? 0.2088 0.2517 0.1975 -0.0240 0.0551  -0.0120 25  GLU   A CA  
654  C  CA  B GLU   A 25  ? 0.2011 0.2315 0.1969 -0.0347 0.0381  -0.0109 25  GLU   A CA  
655  C  C   A GLU   A 25  ? 0.1997 0.2604 0.1744 -0.0323 0.0685  -0.0092 25  GLU   A C   
656  C  C   B GLU   A 25  ? 0.2012 0.2371 0.1959 -0.0350 0.0463  -0.0080 25  GLU   A C   
657  O  O   A GLU   A 25  ? 0.2068 0.2721 0.1774 -0.0362 0.0645  -0.0134 25  GLU   A O   
658  O  O   B GLU   A 25  ? 0.2074 0.2400 0.2011 -0.0389 0.0414  -0.0110 25  GLU   A O   
659  C  CB  A GLU   A 25  ? 0.2347 0.2778 0.2460 -0.0184 0.0513  -0.0140 25  GLU   A CB  
660  C  CB  B GLU   A 25  ? 0.2139 0.2444 0.2365 -0.0341 0.0396  -0.0130 25  GLU   A CB  
661  C  CG  A GLU   A 25  ? 0.2597 0.3009 0.3042 -0.0199 0.0286  -0.0208 25  GLU   A CG  
662  C  CG  B GLU   A 25  ? 0.2348 0.2595 0.2884 -0.0327 0.0344  -0.0204 25  GLU   A CG  
663  C  CD  A GLU   A 25  ? 0.2763 0.3204 0.3524 -0.0185 0.0099  -0.0238 25  GLU   A CD  
664  C  CD  B GLU   A 25  ? 0.2505 0.2741 0.3410 -0.0308 0.0246  -0.0216 25  GLU   A CD  
665  O  OE1 A GLU   A 25  ? 0.2838 0.3306 0.3584 -0.0148 -0.0037 -0.0312 25  GLU   A OE1 
666  O  OE1 B GLU   A 25  ? 0.2595 0.2817 0.3681 -0.0301 0.0183  -0.0217 25  GLU   A OE1 
667  O  OE2 A GLU   A 25  ? 0.2821 0.3266 0.3838 -0.0179 0.0061  -0.0244 25  GLU   A OE2 
668  O  OE2 B GLU   A 25  ? 0.2546 0.2808 0.3618 -0.0286 0.0213  -0.0192 25  GLU   A OE2 
681  N  N   A GLU   A 26  ? 0.1899 0.2570 0.1800 -0.0426 0.0756  -0.0055 26  GLU   A N   
682  N  N   B GLU   A 26  ? 0.1967 0.2349 0.1972 -0.0333 0.0583  -0.0038 26  GLU   A N   
683  C  CA  A GLU   A 26  ? 0.2028 0.2614 0.1580 -0.0553 0.0773  0.0039  26  GLU   A CA  
684  C  CA  B GLU   A 26  ? 0.2053 0.2328 0.2071 -0.0290 0.0627  0.0063  26  GLU   A CA  
685  C  C   A GLU   A 26  ? 0.2036 0.2510 0.1516 -0.0603 0.0616  0.0050  26  GLU   A C   
686  C  C   B GLU   A 26  ? 0.1992 0.2230 0.1880 -0.0222 0.0533  0.0217  26  GLU   A C   
687  O  O   A GLU   A 26  ? 0.2105 0.2559 0.1524 -0.0637 0.0520  0.0039  26  GLU   A O   
688  O  O   B GLU   A 26  ? 0.2062 0.2270 0.1841 -0.0283 0.0521  0.0216  26  GLU   A O   
689  C  CB  A GLU   A 26  ? 0.2233 0.2731 0.1861 -0.0589 0.0781  0.0122  26  GLU   A CB  
690  C  CB  B GLU   A 26  ? 0.2229 0.2356 0.2384 -0.0414 0.0628  0.0004  26  GLU   A CB  
691  C  CG  A GLU   A 26  ? 0.2524 0.2932 0.2598 -0.0589 0.0715  0.0052  26  GLU   A CG  
692  C  CG  B GLU   A 26  ? 0.2344 0.2350 0.2499 -0.0603 0.0862  -0.0129 26  GLU   A CG  
693  C  CD  A GLU   A 26  ? 0.2736 0.3085 0.3096 -0.0631 0.0743  0.0062  26  GLU   A CD  
694  C  CD  B GLU   A 26  ? 0.2431 0.2300 0.2525 -0.0814 0.1066  -0.0323 26  GLU   A CD  
695  O  OE1 A GLU   A 26  ? 0.2714 0.3256 0.3148 -0.0533 0.0902  -0.0132 26  GLU   A OE1 
696  O  OE1 B GLU   A 26  ? 0.2408 0.2350 0.2663 -0.0869 0.1191  -0.0535 26  GLU   A OE1 
697  O  OE2 A GLU   A 26  ? 0.3023 0.3119 0.3300 -0.0639 0.0644  0.0136  26  GLU   A OE2 
698  O  OE2 B GLU   A 26  ? 0.2563 0.2276 0.2237 -0.0857 0.1189  -0.0306 26  GLU   A OE2 
711  N  N   A ALA   A 27  ? 0.1930 0.2339 0.1510 -0.0662 0.0607  0.0050  27  ALA   A N   
712  N  N   B ALA   A 27  ? 0.1859 0.2102 0.1653 -0.0064 0.0471  0.0349  27  ALA   A N   
713  C  CA  A ALA   A 27  ? 0.2023 0.2374 0.1469 -0.0640 0.0526  0.0026  27  ALA   A CA  
714  C  CA  B ALA   A 27  ? 0.1901 0.2138 0.1505 0.0087  0.0318  0.0395  27  ALA   A CA  
715  C  C   A ALA   A 27  ? 0.2311 0.2503 0.1623 -0.0736 0.0605  -0.0121 27  ALA   A C   
716  C  C   B ALA   A 27  ? 0.2124 0.2286 0.1558 0.0178  0.0315  0.0297  27  ALA   A C   
717  O  O   A ALA   A 27  ? 0.2353 0.2487 0.1647 -0.0841 0.0453  -0.0172 27  ALA   A O   
718  O  O   B ALA   A 27  ? 0.2069 0.2257 0.1623 0.0212  0.0264  0.0300  27  ALA   A O   
719  C  CB  A ALA   A 27  ? 0.1878 0.2298 0.1425 -0.0636 0.0336  0.0091  27  ALA   A CB  
720  C  CB  B ALA   A 27  ? 0.1793 0.2091 0.1385 0.0034  0.0202  0.0437  27  ALA   A CB  
731  N  N   A LYS   A 28  ? 0.2677 0.2765 0.1850 -0.0604 0.0623  -0.0344 28  LYS   A N   
732  N  N   B LYS   A 28  ? 0.2451 0.2494 0.1714 0.0268  0.0337  0.0123  28  LYS   A N   
733  C  CA  A LYS   A 28  ? 0.3069 0.3061 0.2202 -0.0501 0.0661  -0.0431 28  LYS   A CA  
734  C  CA  B LYS   A 28  ? 0.2790 0.2777 0.2027 0.0355  0.0285  -0.0041 28  LYS   A CA  
735  C  C   A LYS   A 28  ? 0.3259 0.3301 0.2092 -0.0538 0.0896  -0.0348 28  LYS   A C   
736  C  C   B LYS   A 28  ? 0.3053 0.3001 0.2017 0.0296  0.0383  0.0022  28  LYS   A C   
737  O  O   A LYS   A 28  ? 0.3303 0.3361 0.2429 -0.0541 0.0723  -0.0334 28  LYS   A O   
738  O  O   B LYS   A 28  ? 0.3114 0.3047 0.2123 0.0297  0.0284  0.0044  28  LYS   A O   
739  C  CB  A LYS   A 28  ? 0.3251 0.3146 0.2642 -0.0364 0.0524  -0.0486 28  LYS   A CB  
740  C  CB  B LYS   A 28  ? 0.2894 0.2867 0.2396 0.0465  0.0144  -0.0205 28  LYS   A CB  
741  C  CG  A LYS   A 28  ? 0.3416 0.3227 0.3096 -0.0257 0.0399  -0.0497 28  LYS   A CG  
742  C  CG  B LYS   A 28  ? 0.3024 0.2984 0.2842 0.0515  0.0025  -0.0274 28  LYS   A CG  
743  C  CD  A LYS   A 28  ? 0.3558 0.3343 0.3617 -0.0175 0.0252  -0.0421 28  LYS   A CD  
744  C  CD  B LYS   A 28  ? 0.3163 0.3118 0.3299 0.0544  -0.0085 -0.0291 28  LYS   A CD  
745  C  CE  A LYS   A 28  ? 0.3674 0.3435 0.3989 -0.0116 0.0179  -0.0397 28  LYS   A CE  
746  C  CE  B LYS   A 28  ? 0.3277 0.3217 0.3628 0.0554  -0.0148 -0.0342 28  LYS   A CE  
747  N  NZ  A LYS   A 28  ? 0.3754 0.3481 0.4197 -0.0068 0.0202  -0.0468 28  LYS   A NZ  
748  N  NZ  B LYS   A 28  ? 0.3334 0.3264 0.3779 0.0563  -0.0175 -0.0391 28  LYS   A NZ  
775  N  N   A LYS   A 29  ? 0.3387 0.3478 0.2008 -0.0584 0.1234  -0.0199 29  LYS   A N   
776  N  N   B LYS   A 29  ? 0.3230 0.3186 0.2115 0.0207  0.0584  0.0108  29  LYS   A N   
777  C  CA  A LYS   A 29  ? 0.3584 0.3688 0.2141 -0.0594 0.1407  -0.0059 29  LYS   A CA  
778  C  CA  B LYS   A 29  ? 0.3440 0.3400 0.2418 0.0109  0.0682  0.0166  29  LYS   A CA  
779  C  C   A LYS   A 29  ? 0.3569 0.3605 0.1874 -0.0679 0.1264  0.0024  29  LYS   A C   
780  C  C   B LYS   A 29  ? 0.3476 0.3369 0.2258 -0.0017 0.0593  0.0248  29  LYS   A C   
781  O  O   A LYS   A 29  ? 0.3708 0.3746 0.2014 -0.0623 0.1169  -0.0026 29  LYS   A O   
782  O  O   B LYS   A 29  ? 0.3531 0.3462 0.2299 0.0008  0.0565  0.0252  29  LYS   A O   
783  C  CB  A LYS   A 29  ? 0.3769 0.3969 0.2763 -0.0499 0.1565  -0.0020 29  LYS   A CB  
784  C  CB  B LYS   A 29  ? 0.3594 0.3632 0.2979 0.0145  0.0828  0.0147  29  LYS   A CB  
785  C  CG  A LYS   A 29  ? 0.3960 0.4215 0.3482 -0.0407 0.1556  0.0023  29  LYS   A CG  
786  C  CG  B LYS   A 29  ? 0.3746 0.3832 0.3563 0.0182  0.0887  0.0140  29  LYS   A CG  
787  C  CD  A LYS   A 29  ? 0.4131 0.4411 0.4202 -0.0335 0.1507  0.0022  29  LYS   A CD  
788  C  CD  B LYS   A 29  ? 0.3874 0.3988 0.4126 0.0213  0.0917  0.0122  29  LYS   A CD  
789  C  CE  A LYS   A 29  ? 0.4248 0.4541 0.4679 -0.0281 0.1507  -0.0007 29  LYS   A CE  
790  C  CE  B LYS   A 29  ? 0.3967 0.4096 0.4518 0.0233  0.0953  0.0080  29  LYS   A CE  
791  N  NZ  A LYS   A 29  ? 0.4298 0.4607 0.4998 -0.0244 0.1497  -0.0039 29  LYS   A NZ  
792  N  NZ  B LYS   A 29  ? 0.4012 0.4146 0.4774 0.0248  0.0954  0.0065  29  LYS   A NZ  
819  N  N   A VAL   A 30  ? 0.3416 0.3374 0.1750 -0.0808 0.1099  0.0103  30  VAL   A N   
820  N  N   B VAL   A 30  ? 0.3450 0.3239 0.2132 -0.0154 0.0508  0.0289  30  VAL   A N   
821  C  CA  A VAL   A 30  ? 0.3315 0.3166 0.1683 -0.0979 0.0806  0.0255  30  VAL   A CA  
822  C  CA  B VAL   A 30  ? 0.3428 0.3094 0.2067 -0.0299 0.0317  0.0400  30  VAL   A CA  
823  C  C   A VAL   A 30  ? 0.3267 0.3003 0.1392 -0.0946 0.0591  0.0322  30  VAL   A C   
824  C  C   B VAL   A 30  ? 0.3439 0.3037 0.1855 -0.0381 0.0208  0.0353  30  VAL   A C   
825  O  O   A VAL   A 30  ? 0.3348 0.3042 0.1343 -0.0930 0.0517  0.0307  30  VAL   A O   
826  O  O   B VAL   A 30  ? 0.3480 0.3055 0.1801 -0.0380 0.0151  0.0367  30  VAL   A O   
827  C  CB  A VAL   A 30  ? 0.3290 0.3112 0.2073 -0.1152 0.0625  0.0299  30  VAL   A CB  
828  C  CB  B VAL   A 30  ? 0.3401 0.3001 0.2278 -0.0349 0.0230  0.0500  30  VAL   A CB  
829  C  CG1 A VAL   A 30  ? 0.3305 0.3084 0.2270 -0.1194 0.0496  0.0304  30  VAL   A CG1 
830  C  CG1 B VAL   A 30  ? 0.3405 0.2980 0.2402 -0.0353 0.0163  0.0497  30  VAL   A CG1 
831  C  CG2 A VAL   A 30  ? 0.3270 0.3133 0.2304 -0.1239 0.0617  0.0302  30  VAL   A CG2 
832  C  CG2 B VAL   A 30  ? 0.3392 0.2978 0.2385 -0.0378 0.0222  0.0562  30  VAL   A CG2 
851  N  N   A LYS   A 31  ? 0.3197 0.2854 0.1196 -0.0922 0.0405  0.0266  31  LYS   A N   
852  N  N   B LYS   A 31  ? 0.3405 0.2958 0.1753 -0.0447 0.0101  0.0289  31  LYS   A N   
853  C  CA  A LYS   A 31  ? 0.3305 0.2863 0.1377 -0.0795 0.0157  0.0243  31  LYS   A CA  
854  C  CA  B LYS   A 31  ? 0.3408 0.2926 0.1882 -0.0470 -0.0036 0.0262  31  LYS   A CA  
855  C  C   A LYS   A 31  ? 0.3093 0.2713 0.1121 -0.0703 0.0108  0.0528  31  LYS   A C   
856  C  C   B LYS   A 31  ? 0.3148 0.2726 0.1388 -0.0514 -0.0041 0.0495  31  LYS   A C   
857  O  O   A LYS   A 31  ? 0.3122 0.2824 0.1338 -0.0706 -0.0001 0.0543  31  LYS   A O   
858  O  O   B LYS   A 31  ? 0.3207 0.2782 0.1440 -0.0487 -0.0176 0.0611  31  LYS   A O   
859  C  CB  A LYS   A 31  ? 0.3703 0.3118 0.2460 -0.0710 -0.0082 0.0000  31  LYS   A CB  
860  C  CB  B LYS   A 31  ? 0.3668 0.3115 0.2726 -0.0421 -0.0171 0.0066  31  LYS   A CB  
861  C  CG  A LYS   A 31  ? 0.4077 0.3364 0.3707 -0.0552 -0.0318 -0.0143 31  LYS   A CG  
862  C  CG  B LYS   A 31  ? 0.3919 0.3306 0.3654 -0.0348 -0.0306 -0.0066 31  LYS   A CG  
863  C  CD  A LYS   A 31  ? 0.4359 0.3560 0.4619 -0.0418 -0.0500 -0.0241 31  LYS   A CD  
864  C  CD  B LYS   A 31  ? 0.4106 0.3462 0.4374 -0.0288 -0.0419 -0.0166 31  LYS   A CD  
865  C  CE  A LYS   A 31  ? 0.4538 0.3697 0.5203 -0.0321 -0.0628 -0.0312 31  LYS   A CE  
866  C  CE  B LYS   A 31  ? 0.4221 0.3574 0.4852 -0.0243 -0.0502 -0.0231 31  LYS   A CE  
867  N  NZ  A LYS   A 31  ? 0.4624 0.3764 0.5517 -0.0262 -0.0704 -0.0354 31  LYS   A NZ  
868  N  NZ  B LYS   A 31  ? 0.4277 0.3632 0.5117 -0.0214 -0.0554 -0.0275 31  LYS   A NZ  
895  N  N   . PRO   A 32  ? 0.2818 0.2502 0.1079 -0.0592 0.0080  0.0405  32  PRO   A N   
896  C  CA  . PRO   A 32  ? 0.2593 0.2301 0.1250 -0.0520 -0.0003 0.0515  32  PRO   A CA  
897  C  C   . PRO   A 32  ? 0.2476 0.2284 0.1323 -0.0393 -0.0180 0.0496  32  PRO   A C   
898  O  O   . PRO   A 32  ? 0.2387 0.2251 0.1495 -0.0444 -0.0338 0.0525  32  PRO   A O   
899  C  CB  . PRO   A 32  ? 0.2450 0.2306 0.1444 -0.0520 0.0001  0.0336  32  PRO   A CB  
900  C  CG  . PRO   A 32  ? 0.2438 0.2360 0.1035 -0.0456 -0.0076 0.0258  32  PRO   A CG  
901  C  CD  . PRO   A 32  ? 0.2555 0.2390 0.0975 -0.0519 0.0043  0.0306  32  PRO   A CD  
909  N  N   A THR   A 33  ? 0.2501 0.2274 0.1245 -0.0334 -0.0187 0.0508  33  THR   A N   
910  N  N   B THR   A 33  ? 0.2458 0.2256 0.1284 -0.0332 -0.0188 0.0494  33  THR   A N   
911  C  CA  A THR   A 33  ? 0.2485 0.2251 0.1367 -0.0276 -0.0316 0.0528  33  THR   A CA  
912  C  CA  B THR   A 33  ? 0.2418 0.2226 0.1386 -0.0273 -0.0270 0.0484  33  THR   A CA  
913  C  C   A THR   A 33  ? 0.2219 0.2087 0.1278 -0.0312 -0.0290 0.0426  33  THR   A C   
914  C  C   B THR   A 33  ? 0.2197 0.2083 0.1250 -0.0300 -0.0261 0.0406  33  THR   A C   
915  O  O   A THR   A 33  ? 0.2169 0.2082 0.1442 -0.0349 -0.0479 0.0449  33  THR   A O   
916  O  O   B THR   A 33  ? 0.2163 0.2086 0.1360 -0.0312 -0.0395 0.0414  33  THR   A O   
917  C  CB  A THR   A 33  ? 0.2731 0.2426 0.1565 -0.0222 -0.0316 0.0704  33  THR   A CB  
918  C  CB  B THR   A 33  ? 0.2598 0.2362 0.1602 -0.0212 -0.0267 0.0588  33  THR   A CB  
919  O  OG1 A THR   A 33  ? 0.2945 0.2548 0.1838 -0.0121 -0.0214 0.0828  33  THR   A OG1 
920  O  OG1 B THR   A 33  ? 0.2753 0.2457 0.1805 -0.0114 -0.0224 0.0656  33  THR   A OG1 
921  C  CG2 A THR   A 33  ? 0.2781 0.2516 0.1634 -0.0202 -0.0383 0.0680  33  THR   A CG2 
922  C  CG2 B THR   A 33  ? 0.2632 0.2427 0.1682 -0.0201 -0.0289 0.0582  33  THR   A CG2 
937  N  N   . VAL   A 34  ? 0.2007 0.1935 0.1149 -0.0334 -0.0231 0.0394  34  VAL   A N   
938  C  CA  . VAL   A 34  ? 0.1742 0.1699 0.1104 -0.0272 -0.0155 0.0309  34  VAL   A CA  
939  C  C   . VAL   A 34  ? 0.1595 0.1594 0.1027 -0.0212 -0.0042 0.0254  34  VAL   A C   
940  O  O   . VAL   A 34  ? 0.1612 0.1666 0.1286 -0.0293 -0.0067 0.0383  34  VAL   A O   
941  C  CB  . VAL   A 34  ? 0.1722 0.1677 0.1334 -0.0218 -0.0099 0.0242  34  VAL   A CB  
942  C  CG1 . VAL   A 34  ? 0.1791 0.1706 0.1283 -0.0224 -0.0001 0.0085  34  VAL   A CG1 
943  C  CG2 . VAL   A 34  ? 0.1812 0.1810 0.1676 -0.0099 -0.0196 0.0209  34  VAL   A CG2 
954  N  N   . VAL   A 35  ? 0.1442 0.1463 0.1151 -0.0235 -0.0097 0.0269  35  VAL   A N   
955  C  CA  . VAL   A 35  ? 0.1368 0.1449 0.1033 -0.0209 -0.0039 0.0197  35  VAL   A CA  
956  C  C   . VAL   A 35  ? 0.1324 0.1345 0.1056 -0.0145 0.0033  0.0181  35  VAL   A C   
957  O  O   . VAL   A 35  ? 0.1226 0.1455 0.1283 -0.0205 0.0089  0.0150  35  VAL   A O   
958  C  CB  . VAL   A 35  ? 0.1413 0.1535 0.1173 -0.0112 0.0096  0.0111  35  VAL   A CB  
959  C  CG1 . VAL   A 35  ? 0.1489 0.1569 0.1333 -0.0001 0.0087  0.0069  35  VAL   A CG1 
960  C  CG2 . VAL   A 35  ? 0.1362 0.1568 0.1464 -0.0098 0.0080  0.0032  35  VAL   A CG2 
970  N  N   . VAL   A 36  ? 0.1195 0.1335 0.1056 -0.0125 0.0044  0.0241  36  VAL   A N   
971  C  CA  . VAL   A 36  ? 0.1172 0.1233 0.1031 -0.0056 0.0051  0.0135  36  VAL   A CA  
972  C  C   . VAL   A 36  ? 0.1101 0.1324 0.1113 -0.0136 0.0044  0.0157  36  VAL   A C   
973  O  O   . VAL   A 36  ? 0.1188 0.1297 0.1327 -0.0042 0.0155  0.0208  36  VAL   A O   
974  C  CB  . VAL   A 36  ? 0.1140 0.1181 0.1150 -0.0046 0.0034  0.0119  36  VAL   A CB  
975  C  CG1 . VAL   A 36  ? 0.1225 0.1196 0.1353 -0.0124 0.0063  0.0029  36  VAL   A CG1 
976  C  CG2 . VAL   A 36  ? 0.1251 0.1230 0.1330 -0.0042 0.0000  0.0192  36  VAL   A CG2 
986  N  N   . ASN   A 37  ? 0.1096 0.1175 0.1153 -0.0042 0.0027  0.0154  37  ASN   A N   
987  C  CA  . ASN   A 37  ? 0.1101 0.1148 0.1047 -0.0029 0.0081  0.0175  37  ASN   A CA  
988  C  C   . ASN   A 37  ? 0.1058 0.1101 0.1093 -0.0050 0.0084  0.0209  37  ASN   A C   
989  O  O   . ASN   A 37  ? 0.1216 0.1211 0.1178 0.0054  0.0116  0.0099  37  ASN   A O   
990  C  CB  . ASN   A 37  ? 0.1134 0.1162 0.1144 0.0012  0.0044  0.0121  37  ASN   A CB  
991  C  CG  . ASN   A 37  ? 0.1108 0.1167 0.1247 0.0013  0.0054  0.0093  37  ASN   A CG  
992  O  OD1 . ASN   A 37  ? 0.1153 0.1169 0.1480 0.0013  0.0050  0.0195  37  ASN   A OD1 
993  N  ND2 . ASN   A 37  ? 0.1181 0.1159 0.1315 -0.0043 -0.0016 0.0238  37  ASN   A ND2 
1000 N  N   A ALA   A 38  ? 0.1063 0.1219 0.1128 -0.0001 0.0117  0.0100  38  ALA   A N   
1001 N  N   B ALA   A 38  ? 0.1091 0.1215 0.1148 -0.0016 0.0062  0.0159  38  ALA   A N   
1002 C  CA  A ALA   A 38  ? 0.1187 0.1274 0.1076 -0.0014 0.0059  0.0062  38  ALA   A CA  
1003 C  CA  B ALA   A 38  ? 0.1170 0.1288 0.1202 -0.0021 0.0018  0.0151  38  ALA   A CA  
1004 C  C   A ALA   A 38  ? 0.1187 0.1279 0.1072 0.0007  -0.0065 0.0056  38  ALA   A C   
1005 C  C   B ALA   A 38  ? 0.1140 0.1279 0.1142 -0.0003 -0.0093 0.0110  38  ALA   A C   
1006 O  O   A ALA   A 38  ? 0.1259 0.1163 0.1068 0.0031  -0.0111 -0.0033 38  ALA   A O   
1007 O  O   B ALA   A 38  ? 0.1123 0.1254 0.1185 0.0029  -0.0166 0.0180  38  ALA   A O   
1008 C  CB  A ALA   A 38  ? 0.1212 0.1458 0.1275 -0.0080 -0.0064 0.0037  38  ALA   A CB  
1009 C  CB  B ALA   A 38  ? 0.1216 0.1432 0.1446 -0.0044 -0.0062 0.0103  38  ALA   A CB  
1020 N  N   . ALA   A 39  ? 0.1138 0.1242 0.1205 -0.0008 0.0044  0.0148  39  ALA   A N   
1021 C  CA  . ALA   A 39  ? 0.1223 0.1249 0.1195 -0.0010 0.0040  0.0094  39  ALA   A CA  
1022 C  C   . ALA   A 39  ? 0.1240 0.1204 0.1241 -0.0006 0.0034  0.0109  39  ALA   A C   
1023 O  O   . ALA   A 39  ? 0.1353 0.1204 0.1222 -0.0064 0.0043  0.0084  39  ALA   A O   
1024 C  CB  . ALA   A 39  ? 0.1269 0.1446 0.1357 -0.0066 -0.0039 0.0018  39  ALA   A CB  
1031 N  N   A ASN   A 40  ? 0.1272 0.1242 0.1283 -0.0048 0.0154  0.0041  40  ASN   A N   
1032 N  N   B ASN   A 40  ? 0.1298 0.1184 0.1174 -0.0047 0.0174  0.0112  40  ASN   A N   
1033 C  CA  A ASN   A 40  ? 0.1265 0.1214 0.1218 0.0026  0.0088  0.0020  40  ASN   A CA  
1034 C  CA  B ASN   A 40  ? 0.1306 0.1161 0.1237 -0.0043 0.0109  0.0136  40  ASN   A CA  
1035 C  C   A ASN   A 40  ? 0.1289 0.1096 0.1007 0.0024  0.0103  0.0078  40  ASN   A C   
1036 C  C   B ASN   A 40  ? 0.1316 0.1118 0.1129 -0.0095 0.0137  0.0211  40  ASN   A C   
1037 O  O   A ASN   A 40  ? 0.1307 0.1148 0.1007 -0.0033 0.0160  0.0130  40  ASN   A O   
1038 O  O   B ASN   A 40  ? 0.1288 0.1136 0.1196 -0.0124 0.0101  0.0238  40  ASN   A O   
1039 C  CB  A ASN   A 40  ? 0.1321 0.1281 0.1236 0.0082  -0.0042 0.0014  40  ASN   A CB  
1040 C  CB  B ASN   A 40  ? 0.1388 0.1198 0.1410 -0.0021 0.0027  0.0177  40  ASN   A CB  
1041 C  CG  A ASN   A 40  ? 0.1465 0.1286 0.1495 0.0089  -0.0081 0.0077  40  ASN   A CG  
1042 C  CG  B ASN   A 40  ? 0.1429 0.1233 0.1599 -0.0011 0.0038  0.0156  40  ASN   A CG  
1043 O  OD1 A ASN   A 40  ? 0.1592 0.1249 0.1637 0.0088  -0.0142 0.0082  40  ASN   A OD1 
1044 O  OD1 B ASN   A 40  ? 0.1507 0.1299 0.1704 -0.0065 0.0066  0.0157  40  ASN   A OD1 
1045 N  ND2 A ASN   A 40  ? 0.1554 0.1450 0.1626 0.0098  0.0035  -0.0072 40  ASN   A ND2 
1046 N  ND2 B ASN   A 40  ? 0.1385 0.1327 0.1734 -0.0051 0.0195  -0.0004 40  ASN   A ND2 
1059 N  N   A VAL   A 41  ? 0.1274 0.1168 0.0902 0.0021  0.0011  0.0090  41  VAL   A N   
1060 N  N   B VAL   A 41  ? 0.1368 0.1210 0.1170 -0.0071 0.0117  0.0291  41  VAL   A N   
1061 C  CA  A VAL   A 41  ? 0.1303 0.1167 0.1114 0.0031  0.0097  0.0132  41  VAL   A CA  
1062 C  CA  B VAL   A 41  ? 0.1394 0.1315 0.1115 -0.0032 0.0127  0.0302  41  VAL   A CA  
1063 C  C   A VAL   A 41  ? 0.1232 0.1119 0.1225 0.0022  0.0118  0.0117  41  VAL   A C   
1064 C  C   B VAL   A 41  ? 0.1380 0.1335 0.1091 -0.0008 0.0185  0.0218  41  VAL   A C   
1065 O  O   A VAL   A 41  ? 0.1320 0.1055 0.1290 0.0044  -0.0088 0.0076  41  VAL   A O   
1066 O  O   B VAL   A 41  ? 0.1462 0.1354 0.0929 -0.0020 0.0078  0.0137  41  VAL   A O   
1067 C  CB  A VAL   A 41  ? 0.1344 0.1200 0.1140 0.0050  0.0180  0.0093  41  VAL   A CB  
1068 C  CB  B VAL   A 41  ? 0.1497 0.1421 0.1252 -0.0043 0.0177  0.0275  41  VAL   A CB  
1069 C  CG1 A VAL   A 41  ? 0.1438 0.1304 0.1223 0.0097  0.0103  0.0050  41  VAL   A CG1 
1070 C  CG1 B VAL   A 41  ? 0.1670 0.1492 0.1320 -0.0079 0.0243  0.0196  41  VAL   A CG1 
1071 C  CG2 A VAL   A 41  ? 0.1344 0.1260 0.1087 0.0017  0.0266  0.0073  41  VAL   A CG2 
1072 C  CG2 B VAL   A 41  ? 0.1531 0.1469 0.1274 -0.0037 0.0085  0.0278  41  VAL   A CG2 
1091 N  N   A TYR   A 42  ? 0.1126 0.1076 0.1625 -0.0034 0.0224  0.0176  42  TYR   A N   
1092 N  N   B TYR   A 42  ? 0.1299 0.1301 0.1290 0.0034  0.0297  0.0202  42  TYR   A N   
1093 C  CA  A TYR   A 42  ? 0.1200 0.1044 0.1619 -0.0033 0.0215  0.0228  42  TYR   A CA  
1094 C  CA  B TYR   A 42  ? 0.1287 0.1280 0.1288 0.0019  0.0339  0.0223  42  TYR   A CA  
1095 C  C   A TYR   A 42  ? 0.1190 0.1094 0.1565 -0.0030 0.0170  0.0194  42  TYR   A C   
1096 C  C   B TYR   A 42  ? 0.1284 0.1233 0.1340 -0.0051 0.0293  0.0283  42  TYR   A C   
1097 O  O   A TYR   A 42  ? 0.1188 0.1164 0.1700 -0.0075 0.0108  0.0033  42  TYR   A O   
1098 O  O   B TYR   A 42  ? 0.1259 0.1275 0.1529 -0.0104 0.0287  0.0269  42  TYR   A O   
1099 C  CB  A TYR   A 42  ? 0.1373 0.1206 0.1599 -0.0034 0.0245  0.0294  42  TYR   A CB  
1100 C  CB  B TYR   A 42  ? 0.1396 0.1360 0.1280 0.0043  0.0321  0.0279  42  TYR   A CB  
1101 C  CG  A TYR   A 42  ? 0.1518 0.1369 0.1496 -0.0056 0.0173  0.0381  42  TYR   A CG  
1102 C  CG  B TYR   A 42  ? 0.1562 0.1453 0.1355 0.0131  0.0176  0.0304  42  TYR   A CG  
1103 C  CD1 A TYR   A 42  ? 0.1656 0.1527 0.1538 -0.0155 0.0238  0.0285  42  TYR   A CD1 
1104 C  CD1 B TYR   A 42  ? 0.1610 0.1504 0.1354 0.0112  0.0154  0.0302  42  TYR   A CD1 
1105 C  CD2 A TYR   A 42  ? 0.1615 0.1554 0.1595 -0.0038 0.0157  0.0270  42  TYR   A CD2 
1106 C  CD2 B TYR   A 42  ? 0.1721 0.1600 0.1586 0.0169  0.0144  0.0205  42  TYR   A CD2 
1107 C  CE1 A TYR   A 42  ? 0.1835 0.1642 0.1482 -0.0199 0.0196  0.0232  42  TYR   A CE1 
1108 C  CE1 B TYR   A 42  ? 0.1703 0.1592 0.1375 0.0073  0.0098  0.0270  42  TYR   A CE1 
1109 C  CE2 A TYR   A 42  ? 0.1799 0.1711 0.1700 -0.0140 0.0134  0.0268  42  TYR   A CE2 
1110 C  CE2 B TYR   A 42  ? 0.1854 0.1721 0.1657 0.0114  0.0096  0.0218  42  TYR   A CE2 
1111 C  CZ  A TYR   A 42  ? 0.1924 0.1732 0.1429 -0.0196 0.0201  0.0284  42  TYR   A CZ  
1112 C  CZ  B TYR   A 42  ? 0.1875 0.1718 0.1474 0.0051  0.0101  0.0204  42  TYR   A CZ  
1113 O  OH  A TYR   A 42  ? 0.2100 0.1875 0.1592 -0.0253 0.0131  0.0244  42  TYR   A OH  
1114 O  OH  B TYR   A 42  ? 0.1991 0.1857 0.1609 -0.0043 0.0131  0.0113  42  TYR   A OH  
1133 N  N   . LEU   A 43  ? 0.1268 0.1140 0.1424 -0.0056 0.0198  0.0097  43  LEU   A N   
1134 C  CA  . LEU   A 43  ? 0.1192 0.1143 0.1326 -0.0055 0.0139  0.0082  43  LEU   A CA  
1135 C  C   . LEU   A 43  ? 0.1225 0.1208 0.1323 -0.0061 0.0116  0.0056  43  LEU   A C   
1136 O  O   . LEU   A 43  ? 0.1392 0.1214 0.1509 0.0015  -0.0046 0.0063  43  LEU   A O   
1137 C  CB  . LEU   A 43  ? 0.1256 0.1126 0.1557 -0.0114 0.0089  0.0099  43  LEU   A CB  
1138 C  CG  . LEU   A 43  ? 0.1334 0.1128 0.1549 -0.0020 0.0107  0.0082  43  LEU   A CG  
1139 C  CD1 . LEU   A 43  ? 0.1386 0.1233 0.1758 -0.0018 -0.0010 0.0198  43  LEU   A CD1 
1140 C  CD2 . LEU   A 43  ? 0.1521 0.1204 0.1497 -0.0058 0.0071  0.0184  43  LEU   A CD2 
1153 N  N   A LYS   A 44  ? 0.1298 0.1198 0.1290 -0.0013 0.0107  0.0137  44  LYS   A N   
1154 N  N   B LYS   A 44  ? 0.1300 0.1231 0.1371 -0.0020 0.0071  0.0142  44  LYS   A N   
1155 C  CA  A LYS   A 44  ? 0.1433 0.1206 0.1283 -0.0060 0.0215  0.0181  44  LYS   A CA  
1156 C  CA  B LYS   A 44  ? 0.1411 0.1273 0.1458 -0.0035 0.0108  0.0204  44  LYS   A CA  
1157 C  C   A LYS   A 44  ? 0.1330 0.1230 0.1132 0.0019  0.0045  0.0111  44  LYS   A C   
1158 C  C   B LYS   A 44  ? 0.1282 0.1264 0.1292 -0.0025 0.0057  0.0199  44  LYS   A C   
1159 O  O   A LYS   A 44  ? 0.1482 0.1366 0.1307 0.0044  -0.0021 -0.0085 44  LYS   A O   
1160 O  O   B LYS   A 44  ? 0.1314 0.1363 0.1359 -0.0060 0.0089  0.0191  44  LYS   A O   
1161 C  CB  A LYS   A 44  ? 0.1738 0.1364 0.1689 -0.0079 0.0334  0.0266  44  LYS   A CB  
1162 C  CB  B LYS   A 44  ? 0.1697 0.1428 0.1857 0.0013  0.0156  0.0250  44  LYS   A CB  
1163 C  CG  A LYS   A 44  ? 0.2015 0.1600 0.2349 -0.0123 0.0547  0.0387  44  LYS   A CG  
1164 C  CG  B LYS   A 44  ? 0.1941 0.1705 0.2464 0.0050  0.0232  0.0343  44  LYS   A CG  
1165 C  CD  A LYS   A 44  ? 0.2333 0.2023 0.3406 -0.0151 0.0515  0.0308  44  LYS   A CD  
1166 C  CD  B LYS   A 44  ? 0.2204 0.2077 0.3236 0.0028  0.0155  0.0320  44  LYS   A CD  
1167 C  CE  A LYS   A 44  ? 0.2502 0.2364 0.4123 -0.0118 0.0480  0.0216  44  LYS   A CE  
1168 C  CE  B LYS   A 44  ? 0.2302 0.2305 0.3748 -0.0027 0.0102  0.0307  44  LYS   A CE  
1169 N  NZ  A LYS   A 44  ? 0.2575 0.2574 0.4445 -0.0139 0.0447  0.0158  44  LYS   A NZ  
1170 N  NZ  B LYS   A 44  ? 0.2385 0.2453 0.4004 -0.0133 0.0082  0.0286  44  LYS   A NZ  
1197 N  N   . HIS   A 45  ? 0.1214 0.1142 0.1328 -0.0027 0.0043  0.0158  45  HIS   A N   
1198 C  CA  . HIS   A 45  ? 0.1221 0.1146 0.1295 0.0007  -0.0001 0.0090  45  HIS   A CA  
1199 C  C   . HIS   A 45  ? 0.1251 0.1266 0.1366 -0.0002 0.0023  0.0111  45  HIS   A C   
1200 O  O   . HIS   A 45  ? 0.1430 0.1421 0.1685 0.0188  -0.0083 -0.0032 45  HIS   A O   
1201 C  CB  . HIS   A 45  ? 0.1235 0.1103 0.1275 -0.0027 -0.0010 0.0084  45  HIS   A CB  
1202 C  CG  . HIS   A 45  ? 0.1196 0.1169 0.1176 -0.0058 0.0031  0.0107  45  HIS   A CG  
1203 N  ND1 . HIS   A 45  ? 0.1092 0.1252 0.1333 -0.0054 -0.0014 0.0126  45  HIS   A ND1 
1204 C  CD2 . HIS   A 45  ? 0.1149 0.1236 0.1237 -0.0108 -0.0053 0.0148  45  HIS   A CD2 
1205 C  CE1 . HIS   A 45  ? 0.1144 0.1286 0.1217 -0.0098 0.0016  0.0209  45  HIS   A CE1 
1206 N  NE2 . HIS   A 45  ? 0.1144 0.1285 0.1251 -0.0073 -0.0014 0.0195  45  HIS   A NE2 
1215 N  N   A GLY   A 46  ? 0.1366 0.1365 0.1499 0.0070  -0.0103 0.0160  46  GLY   A N   
1216 N  N   B GLY   A 46  ? 0.1393 0.1310 0.1365 0.0032  -0.0088 0.0090  46  GLY   A N   
1217 C  CA  A GLY   A 46  ? 0.1414 0.1413 0.1766 0.0137  -0.0168 0.0309  46  GLY   A CA  
1218 C  CA  B GLY   A 46  ? 0.1441 0.1348 0.1450 0.0105  -0.0111 0.0155  46  GLY   A CA  
1219 C  C   A GLY   A 46  ? 0.1479 0.1393 0.1722 0.0185  -0.0279 0.0396  46  GLY   A C   
1220 C  C   B GLY   A 46  ? 0.1444 0.1343 0.1266 0.0176  -0.0171 0.0180  46  GLY   A C   
1221 O  O   A GLY   A 46  ? 0.1491 0.1455 0.1985 0.0199  -0.0469 0.0285  46  GLY   A O   
1222 O  O   B GLY   A 46  ? 0.1445 0.1466 0.1548 0.0211  -0.0179 -0.0007 46  GLY   A O   
1229 N  N   A GLY   A 47  ? 0.1438 0.1372 0.1428 0.0194  -0.0109 0.0271  47  GLY   A N   
1230 N  N   B GLY   A 47  ? 0.1419 0.1305 0.1173 0.0178  -0.0079 0.0055  47  GLY   A N   
1231 C  CA  A GLY   A 47  ? 0.1413 0.1395 0.1210 0.0263  -0.0180 0.0072  47  GLY   A CA  
1232 C  CA  B GLY   A 47  ? 0.1397 0.1338 0.1185 0.0170  -0.0163 0.0025  47  GLY   A CA  
1233 C  C   A GLY   A 47  ? 0.1396 0.1347 0.1244 0.0241  -0.0255 0.0050  47  GLY   A C   
1234 C  C   B GLY   A 47  ? 0.1387 0.1236 0.1034 0.0148  -0.0082 -0.0087 47  GLY   A C   
1235 O  O   A GLY   A 47  ? 0.1345 0.1330 0.1391 0.0241  -0.0231 0.0167  47  GLY   A O   
1236 O  O   B GLY   A 47  ? 0.1403 0.1237 0.1030 0.0178  -0.0008 0.0053  47  GLY   A O   
1243 N  N   A GLY   A 48  ? 0.1369 0.1371 0.1235 0.0277  -0.0237 -0.0116 48  GLY   A N   
1244 N  N   B GLY   A 48  ? 0.1388 0.1284 0.1234 0.0069  -0.0070 -0.0091 48  GLY   A N   
1245 C  CA  A GLY   A 48  ? 0.1327 0.1338 0.1548 0.0201  -0.0209 -0.0116 48  GLY   A CA  
1246 C  CA  B GLY   A 48  ? 0.1327 0.1184 0.1297 0.0022  -0.0065 -0.0095 48  GLY   A CA  
1247 C  C   A GLY   A 48  ? 0.1266 0.1280 0.1380 0.0098  -0.0036 -0.0015 48  GLY   A C   
1248 C  C   B GLY   A 48  ? 0.1255 0.1195 0.1309 -0.0029 -0.0010 0.0004  48  GLY   A C   
1249 O  O   A GLY   A 48  ? 0.1368 0.1278 0.1319 -0.0019 0.0006  0.0123  48  GLY   A O   
1250 O  O   B GLY   A 48  ? 0.1358 0.1191 0.1177 -0.0009 0.0152  0.0006  48  GLY   A O   
1257 N  N   A VAL   A 49  ? 0.1205 0.1225 0.1521 0.0058  -0.0121 -0.0002 49  VAL   A N   
1258 N  N   B VAL   A 49  ? 0.1106 0.1194 0.1441 -0.0050 -0.0120 -0.0033 49  VAL   A N   
1259 C  CA  A VAL   A 49  ? 0.1326 0.1182 0.1490 -0.0015 0.0085  0.0042  49  VAL   A CA  
1260 C  CA  B VAL   A 49  ? 0.1061 0.1204 0.1466 -0.0049 -0.0054 0.0055  49  VAL   A CA  
1261 C  C   A VAL   A 49  ? 0.1264 0.1113 0.1270 -0.0016 0.0089  0.0145  49  VAL   A C   
1262 C  C   B VAL   A 49  ? 0.1063 0.1117 0.1261 -0.0025 0.0001  0.0044  49  VAL   A C   
1263 O  O   A VAL   A 49  ? 0.1297 0.1251 0.1332 -0.0082 0.0109  0.0056  49  VAL   A O   
1264 O  O   B VAL   A 49  ? 0.1068 0.1035 0.1265 0.0008  0.0029  0.0086  49  VAL   A O   
1265 C  CB  A VAL   A 49  ? 0.1420 0.1238 0.1587 -0.0027 0.0093  -0.0065 49  VAL   A CB  
1266 C  CB  B VAL   A 49  ? 0.0957 0.1189 0.1495 0.0007  0.0010  0.0050  49  VAL   A CB  
1267 C  CG1 A VAL   A 49  ? 0.1398 0.1111 0.1615 0.0062  0.0138  0.0005  49  VAL   A CG1 
1268 C  CG1 B VAL   A 49  ? 0.0862 0.1123 0.1379 0.0144  0.0018  0.0059  49  VAL   A CG1 
1269 C  CG2 A VAL   A 49  ? 0.1561 0.1388 0.2028 -0.0179 0.0070  -0.0080 49  VAL   A CG2 
1270 C  CG2 B VAL   A 49  ? 0.0969 0.1217 0.1636 -0.0009 0.0126  0.0040  49  VAL   A CG2 
1289 N  N   A ALA   A 50  ? 0.1173 0.1078 0.1291 -0.0056 -0.0145 0.0138  50  ALA   A N   
1290 N  N   B ALA   A 50  ? 0.1097 0.1125 0.1133 -0.0002 0.0014  0.0000  50  ALA   A N   
1291 C  CA  A ALA   A 50  ? 0.1095 0.1089 0.1319 -0.0125 -0.0130 0.0176  50  ALA   A CA  
1292 C  CA  B ALA   A 50  ? 0.1132 0.1164 0.1040 -0.0057 0.0027  -0.0004 50  ALA   A CA  
1293 C  C   A ALA   A 50  ? 0.1044 0.1100 0.1441 -0.0087 -0.0121 0.0129  50  ALA   A C   
1294 C  C   B ALA   A 50  ? 0.1194 0.1178 0.0864 -0.0046 0.0057  -0.0034 50  ALA   A C   
1295 O  O   A ALA   A 50  ? 0.1070 0.1115 0.1662 -0.0029 -0.0116 0.0082  50  ALA   A O   
1296 O  O   B ALA   A 50  ? 0.1244 0.1203 0.0713 -0.0020 0.0134  -0.0023 50  ALA   A O   
1297 C  CB  A ALA   A 50  ? 0.1113 0.1123 0.1221 -0.0106 -0.0110 0.0100  50  ALA   A CB  
1298 C  CB  B ALA   A 50  ? 0.1156 0.1138 0.1023 -0.0053 0.0071  -0.0059 50  ALA   A CB  
1309 N  N   A GLY   A 51  ? 0.1097 0.1080 0.1465 0.0035  -0.0166 0.0159  51  GLY   A N   
1310 N  N   B GLY   A 51  ? 0.1241 0.1172 0.1059 0.0003  -0.0013 -0.0046 51  GLY   A N   
1311 C  CA  A GLY   A 51  ? 0.1262 0.1036 0.1506 0.0056  -0.0195 0.0135  51  GLY   A CA  
1312 C  CA  B GLY   A 51  ? 0.1335 0.1138 0.1206 0.0011  -0.0084 -0.0075 51  GLY   A CA  
1313 C  C   A GLY   A 51  ? 0.1165 0.1119 0.1418 0.0055  -0.0105 0.0026  51  GLY   A C   
1314 C  C   B GLY   A 51  ? 0.1250 0.1190 0.1252 0.0019  -0.0044 -0.0083 51  GLY   A C   
1315 O  O   A GLY   A 51  ? 0.1172 0.1220 0.1588 0.0035  -0.0129 -0.0001 51  GLY   A O   
1316 O  O   B GLY   A 51  ? 0.1274 0.1262 0.1303 0.0000  -0.0084 -0.0118 51  GLY   A O   
1323 N  N   . ALA   A 52  ? 0.1203 0.1221 0.1308 0.0028  -0.0026 -0.0098 52  ALA   A N   
1324 C  CA  . ALA   A 52  ? 0.1223 0.1332 0.1442 -0.0028 0.0025  -0.0107 52  ALA   A CA  
1325 C  C   . ALA   A 52  ? 0.1156 0.1362 0.1195 -0.0097 0.0076  -0.0036 52  ALA   A C   
1326 O  O   . ALA   A 52  ? 0.1274 0.1449 0.1356 -0.0043 0.0021  -0.0101 52  ALA   A O   
1327 C  CB  . ALA   A 52  ? 0.1265 0.1646 0.1686 -0.0118 -0.0042 -0.0050 52  ALA   A CB  
1334 N  N   A LEU   A 53  ? 0.1167 0.1258 0.1218 -0.0059 0.0003  -0.0016 53  LEU   A N   
1335 N  N   B LEU   A 53  ? 0.1086 0.1290 0.1175 -0.0032 0.0020  -0.0049 53  LEU   A N   
1336 C  CA  A LEU   A 53  ? 0.1284 0.1301 0.1192 -0.0074 0.0068  0.0045  53  LEU   A CA  
1337 C  CA  B LEU   A 53  ? 0.1083 0.1316 0.1125 -0.0011 0.0069  -0.0047 53  LEU   A CA  
1338 C  C   A LEU   A 53  ? 0.1302 0.1369 0.1047 -0.0004 0.0025  0.0029  53  LEU   A C   
1339 C  C   B LEU   A 53  ? 0.1062 0.1319 0.0992 0.0068  0.0040  -0.0017 53  LEU   A C   
1340 O  O   A LEU   A 53  ? 0.1429 0.1438 0.1199 -0.0115 0.0031  0.0092  53  LEU   A O   
1341 O  O   B LEU   A 53  ? 0.1116 0.1330 0.1096 0.0037  -0.0017 0.0018  53  LEU   A O   
1342 C  CB  A LEU   A 53  ? 0.1380 0.1340 0.1208 -0.0095 0.0045  0.0121  53  LEU   A CB  
1343 C  CB  B LEU   A 53  ? 0.1130 0.1370 0.1179 -0.0050 -0.0024 -0.0025 53  LEU   A CB  
1344 C  CG  A LEU   A 53  ? 0.1463 0.1314 0.1266 -0.0149 0.0043  0.0149  53  LEU   A CG  
1345 C  CG  B LEU   A 53  ? 0.1252 0.1372 0.1293 -0.0092 -0.0109 -0.0019 53  LEU   A CG  
1346 C  CD1 A LEU   A 53  ? 0.1445 0.1416 0.1306 -0.0024 0.0094  0.0171  53  LEU   A CD1 
1347 C  CD1 B LEU   A 53  ? 0.1258 0.1432 0.1322 -0.0043 -0.0148 -0.0107 53  LEU   A CD1 
1348 C  CD2 A LEU   A 53  ? 0.1672 0.1462 0.1421 -0.0234 0.0132  0.0172  53  LEU   A CD2 
1349 C  CD2 B LEU   A 53  ? 0.1379 0.1454 0.1432 -0.0128 -0.0029 -0.0057 53  LEU   A CD2 
1372 N  N   A ASN   A 54  ? 0.1237 0.1305 0.1109 -0.0017 -0.0053 0.0015  54  ASN   A N   
1373 N  N   B ASN   A 54  ? 0.1059 0.1307 0.1032 0.0030  0.0030  0.0010  54  ASN   A N   
1374 C  CA  A ASN   A 54  ? 0.1148 0.1237 0.1294 -0.0041 -0.0070 -0.0040 54  ASN   A CA  
1375 C  CA  B ASN   A 54  ? 0.1039 0.1294 0.1142 0.0015  -0.0008 0.0024  54  ASN   A CA  
1376 C  C   A ASN   A 54  ? 0.1244 0.1238 0.1312 -0.0122 -0.0055 0.0008  54  ASN   A C   
1377 C  C   B ASN   A 54  ? 0.1179 0.1274 0.1255 -0.0064 -0.0037 -0.0019 54  ASN   A C   
1378 O  O   A ASN   A 54  ? 0.1292 0.1365 0.1369 -0.0092 -0.0080 -0.0061 54  ASN   A O   
1379 O  O   B ASN   A 54  ? 0.1204 0.1337 0.1317 -0.0056 -0.0061 -0.0119 54  ASN   A O   
1380 C  CB  A ASN   A 54  ? 0.1139 0.1179 0.1350 -0.0107 -0.0061 -0.0103 54  ASN   A CB  
1381 C  CB  B ASN   A 54  ? 0.1030 0.1318 0.1118 0.0029  0.0010  0.0099  54  ASN   A CB  
1382 C  CG  A ASN   A 54  ? 0.1146 0.1132 0.1348 -0.0101 -0.0014 -0.0064 54  ASN   A CG  
1383 C  CG  B ASN   A 54  ? 0.1041 0.1293 0.1110 0.0070  0.0022  0.0072  54  ASN   A CG  
1384 O  OD1 A ASN   A 54  ? 0.1156 0.1076 0.1209 -0.0112 -0.0059 0.0107  54  ASN   A OD1 
1385 O  OD1 B ASN   A 54  ? 0.1037 0.1397 0.1295 0.0008  0.0026  0.0014  54  ASN   A OD1 
1386 N  ND2 A ASN   A 54  ? 0.1125 0.1171 0.1694 -0.0071 -0.0118 -0.0043 54  ASN   A ND2 
1387 N  ND2 B ASN   A 54  ? 0.1084 0.1174 0.1145 0.0101  -0.0012 0.0042  54  ASN   A ND2 
1400 N  N   . LYS   A 55  ? 0.1242 0.1262 0.1378 -0.0042 -0.0036 -0.0064 55  LYS   A N   
1401 C  CA  . LYS   A 55  ? 0.1319 0.1354 0.1415 0.0050  -0.0096 -0.0094 55  LYS   A CA  
1402 C  C   . LYS   A 55  ? 0.1294 0.1396 0.1472 -0.0031 0.0010  -0.0192 55  LYS   A C   
1403 O  O   . LYS   A 55  ? 0.1341 0.1494 0.1553 0.0030  -0.0050 -0.0188 55  LYS   A O   
1404 C  CB  . LYS   A 55  ? 0.1400 0.1429 0.1576 0.0170  -0.0069 -0.0132 55  LYS   A CB  
1405 C  CG  . LYS   A 55  ? 0.1515 0.1714 0.1746 0.0241  -0.0177 -0.0225 55  LYS   A CG  
1406 C  CD  . LYS   A 55  ? 0.1646 0.2008 0.1961 0.0353  -0.0096 -0.0184 55  LYS   A CD  
1407 C  CE  . LYS   A 55  ? 0.1861 0.2359 0.2198 0.0418  -0.0217 -0.0168 55  LYS   A CE  
1408 N  NZ  . LYS   A 55  ? 0.1887 0.2458 0.2261 0.0502  -0.0258 -0.0104 55  LYS   A NZ  
1423 N  N   . ALA   A 56  ? 0.1307 0.1507 0.1397 -0.0100 0.0037  -0.0200 56  ALA   A N   
1424 C  CA  . ALA   A 56  ? 0.1435 0.1661 0.1376 -0.0123 0.0099  -0.0157 56  ALA   A CA  
1425 C  C   . ALA   A 56  ? 0.1475 0.1742 0.1186 -0.0112 0.0035  -0.0224 56  ALA   A C   
1426 O  O   . ALA   A 56  ? 0.1591 0.2119 0.1340 0.0033  0.0119  -0.0159 56  ALA   A O   
1427 C  CB  . ALA   A 56  ? 0.1496 0.1895 0.1484 -0.0123 0.0127  -0.0070 56  ALA   A CB  
1433 N  N   . THR   A 57  ? 0.1318 0.1577 0.1237 -0.0076 0.0066  -0.0121 57  THR   A N   
1434 C  CA  . THR   A 57  ? 0.1389 0.1569 0.1215 -0.0095 0.0013  -0.0114 57  THR   A CA  
1435 C  C   . THR   A 57  ? 0.1392 0.1648 0.1335 -0.0046 -0.0042 -0.0197 57  THR   A C   
1436 O  O   . THR   A 57  ? 0.1355 0.1709 0.1524 -0.0075 -0.0105 -0.0272 57  THR   A O   
1437 C  CB  . THR   A 57  ? 0.1401 0.1581 0.1240 -0.0088 -0.0007 -0.0126 57  THR   A CB  
1438 O  OG1 . THR   A 57  ? 0.1297 0.1472 0.1237 -0.0081 0.0035  -0.0056 57  THR   A OG1 
1439 C  CG2 . THR   A 57  ? 0.1448 0.1613 0.1146 -0.0073 -0.0001 0.0044  57  THR   A CG2 
1447 N  N   . ASN   A 58  ? 0.1394 0.1552 0.1488 -0.0053 0.0011  -0.0330 58  ASN   A N   
1448 C  CA  . ASN   A 58  ? 0.1614 0.1465 0.1753 -0.0132 0.0108  -0.0438 58  ASN   A CA  
1449 C  C   . ASN   A 58  ? 0.1401 0.1342 0.1641 -0.0024 0.0016  -0.0206 58  ASN   A C   
1450 O  O   . ASN   A 58  ? 0.1405 0.1509 0.1748 -0.0152 0.0010  -0.0275 58  ASN   A O   
1451 C  CB  . ASN   A 58  ? 0.2079 0.1739 0.2203 -0.0213 0.0414  -0.0614 58  ASN   A CB  
1452 C  CG  . ASN   A 58  ? 0.2567 0.2005 0.2955 -0.0216 0.0448  -0.0505 58  ASN   A CG  
1453 O  OD1 . ASN   A 58  ? 0.2838 0.1955 0.3394 0.0143  0.0807  -0.0366 58  ASN   A OD1 
1454 N  ND2 . ASN   A 58  ? 0.2743 0.2193 0.3267 -0.0279 0.0280  -0.0628 58  ASN   A ND2 
1461 N  N   . ASN   A 59  ? 0.1237 0.1300 0.1445 -0.0021 -0.0118 -0.0165 59  ASN   A N   
1462 C  CA  . ASN   A 59  ? 0.1248 0.1232 0.1514 -0.0023 -0.0061 -0.0034 59  ASN   A CA  
1463 C  C   . ASN   A 59  ? 0.1250 0.1278 0.1371 -0.0089 -0.0069 -0.0028 59  ASN   A C   
1464 O  O   . ASN   A 59  ? 0.1247 0.1330 0.1459 -0.0076 -0.0042 0.0022  59  ASN   A O   
1465 C  CB  . ASN   A 59  ? 0.1305 0.1226 0.1626 0.0031  -0.0162 -0.0136 59  ASN   A CB  
1466 C  CG  . ASN   A 59  ? 0.1312 0.1273 0.1617 -0.0031 -0.0260 0.0012  59  ASN   A CG  
1467 O  OD1 . ASN   A 59  ? 0.1444 0.1347 0.1513 -0.0116 -0.0263 0.0080  59  ASN   A OD1 
1468 N  ND2 . ASN   A 59  ? 0.1417 0.1328 0.1661 -0.0144 -0.0149 0.0060  59  ASN   A ND2 
1475 N  N   . ALA   A 60  ? 0.1190 0.1331 0.1419 -0.0028 -0.0033 -0.0014 60  ALA   A N   
1476 C  CA  . ALA   A 60  ? 0.1226 0.1348 0.1413 -0.0030 -0.0096 -0.0045 60  ALA   A CA  
1477 C  C   . ALA   A 60  ? 0.1227 0.1294 0.1427 -0.0029 -0.0048 0.0003  60  ALA   A C   
1478 O  O   . ALA   A 60  ? 0.1181 0.1277 0.1687 -0.0018 -0.0108 -0.0047 60  ALA   A O   
1479 C  CB  . ALA   A 60  ? 0.1358 0.1461 0.1508 -0.0030 -0.0154 -0.0216 60  ALA   A CB  
1485 N  N   . MET   A 61  ? 0.1149 0.1236 0.1394 -0.0085 -0.0032 -0.0056 61  MET   A N   
1486 C  CA  . MET   A 61  ? 0.1196 0.1168 0.1351 -0.0054 0.0037  0.0010  61  MET   A CA  
1487 C  C   . MET   A 61  ? 0.1189 0.1168 0.1347 -0.0059 -0.0047 -0.0028 61  MET   A C   
1488 O  O   . MET   A 61  ? 0.1263 0.1187 0.1440 -0.0009 0.0026  0.0070  61  MET   A O   
1489 C  CB  . MET   A 61  ? 0.1229 0.1250 0.1194 -0.0067 0.0024  -0.0032 61  MET   A CB  
1490 C  CG  . MET   A 61  ? 0.1243 0.1360 0.1407 -0.0046 -0.0027 0.0077  61  MET   A CG  
1491 S  SD  . MET   A 61  ? 0.1250 0.1318 0.1692 -0.0099 -0.0011 -0.0134 61  MET   A SD  
1492 C  CE  . MET   A 61  ? 0.1470 0.1452 0.1897 -0.0125 0.0173  -0.0100 61  MET   A CE  
1502 N  N   . GLN   A 62  ? 0.1174 0.1187 0.1375 -0.0082 -0.0010 -0.0057 62  GLN   A N   
1503 C  CA  . GLN   A 62  ? 0.1193 0.1183 0.1369 -0.0070 0.0036  0.0006  62  GLN   A CA  
1504 C  C   . GLN   A 62  ? 0.1242 0.1100 0.1397 -0.0005 0.0086  0.0010  62  GLN   A C   
1505 O  O   . GLN   A 62  ? 0.1265 0.1212 0.1423 -0.0057 0.0020  0.0044  62  GLN   A O   
1506 C  CB  . GLN   A 62  ? 0.1230 0.1166 0.1403 -0.0008 0.0028  0.0054  62  GLN   A CB  
1507 C  CG  . GLN   A 62  ? 0.1265 0.1132 0.1420 -0.0070 -0.0035 0.0111  62  GLN   A CG  
1508 C  CD  . GLN   A 62  ? 0.1324 0.1139 0.1337 -0.0063 0.0040  0.0040  62  GLN   A CD  
1509 O  OE1 . GLN   A 62  ? 0.1351 0.1274 0.1415 -0.0044 -0.0014 0.0037  62  GLN   A OE1 
1510 N  NE2 . GLN   A 62  ? 0.1368 0.1279 0.1499 -0.0030 0.0015  -0.0040 62  GLN   A NE2 
1519 N  N   . VAL   A 63  ? 0.1178 0.1163 0.1594 -0.0072 0.0066  -0.0118 63  VAL   A N   
1520 C  CA  . VAL   A 63  ? 0.1214 0.1266 0.1768 -0.0110 0.0056  -0.0094 63  VAL   A CA  
1521 C  C   . VAL   A 63  ? 0.1129 0.1276 0.1637 -0.0145 -0.0005 -0.0095 63  VAL   A C   
1522 O  O   . VAL   A 63  ? 0.1144 0.1313 0.1838 -0.0137 -0.0013 -0.0034 63  VAL   A O   
1523 C  CB  . VAL   A 63  ? 0.1313 0.1413 0.2081 -0.0138 -0.0033 -0.0317 63  VAL   A CB  
1524 C  CG1 . VAL   A 63  ? 0.1426 0.1571 0.2454 -0.0140 -0.0092 -0.0495 63  VAL   A CG1 
1525 C  CG2 . VAL   A 63  ? 0.1436 0.1361 0.2283 -0.0113 0.0059  -0.0325 63  VAL   A CG2 
1535 N  N   . GLU   A 64  ? 0.1157 0.1336 0.1555 -0.0060 -0.0015 -0.0092 64  GLU   A N   
1536 C  CA  . GLU   A 64  ? 0.1123 0.1314 0.1554 -0.0053 -0.0040 0.0015  64  GLU   A CA  
1537 C  C   . GLU   A 64  ? 0.1034 0.1231 0.1560 -0.0092 0.0043  0.0013  64  GLU   A C   
1538 O  O   . GLU   A 64  ? 0.1191 0.1327 0.1588 -0.0031 -0.0017 -0.0022 64  GLU   A O   
1539 C  CB  . GLU   A 64  ? 0.1256 0.1386 0.1547 -0.0106 0.0012  -0.0050 64  GLU   A CB  
1540 C  CG  . GLU   A 64  ? 0.1355 0.1435 0.1709 -0.0100 0.0054  -0.0049 64  GLU   A CG  
1541 C  CD  . GLU   A 64  ? 0.1480 0.1482 0.1731 -0.0158 0.0066  -0.0017 64  GLU   A CD  
1542 O  OE1 . GLU   A 64  ? 0.1443 0.1561 0.2015 -0.0218 0.0145  0.0000  64  GLU   A OE1 
1543 O  OE2 . GLU   A 64  ? 0.1609 0.1510 0.1680 -0.0207 -0.0008 0.0078  64  GLU   A OE2 
1550 N  N   . SER   A 65  ? 0.1029 0.1281 0.1483 0.0005  0.0065  -0.0015 65  SER   A N   
1551 C  CA  . SER   A 65  ? 0.1129 0.1226 0.1500 -0.0024 -0.0042 0.0025  65  SER   A CA  
1552 C  C   . SER   A 65  ? 0.1159 0.1303 0.1452 -0.0012 -0.0064 -0.0015 65  SER   A C   
1553 O  O   . SER   A 65  ? 0.1268 0.1319 0.1677 0.0013  0.0143  -0.0059 65  SER   A O   
1554 C  CB  . SER   A 65  ? 0.1156 0.1175 0.1477 -0.0094 0.0079  0.0074  65  SER   A CB  
1555 O  OG  . SER   A 65  ? 0.1150 0.1300 0.1588 -0.0103 -0.0014 0.0108  65  SER   A OG  
1561 N  N   . ASP   A 66  ? 0.1166 0.1223 0.1485 -0.0039 0.0120  0.0036  66  ASP   A N   
1562 C  CA  . ASP   A 66  ? 0.1251 0.1351 0.1673 -0.0036 0.0069  0.0138  66  ASP   A CA  
1563 C  C   . ASP   A 66  ? 0.1206 0.1278 0.1710 -0.0074 0.0092  0.0176  66  ASP   A C   
1564 O  O   . ASP   A 66  ? 0.1286 0.1414 0.1924 -0.0035 0.0231  0.0273  66  ASP   A O   
1565 C  CB  . ASP   A 66  ? 0.1349 0.1406 0.1999 0.0040  0.0177  0.0344  66  ASP   A CB  
1566 C  CG  . ASP   A 66  ? 0.1549 0.1540 0.2251 -0.0018 0.0053  0.0495  66  ASP   A CG  
1567 O  OD1 . ASP   A 66  ? 0.1569 0.1866 0.2000 -0.0125 -0.0008 0.0485  66  ASP   A OD1 
1568 O  OD2 . ASP   A 66  ? 0.1734 0.1664 0.3152 0.0173  -0.0113 0.0310  66  ASP   A OD2 
1573 N  N   . ASP   A 67  ? 0.1190 0.1346 0.1830 -0.0040 0.0093  0.0176  67  ASP   A N   
1574 C  CA  . ASP   A 67  ? 0.1188 0.1489 0.1958 -0.0048 0.0012  0.0212  67  ASP   A CA  
1575 C  C   . ASP   A 67  ? 0.1188 0.1528 0.1922 -0.0021 0.0128  0.0208  67  ASP   A C   
1576 O  O   . ASP   A 67  ? 0.1186 0.1579 0.2117 -0.0017 0.0237  0.0307  67  ASP   A O   
1577 C  CB  . ASP   A 67  ? 0.1267 0.1553 0.2368 -0.0098 -0.0091 0.0306  67  ASP   A CB  
1578 C  CG  . ASP   A 67  ? 0.1221 0.1704 0.2718 -0.0116 -0.0244 0.0426  67  ASP   A CG  
1579 O  OD1 . ASP   A 67  ? 0.1343 0.1918 0.3493 -0.0117 -0.0349 0.0550  67  ASP   A OD1 
1580 O  OD2 . ASP   A 67  ? 0.1318 0.1748 0.2490 -0.0051 -0.0204 0.0288  67  ASP   A OD2 
1585 N  N   . TYR   A 68  ? 0.1190 0.1366 0.1890 0.0010  0.0170  0.0280  68  TYR   A N   
1586 C  CA  . TYR   A 68  ? 0.1351 0.1324 0.1739 0.0014  0.0186  0.0308  68  TYR   A CA  
1587 C  C   . TYR   A 68  ? 0.1279 0.1318 0.1772 -0.0007 0.0270  0.0197  68  TYR   A C   
1588 O  O   . TYR   A 68  ? 0.1366 0.1387 0.1929 0.0079  0.0346  0.0203  68  TYR   A O   
1589 C  CB  . TYR   A 68  ? 0.1380 0.1281 0.1895 0.0074  0.0370  0.0286  68  TYR   A CB  
1590 C  CG  . TYR   A 68  ? 0.1422 0.1451 0.2244 0.0035  0.0521  0.0361  68  TYR   A CG  
1591 C  CD1 . TYR   A 68  ? 0.1488 0.1540 0.2556 -0.0203 0.0443  0.0019  68  TYR   A CD1 
1592 C  CD2 . TYR   A 68  ? 0.1640 0.1494 0.2700 0.0078  0.0606  0.0442  68  TYR   A CD2 
1593 C  CE1 . TYR   A 68  ? 0.1560 0.1605 0.2893 -0.0138 0.0475  -0.0044 68  TYR   A CE1 
1594 C  CE2 . TYR   A 68  ? 0.1627 0.1566 0.2898 0.0000  0.0685  0.0231  68  TYR   A CE2 
1595 C  CZ  . TYR   A 68  ? 0.1629 0.1579 0.2978 -0.0156 0.0515  -0.0006 68  TYR   A CZ  
1596 O  OH  . TYR   A 68  ? 0.1956 0.1572 0.3056 -0.0133 0.0222  -0.0159 68  TYR   A OH  
1606 N  N   . ILE   A 69  ? 0.1233 0.1266 0.1716 -0.0010 0.0158  0.0198  69  ILE   A N   
1607 C  CA  . ILE   A 69  ? 0.1299 0.1324 0.1608 0.0035  0.0110  0.0092  69  ILE   A CA  
1608 C  C   . ILE   A 69  ? 0.1366 0.1298 0.1537 0.0069  0.0143  0.0183  69  ILE   A C   
1609 O  O   . ILE   A 69  ? 0.1461 0.1379 0.1583 -0.0055 0.0275  0.0160  69  ILE   A O   
1610 C  CB  . ILE   A 69  ? 0.1367 0.1522 0.1721 0.0006  0.0131  -0.0010 69  ILE   A CB  
1611 C  CG1 . ILE   A 69  ? 0.1362 0.1641 0.1666 0.0057  0.0192  -0.0218 69  ILE   A CG1 
1612 C  CG2 . ILE   A 69  ? 0.1582 0.1694 0.1895 0.0065  0.0005  -0.0017 69  ILE   A CG2 
1613 C  CD1 . ILE   A 69  ? 0.1401 0.1727 0.1907 -0.0075 0.0157  -0.0182 69  ILE   A CD1 
1625 N  N   . ALA   A 70  ? 0.1388 0.1334 0.1702 -0.0029 0.0190  0.0207  70  ALA   A N   
1626 C  CA  . ALA   A 70  ? 0.1369 0.1462 0.1906 -0.0099 0.0287  0.0234  70  ALA   A CA  
1627 C  C   . ALA   A 70  ? 0.1340 0.1629 0.1885 -0.0114 0.0296  0.0249  70  ALA   A C   
1628 O  O   . ALA   A 70  ? 0.1516 0.1950 0.2053 0.0063  0.0491  0.0405  70  ALA   A O   
1629 C  CB  . ALA   A 70  ? 0.1448 0.1385 0.2173 -0.0148 0.0195  0.0169  70  ALA   A CB  
1635 N  N   . THR   A 71  ? 0.1322 0.1556 0.1735 -0.0009 0.0206  0.0239  71  THR   A N   
1636 C  CA  . THR   A 71  ? 0.1418 0.1768 0.2037 0.0061  0.0251  0.0306  71  THR   A CA  
1637 C  C   . THR   A 71  ? 0.1290 0.1693 0.2236 0.0120  0.0328  0.0249  71  THR   A C   
1638 O  O   . THR   A 71  ? 0.1348 0.1950 0.2692 0.0075  0.0391  0.0012  71  THR   A O   
1639 C  CB  . THR   A 71  ? 0.1700 0.2050 0.2316 0.0159  -0.0105 0.0372  71  THR   A CB  
1640 O  OG1 . THR   A 71  ? 0.1974 0.2231 0.2408 0.0043  -0.0333 0.0299  71  THR   A OG1 
1641 C  CG2 . THR   A 71  ? 0.1825 0.2188 0.2629 0.0258  -0.0201 0.0504  71  THR   A CG2 
1649 N  N   . ASN   A 72  ? 0.1337 0.1482 0.2008 0.0092  0.0267  0.0256  72  ASN   A N   
1650 C  CA  . ASN   A 72  ? 0.1422 0.1501 0.2071 0.0160  0.0355  0.0254  72  ASN   A CA  
1651 C  C   . ASN   A 72  ? 0.1551 0.1474 0.2047 0.0114  0.0466  0.0164  72  ASN   A C   
1652 O  O   . ASN   A 72  ? 0.1720 0.1476 0.2376 0.0155  0.0487  0.0055  72  ASN   A O   
1653 C  CB  . ASN   A 72  ? 0.1673 0.1590 0.2130 0.0167  0.0374  0.0209  72  ASN   A CB  
1654 C  CG  . ASN   A 72  ? 0.1886 0.1698 0.2249 0.0236  0.0346  0.0271  72  ASN   A CG  
1655 O  OD1 . ASN   A 72  ? 0.2017 0.2050 0.2351 0.0224  0.0376  0.0273  72  ASN   A OD1 
1656 N  ND2 . ASN   A 72  ? 0.2050 0.1641 0.2245 0.0499  0.0178  0.0164  72  ASN   A ND2 
1663 N  N   . GLY   A 73  ? 0.1556 0.1441 0.1841 0.0038  0.0431  0.0158  73  GLY   A N   
1664 C  CA  . GLY   A 73  ? 0.1602 0.1458 0.1689 -0.0022 0.0445  0.0118  73  GLY   A CA  
1665 C  C   . GLY   A 73  ? 0.1602 0.1366 0.1634 0.0008  0.0545  0.0213  73  GLY   A C   
1666 O  O   . GLY   A 73  ? 0.1629 0.1394 0.1788 0.0080  0.0419  0.0275  73  GLY   A O   
1670 N  N   . PRO   A 74  ? 0.1729 0.1396 0.1676 -0.0132 0.0510  0.0122  74  PRO   A N   
1671 C  CA  . PRO   A 74  ? 0.1687 0.1378 0.1749 -0.0066 0.0466  0.0156  74  PRO   A CA  
1672 C  C   . PRO   A 74  ? 0.1593 0.1213 0.1737 -0.0017 0.0317  0.0086  74  PRO   A C   
1673 O  O   . PRO   A 74  ? 0.1686 0.1259 0.1955 0.0042  0.0376  0.0026  74  PRO   A O   
1674 C  CB  . PRO   A 74  ? 0.1801 0.1689 0.1951 0.0001  0.0418  0.0263  74  PRO   A CB  
1675 C  CG  . PRO   A 74  ? 0.2049 0.2039 0.2435 -0.0194 0.0359  0.0196  74  PRO   A CG  
1676 C  CD  . PRO   A 74  ? 0.1887 0.1810 0.1905 -0.0270 0.0393  0.0088  74  PRO   A CD  
1684 N  N   . LEU   A 75  ? 0.1553 0.1186 0.1524 -0.0020 0.0250  0.0072  75  LEU   A N   
1685 C  CA  . LEU   A 75  ? 0.1576 0.1192 0.1421 -0.0054 0.0077  0.0098  75  LEU   A CA  
1686 C  C   . LEU   A 75  ? 0.1710 0.1284 0.1400 0.0035  0.0084  0.0132  75  LEU   A C   
1687 O  O   . LEU   A 75  ? 0.2034 0.1434 0.1479 0.0087  0.0054  0.0101  75  LEU   A O   
1688 C  CB  . LEU   A 75  ? 0.1604 0.1258 0.1434 -0.0142 0.0108  0.0174  75  LEU   A CB  
1689 C  CG  . LEU   A 75  ? 0.1746 0.1588 0.1411 -0.0395 0.0076  0.0110  75  LEU   A CG  
1690 C  CD1 . LEU   A 75  ? 0.1859 0.2104 0.1589 -0.0379 0.0082  -0.0017 75  LEU   A CD1 
1691 C  CD2 . LEU   A 75  ? 0.1996 0.2006 0.2015 -0.0134 0.0099  0.0127  75  LEU   A CD2 
1703 N  N   . LYS   A 76  ? 0.1768 0.1233 0.1454 -0.0055 0.0114  -0.0001 76  LYS   A N   
1704 C  CA  . LYS   A 76  ? 0.1699 0.1481 0.1523 -0.0057 0.0148  -0.0121 76  LYS   A CA  
1705 C  C   . LYS   A 76  ? 0.1569 0.1325 0.1301 -0.0011 0.0165  0.0041  76  LYS   A C   
1706 O  O   . LYS   A 76  ? 0.1600 0.1261 0.1361 0.0019  0.0168  0.0108  76  LYS   A O   
1707 C  CB  . LYS   A 76  ? 0.1725 0.1707 0.1865 0.0051  0.0141  -0.0394 76  LYS   A CB  
1708 C  CG  . LYS   A 76  ? 0.1774 0.1684 0.2362 0.0118  0.0037  -0.0329 76  LYS   A CG  
1709 C  CD  . LYS   A 76  ? 0.1842 0.1678 0.2816 0.0131  -0.0017 -0.0385 76  LYS   A CD  
1710 C  CE  . LYS   A 76  ? 0.1991 0.1863 0.3412 0.0028  -0.0011 -0.0397 76  LYS   A CE  
1711 N  NZ  . LYS   A 76  ? 0.2021 0.1772 0.3854 -0.0136 -0.0089 -0.0452 76  LYS   A NZ  
1725 N  N   . VAL   A 77  ? 0.1668 0.1369 0.1330 -0.0008 0.0242  0.0127  77  VAL   A N   
1726 C  CA  . VAL   A 77  ? 0.1668 0.1358 0.1271 0.0054  0.0154  0.0121  77  VAL   A CA  
1727 C  C   . VAL   A 77  ? 0.1625 0.1307 0.1238 0.0098  0.0111  0.0066  77  VAL   A C   
1728 O  O   . VAL   A 77  ? 0.1687 0.1366 0.1287 0.0119  0.0259  0.0007  77  VAL   A O   
1729 C  CB  . VAL   A 77  ? 0.1829 0.1535 0.1350 0.0062  0.0031  0.0221  77  VAL   A CB  
1730 C  CG1 . VAL   A 77  ? 0.1802 0.1741 0.1546 0.0175  -0.0030 0.0069  77  VAL   A CG1 
1731 C  CG2 . VAL   A 77  ? 0.2077 0.1660 0.1511 0.0040  -0.0026 0.0277  77  VAL   A CG2 
1741 N  N   . GLY   A 78  ? 0.1583 0.1246 0.1233 0.0040  0.0228  0.0092  78  GLY   A N   
1742 C  CA  . GLY   A 78  ? 0.1552 0.1213 0.1398 0.0025  0.0220  0.0119  78  GLY   A CA  
1743 C  C   . GLY   A 78  ? 0.1426 0.1227 0.1351 0.0026  0.0209  0.0151  78  GLY   A C   
1744 O  O   . GLY   A 78  ? 0.1358 0.1290 0.1537 0.0009  0.0131  0.0193  78  GLY   A O   
1748 N  N   . GLY   A 79  ? 0.1473 0.1184 0.1321 -0.0000 0.0199  0.0155  79  GLY   A N   
1749 C  CA  . GLY   A 79  ? 0.1423 0.1238 0.1421 -0.0014 0.0176  0.0106  79  GLY   A CA  
1750 C  C   . GLY   A 79  ? 0.1299 0.1192 0.1361 -0.0003 0.0154  0.0067  79  GLY   A C   
1751 O  O   . GLY   A 79  ? 0.1318 0.1293 0.1465 0.0178  0.0124  0.0087  79  GLY   A O   
1755 N  N   . SER   A 80  ? 0.1232 0.1374 0.1597 0.0003  0.0154  -0.0003 80  SER   A N   
1756 C  CA  . SER   A 80  ? 0.1203 0.1274 0.1493 -0.0001 0.0092  -0.0000 80  SER   A CA  
1757 C  C   . SER   A 80  ? 0.1157 0.1306 0.1443 -0.0046 0.0124  0.0085  80  SER   A C   
1758 O  O   . SER   A 80  ? 0.1150 0.1510 0.1853 0.0040  0.0121  0.0018  80  SER   A O   
1759 C  CB  . SER   A 80  ? 0.1336 0.1245 0.1751 -0.0014 0.0143  0.0060  80  SER   A CB  
1760 O  OG  . SER   A 80  ? 0.1580 0.1241 0.2087 0.0053  -0.0039 0.0267  80  SER   A OG  
1766 N  N   . CYS   A 81  ? 0.1116 0.1263 0.1437 0.0004  -0.0048 0.0118  81  CYS   A N   
1767 C  CA  . CYS   A 81  ? 0.1151 0.1342 0.1443 -0.0054 -0.0062 0.0195  81  CYS   A CA  
1768 C  C   . CYS   A 81  ? 0.1173 0.1258 0.1405 -0.0092 -0.0060 0.0249  81  CYS   A C   
1769 O  O   . CYS   A 81  ? 0.1150 0.1558 0.1560 -0.0001 -0.0009 0.0346  81  CYS   A O   
1770 C  CB  . CYS   A 81  ? 0.1207 0.1427 0.1538 -0.0114 -0.0028 0.0229  81  CYS   A CB  
1771 S  SG  . CYS   A 81  ? 0.1354 0.1291 0.1512 -0.0133 0.0015  0.0152  81  CYS   A SG  
1777 N  N   . VAL   A 82  ? 0.1240 0.1332 0.1408 0.0013  -0.0078 0.0201  82  VAL   A N   
1778 C  CA  . VAL   A 82  ? 0.1337 0.1374 0.1480 -0.0004 -0.0086 0.0293  82  VAL   A CA  
1779 C  C   . VAL   A 82  ? 0.1295 0.1389 0.1483 -0.0002 -0.0069 0.0317  82  VAL   A C   
1780 O  O   . VAL   A 82  ? 0.1198 0.1499 0.1761 0.0010  -0.0087 0.0007  82  VAL   A O   
1781 C  CB  . VAL   A 82  ? 0.1643 0.1487 0.1629 0.0009  0.0020  0.0302  82  VAL   A CB  
1782 C  CG1 . VAL   A 82  ? 0.1807 0.1641 0.1852 0.0059  0.0043  0.0276  82  VAL   A CG1 
1783 C  CG2 . VAL   A 82  ? 0.1677 0.1569 0.1885 0.0029  -0.0009 0.0323  82  VAL   A CG2 
1793 N  N   . LEU   A 83  ? 0.1209 0.1389 0.1435 -0.0044 -0.0062 0.0150  83  LEU   A N   
1794 C  CA  . LEU   A 83  ? 0.1237 0.1380 0.1366 -0.0057 -0.0101 0.0065  83  LEU   A CA  
1795 C  C   . LEU   A 83  ? 0.1316 0.1445 0.1301 -0.0061 -0.0130 0.0152  83  LEU   A C   
1796 O  O   . LEU   A 83  ? 0.1411 0.1481 0.1435 -0.0128 -0.0067 0.0193  83  LEU   A O   
1797 C  CB  . LEU   A 83  ? 0.1345 0.1418 0.1475 -0.0098 -0.0066 0.0101  83  LEU   A CB  
1798 C  CG  . LEU   A 83  ? 0.1446 0.1525 0.1449 -0.0136 0.0062  0.0048  83  LEU   A CG  
1799 C  CD1 . LEU   A 83  ? 0.1565 0.1579 0.1587 -0.0219 0.0069  0.0194  83  LEU   A CD1 
1800 C  CD2 . LEU   A 83  ? 0.1479 0.1713 0.1534 -0.0157 0.0150  0.0135  83  LEU   A CD2 
1812 N  N   . SER   A 84  ? 0.1499 0.1521 0.1349 -0.0149 -0.0133 0.0151  84  SER   A N   
1813 C  CA  . SER   A 84  ? 0.1593 0.1564 0.1217 -0.0135 -0.0158 0.0177  84  SER   A CA  
1814 C  C   . SER   A 84  ? 0.1608 0.1530 0.1183 -0.0193 -0.0007 0.0084  84  SER   A C   
1815 O  O   . SER   A 84  ? 0.1522 0.1636 0.1217 -0.0128 -0.0088 0.0122  84  SER   A O   
1816 C  CB  . SER   A 84  ? 0.1646 0.1795 0.1376 -0.0125 -0.0125 0.0058  84  SER   A CB  
1817 O  OG  . SER   A 84  ? 0.1702 0.1995 0.1357 -0.0101 -0.0178 -0.0003 84  SER   A OG  
1823 N  N   . GLY   A 85  ? 0.1741 0.1652 0.1241 -0.0205 0.0064  0.0080  85  GLY   A N   
1824 C  CA  . GLY   A 85  ? 0.1738 0.1739 0.1404 -0.0239 0.0144  0.0039  85  GLY   A CA  
1825 C  C   . GLY   A 85  ? 0.1701 0.1807 0.1199 -0.0178 -0.0017 0.0035  85  GLY   A C   
1826 O  O   . GLY   A 85  ? 0.1684 0.1876 0.1333 -0.0261 0.0062  -0.0107 85  GLY   A O   
1830 N  N   . HIS   A 86  ? 0.1702 0.1719 0.1108 -0.0167 -0.0079 -0.0008 86  HIS   A N   
1831 C  CA  . HIS   A 86  ? 0.1895 0.1795 0.1063 -0.0172 -0.0074 0.0018  86  HIS   A CA  
1832 C  C   . HIS   A 86  ? 0.2095 0.1917 0.1004 -0.0199 -0.0095 0.0006  86  HIS   A C   
1833 O  O   . HIS   A 86  ? 0.2233 0.2141 0.1209 -0.0151 0.0049  0.0021  86  HIS   A O   
1834 C  CB  . HIS   A 86  ? 0.1857 0.1681 0.1236 -0.0130 -0.0036 0.0030  86  HIS   A CB  
1835 C  CG  . HIS   A 86  ? 0.1792 0.1695 0.1182 -0.0059 0.0053  0.0141  86  HIS   A CG  
1836 N  ND1 . HIS   A 86  ? 0.1887 0.1672 0.1626 -0.0164 -0.0000 0.0087  86  HIS   A ND1 
1837 C  CD2 . HIS   A 86  ? 0.1798 0.1637 0.1223 0.0055  0.0072  0.0124  86  HIS   A CD2 
1838 C  CE1 . HIS   A 86  ? 0.1826 0.1662 0.1577 -0.0129 0.0156  0.0136  86  HIS   A CE1 
1839 N  NE2 . HIS   A 86  ? 0.1783 0.1586 0.1397 0.0051  0.0162  0.0255  86  HIS   A NE2 
1847 N  N   . ASN   A 87  ? 0.2216 0.1977 0.1192 -0.0113 0.0109  -0.0047 87  ASN   A N   
1848 C  CA  . ASN   A 87  ? 0.2415 0.2095 0.1262 -0.0075 0.0320  -0.0092 87  ASN   A CA  
1849 C  C   . ASN   A 87  ? 0.2444 0.2246 0.1640 -0.0172 0.0542  -0.0011 87  ASN   A C   
1850 O  O   . ASN   A 87  ? 0.2691 0.2455 0.2061 -0.0323 0.0865  -0.0133 87  ASN   A O   
1851 C  CB  . ASN   A 87  ? 0.2596 0.2140 0.1385 0.0053  0.0303  -0.0084 87  ASN   A CB  
1852 C  CG  . ASN   A 87  ? 0.2774 0.2268 0.1441 0.0137  0.0462  0.0008  87  ASN   A CG  
1853 O  OD1 . ASN   A 87  ? 0.2973 0.2251 0.1512 0.0309  0.0462  0.0096  87  ASN   A OD1 
1854 N  ND2 . ASN   A 87  ? 0.2820 0.2535 0.1577 0.0104  0.0458  0.0057  87  ASN   A ND2 
1861 N  N   . LEU   A 88  ? 0.2131 0.2132 0.1508 -0.0181 0.0303  0.0111  88  LEU   A N   
1862 C  CA  . LEU   A 88  ? 0.1939 0.2113 0.1651 -0.0293 0.0238  0.0257  88  LEU   A CA  
1863 C  C   . LEU   A 88  ? 0.1878 0.2137 0.1488 -0.0268 0.0229  0.0323  88  LEU   A C   
1864 O  O   . LEU   A 88  ? 0.1914 0.2195 0.1868 -0.0255 0.0325  0.0462  88  LEU   A O   
1865 C  CB  . LEU   A 88  ? 0.1971 0.2243 0.1699 -0.0411 -0.0115 0.0406  88  LEU   A CB  
1866 C  CG  . LEU   A 88  ? 0.2132 0.2439 0.2038 -0.0409 -0.0198 0.0471  88  LEU   A CG  
1867 C  CD1 . LEU   A 88  ? 0.2298 0.2510 0.2032 -0.0383 -0.0218 0.0385  88  LEU   A CD1 
1868 C  CD2 . LEU   A 88  ? 0.2280 0.2602 0.2484 -0.0320 -0.0141 0.0357  88  LEU   A CD2 
1880 N  N   . ALA   A 89  ? 0.1864 0.2099 0.1370 -0.0251 0.0200  0.0104  89  ALA   A N   
1881 C  CA  . ALA   A 89  ? 0.1917 0.2046 0.1214 -0.0219 0.0075  0.0191  89  ALA   A CA  
1882 C  C   . ALA   A 89  ? 0.1975 0.2062 0.1288 -0.0139 -0.0050 0.0159  89  ALA   A C   
1883 O  O   . ALA   A 89  ? 0.1930 0.2030 0.1682 -0.0214 -0.0109 -0.0105 89  ALA   A O   
1884 C  CB  . ALA   A 89  ? 0.1862 0.2045 0.1238 -0.0242 0.0057  0.0209  89  ALA   A CB  
1890 N  N   . LYS   A 90  ? 0.2072 0.2177 0.1248 -0.0252 -0.0225 0.0193  90  LYS   A N   
1891 C  CA  . LYS   A 90  ? 0.2155 0.2345 0.1300 -0.0200 -0.0321 0.0236  90  LYS   A CA  
1892 C  C   . LYS   A 90  ? 0.1928 0.2174 0.1297 -0.0255 -0.0298 0.0167  90  LYS   A C   
1893 O  O   . LYS   A 90  ? 0.1966 0.2338 0.1677 -0.0292 -0.0311 0.0096  90  LYS   A O   
1894 C  CB  . LYS   A 90  ? 0.2428 0.2704 0.1621 -0.0159 -0.0471 0.0451  90  LYS   A CB  
1895 C  CG  . LYS   A 90  ? 0.2835 0.3070 0.2667 -0.0126 -0.0443 0.0544  90  LYS   A CG  
1896 C  CD  . LYS   A 90  ? 0.3258 0.3415 0.3694 -0.0138 -0.0283 0.0538  90  LYS   A CD  
1897 C  CE  . LYS   A 90  ? 0.3686 0.3792 0.4503 -0.0156 -0.0168 0.0508  90  LYS   A CE  
1898 N  NZ  . LYS   A 90  ? 0.3905 0.3945 0.5032 -0.0171 -0.0097 0.0500  90  LYS   A NZ  
1912 N  N   . HIS   A 91  ? 0.1804 0.1887 0.1100 -0.0202 -0.0323 0.0209  91  HIS   A N   
1913 C  CA  . HIS   A 91  ? 0.1717 0.1757 0.1129 -0.0096 -0.0271 0.0170  91  HIS   A CA  
1914 C  C   . HIS   A 91  ? 0.1503 0.1571 0.1066 -0.0122 -0.0135 0.0184  91  HIS   A C   
1915 O  O   . HIS   A 91  ? 0.1461 0.1773 0.1225 -0.0228 -0.0029 0.0186  91  HIS   A O   
1916 C  CB  . HIS   A 91  ? 0.1862 0.2040 0.1637 0.0128  -0.0401 0.0186  91  HIS   A CB  
1917 C  CG  . HIS   A 91  ? 0.2281 0.2522 0.2274 0.0226  -0.0672 0.0108  91  HIS   A CG  
1918 N  ND1 . HIS   A 91  ? 0.2386 0.2797 0.2671 0.0289  -0.0717 -0.0044 91  HIS   A ND1 
1919 C  CD2 . HIS   A 91  ? 0.2551 0.2707 0.2525 0.0317  -0.0852 0.0235  91  HIS   A CD2 
1920 C  CE1 . HIS   A 91  ? 0.2518 0.2886 0.2783 0.0347  -0.0750 0.0088  91  HIS   A CE1 
1921 N  NE2 . HIS   A 91  ? 0.2667 0.2863 0.2714 0.0392  -0.0822 0.0193  91  HIS   A NE2 
1929 N  N   . CYS   A 92  ? 0.1378 0.1512 0.1115 -0.0174 -0.0114 0.0187  92  CYS   A N   
1930 C  CA  . CYS   A 92  ? 0.1286 0.1435 0.1227 -0.0151 -0.0074 0.0124  92  CYS   A CA  
1931 C  C   . CYS   A 92  ? 0.1230 0.1402 0.1134 -0.0123 -0.0021 0.0162  92  CYS   A C   
1932 O  O   . CYS   A 92  ? 0.1281 0.1432 0.1350 -0.0199 -0.0054 0.0133  92  CYS   A O   
1933 C  CB  . CYS   A 92  ? 0.1299 0.1459 0.1313 -0.0055 -0.0093 0.0050  92  CYS   A CB  
1934 S  SG  . CYS   A 92  ? 0.1323 0.1343 0.1226 -0.0103 -0.0044 0.0122  92  CYS   A SG  
1940 N  N   . LEU   A 93  ? 0.1209 0.1223 0.1226 -0.0068 0.0069  0.0156  93  LEU   A N   
1941 C  CA  . LEU   A 93  ? 0.1147 0.1230 0.1307 -0.0040 0.0002  0.0139  93  LEU   A CA  
1942 C  C   . LEU   A 93  ? 0.1132 0.1146 0.1253 0.0007  0.0047  0.0105  93  LEU   A C   
1943 O  O   . LEU   A 93  ? 0.1114 0.1213 0.1232 0.0012  0.0021  0.0146  93  LEU   A O   
1944 C  CB  . LEU   A 93  ? 0.1171 0.1211 0.1351 -0.0016 -0.0005 0.0191  93  LEU   A CB  
1945 C  CG  . LEU   A 93  ? 0.1286 0.1218 0.1459 -0.0016 -0.0021 0.0269  93  LEU   A CG  
1946 C  CD1 . LEU   A 93  ? 0.1321 0.1330 0.1779 0.0035  0.0082  0.0190  93  LEU   A CD1 
1947 C  CD2 . LEU   A 93  ? 0.1387 0.1203 0.1563 -0.0051 0.0020  0.0163  93  LEU   A CD2 
1959 N  N   . HIS   A 94  ? 0.1053 0.1137 0.1235 -0.0021 0.0017  0.0183  94  HIS   A N   
1960 C  CA  . HIS   A 94  ? 0.1077 0.1176 0.1243 -0.0011 0.0006  0.0159  94  HIS   A CA  
1961 C  C   . HIS   A 94  ? 0.1078 0.1113 0.1282 -0.0076 0.0032  0.0113  94  HIS   A C   
1962 O  O   . HIS   A 94  ? 0.1107 0.1363 0.1580 0.0012  0.0013  -0.0048 94  HIS   A O   
1963 C  CB  . HIS   A 94  ? 0.1075 0.1125 0.1371 -0.0066 -0.0004 0.0180  94  HIS   A CB  
1964 C  CG  . HIS   A 94  ? 0.1154 0.1105 0.1215 -0.0058 -0.0034 0.0138  94  HIS   A CG  
1965 N  ND1 . HIS   A 94  ? 0.1156 0.1085 0.1307 -0.0017 0.0029  0.0211  94  HIS   A ND1 
1966 C  CD2 . HIS   A 94  ? 0.1210 0.1267 0.1350 0.0001  -0.0011 0.0062  94  HIS   A CD2 
1967 C  CE1 . HIS   A 94  ? 0.1184 0.1174 0.1302 -0.0055 -0.0059 0.0073  94  HIS   A CE1 
1968 N  NE2 . HIS   A 94  ? 0.1213 0.1218 0.1398 -0.0092 -0.0047 0.0067  94  HIS   A NE2 
1976 N  N   . VAL   A 95  ? 0.1059 0.1085 0.1139 -0.0013 0.0070  0.0096  95  VAL   A N   
1977 C  CA  . VAL   A 95  ? 0.1150 0.1145 0.1106 -0.0029 0.0113  0.0108  95  VAL   A CA  
1978 C  C   . VAL   A 95  ? 0.1179 0.1104 0.1010 -0.0092 0.0027  0.0084  95  VAL   A C   
1979 O  O   . VAL   A 95  ? 0.1203 0.1225 0.1222 0.0050  0.0038  0.0056  95  VAL   A O   
1980 C  CB  . VAL   A 95  ? 0.1167 0.1134 0.1318 -0.0102 0.0062  0.0176  95  VAL   A CB  
1981 C  CG1 . VAL   A 95  ? 0.1348 0.1146 0.1336 -0.0109 0.0066  0.0026  95  VAL   A CG1 
1982 C  CG2 . VAL   A 95  ? 0.1192 0.1179 0.1343 -0.0100 0.0077  0.0215  95  VAL   A CG2 
1992 N  N   . VAL   A 96  ? 0.1200 0.1113 0.1024 -0.0021 0.0038  0.0145  96  VAL   A N   
1993 C  CA  . VAL   A 96  ? 0.1313 0.1148 0.1201 -0.0011 0.0046  0.0144  96  VAL   A CA  
1994 C  C   . VAL   A 96  ? 0.1323 0.1207 0.1205 -0.0037 0.0061  0.0192  96  VAL   A C   
1995 O  O   . VAL   A 96  ? 0.1410 0.1221 0.1435 -0.0029 0.0168  0.0049  96  VAL   A O   
1996 C  CB  . VAL   A 96  ? 0.1300 0.1238 0.1268 -0.0022 0.0214  0.0143  96  VAL   A CB  
1997 C  CG1 . VAL   A 96  ? 0.1432 0.1252 0.1232 -0.0014 0.0147  0.0171  96  VAL   A CG1 
1998 C  CG2 . VAL   A 96  ? 0.1354 0.1309 0.1436 -0.0097 0.0206  0.0146  96  VAL   A CG2 
2008 N  N   A GLY   A 97  ? 0.1307 0.1253 0.1284 -0.0063 0.0056  0.0147  97  GLY   A N   
2009 N  N   B GLY   A 97  ? 0.1349 0.1269 0.1274 -0.0047 0.0038  0.0160  97  GLY   A N   
2010 C  CA  A GLY   A 97  ? 0.1379 0.1370 0.1251 -0.0042 -0.0034 0.0137  97  GLY   A CA  
2011 C  CA  B GLY   A 97  ? 0.1430 0.1365 0.1275 -0.0027 -0.0033 0.0161  97  GLY   A CA  
2012 C  C   A GLY   A 97  ? 0.1377 0.1473 0.1193 -0.0062 0.0026  0.0156  97  GLY   A C   
2013 C  C   B GLY   A 97  ? 0.1451 0.1461 0.1233 -0.0039 -0.0011 0.0184  97  GLY   A C   
2014 O  O   A GLY   A 97  ? 0.1430 0.1467 0.1376 -0.0070 0.0040  0.0198  97  GLY   A O   
2015 O  O   B GLY   A 97  ? 0.1488 0.1440 0.1309 -0.0031 -0.0055 0.0282  97  GLY   A O   
2022 N  N   . PRO   A 98  ? 0.1461 0.1515 0.1160 -0.0002 -0.0026 0.0196  98  PRO   A N   
2023 C  CA  . PRO   A 98  ? 0.1642 0.1779 0.1195 -0.0052 -0.0007 0.0192  98  PRO   A CA  
2024 C  C   . PRO   A 98  ? 0.1719 0.1866 0.1185 -0.0164 -0.0113 0.0397  98  PRO   A C   
2025 O  O   . PRO   A 98  ? 0.1627 0.1610 0.1552 -0.0093 -0.0099 0.0304  98  PRO   A O   
2026 C  CB  . PRO   A 98  ? 0.1800 0.1901 0.1138 0.0032  -0.0080 0.0036  98  PRO   A CB  
2027 C  CG  . PRO   A 98  ? 0.1770 0.1747 0.1265 0.0017  -0.0050 -0.0048 98  PRO   A CG  
2028 C  CD  . PRO   A 98  ? 0.1580 0.1530 0.1238 0.0040  -0.0050 0.0070  98  PRO   A CD  
2036 N  N   A ASN   A 99  ? 0.1802 0.2144 0.1286 -0.0175 -0.0090 0.0488  99  ASN   A N   
2037 N  N   B ASN   A 99  ? 0.1990 0.1936 0.1367 -0.0087 -0.0253 0.0570  99  ASN   A N   
2038 C  CA  A ASN   A 99  ? 0.1981 0.2339 0.1200 -0.0220 -0.0061 0.0556  99  ASN   A CA  
2039 C  CA  B ASN   A 99  ? 0.2300 0.1950 0.1487 -0.0025 -0.0331 0.0740  99  ASN   A CA  
2040 C  C   A ASN   A 99  ? 0.2150 0.2608 0.1165 -0.0376 -0.0054 0.0597  99  ASN   A C   
2041 C  C   B ASN   A 99  ? 0.2484 0.2016 0.1541 0.0001  -0.0367 0.0682  99  ASN   A C   
2042 O  O   A ASN   A 99  ? 0.2203 0.2724 0.1232 -0.0311 -0.0043 0.0562  99  ASN   A O   
2043 O  O   B ASN   A 99  ? 0.2486 0.1818 0.1539 0.0062  -0.0437 0.0564  99  ASN   A O   
2044 C  CB  A ASN   A 99  ? 0.1969 0.2266 0.1208 -0.0182 -0.0179 0.0620  99  ASN   A CB  
2045 C  CB  B ASN   A 99  ? 0.2414 0.1926 0.1790 -0.0058 -0.0422 0.0913  99  ASN   A CB  
2046 C  CG  A ASN   A 99  ? 0.1971 0.2256 0.1188 -0.0177 -0.0223 0.0488  99  ASN   A CG  
2047 C  CG  B ASN   A 99  ? 0.2520 0.1960 0.2031 -0.0094 -0.0449 0.1059  99  ASN   A CG  
2048 O  OD1 A ASN   A 99  ? 0.2043 0.2359 0.1130 -0.0072 -0.0205 0.0328  99  ASN   A OD1 
2049 O  OD1 B ASN   A 99  ? 0.2587 0.2076 0.1920 -0.0095 -0.0466 0.1118  99  ASN   A OD1 
2050 N  ND2 A ASN   A 99  ? 0.1966 0.2186 0.1276 -0.0201 -0.0334 0.0647  99  ASN   A ND2 
2051 N  ND2 B ASN   A 99  ? 0.2575 0.1954 0.2246 -0.0035 -0.0506 0.0945  99  ASN   A ND2 
2064 N  N   A VAL   A 100 ? 0.2293 0.2779 0.1242 -0.0532 -0.0338 0.0569  100 VAL   A N   
2065 N  N   B VAL   A 100 ? 0.2635 0.2307 0.1695 -0.0014 -0.0459 0.0695  100 VAL   A N   
2066 C  CA  A VAL   A 100 ? 0.2534 0.2967 0.1428 -0.0590 -0.0391 0.0503  100 VAL   A CA  
2067 C  CA  B VAL   A 100 ? 0.2796 0.2612 0.1966 -0.0042 -0.0456 0.0573  100 VAL   A CA  
2068 C  C   A VAL   A 100 ? 0.2593 0.3035 0.1333 -0.0584 -0.0385 0.0725  100 VAL   A C   
2069 C  C   B VAL   A 100 ? 0.2876 0.2768 0.2010 0.0040  -0.0501 0.0635  100 VAL   A C   
2070 O  O   A VAL   A 100 ? 0.2631 0.3047 0.1460 -0.0542 -0.0141 0.0729  100 VAL   A O   
2071 O  O   B VAL   A 100 ? 0.2881 0.2800 0.2148 0.0052  -0.0454 0.0548  100 VAL   A O   
2072 C  CB  A VAL   A 100 ? 0.2702 0.3025 0.1826 -0.0657 -0.0423 0.0285  100 VAL   A CB  
2073 C  CB  B VAL   A 100 ? 0.2865 0.2712 0.2237 -0.0102 -0.0432 0.0413  100 VAL   A CB  
2074 C  CG1 A VAL   A 100 ? 0.2736 0.3040 0.2039 -0.0690 -0.0391 0.0277  100 VAL   A CG1 
2075 C  CG1 B VAL   A 100 ? 0.2876 0.2729 0.2349 -0.0144 -0.0416 0.0424  100 VAL   A CG1 
2076 C  CG2 A VAL   A 100 ? 0.2765 0.3042 0.1893 -0.0682 -0.0441 0.0119  100 VAL   A CG2 
2077 C  CG2 B VAL   A 100 ? 0.2893 0.2743 0.2361 -0.0123 -0.0403 0.0321  100 VAL   A CG2 
2096 N  N   A ASN   A 101 ? 0.2668 0.3127 0.1541 -0.0588 -0.0366 0.0951  101 ASN   A N   
2097 N  N   B ASN   A 101 ? 0.2966 0.2838 0.2088 0.0070  -0.0495 0.0767  101 ASN   A N   
2098 C  CA  A ASN   A 101 ? 0.2843 0.3195 0.1640 -0.0586 -0.0332 0.1141  101 ASN   A CA  
2099 C  CA  B ASN   A 101 ? 0.3083 0.2875 0.2224 0.0106  -0.0391 0.0864  101 ASN   A CA  
2100 C  C   A ASN   A 101 ? 0.3118 0.3443 0.1926 -0.0587 -0.0092 0.1332  101 ASN   A C   
2101 C  C   B ASN   A 101 ? 0.3219 0.2978 0.2366 0.0129  -0.0160 0.1061  101 ASN   A C   
2102 O  O   A ASN   A 101 ? 0.3220 0.3489 0.2327 -0.0594 -0.0125 0.1164  101 ASN   A O   
2103 O  O   B ASN   A 101 ? 0.3284 0.2991 0.2357 0.0123  -0.0135 0.1148  101 ASN   A O   
2104 C  CB  A ASN   A 101 ? 0.2763 0.3020 0.1590 -0.0559 -0.0546 0.1046  101 ASN   A CB  
2105 C  CB  B ASN   A 101 ? 0.3062 0.2812 0.2272 0.0086  -0.0416 0.0693  101 ASN   A CB  
2106 C  CG  A ASN   A 101 ? 0.2671 0.2906 0.1522 -0.0505 -0.0721 0.0731  101 ASN   A CG  
2107 C  CG  B ASN   A 101 ? 0.3050 0.2786 0.2432 0.0080  -0.0475 0.0516  101 ASN   A CG  
2108 O  OD1 A ASN   A 101 ? 0.2612 0.2945 0.1712 -0.0367 -0.0713 0.0375  101 ASN   A OD1 
2109 O  OD1 B ASN   A 101 ? 0.3091 0.2818 0.2567 0.0041  -0.0440 0.0451  101 ASN   A OD1 
2110 N  ND2 A ASN   A 101 ? 0.2674 0.2816 0.1456 -0.0591 -0.0701 0.0708  101 ASN   A ND2 
2111 N  ND2 B ASN   A 101 ? 0.3039 0.2745 0.2499 0.0104  -0.0474 0.0398  101 ASN   A ND2 
2124 N  N   A LYS   A 102 ? 0.3257 0.3675 0.2264 -0.0595 0.0094  0.1394  102 LYS   A N   
2125 N  N   B LYS   A 102 ? 0.3282 0.3083 0.2685 0.0125  0.0053  0.1042  102 LYS   A N   
2126 C  CA  A LYS   A 102 ? 0.3435 0.3877 0.2433 -0.0576 0.0069  0.1358  102 LYS   A CA  
2127 C  CA  B LYS   A 102 ? 0.3357 0.3177 0.2764 0.0076  0.0165  0.1014  102 LYS   A CA  
2128 C  C   A LYS   A 102 ? 0.3516 0.4049 0.2251 -0.0420 0.0026  0.1308  102 LYS   A C   
2129 C  C   B LYS   A 102 ? 0.3360 0.3163 0.2645 0.0116  0.0140  0.1128  102 LYS   A C   
2130 O  O   A LYS   A 102 ? 0.3540 0.4157 0.2342 -0.0370 0.0045  0.1230  102 LYS   A O   
2131 O  O   B LYS   A 102 ? 0.3376 0.3125 0.2543 0.0126  0.0247  0.1286  102 LYS   A O   
2132 C  CB  A LYS   A 102 ? 0.3562 0.3928 0.2863 -0.0686 -0.0043 0.1189  102 LYS   A CB  
2133 C  CB  B LYS   A 102 ? 0.3434 0.3289 0.2982 0.0023  0.0169  0.0856  102 LYS   A CB  
2134 C  CG  A LYS   A 102 ? 0.3685 0.3959 0.3182 -0.0782 -0.0160 0.1035  102 LYS   A CG  
2135 C  CG  B LYS   A 102 ? 0.3499 0.3386 0.3097 -0.0035 0.0163  0.0748  102 LYS   A CG  
2136 C  CD  A LYS   A 102 ? 0.3815 0.3996 0.3483 -0.0841 -0.0229 0.0844  102 LYS   A CD  
2137 C  CD  B LYS   A 102 ? 0.3567 0.3485 0.3188 -0.0063 0.0157  0.0632  102 LYS   A CD  
2138 C  CE  A LYS   A 102 ? 0.3906 0.3999 0.3748 -0.0883 -0.0267 0.0736  102 LYS   A CE  
2139 C  CE  B LYS   A 102 ? 0.3621 0.3559 0.3305 -0.0074 0.0143  0.0566  102 LYS   A CE  
2140 N  NZ  A LYS   A 102 ? 0.3951 0.3995 0.3863 -0.0916 -0.0293 0.0684  102 LYS   A NZ  
2141 N  NZ  B LYS   A 102 ? 0.3647 0.3594 0.3336 -0.0070 0.0155  0.0538  102 LYS   A NZ  
2168 N  N   A GLY   A 103 ? 0.3566 0.4147 0.2410 -0.0290 -0.0068 0.1047  103 GLY   A N   
2169 N  N   B GLY   A 103 ? 0.3325 0.3192 0.2557 0.0165  -0.0055 0.1053  103 GLY   A N   
2170 C  CA  A GLY   A 103 ? 0.3586 0.4188 0.2357 -0.0176 -0.0049 0.0843  103 GLY   A CA  
2171 C  CA  B GLY   A 103 ? 0.3277 0.3164 0.2343 0.0178  -0.0159 0.1071  103 GLY   A CA  
2172 C  C   A GLY   A 103 ? 0.3545 0.4210 0.2400 -0.0097 0.0043  0.0656  103 GLY   A C   
2173 C  C   B GLY   A 103 ? 0.3165 0.3106 0.2051 0.0174  -0.0194 0.1011  103 GLY   A C   
2174 O  O   A GLY   A 103 ? 0.3604 0.4269 0.2621 -0.0050 0.0046  0.0556  103 GLY   A O   
2175 O  O   B GLY   A 103 ? 0.3247 0.3161 0.2024 0.0180  -0.0213 0.1067  103 GLY   A O   
2182 N  N   A GLU   A 104 ? 0.3401 0.4128 0.2108 -0.0109 0.0171  0.0567  104 GLU   A N   
2183 N  N   B GLU   A 104 ? 0.2936 0.2969 0.1794 0.0155  -0.0260 0.0881  104 GLU   A N   
2184 C  CA  A GLU   A 104 ? 0.3227 0.4025 0.1821 -0.0171 0.0252  0.0499  104 GLU   A CA  
2185 C  CA  B GLU   A 104 ? 0.2713 0.2816 0.1523 0.0097  -0.0327 0.0715  104 GLU   A CA  
2186 C  C   A GLU   A 104 ? 0.3219 0.4134 0.1796 -0.0149 0.0171  0.0238  104 GLU   A C   
2187 C  C   B GLU   A 104 ? 0.2698 0.2777 0.1660 0.0168  -0.0285 0.0456  104 GLU   A C   
2188 O  O   A GLU   A 104 ? 0.3204 0.4184 0.1951 -0.0137 -0.0014 0.0196  104 GLU   A O   
2189 O  O   B GLU   A 104 ? 0.2672 0.2701 0.1904 0.0210  -0.0301 0.0455  104 GLU   A O   
2190 C  CB  A GLU   A 104 ? 0.3025 0.3828 0.1795 -0.0254 0.0421  0.0723  104 GLU   A CB  
2191 C  CB  B GLU   A 104 ? 0.2537 0.2746 0.1515 -0.0044 -0.0339 0.0744  104 GLU   A CB  
2192 C  CG  A GLU   A 104 ? 0.2878 0.3651 0.1929 -0.0314 0.0510  0.0846  104 GLU   A CG  
2193 C  CG  B GLU   A 104 ? 0.2417 0.2742 0.1737 -0.0170 -0.0390 0.0696  104 GLU   A CG  
2194 C  CD  A GLU   A 104 ? 0.2740 0.3457 0.1892 -0.0343 0.0612  0.1000  104 GLU   A CD  
2195 C  CD  B GLU   A 104 ? 0.2296 0.2717 0.1816 -0.0235 -0.0486 0.0672  104 GLU   A CD  
2196 O  OE1 A GLU   A 104 ? 0.2587 0.3299 0.1662 -0.0334 0.0621  0.0942  104 GLU   A OE1 
2197 O  OE1 B GLU   A 104 ? 0.2159 0.2700 0.1686 -0.0249 -0.0630 0.0618  104 GLU   A OE1 
2198 O  OE2 A GLU   A 104 ? 0.2841 0.3442 0.2072 -0.0373 0.0558  0.1144  104 GLU   A OE2 
2199 O  OE2 B GLU   A 104 ? 0.2388 0.2713 0.2059 -0.0287 -0.0371 0.0637  104 GLU   A OE2 
2212 N  N   A ASP   A 105 ? 0.3221 0.4183 0.1816 -0.0135 0.0236  -0.0026 105 ASP   A N   
2213 N  N   B ASP   A 105 ? 0.2765 0.2817 0.1752 0.0185  -0.0225 0.0215  105 ASP   A N   
2214 C  CA  A ASP   A 105 ? 0.3178 0.4242 0.2056 -0.0119 0.0269  -0.0270 105 ASP   A CA  
2215 C  CA  B ASP   A 105 ? 0.2792 0.2876 0.2008 0.0226  -0.0114 -0.0099 105 ASP   A CA  
2216 C  C   A ASP   A 105 ? 0.2836 0.4093 0.1647 -0.0249 0.0130  -0.0418 105 ASP   A C   
2217 C  C   B ASP   A 105 ? 0.2730 0.2840 0.1872 0.0141  -0.0059 -0.0136 105 ASP   A C   
2218 O  O   A ASP   A 105 ? 0.2671 0.4067 0.1176 -0.0253 0.0123  -0.0564 105 ASP   A O   
2219 O  O   B ASP   A 105 ? 0.2629 0.2813 0.1582 0.0145  -0.0012 -0.0159 105 ASP   A O   
2220 C  CB  A ASP   A 105 ? 0.3417 0.4429 0.2760 0.0009  0.0404  -0.0337 105 ASP   A CB  
2221 C  CB  B ASP   A 105 ? 0.2860 0.2990 0.2435 0.0330  -0.0052 -0.0341 105 ASP   A CB  
2222 C  CG  A ASP   A 105 ? 0.3595 0.4593 0.3387 0.0110  0.0433  -0.0401 105 ASP   A CG  
2223 C  CG  B ASP   A 105 ? 0.2900 0.3079 0.2794 0.0430  -0.0044 -0.0589 105 ASP   A CG  
2224 O  OD1 A ASP   A 105 ? 0.3622 0.4667 0.3527 0.0158  0.0398  -0.0474 105 ASP   A OD1 
2225 O  OD1 B ASP   A 105 ? 0.2899 0.3094 0.2756 0.0435  -0.0084 -0.0764 105 ASP   A OD1 
2226 O  OD2 A ASP   A 105 ? 0.3711 0.4654 0.3710 0.0112  0.0459  -0.0363 105 ASP   A OD2 
2227 O  OD2 B ASP   A 105 ? 0.2958 0.3135 0.3100 0.0449  -0.0083 -0.0581 105 ASP   A OD2 
2236 N  N   A ILE   A 106 ? 0.2647 0.3967 0.1853 -0.0386 -0.0088 -0.0453 106 ILE   A N   
2237 N  N   B ILE   A 106 ? 0.2741 0.2823 0.1991 0.0074  -0.0136 -0.0131 106 ILE   A N   
2238 C  CA  A ILE   A 106 ? 0.2398 0.3768 0.2129 -0.0525 -0.0310 -0.0633 106 ILE   A CA  
2239 C  CA  B ILE   A 106 ? 0.2725 0.2798 0.2192 -0.0018 -0.0229 -0.0168 106 ILE   A CA  
2240 C  C   A ILE   A 106 ? 0.2211 0.3469 0.2170 -0.0749 -0.0371 -0.0870 106 ILE   A C   
2241 C  C   B ILE   A 106 ? 0.2704 0.2657 0.2133 -0.0069 -0.0195 -0.0071 106 ILE   A C   
2242 O  O   A ILE   A 106 ? 0.1992 0.3343 0.2206 -0.0866 -0.0234 -0.0866 106 ILE   A O   
2243 O  O   B ILE   A 106 ? 0.2643 0.2638 0.2109 -0.0107 -0.0165 -0.0055 106 ILE   A O   
2244 C  CB  A ILE   A 106 ? 0.2402 0.3874 0.2532 -0.0366 -0.0463 -0.0433 106 ILE   A CB  
2245 C  CB  B ILE   A 106 ? 0.2749 0.2938 0.2523 -0.0024 -0.0355 -0.0182 106 ILE   A CB  
2246 C  CG1 A ILE   A 106 ? 0.2328 0.3899 0.2817 -0.0210 -0.0546 -0.0234 106 ILE   A CG1 
2247 C  CG1 B ILE   A 106 ? 0.2731 0.3019 0.2725 0.0029  -0.0403 -0.0116 106 ILE   A CG1 
2248 C  CG2 A ILE   A 106 ? 0.2456 0.3906 0.2653 -0.0343 -0.0504 -0.0412 106 ILE   A CG2 
2249 C  CG2 B ILE   A 106 ? 0.2774 0.2962 0.2616 -0.0048 -0.0382 -0.0203 106 ILE   A CG2 
2250 C  CD1 A ILE   A 106 ? 0.2306 0.3895 0.2950 -0.0077 -0.0517 -0.0101 106 ILE   A CD1 
2251 C  CD1 B ILE   A 106 ? 0.2725 0.3045 0.2819 0.0092  -0.0378 -0.0077 106 ILE   A CD1 
2274 N  N   A GLN   A 107 ? 0.2361 0.3313 0.2462 -0.0730 -0.0305 -0.0983 107 GLN   A N   
2275 N  N   B GLN   A 107 ? 0.2745 0.2512 0.2251 -0.0050 -0.0177 0.0023  107 GLN   A N   
2276 C  CA  A GLN   A 107 ? 0.2547 0.3138 0.3104 -0.0598 -0.0096 -0.0886 107 GLN   A CA  
2277 C  CA  B GLN   A 107 ? 0.2818 0.2432 0.2634 -0.0077 -0.0132 0.0087  107 GLN   A CA  
2278 C  C   A GLN   A 107 ? 0.2259 0.2647 0.2878 -0.0526 0.0180  -0.0689 107 GLN   A C   
2279 C  C   B GLN   A 107 ? 0.2569 0.2075 0.2392 -0.0083 -0.0000 0.0206  107 GLN   A C   
2280 O  O   A GLN   A 107 ? 0.2364 0.2638 0.3444 -0.0449 0.0382  -0.0696 107 GLN   A O   
2281 O  O   B GLN   A 107 ? 0.2623 0.2003 0.2521 -0.0098 -0.0049 0.0180  107 GLN   A O   
2282 C  CB  A GLN   A 107 ? 0.2975 0.3434 0.4061 -0.0573 -0.0189 -0.0861 107 GLN   A CB  
2283 C  CB  B GLN   A 107 ? 0.3105 0.2735 0.3291 -0.0133 -0.0243 0.0078  107 GLN   A CB  
2284 C  CG  A GLN   A 107 ? 0.3381 0.3726 0.5055 -0.0497 -0.0278 -0.0750 107 GLN   A CG  
2285 C  CG  B GLN   A 107 ? 0.3364 0.3002 0.3947 -0.0144 -0.0381 0.0150  107 GLN   A CG  
2286 C  CD  A GLN   A 107 ? 0.3709 0.3935 0.5905 -0.0437 -0.0354 -0.0621 107 GLN   A CD  
2287 C  CD  B GLN   A 107 ? 0.3581 0.3225 0.4540 -0.0140 -0.0483 0.0235  107 GLN   A CD  
2288 O  OE1 A GLN   A 107 ? 0.3832 0.4010 0.6253 -0.0429 -0.0389 -0.0571 107 GLN   A OE1 
2289 O  OE1 B GLN   A 107 ? 0.3677 0.3306 0.4725 -0.0138 -0.0511 0.0281  107 GLN   A OE1 
2290 N  NE2 A GLN   A 107 ? 0.3803 0.4005 0.6186 -0.0408 -0.0380 -0.0594 107 GLN   A NE2 
2291 N  NE2 B GLN   A 107 ? 0.3624 0.3296 0.4739 -0.0133 -0.0552 0.0280  107 GLN   A NE2 
2308 N  N   A LEU   A 108 ? 0.1905 0.2158 0.2116 -0.0500 0.0216  -0.0611 108 LEU   A N   
2309 N  N   B LEU   A 108 ? 0.2286 0.1859 0.2033 -0.0126 0.0142  0.0176  108 LEU   A N   
2310 C  CA  A LEU   A 108 ? 0.1755 0.1812 0.1853 -0.0224 0.0223  -0.0265 108 LEU   A CA  
2311 C  CA  B LEU   A 108 ? 0.2052 0.1702 0.1877 -0.0071 0.0211  0.0106  108 LEU   A CA  
2312 C  C   A LEU   A 108 ? 0.1579 0.1457 0.1758 -0.0080 0.0209  0.0007  108 LEU   A C   
2313 C  C   B LEU   A 108 ? 0.1780 0.1476 0.1763 0.0003  0.0217  0.0144  108 LEU   A C   
2314 O  O   A LEU   A 108 ? 0.1493 0.1469 0.1908 -0.0060 0.0261  0.0020  108 LEU   A O   
2315 O  O   B LEU   A 108 ? 0.1765 0.1506 0.1856 0.0035  0.0296  0.0096  108 LEU   A O   
2316 C  CB  A LEU   A 108 ? 0.1831 0.1933 0.1663 -0.0225 0.0272  -0.0149 108 LEU   A CB  
2317 C  CB  B LEU   A 108 ? 0.2119 0.1844 0.1798 -0.0157 0.0274  0.0026  108 LEU   A CB  
2318 C  CG  A LEU   A 108 ? 0.1971 0.2119 0.1989 -0.0204 0.0344  -0.0174 108 LEU   A CG  
2319 C  CG  B LEU   A 108 ? 0.2225 0.2019 0.2005 -0.0208 0.0318  -0.0123 108 LEU   A CG  
2320 C  CD1 A LEU   A 108 ? 0.2109 0.2170 0.2009 -0.0278 0.0435  -0.0141 108 LEU   A CD1 
2321 C  CD1 B LEU   A 108 ? 0.2292 0.2077 0.2032 -0.0272 0.0389  -0.0113 108 LEU   A CD1 
2322 C  CD2 A LEU   A 108 ? 0.1991 0.2263 0.2320 -0.0150 0.0246  -0.0191 108 LEU   A CD2 
2323 C  CD2 B LEU   A 108 ? 0.2264 0.2122 0.2227 -0.0208 0.0272  -0.0201 108 LEU   A CD2 
2346 N  N   . LEU   A 109 ? 0.1568 0.1423 0.1756 0.0039  0.0160  0.0190  109 LEU   A N   
2347 C  CA  . LEU   A 109 ? 0.1478 0.1320 0.1667 -0.0009 0.0043  0.0177  109 LEU   A CA  
2348 C  C   . LEU   A 109 ? 0.1364 0.1282 0.1608 -0.0104 0.0070  0.0121  109 LEU   A C   
2349 O  O   . LEU   A 109 ? 0.1448 0.1226 0.1764 -0.0047 -0.0029 0.0079  109 LEU   A O   
2350 C  CB  . LEU   A 109 ? 0.1494 0.1394 0.1917 0.0140  0.0000  0.0326  109 LEU   A CB  
2351 C  CG  . LEU   A 109 ? 0.1400 0.1463 0.2013 0.0093  0.0081  0.0353  109 LEU   A CG  
2352 C  CD1 . LEU   A 109 ? 0.1453 0.1396 0.2087 0.0050  0.0116  0.0179  109 LEU   A CD1 
2353 C  CD2 . LEU   A 109 ? 0.1413 0.1697 0.2177 0.0060  0.0060  0.0374  109 LEU   A CD2 
2366 N  N   . LYS   A 110 ? 0.1378 0.1283 0.1485 -0.0058 -0.0004 0.0006  110 LYS   A N   
2367 C  CA  . LYS   A 110 ? 0.1309 0.1229 0.1624 -0.0042 -0.0002 0.0052  110 LYS   A CA  
2368 C  C   . LYS   A 110 ? 0.1334 0.1171 0.1504 -0.0060 0.0099  -0.0008 110 LYS   A C   
2369 O  O   . LYS   A 110 ? 0.1282 0.1178 0.1651 -0.0080 0.0071  -0.0011 110 LYS   A O   
2370 C  CB  . LYS   A 110 ? 0.1377 0.1287 0.1812 -0.0070 -0.0115 -0.0019 110 LYS   A CB  
2371 C  CG  . LYS   A 110 ? 0.1379 0.1295 0.1942 -0.0017 -0.0083 -0.0027 110 LYS   A CG  
2372 C  CD  . LYS   A 110 ? 0.1413 0.1311 0.2053 -0.0072 -0.0105 -0.0116 110 LYS   A CD  
2373 C  CE  . LYS   A 110 ? 0.1516 0.1419 0.2254 -0.0071 0.0127  -0.0075 110 LYS   A CE  
2374 N  NZ  . LYS   A 110 ? 0.1501 0.1425 0.2326 -0.0104 0.0229  -0.0004 110 LYS   A NZ  
2388 N  N   . SER   A 111 ? 0.1334 0.1213 0.1509 -0.0009 0.0001  0.0086  111 SER   A N   
2389 C  CA  . SER   A 111 ? 0.1252 0.1281 0.1552 0.0010  0.0056  0.0032  111 SER   A CA  
2390 C  C   . SER   A 111 ? 0.1224 0.1216 0.1413 -0.0093 0.0078  0.0036  111 SER   A C   
2391 O  O   . SER   A 111 ? 0.1336 0.1151 0.1676 -0.0036 0.0083  0.0035  111 SER   A O   
2392 C  CB  . SER   A 111 ? 0.1479 0.1458 0.1627 -0.0039 0.0142  -0.0146 111 SER   A CB  
2393 O  OG  . SER   A 111 ? 0.1903 0.1666 0.1774 0.0002  0.0334  -0.0140 111 SER   A OG  
2399 N  N   . ALA   A 112 ? 0.1307 0.1112 0.1548 -0.0017 0.0123  0.0090  112 ALA   A N   
2400 C  CA  . ALA   A 112 ? 0.1321 0.1153 0.1541 -0.0042 0.0151  0.0027  112 ALA   A CA  
2401 C  C   . ALA   A 112 ? 0.1241 0.1130 0.1480 0.0031  0.0094  0.0088  112 ALA   A C   
2402 O  O   . ALA   A 112 ? 0.1273 0.1084 0.1614 -0.0088 0.0140  0.0130  112 ALA   A O   
2403 C  CB  . ALA   A 112 ? 0.1399 0.1177 0.1627 -0.0026 0.0142  0.0096  112 ALA   A CB  
2409 N  N   . TYR   A 113 ? 0.1131 0.1164 0.1514 -0.0017 0.0104  0.0128  113 TYR   A N   
2410 C  CA  . TYR   A 113 ? 0.1129 0.1145 0.1522 -0.0050 0.0093  0.0123  113 TYR   A CA  
2411 C  C   . TYR   A 113 ? 0.1088 0.1127 0.1479 -0.0083 0.0066  0.0106  113 TYR   A C   
2412 O  O   . TYR   A 113 ? 0.1165 0.1154 0.1576 -0.0037 0.0132  0.0112  113 TYR   A O   
2413 C  CB  . TYR   A 113 ? 0.1153 0.1216 0.1626 -0.0014 0.0040  0.0189  113 TYR   A CB  
2414 C  CG  . TYR   A 113 ? 0.1152 0.1218 0.1523 -0.0036 0.0092  0.0241  113 TYR   A CG  
2415 C  CD1 . TYR   A 113 ? 0.1232 0.1300 0.1443 0.0038  0.0096  0.0208  113 TYR   A CD1 
2416 C  CD2 . TYR   A 113 ? 0.1210 0.1256 0.1569 -0.0046 0.0062  0.0263  113 TYR   A CD2 
2417 C  CE1 . TYR   A 113 ? 0.1271 0.1331 0.1533 -0.0033 0.0082  0.0208  113 TYR   A CE1 
2418 C  CE2 . TYR   A 113 ? 0.1258 0.1377 0.1589 -0.0061 0.0016  0.0266  113 TYR   A CE2 
2419 C  CZ  . TYR   A 113 ? 0.1249 0.1376 0.1554 0.0041  0.0087  0.0281  113 TYR   A CZ  
2420 O  OH  . TYR   A 113 ? 0.1204 0.1488 0.1732 0.0096  0.0049  0.0271  113 TYR   A OH  
2430 N  N   . GLU   A 114 ? 0.1170 0.1095 0.1646 -0.0058 0.0149  0.0110  114 GLU   A N   
2431 C  CA  . GLU   A 114 ? 0.1170 0.1027 0.1684 0.0045  0.0096  0.0168  114 GLU   A CA  
2432 C  C   . GLU   A 114 ? 0.1131 0.1132 0.1640 0.0045  0.0139  0.0132  114 GLU   A C   
2433 O  O   . GLU   A 114 ? 0.1259 0.1168 0.1539 0.0007  0.0056  0.0121  114 GLU   A O   
2434 C  CB  . GLU   A 114 ? 0.1186 0.1120 0.1672 -0.0050 0.0077  0.0144  114 GLU   A CB  
2435 C  CG  . GLU   A 114 ? 0.1251 0.1164 0.1774 -0.0010 0.0158  0.0043  114 GLU   A CG  
2436 C  CD  . GLU   A 114 ? 0.1325 0.1156 0.1764 -0.0025 0.0053  0.0098  114 GLU   A CD  
2437 O  OE1 . GLU   A 114 ? 0.1356 0.1171 0.1829 -0.0069 0.0167  -0.0032 114 GLU   A OE1 
2438 O  OE2 . GLU   A 114 ? 0.1557 0.1216 0.1993 -0.0109 0.0041  -0.0135 114 GLU   A OE2 
2445 N  N   . ASN   A 115 ? 0.1130 0.1136 0.1526 -0.0046 0.0086  0.0099  115 ASN   A N   
2446 C  CA  . ASN   A 115 ? 0.1181 0.1163 0.1599 -0.0093 0.0131  0.0149  115 ASN   A CA  
2447 C  C   . ASN   A 115 ? 0.1182 0.1084 0.1525 -0.0108 0.0046  0.0080  115 ASN   A C   
2448 O  O   . ASN   A 115 ? 0.1230 0.1293 0.1484 -0.0087 0.0090  0.0199  115 ASN   A O   
2449 C  CB  . ASN   A 115 ? 0.1276 0.1274 0.1586 -0.0110 0.0152  0.0100  115 ASN   A CB  
2450 C  CG  . ASN   A 115 ? 0.1263 0.1427 0.1642 -0.0132 0.0192  0.0107  115 ASN   A CG  
2451 O  OD1 . ASN   A 115 ? 0.1300 0.2376 0.1928 -0.0139 0.0268  0.0332  115 ASN   A OD1 
2452 N  ND2 . ASN   A 115 ? 0.1330 0.1250 0.1583 -0.0106 0.0262  0.0196  115 ASN   A ND2 
2459 N  N   . PHE   A 116 ? 0.1140 0.1164 0.1580 -0.0002 0.0125  0.0175  116 PHE   A N   
2460 C  CA  . PHE   A 116 ? 0.1130 0.1223 0.1477 0.0012  0.0140  0.0177  116 PHE   A CA  
2461 C  C   . PHE   A 116 ? 0.1125 0.1294 0.1486 -0.0061 0.0090  0.0178  116 PHE   A C   
2462 O  O   . PHE   A 116 ? 0.1222 0.1320 0.1587 0.0061  0.0114  0.0241  116 PHE   A O   
2463 C  CB  . PHE   A 116 ? 0.1170 0.1178 0.1590 0.0005  0.0118  0.0140  116 PHE   A CB  
2464 C  CG  . PHE   A 116 ? 0.1185 0.1201 0.1478 -0.0017 0.0087  0.0119  116 PHE   A CG  
2465 C  CD1 . PHE   A 116 ? 0.1201 0.1116 0.1544 -0.0101 0.0152  0.0202  116 PHE   A CD1 
2466 C  CD2 . PHE   A 116 ? 0.1263 0.1268 0.1560 -0.0034 0.0163  0.0193  116 PHE   A CD2 
2467 C  CE1 . PHE   A 116 ? 0.1268 0.1117 0.1715 -0.0146 0.0136  0.0141  116 PHE   A CE1 
2468 C  CE2 . PHE   A 116 ? 0.1260 0.1235 0.1697 0.0021  0.0191  0.0130  116 PHE   A CE2 
2469 C  CZ  . PHE   A 116 ? 0.1284 0.1050 0.1648 -0.0011 0.0065  0.0155  116 PHE   A CZ  
2479 N  N   . ASN   A 117 ? 0.1165 0.1221 0.1596 -0.0035 0.0134  0.0168  117 ASN   A N   
2480 C  CA  . ASN   A 117 ? 0.1171 0.1170 0.1688 -0.0027 0.0089  0.0222  117 ASN   A CA  
2481 C  C   . ASN   A 117 ? 0.1176 0.1239 0.1746 0.0029  0.0131  0.0197  117 ASN   A C   
2482 O  O   . ASN   A 117 ? 0.1277 0.1327 0.1971 -0.0046 -0.0089 0.0367  117 ASN   A O   
2483 C  CB  . ASN   A 117 ? 0.1201 0.1257 0.1668 -0.0007 0.0128  0.0265  117 ASN   A CB  
2484 C  CG  . ASN   A 117 ? 0.1181 0.1228 0.1716 -0.0014 0.0082  0.0297  117 ASN   A CG  
2485 O  OD1 . ASN   A 117 ? 0.1183 0.1444 0.1851 -0.0124 0.0167  0.0145  117 ASN   A OD1 
2486 N  ND2 . ASN   A 117 ? 0.1150 0.1256 0.1749 -0.0016 0.0106  0.0246  117 ASN   A ND2 
2493 N  N   . GLN   A 118 ? 0.1172 0.1282 0.1761 -0.0027 -0.0009 0.0244  118 GLN   A N   
2494 C  CA  . GLN   A 118 ? 0.1256 0.1411 0.1789 -0.0033 -0.0026 0.0229  118 GLN   A CA  
2495 C  C   . GLN   A 118 ? 0.1280 0.1501 0.1652 -0.0052 -0.0035 0.0291  118 GLN   A C   
2496 O  O   . GLN   A 118 ? 0.1266 0.1773 0.1922 0.0007  -0.0106 0.0048  118 GLN   A O   
2497 C  CB  . GLN   A 118 ? 0.1253 0.1463 0.1970 -0.0012 0.0103  0.0284  118 GLN   A CB  
2498 C  CG  . GLN   A 118 ? 0.1187 0.1459 0.1943 -0.0010 0.0073  0.0339  118 GLN   A CG  
2499 C  CD  . GLN   A 118 ? 0.1153 0.1454 0.2070 -0.0010 0.0123  0.0282  118 GLN   A CD  
2500 O  OE1 . GLN   A 118 ? 0.1217 0.1604 0.2242 0.0110  0.0026  0.0171  118 GLN   A OE1 
2501 N  NE2 . GLN   A 118 ? 0.1242 0.1403 0.2118 0.0037  0.0069  0.0288  118 GLN   A NE2 
2510 N  N   . HIS   A 119 ? 0.1276 0.1454 0.1583 0.0006  0.0018  0.0292  119 HIS   A N   
2511 C  CA  . HIS   A 119 ? 0.1379 0.1508 0.1663 -0.0047 0.0011  0.0334  119 HIS   A CA  
2512 C  C   . HIS   A 119 ? 0.1473 0.1543 0.1578 -0.0044 0.0048  0.0324  119 HIS   A C   
2513 O  O   . HIS   A 119 ? 0.1486 0.1633 0.1681 -0.0206 -0.0007 0.0358  119 HIS   A O   
2514 C  CB  . HIS   A 119 ? 0.1416 0.1503 0.1745 -0.0051 0.0188  0.0334  119 HIS   A CB  
2515 C  CG  . HIS   A 119 ? 0.1407 0.1532 0.2238 0.0036  0.0163  0.0421  119 HIS   A CG  
2516 N  ND1 . HIS   A 119 ? 0.1532 0.1753 0.2952 -0.0070 0.0091  0.0328  119 HIS   A ND1 
2517 C  CD2 . HIS   A 119 ? 0.1522 0.1643 0.2512 0.0178  0.0343  0.0604  119 HIS   A CD2 
2518 C  CE1 . HIS   A 119 ? 0.1531 0.1736 0.3073 -0.0105 0.0235  0.0525  119 HIS   A CE1 
2519 N  NE2 . HIS   A 119 ? 0.1606 0.1675 0.2897 0.0062  0.0411  0.0746  119 HIS   A NE2 
2527 N  N   . GLU   A 120 ? 0.1455 0.1806 0.1597 0.0035  -0.0011 0.0540  120 GLU   A N   
2528 C  CA  . GLU   A 120 ? 0.1678 0.2125 0.1899 0.0136  -0.0003 0.0905  120 GLU   A CA  
2529 C  C   . GLU   A 120 ? 0.1504 0.1953 0.1627 -0.0027 0.0030  0.0802  120 GLU   A C   
2530 O  O   . GLU   A 120 ? 0.1541 0.1886 0.1743 -0.0071 0.0015  0.0792  120 GLU   A O   
2531 C  CB  . GLU   A 120 ? 0.2309 0.2783 0.2428 0.0343  0.0038  0.1418  120 GLU   A CB  
2532 C  CG  . GLU   A 120 ? 0.3298 0.3568 0.3623 0.0465  0.0098  0.1545  120 GLU   A CG  
2533 C  CD  . GLU   A 120 ? 0.4318 0.4335 0.4906 0.0522  0.0256  0.1483  120 GLU   A CD  
2534 O  OE1 . GLU   A 120 ? 0.4521 0.4433 0.5226 0.0518  0.0296  0.1453  120 GLU   A OE1 
2535 O  OE2 . GLU   A 120 ? 0.4700 0.4705 0.5454 0.0536  0.0322  0.1456  120 GLU   A OE2 
2542 N  N   . VAL   A 121 ? 0.1474 0.1911 0.1424 -0.0029 0.0055  0.0587  121 VAL   A N   
2543 C  CA  . VAL   A 121 ? 0.1589 0.1947 0.1363 -0.0084 0.0167  0.0559  121 VAL   A CA  
2544 C  C   . VAL   A 121 ? 0.1473 0.1727 0.1241 -0.0164 0.0059  0.0435  121 VAL   A C   
2545 O  O   . VAL   A 121 ? 0.1501 0.1760 0.1434 -0.0209 -0.0077 0.0328  121 VAL   A O   
2546 C  CB  . VAL   A 121 ? 0.2015 0.2357 0.1805 0.0071  0.0319  0.0696  121 VAL   A CB  
2547 C  CG1 . VAL   A 121 ? 0.2075 0.2507 0.1798 0.0154  0.0393  0.0806  121 VAL   A CG1 
2548 C  CG2 . VAL   A 121 ? 0.2239 0.2553 0.2194 0.0020  0.0293  0.0523  121 VAL   A CG2 
2558 N  N   . LEU   A 122 ? 0.1374 0.1520 0.1398 -0.0139 0.0057  0.0426  122 LEU   A N   
2559 C  CA  . LEU   A 122 ? 0.1442 0.1413 0.1417 -0.0161 0.0203  0.0334  122 LEU   A CA  
2560 C  C   . LEU   A 122 ? 0.1391 0.1426 0.1361 -0.0164 0.0075  0.0285  122 LEU   A C   
2561 O  O   . LEU   A 122 ? 0.1376 0.1461 0.1657 -0.0197 0.0060  0.0291  122 LEU   A O   
2562 C  CB  . LEU   A 122 ? 0.1643 0.1477 0.1695 -0.0038 0.0150  0.0426  122 LEU   A CB  
2563 C  CG  . LEU   A 122 ? 0.1623 0.1561 0.1612 -0.0004 0.0128  0.0325  122 LEU   A CG  
2564 C  CD1 . LEU   A 122 ? 0.1771 0.1533 0.1835 -0.0087 0.0146  0.0316  122 LEU   A CD1 
2565 C  CD2 . LEU   A 122 ? 0.1594 0.1480 0.1480 -0.0019 0.0263  0.0268  122 LEU   A CD2 
2577 N  N   . LEU   A 123 ? 0.1323 0.1428 0.1300 -0.0167 0.0002  0.0254  123 LEU   A N   
2578 C  CA  . LEU   A 123 ? 0.1279 0.1435 0.1318 -0.0147 0.0021  0.0254  123 LEU   A CA  
2579 C  C   . LEU   A 123 ? 0.1284 0.1366 0.1128 -0.0099 0.0057  0.0295  123 LEU   A C   
2580 O  O   . LEU   A 123 ? 0.1208 0.1512 0.1360 -0.0217 0.0048  0.0347  123 LEU   A O   
2581 C  CB  . LEU   A 123 ? 0.1371 0.1526 0.1236 -0.0168 0.0140  0.0288  123 LEU   A CB  
2582 C  CG  . LEU   A 123 ? 0.1466 0.1623 0.1397 -0.0136 0.0181  0.0179  123 LEU   A CG  
2583 C  CD1 . LEU   A 123 ? 0.1529 0.1683 0.1662 -0.0081 0.0197  0.0103  123 LEU   A CD1 
2584 C  CD2 . LEU   A 123 ? 0.1536 0.1649 0.1586 -0.0073 0.0063  0.0134  123 LEU   A CD2 
2596 N  N   A ALA   A 124 ? 0.1277 0.1284 0.1217 -0.0142 0.0082  0.0234  124 ALA   A N   
2597 N  N   B ALA   A 124 ? 0.1278 0.1329 0.1124 -0.0087 0.0046  0.0207  124 ALA   A N   
2598 C  CA  A ALA   A 124 ? 0.1206 0.1217 0.1247 -0.0122 0.0011  0.0227  124 ALA   A CA  
2599 C  CA  B ALA   A 124 ? 0.1239 0.1319 0.1168 -0.0093 0.0002  0.0216  124 ALA   A CA  
2600 C  C   A ALA   A 124 ? 0.1088 0.1227 0.1398 -0.0116 0.0013  0.0238  124 ALA   A C   
2601 C  C   B ALA   A 124 ? 0.1214 0.1326 0.1123 -0.0058 0.0084  0.0220  124 ALA   A C   
2602 O  O   A ALA   A 124 ? 0.1038 0.1190 0.1566 -0.0202 0.0075  0.0255  124 ALA   A O   
2603 O  O   B ALA   A 124 ? 0.1287 0.1361 0.1128 -0.0018 0.0179  0.0236  124 ALA   A O   
2604 C  CB  A ALA   A 124 ? 0.1192 0.1153 0.1362 -0.0158 0.0128  0.0190  124 ALA   A CB  
2605 C  CB  B ALA   A 124 ? 0.1217 0.1317 0.1297 -0.0083 -0.0003 0.0213  124 ALA   A CB  
2616 N  N   A PRO   A 125 ? 0.1078 0.1269 0.1430 -0.0078 0.0046  0.0309  125 PRO   A N   
2617 N  N   B PRO   A 125 ? 0.1101 0.1289 0.1080 -0.0030 0.0040  0.0271  125 PRO   A N   
2618 C  CA  A PRO   A 125 ? 0.1148 0.1211 0.1520 -0.0070 0.0005  0.0262  125 PRO   A CA  
2619 C  CA  B PRO   A 125 ? 0.1170 0.1295 0.1141 -0.0020 0.0067  0.0176  125 PRO   A CA  
2620 C  C   A PRO   A 125 ? 0.1023 0.1176 0.1435 -0.0077 0.0051  0.0329  125 PRO   A C   
2621 C  C   B PRO   A 125 ? 0.1251 0.1392 0.1156 0.0026  0.0093  0.0100  125 PRO   A C   
2622 O  O   A PRO   A 125 ? 0.1132 0.1178 0.1452 0.0022  0.0027  0.0308  125 PRO   A O   
2623 O  O   B PRO   A 125 ? 0.1342 0.1449 0.1170 0.0012  0.0133  0.0112  125 PRO   A O   
2624 C  CB  A PRO   A 125 ? 0.1261 0.1264 0.1605 -0.0135 0.0025  0.0265  125 PRO   A CB  
2625 C  CB  B PRO   A 125 ? 0.1115 0.1273 0.1134 -0.0096 0.0058  0.0254  125 PRO   A CB  
2626 C  CG  A PRO   A 125 ? 0.1307 0.1280 0.1558 -0.0082 0.0028  0.0276  125 PRO   A CG  
2627 C  CG  B PRO   A 125 ? 0.1054 0.1186 0.1038 -0.0094 0.0105  0.0233  125 PRO   A CG  
2628 C  CD  A PRO   A 125 ? 0.1202 0.1312 0.1454 -0.0044 0.0146  0.0178  125 PRO   A CD  
2629 C  CD  B PRO   A 125 ? 0.0997 0.1131 0.0987 -0.0079 0.0113  0.0208  125 PRO   A CD  
2644 N  N   A LEU   A 126 ? 0.0986 0.1245 0.1429 -0.0050 0.0069  0.0232  126 LEU   A N   
2645 N  N   B LEU   A 126 ? 0.1317 0.1447 0.1314 0.0097  0.0055  -0.0038 126 LEU   A N   
2646 C  CA  A LEU   A 126 ? 0.1119 0.1258 0.1454 -0.0058 0.0044  0.0212  126 LEU   A CA  
2647 C  CA  B LEU   A 126 ? 0.1385 0.1487 0.1569 0.0162  0.0022  -0.0070 126 LEU   A CA  
2648 C  C   A LEU   A 126 ? 0.1212 0.1271 0.1461 0.0031  -0.0013 0.0205  126 LEU   A C   
2649 C  C   B LEU   A 126 ? 0.1367 0.1468 0.1481 0.0261  0.0042  -0.0076 126 LEU   A C   
2650 O  O   A LEU   A 126 ? 0.1313 0.1252 0.1704 0.0086  0.0192  0.0298  126 LEU   A O   
2651 O  O   B LEU   A 126 ? 0.1472 0.1460 0.1673 0.0224  -0.0011 0.0038  126 LEU   A O   
2652 C  CB  A LEU   A 126 ? 0.1161 0.1257 0.1414 -0.0036 0.0046  0.0146  126 LEU   A CB  
2653 C  CB  B LEU   A 126 ? 0.1518 0.1661 0.2212 0.0059  -0.0113 -0.0078 126 LEU   A CB  
2654 C  CG  A LEU   A 126 ? 0.1160 0.1514 0.1473 -0.0174 0.0094  0.0125  126 LEU   A CG  
2655 C  CG  B LEU   A 126 ? 0.1617 0.1804 0.2817 -0.0070 -0.0219 0.0010  126 LEU   A CG  
2656 C  CD1 A LEU   A 126 ? 0.1245 0.1712 0.1782 -0.0240 -0.0007 0.0112  126 LEU   A CD1 
2657 C  CD1 B LEU   A 126 ? 0.1670 0.1794 0.2970 -0.0149 -0.0185 0.0047  126 LEU   A CD1 
2658 C  CD2 A LEU   A 126 ? 0.1335 0.1491 0.1615 -0.0246 0.0071  0.0238  126 LEU   A CD2 
2659 C  CD2 B LEU   A 126 ? 0.1617 0.1909 0.2966 -0.0090 -0.0291 -0.0011 126 LEU   A CD2 
2682 N  N   A LEU   A 127 ? 0.1260 0.1245 0.1436 -0.0038 0.0073  0.0214  127 LEU   A N   
2683 N  N   B LEU   A 127 ? 0.1340 0.1492 0.1427 0.0283  0.0078  -0.0004 127 LEU   A N   
2684 C  CA  A LEU   A 127 ? 0.1306 0.1315 0.1331 -0.0033 0.0068  0.0140  127 LEU   A CA  
2685 C  CA  B LEU   A 127 ? 0.1275 0.1540 0.1340 0.0249  0.0054  0.0127  127 LEU   A CA  
2686 C  C   A LEU   A 127 ? 0.1323 0.1241 0.1348 -0.0074 -0.0025 0.0084  127 LEU   A C   
2687 C  C   B LEU   A 127 ? 0.1244 0.1467 0.1351 0.0228  0.0060  0.0139  127 LEU   A C   
2688 O  O   A LEU   A 127 ? 0.1389 0.1235 0.1323 -0.0222 -0.0013 0.0099  127 LEU   A O   
2689 O  O   B LEU   A 127 ? 0.1329 0.1462 0.1452 0.0209  0.0094  0.0246  127 LEU   A O   
2690 C  CB  A LEU   A 127 ? 0.1432 0.1361 0.1398 0.0110  0.0120  0.0028  127 LEU   A CB  
2691 C  CB  B LEU   A 127 ? 0.1283 0.1653 0.1278 0.0242  0.0033  0.0125  127 LEU   A CB  
2692 C  CG  A LEU   A 127 ? 0.1525 0.1362 0.1486 0.0166  0.0049  0.0039  127 LEU   A CG  
2693 C  CG  B LEU   A 127 ? 0.1268 0.1706 0.1242 0.0208  -0.0052 0.0184  127 LEU   A CG  
2694 C  CD1 A LEU   A 127 ? 0.1561 0.1309 0.1472 0.0078  -0.0051 0.0019  127 LEU   A CD1 
2695 C  CD1 B LEU   A 127 ? 0.1275 0.1683 0.1366 0.0229  0.0042  0.0267  127 LEU   A CD1 
2696 C  CD2 A LEU   A 127 ? 0.1647 0.1280 0.1797 0.0336  -0.0060 0.0071  127 LEU   A CD2 
2697 C  CD2 B LEU   A 127 ? 0.1413 0.1821 0.1260 0.0183  -0.0136 0.0119  127 LEU   A CD2 
2720 N  N   A SER   A 128 ? 0.1388 0.1223 0.1358 -0.0064 -0.0085 0.0081  128 SER   A N   
2721 N  N   B SER   A 128 ? 0.1209 0.1444 0.1297 0.0146  -0.0016 0.0173  128 SER   A N   
2722 C  CA  A SER   A 128 ? 0.1518 0.1277 0.1368 -0.0035 -0.0032 0.0111  128 SER   A CA  
2723 C  CA  B SER   A 128 ? 0.1253 0.1438 0.1260 0.0078  -0.0146 0.0250  128 SER   A CA  
2724 C  C   A SER   A 128 ? 0.1556 0.1323 0.1484 0.0039  -0.0047 0.0121  128 SER   A C   
2725 C  C   B SER   A 128 ? 0.1293 0.1380 0.1389 0.0032  -0.0249 0.0366  128 SER   A C   
2726 O  O   A SER   A 128 ? 0.1678 0.1496 0.1801 0.0050  0.0012  0.0095  128 SER   A O   
2727 O  O   B SER   A 128 ? 0.1269 0.1390 0.1539 -0.0067 -0.0296 0.0304  128 SER   A O   
2728 C  CB  A SER   A 128 ? 0.1526 0.1411 0.1345 -0.0089 -0.0007 0.0112  128 SER   A CB  
2729 C  CB  B SER   A 128 ? 0.1197 0.1498 0.1151 -0.0039 -0.0241 0.0123  128 SER   A CB  
2730 O  OG  A SER   A 128 ? 0.1521 0.1450 0.1353 -0.0084 0.0067  0.0144  128 SER   A OG  
2731 O  OG  B SER   A 128 ? 0.1122 0.1484 0.1322 -0.0074 -0.0142 0.0003  128 SER   A OG  
2742 N  N   A ALA   A 129 ? 0.1462 0.1401 0.1724 0.0020  0.0014  0.0209  129 ALA   A N   
2743 N  N   B ALA   A 129 ? 0.1311 0.1466 0.1588 0.0038  -0.0300 0.0426  129 ALA   A N   
2744 C  CA  A ALA   A 129 ? 0.1365 0.1417 0.1785 0.0072  0.0064  0.0213  129 ALA   A CA  
2745 C  CA  B ALA   A 129 ? 0.1361 0.1510 0.1717 0.0060  -0.0274 0.0389  129 ALA   A CA  
2746 C  C   A ALA   A 129 ? 0.1418 0.1378 0.1508 0.0061  -0.0019 0.0020  129 ALA   A C   
2747 C  C   B ALA   A 129 ? 0.1444 0.1515 0.1641 0.0013  -0.0271 0.0225  129 ALA   A C   
2748 O  O   A ALA   A 129 ? 0.1513 0.1454 0.1512 0.0049  -0.0031 0.0063  129 ALA   A O   
2749 O  O   B ALA   A 129 ? 0.1462 0.1524 0.1562 -0.0058 -0.0273 0.0181  129 ALA   A O   
2750 C  CB  A ALA   A 129 ? 0.1416 0.1581 0.2166 0.0157  0.0128  0.0297  129 ALA   A CB  
2751 C  CB  B ALA   A 129 ? 0.1450 0.1637 0.1858 0.0086  -0.0162 0.0335  129 ALA   A CB  
2762 N  N   A GLY   A 130 ? 0.1387 0.1328 0.1364 0.0048  -0.0049 0.0014  130 GLY   A N   
2763 N  N   B GLY   A 130 ? 0.1531 0.1556 0.1521 0.0036  -0.0301 0.0248  130 GLY   A N   
2764 C  CA  A GLY   A 130 ? 0.1516 0.1317 0.1335 0.0118  -0.0063 -0.0004 130 GLY   A CA  
2765 C  CA  B GLY   A 130 ? 0.1652 0.1560 0.1542 0.0085  -0.0285 0.0203  130 GLY   A CA  
2766 C  C   A GLY   A 130 ? 0.1531 0.1305 0.1373 0.0084  -0.0018 0.0032  130 GLY   A C   
2767 C  C   B GLY   A 130 ? 0.1680 0.1578 0.1578 0.0079  -0.0372 0.0186  130 GLY   A C   
2768 O  O   A GLY   A 130 ? 0.1491 0.1312 0.1389 0.0009  -0.0049 0.0076  130 GLY   A O   
2769 O  O   B GLY   A 130 ? 0.1691 0.1596 0.1632 0.0096  -0.0369 0.0209  130 GLY   A O   
2776 N  N   A ILE   A 131 ? 0.1638 0.1319 0.1510 0.0033  -0.0106 0.0125  131 ILE   A N   
2777 N  N   B ILE   A 131 ? 0.1696 0.1552 0.1672 0.0033  -0.0320 0.0255  131 ILE   A N   
2778 C  CA  A ILE   A 131 ? 0.1787 0.1329 0.1459 -0.0033 -0.0200 0.0038  131 ILE   A CA  
2779 C  CA  B ILE   A 131 ? 0.1729 0.1516 0.1622 0.0041  -0.0385 0.0270  131 ILE   A CA  
2780 C  C   A ILE   A 131 ? 0.1752 0.1408 0.1352 -0.0044 -0.0141 0.0125  131 ILE   A C   
2781 C  C   B ILE   A 131 ? 0.1748 0.1547 0.1527 0.0068  -0.0323 0.0329  131 ILE   A C   
2782 O  O   A ILE   A 131 ? 0.1839 0.1516 0.1511 -0.0003 -0.0146 0.0159  131 ILE   A O   
2783 O  O   B ILE   A 131 ? 0.1874 0.1607 0.1538 0.0050  -0.0198 0.0332  131 ILE   A O   
2784 C  CB  A ILE   A 131 ? 0.1894 0.1438 0.1639 -0.0053 -0.0263 -0.0063 131 ILE   A CB  
2785 C  CB  B ILE   A 131 ? 0.1762 0.1600 0.1821 0.0064  -0.0508 0.0160  131 ILE   A CB  
2786 C  CG1 A ILE   A 131 ? 0.1979 0.1723 0.1691 -0.0109 -0.0333 -0.0094 131 ILE   A CG1 
2787 C  CG1 B ILE   A 131 ? 0.1816 0.1780 0.1944 0.0100  -0.0562 0.0066  131 ILE   A CG1 
2788 C  CG2 A ILE   A 131 ? 0.1948 0.1327 0.1968 -0.0030 -0.0176 -0.0169 131 ILE   A CG2 
2789 C  CG2 B ILE   A 131 ? 0.1757 0.1555 0.1944 0.0039  -0.0448 0.0040  131 ILE   A CG2 
2790 C  CD1 A ILE   A 131 ? 0.2061 0.1819 0.1866 -0.0124 -0.0361 -0.0089 131 ILE   A CD1 
2791 C  CD1 B ILE   A 131 ? 0.1894 0.1870 0.2033 0.0071  -0.0556 0.0011  131 ILE   A CD1 
2814 N  N   A PHE   A 132 ? 0.1657 0.1396 0.1324 -0.0077 -0.0033 0.0141  132 PHE   A N   
2815 N  N   B PHE   A 132 ? 0.1665 0.1532 0.1539 0.0125  -0.0356 0.0283  132 PHE   A N   
2816 C  CA  A PHE   A 132 ? 0.1680 0.1467 0.1342 -0.0093 -0.0013 0.0064  132 PHE   A CA  
2817 C  CA  B PHE   A 132 ? 0.1645 0.1547 0.1642 0.0057  -0.0273 0.0186  132 PHE   A CA  
2818 C  C   A PHE   A 132 ? 0.1645 0.1615 0.1265 -0.0123 -0.0045 0.0074  132 PHE   A C   
2819 C  C   B PHE   A 132 ? 0.1738 0.1690 0.1766 0.0093  -0.0304 0.0116  132 PHE   A C   
2820 O  O   A PHE   A 132 ? 0.1684 0.1701 0.1315 -0.0162 -0.0055 0.0081  132 PHE   A O   
2821 O  O   B PHE   A 132 ? 0.1885 0.1813 0.1886 0.0075  -0.0259 0.0092  132 PHE   A O   
2822 C  CB  A PHE   A 132 ? 0.1698 0.1435 0.1376 -0.0025 -0.0078 0.0148  132 PHE   A CB  
2823 C  CB  B PHE   A 132 ? 0.1552 0.1450 0.1415 0.0009  -0.0231 0.0277  132 PHE   A CB  
2824 C  CG  A PHE   A 132 ? 0.1706 0.1435 0.1444 0.0020  -0.0161 0.0132  132 PHE   A CG  
2825 C  CG  B PHE   A 132 ? 0.1547 0.1414 0.1274 0.0008  -0.0169 0.0127  132 PHE   A CG  
2826 C  CD1 A PHE   A 132 ? 0.1733 0.1515 0.1601 0.0119  -0.0201 0.0029  132 PHE   A CD1 
2827 C  CD1 B PHE   A 132 ? 0.1576 0.1481 0.1399 0.0073  -0.0100 0.0006  132 PHE   A CD1 
2828 C  CD2 A PHE   A 132 ? 0.1687 0.1496 0.1613 -0.0006 -0.0191 0.0054  132 PHE   A CD2 
2829 C  CD2 B PHE   A 132 ? 0.1527 0.1436 0.1293 0.0013  -0.0143 -0.0018 132 PHE   A CD2 
2830 C  CE1 A PHE   A 132 ? 0.1727 0.1585 0.1542 0.0100  -0.0208 -0.0069 132 PHE   A CE1 
2831 C  CE1 B PHE   A 132 ? 0.1544 0.1547 0.1260 0.0085  -0.0092 -0.0041 132 PHE   A CE1 
2832 C  CE2 A PHE   A 132 ? 0.1685 0.1492 0.1669 0.0001  -0.0258 -0.0009 132 PHE   A CE2 
2833 C  CE2 B PHE   A 132 ? 0.1522 0.1526 0.1335 0.0094  -0.0152 -0.0087 132 PHE   A CE2 
2834 C  CZ  A PHE   A 132 ? 0.1702 0.1566 0.1631 0.0041  -0.0263 -0.0061 132 PHE   A CZ  
2835 C  CZ  B PHE   A 132 ? 0.1507 0.1542 0.1225 0.0096  -0.0118 -0.0072 132 PHE   A CZ  
2854 N  N   A GLY   A 133 ? 0.1651 0.1648 0.1400 -0.0070 -0.0192 0.0122  133 GLY   A N   
2855 N  N   B GLY   A 133 ? 0.1719 0.1696 0.1747 0.0082  -0.0354 0.0170  133 GLY   A N   
2856 C  CA  A GLY   A 133 ? 0.1773 0.1708 0.1596 -0.0040 -0.0369 0.0066  133 GLY   A CA  
2857 C  CA  B GLY   A 133 ? 0.1734 0.1730 0.1714 0.0067  -0.0354 0.0089  133 GLY   A CA  
2858 C  C   A GLY   A 133 ? 0.1881 0.1784 0.1630 -0.0087 -0.0516 -0.0054 133 GLY   A C   
2859 C  C   B GLY   A 133 ? 0.1761 0.1813 0.1767 0.0070  -0.0454 -0.0097 133 GLY   A C   
2860 O  O   A GLY   A 133 ? 0.1982 0.1941 0.1689 -0.0019 -0.0499 -0.0259 133 GLY   A O   
2861 O  O   B GLY   A 133 ? 0.1759 0.1930 0.1754 0.0111  -0.0431 -0.0286 133 GLY   A O   
2868 N  N   A ALA   A 134 ? 0.1885 0.1679 0.1554 -0.0186 -0.0479 0.0028  134 ALA   A N   
2869 N  N   B ALA   A 134 ? 0.1809 0.1765 0.1823 0.0049  -0.0459 -0.0081 134 ALA   A N   
2870 C  CA  A ALA   A 134 ? 0.1884 0.1697 0.1871 -0.0203 -0.0511 0.0031  134 ALA   A CA  
2871 C  CA  B ALA   A 134 ? 0.1825 0.1728 0.2022 0.0043  -0.0441 -0.0080 134 ALA   A CA  
2872 C  C   A ALA   A 134 ? 0.1889 0.1731 0.1991 -0.0254 -0.0563 0.0135  134 ALA   A C   
2873 C  C   B ALA   A 134 ? 0.1823 0.1670 0.2117 0.0018  -0.0409 -0.0068 134 ALA   A C   
2874 O  O   A ALA   A 134 ? 0.1977 0.1796 0.2267 -0.0292 -0.0435 0.0128  134 ALA   A O   
2875 O  O   B ALA   A 134 ? 0.1793 0.1595 0.2222 -0.0024 -0.0265 -0.0159 134 ALA   A O   
2876 C  CB  A ALA   A 134 ? 0.1935 0.1687 0.2245 -0.0157 -0.0476 -0.0061 134 ALA   A CB  
2877 C  CB  B ALA   A 134 ? 0.1873 0.1729 0.2259 0.0056  -0.0440 -0.0085 134 ALA   A CB  
2888 N  N   A ASP   A 135 ? 0.1896 0.1739 0.2144 -0.0228 -0.0543 0.0260  135 ASP   A N   
2889 N  N   B ASP   A 135 ? 0.1923 0.1760 0.2212 -0.0044 -0.0456 0.0045  135 ASP   A N   
2890 C  CA  A ASP   A 135 ? 0.1824 0.1847 0.2397 -0.0227 -0.0679 0.0404  135 ASP   A CA  
2891 C  CA  B ASP   A 135 ? 0.1944 0.1829 0.2386 -0.0065 -0.0500 0.0110  135 ASP   A CA  
2892 C  C   A ASP   A 135 ? 0.1749 0.1760 0.2435 -0.0138 -0.0587 0.0536  135 ASP   A C   
2893 C  C   B ASP   A 135 ? 0.1795 0.1649 0.2368 -0.0046 -0.0328 0.0117  135 ASP   A C   
2894 O  O   A ASP   A 135 ? 0.1682 0.1673 0.2525 -0.0169 -0.0575 0.0608  135 ASP   A O   
2895 O  O   B ASP   A 135 ? 0.1741 0.1590 0.2418 -0.0085 -0.0246 0.0188  135 ASP   A O   
2896 C  CB  A ASP   A 135 ? 0.1976 0.2176 0.2765 -0.0352 -0.0803 0.0268  135 ASP   A CB  
2897 C  CB  B ASP   A 135 ? 0.2121 0.2110 0.2571 -0.0081 -0.0641 0.0146  135 ASP   A CB  
2898 C  CG  A ASP   A 135 ? 0.2108 0.2499 0.3200 -0.0526 -0.0846 0.0093  135 ASP   A CG  
2899 C  CG  B ASP   A 135 ? 0.2243 0.2382 0.2833 -0.0086 -0.0680 0.0229  135 ASP   A CG  
2900 O  OD1 A ASP   A 135 ? 0.2048 0.2629 0.3441 -0.0544 -0.0788 0.0100  135 ASP   A OD1 
2901 O  OD1 B ASP   A 135 ? 0.2257 0.2390 0.2930 -0.0043 -0.0659 0.0289  135 ASP   A OD1 
2902 O  OD2 A ASP   A 135 ? 0.2332 0.2697 0.3544 -0.0558 -0.0772 -0.0015 135 ASP   A OD2 
2903 O  OD2 B ASP   A 135 ? 0.2289 0.2528 0.3029 -0.0116 -0.0773 0.0305  135 ASP   A OD2 
2912 N  N   A PRO   A 136 ? 0.1663 0.1743 0.2560 -0.0025 -0.0411 0.0604  136 PRO   A N   
2913 N  N   B PRO   A 136 ? 0.1713 0.1526 0.2373 -0.0005 -0.0178 0.0044  136 PRO   A N   
2914 C  CA  A PRO   A 136 ? 0.1573 0.1713 0.2648 -0.0050 -0.0262 0.0493  136 PRO   A CA  
2915 C  CA  B PRO   A 136 ? 0.1610 0.1570 0.2337 -0.0040 -0.0080 -0.0076 136 PRO   A CA  
2916 C  C   A PRO   A 136 ? 0.1340 0.1651 0.2575 -0.0067 -0.0205 0.0376  136 PRO   A C   
2917 C  C   B PRO   A 136 ? 0.1412 0.1606 0.2114 -0.0019 -0.0030 -0.0064 136 PRO   A C   
2918 O  O   A PRO   A 136 ? 0.1293 0.1633 0.2434 -0.0111 -0.0164 0.0392  136 PRO   A O   
2919 O  O   B PRO   A 136 ? 0.1338 0.1575 0.1884 0.0054  0.0149  -0.0041 136 PRO   A O   
2920 C  CB  A PRO   A 136 ? 0.1753 0.1766 0.2777 0.0050  -0.0215 0.0484  136 PRO   A CB  
2921 C  CB  B PRO   A 136 ? 0.1742 0.1561 0.2470 -0.0021 -0.0067 -0.0072 136 PRO   A CB  
2922 C  CG  A PRO   A 136 ? 0.1813 0.1828 0.2836 0.0108  -0.0277 0.0502  136 PRO   A CG  
2923 C  CG  B PRO   A 136 ? 0.1805 0.1537 0.2611 0.0020  -0.0070 -0.0033 136 PRO   A CG  
2924 C  CD  A PRO   A 136 ? 0.1781 0.1801 0.2716 0.0109  -0.0331 0.0610  136 PRO   A CD  
2925 C  CD  B PRO   A 136 ? 0.1773 0.1469 0.2480 0.0014  -0.0091 0.0069  136 PRO   A CD  
2940 N  N   A ILE   A 137 ? 0.1332 0.1672 0.2559 -0.0072 -0.0349 0.0394  137 ILE   A N   
2941 N  N   B ILE   A 137 ? 0.1401 0.1626 0.2216 -0.0041 -0.0141 -0.0106 137 ILE   A N   
2942 C  CA  A ILE   A 137 ? 0.1345 0.1750 0.2568 -0.0125 -0.0375 0.0436  137 ILE   A CA  
2943 C  CA  B ILE   A 137 ? 0.1451 0.1666 0.2269 -0.0020 -0.0138 -0.0075 137 ILE   A CA  
2944 C  C   A ILE   A 137 ? 0.1349 0.1803 0.2309 -0.0117 -0.0368 0.0431  137 ILE   A C   
2945 C  C   B ILE   A 137 ? 0.1414 0.1703 0.2106 -0.0052 0.0009  -0.0027 137 ILE   A C   
2946 O  O   A ILE   A 137 ? 0.1381 0.1728 0.2286 -0.0170 -0.0298 0.0337  137 ILE   A O   
2947 O  O   B ILE   A 137 ? 0.1358 0.1687 0.2105 -0.0058 0.0047  -0.0039 137 ILE   A O   
2948 C  CB  A ILE   A 137 ? 0.1441 0.1925 0.2787 -0.0150 -0.0451 0.0394  137 ILE   A CB  
2949 C  CB  B ILE   A 137 ? 0.1552 0.1679 0.2485 -0.0003 -0.0320 -0.0051 137 ILE   A CB  
2950 C  CG1 A ILE   A 137 ? 0.1482 0.2080 0.3140 -0.0195 -0.0386 0.0418  137 ILE   A CG1 
2951 C  CG1 B ILE   A 137 ? 0.1674 0.1755 0.2787 0.0054  -0.0478 -0.0007 137 ILE   A CG1 
2952 C  CG2 A ILE   A 137 ? 0.1545 0.1954 0.2774 -0.0178 -0.0400 0.0315  137 ILE   A CG2 
2953 C  CG2 B ILE   A 137 ? 0.1615 0.1685 0.2537 0.0028  -0.0328 -0.0049 137 ILE   A CG2 
2954 C  CD1 A ILE   A 137 ? 0.1549 0.2172 0.3272 -0.0167 -0.0305 0.0499  137 ILE   A CD1 
2955 C  CD1 B ILE   A 137 ? 0.1760 0.1807 0.2946 0.0068  -0.0535 0.0022  137 ILE   A CD1 
2978 N  N   A HIS   A 138 ? 0.1392 0.2003 0.2186 -0.0117 -0.0314 0.0439  138 HIS   A N   
2979 N  N   B HIS   A 138 ? 0.1411 0.1843 0.2038 -0.0057 0.0160  -0.0005 138 HIS   A N   
2980 C  CA  A HIS   A 138 ? 0.1423 0.2090 0.2034 -0.0153 -0.0241 0.0457  138 HIS   A CA  
2981 C  CA  B HIS   A 138 ? 0.1468 0.1879 0.1963 -0.0083 0.0129  0.0119  138 HIS   A CA  
2982 C  C   A HIS   A 138 ? 0.1326 0.1984 0.1976 -0.0081 -0.0225 0.0458  138 HIS   A C   
2983 C  C   B HIS   A 138 ? 0.1400 0.1842 0.1960 -0.0072 0.0037  0.0292  138 HIS   A C   
2984 O  O   A HIS   A 138 ? 0.1354 0.1988 0.1946 -0.0129 -0.0132 0.0446  138 HIS   A O   
2985 O  O   B HIS   A 138 ? 0.1446 0.1828 0.2004 -0.0136 0.0075  0.0241  138 HIS   A O   
2986 C  CB  A HIS   A 138 ? 0.1647 0.2308 0.1921 -0.0205 -0.0311 0.0406  138 HIS   A CB  
2987 C  CB  B HIS   A 138 ? 0.1531 0.1977 0.1879 -0.0037 0.0072  0.0002  138 HIS   A CB  
2988 C  CG  A HIS   A 138 ? 0.1832 0.2430 0.2008 -0.0237 -0.0313 0.0346  138 HIS   A CG  
2989 C  CG  B HIS   A 138 ? 0.1629 0.2033 0.1992 -0.0046 0.0001  -0.0104 138 HIS   A CG  
2990 N  ND1 A HIS   A 138 ? 0.1979 0.2534 0.2166 -0.0252 -0.0307 0.0272  138 HIS   A ND1 
2991 N  ND1 B HIS   A 138 ? 0.1746 0.2103 0.2221 -0.0048 -0.0066 -0.0170 138 HIS   A ND1 
2992 C  CD2 A HIS   A 138 ? 0.1863 0.2502 0.1961 -0.0181 -0.0300 0.0307  138 HIS   A CD2 
2993 C  CD2 B HIS   A 138 ? 0.1631 0.2001 0.1967 -0.0014 0.0045  -0.0100 138 HIS   A CD2 
2994 C  CE1 A HIS   A 138 ? 0.2050 0.2589 0.2188 -0.0176 -0.0299 0.0212  138 HIS   A CE1 
2995 C  CE1 B HIS   A 138 ? 0.1769 0.2091 0.2212 0.0020  -0.0080 -0.0189 138 HIS   A CE1 
2996 N  NE2 A HIS   A 138 ? 0.1963 0.2587 0.1990 -0.0135 -0.0242 0.0235  138 HIS   A NE2 
2997 N  NE2 B HIS   A 138 ? 0.1713 0.2039 0.2029 0.0034  0.0034  -0.0158 138 HIS   A NE2 
3012 N  N   . SER   A 139 ? 0.1287 0.1825 0.2003 -0.0058 -0.0124 0.0481  139 SER   A N   
3013 C  CA  . SER   A 139 ? 0.1268 0.1759 0.1913 -0.0095 -0.0049 0.0498  139 SER   A CA  
3014 C  C   . SER   A 139 ? 0.1207 0.1604 0.1958 -0.0099 -0.0006 0.0373  139 SER   A C   
3015 O  O   . SER   A 139 ? 0.1163 0.1546 0.2083 -0.0091 -0.0004 0.0392  139 SER   A O   
3016 C  CB  . SER   A 139 ? 0.1294 0.1737 0.1959 -0.0179 -0.0090 0.0490  139 SER   A CB  
3017 O  OG  . SER   A 139 ? 0.1368 0.1725 0.2008 -0.0172 -0.0131 0.0569  139 SER   A OG  
3024 N  N   . LEU   A 140 ? 0.1181 0.1620 0.1945 -0.0050 -0.0028 0.0470  140 LEU   A N   
3025 C  CA  . LEU   A 140 ? 0.1180 0.1571 0.1947 -0.0091 0.0021  0.0450  140 LEU   A CA  
3026 C  C   . LEU   A 140 ? 0.1112 0.1685 0.1945 -0.0145 -0.0036 0.0426  140 LEU   A C   
3027 O  O   . LEU   A 140 ? 0.1201 0.1611 0.2056 -0.0048 -0.0045 0.0434  140 LEU   A O   
3028 C  CB  . LEU   A 140 ? 0.1259 0.1609 0.1995 -0.0162 -0.0031 0.0423  140 LEU   A CB  
3029 C  CG  . LEU   A 140 ? 0.1221 0.1691 0.2015 -0.0194 -0.0017 0.0478  140 LEU   A CG  
3030 C  CD1 . LEU   A 140 ? 0.1269 0.1659 0.2020 -0.0095 -0.0007 0.0357  140 LEU   A CD1 
3031 C  CD2 . LEU   A 140 ? 0.1273 0.1875 0.2118 -0.0200 0.0068  0.0482  140 LEU   A CD2 
3043 N  N   . ARG   A 141 ? 0.1227 0.1715 0.2030 -0.0146 -0.0021 0.0377  141 ARG   A N   
3044 C  CA  . ARG   A 141 ? 0.1344 0.1915 0.2047 -0.0304 -0.0167 0.0211  141 ARG   A CA  
3045 C  C   . ARG   A 141 ? 0.1330 0.1701 0.1899 -0.0217 -0.0152 0.0194  141 ARG   A C   
3046 O  O   . ARG   A 141 ? 0.1271 0.1633 0.2113 -0.0160 -0.0001 0.0142  141 ARG   A O   
3047 C  CB  . ARG   A 141 ? 0.1487 0.2245 0.2391 -0.0385 -0.0184 0.0035  141 ARG   A CB  
3048 C  CG  . ARG   A 141 ? 0.1877 0.2643 0.2749 -0.0362 -0.0080 -0.0092 141 ARG   A CG  
3049 C  CD  . ARG   A 141 ? 0.2138 0.2939 0.3018 -0.0416 -0.0058 -0.0169 141 ARG   A CD  
3050 N  NE  . ARG   A 141 ? 0.2072 0.3148 0.3186 -0.0493 -0.0138 -0.0158 141 ARG   A NE  
3051 C  CZ  . ARG   A 141 ? 0.2067 0.3321 0.3305 -0.0659 0.0039  -0.0066 141 ARG   A CZ  
3052 N  NH1 . ARG   A 141 ? 0.1953 0.3359 0.3312 -0.0767 0.0314  -0.0198 141 ARG   A NH1 
3053 N  NH2 . ARG   A 141 ? 0.2062 0.3409 0.3400 -0.0622 -0.0125 0.0012  141 ARG   A NH2 
3067 N  N   . VAL   A 142 ? 0.1304 0.1655 0.1792 -0.0154 -0.0096 0.0147  142 VAL   A N   
3068 C  CA  . VAL   A 142 ? 0.1285 0.1610 0.1804 -0.0139 0.0082  0.0149  142 VAL   A CA  
3069 C  C   . VAL   A 142 ? 0.1162 0.1518 0.1839 -0.0143 0.0047  0.0169  142 VAL   A C   
3070 O  O   . VAL   A 142 ? 0.1222 0.1506 0.1838 -0.0043 0.0053  0.0187  142 VAL   A O   
3071 C  CB  . VAL   A 142 ? 0.1400 0.1672 0.1669 -0.0115 0.0059  0.0189  142 VAL   A CB  
3072 C  CG1 . VAL   A 142 ? 0.1439 0.1594 0.1782 -0.0219 0.0105  0.0165  142 VAL   A CG1 
3073 C  CG2 . VAL   A 142 ? 0.1514 0.1828 0.1864 -0.0073 0.0032  0.0218  142 VAL   A CG2 
3083 N  N   . CYS   A 143 ? 0.1258 0.1458 0.1782 -0.0170 0.0016  0.0162  143 CYS   A N   
3084 C  CA  . CYS   A 143 ? 0.1234 0.1430 0.1823 -0.0090 0.0010  0.0252  143 CYS   A CA  
3085 C  C   . CYS   A 143 ? 0.1195 0.1381 0.1867 -0.0084 0.0074  0.0261  143 CYS   A C   
3086 O  O   . CYS   A 143 ? 0.1155 0.1355 0.1847 -0.0039 0.0042  0.0273  143 CYS   A O   
3087 C  CB  . CYS   A 143 ? 0.1317 0.1371 0.1851 -0.0044 0.0087  0.0354  143 CYS   A CB  
3088 S  SG  . CYS   A 143 ? 0.1462 0.1487 0.1775 0.0061  0.0104  0.0201  143 CYS   A SG  
3094 N  N   . VAL   A 144 ? 0.1178 0.1451 0.2018 -0.0066 0.0069  0.0316  144 VAL   A N   
3095 C  CA  . VAL   A 144 ? 0.1247 0.1490 0.2268 -0.0111 0.0164  0.0294  144 VAL   A CA  
3096 C  C   . VAL   A 144 ? 0.1267 0.1426 0.2066 -0.0166 -0.0060 0.0268  144 VAL   A C   
3097 O  O   . VAL   A 144 ? 0.1378 0.1470 0.2145 -0.0066 -0.0068 0.0263  144 VAL   A O   
3098 C  CB  . VAL   A 144 ? 0.1442 0.1712 0.2896 -0.0024 0.0328  0.0345  144 VAL   A CB  
3099 C  CG1 . VAL   A 144 ? 0.1535 0.1907 0.3211 -0.0077 0.0230  0.0326  144 VAL   A CG1 
3100 C  CG2 . VAL   A 144 ? 0.1344 0.1794 0.3022 -0.0030 0.0398  0.0514  144 VAL   A CG2 
3110 N  N   . ASP   A 145 ? 0.1336 0.1438 0.2167 -0.0160 -0.0017 0.0245  145 ASP   A N   
3111 C  CA  . ASP   A 145 ? 0.1429 0.1504 0.2203 -0.0214 0.0027  0.0122  145 ASP   A CA  
3112 C  C   . ASP   A 145 ? 0.1465 0.1397 0.2258 -0.0116 0.0036  -0.0023 145 ASP   A C   
3113 O  O   . ASP   A 145 ? 0.1584 0.1451 0.2908 -0.0164 0.0041  -0.0294 145 ASP   A O   
3114 C  CB  . ASP   A 145 ? 0.1582 0.1817 0.2434 -0.0284 -0.0131 0.0040  145 ASP   A CB  
3115 C  CG  . ASP   A 145 ? 0.1749 0.2244 0.2716 -0.0498 -0.0272 0.0110  145 ASP   A CG  
3116 O  OD1 . ASP   A 145 ? 0.1645 0.2359 0.2881 -0.0595 -0.0108 0.0171  145 ASP   A OD1 
3117 O  OD2 . ASP   A 145 ? 0.1932 0.2492 0.2797 -0.0567 -0.0499 0.0137  145 ASP   A OD2 
3122 N  N   . THR   A 146 ? 0.1291 0.1330 0.1883 -0.0129 0.0063  0.0047  146 THR   A N   
3123 C  CA  . THR   A 146 ? 0.1228 0.1297 0.1759 -0.0049 0.0059  0.0081  146 THR   A CA  
3124 C  C   . THR   A 146 ? 0.1212 0.1236 0.1829 -0.0033 0.0074  0.0143  146 THR   A C   
3125 O  O   . THR   A 146 ? 0.1299 0.1391 0.1977 0.0062  0.0013  0.0134  146 THR   A O   
3126 C  CB  . THR   A 146 ? 0.1282 0.1330 0.1761 -0.0035 0.0099  0.0107  146 THR   A CB  
3127 O  OG1 . THR   A 146 ? 0.1291 0.1530 0.1801 -0.0027 0.0060  0.0067  146 THR   A OG1 
3128 C  CG2 . THR   A 146 ? 0.1281 0.1351 0.1899 -0.0085 0.0075  0.0080  146 THR   A CG2 
3136 N  N   . VAL   A 147 ? 0.1175 0.1316 0.1772 0.0004  0.0110  0.0184  147 VAL   A N   
3137 C  CA  . VAL   A 147 ? 0.1207 0.1365 0.1725 -0.0102 0.0216  0.0242  147 VAL   A CA  
3138 C  C   . VAL   A 147 ? 0.1217 0.1270 0.1869 -0.0108 0.0171  0.0275  147 VAL   A C   
3139 O  O   . VAL   A 147 ? 0.1258 0.1368 0.2017 -0.0140 0.0093  0.0266  147 VAL   A O   
3140 C  CB  . VAL   A 147 ? 0.1279 0.1372 0.1701 -0.0069 0.0179  0.0272  147 VAL   A CB  
3141 C  CG1 . VAL   A 147 ? 0.1538 0.1412 0.1814 -0.0072 0.0166  0.0345  147 VAL   A CG1 
3142 C  CG2 . VAL   A 147 ? 0.1311 0.1309 0.1639 -0.0077 0.0075  0.0176  147 VAL   A CG2 
3152 N  N   . ARG   A 148 ? 0.1215 0.1282 0.1966 -0.0107 0.0207  0.0424  148 ARG   A N   
3153 C  CA  . ARG   A 148 ? 0.1258 0.1282 0.1912 -0.0090 0.0133  0.0428  148 ARG   A CA  
3154 C  C   . ARG   A 148 ? 0.1368 0.1307 0.1983 -0.0083 0.0140  0.0565  148 ARG   A C   
3155 O  O   . ARG   A 148 ? 0.1644 0.1503 0.2097 -0.0123 0.0208  0.0496  148 ARG   A O   
3156 C  CB  . ARG   A 148 ? 0.1360 0.1323 0.2088 -0.0064 0.0234  0.0351  148 ARG   A CB  
3157 C  CG  . ARG   A 148 ? 0.1568 0.1324 0.2363 -0.0079 0.0410  0.0324  148 ARG   A CG  
3158 C  CD  . ARG   A 148 ? 0.1732 0.1355 0.2547 -0.0024 0.0450  0.0455  148 ARG   A CD  
3159 N  NE  . ARG   A 148 ? 0.1647 0.1394 0.2560 0.0065  0.0450  0.0465  148 ARG   A NE  
3160 C  CZ  . ARG   A 148 ? 0.1598 0.1304 0.2413 0.0056  0.0429  0.0437  148 ARG   A CZ  
3161 N  NH1 . ARG   A 148 ? 0.1636 0.1298 0.2494 -0.0080 0.0391  0.0186  148 ARG   A NH1 
3162 N  NH2 . ARG   A 148 ? 0.1536 0.1509 0.2377 0.0148  0.0406  0.0444  148 ARG   A NH2 
3176 N  N   . THR   A 149 ? 0.1362 0.1427 0.1903 -0.0124 0.0019  0.0460  149 THR   A N   
3177 C  CA  . THR   A 149 ? 0.1382 0.1512 0.1904 -0.0097 0.0078  0.0430  149 THR   A CA  
3178 C  C   . THR   A 149 ? 0.1321 0.1481 0.1835 -0.0141 0.0073  0.0521  149 THR   A C   
3179 O  O   . THR   A 149 ? 0.1311 0.1561 0.1967 -0.0169 0.0105  0.0488  149 THR   A O   
3180 C  CB  . THR   A 149 ? 0.1385 0.1571 0.1872 -0.0126 0.0063  0.0388  149 THR   A CB  
3181 O  OG1 . THR   A 149 ? 0.1406 0.1489 0.1910 -0.0207 0.0055  0.0362  149 THR   A OG1 
3182 C  CG2 . THR   A 149 ? 0.1370 0.1702 0.2111 -0.0067 0.0006  0.0341  149 THR   A CG2 
3190 N  N   . ASN   A 150 ? 0.1402 0.1507 0.1909 -0.0012 0.0025  0.0585  150 ASN   A N   
3191 C  CA  . ASN   A 150 ? 0.1481 0.1592 0.1770 -0.0054 0.0073  0.0524  150 ASN   A CA  
3192 C  C   . ASN   A 150 ? 0.1316 0.1473 0.1759 -0.0083 0.0060  0.0454  150 ASN   A C   
3193 O  O   . ASN   A 150 ? 0.1426 0.1583 0.2106 -0.0118 -0.0134 0.0428  150 ASN   A O   
3194 C  CB  . ASN   A 150 ? 0.1929 0.1804 0.2088 -0.0123 0.0257  0.0727  150 ASN   A CB  
3195 C  CG  . ASN   A 150 ? 0.2465 0.2128 0.2834 -0.0070 0.0200  0.0792  150 ASN   A CG  
3196 O  OD1 . ASN   A 150 ? 0.2668 0.2151 0.3026 -0.0153 0.0228  0.0946  150 ASN   A OD1 
3197 N  ND2 . ASN   A 150 ? 0.2741 0.2399 0.3204 -0.0003 0.0062  0.0812  150 ASN   A ND2 
3204 N  N   . VAL   A 151 ? 0.1346 0.1338 0.1732 -0.0121 0.0048  0.0400  151 VAL   A N   
3205 C  CA  . VAL   A 151 ? 0.1392 0.1408 0.1700 -0.0150 0.0056  0.0431  151 VAL   A CA  
3206 C  C   . VAL   A 151 ? 0.1273 0.1379 0.1750 -0.0213 0.0137  0.0430  151 VAL   A C   
3207 O  O   . VAL   A 151 ? 0.1344 0.1477 0.2170 -0.0135 0.0119  0.0354  151 VAL   A O   
3208 C  CB  . VAL   A 151 ? 0.1653 0.1536 0.1730 -0.0050 0.0063  0.0419  151 VAL   A CB  
3209 C  CG1 . VAL   A 151 ? 0.1597 0.1733 0.1941 -0.0079 0.0069  0.0389  151 VAL   A CG1 
3210 C  CG2 . VAL   A 151 ? 0.1744 0.1510 0.1825 -0.0074 0.0207  0.0326  151 VAL   A CG2 
3220 N  N   . TYR   A 152 ? 0.1298 0.1373 0.1866 -0.0201 0.0132  0.0394  152 TYR   A N   
3221 C  CA  . TYR   A 152 ? 0.1321 0.1399 0.1731 -0.0179 0.0093  0.0379  152 TYR   A CA  
3222 C  C   . TYR   A 152 ? 0.1259 0.1357 0.1624 -0.0118 0.0169  0.0431  152 TYR   A C   
3223 O  O   . TYR   A 152 ? 0.1365 0.1355 0.1645 -0.0228 0.0185  0.0346  152 TYR   A O   
3224 C  CB  . TYR   A 152 ? 0.1495 0.1578 0.1668 -0.0126 0.0174  0.0479  152 TYR   A CB  
3225 C  CG  . TYR   A 152 ? 0.1590 0.1764 0.1591 -0.0189 0.0243  0.0490  152 TYR   A CG  
3226 C  CD1 . TYR   A 152 ? 0.1756 0.1962 0.1698 -0.0034 0.0291  0.0528  152 TYR   A CD1 
3227 C  CD2 . TYR   A 152 ? 0.1638 0.1872 0.1542 -0.0279 0.0220  0.0448  152 TYR   A CD2 
3228 C  CE1 . TYR   A 152 ? 0.2067 0.2094 0.1751 0.0004  0.0170  0.0600  152 TYR   A CE1 
3229 C  CE2 . TYR   A 152 ? 0.1973 0.2044 0.1710 -0.0291 0.0276  0.0489  152 TYR   A CE2 
3230 C  CZ  . TYR   A 152 ? 0.2247 0.2099 0.1667 -0.0183 0.0157  0.0739  152 TYR   A CZ  
3231 O  OH  . TYR   A 152 ? 0.2550 0.2322 0.2075 -0.0147 0.0197  0.0831  152 TYR   A OH  
3241 N  N   A LEU   A 153 ? 0.1201 0.1327 0.1839 -0.0156 0.0204  0.0463  153 LEU   A N   
3242 N  N   B LEU   A 153 ? 0.1255 0.1396 0.1620 -0.0109 0.0165  0.0413  153 LEU   A N   
3243 C  CA  A LEU   A 153 ? 0.1190 0.1263 0.1956 -0.0101 0.0153  0.0517  153 LEU   A CA  
3244 C  CA  B LEU   A 153 ? 0.1240 0.1377 0.1578 -0.0056 0.0194  0.0366  153 LEU   A CA  
3245 C  C   A LEU   A 153 ? 0.1226 0.1275 0.1964 -0.0125 0.0169  0.0382  153 LEU   A C   
3246 C  C   B LEU   A 153 ? 0.1264 0.1420 0.1552 -0.0005 0.0292  0.0280  153 LEU   A C   
3247 O  O   A LEU   A 153 ? 0.1290 0.1375 0.2397 -0.0095 0.0314  0.0332  153 LEU   A O   
3248 O  O   B LEU   A 153 ? 0.1326 0.1488 0.1787 0.0008  0.0536  0.0341  153 LEU   A O   
3249 C  CB  A LEU   A 153 ? 0.1138 0.1228 0.2006 -0.0079 0.0093  0.0388  153 LEU   A CB  
3250 C  CB  B LEU   A 153 ? 0.1191 0.1417 0.1658 -0.0016 0.0155  0.0325  153 LEU   A CB  
3251 C  CG  A LEU   A 153 ? 0.1175 0.1252 0.1948 -0.0107 0.0098  0.0279  153 LEU   A CG  
3252 C  CG  B LEU   A 153 ? 0.1253 0.1488 0.1694 -0.0022 0.0116  0.0298  153 LEU   A CG  
3253 C  CD1 A LEU   A 153 ? 0.1261 0.1120 0.1978 -0.0083 0.0031  0.0268  153 LEU   A CD1 
3254 C  CD1 B LEU   A 153 ? 0.1285 0.1489 0.1823 0.0070  0.0103  0.0286  153 LEU   A CD1 
3255 C  CD2 A LEU   A 153 ? 0.1185 0.1292 0.1664 -0.0077 0.0103  0.0075  153 LEU   A CD2 
3256 C  CD2 B LEU   A 153 ? 0.1303 0.1541 0.1606 -0.0070 0.0076  0.0279  153 LEU   A CD2 
3279 N  N   A ALA   A 154 ? 0.1234 0.1216 0.1594 -0.0103 0.0112  0.0343  154 ALA   A N   
3280 N  N   B ALA   A 154 ? 0.1212 0.1366 0.1120 -0.0038 0.0179  0.0167  154 ALA   A N   
3281 C  CA  A ALA   A 154 ? 0.1334 0.1273 0.1421 -0.0100 0.0092  0.0250  154 ALA   A CA  
3282 C  CA  B ALA   A 154 ? 0.1283 0.1390 0.1181 -0.0007 0.0044  0.0132  154 ALA   A CA  
3283 C  C   A ALA   A 154 ? 0.1252 0.1183 0.1318 -0.0071 0.0060  0.0224  154 ALA   A C   
3284 C  C   B ALA   A 154 ? 0.1213 0.1432 0.1159 -0.0022 0.0068  0.0169  154 ALA   A C   
3285 O  O   A ALA   A 154 ? 0.1392 0.1304 0.1495 -0.0073 0.0059  0.0190  154 ALA   A O   
3286 O  O   B ALA   A 154 ? 0.1284 0.1448 0.0946 -0.0133 0.0018  0.0134  154 ALA   A O   
3287 C  CB  A ALA   A 154 ? 0.1430 0.1395 0.1429 0.0006  -0.0005 0.0162  154 ALA   A CB  
3288 C  CB  B ALA   A 154 ? 0.1361 0.1401 0.1246 -0.0050 -0.0105 0.0014  154 ALA   A CB  
3299 N  N   A VAL   A 155 ? 0.1071 0.0952 0.1045 -0.0067 0.0111  0.0529  155 VAL   A N   
3300 N  N   B VAL   A 155 ? 0.1155 0.1418 0.1295 -0.0013 0.0114  0.0268  155 VAL   A N   
3301 C  CA  A VAL   A 155 ? 0.1260 0.1113 0.1658 -0.0030 -0.0048 0.0587  155 VAL   A CA  
3302 C  CA  B VAL   A 155 ? 0.1405 0.1559 0.1410 -0.0045 0.0100  0.0282  155 VAL   A CA  
3303 C  CA  T VAL   A 155 ? 0.1579 0.1435 0.2009 -0.0144 0.0019  0.0429  155 VAL   A CA  
3304 C  C   A VAL   A 155 ? 0.1260 0.1207 0.2095 0.0068  -0.0074 0.0639  155 VAL   A C   
3305 C  C   B VAL   A 155 ? 0.1479 0.1635 0.1773 0.0058  0.0018  0.0312  155 VAL   A C   
3306 C  C   T VAL   A 155 ? 0.1441 0.1432 0.2084 -0.0111 0.0163  0.0494  155 VAL   A C   
3307 O  O   A VAL   A 155 ? 0.1202 0.1208 0.2418 0.0090  0.0093  0.0433  155 VAL   A O   
3308 O  O   B VAL   A 155 ? 0.1454 0.1580 0.1649 0.0111  -0.0077 0.0087  155 VAL   A O   
3309 O  O   T VAL   A 155 ? 0.1319 0.1409 0.2254 -0.0156 0.0335  0.0417  155 VAL   A O   
3310 C  CB  A VAL   A 155 ? 0.1366 0.1239 0.1656 -0.0023 -0.0077 0.0499  155 VAL   A CB  
3311 C  CB  B VAL   A 155 ? 0.1500 0.1622 0.1220 0.0006  0.0116  0.0134  155 VAL   A CB  
3312 C  CB  T VAL   A 155 ? 0.1660 0.1479 0.1855 -0.0120 -0.0087 0.0365  155 VAL   A CB  
3313 C  CG1 A VAL   A 155 ? 0.1440 0.1336 0.1647 0.0007  -0.0046 0.0441  155 VAL   A CG1 
3314 C  CG1 B VAL   A 155 ? 0.1588 0.1681 0.1172 0.0025  0.0084  0.0145  155 VAL   A CG1 
3315 C  CG1 T VAL   A 155 ? 0.1717 0.1520 0.1758 -0.0119 -0.0060 0.0356  155 VAL   A CG1 
3316 C  CG2 A VAL   A 155 ? 0.1487 0.1351 0.1815 0.0037  -0.0183 0.0420  155 VAL   A CG2 
3317 C  CG2 B VAL   A 155 ? 0.1631 0.1708 0.1348 0.0037  0.0096  0.0034  155 VAL   A CG2 
3318 C  CG2 T VAL   A 155 ? 0.1745 0.1528 0.1962 -0.0073 -0.0184 0.0291  155 VAL   A CG2 
3344 N  N   A PHE   A 156 ? 0.1365 0.1328 0.2373 0.0138  -0.0093 0.0735  156 PHE   A N   
3345 N  N   B PHE   A 156 ? 0.1615 0.1738 0.2138 0.0069  0.0053  0.0487  156 PHE   A N   
3346 N  N   T PHE   A 156 ? 0.1491 0.1475 0.2171 -0.0024 0.0253  0.0550  156 PHE   A N   
3347 C  CA  A PHE   A 156 ? 0.1537 0.1411 0.2597 0.0174  -0.0049 0.0718  156 PHE   A CA  
3348 C  CA  B PHE   A 156 ? 0.1864 0.1793 0.2409 0.0052  0.0139  0.0576  156 PHE   A CA  
3349 C  CA  T PHE   A 156 ? 0.1615 0.1502 0.2141 0.0050  0.0325  0.0604  156 PHE   A CA  
3350 C  C   A PHE   A 156 ? 0.1468 0.1404 0.2688 0.0227  0.0025  0.0658  156 PHE   A C   
3351 C  C   B PHE   A 156 ? 0.2064 0.1975 0.2646 0.0086  0.0155  0.0618  156 PHE   A C   
3352 C  C   T PHE   A 156 ? 0.1541 0.1542 0.2120 0.0158  0.0508  0.0785  156 PHE   A C   
3353 O  O   A PHE   A 156 ? 0.1507 0.1455 0.2836 0.0177  0.0125  0.0537  156 PHE   A O   
3354 O  O   B PHE   A 156 ? 0.2059 0.2027 0.2649 0.0133  0.0153  0.0605  156 PHE   A O   
3355 O  O   T PHE   A 156 ? 0.1592 0.1618 0.2210 0.0216  0.0646  0.0690  156 PHE   A O   
3356 C  CB  A PHE   A 156 ? 0.1785 0.1561 0.2647 0.0187  -0.0081 0.0685  156 PHE   A CB  
3357 C  CB  B PHE   A 156 ? 0.1845 0.1628 0.2167 -0.0008 0.0192  0.0655  156 PHE   A CB  
3358 C  CB  T PHE   A 156 ? 0.1787 0.1510 0.2085 0.0052  0.0264  0.0451  156 PHE   A CB  
3359 C  CG  A PHE   A 156 ? 0.2033 0.1684 0.2666 0.0274  -0.0106 0.0576  156 PHE   A CG  
3360 C  CG  B PHE   A 156 ? 0.1824 0.1542 0.2008 0.0041  0.0158  0.0763  156 PHE   A CG  
3361 C  CG  T PHE   A 156 ? 0.1950 0.1603 0.2100 0.0105  0.0197  0.0357  156 PHE   A CG  
3362 C  CD1 A PHE   A 156 ? 0.2133 0.1738 0.2662 0.0296  -0.0018 0.0509  156 PHE   A CD1 
3363 C  CD1 B PHE   A 156 ? 0.1783 0.1532 0.2136 -0.0016 0.0142  0.0707  156 PHE   A CD1 
3364 C  CD1 T PHE   A 156 ? 0.2020 0.1652 0.2212 0.0115  0.0124  0.0304  156 PHE   A CD1 
3365 C  CD2 A PHE   A 156 ? 0.2167 0.1788 0.2674 0.0372  -0.0147 0.0472  156 PHE   A CD2 
3366 C  CD2 B PHE   A 156 ? 0.1907 0.1558 0.2090 0.0111  0.0090  0.0793  156 PHE   A CD2 
3367 C  CD2 T PHE   A 156 ? 0.2081 0.1699 0.2235 0.0156  0.0124  0.0293  156 PHE   A CD2 
3368 C  CE1 A PHE   A 156 ? 0.2220 0.1802 0.2695 0.0303  0.0047  0.0394  156 PHE   A CE1 
3369 C  CE1 B PHE   A 156 ? 0.1790 0.1527 0.2248 -0.0044 0.0137  0.0632  156 PHE   A CE1 
3370 C  CE1 T PHE   A 156 ? 0.2092 0.1685 0.2273 0.0111  0.0115  0.0276  156 PHE   A CE1 
3371 C  CE2 A PHE   A 156 ? 0.2263 0.1849 0.2681 0.0366  -0.0077 0.0348  156 PHE   A CE2 
3372 C  CE2 B PHE   A 156 ? 0.1946 0.1557 0.2278 0.0070  0.0058  0.0716  156 PHE   A CE2 
3373 C  CE2 T PHE   A 156 ? 0.2155 0.1741 0.2332 0.0144  0.0067  0.0248  156 PHE   A CE2 
3374 C  CZ  A PHE   A 156 ? 0.2276 0.1855 0.2700 0.0339  0.0011  0.0309  156 PHE   A CZ  
3375 C  CZ  B PHE   A 156 ? 0.1853 0.1476 0.2422 -0.0030 0.0122  0.0657  156 PHE   A CZ  
3376 C  CZ  T PHE   A 156 ? 0.2134 0.1699 0.2354 0.0111  0.0080  0.0257  156 PHE   A CZ  
3404 N  N   A ASP   A 157 ? 0.1363 0.1478 0.2630 0.0248  -0.0034 0.0752  157 ASP   A N   
3405 N  N   B ASP   A 157 ? 0.2192 0.2137 0.2780 0.0073  0.0066  0.0654  157 ASP   A N   
3406 N  N   T ASP   A 157 ? 0.1419 0.1662 0.2281 0.0163  0.0470  0.0959  157 ASP   A N   
3407 C  CA  A ASP   A 157 ? 0.1371 0.1623 0.2615 0.0205  -0.0015 0.0718  157 ASP   A CA  
3408 C  CA  B ASP   A 157 ? 0.2426 0.2377 0.2941 0.0055  0.0027  0.0613  157 ASP   A CA  
3409 C  CA  T ASP   A 157 ? 0.1439 0.1825 0.2399 0.0188  0.0404  0.1021  157 ASP   A CA  
3410 C  C   A ASP   A 157 ? 0.1246 0.1710 0.2652 0.0140  0.0059  0.0734  157 ASP   A C   
3411 C  C   B ASP   A 157 ? 0.2482 0.2475 0.3014 0.0102  0.0067  0.0429  157 ASP   A C   
3412 C  C   T ASP   A 157 ? 0.1491 0.1919 0.2396 0.0191  0.0446  0.1119  157 ASP   A C   
3413 O  O   A ASP   A 157 ? 0.1170 0.1680 0.2520 0.0139  -0.0013 0.0721  157 ASP   A O   
3414 O  O   B ASP   A 157 ? 0.2469 0.2442 0.2952 0.0125  0.0029  0.0444  157 ASP   A O   
3415 O  O   T ASP   A 157 ? 0.1437 0.1842 0.2389 0.0172  0.0442  0.1131  157 ASP   A O   
3416 C  CB  A ASP   A 157 ? 0.1459 0.1644 0.2606 0.0264  -0.0031 0.0774  157 ASP   A CB  
3417 C  CB  B ASP   A 157 ? 0.2612 0.2519 0.3045 0.0003  -0.0038 0.0749  157 ASP   A CB  
3418 C  CB  T ASP   A 157 ? 0.1447 0.1898 0.2593 0.0275  0.0336  0.0993  157 ASP   A CB  
3419 C  CG  A ASP   A 157 ? 0.1519 0.1705 0.2600 0.0309  -0.0128 0.0867  157 ASP   A CG  
3420 C  CG  B ASP   A 157 ? 0.2789 0.2672 0.3114 -0.0033 -0.0111 0.0891  157 ASP   A CG  
3421 C  CG  T ASP   A 157 ? 0.1476 0.1953 0.2700 0.0408  0.0242  0.1044  157 ASP   A CG  
3422 O  OD1 A ASP   A 157 ? 0.1575 0.1673 0.2568 0.0264  -0.0220 0.1006  157 ASP   A OD1 
3423 O  OD1 B ASP   A 157 ? 0.2888 0.2677 0.3143 -0.0117 -0.0142 0.1054  157 ASP   A OD1 
3424 O  OD1 T ASP   A 157 ? 0.1364 0.1900 0.2910 0.0481  0.0355  0.1005  157 ASP   A OD1 
3425 O  OD2 A ASP   A 157 ? 0.1441 0.1713 0.2736 0.0301  -0.0070 0.0902  157 ASP   A OD2 
3426 O  OD2 B ASP   A 157 ? 0.2827 0.2738 0.3170 -0.0028 -0.0109 0.0869  157 ASP   A OD2 
3427 O  OD2 T ASP   A 157 ? 0.1544 0.2015 0.2684 0.0452  0.0072  0.1028  157 ASP   A OD2 
3440 N  N   A LYS   A 158 ? 0.1247 0.1785 0.2858 0.0103  0.0225  0.0751  158 LYS   A N   
3441 N  N   B LYS   A 158 ? 0.2570 0.2597 0.3193 0.0117  0.0163  0.0255  158 LYS   A N   
3442 N  N   T LYS   A 158 ? 0.1637 0.2098 0.2557 0.0257  0.0500  0.1098  158 LYS   A N   
3443 C  CA  A LYS   A 158 ? 0.1232 0.1895 0.2957 0.0169  0.0315  0.0738  158 LYS   A CA  
3444 C  CA  B LYS   A 158 ? 0.2620 0.2699 0.3348 0.0149  0.0245  0.0115  158 LYS   A CA  
3445 C  CA  T LYS   A 158 ? 0.1763 0.2286 0.2697 0.0401  0.0461  0.1038  158 LYS   A CA  
3446 C  C   A LYS   A 158 ? 0.1101 0.1990 0.2860 0.0176  0.0194  0.0854  158 LYS   A C   
3447 C  C   B LYS   A 158 ? 0.2507 0.2675 0.3219 0.0135  0.0102  -0.0031 158 LYS   A C   
3448 C  C   T LYS   A 158 ? 0.1737 0.2415 0.2626 0.0418  0.0282  0.1085  158 LYS   A C   
3449 O  O   A LYS   A 158 ? 0.1008 0.1977 0.2955 0.0075  0.0206  0.0896  158 LYS   A O   
3450 O  O   B LYS   A 158 ? 0.2522 0.2684 0.3292 0.0123  0.0204  -0.0127 158 LYS   A O   
3451 O  O   T LYS   A 158 ? 0.1670 0.2426 0.2640 0.0361  0.0299  0.1164  158 LYS   A O   
3452 C  CB  A LYS   A 158 ? 0.1381 0.1945 0.3117 0.0184  0.0544  0.0686  158 LYS   A CB  
3453 C  CB  B LYS   A 158 ? 0.2775 0.2776 0.3565 0.0160  0.0462  0.0175  158 LYS   A CB  
3454 C  CB  T LYS   A 158 ? 0.1941 0.2365 0.2957 0.0457  0.0606  0.0906  158 LYS   A CB  
3455 C  CG  A LYS   A 158 ? 0.1546 0.2011 0.3262 0.0213  0.0637  0.0727  158 LYS   A CG  
3456 C  CG  B LYS   A 158 ? 0.2914 0.2860 0.3764 0.0169  0.0634  0.0261  158 LYS   A CG  
3457 C  CG  T LYS   A 158 ? 0.2116 0.2457 0.3245 0.0500  0.0633  0.0842  158 LYS   A CG  
3458 C  CD  A LYS   A 158 ? 0.1644 0.2094 0.3361 0.0218  0.0789  0.0800  158 LYS   A CD  
3459 C  CD  B LYS   A 158 ? 0.3006 0.2928 0.3855 0.0174  0.0829  0.0350  158 LYS   A CD  
3460 C  CD  T LYS   A 158 ? 0.2259 0.2526 0.3550 0.0523  0.0629  0.0836  158 LYS   A CD  
3461 C  CE  A LYS   A 158 ? 0.1671 0.2149 0.3385 0.0193  0.0976  0.0936  158 LYS   A CE  
3462 C  CE  B LYS   A 158 ? 0.3055 0.2953 0.3889 0.0168  0.1003  0.0456  158 LYS   A CE  
3463 C  CE  T LYS   A 158 ? 0.2345 0.2556 0.3748 0.0520  0.0644  0.0901  158 LYS   A CE  
3464 N  NZ  A LYS   A 158 ? 0.1687 0.2169 0.3393 0.0152  0.1038  0.1006  158 LYS   A NZ  
3465 N  NZ  B LYS   A 158 ? 0.3078 0.2970 0.3946 0.0152  0.1084  0.0527  158 LYS   A NZ  
3466 N  NZ  T LYS   A 158 ? 0.2390 0.2571 0.3855 0.0500  0.0669  0.0951  158 LYS   A NZ  
3506 N  N   A ASN   A 159 ? 0.1185 0.2172 0.2891 0.0147  0.0056  0.0835  159 ASN   A N   
3507 N  N   B ASN   A 159 ? 0.2382 0.2621 0.3059 0.0098  -0.0121 -0.0113 159 ASN   A N   
3508 N  N   T ASN   A 159 ? 0.1857 0.2555 0.2767 0.0329  0.0163  0.0951  159 ASN   A N   
3509 C  CA  A ASN   A 159 ? 0.1214 0.2287 0.2723 0.0240  -0.0214 0.0917  159 ASN   A CA  
3510 C  CA  B ASN   A 159 ? 0.2234 0.2586 0.2903 0.0076  -0.0344 -0.0123 159 ASN   A CA  
3511 C  CA  T ASN   A 159 ? 0.1969 0.2678 0.2744 0.0232  0.0017  0.0833  159 ASN   A CA  
3512 C  C   A ASN   A 159 ? 0.1063 0.2142 0.2389 0.0064  -0.0292 0.0976  159 ASN   A C   
3513 C  C   B ASN   A 159 ? 0.2051 0.2537 0.2690 0.0084  -0.0306 -0.0142 159 ASN   A C   
3514 C  C   T ASN   A 159 ? 0.2019 0.2693 0.2558 0.0002  0.0017  0.0633  159 ASN   A C   
3515 O  O   A ASN   A 159 ? 0.1010 0.2247 0.2371 0.0003  -0.0396 0.0970  159 ASN   A O   
3516 O  O   B ASN   A 159 ? 0.2020 0.2495 0.2543 0.0123  -0.0349 -0.0206 159 ASN   A O   
3517 O  O   T ASN   A 159 ? 0.2059 0.2804 0.2540 -0.0029 -0.0042 0.0509  159 ASN   A O   
3518 C  CB  A ASN   A 159 ? 0.1413 0.2477 0.2979 0.0305  -0.0315 0.0845  159 ASN   A CB  
3519 C  CB  B ASN   A 159 ? 0.2308 0.2666 0.3070 0.0021  -0.0402 -0.0083 159 ASN   A CB  
3520 C  CB  T ASN   A 159 ? 0.2026 0.2760 0.2986 0.0254  -0.0105 0.0857  159 ASN   A CB  
3521 C  CG  A ASN   A 159 ? 0.1689 0.2645 0.3289 0.0272  -0.0243 0.0695  159 ASN   A CG  
3522 C  CG  B ASN   A 159 ? 0.2411 0.2746 0.3304 -0.0016 -0.0378 0.0026  159 ASN   A CG  
3523 C  CG  T ASN   A 159 ? 0.2120 0.2817 0.3250 0.0238  -0.0130 0.0814  159 ASN   A CG  
3524 O  OD1 A ASN   A 159 ? 0.1707 0.2684 0.3418 0.0234  -0.0160 0.0656  159 ASN   A OD1 
3525 O  OD1 B ASN   A 159 ? 0.2481 0.2829 0.3536 0.0020  -0.0331 0.0001  159 ASN   A OD1 
3526 O  OD1 T ASN   A 159 ? 0.2108 0.2827 0.3371 0.0203  -0.0060 0.0802  159 ASN   A OD1 
3527 N  ND2 A ASN   A 159 ? 0.1880 0.2739 0.3449 0.0205  -0.0192 0.0557  159 ASN   A ND2 
3528 N  ND2 B ASN   A 159 ? 0.2422 0.2743 0.3318 0.0027  -0.0349 0.0192  159 ASN   A ND2 
3529 N  ND2 T ASN   A 159 ? 0.2200 0.2868 0.3381 0.0214  -0.0146 0.0734  159 ASN   A ND2 
3548 N  N   A LEU   A 160 ? 0.0949 0.1902 0.2205 -0.0067 -0.0360 0.0973  160 LEU   A N   
3549 N  N   B LEU   A 160 ? 0.1898 0.2458 0.2556 0.0077  -0.0226 -0.0118 160 LEU   A N   
3550 N  N   T LEU   A 160 ? 0.2001 0.2573 0.2482 -0.0186 -0.0030 0.0561  160 LEU   A N   
3551 C  CA  A LEU   A 160 ? 0.1078 0.1744 0.1965 -0.0175 -0.0237 0.0949  160 LEU   A CA  
3552 C  CA  B LEU   A 160 ? 0.1788 0.2356 0.2313 -0.0014 -0.0147 0.0013  160 LEU   A CA  
3553 C  CA  T LEU   A 160 ? 0.2051 0.2474 0.2342 -0.0367 -0.0048 0.0534  160 LEU   A CA  
3554 C  C   A LEU   A 160 ? 0.0923 0.1671 0.1727 -0.0163 -0.0169 0.0853  160 LEU   A C   
3555 C  C   B LEU   A 160 ? 0.1501 0.2237 0.1887 -0.0028 0.0011  0.0036  160 LEU   A C   
3556 O  O   A LEU   A 160 ? 0.0875 0.1612 0.1735 -0.0213 -0.0138 0.0638  160 LEU   A O   
3557 O  O   B LEU   A 160 ? 0.1397 0.2346 0.1752 -0.0044 0.0004  -0.0058 160 LEU   A O   
3558 C  CB  A LEU   A 160 ? 0.1247 0.1748 0.1830 -0.0304 -0.0235 0.0922  160 LEU   A CB  
3559 C  CB  B LEU   A 160 ? 0.1921 0.2393 0.2514 -0.0123 -0.0096 0.0096  160 LEU   A CB  
3560 C  CB  T LEU   A 160 ? 0.2071 0.2394 0.2178 -0.0521 -0.0068 0.0500  160 LEU   A CB  
3561 C  CG  A LEU   A 160 ? 0.1375 0.1820 0.1940 -0.0418 -0.0278 0.0719  160 LEU   A CG  
3562 C  CG  B LEU   A 160 ? 0.2081 0.2454 0.2711 -0.0197 0.0028  0.0064  160 LEU   A CG  
3563 C  CG  T LEU   A 160 ? 0.2104 0.2364 0.2150 -0.0646 -0.0093 0.0409  160 LEU   A CG  
3564 C  CD1 A LEU   A 160 ? 0.1432 0.1905 0.2037 -0.0410 -0.0193 0.0650  160 LEU   A CD1 
3565 C  CD1 B LEU   A 160 ? 0.2136 0.2480 0.2763 -0.0274 0.0005  0.0028  160 LEU   A CD1 
3566 C  CD1 T LEU   A 160 ? 0.2123 0.2393 0.2161 -0.0653 -0.0060 0.0384  160 LEU   A CD1 
3567 C  CD2 A LEU   A 160 ? 0.1407 0.1785 0.1912 -0.0418 -0.0308 0.0690  160 LEU   A CD2 
3568 C  CD2 B LEU   A 160 ? 0.2122 0.2478 0.2754 -0.0202 0.0100  0.0076  160 LEU   A CD2 
3569 C  CD2 T LEU   A 160 ? 0.2117 0.2314 0.2093 -0.0678 -0.0107 0.0381  160 LEU   A CD2 
3602 N  N   A TYR   A 161 ? 0.1149 0.1820 0.1995 -0.0107 0.0014  0.0674  161 TYR   A N   
3603 N  N   B TYR   A 161 ? 0.1423 0.2023 0.1760 0.0012  0.0097  -0.0088 161 TYR   A N   
3604 C  CA  A TYR   A 161 ? 0.1260 0.1733 0.1886 -0.0117 0.0070  0.0635  161 TYR   A CA  
3605 C  CA  B TYR   A 161 ? 0.1386 0.1886 0.1707 0.0014  0.0130  -0.0176 161 TYR   A CA  
3606 C  C   A TYR   A 161 ? 0.1251 0.1760 0.1991 -0.0057 0.0040  0.0544  161 TYR   A C   
3607 C  C   B TYR   A 161 ? 0.1369 0.1972 0.1832 -0.0012 0.0183  -0.0284 161 TYR   A C   
3608 O  O   A TYR   A 161 ? 0.1249 0.1784 0.2010 -0.0121 0.0097  0.0560  161 TYR   A O   
3609 O  O   B TYR   A 161 ? 0.1268 0.1952 0.1907 -0.0021 0.0294  -0.0288 161 TYR   A O   
3610 C  CB  A TYR   A 161 ? 0.1354 0.1664 0.1837 -0.0101 0.0087  0.0520  161 TYR   A CB  
3611 C  CB  B TYR   A 161 ? 0.1387 0.1731 0.1773 0.0011  0.0223  -0.0198 161 TYR   A CB  
3612 C  CG  A TYR   A 161 ? 0.1377 0.1628 0.1883 -0.0096 -0.0003 0.0317  161 TYR   A CG  
3613 C  CG  B TYR   A 161 ? 0.1303 0.1615 0.1754 0.0046  0.0208  -0.0132 161 TYR   A CG  
3614 C  CD1 A TYR   A 161 ? 0.1392 0.1659 0.1882 -0.0033 -0.0063 0.0195  161 TYR   A CD1 
3615 C  CD1 B TYR   A 161 ? 0.1302 0.1566 0.1776 0.0028  0.0218  -0.0185 161 TYR   A CD1 
3616 C  CD2 A TYR   A 161 ? 0.1439 0.1644 0.1957 -0.0017 -0.0035 0.0279  161 TYR   A CD2 
3617 C  CD2 B TYR   A 161 ? 0.1299 0.1598 0.1756 0.0158  0.0180  -0.0036 161 TYR   A CD2 
3618 C  CE1 A TYR   A 161 ? 0.1461 0.1607 0.1937 0.0028  -0.0106 0.0285  161 TYR   A CE1 
3619 C  CE1 B TYR   A 161 ? 0.1366 0.1565 0.1856 0.0043  0.0133  -0.0138 161 TYR   A CE1 
3620 C  CE2 A TYR   A 161 ? 0.1483 0.1653 0.1959 -0.0031 -0.0054 0.0399  161 TYR   A CE2 
3621 C  CE2 B TYR   A 161 ? 0.1354 0.1584 0.1767 0.0067  0.0166  0.0030  161 TYR   A CE2 
3622 C  CZ  A TYR   A 161 ? 0.1561 0.1595 0.1993 -0.0092 -0.0186 0.0471  161 TYR   A CZ  
3623 C  CZ  B TYR   A 161 ? 0.1443 0.1608 0.1861 0.0063  0.0130  -0.0003 161 TYR   A CZ  
3624 O  OH  A TYR   A 161 ? 0.1809 0.1653 0.2205 -0.0170 -0.0234 0.0543  161 TYR   A OH  
3625 O  OH  B TYR   A 161 ? 0.1630 0.1674 0.2043 0.0074  -0.0044 0.0080  161 TYR   A OH  
3644 N  N   A ASP   A 162 ? 0.1244 0.1771 0.2214 -0.0067 0.0097  0.0538  162 ASP   A N   
3645 N  N   B ASP   A 162 ? 0.1395 0.2087 0.1904 -0.0046 0.0161  -0.0357 162 ASP   A N   
3646 C  CA  A ASP   A 162 ? 0.1275 0.1904 0.2271 -0.0121 0.0126  0.0424  162 ASP   A CA  
3647 C  CA  B ASP   A 162 ? 0.1423 0.2200 0.2033 -0.0036 0.0187  -0.0447 162 ASP   A CA  
3648 C  C   A ASP   A 162 ? 0.1253 0.2033 0.2157 -0.0161 0.0155  0.0456  162 ASP   A C   
3649 C  C   B ASP   A 162 ? 0.1472 0.2260 0.2039 -0.0014 0.0187  -0.0615 162 ASP   A C   
3650 O  O   A ASP   A 162 ? 0.1280 0.2032 0.2194 -0.0310 0.0076  0.0433  162 ASP   A O   
3651 O  O   B ASP   A 162 ? 0.1470 0.2261 0.2185 0.0016  0.0160  -0.0642 162 ASP   A O   
3652 C  CB  A ASP   A 162 ? 0.1383 0.2013 0.2460 -0.0116 0.0164  0.0224  162 ASP   A CB  
3653 C  CB  B ASP   A 162 ? 0.1446 0.2244 0.2175 -0.0073 0.0249  -0.0420 162 ASP   A CB  
3654 C  CG  A ASP   A 162 ? 0.1569 0.2137 0.2662 -0.0072 0.0152  0.0012  162 ASP   A CG  
3655 C  CG  B ASP   A 162 ? 0.1487 0.2302 0.2353 -0.0101 0.0292  -0.0420 162 ASP   A CG  
3656 O  OD1 A ASP   A 162 ? 0.1722 0.2181 0.2721 -0.0157 0.0202  -0.0035 162 ASP   A OD1 
3657 O  OD1 B ASP   A 162 ? 0.1615 0.2290 0.2316 -0.0205 0.0222  -0.0465 162 ASP   A OD1 
3658 O  OD2 A ASP   A 162 ? 0.1688 0.2212 0.2765 0.0039  0.0052  -0.0154 162 ASP   A OD2 
3659 O  OD2 B ASP   A 162 ? 0.1553 0.2355 0.2611 0.0019  0.0274  -0.0428 162 ASP   A OD2 
3668 N  N   A LYS   A 163 ? 0.1261 0.2097 0.2232 -0.0184 -0.0085 0.0407  163 LYS   A N   
3669 N  N   B LYS   A 163 ? 0.1570 0.2335 0.2051 0.0004  0.0095  -0.0720 163 LYS   A N   
3670 C  CA  A LYS   A 163 ? 0.1429 0.2239 0.2138 -0.0176 -0.0131 0.0424  163 LYS   A CA  
3671 C  CA  B LYS   A 163 ? 0.1689 0.2455 0.2125 -0.0063 -0.0071 -0.0584 163 LYS   A CA  
3672 C  C   A LYS   A 163 ? 0.1409 0.2072 0.2069 -0.0287 0.0036  0.0337  163 LYS   A C   
3673 C  C   B LYS   A 163 ? 0.1582 0.2414 0.1923 -0.0141 0.0010  -0.0527 163 LYS   A C   
3674 O  O   A LYS   A 163 ? 0.1454 0.2215 0.2232 -0.0309 -0.0057 0.0105  163 LYS   A O   
3675 O  O   B LYS   A 163 ? 0.1545 0.2418 0.2033 -0.0201 0.0027  -0.0654 163 LYS   A O   
3676 C  CB  A LYS   A 163 ? 0.1759 0.2554 0.2583 -0.0029 -0.0283 0.0421  163 LYS   A CB  
3677 C  CB  B LYS   A 163 ? 0.2009 0.2655 0.2578 -0.0020 -0.0121 -0.0481 163 LYS   A CB  
3678 C  CG  A LYS   A 163 ? 0.2130 0.2819 0.3169 -0.0022 -0.0231 0.0438  163 LYS   A CG  
3679 C  CG  B LYS   A 163 ? 0.2305 0.2819 0.3025 -0.0041 -0.0073 -0.0374 163 LYS   A CG  
3680 C  CD  A LYS   A 163 ? 0.2429 0.3002 0.3741 0.0028  -0.0211 0.0429  163 LYS   A CD  
3681 C  CD  B LYS   A 163 ? 0.2530 0.2962 0.3431 -0.0067 -0.0020 -0.0289 163 LYS   A CD  
3682 C  CE  A LYS   A 163 ? 0.2690 0.3112 0.4207 0.0052  -0.0154 0.0454  163 LYS   A CE  
3683 C  CE  B LYS   A 163 ? 0.2684 0.3056 0.3763 -0.0086 0.0004  -0.0224 163 LYS   A CE  
3684 N  NZ  A LYS   A 163 ? 0.2792 0.3170 0.4477 0.0060  -0.0119 0.0480  163 LYS   A NZ  
3685 N  NZ  B LYS   A 163 ? 0.2760 0.3092 0.3928 -0.0090 0.0035  -0.0178 163 LYS   A NZ  
3712 N  N   A LEU   A 164 ? 0.1352 0.1899 0.2002 -0.0352 -0.0065 0.0375  164 LEU   A N   
3713 N  N   B LEU   A 164 ? 0.1405 0.2291 0.1753 -0.0169 0.0133  -0.0374 164 LEU   A N   
3714 C  CA  A LEU   A 164 ? 0.1381 0.1837 0.1931 -0.0298 0.0094  0.0386  164 LEU   A CA  
3715 C  CA  B LEU   A 164 ? 0.1378 0.2152 0.1656 -0.0316 0.0265  -0.0289 164 LEU   A CA  
3716 C  C   A LEU   A 164 ? 0.1510 0.1793 0.1941 -0.0255 0.0112  0.0407  164 LEU   A C   
3717 C  C   B LEU   A 164 ? 0.1430 0.2093 0.1697 -0.0312 0.0363  -0.0308 164 LEU   A C   
3718 O  O   A LEU   A 164 ? 0.1564 0.1847 0.1968 -0.0293 0.0317  0.0186  164 LEU   A O   
3719 O  O   B LEU   A 164 ? 0.1503 0.2133 0.1750 -0.0317 0.0433  -0.0310 164 LEU   A O   
3720 C  CB  A LEU   A 164 ? 0.1325 0.1905 0.1860 -0.0320 0.0121  0.0445  164 LEU   A CB  
3721 C  CB  B LEU   A 164 ? 0.1384 0.2070 0.1601 -0.0374 0.0272  -0.0285 164 LEU   A CB  
3722 C  CG  A LEU   A 164 ? 0.1363 0.2012 0.1873 -0.0298 0.0121  0.0402  164 LEU   A CG  
3723 C  CG  B LEU   A 164 ? 0.1531 0.2038 0.1665 -0.0379 0.0218  -0.0234 164 LEU   A CG  
3724 C  CD1 A LEU   A 164 ? 0.1318 0.2082 0.1896 -0.0352 -0.0152 0.0389  164 LEU   A CD1 
3725 C  CD1 B LEU   A 164 ? 0.1513 0.2043 0.1708 -0.0374 0.0113  -0.0274 164 LEU   A CD1 
3726 C  CD2 A LEU   A 164 ? 0.1522 0.2082 0.1862 -0.0160 0.0245  0.0377  164 LEU   A CD2 
3727 C  CD2 B LEU   A 164 ? 0.1657 0.2011 0.1602 -0.0379 0.0405  -0.0146 164 LEU   A CD2 
3750 N  N   A VAL   A 165 ? 0.1510 0.1745 0.1887 -0.0223 0.0191  0.0384  165 VAL   A N   
3751 N  N   B VAL   A 165 ? 0.1344 0.2070 0.1706 -0.0339 0.0397  -0.0259 165 VAL   A N   
3752 C  CA  A VAL   A 165 ? 0.1541 0.1800 0.1715 -0.0213 0.0250  0.0366  165 VAL   A CA  
3753 C  CA  B VAL   A 165 ? 0.1397 0.2112 0.1763 -0.0280 0.0406  -0.0193 165 VAL   A CA  
3754 C  C   A VAL   A 165 ? 0.1461 0.1879 0.1766 -0.0185 0.0230  0.0421  165 VAL   A C   
3755 C  C   B VAL   A 165 ? 0.1306 0.2170 0.1783 -0.0198 0.0432  -0.0158 165 VAL   A C   
3756 O  O   A VAL   A 165 ? 0.1447 0.1820 0.1709 -0.0150 0.0227  0.0366  165 VAL   A O   
3757 O  O   B VAL   A 165 ? 0.1341 0.2199 0.1747 -0.0128 0.0358  -0.0171 165 VAL   A O   
3758 C  CB  A VAL   A 165 ? 0.1683 0.1826 0.1720 -0.0184 0.0251  0.0276  165 VAL   A CB  
3759 C  CB  B VAL   A 165 ? 0.1533 0.2150 0.1799 -0.0227 0.0363  -0.0215 165 VAL   A CB  
3760 C  CG1 A VAL   A 165 ? 0.1742 0.1903 0.1737 -0.0241 0.0344  0.0256  165 VAL   A CG1 
3761 C  CG1 B VAL   A 165 ? 0.1592 0.2160 0.1889 -0.0285 0.0365  -0.0236 165 VAL   A CG1 
3762 C  CG2 A VAL   A 165 ? 0.1790 0.1810 0.1753 -0.0170 0.0143  0.0306  165 VAL   A CG2 
3763 C  CG2 B VAL   A 165 ? 0.1617 0.2168 0.1820 -0.0175 0.0313  -0.0224 165 VAL   A CG2 
3782 N  N   A SER   A 166 ? 0.1434 0.1963 0.2017 -0.0179 0.0141  0.0418  166 SER   A N   
3783 N  N   B SER   A 166 ? 0.1180 0.2264 0.1992 -0.0223 0.0497  -0.0069 166 SER   A N   
3784 C  CA  A SER   A 166 ? 0.1435 0.2275 0.2324 -0.0214 0.0186  0.0399  166 SER   A CA  
3785 C  CA  B SER   A 166 ? 0.1217 0.2407 0.2117 -0.0251 0.0432  -0.0001 166 SER   A CA  
3786 C  C   A SER   A 166 ? 0.1358 0.2583 0.2323 -0.0257 0.0170  0.0377  166 SER   A C   
3787 C  C   B SER   A 166 ? 0.1425 0.2585 0.2277 -0.0230 0.0253  -0.0008 166 SER   A C   
3788 O  O   A SER   A 166 ? 0.1477 0.2617 0.2823 -0.0330 0.0231  0.0004  166 SER   A O   
3789 O  O   B SER   A 166 ? 0.1549 0.2667 0.2503 -0.0234 0.0382  -0.0171 166 SER   A O   
3790 C  CB  A SER   A 166 ? 0.1663 0.2379 0.2636 -0.0163 0.0148  0.0386  166 SER   A CB  
3791 C  CB  B SER   A 166 ? 0.1191 0.2440 0.2318 -0.0136 0.0333  -0.0028 166 SER   A CB  
3792 O  OG  A SER   A 166 ? 0.1914 0.2520 0.2968 -0.0178 0.0131  0.0505  166 SER   A OG  
3793 O  OG  B SER   A 166 ? 0.1258 0.2449 0.2657 -0.0085 0.0097  0.0074  166 SER   A OG  
3804 N  N   A SER   A 167 ? 0.1347 0.2833 0.1943 -0.0137 -0.0034 0.0594  167 SER   A N   
3805 N  N   B SER   A 167 ? 0.1627 0.2732 0.2388 -0.0126 0.0033  0.0065  167 SER   A N   
3806 C  CA  A SER   A 167 ? 0.1525 0.3087 0.2017 -0.0007 -0.0009 0.0574  167 SER   A CA  
3807 C  CA  B SER   A 167 ? 0.1897 0.2838 0.2674 -0.0062 0.0019  0.0071  167 SER   A CA  
3808 C  C   A SER   A 167 ? 0.1510 0.3056 0.1983 0.0092  -0.0035 0.0563  167 SER   A C   
3809 C  C   B SER   A 167 ? 0.2021 0.2870 0.2981 -0.0146 0.0087  0.0083  167 SER   A C   
3810 O  O   A SER   A 167 ? 0.1527 0.3134 0.1886 0.0143  -0.0013 0.0434  167 SER   A O   
3811 O  O   B SER   A 167 ? 0.2152 0.2983 0.3249 -0.0246 0.0046  0.0050  167 SER   A O   
3812 C  CB  A SER   A 167 ? 0.1549 0.3328 0.2073 0.0090  0.0185  0.0570  167 SER   A CB  
3813 C  CB  B SER   A 167 ? 0.2001 0.2897 0.2733 0.0099  0.0084  0.0066  167 SER   A CB  
3814 O  OG  A SER   A 167 ? 0.1516 0.3472 0.2157 0.0120  0.0399  0.0643  167 SER   A OG  
3815 O  OG  B SER   A 167 ? 0.2064 0.2919 0.2751 0.0226  0.0128  0.0130  167 SER   A OG  
3826 N  N   A PHE   A 168 ? 0.1503 0.2964 0.2099 0.0160  0.0095  0.0624  168 PHE   A N   
3827 N  N   B PHE   A 168 ? 0.1965 0.2785 0.2868 -0.0167 0.0199  0.0121  168 PHE   A N   
3828 C  CA  A PHE   A 168 ? 0.1511 0.2921 0.2292 0.0123  0.0230  0.0483  168 PHE   A CA  
3829 C  CA  B PHE   A 168 ? 0.1990 0.2738 0.2677 -0.0159 0.0255  0.0076  168 PHE   A CA  
3830 C  C   A PHE   A 168 ? 0.1581 0.3043 0.2651 0.0037  0.0541  0.0309  168 PHE   A C   
3831 C  C   B PHE   A 168 ? 0.2118 0.2840 0.2874 -0.0121 0.0488  0.0131  168 PHE   A C   
3832 O  O   A PHE   A 168 ? 0.1588 0.3107 0.3063 0.0035  0.0592  0.0439  168 PHE   A O   
3833 O  O   B PHE   A 168 ? 0.2090 0.2843 0.2859 -0.0114 0.0733  0.0154  168 PHE   A O   
3834 C  CB  A PHE   A 168 ? 0.1508 0.2779 0.2316 0.0045  0.0123  0.0517  168 PHE   A CB  
3835 C  CB  B PHE   A 168 ? 0.1996 0.2636 0.2456 -0.0217 0.0045  0.0069  168 PHE   A CB  
3836 C  CG  A PHE   A 168 ? 0.1456 0.2697 0.2291 -0.0072 0.0081  0.0673  168 PHE   A CG  
3837 C  CG  B PHE   A 168 ? 0.1957 0.2487 0.2185 -0.0288 -0.0186 0.0121  168 PHE   A CG  
3838 C  CD1 A PHE   A 168 ? 0.1473 0.2669 0.2340 -0.0151 0.0067  0.0787  168 PHE   A CD1 
3839 C  CD1 B PHE   A 168 ? 0.1908 0.2439 0.2032 -0.0326 -0.0339 0.0180  168 PHE   A CD1 
3840 C  CD2 A PHE   A 168 ? 0.1436 0.2709 0.2304 -0.0111 0.0225  0.0721  168 PHE   A CD2 
3841 C  CD2 B PHE   A 168 ? 0.1975 0.2403 0.2081 -0.0296 -0.0256 0.0122  168 PHE   A CD2 
3842 C  CE1 A PHE   A 168 ? 0.1438 0.2673 0.2359 -0.0150 0.0100  0.0889  168 PHE   A CE1 
3843 C  CE1 B PHE   A 168 ? 0.1834 0.2382 0.1940 -0.0404 -0.0414 0.0180  168 PHE   A CE1 
3844 C  CE2 A PHE   A 168 ? 0.1511 0.2700 0.2391 -0.0100 0.0221  0.0816  168 PHE   A CE2 
3845 C  CE2 B PHE   A 168 ? 0.1981 0.2370 0.2011 -0.0311 -0.0299 0.0180  168 PHE   A CE2 
3846 C  CZ  A PHE   A 168 ? 0.1478 0.2692 0.2384 -0.0118 0.0174  0.0887  168 PHE   A CZ  
3847 C  CZ  B PHE   A 168 ? 0.1914 0.2359 0.1975 -0.0360 -0.0351 0.0204  168 PHE   A CZ  
3866 N  N   A LEU   A 169 ? 0.1895 0.3075 0.2858 -0.0079 0.0617  -0.0002 169 LEU   A N   
3867 N  N   B LEU   A 169 ? 0.2304 0.2979 0.3152 -0.0071 0.0413  0.0163  169 LEU   A N   
3868 C  CA  A LEU   A 169 ? 0.2272 0.3113 0.3233 -0.0046 0.0403  -0.0049 169 LEU   A CA  
3869 C  CA  B LEU   A 169 ? 0.2512 0.3137 0.3373 -0.0020 0.0319  0.0131  169 LEU   A CA  
3870 C  C   A LEU   A 169 ? 0.2248 0.3036 0.3316 -0.0028 0.0419  0.0119  169 LEU   A C   
3871 C  C   B LEU   A 169 ? 0.2625 0.3229 0.3582 0.0036  0.0271  0.0094  169 LEU   A C   
3872 O  O   A LEU   A 169 ? 0.2380 0.3060 0.3399 -0.0021 0.0366  0.0169  169 LEU   A O   
3873 O  O   B LEU   A 169 ? 0.2639 0.3280 0.3635 0.0054  0.0201  0.0069  169 LEU   A O   
3874 C  CB  A LEU   A 169 ? 0.2547 0.3204 0.3289 -0.0025 0.0301  -0.0246 169 LEU   A CB  
3875 C  CB  B LEU   A 169 ? 0.2604 0.3210 0.3372 -0.0007 0.0286  0.0136  169 LEU   A CB  
3876 C  CG  A LEU   A 169 ? 0.2800 0.3276 0.3331 -0.0020 0.0192  -0.0516 169 LEU   A CG  
3877 C  CG  B LEU   A 169 ? 0.2670 0.3268 0.3377 0.0003  0.0268  0.0151  169 LEU   A CG  
3878 C  CD1 A LEU   A 169 ? 0.2878 0.3289 0.3386 -0.0011 0.0136  -0.0594 169 LEU   A CD1 
3879 C  CD1 B LEU   A 169 ? 0.2672 0.3278 0.3339 0.0004  0.0298  0.0164  169 LEU   A CD1 
3880 C  CD2 A LEU   A 169 ? 0.2870 0.3303 0.3287 -0.0033 0.0185  -0.0631 169 LEU   A CD2 
3881 C  CD2 B LEU   A 169 ? 0.2721 0.3304 0.3457 -0.0007 0.0219  0.0145  169 LEU   A CD2 
3882 O  OXT A LEU   A 169 ? 0.2062 0.3001 0.3249 -0.0019 0.0541  0.0148  169 LEU   A OXT 
3883 O  OXT B LEU   A 169 ? 0.2715 0.3269 0.3681 0.0032  0.0296  0.0084  169 LEU   A OXT 
3906 N  N   A SER   B 1   ? 0.3775 0.3429 0.3660 -0.1065 -0.0758 0.0398  1   SER   B N   
3907 N  N   B SER   B 1   ? 0.3306 0.3254 0.3463 -0.0954 -0.0571 0.0382  1   SER   B N   
3908 C  CA  A SER   B 1   ? 0.3704 0.3472 0.3723 -0.1096 -0.0790 0.0358  1   SER   B CA  
3909 C  CA  B SER   B 1   ? 0.3232 0.3292 0.3459 -0.0981 -0.0601 0.0349  1   SER   B CA  
3910 C  C   A SER   B 1   ? 0.3471 0.3471 0.3516 -0.1098 -0.0829 0.0560  1   SER   B C   
3911 C  C   B SER   B 1   ? 0.3015 0.3290 0.3181 -0.0983 -0.0680 0.0526  1   SER   B C   
3912 O  O   A SER   B 1   ? 0.3566 0.3504 0.3311 -0.1068 -0.0759 0.0546  1   SER   B O   
3913 O  O   B SER   B 1   ? 0.3060 0.3299 0.2962 -0.0979 -0.0670 0.0498  1   SER   B O   
3914 C  CB  A SER   B 1   ? 0.3825 0.3485 0.3947 -0.1105 -0.0757 0.0187  1   SER   B CB  
3915 C  CB  B SER   B 1   ? 0.3333 0.3307 0.3707 -0.0986 -0.0528 0.0197  1   SER   B CB  
3916 O  OG  A SER   B 1   ? 0.3945 0.3569 0.4335 -0.1074 -0.0752 0.0127  1   SER   B OG  
3917 O  OG  B SER   B 1   ? 0.3428 0.3374 0.4028 -0.0969 -0.0513 0.0136  1   SER   B OG  
3932 N  N   A MET   B 2   ? 0.3177 0.3419 0.3423 -0.1082 -0.0852 0.0893  2   MET   B N   
3933 N  N   B MET   B 2   ? 0.2800 0.3274 0.3012 -0.0942 -0.0700 0.0840  2   MET   B N   
3934 C  CA  A MET   B 2   ? 0.2931 0.3401 0.3530 -0.0924 -0.0839 0.1088  2   MET   B CA  
3935 C  CA  B MET   B 2   ? 0.2629 0.3277 0.2959 -0.0770 -0.0705 0.1027  2   MET   B CA  
3936 C  C   A MET   B 2   ? 0.2512 0.3198 0.3103 -0.0790 -0.1014 0.1304  2   MET   B C   
3937 C  C   B MET   B 2   ? 0.2383 0.3133 0.2693 -0.0629 -0.0681 0.1114  2   MET   B C   
3938 O  O   A MET   B 2   ? 0.2438 0.3326 0.3050 -0.0684 -0.1160 0.1363  2   MET   B O   
3939 O  O   B MET   B 2   ? 0.2358 0.3249 0.2764 -0.0528 -0.0673 0.1039  2   MET   B O   
3940 C  CB  A MET   B 2   ? 0.3194 0.3669 0.4309 -0.0737 -0.0575 0.0867  2   MET   B CB  
3941 C  CB  B MET   B 2   ? 0.2778 0.3473 0.3321 -0.0616 -0.0697 0.1005  2   MET   B CB  
3942 C  CG  A MET   B 2   ? 0.3447 0.3910 0.5005 -0.0524 -0.0349 0.0718  2   MET   B CG  
3943 C  CG  B MET   B 2   ? 0.2908 0.3645 0.3538 -0.0442 -0.0684 0.1129  2   MET   B CG  
3944 S  SD  A MET   B 2   ? 0.3689 0.4127 0.5685 -0.0337 -0.0218 0.0622  2   MET   B SD  
3945 S  SD  B MET   B 2   ? 0.3052 0.3832 0.3690 -0.0284 -0.0731 0.1256  2   MET   B SD  
3946 C  CE  A MET   B 2   ? 0.3722 0.4198 0.5740 -0.0310 -0.0147 0.0649  2   MET   B CE  
3947 C  CE  B MET   B 2   ? 0.3052 0.3864 0.3810 -0.0276 -0.0711 0.1162  2   MET   B CE  
3966 N  N   A VAL   B 3   ? 0.2204 0.2804 0.2861 -0.0832 -0.0932 0.1385  3   VAL   B N   
3967 N  N   B VAL   B 3   ? 0.2182 0.2838 0.2459 -0.0640 -0.0607 0.1219  3   VAL   B N   
3968 C  CA  A VAL   B 3   ? 0.2098 0.2481 0.2831 -0.0720 -0.0780 0.1202  3   VAL   B CA  
3969 C  CA  B VAL   B 3   ? 0.2094 0.2583 0.2451 -0.0548 -0.0493 0.1078  3   VAL   B CA  
3970 C  C   A VAL   B 3   ? 0.1875 0.2302 0.2476 -0.0634 -0.0715 0.1037  3   VAL   B C   
3971 C  C   B VAL   B 3   ? 0.1911 0.2405 0.2272 -0.0502 -0.0508 0.1013  3   VAL   B C   
3972 O  O   A VAL   B 3   ? 0.1842 0.2254 0.2460 -0.0629 -0.0732 0.1032  3   VAL   B O   
3973 O  O   B VAL   B 3   ? 0.1897 0.2466 0.2263 -0.0393 -0.0502 0.1030  3   VAL   B O   
3974 C  CB  A VAL   B 3   ? 0.2248 0.2451 0.3301 -0.0700 -0.0673 0.1034  3   VAL   B CB  
3975 C  CB  B VAL   B 3   ? 0.2213 0.2526 0.2748 -0.0517 -0.0395 0.0933  3   VAL   B CB  
3976 C  CG1 A VAL   B 3   ? 0.2355 0.2432 0.3489 -0.0710 -0.0617 0.0995  3   VAL   B CG1 
3977 C  CG1 B VAL   B 3   ? 0.2292 0.2501 0.2885 -0.0521 -0.0334 0.0880  3   VAL   B CG1 
3978 C  CG2 A VAL   B 3   ? 0.2258 0.2490 0.3486 -0.0652 -0.0573 0.1057  3   VAL   B CG2 
3979 C  CG2 B VAL   B 3   ? 0.2218 0.2524 0.2849 -0.0495 -0.0368 0.0928  3   VAL   B CG2 
3998 N  N   . ASN   B 4   ? 0.1800 0.2156 0.2204 -0.0545 -0.0570 0.0914  4   ASN   B N   
3999 C  CA  . ASN   B 4   ? 0.1776 0.2093 0.1865 -0.0541 -0.0457 0.0509  4   ASN   B CA  
4000 C  C   . ASN   B 4   ? 0.1790 0.2255 0.1802 -0.0563 -0.0374 0.0382  4   ASN   B C   
4001 O  O   . ASN   B 4   ? 0.1821 0.2337 0.1955 -0.0544 -0.0267 0.0168  4   ASN   B O   
4002 C  CB  . ASN   B 4   ? 0.1804 0.2075 0.1601 -0.0510 -0.0519 0.0400  4   ASN   B CB  
4003 C  CG  . ASN   B 4   ? 0.1835 0.1954 0.1522 -0.0472 -0.0455 0.0381  4   ASN   B CG  
4004 O  OD1 . ASN   B 4   ? 0.1818 0.1802 0.1630 -0.0440 -0.0476 0.0289  4   ASN   B OD1 
4005 N  ND2 . ASN   B 4   ? 0.1920 0.2034 0.1597 -0.0249 -0.0333 0.0289  4   ASN   B ND2 
4013 N  N   . SER   B 5   ? 0.1897 0.2489 0.1804 -0.0571 -0.0321 0.0334  5   SER   B N   
4014 C  CA  . SER   B 5   ? 0.2201 0.2819 0.1988 -0.0462 -0.0146 0.0351  5   SER   B CA  
4015 C  C   . SER   B 5   ? 0.2393 0.2873 0.2323 -0.0635 0.0143  0.0355  5   SER   B C   
4016 O  O   . SER   B 5   ? 0.2575 0.2838 0.3158 -0.0599 0.0545  0.0350  5   SER   B O   
4017 C  CB  . SER   B 5   ? 0.2365 0.2993 0.2198 -0.0364 -0.0115 0.0448  5   SER   B CB  
4018 O  OG  . SER   B 5   ? 0.2631 0.3227 0.2719 -0.0273 -0.0049 0.0536  5   SER   B OG  
4024 N  N   . PHE   B 6   ? 0.2562 0.3052 0.2051 -0.0651 0.0254  0.0407  6   PHE   B N   
4025 C  CA  . PHE   B 6   ? 0.2688 0.3087 0.1798 -0.0842 0.0328  0.0180  6   PHE   B CA  
4026 C  C   . PHE   B 6   ? 0.3226 0.3413 0.2125 -0.0907 0.0639  -0.0100 6   PHE   B C   
4027 O  O   . PHE   B 6   ? 0.3359 0.3725 0.2523 -0.0840 0.0516  -0.0324 6   PHE   B O   
4028 C  CB  . PHE   B 6   ? 0.2396 0.2829 0.1565 -0.0786 0.0113  0.0130  6   PHE   B CB  
4029 C  CG  . PHE   B 6   ? 0.2084 0.2505 0.1533 -0.0730 -0.0036 0.0121  6   PHE   B CG  
4030 C  CD1 . PHE   B 6   ? 0.2113 0.2242 0.1373 -0.0659 -0.0080 0.0132  6   PHE   B CD1 
4031 C  CD2 . PHE   B 6   ? 0.1854 0.2478 0.1725 -0.0625 -0.0004 0.0381  6   PHE   B CD2 
4032 C  CE1 . PHE   B 6   ? 0.2044 0.1992 0.1421 -0.0578 -0.0148 0.0085  6   PHE   B CE1 
4033 C  CE2 . PHE   B 6   ? 0.1877 0.2329 0.2022 -0.0502 0.0035  0.0366  6   PHE   B CE2 
4034 C  CZ  . PHE   B 6   ? 0.1946 0.2050 0.1792 -0.0513 -0.0042 0.0179  6   PHE   B CZ  
4044 N  N   . SER   B 7   ? 0.3602 0.3240 0.2331 -0.1125 0.0974  -0.0355 7   SER   B N   
4045 C  CA  . SER   B 7   ? 0.3957 0.3297 0.2804 -0.1127 0.1194  -0.0442 7   SER   B CA  
4046 C  C   . SER   B 7   ? 0.3945 0.3181 0.2705 -0.1144 0.1363  -0.0540 7   SER   B C   
4047 O  O   . SER   B 7   ? 0.4014 0.3206 0.3044 -0.1151 0.1341  -0.0565 7   SER   B O   
4048 C  CB  . SER   B 7   ? 0.4204 0.3463 0.3487 -0.1083 0.1276  -0.0437 7   SER   B CB  
4049 O  OG  . SER   B 7   ? 0.4347 0.3560 0.4010 -0.1083 0.1249  -0.0347 7   SER   B OG  
4055 N  N   . GLY   B 8   ? 0.3921 0.3087 0.2810 -0.1003 0.1400  -0.0625 8   GLY   B N   
4056 C  CA  . GLY   B 8   ? 0.3766 0.2916 0.2781 -0.0917 0.1435  -0.0712 8   GLY   B CA  
4057 C  C   . GLY   B 8   ? 0.3531 0.2655 0.2770 -0.0878 0.1392  -0.0667 8   GLY   B C   
4058 O  O   . GLY   B 8   ? 0.3602 0.2710 0.3108 -0.0775 0.1413  -0.0735 8   GLY   B O   
4062 N  N   . TYR   B 9   ? 0.3344 0.2434 0.2501 -0.0769 0.1108  -0.0781 9   TYR   B N   
4063 C  CA  . TYR   B 9   ? 0.3117 0.2194 0.2190 -0.0654 0.0835  -0.0587 9   TYR   B CA  
4064 C  C   . TYR   B 9   ? 0.3077 0.2171 0.2029 -0.0618 0.0540  -0.0464 9   TYR   B C   
4065 O  O   . TYR   B 9   ? 0.3219 0.2354 0.2416 -0.0671 0.0522  -0.0360 9   TYR   B O   
4066 C  CB  . TYR   B 9   ? 0.2984 0.1975 0.2246 -0.0589 0.0798  -0.0536 9   TYR   B CB  
4067 C  CG  . TYR   B 9   ? 0.2861 0.1769 0.2317 -0.0627 0.0726  -0.0527 9   TYR   B CG  
4068 C  CD1 . TYR   B 9   ? 0.2901 0.1718 0.2429 -0.0768 0.0775  -0.0473 9   TYR   B CD1 
4069 C  CD2 . TYR   B 9   ? 0.2694 0.1684 0.2213 -0.0582 0.0674  -0.0539 9   TYR   B CD2 
4070 C  CE1 . TYR   B 9   ? 0.2835 0.1831 0.2429 -0.0821 0.0835  -0.0572 9   TYR   B CE1 
4071 C  CE2 . TYR   B 9   ? 0.2700 0.1666 0.2316 -0.0559 0.0678  -0.0560 9   TYR   B CE2 
4072 C  CZ  . TYR   B 9   ? 0.2752 0.1838 0.2445 -0.0723 0.0775  -0.0635 9   TYR   B CZ  
4073 O  OH  . TYR   B 9   ? 0.2755 0.1987 0.2550 -0.0869 0.0697  -0.0732 9   TYR   B OH  
4083 N  N   . LEU   B 10  ? 0.2885 0.1890 0.1859 -0.0589 0.0299  -0.0455 10  LEU   B N   
4084 C  CA  . LEU   B 10  ? 0.2850 0.1838 0.1878 -0.0706 -0.0073 -0.0430 10  LEU   B CA  
4085 C  C   . LEU   B 10  ? 0.2693 0.1859 0.1953 -0.0671 -0.0215 -0.0370 10  LEU   B C   
4086 O  O   . LEU   B 10  ? 0.2527 0.1839 0.1985 -0.0519 -0.0123 -0.0251 10  LEU   B O   
4087 C  CB  . LEU   B 10  ? 0.3027 0.1820 0.2129 -0.0744 -0.0215 -0.0233 10  LEU   B CB  
4088 C  CG  . LEU   B 10  ? 0.3239 0.1901 0.2539 -0.0734 -0.0483 -0.0143 10  LEU   B CG  
4089 C  CD1 . LEU   B 10  ? 0.3384 0.2018 0.2764 -0.0680 -0.0478 -0.0115 10  LEU   B CD1 
4090 C  CD2 . LEU   B 10  ? 0.3334 0.1951 0.2891 -0.0744 -0.0469 0.0073  10  LEU   B CD2 
4102 N  N   . LYS   B 11  ? 0.2852 0.2095 0.1914 -0.0650 -0.0289 -0.0235 11  LYS   B N   
4103 C  CA  . LYS   B 11  ? 0.3031 0.2384 0.2300 -0.0519 -0.0416 -0.0318 11  LYS   B CA  
4104 C  C   . LYS   B 11  ? 0.2866 0.2202 0.2355 -0.0688 -0.0362 -0.0388 11  LYS   B C   
4105 O  O   . LYS   B 11  ? 0.3033 0.2380 0.2655 -0.0848 -0.0341 -0.0717 11  LYS   B O   
4106 C  CB  . LYS   B 11  ? 0.3355 0.2871 0.3022 -0.0256 -0.0458 -0.0409 11  LYS   B CB  
4107 C  CG  . LYS   B 11  ? 0.3658 0.3184 0.3833 -0.0082 -0.0434 -0.0510 11  LYS   B CG  
4108 C  CD  . LYS   B 11  ? 0.3913 0.3395 0.4486 0.0033  -0.0406 -0.0582 11  LYS   B CD  
4109 C  CE  . LYS   B 11  ? 0.4095 0.3549 0.5009 0.0051  -0.0411 -0.0645 11  LYS   B CE  
4110 N  NZ  . LYS   B 11  ? 0.4198 0.3646 0.5307 0.0036  -0.0427 -0.0657 11  LYS   B NZ  
4124 N  N   . LEU   B 12  ? 0.2505 0.1907 0.2346 -0.0619 -0.0363 -0.0420 12  LEU   B N   
4125 C  CA  . LEU   B 12  ? 0.2303 0.1727 0.2495 -0.0535 -0.0312 -0.0322 12  LEU   B CA  
4126 C  C   . LEU   B 12  ? 0.2132 0.1739 0.2508 -0.0557 -0.0424 -0.0233 12  LEU   B C   
4127 O  O   . LEU   B 12  ? 0.2119 0.1780 0.2793 -0.0620 -0.0555 -0.0190 12  LEU   B O   
4128 C  CB  . LEU   B 12  ? 0.2303 0.1564 0.2452 -0.0385 -0.0217 -0.0347 12  LEU   B CB  
4129 C  CG  . LEU   B 12  ? 0.2309 0.1530 0.2516 -0.0415 -0.0121 -0.0266 12  LEU   B CG  
4130 C  CD1 . LEU   B 12  ? 0.2413 0.1569 0.2507 -0.0290 -0.0169 -0.0037 12  LEU   B CD1 
4131 C  CD2 . LEU   B 12  ? 0.2374 0.1583 0.2643 -0.0434 -0.0055 -0.0311 12  LEU   B CD2 
4143 N  N   . THR   B 13  ? 0.2038 0.1786 0.2524 -0.0563 -0.0423 -0.0307 13  THR   B N   
4144 C  CA  . THR   B 13  ? 0.2045 0.1866 0.2409 -0.0614 -0.0518 -0.0171 13  THR   B CA  
4145 C  C   . THR   B 13  ? 0.2436 0.2038 0.2546 -0.0704 -0.0661 -0.0137 13  THR   B C   
4146 O  O   . THR   B 13  ? 0.2605 0.2066 0.2603 -0.0665 -0.0299 -0.0178 13  THR   B O   
4147 C  CB  . THR   B 13  ? 0.1864 0.1893 0.2389 -0.0548 -0.0466 -0.0068 13  THR   B CB  
4148 O  OG1 . THR   B 13  ? 0.1799 0.1840 0.2551 -0.0492 -0.0408 -0.0110 13  THR   B OG1 
4149 C  CG2 . THR   B 13  ? 0.1940 0.1968 0.2422 -0.0486 -0.0302 0.0044  13  THR   B CG2 
4157 N  N   A ASP   B 14  ? 0.2568 0.2191 0.2627 -0.0734 -0.0999 -0.0018 14  ASP   B N   
4158 N  N   B ASP   B 14  ? 0.2542 0.2156 0.2622 -0.0694 -0.0844 0.0016  14  ASP   B N   
4159 C  CA  A ASP   B 14  ? 0.2687 0.2334 0.2901 -0.0727 -0.1063 0.0134  14  ASP   B CA  
4160 C  CA  B ASP   B 14  ? 0.2633 0.2261 0.2799 -0.0667 -0.0857 0.0155  14  ASP   B CA  
4161 C  C   A ASP   B 14  ? 0.2560 0.2146 0.2531 -0.0710 -0.0885 0.0174  14  ASP   B C   
4162 C  C   B ASP   B 14  ? 0.2493 0.2087 0.2490 -0.0671 -0.0792 0.0175  14  ASP   B C   
4163 O  O   A ASP   B 14  ? 0.2768 0.2239 0.2507 -0.0700 -0.0830 0.0261  14  ASP   B O   
4164 O  O   B ASP   B 14  ? 0.2620 0.2096 0.2457 -0.0681 -0.0771 0.0222  14  ASP   B O   
4165 C  CB  A ASP   B 14  ? 0.2913 0.2669 0.3789 -0.0729 -0.1197 0.0101  14  ASP   B CB  
4166 C  CB  B ASP   B 14  ? 0.2846 0.2543 0.3437 -0.0633 -0.0874 0.0177  14  ASP   B CB  
4167 C  CG  A ASP   B 14  ? 0.3189 0.2964 0.4546 -0.0683 -0.1136 -0.0029 14  ASP   B CG  
4168 C  CG  B ASP   B 14  ? 0.3073 0.2795 0.3982 -0.0586 -0.0815 0.0113  14  ASP   B CG  
4169 O  OD1 A ASP   B 14  ? 0.3351 0.3042 0.4736 -0.0717 -0.1117 -0.0155 14  ASP   B OD1 
4170 O  OD1 B ASP   B 14  ? 0.3188 0.2910 0.4122 -0.0573 -0.0772 0.0044  14  ASP   B OD1 
4171 O  OD2 A ASP   B 14  ? 0.3228 0.3086 0.4897 -0.0664 -0.1066 -0.0015 14  ASP   B OD2 
4172 O  OD2 B ASP   B 14  ? 0.3110 0.2848 0.4200 -0.0630 -0.0804 0.0123  14  ASP   B OD2 
4181 N  N   . ASN   B 15  ? 0.2204 0.1911 0.2290 -0.0620 -0.0759 0.0177  15  ASN   B N   
4182 C  CA  . ASN   B 15  ? 0.1783 0.1641 0.2158 -0.0414 -0.0538 0.0018  15  ASN   B CA  
4183 C  C   . ASN   B 15  ? 0.1590 0.1517 0.1990 -0.0286 -0.0415 0.0025  15  ASN   B C   
4184 O  O   . ASN   B 15  ? 0.1586 0.1488 0.2175 -0.0273 -0.0417 -0.0134 15  ASN   B O   
4185 C  CB  . ASN   B 15  ? 0.1729 0.1590 0.2352 -0.0195 -0.0508 0.0070  15  ASN   B CB  
4186 C  CG  . ASN   B 15  ? 0.1581 0.1599 0.2338 -0.0246 -0.0273 0.0102  15  ASN   B CG  
4187 O  OD1 . ASN   B 15  ? 0.1628 0.1859 0.2717 -0.0438 -0.0333 0.0212  15  ASN   B OD1 
4188 N  ND2 . ASN   B 15  ? 0.1606 0.1382 0.2234 -0.0167 -0.0036 -0.0038 15  ASN   B ND2 
4196 N  N   . VAL   B 16  ? 0.1645 0.1431 0.2055 -0.0343 -0.0476 -0.0007 16  VAL   B N   
4197 C  CA  . VAL   B 16  ? 0.1675 0.1453 0.1914 -0.0323 -0.0326 -0.0197 16  VAL   B CA  
4198 C  C   . VAL   B 16  ? 0.1626 0.1572 0.1878 -0.0388 -0.0315 -0.0120 16  VAL   B C   
4199 O  O   . VAL   B 16  ? 0.1643 0.1658 0.2091 -0.0369 -0.0308 -0.0192 16  VAL   B O   
4200 C  CB  . VAL   B 16  ? 0.1725 0.1438 0.1992 -0.0205 -0.0241 -0.0205 16  VAL   B CB  
4201 C  CG1 . VAL   B 16  ? 0.1849 0.1426 0.1962 -0.0068 -0.0170 -0.0188 16  VAL   B CG1 
4202 C  CG2 . VAL   B 16  ? 0.1774 0.1519 0.2235 -0.0138 -0.0212 -0.0183 16  VAL   B CG2 
4212 N  N   . TYR   B 17  ? 0.1672 0.1644 0.1900 -0.0355 -0.0259 -0.0220 17  TYR   B N   
4213 C  CA  . TYR   B 17  ? 0.1750 0.1744 0.1863 -0.0400 -0.0223 -0.0003 17  TYR   B CA  
4214 C  C   . TYR   B 17  ? 0.1674 0.1510 0.1865 -0.0420 -0.0152 -0.0070 17  TYR   B C   
4215 O  O   . TYR   B 17  ? 0.1722 0.1563 0.1880 -0.0331 -0.0211 -0.0312 17  TYR   B O   
4216 C  CB  . TYR   B 17  ? 0.2039 0.2148 0.2015 -0.0257 -0.0223 0.0361  17  TYR   B CB  
4217 C  CG  . TYR   B 17  ? 0.2310 0.2634 0.2370 -0.0171 -0.0374 0.0379  17  TYR   B CG  
4218 C  CD1 . TYR   B 17  ? 0.2492 0.2812 0.2650 -0.0135 -0.0464 0.0457  17  TYR   B CD1 
4219 C  CD2 . TYR   B 17  ? 0.2534 0.2880 0.2598 -0.0079 -0.0474 0.0352  17  TYR   B CD2 
4220 C  CE1 . TYR   B 17  ? 0.2695 0.3028 0.2840 -0.0039 -0.0588 0.0394  17  TYR   B CE1 
4221 C  CE2 . TYR   B 17  ? 0.2706 0.3056 0.2842 0.0034  -0.0656 0.0403  17  TYR   B CE2 
4222 C  CZ  . TYR   B 17  ? 0.2825 0.3167 0.2974 0.0061  -0.0698 0.0413  17  TYR   B CZ  
4223 O  OH  . TYR   B 17  ? 0.2996 0.3356 0.3185 0.0136  -0.0770 0.0450  17  TYR   B OH  
4233 N  N   . ILE   B 18  ? 0.1780 0.1517 0.1768 -0.0323 -0.0012 -0.0230 18  ILE   B N   
4234 C  CA  . ILE   B 18  ? 0.1827 0.1459 0.1843 -0.0348 -0.0036 -0.0280 18  ILE   B CA  
4235 C  C   . ILE   B 18  ? 0.1903 0.1481 0.1812 -0.0467 -0.0010 -0.0335 18  ILE   B C   
4236 O  O   . ILE   B 18  ? 0.2133 0.1653 0.1941 -0.0397 0.0098  -0.0392 18  ILE   B O   
4237 C  CB  . ILE   B 18  ? 0.1905 0.1482 0.1920 -0.0426 -0.0102 -0.0190 18  ILE   B CB  
4238 C  CG1 . ILE   B 18  ? 0.1866 0.1550 0.1962 -0.0441 0.0002  -0.0100 18  ILE   B CG1 
4239 C  CG2 . ILE   B 18  ? 0.1985 0.1527 0.2071 -0.0443 -0.0170 -0.0138 18  ILE   B CG2 
4240 C  CD1 . ILE   B 18  ? 0.1952 0.1836 0.2214 -0.0333 -0.0119 0.0137  18  ILE   B CD1 
4252 N  N   . LYS   B 19  ? 0.1937 0.1512 0.1875 -0.0269 0.0259  -0.0417 19  LYS   B N   
4253 C  CA  . LYS   B 19  ? 0.2016 0.1587 0.2125 -0.0267 0.0280  -0.0449 19  LYS   B CA  
4254 C  C   . LYS   B 19  ? 0.1815 0.1535 0.2314 -0.0265 0.0331  -0.0547 19  LYS   B C   
4255 O  O   . LYS   B 19  ? 0.1777 0.1565 0.2083 -0.0172 0.0249  -0.0425 19  LYS   B O   
4256 C  CB  . LYS   B 19  ? 0.2203 0.1761 0.2183 -0.0385 0.0429  -0.0295 19  LYS   B CB  
4257 C  CG  . LYS   B 19  ? 0.2465 0.1966 0.2492 -0.0488 0.0495  -0.0347 19  LYS   B CG  
4258 C  CD  . LYS   B 19  ? 0.2762 0.2288 0.2547 -0.0517 0.0596  -0.0334 19  LYS   B CD  
4259 C  CE  . LYS   B 19  ? 0.3017 0.2561 0.2708 -0.0495 0.0596  -0.0374 19  LYS   B CE  
4260 N  NZ  . LYS   B 19  ? 0.3166 0.2707 0.2720 -0.0530 0.0656  -0.0353 19  LYS   B NZ  
4274 N  N   . ASN   B 20  ? 0.1780 0.1647 0.2674 -0.0211 0.0441  -0.0610 20  ASN   B N   
4275 C  CA  . ASN   B 20  ? 0.1818 0.1799 0.2854 -0.0173 0.0493  -0.0794 20  ASN   B CA  
4276 C  C   . ASN   B 20  ? 0.1828 0.1984 0.2871 -0.0220 0.0607  -0.0897 20  ASN   B C   
4277 O  O   . ASN   B 20  ? 0.2047 0.2331 0.3062 -0.0355 0.0615  -0.0936 20  ASN   B O   
4278 C  CB  . ASN   B 20  ? 0.2125 0.1828 0.3225 0.0040  0.0426  -0.0745 20  ASN   B CB  
4279 C  CG  . ASN   B 20  ? 0.2420 0.1859 0.3435 0.0342  0.0414  -0.0836 20  ASN   B CG  
4280 O  OD1 . ASN   B 20  ? 0.2761 0.2115 0.3769 0.0499  0.0396  -0.0856 20  ASN   B OD1 
4281 N  ND2 . ASN   B 20  ? 0.2318 0.1860 0.3341 0.0363  0.0296  -0.0716 20  ASN   B ND2 
4288 N  N   . ALA   B 21  ? 0.1782 0.1836 0.2863 -0.0304 0.0649  -0.0648 21  ALA   B N   
4289 C  CA  . ALA   B 21  ? 0.1920 0.1882 0.2900 -0.0276 0.0500  -0.0526 21  ALA   B CA  
4290 C  C   . ALA   B 21  ? 0.1922 0.1627 0.2720 -0.0228 0.0453  -0.0415 21  ALA   B C   
4291 O  O   . ALA   B 21  ? 0.1953 0.1528 0.2708 -0.0318 0.0430  -0.0313 21  ALA   B O   
4292 C  CB  . ALA   B 21  ? 0.2113 0.2115 0.3003 -0.0345 0.0444  -0.0431 21  ALA   B CB  
4298 N  N   . ASP   B 22  ? 0.1847 0.1564 0.2667 -0.0208 0.0373  -0.0379 22  ASP   B N   
4299 C  CA  . ASP   B 22  ? 0.1779 0.1523 0.2519 -0.0073 0.0215  -0.0309 22  ASP   B CA  
4300 C  C   . ASP   B 22  ? 0.1716 0.1449 0.2098 -0.0136 0.0171  -0.0157 22  ASP   B C   
4301 O  O   . ASP   B 22  ? 0.1714 0.1468 0.2140 -0.0145 0.0159  -0.0126 22  ASP   B O   
4302 C  CB  . ASP   B 22  ? 0.1850 0.1581 0.2835 -0.0034 0.0253  -0.0094 22  ASP   B CB  
4303 C  CG  . ASP   B 22  ? 0.1887 0.1730 0.3271 -0.0004 0.0054  -0.0065 22  ASP   B CG  
4304 O  OD1 . ASP   B 22  ? 0.2010 0.1693 0.3235 0.0016  -0.0165 -0.0011 22  ASP   B OD1 
4305 O  OD2 . ASP   B 22  ? 0.1984 0.2007 0.3826 0.0086  -0.0052 -0.0202 22  ASP   B OD2 
4310 N  N   . ILE   B 23  ? 0.1749 0.1402 0.1815 -0.0121 0.0042  0.0066  23  ILE   B N   
4311 C  CA  . ILE   B 23  ? 0.1658 0.1361 0.1671 -0.0111 0.0015  0.0062  23  ILE   B CA  
4312 C  C   . ILE   B 23  ? 0.1534 0.1360 0.1668 -0.0090 -0.0033 -0.0009 23  ILE   B C   
4313 O  O   . ILE   B 23  ? 0.1468 0.1433 0.1566 -0.0112 -0.0013 0.0055  23  ILE   B O   
4314 C  CB  . ILE   B 23  ? 0.1624 0.1395 0.1752 -0.0190 0.0056  0.0134  23  ILE   B CB  
4315 C  CG1 . ILE   B 23  ? 0.1675 0.1512 0.1842 -0.0123 0.0067  0.0240  23  ILE   B CG1 
4316 C  CG2 . ILE   B 23  ? 0.1668 0.1643 0.1894 -0.0168 0.0077  0.0023  23  ILE   B CG2 
4317 C  CD1 . ILE   B 23  ? 0.1715 0.1641 0.1934 -0.0098 0.0037  0.0174  23  ILE   B CD1 
4329 N  N   . VAL   B 24  ? 0.1540 0.1379 0.1777 -0.0107 -0.0042 0.0002  24  VAL   B N   
4330 C  CA  . VAL   B 24  ? 0.1492 0.1416 0.2012 -0.0023 -0.0159 -0.0010 24  VAL   B CA  
4331 C  C   . VAL   B 24  ? 0.1466 0.1447 0.1998 -0.0130 -0.0008 0.0042  24  VAL   B C   
4332 O  O   . VAL   B 24  ? 0.1506 0.1568 0.2134 -0.0184 -0.0049 0.0087  24  VAL   B O   
4333 C  CB  . VAL   B 24  ? 0.1637 0.1637 0.2065 0.0030  -0.0227 -0.0033 24  VAL   B CB  
4334 C  CG1 . VAL   B 24  ? 0.1669 0.1664 0.2343 -0.0107 -0.0312 0.0012  24  VAL   B CG1 
4335 C  CG2 . VAL   B 24  ? 0.1669 0.1897 0.2077 0.0088  -0.0278 -0.0146 24  VAL   B CG2 
4345 N  N   . GLU   B 25  ? 0.1695 0.1584 0.2008 -0.0120 0.0038  0.0041  25  GLU   B N   
4346 C  CA  . GLU   B 25  ? 0.1781 0.1829 0.2249 -0.0047 0.0175  -0.0021 25  GLU   B CA  
4347 C  C   . GLU   B 25  ? 0.1719 0.1764 0.1917 -0.0138 0.0150  0.0024  25  GLU   B C   
4348 O  O   . GLU   B 25  ? 0.1830 0.1957 0.2022 -0.0136 0.0247  0.0069  25  GLU   B O   
4349 C  CB  . GLU   B 25  ? 0.2187 0.2235 0.2867 0.0152  0.0435  -0.0104 25  GLU   B CB  
4350 C  CG  . GLU   B 25  ? 0.2691 0.2739 0.3981 0.0251  0.0484  -0.0122 25  GLU   B CG  
4351 C  CD  . GLU   B 25  ? 0.3068 0.3229 0.5004 0.0221  0.0438  -0.0127 25  GLU   B CD  
4352 O  OE1 . GLU   B 25  ? 0.3364 0.3497 0.5296 0.0235  0.0467  -0.0097 25  GLU   B OE1 
4353 O  OE2 . GLU   B 25  ? 0.3313 0.3465 0.5315 0.0217  0.0363  -0.0175 25  GLU   B OE2 
4360 N  N   . GLU   B 26  ? 0.1698 0.1681 0.1738 -0.0272 0.0105  0.0034  26  GLU   B N   
4361 C  CA  . GLU   B 26  ? 0.1716 0.1836 0.1844 -0.0389 -0.0064 -0.0001 26  GLU   B CA  
4362 C  C   . GLU   B 26  ? 0.1542 0.1834 0.1618 -0.0278 0.0068  0.0152  26  GLU   B C   
4363 O  O   . GLU   B 26  ? 0.1775 0.2111 0.1675 -0.0219 -0.0008 0.0239  26  GLU   B O   
4364 C  CB  . GLU   B 26  ? 0.2063 0.2054 0.1996 -0.0482 -0.0009 0.0103  26  GLU   B CB  
4365 C  CG  . GLU   B 26  ? 0.2503 0.2423 0.2567 -0.0516 0.0130  -0.0114 26  GLU   B CG  
4366 C  CD  . GLU   B 26  ? 0.2714 0.2660 0.2629 -0.0725 0.0314  -0.0463 26  GLU   B CD  
4367 O  OE1 . GLU   B 26  ? 0.2905 0.2496 0.2747 -0.0816 0.0705  -0.0437 26  GLU   B OE1 
4368 O  OE2 . GLU   B 26  ? 0.2773 0.3075 0.3081 -0.0656 0.0244  -0.0484 26  GLU   B OE2 
4375 N  N   . ALA   B 27  ? 0.1472 0.1688 0.1606 -0.0230 0.0077  0.0178  27  ALA   B N   
4376 C  CA  . ALA   B 27  ? 0.1455 0.1595 0.1778 -0.0144 0.0035  0.0253  27  ALA   B CA  
4377 C  C   . ALA   B 27  ? 0.1483 0.1685 0.2009 -0.0155 0.0146  0.0354  27  ALA   B C   
4378 O  O   . ALA   B 27  ? 0.1629 0.1784 0.2048 -0.0048 0.0133  0.0454  27  ALA   B O   
4379 C  CB  . ALA   B 27  ? 0.1620 0.1465 0.1792 -0.0171 0.0107  0.0218  27  ALA   B CB  
4385 N  N   . LYS   B 28  ? 0.1452 0.1822 0.2410 -0.0233 0.0215  0.0500  28  LYS   B N   
4386 C  CA  . LYS   B 28  ? 0.1622 0.2267 0.2624 -0.0131 0.0515  0.0801  28  LYS   B CA  
4387 C  C   . LYS   B 28  ? 0.1928 0.2545 0.2500 -0.0031 0.0656  0.0711  28  LYS   B C   
4388 O  O   . LYS   B 28  ? 0.2156 0.2570 0.2643 -0.0055 0.0657  0.0690  28  LYS   B O   
4389 C  CB  . LYS   B 28  ? 0.1841 0.2581 0.3184 -0.0015 0.0719  0.1020  28  LYS   B CB  
4390 C  CG  . LYS   B 28  ? 0.2102 0.2977 0.3639 0.0065  0.0763  0.1159  28  LYS   B CG  
4391 C  CD  . LYS   B 28  ? 0.2601 0.3442 0.4232 0.0133  0.0903  0.1191  28  LYS   B CD  
4392 C  CE  . LYS   B 28  ? 0.3133 0.3904 0.4737 0.0214  0.0903  0.1239  28  LYS   B CE  
4393 N  NZ  . LYS   B 28  ? 0.3362 0.4042 0.4941 0.0277  0.0853  0.1323  28  LYS   B NZ  
4407 N  N   A LYS   B 29  ? 0.2096 0.2750 0.2514 0.0115  0.0697  0.0653  29  LYS   B N   
4408 N  N   B LYS   B 29  ? 0.2118 0.2768 0.2586 0.0058  0.0641  0.0652  29  LYS   B N   
4409 C  CA  A LYS   B 29  ? 0.2497 0.3040 0.2787 0.0133  0.0648  0.0626  29  LYS   B CA  
4410 C  CA  B LYS   B 29  ? 0.2454 0.3035 0.2824 0.0079  0.0566  0.0620  29  LYS   B CA  
4411 C  C   A LYS   B 29  ? 0.2462 0.3063 0.2382 0.0130  0.0519  0.0749  29  LYS   B C   
4412 C  C   B LYS   B 29  ? 0.2408 0.3044 0.2449 0.0088  0.0470  0.0716  29  LYS   B C   
4413 O  O   A LYS   B 29  ? 0.2625 0.3212 0.2411 0.0175  0.0493  0.0781  29  LYS   B O   
4414 O  O   B LYS   B 29  ? 0.2520 0.3156 0.2490 0.0116  0.0446  0.0727  29  LYS   B O   
4415 C  CB  A LYS   B 29  ? 0.2986 0.3328 0.3609 0.0128  0.0586  0.0432  29  LYS   B CB  
4416 C  CB  B LYS   B 29  ? 0.2864 0.3297 0.3523 0.0078  0.0497  0.0464  29  LYS   B CB  
4417 C  CG  A LYS   B 29  ? 0.3376 0.3570 0.4409 0.0126  0.0547  0.0318  29  LYS   B CG  
4418 C  CG  B LYS   B 29  ? 0.3194 0.3515 0.4199 0.0079  0.0446  0.0361  29  LYS   B CG  
4419 C  CD  A LYS   B 29  ? 0.3668 0.3744 0.5033 0.0116  0.0588  0.0222  29  LYS   B CD  
4420 C  CD  B LYS   B 29  ? 0.3431 0.3675 0.4734 0.0072  0.0445  0.0268  29  LYS   B CD  
4421 C  CE  A LYS   B 29  ? 0.3884 0.3852 0.5446 0.0105  0.0627  0.0146  29  LYS   B CE  
4422 C  CE  B LYS   B 29  ? 0.3591 0.3779 0.5101 0.0061  0.0462  0.0198  29  LYS   B CE  
4423 N  NZ  A LYS   B 29  ? 0.3989 0.3910 0.5687 0.0099  0.0629  0.0090  29  LYS   B NZ  
4424 N  NZ  B LYS   B 29  ? 0.3668 0.3835 0.5310 0.0058  0.0456  0.0153  29  LYS   B NZ  
4451 N  N   . VAL   B 30  ? 0.2205 0.2935 0.2256 0.0051  0.0396  0.0728  30  VAL   B N   
4452 C  CA  . VAL   B 30  ? 0.1995 0.2798 0.2483 -0.0115 0.0014  0.0784  30  VAL   B CA  
4453 C  C   . VAL   B 30  ? 0.1762 0.2733 0.2391 -0.0129 0.0044  0.0980  30  VAL   B C   
4454 O  O   . VAL   B 30  ? 0.1929 0.2923 0.2471 -0.0049 0.0013  0.1147  30  VAL   B O   
4455 C  CB  . VAL   B 30  ? 0.2035 0.2719 0.2989 -0.0304 -0.0292 0.0668  30  VAL   B CB  
4456 C  CG1 . VAL   B 30  ? 0.2095 0.2761 0.3012 -0.0307 -0.0231 0.0615  30  VAL   B CG1 
4457 C  CG2 . VAL   B 30  ? 0.2165 0.2726 0.3212 -0.0388 -0.0438 0.0516  30  VAL   B CG2 
4468 N  N   . LYS   B 31  ? 0.1671 0.2345 0.2711 -0.0310 0.0045  0.1055  31  LYS   B N   
4469 C  CA  . LYS   B 31  ? 0.1548 0.2281 0.3152 -0.0429 -0.0029 0.1103  31  LYS   B CA  
4470 C  C   . LYS   B 31  ? 0.1478 0.1928 0.2768 -0.0363 -0.0251 0.0880  31  LYS   B C   
4471 O  O   . LYS   B 31  ? 0.1618 0.2036 0.2920 -0.0312 -0.0209 0.1016  31  LYS   B O   
4472 C  CB  . LYS   B 31  ? 0.1741 0.2790 0.3755 -0.0375 0.0232  0.1239  31  LYS   B CB  
4473 C  CG  . LYS   B 31  ? 0.2078 0.3274 0.4273 -0.0412 0.0422  0.1185  31  LYS   B CG  
4474 C  CD  . LYS   B 31  ? 0.2540 0.3814 0.4779 -0.0418 0.0427  0.0994  31  LYS   B CD  
4475 C  CE  . LYS   B 31  ? 0.2790 0.4161 0.5252 -0.0438 0.0385  0.0845  31  LYS   B CE  
4476 N  NZ  . LYS   B 31  ? 0.3092 0.4433 0.5437 -0.0380 0.0289  0.0776  31  LYS   B NZ  
4490 N  N   . PRO   B 32  ? 0.1609 0.1553 0.2017 -0.0368 -0.0402 0.0496  32  PRO   B N   
4491 C  CA  . PRO   B 32  ? 0.1717 0.1519 0.1582 -0.0393 -0.0394 0.0288  32  PRO   B CA  
4492 C  C   . PRO   B 32  ? 0.1793 0.1427 0.1702 -0.0417 -0.0501 0.0378  32  PRO   B C   
4493 O  O   . PRO   B 32  ? 0.1946 0.1458 0.2080 -0.0442 -0.0716 0.0404  32  PRO   B O   
4494 C  CB  . PRO   B 32  ? 0.1873 0.1422 0.1544 -0.0421 -0.0266 0.0181  32  PRO   B CB  
4495 C  CG  . PRO   B 32  ? 0.2015 0.1353 0.1652 -0.0300 -0.0429 0.0225  32  PRO   B CG  
4496 C  CD  . PRO   B 32  ? 0.1863 0.1404 0.1911 -0.0261 -0.0507 0.0285  32  PRO   B CD  
4504 N  N   . THR   B 33  ? 0.1807 0.1308 0.1554 -0.0318 -0.0457 0.0258  33  THR   B N   
4505 C  CA  . THR   B 33  ? 0.1896 0.1386 0.1475 -0.0321 -0.0424 0.0272  33  THR   B CA  
4506 C  C   . THR   B 33  ? 0.1898 0.1287 0.1501 -0.0347 -0.0456 0.0156  33  THR   B C   
4507 O  O   . THR   B 33  ? 0.2146 0.1325 0.1611 -0.0440 -0.0545 0.0194  33  THR   B O   
4508 C  CB  . THR   B 33  ? 0.1994 0.1523 0.1523 -0.0186 -0.0520 0.0271  33  THR   B CB  
4509 O  OG1 . THR   B 33  ? 0.1939 0.1553 0.1612 -0.0250 -0.0525 0.0320  33  THR   B OG1 
4510 C  CG2 . THR   B 33  ? 0.2266 0.1609 0.1732 -0.0100 -0.0467 0.0213  33  THR   B CG2 
4518 N  N   . VAL   B 34  ? 0.1766 0.1282 0.1362 -0.0362 -0.0375 0.0110  34  VAL   B N   
4519 C  CA  . VAL   B 34  ? 0.1602 0.1286 0.1268 -0.0302 -0.0310 0.0057  34  VAL   B CA  
4520 C  C   . VAL   B 34  ? 0.1469 0.1215 0.1204 -0.0269 -0.0173 0.0038  34  VAL   B C   
4521 O  O   . VAL   B 34  ? 0.1663 0.1234 0.1295 -0.0255 -0.0295 0.0053  34  VAL   B O   
4522 C  CB  . VAL   B 34  ? 0.1667 0.1385 0.1595 -0.0128 -0.0304 0.0016  34  VAL   B CB  
4523 C  CG1 . VAL   B 34  ? 0.1642 0.1502 0.1577 -0.0065 -0.0151 0.0013  34  VAL   B CG1 
4524 C  CG2 . VAL   B 34  ? 0.1724 0.1412 0.1923 -0.0103 -0.0303 0.0076  34  VAL   B CG2 
4534 N  N   . VAL   B 35  ? 0.1352 0.1191 0.1231 -0.0267 -0.0158 0.0078  35  VAL   B N   
4535 C  CA  . VAL   B 35  ? 0.1351 0.1162 0.1193 -0.0204 -0.0091 0.0094  35  VAL   B CA  
4536 C  C   . VAL   B 35  ? 0.1261 0.1132 0.1161 -0.0151 -0.0135 0.0027  35  VAL   B C   
4537 O  O   . VAL   B 35  ? 0.1296 0.1206 0.1286 -0.0227 -0.0004 0.0008  35  VAL   B O   
4538 C  CB  . VAL   B 35  ? 0.1299 0.1372 0.1263 -0.0160 0.0022  0.0068  35  VAL   B CB  
4539 C  CG1 . VAL   B 35  ? 0.1249 0.1499 0.1435 -0.0220 0.0049  -0.0006 35  VAL   B CG1 
4540 C  CG2 . VAL   B 35  ? 0.1323 0.1382 0.1445 -0.0082 0.0000  -0.0000 35  VAL   B CG2 
4550 N  N   . VAL   B 36  ? 0.1278 0.1143 0.1124 -0.0177 -0.0089 0.0088  36  VAL   B N   
4551 C  CA  . VAL   B 36  ? 0.1251 0.1097 0.1147 -0.0123 -0.0029 0.0094  36  VAL   B CA  
4552 C  C   . VAL   B 36  ? 0.1202 0.1121 0.1045 -0.0112 -0.0003 0.0076  36  VAL   B C   
4553 O  O   . VAL   B 36  ? 0.1283 0.1195 0.1330 -0.0099 -0.0005 -0.0040 36  VAL   B O   
4554 C  CB  . VAL   B 36  ? 0.1234 0.1174 0.1231 -0.0141 -0.0030 0.0102  36  VAL   B CB  
4555 C  CG1 . VAL   B 36  ? 0.1234 0.1321 0.1266 -0.0196 -0.0061 0.0074  36  VAL   B CG1 
4556 C  CG2 . VAL   B 36  ? 0.1357 0.1217 0.1377 -0.0111 -0.0169 0.0087  36  VAL   B CG2 
4566 N  N   . ASN   B 37  ? 0.1246 0.1200 0.1061 -0.0005 -0.0048 0.0026  37  ASN   B N   
4567 C  CA  . ASN   B 37  ? 0.1240 0.1224 0.1202 0.0016  -0.0096 0.0064  37  ASN   B CA  
4568 C  C   . ASN   B 37  ? 0.1214 0.1232 0.1157 0.0023  -0.0108 0.0051  37  ASN   B C   
4569 O  O   . ASN   B 37  ? 0.1307 0.1266 0.1277 0.0021  0.0009  0.0080  37  ASN   B O   
4570 C  CB  . ASN   B 37  ? 0.1237 0.1265 0.1238 -0.0006 -0.0086 0.0027  37  ASN   B CB  
4571 C  CG  . ASN   B 37  ? 0.1251 0.1254 0.1254 -0.0003 -0.0066 0.0060  37  ASN   B CG  
4572 O  OD1 . ASN   B 37  ? 0.1324 0.1284 0.1475 0.0097  -0.0160 0.0045  37  ASN   B OD1 
4573 N  ND2 . ASN   B 37  ? 0.1325 0.1240 0.1287 0.0004  -0.0152 0.0073  37  ASN   B ND2 
4580 N  N   . ALA   B 38  ? 0.1312 0.1190 0.1189 0.0072  0.0047  0.0066  38  ALA   B N   
4581 C  CA  . ALA   B 38  ? 0.1472 0.1250 0.1233 0.0019  0.0042  0.0101  38  ALA   B CA  
4582 C  C   . ALA   B 38  ? 0.1388 0.1204 0.1192 0.0050  0.0090  0.0102  38  ALA   B C   
4583 O  O   . ALA   B 38  ? 0.1496 0.1273 0.1332 0.0100  0.0024  0.0116  38  ALA   B O   
4584 C  CB  . ALA   B 38  ? 0.1587 0.1307 0.1293 -0.0104 0.0032  0.0074  38  ALA   B CB  
4590 N  N   . ALA   B 39  ? 0.1367 0.1257 0.1106 0.0091  0.0027  0.0097  39  ALA   B N   
4591 C  CA  . ALA   B 39  ? 0.1471 0.1305 0.1141 0.0057  -0.0107 0.0083  39  ALA   B CA  
4592 C  C   . ALA   B 39  ? 0.1482 0.1362 0.1035 0.0101  -0.0083 0.0047  39  ALA   B C   
4593 O  O   . ALA   B 39  ? 0.1481 0.1421 0.1341 0.0008  -0.0009 0.0125  39  ALA   B O   
4594 C  CB  . ALA   B 39  ? 0.1471 0.1339 0.1324 0.0018  -0.0015 0.0021  39  ALA   B CB  
4600 N  N   . ASN   B 40  ? 0.1475 0.1567 0.1108 0.0009  -0.0009 -0.0038 40  ASN   B N   
4601 C  CA  . ASN   B 40  ? 0.1553 0.1623 0.1277 0.0042  -0.0025 -0.0066 40  ASN   B CA  
4602 C  C   . ASN   B 40  ? 0.1621 0.1599 0.1102 0.0122  -0.0042 0.0056  40  ASN   B C   
4603 O  O   . ASN   B 40  ? 0.1599 0.1494 0.1219 0.0133  -0.0105 -0.0023 40  ASN   B O   
4604 C  CB  . ASN   B 40  ? 0.1717 0.1587 0.1460 0.0155  -0.0102 0.0143  40  ASN   B CB  
4605 C  CG  . ASN   B 40  ? 0.1754 0.1654 0.1735 0.0101  -0.0203 0.0206  40  ASN   B CG  
4606 O  OD1 . ASN   B 40  ? 0.1750 0.1651 0.2620 0.0079  -0.0344 0.0213  40  ASN   B OD1 
4607 N  ND2 . ASN   B 40  ? 0.1779 0.1614 0.1737 0.0007  -0.0193 0.0150  40  ASN   B ND2 
4614 N  N   . VAL   B 41  ? 0.1709 0.1629 0.1219 0.0154  0.0009  0.0001  41  VAL   B N   
4615 C  CA  . VAL   B 41  ? 0.1714 0.1754 0.1221 0.0139  -0.0024 -0.0052 41  VAL   B CA  
4616 C  C   . VAL   B 41  ? 0.1734 0.1739 0.1167 0.0198  -0.0062 -0.0044 41  VAL   B C   
4617 O  O   . VAL   B 41  ? 0.1740 0.1740 0.1277 0.0184  -0.0150 -0.0073 41  VAL   B O   
4618 C  CB  . VAL   B 41  ? 0.1948 0.1913 0.1483 -0.0015 0.0196  -0.0184 41  VAL   B CB  
4619 C  CG1 . VAL   B 41  ? 0.1904 0.1972 0.1643 -0.0056 0.0245  -0.0189 41  VAL   B CG1 
4620 C  CG2 . VAL   B 41  ? 0.2084 0.2044 0.1541 -0.0104 0.0230  -0.0273 41  VAL   B CG2 
4630 N  N   . TYR   B 42  ? 0.1807 0.1714 0.1208 0.0182  -0.0143 0.0021  42  TYR   B N   
4631 C  CA  . TYR   B 42  ? 0.1876 0.1786 0.1271 0.0190  -0.0203 -0.0151 42  TYR   B CA  
4632 C  C   . TYR   B 42  ? 0.1675 0.1643 0.1342 0.0194  -0.0260 -0.0129 42  TYR   B C   
4633 O  O   . TYR   B 42  ? 0.1715 0.1721 0.1646 0.0150  -0.0290 -0.0160 42  TYR   B O   
4634 C  CB  . TYR   B 42  ? 0.2132 0.2091 0.1308 0.0130  -0.0336 0.0005  42  TYR   B CB  
4635 C  CG  . TYR   B 42  ? 0.2116 0.2254 0.1290 -0.0014 -0.0389 0.0130  42  TYR   B CG  
4636 C  CD1 . TYR   B 42  ? 0.2094 0.2253 0.1020 -0.0024 -0.0216 -0.0006 42  TYR   B CD1 
4637 C  CD2 . TYR   B 42  ? 0.2238 0.2349 0.1834 -0.0019 -0.0147 0.0201  42  TYR   B CD2 
4638 C  CE1 . TYR   B 42  ? 0.2233 0.2409 0.1099 0.0017  -0.0150 0.0051  42  TYR   B CE1 
4639 C  CE2 . TYR   B 42  ? 0.2257 0.2494 0.1829 0.0010  0.0096  0.0320  42  TYR   B CE2 
4640 C  CZ  . TYR   B 42  ? 0.2413 0.2661 0.1542 0.0144  0.0119  0.0139  42  TYR   B CZ  
4641 O  OH  . TYR   B 42  ? 0.2737 0.2941 0.2007 0.0351  0.0240  0.0246  42  TYR   B OH  
4651 N  N   . LEU   B 43  ? 0.1569 0.1449 0.1244 0.0152  -0.0186 -0.0086 43  LEU   B N   
4652 C  CA  . LEU   B 43  ? 0.1574 0.1452 0.1244 0.0036  -0.0199 -0.0005 43  LEU   B CA  
4653 C  C   . LEU   B 43  ? 0.1616 0.1478 0.1231 0.0050  -0.0195 0.0006  43  LEU   B C   
4654 O  O   . LEU   B 43  ? 0.1554 0.1509 0.1556 0.0092  -0.0213 0.0050  43  LEU   B O   
4655 C  CB  . LEU   B 43  ? 0.1537 0.1432 0.1374 0.0003  -0.0266 -0.0045 43  LEU   B CB  
4656 C  CG  . LEU   B 43  ? 0.1568 0.1392 0.1412 0.0042  -0.0226 -0.0062 43  LEU   B CG  
4657 C  CD1 . LEU   B 43  ? 0.1664 0.1461 0.1768 0.0042  -0.0466 -0.0091 43  LEU   B CD1 
4658 C  CD2 . LEU   B 43  ? 0.1529 0.1384 0.1545 -0.0009 -0.0294 -0.0097 43  LEU   B CD2 
4670 N  N   . LYS   B 44  ? 0.1630 0.1485 0.1268 0.0111  -0.0097 -0.0044 44  LYS   B N   
4671 C  CA  . LYS   B 44  ? 0.1717 0.1583 0.1332 0.0127  -0.0144 0.0032  44  LYS   B CA  
4672 C  C   . LYS   B 44  ? 0.1570 0.1512 0.1345 0.0169  -0.0152 -0.0020 44  LYS   B C   
4673 O  O   . LYS   B 44  ? 0.1818 0.1523 0.1598 0.0081  -0.0114 0.0044  44  LYS   B O   
4674 C  CB  . LYS   B 44  ? 0.1947 0.1762 0.1538 0.0214  -0.0266 0.0042  44  LYS   B CB  
4675 C  CG  . LYS   B 44  ? 0.2365 0.1991 0.1911 0.0144  -0.0523 0.0072  44  LYS   B CG  
4676 C  CD  . LYS   B 44  ? 0.2760 0.2172 0.2584 0.0001  -0.0608 -0.0013 44  LYS   B CD  
4677 C  CE  . LYS   B 44  ? 0.3082 0.2484 0.3099 -0.0071 -0.0667 0.0121  44  LYS   B CE  
4678 N  NZ  . LYS   B 44  ? 0.3210 0.2618 0.3386 -0.0049 -0.0765 0.0329  44  LYS   B NZ  
4692 N  N   . HIS   B 45  ? 0.1554 0.1550 0.1362 0.0107  -0.0107 0.0067  45  HIS   B N   
4693 C  CA  . HIS   B 45  ? 0.1533 0.1524 0.1350 0.0129  -0.0074 0.0012  45  HIS   B CA  
4694 C  C   . HIS   B 45  ? 0.1786 0.1675 0.1754 0.0207  -0.0177 -0.0079 45  HIS   B C   
4695 O  O   . HIS   B 45  ? 0.1894 0.1967 0.2245 0.0443  0.0072  -0.0027 45  HIS   B O   
4696 C  CB  . HIS   B 45  ? 0.1479 0.1551 0.1347 0.0037  -0.0095 -0.0015 45  HIS   B CB  
4697 C  CG  . HIS   B 45  ? 0.1519 0.1502 0.1307 -0.0029 -0.0099 0.0012  45  HIS   B CG  
4698 N  ND1 . HIS   B 45  ? 0.1563 0.1417 0.1415 0.0040  -0.0167 -0.0045 45  HIS   B ND1 
4699 C  CD2 . HIS   B 45  ? 0.1605 0.1501 0.1481 -0.0114 -0.0193 0.0014  45  HIS   B CD2 
4700 C  CE1 . HIS   B 45  ? 0.1645 0.1368 0.1280 -0.0015 -0.0223 -0.0095 45  HIS   B CE1 
4701 N  NE2 . HIS   B 45  ? 0.1650 0.1381 0.1358 -0.0016 -0.0200 -0.0018 45  HIS   B NE2 
4709 N  N   A GLY   B 46  ? 0.1911 0.1621 0.2125 0.0247  -0.0353 0.0040  46  GLY   B N   
4710 N  N   B GLY   B 46  ? 0.1889 0.1674 0.1976 0.0220  -0.0302 0.0056  46  GLY   B N   
4711 C  CA  A GLY   B 46  ? 0.2036 0.1743 0.2635 0.0195  -0.0458 0.0051  46  GLY   B CA  
4712 C  CA  B GLY   B 46  ? 0.1999 0.1786 0.2293 0.0180  -0.0390 0.0127  46  GLY   B CA  
4713 C  C   A GLY   B 46  ? 0.2015 0.1914 0.3048 0.0236  -0.0419 0.0043  46  GLY   B C   
4714 C  C   B GLY   B 46  ? 0.2024 0.1947 0.2605 0.0204  -0.0359 0.0204  46  GLY   B C   
4715 O  O   A GLY   B 46  ? 0.2043 0.2019 0.3861 0.0302  -0.0327 -0.0175 46  GLY   B O   
4716 O  O   B GLY   B 46  ? 0.2089 0.2049 0.2834 0.0242  -0.0320 0.0337  46  GLY   B O   
4723 N  N   . GLY   B 47  ? 0.2006 0.1984 0.2692 0.0108  -0.0219 0.0029  47  GLY   B N   
4724 C  CA  . GLY   B 47  ? 0.1887 0.1712 0.2227 0.0076  -0.0170 0.0044  47  GLY   B CA  
4725 C  C   . GLY   B 47  ? 0.1686 0.1524 0.1819 0.0087  0.0048  0.0076  47  GLY   B C   
4726 O  O   . GLY   B 47  ? 0.1802 0.1404 0.1857 0.0067  -0.0037 0.0105  47  GLY   B O   
4731 N  N   . GLY   B 48  ? 0.1517 0.1429 0.1821 0.0055  -0.0114 0.0175  48  GLY   B N   
4732 C  CA  . GLY   B 48  ? 0.1491 0.1378 0.1873 -0.0011 -0.0020 0.0119  48  GLY   B CA  
4733 C  C   . GLY   B 48  ? 0.1416 0.1366 0.1762 0.0060  0.0034  0.0023  48  GLY   B C   
4734 O  O   . GLY   B 48  ? 0.1403 0.1393 0.1922 0.0038  -0.0093 0.0056  48  GLY   B O   
4738 N  N   . VAL   B 49  ? 0.1448 0.1450 0.1565 0.0124  0.0012  0.0060  49  VAL   B N   
4739 C  CA  . VAL   B 49  ? 0.1452 0.1511 0.1453 0.0114  -0.0103 -0.0030 49  VAL   B CA  
4740 C  C   . VAL   B 49  ? 0.1365 0.1417 0.1359 0.0121  -0.0046 0.0084  49  VAL   B C   
4741 O  O   . VAL   B 49  ? 0.1517 0.1418 0.1466 0.0069  -0.0022 0.0022  49  VAL   B O   
4742 C  CB  . VAL   B 49  ? 0.1516 0.1673 0.1693 0.0094  -0.0195 -0.0033 49  VAL   B CB  
4743 C  CG1 . VAL   B 49  ? 0.1502 0.1773 0.1724 0.0065  -0.0248 0.0015  49  VAL   B CG1 
4744 C  CG2 . VAL   B 49  ? 0.1727 0.1773 0.1932 -0.0040 -0.0356 -0.0153 49  VAL   B CG2 
4754 N  N   . ALA   B 50  ? 0.1313 0.1313 0.1421 0.0056  -0.0038 0.0051  50  ALA   B N   
4755 C  CA  . ALA   B 50  ? 0.1350 0.1289 0.1342 0.0084  -0.0056 0.0090  50  ALA   B CA  
4756 C  C   . ALA   B 50  ? 0.1407 0.1358 0.1316 0.0060  -0.0038 0.0056  50  ALA   B C   
4757 O  O   . ALA   B 50  ? 0.1450 0.1372 0.1347 0.0077  0.0009  -0.0069 50  ALA   B O   
4758 C  CB  . ALA   B 50  ? 0.1406 0.1340 0.1363 0.0014  -0.0014 0.0060  50  ALA   B CB  
4764 N  N   . GLY   B 51  ? 0.1426 0.1461 0.1430 0.0119  -0.0133 0.0102  51  GLY   B N   
4765 C  CA  . GLY   B 51  ? 0.1405 0.1527 0.1600 0.0223  -0.0130 0.0071  51  GLY   B CA  
4766 C  C   . GLY   B 51  ? 0.1384 0.1459 0.1631 0.0196  -0.0077 0.0072  51  GLY   B C   
4767 O  O   . GLY   B 51  ? 0.1439 0.1556 0.1841 0.0093  -0.0067 0.0034  51  GLY   B O   
4771 N  N   . ALA   B 52  ? 0.1383 0.1364 0.1570 0.0140  -0.0050 0.0107  52  ALA   B N   
4772 C  CA  . ALA   B 52  ? 0.1453 0.1475 0.1641 0.0173  0.0040  -0.0000 52  ALA   B CA  
4773 C  C   . ALA   B 52  ? 0.1349 0.1481 0.1558 0.0094  0.0040  -0.0034 52  ALA   B C   
4774 O  O   . ALA   B 52  ? 0.1396 0.1511 0.1719 0.0119  -0.0026 -0.0001 52  ALA   B O   
4775 C  CB  . ALA   B 52  ? 0.1645 0.1509 0.1723 0.0065  0.0065  -0.0069 52  ALA   B CB  
4781 N  N   . LEU   B 53  ? 0.1300 0.1433 0.1455 0.0166  -0.0031 -0.0012 53  LEU   B N   
4782 C  CA  . LEU   B 53  ? 0.1331 0.1544 0.1353 0.0128  -0.0038 0.0007  53  LEU   B CA  
4783 C  C   . LEU   B 53  ? 0.1394 0.1447 0.1391 0.0126  0.0014  0.0018  53  LEU   B C   
4784 O  O   . LEU   B 53  ? 0.1467 0.1488 0.1533 0.0011  0.0034  0.0158  53  LEU   B O   
4785 C  CB  . LEU   B 53  ? 0.1326 0.1586 0.1456 0.0077  -0.0034 0.0141  53  LEU   B CB  
4786 C  CG  . LEU   B 53  ? 0.1298 0.1659 0.1547 0.0046  -0.0089 0.0198  53  LEU   B CG  
4787 C  CD1 . LEU   B 53  ? 0.1394 0.1861 0.1788 0.0097  -0.0064 0.0003  53  LEU   B CD1 
4788 C  CD2 . LEU   B 53  ? 0.1433 0.1953 0.1772 -0.0030 -0.0157 -0.0048 53  LEU   B CD2 
4800 N  N   . ASN   B 54  ? 0.1358 0.1328 0.1412 0.0070  -0.0026 0.0039  54  ASN   B N   
4801 C  CA  . ASN   B 54  ? 0.1393 0.1458 0.1563 0.0052  -0.0012 -0.0004 54  ASN   B CA  
4802 C  C   . ASN   B 54  ? 0.1373 0.1513 0.1691 0.0005  0.0014  0.0003  54  ASN   B C   
4803 O  O   . ASN   B 54  ? 0.1327 0.1558 0.1781 0.0003  0.0059  -0.0002 54  ASN   B O   
4804 C  CB  . ASN   B 54  ? 0.1451 0.1568 0.1656 0.0042  -0.0016 0.0027  54  ASN   B CB  
4805 C  CG  . ASN   B 54  ? 0.1402 0.1641 0.1664 0.0054  -0.0064 0.0018  54  ASN   B CG  
4806 O  OD1 . ASN   B 54  ? 0.1353 0.1638 0.1714 -0.0003 -0.0104 -0.0107 54  ASN   B OD1 
4807 N  ND2 . ASN   B 54  ? 0.1559 0.1830 0.1952 0.0003  -0.0299 0.0138  54  ASN   B ND2 
4814 N  N   . LYS   B 55  ? 0.1322 0.1579 0.1833 0.0085  -0.0018 0.0006  55  LYS   B N   
4815 C  CA  . LYS   B 55  ? 0.1395 0.1741 0.1948 0.0150  -0.0054 -0.0008 55  LYS   B CA  
4816 C  C   . LYS   B 55  ? 0.1384 0.1655 0.1894 0.0130  0.0082  -0.0090 55  LYS   B C   
4817 O  O   . LYS   B 55  ? 0.1331 0.1779 0.2116 0.0109  0.0077  -0.0092 55  LYS   B O   
4818 C  CB  . LYS   B 55  ? 0.1502 0.1840 0.2440 0.0278  0.0083  0.0094  55  LYS   B CB  
4819 C  CG  . LYS   B 55  ? 0.1955 0.2078 0.3294 0.0343  0.0222  0.0239  55  LYS   B CG  
4820 C  CD  . LYS   B 55  ? 0.2336 0.2294 0.4016 0.0380  0.0345  0.0411  55  LYS   B CD  
4821 C  CE  . LYS   B 55  ? 0.2546 0.2538 0.4692 0.0378  0.0493  0.0440  55  LYS   B CE  
4822 N  NZ  . LYS   B 55  ? 0.2591 0.2686 0.5011 0.0374  0.0360  0.0541  55  LYS   B NZ  
4836 N  N   . ALA   B 56  ? 0.1387 0.1718 0.1708 0.0099  0.0002  -0.0105 56  ALA   B N   
4837 C  CA  . ALA   B 56  ? 0.1513 0.1864 0.1657 0.0054  0.0003  -0.0099 56  ALA   B CA  
4838 C  C   . ALA   B 56  ? 0.1529 0.1822 0.1681 0.0068  0.0101  0.0029  56  ALA   B C   
4839 O  O   . ALA   B 56  ? 0.1631 0.1941 0.1894 0.0050  0.0306  -0.0010 56  ALA   B O   
4840 C  CB  . ALA   B 56  ? 0.1630 0.2067 0.1767 -0.0111 0.0028  -0.0072 56  ALA   B CB  
4846 N  N   . THR   B 57  ? 0.1476 0.1719 0.1732 0.0073  0.0129  0.0022  57  THR   B N   
4847 C  CA  . THR   B 57  ? 0.1498 0.1737 0.1723 0.0029  0.0213  0.0024  57  THR   B CA  
4848 C  C   . THR   B 57  ? 0.1494 0.1796 0.1940 0.0007  0.0237  -0.0007 57  THR   B C   
4849 O  O   . THR   B 57  ? 0.1600 0.1815 0.1965 -0.0126 0.0159  0.0020  57  THR   B O   
4850 C  CB  . THR   B 57  ? 0.1552 0.1573 0.1562 -0.0004 0.0141  0.0082  57  THR   B CB  
4851 O  OG1 . THR   B 57  ? 0.1546 0.1489 0.1777 -0.0043 0.0130  -0.0008 57  THR   B OG1 
4852 C  CG2 . THR   B 57  ? 0.1511 0.1665 0.1557 0.0038  0.0092  0.0090  57  THR   B CG2 
4860 N  N   . ASN   B 58  ? 0.1314 0.1957 0.2230 -0.0084 0.0137  -0.0139 58  ASN   B N   
4861 C  CA  . ASN   B 58  ? 0.1564 0.2348 0.2705 -0.0224 0.0322  -0.0050 58  ASN   B CA  
4862 C  C   . ASN   B 58  ? 0.1410 0.2147 0.2197 -0.0145 0.0003  -0.0044 58  ASN   B C   
4863 O  O   . ASN   B 58  ? 0.1461 0.2267 0.2221 -0.0158 0.0029  -0.0158 58  ASN   B O   
4864 C  CB  . ASN   B 58  ? 0.2497 0.3100 0.4023 -0.0323 0.0841  0.0116  58  ASN   B CB  
4865 C  CG  . ASN   B 58  ? 0.3706 0.3966 0.5518 -0.0362 0.1137  0.0331  58  ASN   B CG  
4866 O  OD1 . ASN   B 58  ? 0.3926 0.4104 0.6110 -0.0364 0.1185  0.0354  58  ASN   B OD1 
4867 N  ND2 . ASN   B 58  ? 0.4358 0.4371 0.5961 -0.0381 0.1285  0.0398  58  ASN   B ND2 
4874 N  N   . ASN   B 59  ? 0.1420 0.2007 0.1933 -0.0084 -0.0056 0.0066  59  ASN   B N   
4875 C  CA  . ASN   B 59  ? 0.1410 0.2013 0.1829 -0.0116 -0.0194 0.0131  59  ASN   B CA  
4876 C  C   . ASN   B 59  ? 0.1362 0.1909 0.1681 -0.0153 -0.0145 -0.0005 59  ASN   B C   
4877 O  O   . ASN   B 59  ? 0.1419 0.1956 0.1743 -0.0147 -0.0099 -0.0017 59  ASN   B O   
4878 C  CB  . ASN   B 59  ? 0.1505 0.2193 0.2006 -0.0045 -0.0235 0.0165  59  ASN   B CB  
4879 C  CG  . ASN   B 59  ? 0.1641 0.2334 0.2153 -0.0015 -0.0335 0.0119  59  ASN   B CG  
4880 O  OD1 . ASN   B 59  ? 0.1685 0.2422 0.2027 -0.0020 -0.0197 0.0243  59  ASN   B OD1 
4881 N  ND2 . ASN   B 59  ? 0.1702 0.2410 0.2264 -0.0078 -0.0333 -0.0022 59  ASN   B ND2 
4888 N  N   . ALA   B 60  ? 0.1397 0.1797 0.1748 -0.0122 0.0001  -0.0015 60  ALA   B N   
4889 C  CA  . ALA   B 60  ? 0.1501 0.1682 0.1794 -0.0165 -0.0035 0.0055  60  ALA   B CA  
4890 C  C   . ALA   B 60  ? 0.1487 0.1566 0.1581 -0.0116 -0.0089 0.0075  60  ALA   B C   
4891 O  O   . ALA   B 60  ? 0.1533 0.1587 0.1768 -0.0141 -0.0036 -0.0059 60  ALA   B O   
4892 C  CB  . ALA   B 60  ? 0.1637 0.1639 0.2126 -0.0184 0.0027  0.0078  60  ALA   B CB  
4898 N  N   . MET   B 61  ? 0.1367 0.1500 0.1558 -0.0102 -0.0074 0.0059  61  MET   B N   
4899 C  CA  . MET   B 61  ? 0.1340 0.1428 0.1528 -0.0067 -0.0143 0.0058  61  MET   B CA  
4900 C  C   . MET   B 61  ? 0.1438 0.1383 0.1590 -0.0084 -0.0103 0.0101  61  MET   B C   
4901 O  O   . MET   B 61  ? 0.1462 0.1375 0.1476 -0.0027 -0.0083 -0.0066 61  MET   B O   
4902 C  CB  . MET   B 61  ? 0.1357 0.1459 0.1435 -0.0018 -0.0127 -0.0016 61  MET   B CB  
4903 C  CG  . MET   B 61  ? 0.1362 0.1457 0.1349 0.0009  -0.0107 -0.0003 61  MET   B CG  
4904 S  SD  . MET   B 61  ? 0.1350 0.1470 0.1663 -0.0026 -0.0064 -0.0077 61  MET   B SD  
4905 C  CE  . MET   B 61  ? 0.1410 0.1733 0.1844 0.0044  -0.0028 -0.0169 61  MET   B CE  
4915 N  N   . GLN   B 62  ? 0.1435 0.1473 0.1517 -0.0018 -0.0154 0.0093  62  GLN   B N   
4916 C  CA  . GLN   B 62  ? 0.1454 0.1529 0.1543 0.0023  -0.0115 -0.0032 62  GLN   B CA  
4917 C  C   . GLN   B 62  ? 0.1410 0.1609 0.1562 -0.0009 -0.0199 -0.0056 62  GLN   B C   
4918 O  O   . GLN   B 62  ? 0.1533 0.1596 0.1585 0.0006  -0.0264 -0.0138 62  GLN   B O   
4919 C  CB  . GLN   B 62  ? 0.1487 0.1548 0.1547 0.0046  -0.0103 0.0052  62  GLN   B CB  
4920 C  CG  . GLN   B 62  ? 0.1562 0.1627 0.1452 0.0058  -0.0254 0.0014  62  GLN   B CG  
4921 C  CD  . GLN   B 62  ? 0.1558 0.1548 0.1471 0.0056  -0.0237 0.0080  62  GLN   B CD  
4922 O  OE1 . GLN   B 62  ? 0.1528 0.1504 0.1683 0.0034  -0.0233 -0.0044 62  GLN   B OE1 
4923 N  NE2 . GLN   B 62  ? 0.1595 0.1619 0.1595 0.0065  -0.0254 -0.0121 62  GLN   B NE2 
4932 N  N   . VAL   B 63  ? 0.1367 0.1655 0.1706 -0.0066 -0.0218 -0.0117 63  VAL   B N   
4933 C  CA  . VAL   B 63  ? 0.1510 0.1650 0.1969 -0.0137 -0.0304 -0.0049 63  VAL   B CA  
4934 C  C   . VAL   B 63  ? 0.1567 0.1529 0.1822 -0.0194 -0.0366 -0.0101 63  VAL   B C   
4935 O  O   . VAL   B 63  ? 0.1662 0.1543 0.1949 -0.0140 -0.0440 -0.0153 63  VAL   B O   
4936 C  CB  . VAL   B 63  ? 0.1523 0.1799 0.2304 -0.0164 -0.0306 -0.0079 63  VAL   B CB  
4937 C  CG1 . VAL   B 63  ? 0.1638 0.1806 0.2458 -0.0256 -0.0171 -0.0101 63  VAL   B CG1 
4938 C  CG2 . VAL   B 63  ? 0.1472 0.2033 0.2402 -0.0118 -0.0332 -0.0140 63  VAL   B CG2 
4948 N  N   . GLU   B 64  ? 0.1557 0.1481 0.1748 -0.0131 -0.0286 -0.0073 64  GLU   B N   
4949 C  CA  . GLU   B 64  ? 0.1566 0.1370 0.1617 -0.0099 -0.0325 -0.0006 64  GLU   B CA  
4950 C  C   . GLU   B 64  ? 0.1494 0.1357 0.1580 -0.0046 -0.0312 -0.0068 64  GLU   B C   
4951 O  O   . GLU   B 64  ? 0.1626 0.1458 0.1528 -0.0078 -0.0320 -0.0108 64  GLU   B O   
4952 C  CB  . GLU   B 64  ? 0.1543 0.1488 0.1598 -0.0151 -0.0253 -0.0023 64  GLU   B CB  
4953 C  CG  . GLU   B 64  ? 0.1605 0.1541 0.1699 -0.0233 -0.0222 -0.0092 64  GLU   B CG  
4954 C  CD  . GLU   B 64  ? 0.1631 0.1635 0.1727 -0.0300 -0.0203 -0.0062 64  GLU   B CD  
4955 O  OE1 . GLU   B 64  ? 0.1675 0.1833 0.1788 -0.0333 -0.0158 -0.0230 64  GLU   B OE1 
4956 O  OE2 . GLU   B 64  ? 0.1791 0.1740 0.1708 -0.0286 -0.0347 -0.0111 64  GLU   B OE2 
4963 N  N   . SER   B 65  ? 0.1491 0.1377 0.1544 -0.0063 -0.0188 -0.0160 65  SER   B N   
4964 C  CA  . SER   B 65  ? 0.1473 0.1350 0.1504 -0.0035 -0.0190 -0.0128 65  SER   B CA  
4965 C  C   . SER   B 65  ? 0.1513 0.1383 0.1516 0.0032  -0.0215 -0.0156 65  SER   B C   
4966 O  O   . SER   B 65  ? 0.1535 0.1478 0.1494 0.0027  -0.0207 -0.0202 65  SER   B O   
4967 C  CB  . SER   B 65  ? 0.1470 0.1422 0.1515 -0.0065 -0.0174 -0.0103 65  SER   B CB  
4968 O  OG  . SER   B 65  ? 0.1491 0.1412 0.1622 -0.0086 -0.0189 -0.0216 65  SER   B OG  
4974 N  N   . ASP   B 66  ? 0.1617 0.1477 0.1559 -0.0019 -0.0302 -0.0150 66  ASP   B N   
4975 C  CA  . ASP   B 66  ? 0.1706 0.1566 0.1445 0.0018  -0.0338 -0.0078 66  ASP   B CA  
4976 C  C   . ASP   B 66  ? 0.1771 0.1624 0.1516 -0.0023 -0.0309 -0.0118 66  ASP   B C   
4977 O  O   . ASP   B 66  ? 0.1814 0.1606 0.1611 0.0057  -0.0285 -0.0151 66  ASP   B O   
4978 C  CB  . ASP   B 66  ? 0.1790 0.1733 0.1625 0.0131  -0.0427 -0.0129 66  ASP   B CB  
4979 C  CG  . ASP   B 66  ? 0.2059 0.1920 0.1915 0.0205  -0.0554 -0.0059 66  ASP   B CG  
4980 O  OD1 . ASP   B 66  ? 0.2280 0.1848 0.1951 0.0157  -0.0509 0.0050  66  ASP   B OD1 
4981 O  OD2 . ASP   B 66  ? 0.2211 0.2093 0.2571 0.0400  -0.0525 -0.0052 66  ASP   B OD2 
4986 N  N   . ASP   B 67  ? 0.1735 0.1532 0.1448 -0.0074 -0.0304 -0.0246 67  ASP   B N   
4987 C  CA  . ASP   B 67  ? 0.1869 0.1502 0.1523 -0.0057 -0.0268 -0.0102 67  ASP   B CA  
4988 C  C   . ASP   B 67  ? 0.1796 0.1502 0.1711 -0.0004 -0.0275 -0.0183 67  ASP   B C   
4989 O  O   . ASP   B 67  ? 0.1813 0.1523 0.1751 0.0046  -0.0186 -0.0231 67  ASP   B O   
4990 C  CB  . ASP   B 67  ? 0.2094 0.1556 0.1722 -0.0142 -0.0335 -0.0058 67  ASP   B CB  
4991 C  CG  . ASP   B 67  ? 0.2453 0.1622 0.1834 -0.0133 -0.0634 -0.0092 67  ASP   B CG  
4992 O  OD1 . ASP   B 67  ? 0.2645 0.1661 0.2079 -0.0157 -0.0654 -0.0083 67  ASP   B OD1 
4993 O  OD2 . ASP   B 67  ? 0.2635 0.1714 0.1945 0.0012  -0.0671 -0.0051 67  ASP   B OD2 
4998 N  N   . TYR   B 68  ? 0.1722 0.1533 0.1540 0.0006  -0.0397 -0.0215 68  TYR   B N   
4999 C  CA  . TYR   B 68  ? 0.1686 0.1676 0.1710 0.0023  -0.0415 -0.0275 68  TYR   B CA  
5000 C  C   . TYR   B 68  ? 0.1638 0.1613 0.1657 0.0035  -0.0376 -0.0373 68  TYR   B C   
5001 O  O   . TYR   B 68  ? 0.1658 0.1690 0.1724 0.0093  -0.0328 -0.0461 68  TYR   B O   
5002 C  CB  . TYR   B 68  ? 0.1711 0.1804 0.1820 0.0081  -0.0418 -0.0441 68  TYR   B CB  
5003 C  CG  . TYR   B 68  ? 0.1834 0.1943 0.1907 0.0139  -0.0398 -0.0621 68  TYR   B CG  
5004 C  CD1 . TYR   B 68  ? 0.1866 0.1996 0.2190 -0.0025 -0.0329 -0.0639 68  TYR   B CD1 
5005 C  CD2 . TYR   B 68  ? 0.1923 0.2152 0.2058 0.0252  -0.0518 -0.0491 68  TYR   B CD2 
5006 C  CE1 . TYR   B 68  ? 0.1914 0.2149 0.2398 -0.0032 -0.0330 -0.0558 68  TYR   B CE1 
5007 C  CE2 . TYR   B 68  ? 0.1921 0.2210 0.2083 0.0222  -0.0395 -0.0612 68  TYR   B CE2 
5008 C  CZ  . TYR   B 68  ? 0.1871 0.2220 0.2297 0.0073  -0.0364 -0.0606 68  TYR   B CZ  
5009 O  OH  . TYR   B 68  ? 0.1816 0.2439 0.2460 0.0049  -0.0341 -0.0433 68  TYR   B OH  
5019 N  N   . ILE   B 69  ? 0.1667 0.1542 0.1646 0.0052  -0.0369 -0.0332 69  ILE   B N   
5020 C  CA  . ILE   B 69  ? 0.1732 0.1551 0.1753 -0.0017 -0.0179 -0.0351 69  ILE   B CA  
5021 C  C   . ILE   B 69  ? 0.1726 0.1516 0.1698 0.0071  -0.0294 -0.0263 69  ILE   B C   
5022 O  O   . ILE   B 69  ? 0.1781 0.1593 0.1650 0.0026  -0.0218 -0.0324 69  ILE   B O   
5023 C  CB  . ILE   B 69  ? 0.1760 0.1559 0.1994 -0.0028 0.0024  -0.0307 69  ILE   B CB  
5024 C  CG1 . ILE   B 69  ? 0.1750 0.1625 0.2130 -0.0042 0.0041  -0.0285 69  ILE   B CG1 
5025 C  CG2 . ILE   B 69  ? 0.1872 0.1615 0.2042 0.0001  0.0064  -0.0235 69  ILE   B CG2 
5026 C  CD1 . ILE   B 69  ? 0.1651 0.1709 0.2221 -0.0148 0.0101  -0.0316 69  ILE   B CD1 
5038 N  N   . ALA   B 70  ? 0.1687 0.1555 0.1739 0.0052  -0.0352 -0.0231 70  ALA   B N   
5039 C  CA  . ALA   B 70  ? 0.1723 0.1599 0.1577 0.0058  -0.0403 -0.0288 70  ALA   B CA  
5040 C  C   . ALA   B 70  ? 0.1787 0.1568 0.1706 0.0036  -0.0409 -0.0330 70  ALA   B C   
5041 O  O   . ALA   B 70  ? 0.1850 0.1611 0.1680 0.0050  -0.0369 -0.0365 70  ALA   B O   
5042 C  CB  . ALA   B 70  ? 0.1735 0.1746 0.1661 -0.0033 -0.0443 -0.0276 70  ALA   B CB  
5048 N  N   . THR   B 71  ? 0.1832 0.1582 0.1807 0.0028  -0.0538 -0.0323 71  THR   B N   
5049 C  CA  . THR   B 71  ? 0.1967 0.1612 0.2001 0.0129  -0.0678 -0.0337 71  THR   B CA  
5050 C  C   . THR   B 71  ? 0.1892 0.1637 0.2256 0.0315  -0.0638 -0.0517 71  THR   B C   
5051 O  O   . THR   B 71  ? 0.1988 0.1702 0.2683 0.0345  -0.0560 -0.0637 71  THR   B O   
5052 C  CB  . THR   B 71  ? 0.2277 0.1796 0.2174 0.0022  -0.0786 -0.0092 71  THR   B CB  
5053 O  OG1 . THR   B 71  ? 0.2465 0.2087 0.2504 -0.0182 -0.0742 0.0156  71  THR   B OG1 
5054 C  CG2 . THR   B 71  ? 0.2470 0.1763 0.2472 0.0027  -0.0654 0.0035  71  THR   B CG2 
5062 N  N   . ASN   B 72  ? 0.1770 0.1696 0.2195 0.0212  -0.0587 -0.0730 72  ASN   B N   
5063 C  CA  . ASN   B 72  ? 0.1780 0.1823 0.2214 0.0180  -0.0494 -0.0802 72  ASN   B CA  
5064 C  C   . ASN   B 72  ? 0.1788 0.1955 0.2318 0.0051  -0.0305 -0.0763 72  ASN   B C   
5065 O  O   . ASN   B 72  ? 0.1762 0.2115 0.2684 0.0071  -0.0140 -0.0753 72  ASN   B O   
5066 C  CB  . ASN   B 72  ? 0.1830 0.1991 0.2272 0.0183  -0.0567 -0.0658 72  ASN   B CB  
5067 C  CG  . ASN   B 72  ? 0.1970 0.2166 0.2335 0.0347  -0.0590 -0.0459 72  ASN   B CG  
5068 O  OD1 . ASN   B 72  ? 0.2173 0.2363 0.2385 0.0186  -0.0399 -0.0544 72  ASN   B OD1 
5069 N  ND2 . ASN   B 72  ? 0.2076 0.2237 0.2828 0.0514  -0.0459 -0.0076 72  ASN   B ND2 
5076 N  N   . GLY   B 73  ? 0.1835 0.1964 0.2067 0.0045  -0.0344 -0.0701 73  GLY   B N   
5077 C  CA  . GLY   B 73  ? 0.1745 0.2056 0.1884 0.0027  -0.0305 -0.0551 73  GLY   B CA  
5078 C  C   . GLY   B 73  ? 0.1720 0.2028 0.1486 0.0099  -0.0270 -0.0474 73  GLY   B C   
5079 O  O   . GLY   B 73  ? 0.1614 0.1877 0.1590 0.0101  -0.0185 -0.0287 73  GLY   B O   
5083 N  N   . PRO   B 74  ? 0.1732 0.2116 0.1406 0.0075  -0.0278 -0.0384 74  PRO   B N   
5084 C  CA  . PRO   B 74  ? 0.1644 0.2064 0.1301 0.0117  -0.0176 -0.0241 74  PRO   B CA  
5085 C  C   . PRO   B 74  ? 0.1507 0.1896 0.1376 0.0118  -0.0130 -0.0194 74  PRO   B C   
5086 O  O   . PRO   B 74  ? 0.1560 0.1891 0.1783 0.0084  -0.0095 -0.0286 74  PRO   B O   
5087 C  CB  . PRO   B 74  ? 0.1833 0.2270 0.1393 0.0072  -0.0155 -0.0157 74  PRO   B CB  
5088 C  CG  . PRO   B 74  ? 0.2005 0.2400 0.1587 0.0071  -0.0135 -0.0135 74  PRO   B CG  
5089 C  CD  . PRO   B 74  ? 0.1987 0.2318 0.1550 0.0081  -0.0101 -0.0259 74  PRO   B CD  
5097 N  N   . LEU   B 75  ? 0.1499 0.1805 0.1222 0.0141  -0.0134 -0.0194 75  LEU   B N   
5098 C  CA  . LEU   B 75  ? 0.1529 0.1779 0.1205 0.0116  -0.0123 -0.0066 75  LEU   B CA  
5099 C  C   . LEU   B 75  ? 0.1600 0.1920 0.1301 0.0140  -0.0056 -0.0067 75  LEU   B C   
5100 O  O   . LEU   B 75  ? 0.1790 0.2014 0.1378 0.0044  -0.0083 0.0016  75  LEU   B O   
5101 C  CB  . LEU   B 75  ? 0.1633 0.1863 0.1173 -0.0004 -0.0213 0.0123  75  LEU   B CB  
5102 C  CG  . LEU   B 75  ? 0.1954 0.2041 0.1221 -0.0209 -0.0063 0.0032  75  LEU   B CG  
5103 C  CD1 . LEU   B 75  ? 0.2281 0.2185 0.1350 -0.0309 0.0169  0.0008  75  LEU   B CD1 
5104 C  CD2 . LEU   B 75  ? 0.2337 0.2261 0.1957 -0.0147 0.0116  0.0083  75  LEU   B CD2 
5116 N  N   . LYS   B 76  ? 0.1582 0.2124 0.1526 0.0101  -0.0018 0.0014  76  LYS   B N   
5117 C  CA  . LYS   B 76  ? 0.1719 0.2184 0.1785 0.0033  0.0214  0.0033  76  LYS   B CA  
5118 C  C   . LYS   B 76  ? 0.1640 0.2029 0.1447 0.0119  0.0106  0.0223  76  LYS   B C   
5119 O  O   . LYS   B 76  ? 0.1634 0.1850 0.1453 0.0090  0.0034  0.0156  76  LYS   B O   
5120 C  CB  . LYS   B 76  ? 0.1913 0.2222 0.2421 -0.0047 0.0379  -0.0372 76  LYS   B CB  
5121 C  CG  . LYS   B 76  ? 0.1996 0.2438 0.2864 0.0023  0.0281  -0.0404 76  LYS   B CG  
5122 C  CD  . LYS   B 76  ? 0.1973 0.2564 0.3204 0.0080  0.0208  -0.0556 76  LYS   B CD  
5123 C  CE  . LYS   B 76  ? 0.1986 0.2757 0.3716 0.0085  0.0103  -0.0662 76  LYS   B CE  
5124 N  NZ  . LYS   B 76  ? 0.1957 0.2827 0.3877 0.0068  -0.0089 -0.0860 76  LYS   B NZ  
5138 N  N   . VAL   B 77  ? 0.1754 0.2160 0.1455 0.0182  0.0113  0.0262  77  VAL   B N   
5139 C  CA  . VAL   B 77  ? 0.1718 0.2049 0.1648 0.0260  0.0219  0.0463  77  VAL   B CA  
5140 C  C   . VAL   B 77  ? 0.1570 0.1836 0.1642 0.0242  0.0237  0.0360  77  VAL   B C   
5141 O  O   . VAL   B 77  ? 0.1577 0.1790 0.1634 0.0264  0.0229  0.0254  77  VAL   B O   
5142 C  CB  . VAL   B 77  ? 0.1828 0.2158 0.2011 0.0231  0.0297  0.0598  77  VAL   B CB  
5143 C  CG1 . VAL   B 77  ? 0.1882 0.2116 0.2260 0.0150  0.0304  0.0761  77  VAL   B CG1 
5144 C  CG2 . VAL   B 77  ? 0.1902 0.2296 0.2170 0.0181  0.0125  0.0572  77  VAL   B CG2 
5154 N  N   . GLY   B 78  ? 0.1501 0.1674 0.1587 0.0187  0.0203  0.0276  78  GLY   B N   
5155 C  CA  . GLY   B 78  ? 0.1473 0.1615 0.1613 0.0147  0.0252  0.0177  78  GLY   B CA  
5156 C  C   . GLY   B 78  ? 0.1401 0.1544 0.1439 0.0150  0.0140  0.0217  78  GLY   B C   
5157 O  O   . GLY   B 78  ? 0.1470 0.1511 0.1537 0.0216  0.0137  0.0176  78  GLY   B O   
5161 N  N   . GLY   B 79  ? 0.1409 0.1609 0.1433 0.0108  0.0138  0.0161  79  GLY   B N   
5162 C  CA  . GLY   B 79  ? 0.1419 0.1510 0.1419 0.0173  0.0118  0.0135  79  GLY   B CA  
5163 C  C   . GLY   B 79  ? 0.1302 0.1378 0.1367 0.0161  0.0055  0.0089  79  GLY   B C   
5164 O  O   . GLY   B 79  ? 0.1406 0.1383 0.1493 0.0137  0.0170  0.0195  79  GLY   B O   
5168 N  N   . SER   B 80  ? 0.1362 0.1304 0.1434 0.0077  0.0141  0.0036  80  SER   B N   
5169 C  CA  . SER   B 80  ? 0.1320 0.1328 0.1404 0.0046  0.0102  0.0064  80  SER   B CA  
5170 C  C   . SER   B 80  ? 0.1382 0.1298 0.1384 0.0105  -0.0071 0.0031  80  SER   B C   
5171 O  O   . SER   B 80  ? 0.1503 0.1350 0.1707 0.0125  0.0040  -0.0019 80  SER   B O   
5172 C  CB  . SER   B 80  ? 0.1349 0.1345 0.1499 -0.0017 0.0038  0.0113  80  SER   B CB  
5173 O  OG  . SER   B 80  ? 0.1448 0.1497 0.1674 -0.0036 -0.0129 0.0096  80  SER   B OG  
5179 N  N   . CYS   B 81  ? 0.1370 0.1188 0.1423 0.0001  -0.0090 -0.0004 81  CYS   B N   
5180 C  CA  . CYS   B 81  ? 0.1401 0.1184 0.1510 0.0048  -0.0144 -0.0008 81  CYS   B CA  
5181 C  C   . CYS   B 81  ? 0.1340 0.1160 0.1272 -0.0010 -0.0134 -0.0034 81  CYS   B C   
5182 O  O   . CYS   B 81  ? 0.1568 0.1195 0.1479 0.0069  -0.0011 -0.0036 81  CYS   B O   
5183 C  CB  . CYS   B 81  ? 0.1522 0.1305 0.1521 -0.0000 -0.0162 -0.0023 81  CYS   B CB  
5184 S  SG  . CYS   B 81  ? 0.1531 0.1512 0.1441 -0.0015 -0.0265 -0.0088 81  CYS   B SG  
5190 N  N   . VAL   B 82  ? 0.1360 0.1130 0.1495 -0.0021 -0.0139 -0.0029 82  VAL   B N   
5191 C  CA  . VAL   B 82  ? 0.1450 0.1188 0.1383 -0.0053 -0.0162 0.0020  82  VAL   B CA  
5192 C  C   . VAL   B 82  ? 0.1543 0.1170 0.1460 -0.0004 -0.0082 -0.0074 82  VAL   B C   
5193 O  O   . VAL   B 82  ? 0.1597 0.1203 0.1740 -0.0017 -0.0063 -0.0176 82  VAL   B O   
5194 C  CB  . VAL   B 82  ? 0.1571 0.1430 0.1544 -0.0024 -0.0160 0.0021  82  VAL   B CB  
5195 C  CG1 . VAL   B 82  ? 0.1749 0.1630 0.1623 0.0054  -0.0116 0.0144  82  VAL   B CG1 
5196 C  CG2 . VAL   B 82  ? 0.1587 0.1593 0.1684 -0.0051 -0.0326 0.0121  82  VAL   B CG2 
5206 N  N   . LEU   B 83  ? 0.1435 0.1162 0.1423 -0.0125 -0.0167 -0.0092 83  LEU   B N   
5207 C  CA  . LEU   B 83  ? 0.1427 0.1234 0.1331 -0.0098 -0.0178 -0.0040 83  LEU   B CA  
5208 C  C   . LEU   B 83  ? 0.1453 0.1220 0.1285 -0.0179 -0.0237 0.0005  83  LEU   B C   
5209 O  O   . LEU   B 83  ? 0.1478 0.1299 0.1261 -0.0221 -0.0175 0.0019  83  LEU   B O   
5210 C  CB  . LEU   B 83  ? 0.1513 0.1382 0.1388 -0.0074 -0.0234 -0.0083 83  LEU   B CB  
5211 C  CG  . LEU   B 83  ? 0.1687 0.1506 0.1417 -0.0125 -0.0106 -0.0071 83  LEU   B CG  
5212 C  CD1 . LEU   B 83  ? 0.1772 0.1603 0.1489 -0.0055 -0.0215 -0.0029 83  LEU   B CD1 
5213 C  CD2 . LEU   B 83  ? 0.1869 0.1617 0.1623 -0.0022 -0.0099 -0.0191 83  LEU   B CD2 
5225 N  N   . SER   B 84  ? 0.1480 0.1317 0.1529 -0.0228 -0.0203 0.0032  84  SER   B N   
5226 C  CA  . SER   B 84  ? 0.1482 0.1543 0.1436 -0.0250 -0.0188 0.0124  84  SER   B CA  
5227 C  C   . SER   B 84  ? 0.1375 0.1705 0.1078 -0.0213 -0.0180 0.0209  84  SER   B C   
5228 O  O   . SER   B 84  ? 0.1453 0.1553 0.1149 -0.0179 -0.0133 0.0044  84  SER   B O   
5229 C  CB  . SER   B 84  ? 0.1649 0.1567 0.1894 -0.0289 0.0027  0.0049  84  SER   B CB  
5230 O  OG  . SER   B 84  ? 0.1671 0.1674 0.2385 -0.0356 0.0043  0.0207  84  SER   B OG  
5236 N  N   . GLY   B 85  ? 0.1415 0.1845 0.1335 -0.0253 -0.0129 0.0177  85  GLY   B N   
5237 C  CA  . GLY   B 85  ? 0.1413 0.1942 0.1518 -0.0369 -0.0013 -0.0023 85  GLY   B CA  
5238 C  C   . GLY   B 85  ? 0.1384 0.1818 0.1271 -0.0403 -0.0002 0.0052  85  GLY   B C   
5239 O  O   . GLY   B 85  ? 0.1465 0.1829 0.1413 -0.0486 0.0106  -0.0063 85  GLY   B O   
5243 N  N   . HIS   B 86  ? 0.1407 0.1647 0.1414 -0.0313 -0.0129 0.0153  86  HIS   B N   
5244 C  CA  . HIS   B 86  ? 0.1465 0.1621 0.1491 -0.0330 -0.0173 0.0174  86  HIS   B CA  
5245 C  C   . HIS   B 86  ? 0.1463 0.1741 0.1441 -0.0423 -0.0071 0.0313  86  HIS   B C   
5246 O  O   . HIS   B 86  ? 0.1589 0.1824 0.1508 -0.0363 0.0010  0.0263  86  HIS   B O   
5247 C  CB  . HIS   B 86  ? 0.1540 0.1612 0.1545 -0.0244 -0.0227 0.0104  86  HIS   B CB  
5248 C  CG  . HIS   B 86  ? 0.1547 0.1724 0.1511 -0.0118 -0.0222 0.0140  86  HIS   B CG  
5249 N  ND1 . HIS   B 86  ? 0.1631 0.1907 0.1606 -0.0190 -0.0245 -0.0040 86  HIS   B ND1 
5250 C  CD2 . HIS   B 86  ? 0.1573 0.1715 0.1621 -0.0054 -0.0219 0.0115  86  HIS   B CD2 
5251 C  CE1 . HIS   B 86  ? 0.1732 0.1888 0.1544 -0.0169 -0.0123 -0.0185 86  HIS   B CE1 
5252 N  NE2 . HIS   B 86  ? 0.1688 0.1799 0.1464 -0.0006 -0.0117 0.0050  86  HIS   B NE2 
5260 N  N   . ASN   B 87  ? 0.1513 0.1794 0.1530 -0.0357 0.0032  0.0267  87  ASN   B N   
5261 C  CA  . ASN   B 87  ? 0.1587 0.1979 0.1510 -0.0334 0.0223  0.0189  87  ASN   B CA  
5262 C  C   . ASN   B 87  ? 0.1675 0.1832 0.1411 -0.0284 0.0241  0.0192  87  ASN   B C   
5263 O  O   . ASN   B 87  ? 0.1911 0.1915 0.1740 -0.0239 0.0427  0.0106  87  ASN   B O   
5264 C  CB  . ASN   B 87  ? 0.1585 0.2312 0.1836 -0.0325 0.0295  0.0191  87  ASN   B CB  
5265 C  CG  . ASN   B 87  ? 0.1675 0.2484 0.1998 0.0047  0.0307  0.0283  87  ASN   B CG  
5266 O  OD1 . ASN   B 87  ? 0.1589 0.2303 0.1831 0.0095  0.0430  0.0440  87  ASN   B OD1 
5267 N  ND2 . ASN   B 87  ? 0.2026 0.2622 0.2312 0.0101  0.0302  0.0263  87  ASN   B ND2 
5274 N  N   . LEU   B 88  ? 0.1536 0.1703 0.1256 -0.0314 0.0095  0.0099  88  LEU   B N   
5275 C  CA  . LEU   B 88  ? 0.1641 0.1658 0.1306 -0.0335 0.0080  -0.0007 88  LEU   B CA  
5276 C  C   . LEU   B 88  ? 0.1645 0.1535 0.1368 -0.0400 0.0013  0.0048  88  LEU   B C   
5277 O  O   . LEU   B 88  ? 0.1864 0.1639 0.1691 -0.0248 -0.0269 -0.0061 88  LEU   B O   
5278 C  CB  . LEU   B 88  ? 0.1807 0.1720 0.1542 -0.0412 -0.0056 0.0072  88  LEU   B CB  
5279 C  CG  . LEU   B 88  ? 0.2219 0.1994 0.1770 -0.0344 -0.0252 0.0269  88  LEU   B CG  
5280 C  CD1 . LEU   B 88  ? 0.2309 0.2280 0.2004 -0.0494 -0.0165 0.0430  88  LEU   B CD1 
5281 C  CD2 . LEU   B 88  ? 0.2607 0.2243 0.2306 0.0037  -0.0483 0.0080  88  LEU   B CD2 
5293 N  N   . ALA   B 89  ? 0.1555 0.1525 0.1286 -0.0380 0.0133  0.0037  89  ALA   B N   
5294 C  CA  . ALA   B 89  ? 0.1548 0.1505 0.1182 -0.0389 -0.0002 0.0080  89  ALA   B CA  
5295 C  C   . ALA   B 89  ? 0.1652 0.1500 0.1210 -0.0429 0.0132  0.0083  89  ALA   B C   
5296 O  O   . ALA   B 89  ? 0.1475 0.1611 0.1590 -0.0411 0.0167  -0.0254 89  ALA   B O   
5297 C  CB  . ALA   B 89  ? 0.1449 0.1529 0.1277 -0.0373 0.0022  0.0182  89  ALA   B CB  
5303 N  N   . LYS   B 90  ? 0.1985 0.1347 0.1321 -0.0478 0.0031  0.0104  90  LYS   B N   
5304 C  CA  . LYS   B 90  ? 0.2109 0.1330 0.1346 -0.0458 -0.0067 0.0120  90  LYS   B CA  
5305 C  C   . LYS   B 90  ? 0.1928 0.1277 0.1461 -0.0467 -0.0052 0.0016  90  LYS   B C   
5306 O  O   . LYS   B 90  ? 0.1993 0.1482 0.1620 -0.0599 0.0018  0.0029  90  LYS   B O   
5307 C  CB  . LYS   B 90  ? 0.2255 0.1385 0.1645 -0.0380 -0.0021 0.0175  90  LYS   B CB  
5308 C  CG  . LYS   B 90  ? 0.2273 0.1575 0.1612 -0.0237 0.0226  0.0165  90  LYS   B CG  
5309 C  CD  . LYS   B 90  ? 0.2571 0.1784 0.2114 -0.0139 0.0433  -0.0002 90  LYS   B CD  
5310 C  CE  . LYS   B 90  ? 0.2706 0.1924 0.2653 -0.0160 0.0548  -0.0058 90  LYS   B CE  
5311 N  NZ  . LYS   B 90  ? 0.2791 0.1843 0.2613 -0.0251 0.0701  -0.0024 90  LYS   B NZ  
5325 N  N   . HIS   B 91  ? 0.1640 0.1213 0.1238 -0.0324 -0.0178 0.0105  91  HIS   B N   
5326 C  CA  . HIS   B 91  ? 0.1550 0.1230 0.1322 -0.0251 -0.0151 0.0015  91  HIS   B CA  
5327 C  C   . HIS   B 91  ? 0.1428 0.1227 0.1167 -0.0239 -0.0065 -0.0009 91  HIS   B C   
5328 O  O   . HIS   B 91  ? 0.1549 0.1292 0.1193 -0.0251 -0.0151 0.0065  91  HIS   B O   
5329 C  CB  . HIS   B 91  ? 0.1742 0.1263 0.1674 -0.0061 -0.0046 0.0125  91  HIS   B CB  
5330 C  CG  . HIS   B 91  ? 0.2158 0.1421 0.2404 0.0072  0.0225  0.0271  91  HIS   B CG  
5331 N  ND1 . HIS   B 91  ? 0.2426 0.1447 0.3042 0.0015  0.0312  0.0119  91  HIS   B ND1 
5332 C  CD2 . HIS   B 91  ? 0.2236 0.1707 0.2875 0.0197  0.0132  0.0548  91  HIS   B CD2 
5333 C  CE1 . HIS   B 91  ? 0.2466 0.1642 0.3185 0.0143  0.0289  0.0220  91  HIS   B CE1 
5334 N  NE2 . HIS   B 91  ? 0.2392 0.1791 0.3208 0.0271  0.0245  0.0576  91  HIS   B NE2 
5342 N  N   . CYS   B 92  ? 0.1361 0.1214 0.1208 -0.0245 -0.0111 -0.0030 92  CYS   B N   
5343 C  CA  . CYS   B 92  ? 0.1349 0.1187 0.1234 -0.0222 -0.0082 0.0025  92  CYS   B CA  
5344 C  C   . CYS   B 92  ? 0.1326 0.1153 0.1104 -0.0114 -0.0016 0.0018  92  CYS   B C   
5345 O  O   . CYS   B 92  ? 0.1382 0.1228 0.1337 -0.0150 -0.0022 0.0013  92  CYS   B O   
5346 C  CB  . CYS   B 92  ? 0.1362 0.1316 0.1203 -0.0127 -0.0030 -0.0004 92  CYS   B CB  
5347 S  SG  . CYS   B 92  ? 0.1383 0.1318 0.1183 -0.0117 -0.0094 0.0034  92  CYS   B SG  
5353 N  N   . LEU   B 93  ? 0.1205 0.1228 0.1134 -0.0117 -0.0074 -0.0029 93  LEU   B N   
5354 C  CA  . LEU   B 93  ? 0.1264 0.1202 0.1144 0.0002  -0.0063 0.0032  93  LEU   B CA  
5355 C  C   . LEU   B 93  ? 0.1191 0.1185 0.1043 0.0010  -0.0071 0.0072  93  LEU   B C   
5356 O  O   . LEU   B 93  ? 0.1247 0.1155 0.1246 -0.0021 -0.0050 0.0029  93  LEU   B O   
5357 C  CB  . LEU   B 93  ? 0.1272 0.1174 0.1276 -0.0007 -0.0110 0.0056  93  LEU   B CB  
5358 C  CG  . LEU   B 93  ? 0.1254 0.1310 0.1446 -0.0051 -0.0097 0.0120  93  LEU   B CG  
5359 C  CD1 . LEU   B 93  ? 0.1266 0.1364 0.1430 0.0065  -0.0013 -0.0007 93  LEU   B CD1 
5360 C  CD2 . LEU   B 93  ? 0.1296 0.1308 0.1502 -0.0009 -0.0122 0.0052  93  LEU   B CD2 
5372 N  N   . HIS   B 94  ? 0.1243 0.1182 0.1042 -0.0045 -0.0129 0.0079  94  HIS   B N   
5373 C  CA  . HIS   B 94  ? 0.1243 0.1163 0.1136 0.0021  0.0003  0.0034  94  HIS   B CA  
5374 C  C   . HIS   B 94  ? 0.1258 0.1167 0.1256 0.0024  -0.0094 0.0087  94  HIS   B C   
5375 O  O   . HIS   B 94  ? 0.1291 0.1259 0.1650 -0.0026 0.0155  -0.0029 94  HIS   B O   
5376 C  CB  . HIS   B 94  ? 0.1235 0.1207 0.1279 0.0004  -0.0070 0.0017  94  HIS   B CB  
5377 C  CG  . HIS   B 94  ? 0.1289 0.1150 0.1282 -0.0045 -0.0187 0.0023  94  HIS   B CG  
5378 N  ND1 . HIS   B 94  ? 0.1313 0.1288 0.1231 -0.0045 -0.0208 0.0018  94  HIS   B ND1 
5379 C  CD2 . HIS   B 94  ? 0.1340 0.1198 0.1358 -0.0012 -0.0172 -0.0002 94  HIS   B CD2 
5380 C  CE1 . HIS   B 94  ? 0.1349 0.1262 0.1160 -0.0089 -0.0198 0.0043  94  HIS   B CE1 
5381 N  NE2 . HIS   B 94  ? 0.1298 0.1256 0.1327 -0.0133 -0.0153 0.0025  94  HIS   B NE2 
5389 N  N   . VAL   B 95  ? 0.1178 0.1105 0.1300 0.0000  0.0004  0.0044  95  VAL   B N   
5390 C  CA  . VAL   B 95  ? 0.1219 0.1205 0.1261 -0.0004 0.0020  0.0073  95  VAL   B CA  
5391 C  C   . VAL   B 95  ? 0.1295 0.1199 0.1248 0.0020  0.0044  0.0072  95  VAL   B C   
5392 O  O   . VAL   B 95  ? 0.1329 0.1178 0.1456 0.0041  0.0059  0.0163  95  VAL   B O   
5393 C  CB  . VAL   B 95  ? 0.1277 0.1208 0.1296 0.0006  -0.0035 0.0079  95  VAL   B CB  
5394 C  CG1 . VAL   B 95  ? 0.1392 0.1372 0.1441 -0.0039 -0.0000 0.0178  95  VAL   B CG1 
5395 C  CG2 . VAL   B 95  ? 0.1349 0.1184 0.1403 0.0063  -0.0054 0.0044  95  VAL   B CG2 
5405 N  N   . VAL   B 96  ? 0.1395 0.1252 0.1258 0.0125  0.0070  0.0175  96  VAL   B N   
5406 C  CA  . VAL   B 96  ? 0.1409 0.1440 0.1145 0.0135  0.0088  0.0195  96  VAL   B CA  
5407 C  C   . VAL   B 96  ? 0.1436 0.1433 0.1273 0.0097  0.0153  0.0188  96  VAL   B C   
5408 O  O   . VAL   B 96  ? 0.1485 0.1481 0.1497 0.0048  0.0212  0.0073  96  VAL   B O   
5409 C  CB  . VAL   B 96  ? 0.1482 0.1606 0.1182 0.0136  0.0082  0.0126  96  VAL   B CB  
5410 C  CG1 . VAL   B 96  ? 0.1483 0.1760 0.1335 0.0174  0.0082  0.0076  96  VAL   B CG1 
5411 C  CG2 . VAL   B 96  ? 0.1576 0.1669 0.1361 0.0078  0.0012  -0.0010 96  VAL   B CG2 
5421 N  N   . GLY   B 97  ? 0.1466 0.1427 0.1312 0.0095  0.0042  0.0249  97  GLY   B N   
5422 C  CA  . GLY   B 97  ? 0.1652 0.1468 0.1315 0.0029  0.0107  0.0235  97  GLY   B CA  
5423 C  C   . GLY   B 97  ? 0.1857 0.1536 0.1493 0.0096  0.0033  0.0163  97  GLY   B C   
5424 O  O   . GLY   B 97  ? 0.1994 0.1572 0.1464 0.0039  0.0027  0.0112  97  GLY   B O   
5428 N  N   . PRO   B 98  ? 0.1960 0.1561 0.1608 0.0128  0.0292  0.0281  98  PRO   B N   
5429 C  CA  . PRO   B 98  ? 0.2109 0.1756 0.1661 0.0219  0.0415  0.0247  98  PRO   B CA  
5430 C  C   . PRO   B 98  ? 0.2222 0.1811 0.1325 0.0358  0.0461  0.0478  98  PRO   B C   
5431 O  O   . PRO   B 98  ? 0.2117 0.1758 0.1587 0.0338  0.0433  0.0431  98  PRO   B O   
5432 C  CB  . PRO   B 98  ? 0.2051 0.1813 0.1867 0.0140  0.0530  0.0291  98  PRO   B CB  
5433 C  CG  . PRO   B 98  ? 0.1967 0.1715 0.1833 0.0103  0.0415  0.0399  98  PRO   B CG  
5434 C  CD  . PRO   B 98  ? 0.1806 0.1587 0.1736 0.0175  0.0400  0.0365  98  PRO   B CD  
5442 N  N   . ASN   B 99  ? 0.2361 0.1973 0.1544 0.0491  0.0426  0.0273  99  ASN   B N   
5443 C  CA  . ASN   B 99  ? 0.2596 0.2064 0.1576 0.0639  0.0393  0.0516  99  ASN   B CA  
5444 C  C   . ASN   B 99  ? 0.2885 0.2398 0.1934 0.0616  0.0649  0.0799  99  ASN   B C   
5445 O  O   . ASN   B 99  ? 0.3033 0.2411 0.1955 0.0622  0.0545  0.0775  99  ASN   B O   
5446 C  CB  . ASN   B 99  ? 0.2670 0.2009 0.1676 0.0638  0.0307  0.0430  99  ASN   B CB  
5447 C  CG  . ASN   B 99  ? 0.2673 0.2092 0.1870 0.0565  0.0235  0.0365  99  ASN   B CG  
5448 O  OD1 . ASN   B 99  ? 0.2652 0.2119 0.2108 0.0587  0.0226  0.0492  99  ASN   B OD1 
5449 N  ND2 . ASN   B 99  ? 0.2668 0.2118 0.1918 0.0575  0.0013  0.0321  99  ASN   B ND2 
5456 N  N   A VAL   B 100 ? 0.3046 0.2572 0.2476 0.0529  0.0710  0.1065  100 VAL   B N   
5457 N  N   B VAL   B 100 ? 0.3071 0.2578 0.2449 0.0531  0.0633  0.0999  100 VAL   B N   
5458 C  CA  A VAL   B 100 ? 0.3298 0.2786 0.3024 0.0428  0.0724  0.1252  100 VAL   B CA  
5459 C  CA  B VAL   B 100 ? 0.3310 0.2771 0.2935 0.0440  0.0588  0.1150  100 VAL   B CA  
5460 C  C   A VAL   B 100 ? 0.3499 0.2843 0.2862 0.0464  0.0707  0.1425  100 VAL   B C   
5461 C  C   B VAL   B 100 ? 0.3502 0.2828 0.2857 0.0471  0.0578  0.1341  100 VAL   B C   
5462 O  O   A VAL   B 100 ? 0.3565 0.2960 0.2901 0.0436  0.0831  0.1346  100 VAL   B O   
5463 O  O   B VAL   B 100 ? 0.3549 0.2894 0.2855 0.0444  0.0633  0.1273  100 VAL   B O   
5464 C  CB  A VAL   B 100 ? 0.3380 0.2972 0.3710 0.0249  0.0707  0.1303  100 VAL   B CB  
5465 C  CB  B VAL   B 100 ? 0.3371 0.2917 0.3475 0.0296  0.0541  0.1142  100 VAL   B CB  
5466 C  CG1 A VAL   B 100 ? 0.3436 0.3034 0.3952 0.0222  0.0722  0.1309  100 VAL   B CG1 
5467 C  CG1 B VAL   B 100 ? 0.3411 0.2963 0.3663 0.0273  0.0541  0.1134  100 VAL   B CG1 
5468 C  CG2 A VAL   B 100 ? 0.3380 0.3028 0.3898 0.0160  0.0702  0.1372  100 VAL   B CG2 
5469 C  CG2 B VAL   B 100 ? 0.3374 0.2963 0.3634 0.0228  0.0524  0.1167  100 VAL   B CG2 
5488 N  N   . ASN   B 101 ? 0.3655 0.2873 0.2937 0.0529  0.0489  0.1451  101 ASN   B N   
5489 C  CA  . ASN   B 101 ? 0.4062 0.3038 0.3000 0.0569  0.0143  0.1459  101 ASN   B CA  
5490 C  C   . ASN   B 101 ? 0.4547 0.3467 0.2963 0.0502  -0.0066 0.1530  101 ASN   B C   
5491 O  O   . ASN   B 101 ? 0.4597 0.3588 0.3208 0.0567  -0.0091 0.1298  101 ASN   B O   
5492 C  CB  . ASN   B 101 ? 0.4015 0.2852 0.3170 0.0555  0.0130  0.1249  101 ASN   B CB  
5493 C  CG  . ASN   B 101 ? 0.3984 0.2661 0.3183 0.0559  0.0125  0.1196  101 ASN   B CG  
5494 O  OD1 . ASN   B 101 ? 0.4020 0.2645 0.3410 0.0454  0.0318  0.1123  101 ASN   B OD1 
5495 N  ND2 . ASN   B 101 ? 0.3944 0.2617 0.3117 0.0597  0.0052  0.1040  101 ASN   B ND2 
5503 N  N   A LYS   B 102 ? 0.4769 0.3684 0.3136 0.0389  -0.0049 0.1440  102 LYS   B N   
5504 N  N   B LYS   B 102 ? 0.4741 0.3698 0.3189 0.0391  -0.0054 0.1388  102 LYS   B N   
5505 C  CA  A LYS   B 102 ? 0.4972 0.3979 0.3398 0.0224  0.0037  0.1107  102 LYS   B CA  
5506 C  CA  B LYS   B 102 ? 0.4912 0.3966 0.3440 0.0250  0.0019  0.1099  102 LYS   B CA  
5507 C  C   A LYS   B 102 ? 0.4951 0.4004 0.3147 0.0218  0.0100  0.1152  102 LYS   B C   
5508 C  C   B LYS   B 102 ? 0.4910 0.3993 0.3215 0.0228  0.0101  0.1147  102 LYS   B C   
5509 O  O   A LYS   B 102 ? 0.5024 0.4063 0.3216 0.0225  -0.0020 0.1094  102 LYS   B O   
5510 O  O   B LYS   B 102 ? 0.4965 0.4041 0.3264 0.0232  0.0008  0.1110  102 LYS   B O   
5511 C  CB  A LYS   B 102 ? 0.5158 0.4227 0.3987 0.0075  0.0127  0.0681  102 LYS   B CB  
5512 C  CB  B LYS   B 102 ? 0.5054 0.4182 0.3969 0.0142  0.0063  0.0726  102 LYS   B CB  
5513 C  CG  A LYS   B 102 ? 0.5311 0.4439 0.4574 -0.0046 0.0239  0.0301  102 LYS   B CG  
5514 C  CG  B LYS   B 102 ? 0.5167 0.4363 0.4481 0.0057  0.0129  0.0388  102 LYS   B CG  
5515 C  CD  A LYS   B 102 ? 0.5440 0.4604 0.5171 -0.0130 0.0356  -0.0004 102 LYS   B CD  
5516 C  CD  B LYS   B 102 ? 0.5260 0.4501 0.4977 -0.0001 0.0200  0.0112  102 LYS   B CD  
5517 C  CE  A LYS   B 102 ? 0.5537 0.4711 0.5622 -0.0190 0.0431  -0.0235 102 LYS   B CE  
5518 C  CE  B LYS   B 102 ? 0.5330 0.4592 0.5352 -0.0042 0.0241  -0.0091 102 LYS   B CE  
5519 N  NZ  A LYS   B 102 ? 0.5592 0.4770 0.5883 -0.0212 0.0450  -0.0357 102 LYS   B NZ  
5520 N  NZ  B LYS   B 102 ? 0.5370 0.4642 0.5567 -0.0059 0.0250  -0.0196 102 LYS   B NZ  
5547 N  N   . GLY   B 103 ? 0.4825 0.3949 0.3086 0.0207  0.0280  0.1148  103 GLY   B N   
5548 C  CA  . GLY   B 103 ? 0.4605 0.3856 0.3125 0.0205  0.0562  0.0931  103 GLY   B CA  
5549 C  C   . GLY   B 103 ? 0.4352 0.3713 0.3079 0.0190  0.0834  0.0731  103 GLY   B C   
5550 O  O   . GLY   B 103 ? 0.4397 0.3777 0.3185 0.0169  0.0889  0.0744  103 GLY   B O   
5555 N  N   A GLU   B 104 ? 0.4188 0.3603 0.2968 0.0241  0.1011  0.0607  104 GLU   B N   
5556 N  N   B GLU   B 104 ? 0.4190 0.3587 0.3079 0.0151  0.0809  0.0581  104 GLU   B N   
5557 C  CA  A GLU   B 104 ? 0.4010 0.3495 0.2819 0.0331  0.1098  0.0451  104 GLU   B CA  
5558 C  CA  B GLU   B 104 ? 0.4016 0.3458 0.3015 0.0132  0.0741  0.0413  104 GLU   B CA  
5559 C  C   A GLU   B 104 ? 0.4034 0.3514 0.2950 0.0205  0.1441  0.0500  104 GLU   B C   
5560 C  C   B GLU   B 104 ? 0.3973 0.3422 0.3129 0.0081  0.0931  0.0414  104 GLU   B C   
5561 O  O   A GLU   B 104 ? 0.4074 0.3573 0.3216 0.0170  0.1384  0.0472  104 GLU   B O   
5562 O  O   B GLU   B 104 ? 0.3993 0.3441 0.3287 0.0066  0.0901  0.0364  104 GLU   B O   
5563 C  CB  A GLU   B 104 ? 0.3852 0.3353 0.2740 0.0551  0.0730  0.0145  104 GLU   B CB  
5564 C  CB  B GLU   B 104 ? 0.3909 0.3352 0.2920 0.0157  0.0446  0.0181  104 GLU   B CB  
5565 C  CG  A GLU   B 104 ? 0.3703 0.3238 0.2553 0.0763  0.0340  -0.0179 104 GLU   B CG  
5566 C  CG  B GLU   B 104 ? 0.3814 0.3262 0.2778 0.0182  0.0150  -0.0067 104 GLU   B CG  
5567 C  CD  A GLU   B 104 ? 0.3576 0.3133 0.2361 0.0943  -0.0020 -0.0351 104 GLU   B CD  
5568 C  CD  B GLU   B 104 ? 0.3743 0.3176 0.2655 0.0185  -0.0101 -0.0218 104 GLU   B CD  
5569 O  OE1 A GLU   B 104 ? 0.3447 0.3018 0.1961 0.1086  0.0003  -0.0348 104 GLU   B OE1 
5570 O  OE1 B GLU   B 104 ? 0.3696 0.3123 0.2485 0.0184  -0.0108 -0.0205 104 GLU   B OE1 
5571 O  OE2 A GLU   B 104 ? 0.3581 0.3172 0.2377 0.0939  -0.0303 -0.0469 104 GLU   B OE2 
5572 O  OE2 B GLU   B 104 ? 0.3730 0.3169 0.2635 0.0175  -0.0293 -0.0327 104 GLU   B OE2 
5585 N  N   A ASP   B 105 ? 0.3980 0.3477 0.2853 0.0110  0.1761  0.0568  105 ASP   B N   
5586 N  N   B ASP   B 105 ? 0.3888 0.3370 0.3050 0.0036  0.1117  0.0461  105 ASP   B N   
5587 C  CA  A ASP   B 105 ? 0.3978 0.3454 0.3094 0.0041  0.1897  0.0438  105 ASP   B CA  
5588 C  CA  B ASP   B 105 ? 0.3839 0.3321 0.3122 0.0000  0.1227  0.0402  105 ASP   B CA  
5589 C  C   A ASP   B 105 ? 0.3826 0.3179 0.2773 -0.0064 0.1836  0.0437  105 ASP   B C   
5590 C  C   B ASP   B 105 ? 0.3753 0.3185 0.2922 -0.0049 0.1225  0.0335  105 ASP   B C   
5591 O  O   A ASP   B 105 ? 0.3684 0.3128 0.2685 -0.0084 0.1769  0.0438  105 ASP   B O   
5592 O  O   B ASP   B 105 ? 0.3723 0.3145 0.2798 -0.0074 0.1284  0.0358  105 ASP   B O   
5593 C  CB  A ASP   B 105 ? 0.4139 0.3680 0.3885 0.0104  0.1947  0.0236  105 ASP   B CB  
5594 C  CB  B ASP   B 105 ? 0.3871 0.3400 0.3479 0.0023  0.1299  0.0379  105 ASP   B CB  
5595 C  CG  A ASP   B 105 ? 0.4257 0.3863 0.4601 0.0131  0.2059  0.0090  105 ASP   B CG  
5596 C  CG  B ASP   B 105 ? 0.3894 0.3453 0.3805 0.0009  0.1419  0.0390  105 ASP   B CG  
5597 O  OD1 A ASP   B 105 ? 0.4263 0.3908 0.4710 0.0088  0.2190  0.0102  105 ASP   B OD1 
5598 O  OD1 B ASP   B 105 ? 0.3886 0.3490 0.3865 -0.0041 0.1479  0.0424  105 ASP   B OD1 
5599 O  OD2 A ASP   B 105 ? 0.4318 0.3949 0.4989 0.0180  0.2009  -0.0007 105 ASP   B OD2 
5600 O  OD2 B ASP   B 105 ? 0.3884 0.3456 0.3883 0.0003  0.1512  0.0407  105 ASP   B OD2 
5609 N  N   A ILE   B 106 ? 0.3749 0.2929 0.2898 -0.0133 0.1727  0.0471  106 ILE   B N   
5610 N  N   B ILE   B 106 ? 0.3670 0.3080 0.2942 -0.0051 0.1102  0.0262  106 ILE   B N   
5611 C  CA  A ILE   B 106 ? 0.3554 0.2632 0.3012 -0.0259 0.1778  0.0469  106 ILE   B CA  
5612 C  CA  B ILE   B 106 ? 0.3535 0.2972 0.3030 -0.0073 0.1056  0.0165  106 ILE   B CA  
5613 C  C   A ILE   B 106 ? 0.3263 0.2555 0.2980 -0.0158 0.1776  0.0307  106 ILE   B C   
5614 C  C   B ILE   B 106 ? 0.3336 0.2944 0.3016 -0.0018 0.1020  0.0044  106 ILE   B C   
5615 O  O   A ILE   B 106 ? 0.3204 0.2327 0.2964 -0.0156 0.1746  0.0361  106 ILE   B O   
5616 O  O   B ILE   B 106 ? 0.3312 0.2858 0.3007 -0.0035 0.0946  0.0009  106 ILE   B O   
5617 C  CB  A ILE   B 106 ? 0.3718 0.2499 0.3236 -0.0392 0.1654  0.0529  106 ILE   B CB  
5618 C  CB  B ILE   B 106 ? 0.3625 0.2938 0.3134 -0.0132 0.1025  0.0169  106 ILE   B CB  
5619 C  CG1 A ILE   B 106 ? 0.3797 0.2482 0.3263 -0.0339 0.1578  0.0436  106 ILE   B CG1 
5620 C  CG1 B ILE   B 106 ? 0.3669 0.2931 0.3156 -0.0109 0.0990  0.0153  106 ILE   B CG1 
5621 C  CG2 A ILE   B 106 ? 0.3747 0.2471 0.3396 -0.0525 0.1653  0.0596  106 ILE   B CG2 
5622 C  CG2 B ILE   B 106 ? 0.3649 0.2946 0.3234 -0.0181 0.1031  0.0166  106 ILE   B CG2 
5623 C  CD1 A ILE   B 106 ? 0.3845 0.2493 0.3224 -0.0267 0.1510  0.0424  106 ILE   B CD1 
5624 C  CD1 B ILE   B 106 ? 0.3693 0.2935 0.3157 -0.0077 0.0956  0.0160  106 ILE   B CD1 
5647 N  N   A GLN   B 107 ? 0.3108 0.2767 0.3177 -0.0097 0.1635  0.0205  107 GLN   B N   
5648 N  N   B GLN   B 107 ? 0.3193 0.3028 0.3165 0.0021  0.1001  0.0015  107 GLN   B N   
5649 C  CA  A GLN   B 107 ? 0.2941 0.2966 0.3358 -0.0088 0.1460  0.0202  107 GLN   B CA  
5650 C  CA  B GLN   B 107 ? 0.3053 0.3099 0.3312 0.0039  0.0961  0.0062  107 GLN   B CA  
5651 C  C   A GLN   B 107 ? 0.2661 0.2794 0.3030 -0.0027 0.1184  0.0135  107 GLN   B C   
5652 C  C   B GLN   B 107 ? 0.2753 0.2885 0.2983 0.0064  0.0941  0.0061  107 GLN   B C   
5653 O  O   A GLN   B 107 ? 0.2601 0.2794 0.3353 0.0011  0.0924  -0.0039 107 GLN   B O   
5654 O  O   B GLN   B 107 ? 0.2733 0.2914 0.3158 0.0077  0.0791  -0.0063 107 GLN   B O   
5655 C  CB  A GLN   B 107 ? 0.3222 0.3362 0.4092 -0.0055 0.1208  0.0217  107 GLN   B CB  
5656 C  CB  B GLN   B 107 ? 0.3273 0.3383 0.3898 0.0067  0.0813  0.0095  107 GLN   B CB  
5657 C  CG  A GLN   B 107 ? 0.3508 0.3723 0.4823 -0.0001 0.0868  0.0231  107 GLN   B CG  
5658 C  CG  B GLN   B 107 ? 0.3481 0.3641 0.4482 0.0099  0.0614  0.0128  107 GLN   B CG  
5659 C  CD  A GLN   B 107 ? 0.3718 0.4005 0.5407 0.0009  0.0636  0.0272  107 GLN   B CD  
5660 C  CD  B GLN   B 107 ? 0.3636 0.3843 0.4956 0.0102  0.0470  0.0169  107 GLN   B CD  
5661 O  OE1 A GLN   B 107 ? 0.3802 0.4109 0.5623 -0.0009 0.0589  0.0259  107 GLN   B OE1 
5662 O  OE1 B GLN   B 107 ? 0.3694 0.3916 0.5113 0.0088  0.0445  0.0170  107 GLN   B OE1 
5663 N  NE2 A GLN   B 107 ? 0.3786 0.4093 0.5599 0.0049  0.0544  0.0325  107 GLN   B NE2 
5664 N  NE2 B GLN   B 107 ? 0.3687 0.3906 0.5130 0.0128  0.0416  0.0204  107 GLN   B NE2 
5681 N  N   . LEU   B 108 ? 0.2485 0.2635 0.2695 0.0161  0.0980  0.0129  108 LEU   B N   
5682 C  CA  . LEU   B 108 ? 0.2260 0.2341 0.2241 0.0317  0.0710  0.0288  108 LEU   B CA  
5683 C  C   . LEU   B 108 ? 0.1875 0.1889 0.2114 0.0328  0.0480  0.0350  108 LEU   B C   
5684 O  O   . LEU   B 108 ? 0.1874 0.1789 0.1960 0.0284  0.0383  0.0282  108 LEU   B O   
5685 C  CB  . LEU   B 108 ? 0.2423 0.2543 0.2087 0.0312  0.0681  0.0365  108 LEU   B CB  
5686 C  CG  . LEU   B 108 ? 0.2547 0.2841 0.2191 0.0363  0.0583  0.0097  108 LEU   B CG  
5687 C  CD1 . LEU   B 108 ? 0.2628 0.2981 0.1992 0.0274  0.0658  0.0113  108 LEU   B CD1 
5688 C  CD2 . LEU   B 108 ? 0.2661 0.2960 0.2324 0.0434  0.0459  -0.0088 108 LEU   B CD2 
5701 N  N   . LEU   B 109 ? 0.1738 0.1632 0.2098 0.0230  0.0425  0.0282  109 LEU   B N   
5702 C  CA  . LEU   B 109 ? 0.1537 0.1387 0.2243 0.0129  0.0372  0.0316  109 LEU   B CA  
5703 C  C   . LEU   B 109 ? 0.1426 0.1283 0.2238 0.0054  0.0353  0.0183  109 LEU   B C   
5704 O  O   . LEU   B 109 ? 0.1412 0.1278 0.2040 0.0048  0.0326  0.0317  109 LEU   B O   
5705 C  CB  . LEU   B 109 ? 0.1603 0.1326 0.2259 0.0068  0.0281  0.0435  109 LEU   B CB  
5706 C  CG  . LEU   B 109 ? 0.1621 0.1357 0.2174 0.0008  0.0224  0.0255  109 LEU   B CG  
5707 C  CD1 . LEU   B 109 ? 0.1612 0.1457 0.1964 0.0131  0.0256  0.0244  109 LEU   B CD1 
5708 C  CD2 . LEU   B 109 ? 0.1686 0.1409 0.2276 0.0022  0.0127  0.0251  109 LEU   B CD2 
5720 N  N   . LYS   B 110 ? 0.1376 0.1286 0.2167 -0.0006 0.0303  0.0242  110 LYS   B N   
5721 C  CA  . LYS   B 110 ? 0.1379 0.1254 0.2019 0.0001  0.0287  0.0190  110 LYS   B CA  
5722 C  C   . LYS   B 110 ? 0.1345 0.1295 0.1916 0.0021  0.0261  0.0096  110 LYS   B C   
5723 O  O   . LYS   B 110 ? 0.1288 0.1363 0.1898 -0.0031 0.0225  0.0092  110 LYS   B O   
5724 C  CB  . LYS   B 110 ? 0.1408 0.1277 0.2265 0.0012  0.0297  0.0105  110 LYS   B CB  
5725 C  CG  . LYS   B 110 ? 0.1377 0.1295 0.2379 -0.0055 0.0207  0.0158  110 LYS   B CG  
5726 C  CD  . LYS   B 110 ? 0.1420 0.1255 0.2490 -0.0040 0.0229  0.0156  110 LYS   B CD  
5727 C  CE  . LYS   B 110 ? 0.1415 0.1414 0.2673 -0.0008 0.0191  0.0082  110 LYS   B CE  
5728 N  NZ  . LYS   B 110 ? 0.1396 0.1556 0.2580 0.0029  0.0052  0.0069  110 LYS   B NZ  
5742 N  N   . SER   B 111 ? 0.1418 0.1283 0.2078 0.0002  0.0255  0.0114  111 SER   B N   
5743 C  CA  . SER   B 111 ? 0.1439 0.1290 0.1963 0.0048  0.0181  0.0132  111 SER   B CA  
5744 C  C   . SER   B 111 ? 0.1364 0.1245 0.1825 0.0019  0.0146  0.0054  111 SER   B C   
5745 O  O   . SER   B 111 ? 0.1357 0.1297 0.1962 0.0010  0.0120  0.0103  111 SER   B O   
5746 C  CB  . SER   B 111 ? 0.1532 0.1533 0.2074 0.0101  0.0316  0.0289  111 SER   B CB  
5747 O  OG  . SER   B 111 ? 0.1711 0.1895 0.2104 0.0173  0.0406  0.0257  111 SER   B OG  
5753 N  N   . ALA   B 112 ? 0.1294 0.1306 0.1874 0.0074  0.0179  0.0209  112 ALA   B N   
5754 C  CA  . ALA   B 112 ? 0.1296 0.1346 0.1756 0.0060  0.0102  0.0105  112 ALA   B CA  
5755 C  C   . ALA   B 112 ? 0.1226 0.1275 0.1634 0.0037  0.0119  0.0105  112 ALA   B C   
5756 O  O   . ALA   B 112 ? 0.1218 0.1310 0.1744 0.0014  0.0161  0.0040  112 ALA   B O   
5757 C  CB  . ALA   B 112 ? 0.1350 0.1389 0.1915 0.0046  0.0167  0.0203  112 ALA   B CB  
5763 N  N   . TYR   B 113 ? 0.1203 0.1215 0.1789 0.0019  0.0140  0.0131  113 TYR   B N   
5764 C  CA  . TYR   B 113 ? 0.1202 0.1154 0.1724 -0.0007 0.0079  0.0058  113 TYR   B CA  
5765 C  C   . TYR   B 113 ? 0.1161 0.1151 0.1667 -0.0058 0.0079  0.0084  113 TYR   B C   
5766 O  O   . TYR   B 113 ? 0.1205 0.1121 0.1645 -0.0031 0.0028  0.0048  113 TYR   B O   
5767 C  CB  . TYR   B 113 ? 0.1295 0.1109 0.1794 -0.0020 0.0202  0.0156  113 TYR   B CB  
5768 C  CG  . TYR   B 113 ? 0.1298 0.1125 0.1862 -0.0045 0.0165  0.0128  113 TYR   B CG  
5769 C  CD1 . TYR   B 113 ? 0.1348 0.1116 0.1994 -0.0045 0.0195  0.0174  113 TYR   B CD1 
5770 C  CD2 . TYR   B 113 ? 0.1362 0.1151 0.1859 -0.0046 0.0056  0.0098  113 TYR   B CD2 
5771 C  CE1 . TYR   B 113 ? 0.1365 0.1165 0.1966 -0.0009 0.0233  0.0045  113 TYR   B CE1 
5772 C  CE2 . TYR   B 113 ? 0.1406 0.1052 0.1984 -0.0012 0.0158  0.0169  113 TYR   B CE2 
5773 C  CZ  . TYR   B 113 ? 0.1328 0.1136 0.2084 0.0060  0.0179  0.0059  113 TYR   B CZ  
5774 O  OH  . TYR   B 113 ? 0.1393 0.1115 0.2304 0.0084  0.0257  0.0098  113 TYR   B OH  
5784 N  N   . GLU   B 114 ? 0.1169 0.1090 0.1830 -0.0031 0.0120  0.0071  114 GLU   B N   
5785 C  CA  . GLU   B 114 ? 0.1149 0.1067 0.1786 0.0013  0.0073  0.0043  114 GLU   B CA  
5786 C  C   . GLU   B 114 ? 0.1179 0.1093 0.1688 -0.0020 0.0075  0.0005  114 GLU   B C   
5787 O  O   . GLU   B 114 ? 0.1177 0.1093 0.1761 0.0014  0.0040  0.0128  114 GLU   B O   
5788 C  CB  . GLU   B 114 ? 0.1168 0.1196 0.1848 -0.0027 0.0103  0.0073  114 GLU   B CB  
5789 C  CG  . GLU   B 114 ? 0.1248 0.1164 0.1814 -0.0020 0.0132  0.0043  114 GLU   B CG  
5790 C  CD  . GLU   B 114 ? 0.1203 0.1208 0.1929 -0.0073 0.0078  0.0072  114 GLU   B CD  
5791 O  OE1 . GLU   B 114 ? 0.1191 0.1357 0.1836 -0.0067 0.0187  0.0075  114 GLU   B OE1 
5792 O  OE2 . GLU   B 114 ? 0.1218 0.1400 0.2132 -0.0163 0.0119  0.0110  114 GLU   B OE2 
5799 N  N   . ASN   B 115 ? 0.1205 0.1080 0.1702 -0.0033 0.0051  0.0023  115 ASN   B N   
5800 C  CA  . ASN   B 115 ? 0.1249 0.1145 0.1446 -0.0074 0.0021  0.0055  115 ASN   B CA  
5801 C  C   . ASN   B 115 ? 0.1180 0.1102 0.1566 -0.0104 -0.0074 0.0005  115 ASN   B C   
5802 O  O   . ASN   B 115 ? 0.1276 0.1140 0.1658 -0.0118 0.0029  0.0086  115 ASN   B O   
5803 C  CB  . ASN   B 115 ? 0.1315 0.1263 0.1540 -0.0071 0.0068  0.0063  115 ASN   B CB  
5804 C  CG  . ASN   B 115 ? 0.1394 0.1277 0.1534 0.0029  0.0036  0.0008  115 ASN   B CG  
5805 O  OD1 . ASN   B 115 ? 0.1844 0.1394 0.1820 0.0025  0.0142  -0.0066 115 ASN   B OD1 
5806 N  ND2 . ASN   B 115 ? 0.1375 0.1387 0.1504 -0.0020 0.0067  0.0034  115 ASN   B ND2 
5813 N  N   . PHE   B 116 ? 0.1172 0.1121 0.1489 -0.0048 0.0024  0.0029  116 PHE   B N   
5814 C  CA  . PHE   B 116 ? 0.1238 0.1168 0.1541 -0.0072 0.0019  -0.0000 116 PHE   B CA  
5815 C  C   . PHE   B 116 ? 0.1234 0.1031 0.1467 -0.0101 -0.0013 0.0054  116 PHE   B C   
5816 O  O   . PHE   B 116 ? 0.1278 0.1168 0.1552 -0.0054 -0.0013 0.0063  116 PHE   B O   
5817 C  CB  . PHE   B 116 ? 0.1188 0.1139 0.1554 -0.0023 -0.0109 0.0041  116 PHE   B CB  
5818 C  CG  . PHE   B 116 ? 0.1195 0.1112 0.1553 -0.0054 0.0035  0.0053  116 PHE   B CG  
5819 C  CD1 . PHE   B 116 ? 0.1228 0.1198 0.1746 -0.0014 0.0018  0.0035  116 PHE   B CD1 
5820 C  CD2 . PHE   B 116 ? 0.1250 0.1218 0.1500 -0.0057 0.0055  0.0026  116 PHE   B CD2 
5821 C  CE1 . PHE   B 116 ? 0.1265 0.1206 0.1643 -0.0037 -0.0072 0.0043  116 PHE   B CE1 
5822 C  CE2 . PHE   B 116 ? 0.1293 0.1151 0.1515 -0.0021 0.0023  0.0048  116 PHE   B CE2 
5823 C  CZ  . PHE   B 116 ? 0.1208 0.1222 0.1559 -0.0037 -0.0091 0.0094  116 PHE   B CZ  
5833 N  N   . ASN   B 117 ? 0.1249 0.1100 0.1581 -0.0021 -0.0054 0.0054  117 ASN   B N   
5834 C  CA  . ASN   B 117 ? 0.1306 0.1117 0.1529 0.0003  -0.0123 -0.0013 117 ASN   B CA  
5835 C  C   . ASN   B 117 ? 0.1318 0.1132 0.1693 0.0007  -0.0077 0.0062  117 ASN   B C   
5836 O  O   . ASN   B 117 ? 0.1345 0.1194 0.1949 -0.0022 -0.0245 0.0102  117 ASN   B O   
5837 C  CB  . ASN   B 117 ? 0.1285 0.1152 0.1705 -0.0002 -0.0101 -0.0007 117 ASN   B CB  
5838 C  CG  . ASN   B 117 ? 0.1246 0.1223 0.1830 0.0015  0.0029  -0.0047 117 ASN   B CG  
5839 O  OD1 . ASN   B 117 ? 0.1444 0.1218 0.1904 -0.0118 0.0033  -0.0070 117 ASN   B OD1 
5840 N  ND2 . ASN   B 117 ? 0.1270 0.1228 0.1756 0.0003  -0.0019 -0.0070 117 ASN   B ND2 
5847 N  N   . GLN   B 118 ? 0.1313 0.1085 0.1630 -0.0076 -0.0117 0.0011  118 GLN   B N   
5848 C  CA  . GLN   B 118 ? 0.1349 0.1120 0.1804 0.0007  -0.0081 0.0021  118 GLN   B CA  
5849 C  C   . GLN   B 118 ? 0.1371 0.1106 0.1766 -0.0014 -0.0043 0.0016  118 GLN   B C   
5850 O  O   . GLN   B 118 ? 0.1546 0.1151 0.2136 -0.0035 0.0083  0.0024  118 GLN   B O   
5851 C  CB  . GLN   B 118 ? 0.1423 0.1181 0.1901 0.0034  -0.0125 -0.0032 118 GLN   B CB  
5852 C  CG  . GLN   B 118 ? 0.1502 0.1169 0.1890 0.0068  -0.0110 -0.0045 118 GLN   B CG  
5853 C  CD  . GLN   B 118 ? 0.1529 0.1096 0.1877 0.0038  -0.0105 -0.0092 118 GLN   B CD  
5854 O  OE1 . GLN   B 118 ? 0.1566 0.1159 0.2073 0.0056  -0.0005 0.0007  118 GLN   B OE1 
5855 N  NE2 . GLN   B 118 ? 0.1562 0.1204 0.1807 0.0041  -0.0148 0.0011  118 GLN   B NE2 
5864 N  N   . HIS   B 119 ? 0.1350 0.1187 0.1547 -0.0037 -0.0036 0.0108  119 HIS   B N   
5865 C  CA  . HIS   B 119 ? 0.1429 0.1330 0.1450 -0.0038 -0.0129 0.0116  119 HIS   B CA  
5866 C  C   . HIS   B 119 ? 0.1456 0.1309 0.1463 -0.0067 -0.0243 0.0052  119 HIS   B C   
5867 O  O   . HIS   B 119 ? 0.1590 0.1299 0.1608 -0.0252 -0.0184 0.0057  119 HIS   B O   
5868 C  CB  . HIS   B 119 ? 0.1511 0.1428 0.1492 -0.0015 -0.0159 0.0021  119 HIS   B CB  
5869 C  CG  . HIS   B 119 ? 0.1553 0.1647 0.1648 0.0108  -0.0344 -0.0169 119 HIS   B CG  
5870 N  ND1 . HIS   B 119 ? 0.1672 0.1806 0.2084 0.0051  -0.0453 -0.0379 119 HIS   B ND1 
5871 C  CD2 . HIS   B 119 ? 0.1706 0.1832 0.1706 0.0395  -0.0381 -0.0232 119 HIS   B CD2 
5872 C  CE1 . HIS   B 119 ? 0.1839 0.1987 0.2182 0.0201  -0.0487 -0.0490 119 HIS   B CE1 
5873 N  NE2 . HIS   B 119 ? 0.1882 0.2056 0.1898 0.0366  -0.0477 -0.0434 119 HIS   B NE2 
5881 N  N   . GLU   B 120 ? 0.1643 0.1368 0.1455 -0.0090 -0.0292 0.0147  120 GLU   B N   
5882 C  CA  . GLU   B 120 ? 0.1904 0.1462 0.1626 -0.0083 -0.0421 0.0254  120 GLU   B CA  
5883 C  C   . GLU   B 120 ? 0.1726 0.1376 0.1583 -0.0149 -0.0311 0.0278  120 GLU   B C   
5884 O  O   . GLU   B 120 ? 0.1672 0.1506 0.1557 -0.0162 -0.0304 0.0156  120 GLU   B O   
5885 C  CB  . GLU   B 120 ? 0.2528 0.1764 0.2271 0.0086  -0.0737 0.0405  120 GLU   B CB  
5886 C  CG  . GLU   B 120 ? 0.3060 0.2517 0.3311 0.0197  -0.0996 0.0638  120 GLU   B CG  
5887 C  CD  . GLU   B 120 ? 0.3481 0.3201 0.4455 0.0190  -0.1101 0.0807  120 GLU   B CD  
5888 O  OE1 . GLU   B 120 ? 0.3699 0.3596 0.4883 0.0137  -0.1049 0.0908  120 GLU   B OE1 
5889 O  OE2 . GLU   B 120 ? 0.3695 0.3625 0.5028 0.0180  -0.1114 0.0762  120 GLU   B OE2 
5896 N  N   . VAL   B 121 ? 0.1615 0.1316 0.1558 -0.0202 -0.0197 0.0227  121 VAL   B N   
5897 C  CA  . VAL   B 121 ? 0.1600 0.1392 0.1345 -0.0186 -0.0197 0.0134  121 VAL   B CA  
5898 C  C   . VAL   B 121 ? 0.1505 0.1355 0.1278 -0.0249 -0.0163 0.0117  121 VAL   B C   
5899 O  O   . VAL   B 121 ? 0.1569 0.1339 0.1526 -0.0295 -0.0238 0.0072  121 VAL   B O   
5900 C  CB  . VAL   B 121 ? 0.1832 0.1767 0.1463 -0.0037 -0.0227 0.0212  121 VAL   B CB  
5901 C  CG1 . VAL   B 121 ? 0.1904 0.1906 0.1808 -0.0146 -0.0156 0.0170  121 VAL   B CG1 
5902 C  CG2 . VAL   B 121 ? 0.2043 0.1993 0.1428 0.0050  -0.0173 0.0121  121 VAL   B CG2 
5912 N  N   . LEU   B 122 ? 0.1417 0.1300 0.1293 -0.0186 -0.0170 0.0085  122 LEU   B N   
5913 C  CA  . LEU   B 122 ? 0.1378 0.1381 0.1108 -0.0201 -0.0169 0.0080  122 LEU   B CA  
5914 C  C   . LEU   B 122 ? 0.1360 0.1301 0.1216 -0.0263 -0.0154 0.0027  122 LEU   B C   
5915 O  O   . LEU   B 122 ? 0.1407 0.1332 0.1573 -0.0276 -0.0221 -0.0044 122 LEU   B O   
5916 C  CB  . LEU   B 122 ? 0.1639 0.1482 0.1487 -0.0003 -0.0219 0.0098  122 LEU   B CB  
5917 C  CG  . LEU   B 122 ? 0.1488 0.1493 0.1563 -0.0119 -0.0118 0.0089  122 LEU   B CG  
5918 C  CD1 . LEU   B 122 ? 0.1524 0.1700 0.1627 -0.0207 -0.0167 0.0011  122 LEU   B CD1 
5919 C  CD2 . LEU   B 122 ? 0.1503 0.1482 0.1327 -0.0124 -0.0086 -0.0021 122 LEU   B CD2 
5931 N  N   . LEU   B 123 ? 0.1407 0.1199 0.1243 -0.0234 -0.0109 0.0059  123 LEU   B N   
5932 C  CA  . LEU   B 123 ? 0.1410 0.1198 0.1266 -0.0222 -0.0146 -0.0014 123 LEU   B CA  
5933 C  C   . LEU   B 123 ? 0.1358 0.1192 0.1277 -0.0231 -0.0136 0.0026  123 LEU   B C   
5934 O  O   . LEU   B 123 ? 0.1433 0.1163 0.1340 -0.0269 -0.0142 0.0035  123 LEU   B O   
5935 C  CB  . LEU   B 123 ? 0.1463 0.1217 0.1343 -0.0226 -0.0117 -0.0025 123 LEU   B CB  
5936 C  CG  . LEU   B 123 ? 0.1380 0.1282 0.1475 -0.0178 -0.0051 0.0071  123 LEU   B CG  
5937 C  CD1 . LEU   B 123 ? 0.1511 0.1304 0.1641 -0.0135 0.0060  -0.0129 123 LEU   B CD1 
5938 C  CD2 . LEU   B 123 ? 0.1484 0.1390 0.1622 -0.0142 0.0008  0.0194  123 LEU   B CD2 
5950 N  N   . ALA   B 124 ? 0.1337 0.1162 0.1256 -0.0208 -0.0040 -0.0034 124 ALA   B N   
5951 C  CA  . ALA   B 124 ? 0.1284 0.1149 0.1380 -0.0135 -0.0077 -0.0073 124 ALA   B CA  
5952 C  C   . ALA   B 124 ? 0.1240 0.1153 0.1330 -0.0176 -0.0109 -0.0010 124 ALA   B C   
5953 O  O   . ALA   B 124 ? 0.1337 0.1164 0.1473 -0.0134 -0.0092 0.0008  124 ALA   B O   
5954 C  CB  . ALA   B 124 ? 0.1324 0.1196 0.1410 -0.0039 0.0016  -0.0061 124 ALA   B CB  
5960 N  N   . PRO   B 125 ? 0.1297 0.1142 0.1425 -0.0152 -0.0120 0.0111  125 PRO   B N   
5961 C  CA  . PRO   B 125 ? 0.1396 0.1200 0.1541 -0.0143 -0.0131 0.0198  125 PRO   B CA  
5962 C  C   . PRO   B 125 ? 0.1362 0.1124 0.1629 -0.0133 -0.0054 0.0071  125 PRO   B C   
5963 O  O   . PRO   B 125 ? 0.1385 0.1141 0.1777 -0.0080 0.0028  0.0147  125 PRO   B O   
5964 C  CB  . PRO   B 125 ? 0.1411 0.1440 0.1582 -0.0177 -0.0130 0.0348  125 PRO   B CB  
5965 C  CG  . PRO   B 125 ? 0.1462 0.1475 0.1478 -0.0293 -0.0130 0.0179  125 PRO   B CG  
5966 C  CD  . PRO   B 125 ? 0.1423 0.1253 0.1384 -0.0300 -0.0027 0.0070  125 PRO   B CD  
5974 N  N   . LEU   B 126 ? 0.1369 0.1084 0.1847 -0.0095 0.0150  0.0106  126 LEU   B N   
5975 C  CA  . LEU   B 126 ? 0.1509 0.1177 0.1864 -0.0073 0.0271  0.0136  126 LEU   B CA  
5976 C  C   . LEU   B 126 ? 0.1479 0.1259 0.1913 0.0050  0.0273  0.0198  126 LEU   B C   
5977 O  O   . LEU   B 126 ? 0.1665 0.1571 0.1954 0.0226  -0.0002 -0.0020 126 LEU   B O   
5978 C  CB  . LEU   B 126 ? 0.1672 0.1248 0.2177 -0.0141 0.0269  0.0044  126 LEU   B CB  
5979 C  CG  . LEU   B 126 ? 0.1784 0.1331 0.2257 -0.0220 0.0291  -0.0139 126 LEU   B CG  
5980 C  CD1 . LEU   B 126 ? 0.1907 0.1409 0.2727 -0.0192 0.0126  -0.0205 126 LEU   B CD1 
5981 C  CD2 . LEU   B 126 ? 0.1779 0.1444 0.2173 -0.0293 0.0201  -0.0171 126 LEU   B CD2 
5993 N  N   . LEU   B 127 ? 0.1418 0.1168 0.1960 0.0030  0.0272  0.0133  127 LEU   B N   
5994 C  CA  . LEU   B 127 ? 0.1389 0.1280 0.2003 -0.0043 0.0283  0.0219  127 LEU   B CA  
5995 C  C   . LEU   B 127 ? 0.1355 0.1251 0.1945 0.0018  0.0215  0.0229  127 LEU   B C   
5996 O  O   . LEU   B 127 ? 0.1419 0.1263 0.2064 -0.0103 0.0111  0.0247  127 LEU   B O   
5997 C  CB  . LEU   B 127 ? 0.1521 0.1272 0.2044 0.0012  0.0244  0.0251  127 LEU   B CB  
5998 C  CG  . LEU   B 127 ? 0.1629 0.1257 0.2157 0.0047  0.0288  0.0143  127 LEU   B CG  
5999 C  CD1 . LEU   B 127 ? 0.1713 0.1198 0.2271 0.0052  0.0256  0.0103  127 LEU   B CD1 
6000 C  CD2 . LEU   B 127 ? 0.1622 0.1375 0.2361 -0.0052 0.0338  0.0296  127 LEU   B CD2 
6012 N  N   . SER   B 128 ? 0.1398 0.1257 0.1878 0.0041  0.0064  0.0148  128 SER   B N   
6013 C  CA  . SER   B 128 ? 0.1530 0.1358 0.1894 0.0126  -0.0025 0.0251  128 SER   B CA  
6014 C  C   . SER   B 128 ? 0.1660 0.1410 0.2128 0.0120  -0.0206 0.0243  128 SER   B C   
6015 O  O   . SER   B 128 ? 0.1829 0.1437 0.2387 0.0100  -0.0095 0.0354  128 SER   B O   
6016 C  CB  . SER   B 128 ? 0.1637 0.1358 0.1934 0.0094  0.0103  0.0294  128 SER   B CB  
6017 O  OG  . SER   B 128 ? 0.1723 0.1488 0.1996 0.0101  0.0137  0.0363  128 SER   B OG  
6023 N  N   . ALA   B 129 ? 0.1800 0.1415 0.2422 0.0245  -0.0128 0.0076  129 ALA   B N   
6024 C  CA  . ALA   B 129 ? 0.1957 0.1433 0.2468 0.0280  -0.0122 -0.0009 129 ALA   B CA  
6025 C  C   . ALA   B 129 ? 0.1805 0.1383 0.2302 0.0211  0.0070  0.0102  129 ALA   B C   
6026 O  O   . ALA   B 129 ? 0.1636 0.1453 0.2345 0.0209  0.0012  0.0114  129 ALA   B O   
6027 C  CB  . ALA   B 129 ? 0.2157 0.1685 0.2804 0.0341  -0.0051 -0.0139 129 ALA   B CB  
6033 N  N   . GLY   B 130 ? 0.1808 0.1363 0.2327 0.0263  0.0078  0.0010  130 GLY   B N   
6034 C  CA  . GLY   B 130 ? 0.1855 0.1485 0.2455 0.0218  0.0267  -0.0008 130 GLY   B CA  
6035 C  C   . GLY   B 130 ? 0.1845 0.1506 0.2457 0.0190  0.0231  0.0074  130 GLY   B C   
6036 O  O   . GLY   B 130 ? 0.2019 0.1617 0.2507 0.0168  0.0157  0.0189  130 GLY   B O   
6040 N  N   . ILE   B 131 ? 0.1798 0.1667 0.2593 0.0309  0.0214  0.0028  131 ILE   B N   
6041 C  CA  . ILE   B 131 ? 0.1987 0.1820 0.2578 0.0298  0.0069  0.0160  131 ILE   B CA  
6042 C  C   . ILE   B 131 ? 0.2139 0.1749 0.2208 0.0231  0.0027  0.0204  131 ILE   B C   
6043 O  O   . ILE   B 131 ? 0.2419 0.1870 0.2271 0.0285  -0.0212 0.0211  131 ILE   B O   
6044 C  CB  . ILE   B 131 ? 0.1955 0.2153 0.2976 0.0254  -0.0052 0.0238  131 ILE   B CB  
6045 C  CG1 . ILE   B 131 ? 0.1945 0.2392 0.3135 -0.0011 0.0055  0.0288  131 ILE   B CG1 
6046 C  CG2 . ILE   B 131 ? 0.1975 0.2264 0.3232 0.0280  -0.0010 0.0189  131 ILE   B CG2 
6047 C  CD1 . ILE   B 131 ? 0.1978 0.2611 0.3275 -0.0155 0.0067  0.0352  131 ILE   B CD1 
6059 N  N   . PHE   B 132 ? 0.1969 0.1540 0.2080 0.0166  0.0191  0.0203  132 PHE   B N   
6060 C  CA  . PHE   B 132 ? 0.2072 0.1573 0.2082 0.0110  0.0402  0.0132  132 PHE   B CA  
6061 C  C   . PHE   B 132 ? 0.2243 0.1686 0.2247 0.0112  0.0514  0.0132  132 PHE   B C   
6062 O  O   . PHE   B 132 ? 0.2412 0.1939 0.2436 0.0053  0.0590  0.0169  132 PHE   B O   
6063 C  CB  . PHE   B 132 ? 0.1950 0.1534 0.1890 0.0192  0.0334  0.0268  132 PHE   B CB  
6064 C  CG  . PHE   B 132 ? 0.1905 0.1535 0.1820 0.0217  0.0288  0.0259  132 PHE   B CG  
6065 C  CD1 . PHE   B 132 ? 0.1969 0.1538 0.2184 0.0180  0.0243  0.0217  132 PHE   B CD1 
6066 C  CD2 . PHE   B 132 ? 0.1893 0.1600 0.1626 0.0302  0.0237  0.0257  132 PHE   B CD2 
6067 C  CE1 . PHE   B 132 ? 0.1996 0.1594 0.2286 0.0083  0.0164  0.0226  132 PHE   B CE1 
6068 C  CE2 . PHE   B 132 ? 0.1960 0.1663 0.1678 0.0215  0.0098  0.0175  132 PHE   B CE2 
6069 C  CZ  . PHE   B 132 ? 0.1984 0.1608 0.2032 0.0093  -0.0048 0.0281  132 PHE   B CZ  
6079 N  N   . GLY   B 133 ? 0.2200 0.1589 0.2317 0.0068  0.0334  0.0319  133 GLY   B N   
6080 C  CA  . GLY   B 133 ? 0.2289 0.1711 0.2465 -0.0124 0.0300  0.0462  133 GLY   B CA  
6081 C  C   . GLY   B 133 ? 0.2359 0.1830 0.2394 -0.0227 0.0423  0.0509  133 GLY   B C   
6082 O  O   . GLY   B 133 ? 0.2577 0.1976 0.2761 -0.0370 0.0409  0.0646  133 GLY   B O   
6086 N  N   . ALA   B 134 ? 0.2179 0.1779 0.2260 -0.0229 0.0442  0.0338  134 ALA   B N   
6087 C  CA  . ALA   B 134 ? 0.2080 0.1760 0.2363 -0.0161 0.0524  0.0192  134 ALA   B CA  
6088 C  C   . ALA   B 134 ? 0.2141 0.1664 0.2498 -0.0078 0.0432  0.0300  134 ALA   B C   
6089 O  O   . ALA   B 134 ? 0.2203 0.1824 0.2611 0.0048  0.0351  0.0178  134 ALA   B O   
6090 C  CB  . ALA   B 134 ? 0.2050 0.1776 0.2544 -0.0081 0.0386  0.0136  134 ALA   B CB  
6096 N  N   . ASP   B 135 ? 0.2252 0.1639 0.2501 -0.0087 0.0215  0.0370  135 ASP   B N   
6097 C  CA  . ASP   B 135 ? 0.2426 0.1542 0.2730 -0.0117 0.0078  0.0387  135 ASP   B CA  
6098 C  C   . ASP   B 135 ? 0.2218 0.1383 0.2600 -0.0019 0.0062  0.0344  135 ASP   B C   
6099 O  O   . ASP   B 135 ? 0.2191 0.1341 0.2627 0.0006  0.0094  0.0354  135 ASP   B O   
6100 C  CB  . ASP   B 135 ? 0.2733 0.1648 0.2982 -0.0329 0.0086  0.0441  135 ASP   B CB  
6101 C  CG  . ASP   B 135 ? 0.3048 0.1670 0.3375 -0.0522 0.0111  0.0387  135 ASP   B CG  
6102 O  OD1 . ASP   B 135 ? 0.3088 0.1505 0.3339 -0.0345 0.0025  0.0363  135 ASP   B OD1 
6103 O  OD2 . ASP   B 135 ? 0.3294 0.2007 0.3778 -0.0705 0.0113  0.0206  135 ASP   B OD2 
6108 N  N   . PRO   B 136 ? 0.2103 0.1435 0.2722 0.0184  -0.0021 0.0268  136 PRO   B N   
6109 C  CA  . PRO   B 136 ? 0.1906 0.1350 0.2677 0.0166  0.0013  0.0170  136 PRO   B CA  
6110 C  C   . PRO   B 136 ? 0.1755 0.1255 0.2762 0.0136  0.0069  0.0128  136 PRO   B C   
6111 O  O   . PRO   B 136 ? 0.1630 0.1249 0.2602 0.0090  0.0038  0.0175  136 PRO   B O   
6112 C  CB  . PRO   B 136 ? 0.1980 0.1631 0.2793 0.0308  -0.0044 0.0099  136 PRO   B CB  
6113 C  CG  . PRO   B 136 ? 0.2166 0.1695 0.2960 0.0320  -0.0004 0.0081  136 PRO   B CG  
6114 C  CD  . PRO   B 136 ? 0.2160 0.1590 0.2886 0.0387  0.0040  0.0114  136 PRO   B CD  
6122 N  N   . ILE   B 137 ? 0.1841 0.1161 0.2873 0.0082  -0.0013 0.0066  137 ILE   B N   
6123 C  CA  . ILE   B 137 ? 0.1901 0.1132 0.2948 -0.0029 0.0008  0.0028  137 ILE   B CA  
6124 C  C   . ILE   B 137 ? 0.1817 0.1227 0.2777 -0.0069 0.0112  0.0160  137 ILE   B C   
6125 O  O   . ILE   B 137 ? 0.1743 0.1304 0.2618 -0.0091 0.0124  0.0103  137 ILE   B O   
6126 C  CB  . ILE   B 137 ? 0.2150 0.1271 0.3451 -0.0050 0.0023  0.0083  137 ILE   B CB  
6127 C  CG1 . ILE   B 137 ? 0.2400 0.1408 0.4030 0.0022  0.0094  -0.0022 137 ILE   B CG1 
6128 C  CG2 . ILE   B 137 ? 0.2205 0.1352 0.3500 -0.0257 0.0036  0.0086  137 ILE   B CG2 
6129 C  CD1 . ILE   B 137 ? 0.2588 0.1714 0.4419 0.0174  0.0026  0.0054  137 ILE   B CD1 
6141 N  N   . HIS   B 138 ? 0.1838 0.1235 0.2837 -0.0051 0.0205  0.0195  138 HIS   B N   
6142 C  CA  . HIS   B 138 ? 0.1911 0.1323 0.2747 -0.0042 0.0362  0.0213  138 HIS   B CA  
6143 C  C   . HIS   B 138 ? 0.1763 0.1336 0.2532 -0.0038 0.0378  0.0228  138 HIS   B C   
6144 O  O   . HIS   B 138 ? 0.1697 0.1393 0.2777 0.0045  0.0439  0.0340  138 HIS   B O   
6145 C  CB  . HIS   B 138 ? 0.2153 0.1415 0.2900 -0.0060 0.0542  0.0208  138 HIS   B CB  
6146 C  CG  . HIS   B 138 ? 0.2422 0.1572 0.2977 -0.0097 0.0679  0.0440  138 HIS   B CG  
6147 N  ND1 . HIS   B 138 ? 0.2508 0.1763 0.3202 -0.0086 0.0823  0.0337  138 HIS   B ND1 
6148 C  CD2 . HIS   B 138 ? 0.2587 0.1647 0.2998 -0.0101 0.0729  0.0345  138 HIS   B CD2 
6149 C  CE1 . HIS   B 138 ? 0.2577 0.1769 0.3089 -0.0078 0.0901  0.0329  138 HIS   B CE1 
6150 N  NE2 . HIS   B 138 ? 0.2644 0.1634 0.2929 -0.0027 0.0850  0.0225  138 HIS   B NE2 
6158 N  N   . SER   B 139 ? 0.1735 0.1231 0.2495 0.0023  0.0296  0.0157  139 SER   B N   
6159 C  CA  . SER   B 139 ? 0.1714 0.1138 0.2431 -0.0025 0.0309  0.0095  139 SER   B CA  
6160 C  C   . SER   B 139 ? 0.1473 0.1048 0.2459 -0.0025 0.0246  0.0121  139 SER   B C   
6161 O  O   . SER   B 139 ? 0.1473 0.1113 0.2408 0.0010  0.0110  0.0119  139 SER   B O   
6162 C  CB  . SER   B 139 ? 0.1767 0.1161 0.2500 0.0027  0.0115  0.0130  139 SER   B CB  
6163 O  OG  . SER   B 139 ? 0.1737 0.1172 0.2443 0.0011  -0.0053 0.0161  139 SER   B OG  
6169 N  N   . LEU   B 140 ? 0.1454 0.1035 0.2456 -0.0071 0.0235  0.0034  140 LEU   B N   
6170 C  CA  . LEU   B 140 ? 0.1415 0.1128 0.2399 -0.0014 0.0181  0.0092  140 LEU   B CA  
6171 C  C   . LEU   B 140 ? 0.1377 0.1158 0.2493 -0.0053 0.0070  0.0003  140 LEU   B C   
6172 O  O   . LEU   B 140 ? 0.1391 0.1234 0.2477 -0.0014 0.0019  0.0071  140 LEU   B O   
6173 C  CB  . LEU   B 140 ? 0.1446 0.1134 0.2438 -0.0099 0.0217  -0.0001 140 LEU   B CB  
6174 C  CG  . LEU   B 140 ? 0.1544 0.1142 0.2367 -0.0100 0.0100  0.0034  140 LEU   B CG  
6175 C  CD1 . LEU   B 140 ? 0.1642 0.1279 0.2491 -0.0029 0.0195  0.0025  140 LEU   B CD1 
6176 C  CD2 . LEU   B 140 ? 0.1728 0.1271 0.2530 -0.0135 0.0005  -0.0094 140 LEU   B CD2 
6188 N  N   . ARG   B 141 ? 0.1346 0.1154 0.2629 -0.0100 0.0109  -0.0021 141 ARG   B N   
6189 C  CA  . ARG   B 141 ? 0.1408 0.1156 0.2959 -0.0132 0.0272  0.0007  141 ARG   B CA  
6190 C  C   . ARG   B 141 ? 0.1343 0.1156 0.2755 -0.0116 0.0232  -0.0002 141 ARG   B C   
6191 O  O   . ARG   B 141 ? 0.1390 0.1156 0.2787 -0.0158 0.0172  -0.0108 141 ARG   B O   
6192 C  CB  . ARG   B 141 ? 0.1575 0.1243 0.3237 -0.0194 0.0430  0.0019  141 ARG   B CB  
6193 C  CG  . ARG   B 141 ? 0.1848 0.1529 0.3405 -0.0247 0.0416  -0.0010 141 ARG   B CG  
6194 C  CD  . ARG   B 141 ? 0.2237 0.1771 0.3410 -0.0171 0.0179  -0.0175 141 ARG   B CD  
6195 N  NE  . ARG   B 141 ? 0.2433 0.1785 0.3342 -0.0252 0.0239  -0.0231 141 ARG   B NE  
6196 C  CZ  . ARG   B 141 ? 0.2531 0.1631 0.3099 -0.0176 0.0366  -0.0330 141 ARG   B CZ  
6197 N  NH1 . ARG   B 141 ? 0.2660 0.1570 0.3081 -0.0172 0.0317  -0.0305 141 ARG   B NH1 
6198 N  NH2 . ARG   B 141 ? 0.2649 0.1719 0.3197 -0.0082 0.0281  -0.0204 141 ARG   B NH2 
6212 N  N   . VAL   B 142 ? 0.1380 0.1135 0.2633 -0.0049 0.0223  -0.0032 142 VAL   B N   
6213 C  CA  . VAL   B 142 ? 0.1366 0.1127 0.2494 -0.0038 0.0289  -0.0011 142 VAL   B CA  
6214 C  C   . VAL   B 142 ? 0.1317 0.1127 0.2467 -0.0044 0.0158  -0.0091 142 VAL   B C   
6215 O  O   . VAL   B 142 ? 0.1422 0.1099 0.2593 0.0012  0.0118  0.0003  142 VAL   B O   
6216 C  CB  . VAL   B 142 ? 0.1487 0.1279 0.2514 0.0022  0.0285  0.0151  142 VAL   B CB  
6217 C  CG1 . VAL   B 142 ? 0.1408 0.1277 0.2504 0.0105  0.0287  0.0114  142 VAL   B CG1 
6218 C  CG2 . VAL   B 142 ? 0.1709 0.1260 0.2653 0.0062  0.0250  0.0207  142 VAL   B CG2 
6228 N  N   . CYS   B 143 ? 0.1305 0.1155 0.2366 -0.0031 0.0116  0.0042  143 CYS   B N   
6229 C  CA  . CYS   B 143 ? 0.1277 0.1131 0.2295 -0.0098 0.0167  0.0038  143 CYS   B CA  
6230 C  C   . CYS   B 143 ? 0.1218 0.1167 0.2329 -0.0062 0.0159  -0.0072 143 CYS   B C   
6231 O  O   . CYS   B 143 ? 0.1276 0.1227 0.2273 -0.0067 0.0024  -0.0031 143 CYS   B O   
6232 C  CB  . CYS   B 143 ? 0.1336 0.1228 0.2252 -0.0069 0.0103  -0.0003 143 CYS   B CB  
6233 S  SG  . CYS   B 143 ? 0.1361 0.1361 0.2186 -0.0052 0.0110  0.0052  143 CYS   B SG  
6239 N  N   . VAL   B 144 ? 0.1327 0.1173 0.2469 -0.0054 0.0060  -0.0198 144 VAL   B N   
6240 C  CA  . VAL   B 144 ? 0.1409 0.1245 0.2675 -0.0112 -0.0046 -0.0225 144 VAL   B CA  
6241 C  C   . VAL   B 144 ? 0.1320 0.1260 0.2676 -0.0117 -0.0003 -0.0055 144 VAL   B C   
6242 O  O   . VAL   B 144 ? 0.1452 0.1463 0.2812 0.0012  0.0007  0.0109  144 VAL   B O   
6243 C  CB  . VAL   B 144 ? 0.1643 0.1375 0.3247 -0.0155 -0.0140 -0.0332 144 VAL   B CB  
6244 C  CG1 . VAL   B 144 ? 0.1895 0.1740 0.3603 -0.0057 -0.0213 -0.0281 144 VAL   B CG1 
6245 C  CG2 . VAL   B 144 ? 0.1753 0.1364 0.3208 -0.0010 -0.0246 -0.0387 144 VAL   B CG2 
6255 N  N   . ASP   B 145 ? 0.1317 0.1230 0.2749 -0.0096 -0.0021 -0.0142 145 ASP   B N   
6256 C  CA  . ASP   B 145 ? 0.1327 0.1242 0.2958 -0.0081 0.0082  -0.0118 145 ASP   B CA  
6257 C  C   . ASP   B 145 ? 0.1281 0.1277 0.2796 -0.0065 0.0162  -0.0097 145 ASP   B C   
6258 O  O   . ASP   B 145 ? 0.1280 0.1438 0.3386 -0.0100 0.0168  -0.0204 145 ASP   B O   
6259 C  CB  . ASP   B 145 ? 0.1442 0.1340 0.3379 -0.0167 0.0247  -0.0089 145 ASP   B CB  
6260 C  CG  . ASP   B 145 ? 0.1601 0.1397 0.3868 -0.0228 0.0386  -0.0065 145 ASP   B CG  
6261 O  OD1 . ASP   B 145 ? 0.1645 0.1433 0.3934 -0.0224 0.0095  -0.0110 145 ASP   B OD1 
6262 O  OD2 . ASP   B 145 ? 0.1850 0.1489 0.4255 -0.0268 0.0610  0.0002  145 ASP   B OD2 
6267 N  N   . THR   B 146 ? 0.1221 0.1169 0.2337 -0.0085 0.0084  0.0017  146 THR   B N   
6268 C  CA  . THR   B 146 ? 0.1315 0.1159 0.2156 -0.0042 0.0129  -0.0048 146 THR   B CA  
6269 C  C   . THR   B 146 ? 0.1291 0.1173 0.2115 -0.0036 -0.0002 0.0016  146 THR   B C   
6270 O  O   . THR   B 146 ? 0.1317 0.1167 0.2169 -0.0048 0.0009  0.0020  146 THR   B O   
6271 C  CB  . THR   B 146 ? 0.1359 0.1151 0.2297 -0.0054 0.0200  0.0059  146 THR   B CB  
6272 O  OG1 . THR   B 146 ? 0.1382 0.1169 0.2397 -0.0061 0.0185  0.0123  146 THR   B OG1 
6273 C  CG2 . THR   B 146 ? 0.1439 0.1191 0.2285 -0.0067 0.0167  0.0089  146 THR   B CG2 
6281 N  N   . VAL   B 147 ? 0.1334 0.1219 0.2055 -0.0039 0.0135  0.0061  147 VAL   B N   
6282 C  CA  . VAL   B 147 ? 0.1349 0.1189 0.1925 -0.0083 0.0040  -0.0003 147 VAL   B CA  
6283 C  C   . VAL   B 147 ? 0.1297 0.1182 0.2070 -0.0132 -0.0066 -0.0029 147 VAL   B C   
6284 O  O   . VAL   B 147 ? 0.1457 0.1283 0.2230 -0.0200 -0.0248 -0.0107 147 VAL   B O   
6285 C  CB  . VAL   B 147 ? 0.1369 0.1329 0.1851 -0.0042 -0.0035 0.0021  147 VAL   B CB  
6286 C  CG1 . VAL   B 147 ? 0.1349 0.1473 0.1773 -0.0120 0.0005  0.0057  147 VAL   B CG1 
6287 C  CG2 . VAL   B 147 ? 0.1414 0.1219 0.1944 -0.0059 0.0065  -0.0028 147 VAL   B CG2 
6297 N  N   . ARG   B 148 ? 0.1354 0.1186 0.1988 -0.0068 -0.0109 -0.0091 148 ARG   B N   
6298 C  CA  . ARG   B 148 ? 0.1348 0.1312 0.1911 -0.0096 -0.0195 -0.0056 148 ARG   B CA  
6299 C  C   . ARG   B 148 ? 0.1411 0.1434 0.1828 -0.0082 -0.0232 -0.0066 148 ARG   B C   
6300 O  O   . ARG   B 148 ? 0.1615 0.1723 0.1792 -0.0238 -0.0321 0.0042  148 ARG   B O   
6301 C  CB  . ARG   B 148 ? 0.1364 0.1356 0.1975 -0.0049 -0.0289 -0.0163 148 ARG   B CB  
6302 C  CG  . ARG   B 148 ? 0.1392 0.1520 0.2127 -0.0068 -0.0216 -0.0309 148 ARG   B CG  
6303 C  CD  . ARG   B 148 ? 0.1448 0.1672 0.2240 0.0076  -0.0238 -0.0325 148 ARG   B CD  
6304 N  NE  . ARG   B 148 ? 0.1463 0.1637 0.2159 0.0221  -0.0299 -0.0292 148 ARG   B NE  
6305 C  CZ  . ARG   B 148 ? 0.1392 0.1528 0.1953 0.0130  -0.0229 -0.0180 148 ARG   B CZ  
6306 N  NH1 . ARG   B 148 ? 0.1330 0.1583 0.2023 -0.0038 -0.0038 -0.0130 148 ARG   B NH1 
6307 N  NH2 . ARG   B 148 ? 0.1635 0.1367 0.1953 0.0192  -0.0105 -0.0143 148 ARG   B NH2 
6321 N  N   . THR   B 149 ? 0.1373 0.1314 0.1880 -0.0102 -0.0239 -0.0024 149 THR   B N   
6322 C  CA  . THR   B 149 ? 0.1442 0.1395 0.1807 -0.0125 -0.0229 0.0046  149 THR   B CA  
6323 C  C   . THR   B 149 ? 0.1432 0.1314 0.1626 -0.0162 -0.0260 0.0018  149 THR   B C   
6324 O  O   . THR   B 149 ? 0.1501 0.1348 0.1750 -0.0221 -0.0107 0.0052  149 THR   B O   
6325 C  CB  . THR   B 149 ? 0.1483 0.1330 0.1803 -0.0118 -0.0223 0.0026  149 THR   B CB  
6326 O  OG1 . THR   B 149 ? 0.1490 0.1374 0.1764 -0.0228 -0.0255 0.0055  149 THR   B OG1 
6327 C  CG2 . THR   B 149 ? 0.1530 0.1360 0.1965 -0.0032 -0.0195 0.0013  149 THR   B CG2 
6335 N  N   . ASN   B 150 ? 0.1500 0.1301 0.1706 -0.0174 -0.0312 -0.0019 150 ASN   B N   
6336 C  CA  . ASN   B 150 ? 0.1579 0.1505 0.1583 -0.0208 -0.0277 -0.0051 150 ASN   B CA  
6337 C  C   . ASN   B 150 ? 0.1511 0.1396 0.1537 -0.0167 -0.0222 -0.0022 150 ASN   B C   
6338 O  O   . ASN   B 150 ? 0.1583 0.1387 0.1766 -0.0276 -0.0374 -0.0002 150 ASN   B O   
6339 C  CB  . ASN   B 150 ? 0.1804 0.1838 0.1645 -0.0201 -0.0388 0.0053  150 ASN   B CB  
6340 C  CG  . ASN   B 150 ? 0.2054 0.2242 0.1989 -0.0208 -0.0363 0.0247  150 ASN   B CG  
6341 O  OD1 . ASN   B 150 ? 0.2110 0.2406 0.2136 -0.0312 -0.0522 0.0190  150 ASN   B OD1 
6342 N  ND2 . ASN   B 150 ? 0.2234 0.2433 0.2366 -0.0057 -0.0455 0.0658  150 ASN   B ND2 
6349 N  N   . VAL   B 151 ? 0.1432 0.1378 0.1591 -0.0194 -0.0226 0.0033  151 VAL   B N   
6350 C  CA  . VAL   B 151 ? 0.1457 0.1416 0.1648 -0.0206 -0.0206 -0.0011 151 VAL   B CA  
6351 C  C   . VAL   B 151 ? 0.1465 0.1332 0.1668 -0.0307 -0.0212 -0.0014 151 VAL   B C   
6352 O  O   . VAL   B 151 ? 0.1528 0.1433 0.1919 -0.0292 -0.0121 -0.0101 151 VAL   B O   
6353 C  CB  . VAL   B 151 ? 0.1633 0.1489 0.1734 -0.0098 -0.0173 -0.0078 151 VAL   B CB  
6354 C  CG1 . VAL   B 151 ? 0.1665 0.1555 0.1954 -0.0120 -0.0007 -0.0143 151 VAL   B CG1 
6355 C  CG2 . VAL   B 151 ? 0.1779 0.1643 0.1709 -0.0002 -0.0112 0.0097  151 VAL   B CG2 
6365 N  N   . TYR   B 152 ? 0.1404 0.1210 0.1609 -0.0245 -0.0195 -0.0012 152 TYR   B N   
6366 C  CA  . TYR   B 152 ? 0.1453 0.1415 0.1516 -0.0263 -0.0136 -0.0081 152 TYR   B CA  
6367 C  C   . TYR   B 152 ? 0.1402 0.1283 0.1395 -0.0207 -0.0075 -0.0088 152 TYR   B C   
6368 O  O   . TYR   B 152 ? 0.1501 0.1289 0.1458 -0.0263 -0.0100 -0.0008 152 TYR   B O   
6369 C  CB  . TYR   B 152 ? 0.1556 0.1519 0.1582 -0.0284 -0.0059 0.0057  152 TYR   B CB  
6370 C  CG  . TYR   B 152 ? 0.1719 0.1635 0.1511 -0.0404 -0.0088 0.0024  152 TYR   B CG  
6371 C  CD1 . TYR   B 152 ? 0.1850 0.1767 0.1374 -0.0319 -0.0141 0.0097  152 TYR   B CD1 
6372 C  CD2 . TYR   B 152 ? 0.1962 0.1803 0.1541 -0.0403 -0.0089 -0.0053 152 TYR   B CD2 
6373 C  CE1 . TYR   B 152 ? 0.1991 0.1934 0.1492 -0.0294 -0.0243 0.0171  152 TYR   B CE1 
6374 C  CE2 . TYR   B 152 ? 0.2076 0.2009 0.1493 -0.0358 -0.0158 -0.0079 152 TYR   B CE2 
6375 C  CZ  . TYR   B 152 ? 0.2093 0.2146 0.1424 -0.0321 -0.0350 0.0178  152 TYR   B CZ  
6376 O  OH  . TYR   B 152 ? 0.2309 0.2451 0.1848 -0.0220 -0.0381 0.0194  152 TYR   B OH  
6386 N  N   . LEU   B 153 ? 0.1436 0.1227 0.1567 -0.0308 -0.0078 -0.0056 153 LEU   B N   
6387 C  CA  . LEU   B 153 ? 0.1455 0.1173 0.1504 -0.0204 -0.0063 -0.0066 153 LEU   B CA  
6388 C  C   . LEU   B 153 ? 0.1471 0.1179 0.1596 -0.0243 -0.0050 -0.0106 153 LEU   B C   
6389 O  O   . LEU   B 153 ? 0.1539 0.1405 0.1718 -0.0119 -0.0059 -0.0337 153 LEU   B O   
6390 C  CB  . LEU   B 153 ? 0.1493 0.1222 0.1636 -0.0231 -0.0014 -0.0042 153 LEU   B CB  
6391 C  CG  . LEU   B 153 ? 0.1443 0.1347 0.1846 -0.0239 -0.0002 -0.0031 153 LEU   B CG  
6392 C  CD1 . LEU   B 153 ? 0.1552 0.1496 0.2033 -0.0255 -0.0014 0.0075  153 LEU   B CD1 
6393 C  CD2 . LEU   B 153 ? 0.1485 0.1473 0.1774 -0.0242 0.0074  0.0007  153 LEU   B CD2 
6405 N  N   . ALA   B 154 ? 0.1441 0.1185 0.1647 -0.0067 -0.0107 -0.0108 154 ALA   B N   
6406 C  CA  . ALA   B 154 ? 0.1540 0.1357 0.1841 -0.0046 -0.0141 -0.0248 154 ALA   B CA  
6407 C  C   . ALA   B 154 ? 0.1623 0.1344 0.1927 0.0041  -0.0220 -0.0262 154 ALA   B C   
6408 O  O   . ALA   B 154 ? 0.1928 0.1358 0.2023 0.0039  -0.0068 -0.0070 154 ALA   B O   
6409 C  CB  . ALA   B 154 ? 0.1521 0.1529 0.2106 -0.0038 -0.0115 -0.0256 154 ALA   B CB  
6415 N  N   . VAL   B 155 ? 0.1312 0.1283 0.2064 -0.0017 0.0037  -0.0178 155 VAL   B N   
6416 C  CA  . VAL   B 155 ? 0.1265 0.1292 0.2172 -0.0013 -0.0059 -0.0124 155 VAL   B CA  
6417 C  C   . VAL   B 155 ? 0.1333 0.1251 0.2159 -0.0031 -0.0035 -0.0203 155 VAL   B C   
6418 O  O   . VAL   B 155 ? 0.1510 0.1446 0.2535 0.0004  -0.0052 -0.0403 155 VAL   B O   
6419 C  CB  . VAL   B 155 ? 0.1327 0.1433 0.2603 -0.0084 -0.0136 0.0005  155 VAL   B CB  
6420 C  CG1 . VAL   B 155 ? 0.1399 0.1364 0.2445 -0.0162 -0.0055 -0.0108 155 VAL   B CG1 
6421 C  CG2 . VAL   B 155 ? 0.1276 0.1521 0.2927 -0.0116 -0.0154 0.0315  155 VAL   B CG2 
6431 N  N   . PHE   B 156 ? 0.1239 0.1389 0.2341 -0.0003 0.0009  -0.0164 156 PHE   B N   
6432 C  CA  . PHE   B 156 ? 0.1272 0.1430 0.2713 0.0068  0.0006  -0.0183 156 PHE   B CA  
6433 C  C   . PHE   B 156 ? 0.1290 0.1534 0.3038 0.0108  -0.0082 -0.0362 156 PHE   B C   
6434 O  O   . PHE   B 156 ? 0.1512 0.1731 0.3297 0.0214  0.0023  -0.0415 156 PHE   B O   
6435 C  CB  . PHE   B 156 ? 0.1378 0.1416 0.2624 -0.0016 -0.0088 -0.0132 156 PHE   B CB  
6436 C  CG  . PHE   B 156 ? 0.1351 0.1530 0.2749 -0.0020 -0.0077 0.0079  156 PHE   B CG  
6437 C  CD1 . PHE   B 156 ? 0.1358 0.1796 0.3135 0.0001  0.0028  0.0394  156 PHE   B CD1 
6438 C  CD2 . PHE   B 156 ? 0.1402 0.1567 0.2678 0.0040  -0.0107 0.0097  156 PHE   B CD2 
6439 C  CE1 . PHE   B 156 ? 0.1412 0.1931 0.3260 0.0001  -0.0014 0.0365  156 PHE   B CE1 
6440 C  CE2 . PHE   B 156 ? 0.1486 0.1843 0.2920 0.0093  -0.0078 0.0136  156 PHE   B CE2 
6441 C  CZ  . PHE   B 156 ? 0.1373 0.1951 0.3200 0.0106  -0.0157 0.0208  156 PHE   B CZ  
6451 N  N   . ASP   B 157 ? 0.1328 0.1424 0.3198 0.0135  -0.0197 -0.0196 157 ASP   B N   
6452 C  CA  . ASP   B 157 ? 0.1378 0.1513 0.3549 0.0099  -0.0246 -0.0251 157 ASP   B CA  
6453 C  C   . ASP   B 157 ? 0.1422 0.1501 0.3581 0.0056  -0.0169 -0.0458 157 ASP   B C   
6454 O  O   . ASP   B 157 ? 0.1304 0.1517 0.3391 0.0030  -0.0170 -0.0415 157 ASP   B O   
6455 C  CB  . ASP   B 157 ? 0.1609 0.1704 0.3682 0.0028  -0.0492 -0.0126 157 ASP   B CB  
6456 C  CG  . ASP   B 157 ? 0.1947 0.1841 0.3992 -0.0041 -0.0302 -0.0188 157 ASP   B CG  
6457 O  OD1 . ASP   B 157 ? 0.2058 0.1758 0.4248 0.0072  -0.0224 -0.0178 157 ASP   B OD1 
6458 O  OD2 . ASP   B 157 ? 0.2252 0.2018 0.4279 -0.0054 -0.0163 -0.0127 157 ASP   B OD2 
6463 N  N   . LYS   B 158 ? 0.1523 0.1719 0.3771 0.0101  -0.0040 -0.0735 158 LYS   B N   
6464 C  CA  . LYS   B 158 ? 0.1666 0.1859 0.3814 0.0072  0.0008  -0.0883 158 LYS   B CA  
6465 C  C   . LYS   B 158 ? 0.1669 0.1713 0.3773 0.0040  -0.0077 -0.0764 158 LYS   B C   
6466 O  O   . LYS   B 158 ? 0.1695 0.1717 0.3738 -0.0081 -0.0054 -0.0867 158 LYS   B O   
6467 C  CB  . LYS   B 158 ? 0.1926 0.2226 0.3832 0.0077  0.0135  -0.1059 158 LYS   B CB  
6468 C  CG  . LYS   B 158 ? 0.2246 0.2562 0.3898 0.0125  0.0213  -0.1129 158 LYS   B CG  
6469 C  CD  . LYS   B 158 ? 0.2507 0.2998 0.4030 0.0105  0.0205  -0.1028 158 LYS   B CD  
6470 C  CE  . LYS   B 158 ? 0.2666 0.3273 0.4126 0.0139  0.0168  -0.0983 158 LYS   B CE  
6471 N  NZ  . LYS   B 158 ? 0.2638 0.3385 0.4103 0.0102  0.0143  -0.0964 158 LYS   B NZ  
6485 N  N   A ASN   B 159 ? 0.1670 0.1582 0.3941 0.0061  -0.0218 -0.0588 159 ASN   B N   
6486 N  N   B ASN   B 159 ? 0.1677 0.1659 0.3773 0.0034  -0.0201 -0.0580 159 ASN   B N   
6487 C  CA  A ASN   B 159 ? 0.1778 0.1517 0.4104 0.0180  -0.0306 -0.0478 159 ASN   B CA  
6488 C  CA  B ASN   B 159 ? 0.1754 0.1640 0.3784 0.0101  -0.0280 -0.0450 159 ASN   B CA  
6489 C  C   A ASN   B 159 ? 0.1640 0.1388 0.3987 0.0150  -0.0390 -0.0426 159 ASN   B C   
6490 C  C   B ASN   B 159 ? 0.1626 0.1485 0.3806 0.0077  -0.0401 -0.0415 159 ASN   B C   
6491 O  O   A ASN   B 159 ? 0.1623 0.1351 0.4193 0.0047  -0.0423 -0.0297 159 ASN   B O   
6492 O  O   B ASN   B 159 ? 0.1601 0.1485 0.3949 -0.0048 -0.0467 -0.0341 159 ASN   B O   
6493 C  CB  A ASN   B 159 ? 0.2010 0.1650 0.4346 0.0256  -0.0372 -0.0503 159 ASN   B CB  
6494 C  CB  B ASN   B 159 ? 0.1950 0.1804 0.3786 0.0150  -0.0285 -0.0405 159 ASN   B CB  
6495 C  CG  A ASN   B 159 ? 0.2239 0.1871 0.4628 0.0252  -0.0494 -0.0659 159 ASN   B CG  
6496 C  CG  B ASN   B 159 ? 0.2138 0.2014 0.3888 0.0151  -0.0337 -0.0419 159 ASN   B CG  
6497 O  OD1 A ASN   B 159 ? 0.2380 0.1940 0.4694 0.0267  -0.0532 -0.0774 159 ASN   B OD1 
6498 O  OD1 B ASN   B 159 ? 0.2262 0.2115 0.3898 0.0172  -0.0348 -0.0416 159 ASN   B OD1 
6499 N  ND2 A ASN   B 159 ? 0.2262 0.1989 0.4790 0.0293  -0.0530 -0.0603 159 ASN   B ND2 
6500 N  ND2 B ASN   B 159 ? 0.2162 0.2101 0.3991 0.0181  -0.0352 -0.0378 159 ASN   B ND2 
6513 N  N   . LEU   B 160 ? 0.1558 0.1382 0.3806 0.0082  -0.0420 -0.0375 160 LEU   B N   
6514 C  CA  . LEU   B 160 ? 0.1505 0.1421 0.3441 0.0121  -0.0346 -0.0222 160 LEU   B CA  
6515 C  C   . LEU   B 160 ? 0.1435 0.1328 0.3278 0.0056  -0.0250 -0.0285 160 LEU   B C   
6516 O  O   . LEU   B 160 ? 0.1340 0.1414 0.3128 -0.0014 -0.0221 -0.0134 160 LEU   B O   
6517 C  CB  . LEU   B 160 ? 0.1472 0.1525 0.3214 0.0049  -0.0357 -0.0141 160 LEU   B CB  
6518 C  CG  . LEU   B 160 ? 0.1516 0.1679 0.2966 0.0067  -0.0363 -0.0059 160 LEU   B CG  
6519 C  CD1 . LEU   B 160 ? 0.1654 0.1832 0.2930 -0.0008 -0.0234 -0.0061 160 LEU   B CD1 
6520 C  CD2 . LEU   B 160 ? 0.1548 0.1725 0.2927 0.0219  -0.0348 -0.0089 160 LEU   B CD2 
6533 N  N   . TYR   B 161 ? 0.1424 0.1347 0.3398 -0.0034 -0.0025 -0.0397 161 TYR   B N   
6534 C  CA  . TYR   B 161 ? 0.1484 0.1378 0.3185 -0.0142 0.0152  -0.0434 161 TYR   B CA  
6535 C  C   . TYR   B 161 ? 0.1519 0.1398 0.3107 -0.0141 0.0153  -0.0414 161 TYR   B C   
6536 O  O   . TYR   B 161 ? 0.1531 0.1418 0.2989 -0.0190 0.0049  -0.0363 161 TYR   B O   
6537 C  CB  . TYR   B 161 ? 0.1655 0.1477 0.3173 -0.0211 0.0341  -0.0474 161 TYR   B CB  
6538 C  CG  . TYR   B 161 ? 0.1878 0.1537 0.3072 -0.0271 0.0430  -0.0563 161 TYR   B CG  
6539 C  CD1 . TYR   B 161 ? 0.1959 0.1515 0.3013 -0.0383 0.0475  -0.0526 161 TYR   B CD1 
6540 C  CD2 . TYR   B 161 ? 0.2093 0.1621 0.3032 -0.0252 0.0366  -0.0639 161 TYR   B CD2 
6541 C  CE1 . TYR   B 161 ? 0.2177 0.1732 0.2996 -0.0409 0.0379  -0.0530 161 TYR   B CE1 
6542 C  CE2 . TYR   B 161 ? 0.2317 0.1788 0.3085 -0.0326 0.0393  -0.0598 161 TYR   B CE2 
6543 C  CZ  . TYR   B 161 ? 0.2334 0.1837 0.3035 -0.0487 0.0304  -0.0513 161 TYR   B CZ  
6544 O  OH  . TYR   B 161 ? 0.2639 0.2125 0.3221 -0.0505 0.0237  -0.0458 161 TYR   B OH  
6554 N  N   . ASP   B 162 ? 0.1618 0.1379 0.3285 -0.0092 0.0007  -0.0574 162 ASP   B N   
6555 C  CA  . ASP   B 162 ? 0.1703 0.1472 0.3276 -0.0027 -0.0063 -0.0524 162 ASP   B CA  
6556 C  C   . ASP   B 162 ? 0.1623 0.1391 0.3182 -0.0048 -0.0101 -0.0424 162 ASP   B C   
6557 O  O   . ASP   B 162 ? 0.1698 0.1450 0.3239 -0.0131 -0.0229 -0.0298 162 ASP   B O   
6558 C  CB  . ASP   B 162 ? 0.1910 0.1650 0.3443 0.0036  -0.0072 -0.0735 162 ASP   B CB  
6559 C  CG  . ASP   B 162 ? 0.1939 0.1922 0.3656 0.0073  -0.0076 -0.0861 162 ASP   B CG  
6560 O  OD1 . ASP   B 162 ? 0.1946 0.2136 0.3492 -0.0017 0.0144  -0.0782 162 ASP   B OD1 
6561 O  OD2 . ASP   B 162 ? 0.2069 0.2152 0.3969 0.0251  -0.0094 -0.0840 162 ASP   B OD2 
6566 N  N   . LYS   B 163 ? 0.1582 0.1299 0.3133 -0.0083 -0.0171 -0.0306 163 LYS   B N   
6567 C  CA  . LYS   B 163 ? 0.1689 0.1409 0.3170 -0.0166 -0.0125 -0.0092 163 LYS   B CA  
6568 C  C   . LYS   B 163 ? 0.1418 0.1336 0.2961 -0.0155 -0.0171 -0.0005 163 LYS   B C   
6569 O  O   . LYS   B 163 ? 0.1437 0.1434 0.3168 -0.0168 -0.0105 -0.0043 163 LYS   B O   
6570 C  CB  . LYS   B 163 ? 0.2125 0.1786 0.3569 -0.0167 -0.0137 0.0107  163 LYS   B CB  
6571 C  CG  . LYS   B 163 ? 0.2927 0.2582 0.4242 -0.0222 -0.0101 0.0180  163 LYS   B CG  
6572 C  CD  . LYS   B 163 ? 0.3713 0.3413 0.4933 -0.0357 -0.0158 0.0166  163 LYS   B CD  
6573 C  CE  . LYS   B 163 ? 0.4332 0.4124 0.5416 -0.0439 -0.0152 0.0160  163 LYS   B CE  
6574 N  NZ  . LYS   B 163 ? 0.4731 0.4523 0.5736 -0.0472 -0.0153 0.0109  163 LYS   B NZ  
6588 N  N   . LEU   B 164 ? 0.1347 0.1263 0.2756 -0.0142 -0.0151 -0.0050 164 LEU   B N   
6589 C  CA  . LEU   B 164 ? 0.1366 0.1261 0.2623 -0.0132 -0.0198 -0.0031 164 LEU   B CA  
6590 C  C   . LEU   B 164 ? 0.1444 0.1250 0.2626 -0.0183 -0.0236 0.0054  164 LEU   B C   
6591 O  O   . LEU   B 164 ? 0.1470 0.1491 0.2832 -0.0162 -0.0250 0.0012  164 LEU   B O   
6592 C  CB  . LEU   B 164 ? 0.1329 0.1271 0.2501 -0.0109 -0.0151 -0.0005 164 LEU   B CB  
6593 C  CG  . LEU   B 164 ? 0.1434 0.1451 0.2555 -0.0127 -0.0102 0.0066  164 LEU   B CG  
6594 C  CD1 . LEU   B 164 ? 0.1454 0.1461 0.2552 -0.0123 -0.0142 -0.0079 164 LEU   B CD1 
6595 C  CD2 . LEU   B 164 ? 0.1593 0.1791 0.2687 -0.0138 -0.0044 -0.0109 164 LEU   B CD2 
6607 N  N   . VAL   B 165 ? 0.1720 0.1331 0.2841 -0.0211 -0.0319 -0.0119 165 VAL   B N   
6608 C  CA  . VAL   B 165 ? 0.2013 0.1471 0.2898 -0.0316 -0.0509 -0.0059 165 VAL   B CA  
6609 C  C   . VAL   B 165 ? 0.2248 0.1583 0.3219 -0.0370 -0.0716 -0.0055 165 VAL   B C   
6610 O  O   . VAL   B 165 ? 0.2434 0.1741 0.3333 -0.0412 -0.0774 -0.0047 165 VAL   B O   
6611 C  CB  . VAL   B 165 ? 0.2213 0.1607 0.2873 -0.0144 -0.0301 -0.0134 165 VAL   B CB  
6612 C  CG1 . VAL   B 165 ? 0.2372 0.1714 0.3022 -0.0115 -0.0228 -0.0076 165 VAL   B CG1 
6613 C  CG2 . VAL   B 165 ? 0.2163 0.1693 0.2786 -0.0085 -0.0206 -0.0037 165 VAL   B CG2 
6623 N  N   . SER   B 166 ? 0.2371 0.1472 0.3471 -0.0331 -0.0746 -0.0249 166 SER   B N   
6624 C  CA  . SER   B 166 ? 0.2334 0.1461 0.3959 -0.0366 -0.0625 -0.0349 166 SER   B CA  
6625 C  C   . SER   B 166 ? 0.2207 0.1574 0.4098 -0.0389 -0.0720 -0.0082 166 SER   B C   
6626 O  O   . SER   B 166 ? 0.2242 0.1831 0.4368 -0.0506 -0.0819 -0.0334 166 SER   B O   
6627 C  CB  . SER   B 166 ? 0.2337 0.1602 0.4157 -0.0275 -0.0544 -0.0417 166 SER   B CB  
6628 O  OG  . SER   B 166 ? 0.2227 0.1600 0.4341 -0.0208 -0.0543 -0.0209 166 SER   B OG  
6634 N  N   . SER   B 167 ? 0.1998 0.1493 0.3908 -0.0444 -0.0821 0.0380  167 SER   B N   
6635 C  CA  . SER   B 167 ? 0.1955 0.1566 0.3763 -0.0392 -0.0560 0.0351  167 SER   B CA  
6636 C  C   . SER   B 167 ? 0.1870 0.1709 0.3533 -0.0502 -0.0522 0.0508  167 SER   B C   
6637 O  O   . SER   B 167 ? 0.1898 0.1825 0.3518 -0.0596 -0.0459 0.0522  167 SER   B O   
6638 C  CB  . SER   B 167 ? 0.1880 0.1651 0.3748 -0.0306 -0.0231 0.0257  167 SER   B CB  
6639 O  OG  . SER   B 167 ? 0.1774 0.1768 0.3602 -0.0213 -0.0048 0.0235  167 SER   B OG  
6645 N  N   . PHE   B 168 ? 0.1812 0.1671 0.3401 -0.0429 -0.0364 0.0510  168 PHE   B N   
6646 C  CA  . PHE   B 168 ? 0.1861 0.1642 0.3126 -0.0435 -0.0302 0.0318  168 PHE   B CA  
6647 C  C   . PHE   B 168 ? 0.1643 0.1517 0.2694 -0.0284 -0.0100 0.0183  168 PHE   B C   
6648 O  O   . PHE   B 168 ? 0.2009 0.1460 0.2644 -0.0037 -0.0074 0.0052  168 PHE   B O   
6649 C  CB  . PHE   B 168 ? 0.2071 0.1682 0.3134 -0.0492 -0.0479 0.0449  168 PHE   B CB  
6650 C  CG  . PHE   B 168 ? 0.2330 0.1504 0.2962 -0.0480 -0.0474 0.0199  168 PHE   B CG  
6651 C  CD1 . PHE   B 168 ? 0.2626 0.1531 0.2991 -0.0432 -0.0506 0.0134  168 PHE   B CD1 
6652 C  CD2 . PHE   B 168 ? 0.2192 0.1448 0.2890 -0.0448 -0.0449 0.0199  168 PHE   B CD2 
6653 C  CE1 . PHE   B 168 ? 0.2749 0.1635 0.3005 -0.0333 -0.0463 0.0101  168 PHE   B CE1 
6654 C  CE2 . PHE   B 168 ? 0.2482 0.1524 0.2937 -0.0298 -0.0483 0.0093  168 PHE   B CE2 
6655 C  CZ  . PHE   B 168 ? 0.2630 0.1553 0.2976 -0.0206 -0.0532 0.0175  168 PHE   B CZ  
6665 N  N   . LEU   B 169 ? 0.1675 0.1617 0.2718 -0.0083 0.0064  -0.0013 169 LEU   B N   
6666 C  CA  . LEU   B 169 ? 0.1879 0.1910 0.3024 -0.0141 0.0101  -0.0276 169 LEU   B CA  
6667 C  C   . LEU   B 169 ? 0.2168 0.2152 0.3540 0.0016  0.0039  -0.0490 169 LEU   B C   
6668 O  O   . LEU   B 169 ? 0.2372 0.2342 0.4053 -0.0030 0.0002  -0.0725 169 LEU   B O   
6669 C  CB  . LEU   B 169 ? 0.2065 0.2308 0.3092 -0.0192 0.0059  -0.0064 169 LEU   B CB  
6670 C  CG  . LEU   B 169 ? 0.2461 0.2679 0.3435 -0.0097 0.0085  -0.0020 169 LEU   B CG  
6671 C  CD1 . LEU   B 169 ? 0.2568 0.2868 0.3447 -0.0062 0.0056  0.0120  169 LEU   B CD1 
6672 C  CD2 . LEU   B 169 ? 0.2392 0.2738 0.3400 0.0031  0.0267  -0.0194 169 LEU   B CD2 
6673 O  OXT . LEU   B 169 ? 0.2362 0.2300 0.3449 0.0318  0.0134  -0.0491 169 LEU   B OXT 
6685 C  C1  T TFA   C .   ? 0.1431 0.1668 0.1463 -0.0154 0.0087  0.0206  201 TFA   A C1  
6686 C  C2  T TFA   C .   ? 0.1701 0.1873 0.1887 -0.0229 0.0101  0.0102  201 TFA   A C2  
6687 O  O   T TFA   C .   ? 0.1223 0.1499 0.1240 -0.0163 0.0102  0.0272  201 TFA   A O   
6688 F  F1  T TFA   C .   ? 0.1746 0.1886 0.2127 -0.0251 0.0189  0.0078  201 TFA   A F1  
6689 F  F2  T TFA   C .   ? 0.1791 0.1973 0.1840 -0.0254 0.0054  0.0156  201 TFA   A F2  
6690 F  F3  T TFA   C .   ? 0.1841 0.1989 0.2065 -0.0281 0.0210  -0.0024 201 TFA   A F3  
6691 O  OXT T TFA   C .   ? 0.1298 0.1649 0.1453 -0.0069 0.0091  0.0185  201 TFA   A OXT 
6692 N  N2  B A1A94 D .   ? 0.1401 0.1155 0.1919 -0.0016 -0.0085 0.0149  202 A1A94 A N2  
6693 C  C3  B A1A94 D .   ? 0.1692 0.1613 0.1900 0.0011  -0.0110 0.0153  202 A1A94 A C3  
6694 C  C6  B A1A94 D .   ? 0.1743 0.1847 0.2091 -0.0025 -0.0110 0.0109  202 A1A94 A C6  
6695 C  C9  B A1A94 D .   ? 0.1691 0.1844 0.2027 0.0003  -0.0110 0.0069  202 A1A94 A C9  
6696 C  C12 B A1A94 D .   ? 0.1286 0.1118 0.1742 0.0033  -0.0112 0.0234  202 A1A94 A C12 
6697 C  C14 B A1A94 D .   ? 0.1257 0.1221 0.1675 -0.0001 -0.0003 0.0245  202 A1A94 A C14 
6698 C  C1  B A1A94 D .   ? 0.1613 0.1508 0.2089 0.0054  0.0084  0.0042  202 A1A94 A C1  
6699 C  C10 B A1A94 D .   ? 0.1323 0.1146 0.1773 -0.0025 -0.0076 0.0205  202 A1A94 A C10 
6700 C  C11 B A1A94 D .   ? 0.1401 0.1180 0.1919 0.0028  -0.0055 0.0200  202 A1A94 A C11 
6701 C  C13 B A1A94 D .   ? 0.1258 0.1171 0.1744 0.0001  -0.0073 0.0234  202 A1A94 A C13 
6702 C  C15 B A1A94 D .   ? 0.1250 0.1161 0.1668 -0.0017 -0.0097 0.0235  202 A1A94 A C15 
6703 C  C2  B A1A94 D .   ? 0.1544 0.1361 0.1808 -0.0012 -0.0020 0.0221  202 A1A94 A C2  
6704 C  C4  B A1A94 D .   ? 0.1705 0.1753 0.1999 -0.0009 -0.0086 0.0114  202 A1A94 A C4  
6705 C  C5  B A1A94 D .   ? 0.1727 0.1792 0.2065 -0.0055 -0.0125 0.0098  202 A1A94 A C5  
6706 C  C7  B A1A94 D .   ? 0.1758 0.1855 0.2179 0.0040  -0.0170 0.0198  202 A1A94 A C7  
6707 C  C8  B A1A94 D .   ? 0.1750 0.1903 0.2195 -0.0006 -0.0136 0.0060  202 A1A94 A C8  
6708 I  I1  B A1A94 D .   ? 0.1820 0.1874 0.2260 0.0174  -0.0284 0.0403  202 A1A94 A I1  
6709 N  N1  B A1A94 D .   ? 0.1387 0.1106 0.1685 -0.0016 -0.0042 0.0254  202 A1A94 A N1  
6710 N  N3  B A1A94 D .   ? 0.1379 0.1172 0.1840 0.0009  -0.0112 0.0235  202 A1A94 A N3  
6711 N  N4  B A1A94 D .   ? 0.1257 0.1094 0.1594 -0.0004 -0.0099 0.0236  202 A1A94 A N4  
6712 O  O1  B A1A94 D .   ? 0.1674 0.1653 0.2337 -0.0013 0.0237  0.0072  202 A1A94 A O1  
6728 O  O1  C A1A93 E .   ? 0.1382 0.1683 0.2038 -0.0087 0.0004  0.0001  203 A1A93 A O1  
6729 C  C1  C A1A93 E .   ? 0.1343 0.1622 0.1894 -0.0027 -0.0067 -0.0013 203 A1A93 A C1  
6730 C  C2  C A1A93 E .   ? 0.1298 0.1562 0.1744 -0.0005 -0.0123 0.0059  203 A1A93 A C2  
6731 C  C3  C A1A93 E .   ? 0.1371 0.1593 0.1737 0.0019  -0.0152 0.0115  203 A1A93 A C3  
6732 C  C4  C A1A93 E .   ? 0.1479 0.1613 0.1682 0.0044  -0.0179 0.0208  203 A1A93 A C4  
6733 C  C5  C A1A93 E .   ? 0.1541 0.1645 0.1690 0.0034  -0.0151 0.0200  203 A1A93 A C5  
6734 C  C6  C A1A93 E .   ? 0.1603 0.1639 0.1635 0.0060  -0.0154 0.0277  203 A1A93 A C6  
6735 C  C7  C A1A93 E .   ? 0.1657 0.1663 0.1625 0.0113  -0.0212 0.0310  203 A1A93 A C7  
6736 C  C8  C A1A93 E .   ? 0.1629 0.1657 0.1614 0.0113  -0.0233 0.0329  203 A1A93 A C8  
6737 C  C10 C A1A93 E .   ? 0.1258 0.1493 0.1602 -0.0018 -0.0090 0.0134  203 A1A93 A C10 
6738 C  C11 C A1A93 E .   ? 0.1284 0.1477 0.1593 -0.0013 -0.0050 0.0145  203 A1A93 A C11 
6739 C  C12 C A1A93 E .   ? 0.1259 0.1446 0.1513 -0.0013 -0.0070 0.0165  203 A1A93 A C12 
6740 C  C13 C A1A93 E .   ? 0.1258 0.1484 0.1554 -0.0018 -0.0070 0.0165  203 A1A93 A C13 
6741 C  C14 C A1A93 E .   ? 0.1266 0.1484 0.1528 -0.0027 -0.0031 0.0205  203 A1A93 A C14 
6742 C  C15 C A1A93 E .   ? 0.1259 0.1455 0.1534 -0.0038 -0.0063 0.0193  203 A1A93 A C15 
6743 C  C9  C A1A93 E .   ? 0.1571 0.1644 0.1619 0.0088  -0.0234 0.0282  203 A1A93 A C9  
6744 I  I1  C A1A93 E .   ? 0.1755 0.1729 0.1635 0.0166  -0.0241 0.0243  203 A1A93 A I1  
6745 N  N1  C A1A93 E .   ? 0.1248 0.1487 0.1640 -0.0014 -0.0151 0.0099  203 A1A93 A N1  
6746 N  N2  C A1A93 E .   ? 0.1275 0.1482 0.1618 -0.0031 -0.0071 0.0132  203 A1A93 A N2  
6747 N  N3  C A1A93 E .   ? 0.1282 0.1464 0.1540 -0.0026 -0.0067 0.0162  203 A1A93 A N3  
6748 N  N4  C A1A93 E .   ? 0.1251 0.1423 0.1462 -0.0031 -0.0070 0.0175  203 A1A93 A N4  
6764 CL CL  B CL    F .   ? 0.1620 0.1682 0.2802 -0.0147 -0.0150 -0.0111 204 CL    A CL  
6765 O  O   . HOH   G .   ? 0.2209 0.2189 0.3198 -0.0054 0.0833  0.0616  301 HOH   A O   
6766 O  O   . HOH   G .   ? 0.3977 0.8888 0.4495 -0.1159 0.0345  0.1141  302 HOH   A O   
6767 O  O   . HOH   G .   ? 0.2688 0.2373 0.4394 -0.0515 -0.0581 0.0614  303 HOH   A O   
6768 O  O   . HOH   G .   ? 0.5716 0.4791 0.3644 0.2003  -0.1292 0.0940  304 HOH   A O   
6769 O  O   . HOH   G .   ? 0.2686 0.6397 0.4260 -0.0787 -0.0890 0.1339  305 HOH   A O   
6770 O  O   . HOH   G .   ? 0.7753 0.6227 0.4224 -0.1395 0.0003  0.2597  306 HOH   A O   
6771 O  O   . HOH   G .   ? 0.5625 0.6277 0.5531 -0.1330 -0.1325 -0.0687 307 HOH   A O   
6772 O  O   A HOH   G .   ? 0.1037 0.3605 0.2113 -0.0057 0.0142  0.0883  308 HOH   A O   
6773 O  O   . HOH   G .   ? 0.7442 0.5118 0.3476 -0.1144 -0.0593 0.0757  309 HOH   A O   
6774 O  O   . HOH   G .   ? 0.5869 0.4683 0.5068 -0.0897 0.1856  0.1842  310 HOH   A O   
6775 O  O   A HOH   G .   ? 0.2364 0.3393 0.4468 -0.0232 0.0866  0.1780  311 HOH   A O   
6776 O  O   . HOH   G .   ? 0.6348 0.4378 0.3190 -0.0216 -0.0503 0.0539  312 HOH   A O   
6777 O  O   . HOH   G .   ? 0.3174 0.3110 0.1650 -0.0479 0.0558  0.0374  313 HOH   A O   
6778 O  O   . HOH   G .   ? 0.2060 0.1844 0.2813 0.0087  -0.0593 -0.0203 314 HOH   A O   
6779 O  O   . HOH   G .   ? 0.3283 0.3160 0.2722 -0.1013 0.0146  0.0803  315 HOH   A O   
6780 O  O   . HOH   G .   ? 0.4961 0.3332 0.5002 -0.0204 0.1956  -0.0269 316 HOH   A O   
6781 O  O   . HOH   G .   ? 0.2035 0.1871 0.3479 -0.0463 -0.0012 -0.0119 317 HOH   A O   
6782 O  O   . HOH   G .   ? 0.6239 0.3857 0.5582 -0.0791 0.1492  0.1500  318 HOH   A O   
6783 O  O   . HOH   G .   ? 0.5618 0.6299 0.3778 0.2224  -0.0539 -0.0466 319 HOH   A O   
6784 O  O   . HOH   G .   ? 0.3275 0.6678 0.5385 -0.0524 -0.0914 0.1226  320 HOH   A O   
6785 O  O   . HOH   G .   ? 0.2417 0.1926 0.2300 -0.0217 0.0148  0.0002  321 HOH   A O   
6786 O  O   A HOH   G .   ? 0.1479 0.2116 0.1583 0.0376  0.0162  0.0135  322 HOH   A O   
6787 O  O   . HOH   G .   ? 0.1713 0.2967 0.2739 0.0303  -0.0173 -0.0216 323 HOH   A O   
6788 O  O   . HOH   G .   ? 0.4275 0.4917 0.7233 0.1508  0.1330  -0.0301 324 HOH   A O   
6789 O  O   . HOH   G .   ? 0.3937 0.3400 0.3915 -0.1019 0.1878  -0.0099 325 HOH   A O   
6790 O  O   B HOH   G .   ? 0.2188 0.3501 0.3477 0.0334  0.0218  0.0278  326 HOH   A O   
6791 O  O   . HOH   G .   ? 0.3550 0.2904 0.2656 -0.0342 -0.0061 0.0184  327 HOH   A O   
6792 O  O   . HOH   G .   ? 0.1680 0.1562 0.2038 0.0189  -0.0196 0.0283  328 HOH   A O   
6793 O  O   . HOH   G .   ? 0.2809 0.4401 0.3361 -0.1374 -0.0588 -0.0082 329 HOH   A O   
6794 O  O   . HOH   G .   ? 0.3071 0.5571 0.7704 0.0551  0.1173  0.0990  330 HOH   A O   
6795 O  O   B HOH   G .   ? 0.2455 0.1682 0.2441 0.0183  -0.0457 0.0486  331 HOH   A O   
6796 O  O   . HOH   G .   ? 0.1518 0.1456 0.2108 -0.0204 0.0066  0.0119  332 HOH   A O   
6797 O  O   A HOH   G .   ? 0.3786 0.1436 0.1919 0.0217  -0.0118 0.0240  333 HOH   A O   
6798 O  O   . HOH   G .   ? 0.3301 0.2774 0.5535 0.0655  0.1288  0.0379  334 HOH   A O   
6799 O  O   . HOH   G .   ? 0.5750 0.5788 0.5256 0.0191  0.2683  -0.1259 335 HOH   A O   
6800 O  O   . HOH   G .   ? 0.5177 0.4635 0.3105 -0.1327 0.1599  0.0522  336 HOH   A O   
6801 O  O   . HOH   G .   ? 0.1922 0.3658 0.3930 -0.0295 0.0182  -0.1022 337 HOH   A O   
6802 O  O   . HOH   G .   ? 0.4316 0.4374 0.4180 -0.1705 -0.0861 0.2208  338 HOH   A O   
6803 O  O   . HOH   G .   ? 0.4790 0.2830 0.2888 -0.1289 0.0402  0.0414  339 HOH   A O   
6804 O  O   . HOH   G .   ? 0.2395 0.2131 0.2606 0.0516  0.0338  0.0438  340 HOH   A O   
6805 O  O   . HOH   G .   ? 0.5099 0.1719 0.4900 0.0178  -0.1567 0.0331  341 HOH   A O   
6806 O  O   . HOH   G .   ? 0.4857 0.5697 0.4297 -0.0010 -0.0664 -0.0757 342 HOH   A O   
6807 O  O   . HOH   G .   ? 0.2952 0.2527 0.4512 -0.0389 -0.1334 0.1103  343 HOH   A O   
6808 O  O   B HOH   G .   ? 0.1754 0.2456 0.3767 -0.0770 0.0467  -0.0059 344 HOH   A O   
6809 O  O   . HOH   G .   ? 0.1571 0.1946 0.2588 0.0196  -0.0419 -0.0660 345 HOH   A O   
6810 O  O   . HOH   G .   ? 0.2140 0.1631 0.1379 -0.0107 0.0183  0.0143  346 HOH   A O   
6811 O  O   . HOH   G .   ? 0.2577 0.2808 0.3881 -0.0210 0.1039  -0.0294 347 HOH   A O   
6812 O  O   . HOH   G .   ? 0.3058 0.4175 0.2237 -0.0138 0.0567  0.0366  348 HOH   A O   
6813 O  O   . HOH   G .   ? 0.2081 0.4412 0.3973 -0.0356 -0.0630 0.1929  349 HOH   A O   
6814 O  O   . HOH   G .   ? 0.2302 0.3956 0.3941 0.0889  -0.0745 -0.0209 350 HOH   A O   
6815 O  O   . HOH   G .   ? 0.1464 0.2145 0.1973 0.0013  -0.0031 0.0519  351 HOH   A O   
6816 O  O   . HOH   G .   ? 0.4963 0.1935 0.4822 0.0538  0.0272  0.0222  352 HOH   A O   
6817 O  O   B HOH   G .   ? 0.1661 0.1898 0.2205 0.0230  -0.0174 -0.0373 353 HOH   A O   
6818 O  O   . HOH   G .   ? 0.3015 0.3739 0.2010 -0.0808 -0.0193 -0.0759 354 HOH   A O   
6819 O  O   . HOH   G .   ? 0.3411 0.3897 0.5845 0.0586  0.0914  -0.1529 355 HOH   A O   
6820 O  O   . HOH   G .   ? 0.3361 0.4922 0.3415 0.2019  0.0697  0.0601  356 HOH   A O   
6821 O  O   . HOH   G .   ? 0.1358 0.1899 0.2439 0.0087  -0.0129 0.0055  357 HOH   A O   
6822 O  O   . HOH   G .   ? 0.1986 0.1927 0.3772 0.0173  0.1032  -0.0093 358 HOH   A O   
6823 O  O   . HOH   G .   ? 0.1993 0.1602 0.2162 0.0163  -0.0345 0.0008  359 HOH   A O   
6824 O  O   A HOH   G .   ? 0.1817 0.3066 0.1890 0.0331  0.0253  0.0403  360 HOH   A O   
6825 O  O   . HOH   G .   ? 0.4637 0.2402 0.4158 -0.1402 0.1851  -0.0650 361 HOH   A O   
6826 O  O   . HOH   G .   ? 0.1793 0.2148 0.3475 -0.0045 0.0855  0.0675  362 HOH   A O   
6827 O  O   . HOH   G .   ? 0.3942 0.2943 0.3565 -0.1095 -0.0548 -0.0055 363 HOH   A O   
6828 O  O   . HOH   G .   ? 0.5982 0.3712 0.2749 0.0780  0.0319  0.1181  364 HOH   A O   
6829 O  O   . HOH   G .   ? 0.2803 0.4431 0.3077 -0.0727 0.0653  0.0107  365 HOH   A O   
6830 O  O   . HOH   G .   ? 0.3255 0.3655 0.4415 -0.0861 -0.1183 -0.0936 366 HOH   A O   
6831 O  O   . HOH   G .   ? 0.7498 0.4648 0.6440 -0.0449 -0.1335 0.1139  367 HOH   A O   
6832 O  O   . HOH   G .   ? 0.1313 0.1249 0.1305 -0.0018 0.0067  0.0077  368 HOH   A O   
6833 O  O   . HOH   G .   ? 0.1815 0.1861 0.2374 -0.0267 0.0139  0.0273  369 HOH   A O   
6834 O  O   . HOH   G .   ? 0.2607 0.4472 0.3118 0.0556  0.0788  0.1966  370 HOH   A O   
6835 O  O   . HOH   G .   ? 0.5955 0.5479 0.7689 -0.0965 0.0001  0.2197  371 HOH   A O   
6836 O  O   . HOH   G .   ? 0.1407 0.1453 0.1448 -0.0030 -0.0135 -0.0031 372 HOH   A O   
6837 O  O   . HOH   G .   ? 0.1493 0.1247 0.2132 -0.0054 0.0147  -0.0067 373 HOH   A O   
6838 O  O   . HOH   G .   ? 0.3189 0.2693 0.3622 0.0063  -0.0937 -0.0458 374 HOH   A O   
6839 O  O   . HOH   G .   ? 0.3785 0.2025 0.4598 -0.1082 0.0588  0.0246  375 HOH   A O   
6840 O  O   . HOH   G .   ? 0.3364 0.7880 0.4992 -0.0743 -0.1638 0.1011  376 HOH   A O   
6841 O  O   . HOH   G .   ? 0.2963 0.2227 0.4844 -0.0559 -0.0185 0.0014  377 HOH   A O   
6842 O  O   . HOH   G .   ? 0.3971 0.6047 0.4181 -0.0368 0.0101  0.1662  378 HOH   A O   
6843 O  O   . HOH   G .   ? 0.3937 0.5915 0.6487 0.0444  -0.0429 0.2404  379 HOH   A O   
6844 O  O   . HOH   G .   ? 0.3935 0.2073 0.2033 0.1168  0.0443  0.0129  380 HOH   A O   
6845 O  O   T HOH   G .   ? 0.1142 0.1327 0.2229 -0.0172 0.0187  0.0410  381 HOH   A O   
6846 O  O   . HOH   G .   ? 0.1921 0.2382 0.3438 0.0130  0.0855  -0.0509 382 HOH   A O   
6847 O  O   . HOH   G .   ? 0.1966 0.2110 0.2085 -0.0236 -0.0470 0.0376  383 HOH   A O   
6848 O  O   . HOH   G .   ? 0.1766 0.2689 0.2696 0.0505  0.0493  0.1013  384 HOH   A O   
6849 O  O   . HOH   G .   ? 0.1832 0.1766 0.1772 0.0027  0.0039  0.0262  385 HOH   A O   
6850 O  O   A HOH   G .   ? 0.2691 0.3423 0.3668 0.0235  0.0180  0.0718  386 HOH   A O   
6851 O  O   . HOH   G .   ? 0.1618 0.1585 0.2170 -0.0249 0.0141  0.0247  387 HOH   A O   
6852 O  O   . HOH   G .   ? 0.1986 0.4111 0.4213 -0.0461 -0.0092 0.1132  388 HOH   A O   
6853 O  O   . HOH   G .   ? 0.1745 0.2168 0.1875 -0.0099 0.0047  0.0694  389 HOH   A O   
6854 O  O   . HOH   G .   ? 0.3085 0.2545 0.2092 0.0310  0.0739  0.0150  390 HOH   A O   
6855 O  O   . HOH   G .   ? 0.2523 0.1876 0.1693 -0.0466 0.0229  0.0236  391 HOH   A O   
6856 O  O   . HOH   G .   ? 0.3389 0.7257 0.3473 0.1756  0.0592  -0.1124 392 HOH   A O   
6857 O  O   . HOH   G .   ? 0.1543 0.1741 0.1926 0.0040  -0.0250 0.0051  393 HOH   A O   
6858 O  O   A HOH   G .   ? 0.1616 0.1668 0.2366 0.0024  -0.0449 0.0232  394 HOH   A O   
6859 O  O   . HOH   G .   ? 0.3183 0.2318 0.3062 -0.0136 -0.0463 0.0789  395 HOH   A O   
6860 O  O   . HOH   G .   ? 0.1387 0.1614 0.1737 0.0150  -0.0275 -0.0220 396 HOH   A O   
6861 O  O   . HOH   G .   ? 0.2342 0.1623 0.2440 0.0019  0.0205  0.0194  397 HOH   A O   
6862 O  O   A HOH   G .   ? 0.1898 0.1837 0.2943 -0.0159 0.0353  -0.0123 398 HOH   A O   
6863 O  O   . HOH   G .   ? 0.2599 0.3836 0.3680 -0.0589 0.1206  -0.0980 399 HOH   A O   
6864 O  O   . HOH   G .   ? 0.1823 0.2007 0.2731 -0.0151 -0.0124 0.0833  400 HOH   A O   
6865 O  O   B HOH   G .   ? 0.3201 0.3193 0.2246 -0.0416 -0.0401 -0.0110 401 HOH   A O   
6866 O  O   . HOH   G .   ? 0.1815 0.1858 0.3827 0.0384  0.0999  0.1087  402 HOH   A O   
6867 O  O   . HOH   G .   ? 0.1267 0.1388 0.1771 -0.0016 -0.0144 0.0083  403 HOH   A O   
6868 O  O   . HOH   G .   ? 0.4198 0.4958 0.2180 -0.0732 -0.1184 0.0091  404 HOH   A O   
6869 O  O   . HOH   G .   ? 0.5613 0.3051 0.4571 0.0868  -0.0676 0.0356  405 HOH   A O   
6870 O  O   . HOH   G .   ? 0.3036 0.2394 0.2146 -0.0668 -0.0856 0.0311  406 HOH   A O   
6871 O  O   . HOH   G .   ? 0.6822 0.4183 0.5444 -0.0157 -0.1173 -0.0529 407 HOH   A O   
6872 O  O   . HOH   G .   ? 0.2520 0.2009 0.2305 -0.0603 -0.0135 0.0563  408 HOH   A O   
6873 O  O   . HOH   G .   ? 0.2047 0.1705 0.2761 0.0067  -0.0294 0.0106  409 HOH   A O   
6874 O  O   . HOH   G .   ? 0.4554 0.4416 0.1916 0.0100  0.0845  0.0892  410 HOH   A O   
6875 O  O   . HOH   G .   ? 0.3147 0.3176 0.6083 -0.0390 0.1355  -0.0558 411 HOH   A O   
6876 O  O   . HOH   G .   ? 0.3311 0.3351 0.4060 -0.1420 0.1437  -0.0371 412 HOH   A O   
6877 O  O   . HOH   G .   ? 0.2930 0.3408 0.7531 -0.0230 0.1271  -0.0504 413 HOH   A O   
6878 O  O   . HOH   G .   ? 0.1746 0.1369 0.1522 -0.0234 0.0124  0.0008  414 HOH   A O   
6879 O  O   . HOH   G .   ? 0.2154 0.1774 0.3349 0.0273  -0.0674 0.0279  415 HOH   A O   
6880 O  O   . HOH   G .   ? 0.1487 0.1609 0.2839 0.0004  0.0039  0.0218  416 HOH   A O   
6881 O  O   . HOH   G .   ? 0.1840 0.2576 0.3637 -0.0015 -0.0189 0.0345  417 HOH   A O   
6882 O  O   . HOH   G .   ? 0.2074 0.2686 0.2484 -0.0051 -0.0622 0.0397  418 HOH   A O   
6883 O  O   . HOH   G .   ? 0.4775 0.4697 0.3370 0.1401  -0.1123 -0.1240 419 HOH   A O   
6884 O  O   . HOH   G .   ? 0.4699 0.7039 0.5720 0.2514  0.1319  0.0883  420 HOH   A O   
6885 O  O   . HOH   G .   ? 0.2987 0.5721 0.1576 -0.0392 0.0431  0.0113  421 HOH   A O   
6886 O  O   . HOH   G .   ? 0.2174 0.3947 0.2382 0.1464  -0.0044 0.0122  422 HOH   A O   
6887 O  O   . HOH   G .   ? 0.3344 0.1299 0.1898 0.0006  -0.0464 0.0114  423 HOH   A O   
6888 O  O   . HOH   G .   ? 0.1637 0.2166 0.2813 -0.0129 -0.0063 0.0604  424 HOH   A O   
6889 O  O   A HOH   G .   ? 0.2033 0.2043 0.2516 0.0193  -0.0150 0.0695  425 HOH   A O   
6890 O  O   . HOH   G .   ? 0.6450 0.4407 0.4609 0.1940  -0.0627 0.1614  426 HOH   A O   
6891 O  O   . HOH   G .   ? 0.4335 0.6700 0.3108 -0.0878 -0.0210 0.1476  427 HOH   A O   
6892 O  O   . HOH   G .   ? 0.5316 0.6820 0.5537 0.1103  0.0699  0.0522  428 HOH   A O   
6893 O  O   . HOH   G .   ? 0.6345 0.6681 0.5725 -0.1272 0.0763  0.0761  429 HOH   A O   
6894 O  O   . HOH   G .   ? 0.4314 0.2151 0.5064 -0.0727 -0.2304 0.1018  430 HOH   A O   
6895 O  O   . HOH   G .   ? 0.5847 0.4203 0.4453 -0.0457 -0.1587 0.0046  431 HOH   A O   
6896 O  O   A HOH   G .   ? 0.1880 0.1982 0.3192 0.0113  -0.0483 -0.0723 432 HOH   A O   
6897 O  O   . HOH   G .   ? 0.6190 0.5634 0.6504 -0.1414 -0.1222 -0.0375 433 HOH   A O   
6898 O  O   A HOH   G .   ? 0.2212 0.1524 0.2125 -0.0114 -0.0663 0.0215  434 HOH   A O   
6899 O  O   . HOH   G .   ? 0.6954 0.7099 0.4273 0.0939  0.2794  -0.0882 435 HOH   A O   
6900 O  O   . HOH   G .   ? 0.2751 0.2995 0.4541 0.0347  0.0733  -0.0863 436 HOH   A O   
6901 O  O   A HOH   G .   ? 0.6479 0.5265 0.4540 -0.1098 0.1045  0.1917  437 HOH   A O   
6902 O  O   . HOH   G .   ? 0.9173 0.9072 0.7219 -0.1159 -0.0211 0.0446  438 HOH   A O   
6903 O  O   . HOH   G .   ? 0.7539 0.5917 0.6528 0.0588  -0.0840 0.0569  439 HOH   A O   
6904 O  O   . HOH   G .   ? 0.7535 0.7604 0.6528 -0.1338 0.0479  -0.1262 440 HOH   A O   
6905 O  O   . HOH   G .   ? 0.3467 0.2514 0.1676 -0.0639 0.0402  0.0443  441 HOH   A O   
6906 O  O   . HOH   G .   ? 0.2502 0.1565 0.2646 0.0087  0.0087  0.0107  442 HOH   A O   
6907 O  O   B HOH   G .   ? 0.3445 0.1625 0.2809 -0.0167 0.1063  0.0261  443 HOH   A O   
6908 O  O   . HOH   G .   ? 0.1872 0.2227 0.4458 -0.0262 -0.0794 0.0569  444 HOH   A O   
6909 O  O   . HOH   G .   ? 0.1623 0.1632 0.1463 -0.0005 -0.0198 -0.0053 445 HOH   A O   
6910 O  O   . HOH   G .   ? 0.4406 0.4665 0.5088 -0.1117 -0.1028 -0.1253 446 HOH   A O   
6911 O  O   . HOH   G .   ? 0.3808 0.3707 0.2883 0.2229  -0.0465 -0.0331 447 HOH   A O   
6912 O  O   . HOH   G .   ? 0.5724 0.6262 0.6472 0.0713  0.0121  -0.1261 448 HOH   A O   
6913 O  O   . HOH   G .   ? 0.6291 0.8077 0.4094 0.2342  -0.1001 0.1442  449 HOH   A O   
6914 O  O   . HOH   G .   ? 0.2291 0.2018 0.2456 0.0051  0.0221  0.0315  450 HOH   A O   
6915 O  O   A HOH   G .   ? 0.4864 0.2816 0.2468 -0.0213 0.0538  0.1115  451 HOH   A O   
6916 O  O   . HOH   G .   ? 0.2110 0.2468 0.2360 0.0055  -0.0157 -0.0474 452 HOH   A O   
6917 O  O   . HOH   G .   ? 0.6238 0.5658 0.7828 0.0790  -0.1251 0.1886  453 HOH   A O   
6918 O  O   A HOH   G .   ? 0.4863 0.4504 0.5095 0.0450  0.1263  0.2455  454 HOH   A O   
6919 O  O   . HOH   G .   ? 0.4307 0.4627 0.4458 0.0551  -0.0477 0.1464  455 HOH   A O   
6920 O  O   . HOH   G .   ? 0.4616 0.3210 0.3451 0.0945  0.1237  0.0311  456 HOH   A O   
6921 O  O   . HOH   G .   ? 0.6352 0.5887 0.5029 -0.0536 0.1167  0.1348  457 HOH   A O   
6922 O  O   . HOH   G .   ? 0.3027 0.3375 0.3817 0.1132  -0.0461 0.0629  458 HOH   A O   
6923 O  O   . HOH   G .   ? 0.4421 0.3306 0.4218 0.0570  0.1083  0.0446  459 HOH   A O   
6924 O  O   . HOH   G .   ? 0.2791 0.3020 0.3519 -0.0721 0.0277  -0.0816 460 HOH   A O   
6925 O  O   . HOH   G .   ? 0.6711 0.7770 0.4618 0.1020  -0.1197 -0.0028 461 HOH   A O   
6926 O  O   B HOH   G .   ? 0.3317 0.1858 0.3538 -0.0348 -0.0247 0.0862  462 HOH   A O   
6927 O  O   . HOH   G .   ? 0.3073 0.4968 0.5280 -0.1544 0.0697  -0.1614 463 HOH   A O   
6928 O  O   . HOH   G .   ? 0.3699 0.4266 0.5411 0.0759  -0.0127 0.1460  464 HOH   A O   
6929 O  O   . HOH   G .   ? 0.6550 0.3512 0.7498 0.0641  0.0366  0.2553  465 HOH   A O   
6930 O  O   . HOH   G .   ? 0.2783 0.1613 0.2489 0.0323  -0.0933 -0.0325 466 HOH   A O   
6931 O  O   . HOH   G .   ? 0.2451 0.2453 0.3221 -0.0708 0.0425  -0.0210 467 HOH   A O   
6932 O  O   . HOH   G .   ? 0.6790 0.7043 0.6640 0.1644  0.1746  0.2230  468 HOH   A O   
6933 O  O   . HOH   G .   ? 0.2653 0.4140 0.5142 0.0591  0.0184  -0.1956 469 HOH   A O   
6934 O  O   . HOH   G .   ? 0.3501 0.4175 0.4231 -0.0999 -0.0236 0.0228  470 HOH   A O   
6935 O  O   A HOH   G .   ? 0.2563 0.2113 0.4186 0.0781  -0.1425 -0.0418 471 HOH   A O   
6936 O  O   . HOH   G .   ? 0.4904 0.6292 0.3990 0.0791  -0.1031 -0.0639 472 HOH   A O   
6937 O  O   . HOH   G .   ? 0.3749 0.6134 0.3592 -0.0639 -0.0520 0.2033  473 HOH   A O   
6938 O  O   . HOH   G .   ? 0.4383 0.5240 0.3723 0.0453  -0.0778 -0.0780 474 HOH   A O   
6939 O  O   . HOH   G .   ? 0.5440 0.4651 0.4561 0.0098  0.1231  0.0187  475 HOH   A O   
6940 O  O   . HOH   G .   ? 0.3409 0.2201 0.3923 0.0073  0.1131  0.0059  476 HOH   A O   
6941 O  O   B HOH   G .   ? 0.4817 0.2886 0.4193 -0.0812 -0.1066 0.1595  477 HOH   A O   
6942 O  O   . HOH   G .   ? 0.4388 0.4946 0.3372 -0.0364 -0.0375 0.0203  478 HOH   A O   
6943 O  O   . HOH   G .   ? 0.4476 0.5006 0.2687 -0.0381 -0.0211 -0.0223 479 HOH   A O   
6944 O  O   . HOH   G .   ? 0.5302 0.4740 0.6075 -0.1639 -0.1272 0.0108  480 HOH   A O   
6945 O  O   . HOH   G .   ? 0.4966 0.5159 0.5074 -0.1770 -0.0978 -0.0351 481 HOH   A O   
6946 O  O   . HOH   G .   ? 0.2443 0.2213 0.2445 0.0190  0.0028  0.0091  482 HOH   A O   
6947 O  O   . HOH   G .   ? 0.7710 0.3492 0.3157 -0.0105 -0.1352 0.0252  483 HOH   A O   
6948 O  O   . HOH   G .   ? 0.7220 0.6037 0.7381 -0.0527 0.1220  -0.1124 484 HOH   A O   
6949 O  O   . HOH   G .   ? 0.5921 0.3966 0.4375 -0.0225 -0.0299 -0.0985 485 HOH   A O   
6950 O  O   . HOH   G .   ? 0.4358 0.2715 0.3510 -0.0310 -0.1360 0.0538  486 HOH   A O   
6951 O  O   . HOH   G .   ? 0.6253 0.3655 0.4567 -0.0581 0.1205  -0.0475 487 HOH   A O   
6952 O  O   B HOH   G .   ? 0.5113 0.4972 0.4107 0.0190  -0.1409 -0.0121 488 HOH   A O   
6953 O  O   . HOH   G .   ? 0.3083 0.4557 0.3458 -0.0234 -0.0089 -0.0941 489 HOH   A O   
6954 O  O   . HOH   G .   ? 0.5542 0.6405 0.4259 -0.1243 0.0837  0.0770  490 HOH   A O   
6955 O  O   . HOH   G .   ? 0.2709 0.5292 0.3588 0.1145  0.0968  0.2388  491 HOH   A O   
6956 O  O   . HOH   G .   ? 0.2783 0.3759 0.4224 -0.0084 0.1057  0.0745  492 HOH   A O   
6957 O  O   . HOH   G .   ? 0.6457 0.4624 0.5550 -0.0667 -0.1233 -0.0762 493 HOH   A O   
6958 O  O   . HOH   G .   ? 0.3909 0.3656 0.4302 -0.1049 0.0283  0.0822  494 HOH   A O   
6959 O  O   . HOH   G .   ? 0.4742 0.3393 0.2379 -0.0648 0.1464  -0.0367 495 HOH   A O   
6960 O  O   . HOH   G .   ? 0.5228 0.5708 0.7404 0.1037  0.1862  -0.1054 496 HOH   A O   
6961 O  O   . HOH   G .   ? 0.4980 0.6304 0.5045 -0.0134 -0.1205 0.0153  497 HOH   A O   
6962 O  O   . HOH   G .   ? 0.2547 0.2288 0.6804 -0.0012 -0.1219 -0.0029 498 HOH   A O   
6963 O  O   . HOH   G .   ? 0.4841 0.3465 0.4420 -0.0178 0.2292  0.0298  499 HOH   A O   
6964 O  O   . HOH   G .   ? 0.2776 0.2059 0.5572 0.0173  0.0598  0.1019  500 HOH   A O   
6965 O  O   . HOH   G .   ? 0.6525 0.2696 0.4122 -0.0261 -0.0024 0.0629  501 HOH   A O   
6966 O  O   . HOH   G .   ? 0.2324 0.3138 0.4566 -0.0004 0.0929  -0.0590 502 HOH   A O   
6967 O  O   . HOH   G .   ? 0.4767 0.2594 0.3633 -0.1392 0.0010  0.0307  503 HOH   A O   
6968 O  O   . HOH   G .   ? 0.2637 0.3587 0.3071 0.0826  -0.0614 0.0513  504 HOH   A O   
6969 O  O   . HOH   G .   ? 0.3738 0.8192 0.5114 -0.0832 -0.0293 0.2313  505 HOH   A O   
6970 O  O   B HOH   G .   ? 0.2199 0.2760 0.2584 0.0059  0.0380  0.0003  506 HOH   A O   
6971 O  O   . HOH   G .   ? 0.2856 0.4459 0.5013 0.0738  -0.0830 -0.0325 507 HOH   A O   
6972 O  O   . HOH   G .   ? 0.5427 0.7312 0.5031 0.1192  -0.0469 0.1322  508 HOH   A O   
6973 O  O   . HOH   G .   ? 0.6536 0.4890 0.5408 -0.0497 -0.0216 0.0405  509 HOH   A O   
6974 O  O   B HOH   G .   ? 0.3707 0.2004 0.3992 -0.0587 0.1285  0.0477  510 HOH   A O   
6975 O  O   A HOH   G .   ? 0.5607 0.4723 0.3771 0.1961  -0.1082 0.0763  511 HOH   A O   
6976 O  O   . HOH   G .   ? 0.2729 0.2101 0.4362 0.0077  0.0231  0.0362  512 HOH   A O   
6977 O  O   . HOH   G .   ? 0.5112 0.6787 0.4020 0.2876  -0.0012 0.0940  513 HOH   A O   
6978 O  O   . HOH   G .   ? 0.5529 0.5893 0.4596 -0.0812 -0.0751 -0.1257 514 HOH   A O   
6979 O  O   T HOH   G .   ? 0.1197 0.1531 0.2462 -0.0255 -0.0284 0.0951  515 HOH   A O   
6980 O  O   A HOH   G .   ? 0.4235 0.6895 0.3650 0.1531  -0.0237 -0.0543 516 HOH   A O   
6981 O  O   B HOH   G .   ? 0.2823 0.4404 0.3836 0.1117  -0.0007 0.0813  517 HOH   A O   
6982 O  O   . HOH   G .   ? 0.2547 0.7399 0.4069 0.0163  0.0214  -0.0408 518 HOH   A O   
6983 O  O   B HOH   G .   ? 0.4912 0.1842 0.2897 0.0155  -0.0771 0.0376  519 HOH   A O   
6984 O  O   . HOH   G .   ? 0.5000 0.7481 0.5523 -0.1035 -0.0895 0.0329  520 HOH   A O   
6985 O  O   . HOH   G .   ? 0.5000 0.4457 0.4562 0.1207  0.0407  0.1317  521 HOH   A O   
6986 O  O   . HOH   G .   ? 0.2910 0.4693 0.5742 -0.0025 -0.0941 0.2697  522 HOH   A O   
6987 O  O   . HOH   H .   ? 0.2336 0.2006 0.2837 0.0219  0.0760  0.0338  201 HOH   B O   
6988 O  O   . HOH   H .   ? 0.3327 0.4471 0.5110 -0.1158 0.0457  -0.1600 202 HOH   B O   
6989 O  O   . HOH   H .   ? 0.4838 0.3345 0.3724 -0.0531 0.0160  -0.1408 203 HOH   B O   
6990 O  O   . HOH   H .   ? 0.3390 0.4659 0.6233 -0.0946 0.0192  -0.1020 204 HOH   B O   
6991 O  O   . HOH   H .   ? 0.2821 0.7011 0.4125 0.0749  0.0238  0.2926  205 HOH   B O   
6992 O  O   . HOH   H .   ? 0.6598 0.6115 0.5691 0.2370  -0.0092 0.0524  206 HOH   B O   
6993 O  O   . HOH   H .   ? 0.3382 0.5734 0.4938 0.2330  0.0094  -0.0900 207 HOH   B O   
6994 O  O   . HOH   H .   ? 0.4952 0.3915 0.6110 0.0595  -0.1008 0.2455  208 HOH   B O   
6995 O  O   . HOH   H .   ? 0.4749 0.4777 0.2749 0.0298  -0.0383 -0.1295 209 HOH   B O   
6996 O  O   . HOH   H .   ? 0.1965 0.2235 0.2912 0.0122  0.0198  -0.0372 210 HOH   B O   
6997 O  O   . HOH   H .   ? 0.4784 0.6566 0.3636 0.2925  -0.1205 -0.0501 211 HOH   B O   
6998 O  O   . HOH   H .   ? 0.6614 0.4202 0.4293 0.0711  0.1373  0.0345  212 HOH   B O   
6999 O  O   . HOH   H .   ? 0.2884 0.5188 0.5336 -0.0184 0.1748  -0.1657 213 HOH   B O   
7000 O  O   . HOH   H .   ? 0.2904 0.2779 0.6409 0.0596  -0.1054 0.0604  214 HOH   B O   
7001 O  O   . HOH   H .   ? 0.3858 0.4421 0.4006 0.0215  0.0574  -0.1545 215 HOH   B O   
7002 O  O   . HOH   H .   ? 0.1606 0.1885 0.2644 -0.0173 -0.0072 0.0055  216 HOH   B O   
7003 O  O   . HOH   H .   ? 0.6014 0.2680 0.4615 -0.1834 -0.0066 0.0134  217 HOH   B O   
7004 O  O   . HOH   H .   ? 0.2934 0.2005 0.5093 0.0280  0.1842  0.0970  218 HOH   B O   
7005 O  O   . HOH   H .   ? 0.3061 0.2893 0.5915 0.0232  0.0615  0.0052  219 HOH   B O   
7006 O  O   . HOH   H .   ? 0.3770 0.3960 0.4693 0.0791  -0.0674 -0.0252 220 HOH   B O   
7007 O  O   . HOH   H .   ? 0.4248 0.3734 0.3333 0.0126  -0.1087 0.0618  221 HOH   B O   
7008 O  O   . HOH   H .   ? 0.4056 0.4756 0.4233 0.2270  -0.0338 0.0340  222 HOH   B O   
7009 O  O   . HOH   H .   ? 0.4407 0.6937 0.3073 0.2306  0.0462  0.0021  223 HOH   B O   
7010 O  O   . HOH   H .   ? 0.3806 0.4006 0.5764 -0.1589 -0.0208 0.0972  224 HOH   B O   
7011 O  O   . HOH   H .   ? 0.4651 0.1961 0.2840 -0.0051 -0.0761 0.0023  225 HOH   B O   
7012 O  O   . HOH   H .   ? 0.3065 0.2109 0.4650 0.0087  0.1669  0.0214  226 HOH   B O   
7013 O  O   . HOH   H .   ? 0.4267 0.5133 0.6895 0.0313  -0.1518 -0.1169 227 HOH   B O   
7014 O  O   . HOH   H .   ? 0.2344 0.1841 0.2682 -0.0266 0.1044  0.0027  228 HOH   B O   
7015 O  O   . HOH   H .   ? 0.2070 0.2212 0.3939 -0.0326 -0.0038 -0.0677 229 HOH   B O   
7016 O  O   . HOH   H .   ? 0.6334 0.5818 0.3111 0.1222  0.0309  0.0208  230 HOH   B O   
7017 O  O   . HOH   H .   ? 0.1637 0.2004 0.2958 -0.0163 0.0170  -0.0104 231 HOH   B O   
7018 O  O   . HOH   H .   ? 0.3652 0.2698 0.4009 0.0835  -0.0120 -0.0527 232 HOH   B O   
7019 O  O   . HOH   H .   ? 0.3588 0.3168 0.2080 0.0511  0.0797  0.0478  233 HOH   B O   
7020 O  O   . HOH   H .   ? 0.8006 0.4562 0.4367 0.2287  -0.0444 -0.1503 234 HOH   B O   
7021 O  O   . HOH   H .   ? 0.2599 0.3580 0.2688 -0.0797 0.0630  -0.0657 235 HOH   B O   
7022 O  O   . HOH   H .   ? 0.6617 0.3779 0.2360 0.0091  0.1199  -0.0057 236 HOH   B O   
7023 O  O   . HOH   H .   ? 0.2964 0.1748 0.6205 -0.0168 -0.1004 -0.0476 237 HOH   B O   
7024 O  O   . HOH   H .   ? 0.2012 0.3980 0.2304 -0.0523 -0.0238 0.0670  238 HOH   B O   
7025 O  O   . HOH   H .   ? 0.2149 0.3424 0.3253 -0.0554 -0.0492 -0.0320 239 HOH   B O   
7026 O  O   . HOH   H .   ? 0.3739 0.1714 0.2004 0.0192  -0.0905 -0.0119 240 HOH   B O   
7027 O  O   . HOH   H .   ? 0.2102 0.2277 0.3063 -0.0519 0.0231  -0.0343 241 HOH   B O   
7028 O  O   . HOH   H .   ? 0.1550 0.1436 0.2410 -0.0006 0.0101  -0.0095 242 HOH   B O   
7029 O  O   . HOH   H .   ? 0.2859 0.2534 0.3037 0.0582  0.0108  -0.0909 243 HOH   B O   
7030 O  O   . HOH   H .   ? 0.1403 0.1436 0.1513 -0.0147 -0.0088 -0.0014 244 HOH   B O   
7031 O  O   . HOH   H .   ? 0.4611 0.2941 0.3914 -0.2093 0.0242  0.0031  245 HOH   B O   
7032 O  O   . HOH   H .   ? 0.2057 0.1275 0.3182 0.0081  -0.0525 -0.0126 246 HOH   B O   
7033 O  O   . HOH   H .   ? 0.3259 0.4025 0.1937 0.0385  0.0764  0.0000  247 HOH   B O   
7034 O  O   . HOH   H .   ? 0.3578 0.2624 0.4289 0.0447  -0.0980 -0.1306 248 HOH   B O   
7035 O  O   . HOH   H .   ? 0.1398 0.1272 0.1514 0.0020  -0.0024 0.0065  249 HOH   B O   
7036 O  O   . HOH   H .   ? 0.2449 0.4599 0.6077 0.0437  -0.0030 -0.1335 250 HOH   B O   
7037 O  O   . HOH   H .   ? 0.2080 0.1909 0.1952 -0.0314 -0.0435 0.0177  251 HOH   B O   
7038 O  O   . HOH   H .   ? 0.2284 0.4579 0.5854 0.1213  -0.0482 -0.1188 252 HOH   B O   
7039 O  O   . HOH   H .   ? 0.2990 0.2185 0.2988 0.0908  0.0986  0.0154  253 HOH   B O   
7040 O  O   . HOH   H .   ? 0.2754 0.4738 0.3406 -0.1063 -0.0277 -0.1166 254 HOH   B O   
7041 O  O   . HOH   H .   ? 0.2510 0.2072 0.1753 0.0165  -0.0241 0.0007  255 HOH   B O   
7042 O  O   . HOH   H .   ? 0.2386 0.2206 0.2402 0.0776  -0.0856 -0.0647 256 HOH   B O   
7043 O  O   . HOH   H .   ? 0.3220 0.2428 0.3069 -0.0424 0.0345  -0.0466 257 HOH   B O   
7044 O  O   . HOH   H .   ? 0.4158 0.3585 0.3762 -0.0804 0.0795  -0.1097 258 HOH   B O   
7045 O  O   . HOH   H .   ? 0.2083 0.1516 0.1883 -0.0316 -0.0351 0.0248  259 HOH   B O   
7046 O  O   . HOH   H .   ? 0.3799 0.3184 0.4483 -0.0026 -0.1285 -0.0493 260 HOH   B O   
7047 O  O   . HOH   H .   ? 0.1661 0.1625 0.2703 -0.0260 -0.0164 0.0015  261 HOH   B O   
7048 O  O   . HOH   H .   ? 0.2224 0.2020 0.1962 0.0150  -0.0130 0.0038  262 HOH   B O   
7049 O  O   . HOH   H .   ? 0.2215 0.2911 0.2066 -0.0527 0.0285  0.0340  263 HOH   B O   
7050 O  O   . HOH   H .   ? 0.2410 0.3771 0.3893 0.0082  0.1172  0.0252  264 HOH   B O   
7051 O  O   . HOH   H .   ? 0.1325 0.1597 0.1898 -0.0063 0.0077  0.0149  265 HOH   B O   
7052 O  O   . HOH   H .   ? 0.5160 0.3152 0.5193 0.0864  0.0476  -0.0642 266 HOH   B O   
7053 O  O   . HOH   H .   ? 0.2279 0.2515 0.2263 -0.0382 -0.0681 -0.0353 267 HOH   B O   
7054 O  O   . HOH   H .   ? 0.2049 0.4324 0.5413 -0.0569 -0.0195 -0.1502 268 HOH   B O   
7055 O  O   . HOH   H .   ? 0.2277 0.1914 0.3272 0.0020  -0.0465 -0.0261 269 HOH   B O   
7056 O  O   . HOH   H .   ? 0.3173 0.4740 0.3822 -0.0483 -0.1239 0.1237  270 HOH   B O   
7057 O  O   . HOH   H .   ? 0.3111 0.3765 0.5325 0.0973  -0.0659 -0.1044 271 HOH   B O   
7058 O  O   . HOH   H .   ? 0.2559 0.1995 0.2907 -0.0673 0.0097  -0.0020 272 HOH   B O   
7059 O  O   . HOH   H .   ? 0.1632 0.1350 0.4203 -0.0071 -0.0288 -0.0100 273 HOH   B O   
7060 O  O   . HOH   H .   ? 0.1841 0.1770 0.1618 -0.0432 -0.0372 0.0092  274 HOH   B O   
7061 O  O   . HOH   H .   ? 0.2488 0.2829 0.2249 -0.0468 -0.0871 0.0183  275 HOH   B O   
7062 O  O   . HOH   H .   ? 0.2183 0.2651 0.2278 0.0672  -0.0145 -0.0193 276 HOH   B O   
7063 O  O   . HOH   H .   ? 0.4739 0.6162 0.2479 0.0047  -0.0767 0.0322  277 HOH   B O   
7064 O  O   . HOH   H .   ? 0.1964 0.1481 0.2115 -0.0280 -0.0146 0.0151  278 HOH   B O   
7065 O  O   . HOH   H .   ? 0.2196 0.3377 0.3083 -0.0305 0.0283  -0.1198 279 HOH   B O   
7066 O  O   . HOH   H .   ? 0.3221 0.6997 0.7367 0.0858  -0.0885 -0.0844 280 HOH   B O   
7067 O  O   . HOH   H .   ? 0.2869 0.2081 0.5447 0.0187  0.0589  0.0719  281 HOH   B O   
7068 O  O   . HOH   H .   ? 0.2623 0.4687 0.5316 -0.1034 -0.1436 0.0949  282 HOH   B O   
7069 O  O   . HOH   H .   ? 0.1612 0.1448 0.1853 0.0002  0.0068  0.0010  283 HOH   B O   
7070 O  O   . HOH   H .   ? 0.1594 0.1571 0.3028 -0.0095 0.0110  -0.0060 284 HOH   B O   
7071 O  O   . HOH   H .   ? 0.2440 0.6452 0.2397 0.0655  -0.0310 -0.0296 285 HOH   B O   
7072 O  O   . HOH   H .   ? 0.4584 0.4469 0.4849 0.0393  -0.1538 -0.0189 286 HOH   B O   
7073 O  O   . HOH   H .   ? 0.1608 0.2038 0.2736 0.0208  -0.0091 0.0069  287 HOH   B O   
7074 O  O   . HOH   H .   ? 0.2369 0.2663 0.2861 0.0158  -0.0814 0.0232  288 HOH   B O   
7075 O  O   . HOH   H .   ? 0.3382 0.6957 0.3284 0.1324  -0.0736 0.1234  289 HOH   B O   
7076 O  O   . HOH   H .   ? 0.1607 0.1995 0.1441 -0.0146 -0.0202 0.0060  290 HOH   B O   
7077 O  O   . HOH   H .   ? 0.3740 0.2153 0.3658 -0.0975 -0.1897 0.0857  291 HOH   B O   
7078 O  O   . HOH   H .   ? 0.1710 0.1575 0.2279 0.0112  0.0104  0.0182  292 HOH   B O   
7079 O  O   . HOH   H .   ? 0.1694 0.3216 0.4630 0.0276  0.0129  -0.1319 293 HOH   B O   
7080 O  O   . HOH   H .   ? 0.4935 0.3696 0.2362 0.1338  -0.0818 0.0373  294 HOH   B O   
7081 O  O   . HOH   H .   ? 0.5429 0.3616 0.2751 0.2488  0.0883  0.0727  295 HOH   B O   
7082 O  O   . HOH   H .   ? 0.3397 0.2966 0.2013 0.0327  -0.0819 -0.0119 296 HOH   B O   
7083 O  O   . HOH   H .   ? 0.4509 0.3972 0.2667 0.0379  0.0064  -0.1085 297 HOH   B O   
7084 O  O   . HOH   H .   ? 0.6096 0.6985 0.5323 0.3453  -0.0021 -0.0567 298 HOH   B O   
7085 O  O   . HOH   H .   ? 0.2947 0.2869 0.4796 -0.0327 -0.0790 0.1264  299 HOH   B O   
7086 O  O   . HOH   H .   ? 0.2074 0.1634 0.2392 -0.0256 -0.0297 0.0004  300 HOH   B O   
7087 O  O   . HOH   H .   ? 0.1999 0.2698 0.6554 0.0390  -0.0469 -0.1312 301 HOH   B O   
7088 O  O   . HOH   H .   ? 0.3234 0.2888 0.2699 -0.0143 0.0155  -0.1336 302 HOH   B O   
7089 O  O   . HOH   H .   ? 0.3456 0.1888 0.3276 0.0725  0.1162  0.0412  303 HOH   B O   
7090 O  O   . HOH   H .   ? 0.4101 0.4107 0.4672 -0.0672 -0.0063 0.1344  304 HOH   B O   
7091 O  O   . HOH   H .   ? 0.2869 0.2892 0.3524 -0.0672 0.1121  -0.0964 305 HOH   B O   
7092 O  O   . HOH   H .   ? 0.4470 0.4519 0.2107 0.0279  0.0777  0.0638  306 HOH   B O   
7093 O  O   . HOH   H .   ? 0.1568 0.1411 0.2833 0.0052  -0.0010 -0.0082 307 HOH   B O   
7094 O  O   . HOH   H .   ? 0.2045 0.1515 0.3330 0.0355  -0.0918 -0.0060 308 HOH   B O   
7095 O  O   . HOH   H .   ? 0.2170 0.3294 0.4977 -0.0230 -0.0529 -0.0413 309 HOH   B O   
7096 O  O   . HOH   H .   ? 0.5122 0.2933 0.2234 -0.1749 0.0626  -0.0207 310 HOH   B O   
7097 O  O   . HOH   H .   ? 0.2385 0.1483 0.2306 -0.0195 -0.0187 0.0278  311 HOH   B O   
7098 O  O   . HOH   H .   ? 0.3758 0.2221 0.2526 0.1399  0.0898  0.0324  312 HOH   B O   
7099 O  O   . HOH   H .   ? 0.1535 0.1813 0.2867 -0.0227 0.0000  0.0096  313 HOH   B O   
7100 O  O   . HOH   H .   ? 0.3011 0.3129 0.4077 -0.0937 0.1136  -0.0344 314 HOH   B O   
7101 O  O   . HOH   H .   ? 0.3190 0.3945 0.8294 -0.0318 -0.0963 0.2177  315 HOH   B O   
7102 O  O   . HOH   H .   ? 0.2169 0.1989 0.1792 -0.0049 0.0208  0.0199  316 HOH   B O   
7103 O  O   . HOH   H .   ? 0.4605 0.4474 0.2726 0.0400  -0.0424 -0.0915 317 HOH   B O   
7104 O  O   . HOH   H .   ? 0.2711 0.3032 0.4860 -0.0460 -0.1422 0.1175  318 HOH   B O   
7105 O  O   . HOH   H .   ? 0.1515 0.1527 0.2739 -0.0078 -0.0167 -0.0098 319 HOH   B O   
7106 O  O   . HOH   H .   ? 0.1651 0.2909 0.2258 -0.0162 -0.0153 0.0687  320 HOH   B O   
7107 O  O   . HOH   H .   ? 0.2095 0.5322 0.5156 -0.0379 0.0080  -0.0294 321 HOH   B O   
7108 O  O   . HOH   H .   ? 0.4411 0.4289 0.2262 0.1107  -0.0713 -0.0231 322 HOH   B O   
7109 O  O   . HOH   H .   ? 0.3956 0.4193 0.6494 0.0508  0.0090  0.0742  323 HOH   B O   
7110 O  O   . HOH   H .   ? 0.4215 0.3016 0.5241 0.1129  0.2113  0.1727  324 HOH   B O   
7111 O  O   . HOH   H .   ? 0.2913 0.2217 0.2292 0.0288  -0.0282 0.0300  325 HOH   B O   
7112 O  O   . HOH   H .   ? 0.6563 0.5605 0.5057 -0.1238 0.0039  0.1614  326 HOH   B O   
7113 O  O   . HOH   H .   ? 0.1773 0.1964 0.2811 0.0316  0.0385  0.0193  327 HOH   B O   
7114 O  O   . HOH   H .   ? 0.6230 0.4648 0.5385 0.1366  0.1568  0.0435  328 HOH   B O   
7115 O  O   . HOH   H .   ? 0.7650 0.2134 0.3068 0.0138  -0.0881 0.0094  329 HOH   B O   
7116 O  O   . HOH   H .   ? 0.5882 0.4917 0.6935 0.1215  -0.1269 0.2224  330 HOH   B O   
7117 O  O   . HOH   H .   ? 0.1623 0.2726 0.3123 0.0343  -0.0183 -0.0699 331 HOH   B O   
7118 O  O   . HOH   H .   ? 0.4439 0.2551 0.2746 0.0384  0.0210  0.0887  332 HOH   B O   
7119 O  O   . HOH   H .   ? 0.5618 0.3278 0.3560 0.0141  0.1027  0.1210  333 HOH   B O   
7120 O  O   . HOH   H .   ? 0.2657 0.1896 0.5777 -0.0047 -0.0032 0.0435  334 HOH   B O   
7121 O  O   . HOH   H .   ? 0.5841 0.4340 0.6047 -0.0913 -0.1066 -0.1376 335 HOH   B O   
7122 O  O   . HOH   H .   ? 0.4675 0.5499 0.3379 0.0100  -0.1014 0.0722  336 HOH   B O   
7123 O  O   . HOH   H .   ? 0.2256 0.2366 0.5487 -0.0511 -0.0036 0.1434  337 HOH   B O   
7124 O  O   . HOH   H .   ? 0.1726 0.1402 0.2246 0.0072  -0.0176 0.0050  338 HOH   B O   
7125 O  O   . HOH   H .   ? 0.5873 0.3285 0.4643 -0.0005 0.1363  -0.1679 339 HOH   B O   
7126 O  O   . HOH   H .   ? 0.5228 0.3130 0.2876 0.0771  -0.1330 -0.0789 340 HOH   B O   
7127 O  O   . HOH   H .   ? 0.3944 0.7088 0.4020 0.0354  -0.0555 0.1402  341 HOH   B O   
7128 O  O   . HOH   H .   ? 0.3678 0.6353 0.3948 -0.0987 -0.0972 -0.0700 342 HOH   B O   
7129 O  O   . HOH   H .   ? 0.1868 0.6291 0.5611 -0.0032 -0.0263 -0.0448 343 HOH   B O   
7130 O  O   . HOH   H .   ? 0.6909 0.6170 0.2776 0.0435  -0.0660 0.1349  344 HOH   B O   
7131 O  O   . HOH   H .   ? 0.2033 0.1803 0.2761 -0.0050 0.0566  -0.0062 345 HOH   B O   
7132 O  O   . HOH   H .   ? 0.4213 0.4837 0.5692 -0.0201 -0.0985 0.0803  346 HOH   B O   
7133 O  O   . HOH   H .   ? 0.2011 0.4030 0.5292 0.0455  0.0286  -0.0162 347 HOH   B O   
7134 O  O   . HOH   H .   ? 0.4605 0.5459 0.4860 -0.1249 0.0777  0.0445  348 HOH   B O   
7135 O  O   . HOH   H .   ? 0.2385 0.5800 0.3684 0.1540  -0.0484 -0.1537 349 HOH   B O   
7136 O  O   . HOH   H .   ? 0.4240 0.6527 0.7193 0.0359  0.0636  -0.0435 350 HOH   B O   
7137 O  O   . HOH   H .   ? 0.2725 0.2305 0.5249 -0.0319 -0.0902 -0.0645 351 HOH   B O   
7138 O  O   . HOH   H .   ? 0.3997 0.2321 0.3608 -0.0909 0.0577  -0.1062 352 HOH   B O   
7139 O  O   . HOH   H .   ? 0.3154 0.1880 0.3852 0.0448  -0.1295 -0.0595 353 HOH   B O   
7140 O  O   . HOH   H .   ? 0.3473 0.2942 0.3792 -0.0862 -0.0268 -0.0765 354 HOH   B O   
7141 O  O   . HOH   H .   ? 0.4972 0.3518 0.4401 0.0623  0.1119  -0.0675 355 HOH   B O   
7142 O  O   . HOH   H .   ? 0.3208 0.5268 0.4666 -0.1519 0.0237  -0.0605 356 HOH   B O   
7143 O  O   . HOH   H .   ? 0.5000 0.3291 0.4463 -0.1287 0.1552  0.0515  357 HOH   B O   
7144 O  O   . HOH   H .   ? 0.4753 0.5395 0.5074 0.2042  -0.1332 0.1339  358 HOH   B O   
7145 O  O   . HOH   H .   ? 0.4735 0.4703 0.5181 -0.0498 0.0417  -0.0538 359 HOH   B O   
7146 O  O   . HOH   H .   ? 0.6193 0.3677 0.4612 -0.0294 -0.1504 -0.0716 360 HOH   B O   
7147 O  O   . HOH   H .   ? 0.4682 0.3905 0.6140 0.0462  0.0911  0.1003  361 HOH   B O   
7148 O  O   . HOH   H .   ? 0.4180 0.5448 0.2882 0.1727  -0.0427 -0.0094 362 HOH   B O   
7149 O  O   . HOH   H .   ? 0.2240 0.4207 0.6425 -0.1006 -0.0636 -0.0687 363 HOH   B O   
7150 O  O   . HOH   H .   ? 0.4940 0.3236 0.5011 -0.1229 -0.0331 0.0180  364 HOH   B O   
7151 O  O   . HOH   H .   ? 0.6620 0.4883 0.3832 0.1772  0.0719  0.0849  365 HOH   B O   
7152 O  O   . HOH   H .   ? 0.5469 0.4851 0.3234 0.1355  -0.1599 0.0238  366 HOH   B O   
7153 O  O   . HOH   H .   ? 0.4589 0.4723 0.5218 0.1861  -0.1460 0.0223  367 HOH   B O   
7154 O  O   . HOH   H .   ? 0.6098 0.2281 0.3342 -0.0069 0.0224  0.0683  368 HOH   B O   
7155 O  O   . HOH   H .   ? 0.5566 0.4762 0.4221 -0.0146 -0.1195 -0.0902 369 HOH   B O   
7156 O  O   . HOH   H .   ? 0.4343 0.5900 0.4748 0.2758  0.1267  0.1677  370 HOH   B O   
7157 O  O   . HOH   H .   ? 0.7544 0.6820 0.4220 0.2186  -0.1277 0.0652  371 HOH   B O   
7158 O  O   . HOH   H .   ? 0.6137 0.3498 0.2658 -0.1161 -0.0918 -0.0217 372 HOH   B O   
7159 O  O   . HOH   H .   ? 0.3740 0.3010 0.4169 0.0593  -0.1448 -0.0220 373 HOH   B O   
7160 O  O   . HOH   H .   ? 0.4773 0.5306 0.4753 -0.1035 -0.0997 0.0607  374 HOH   B O   
7161 O  O   . HOH   H .   ? 0.4109 0.6725 0.6430 0.1233  0.0568  0.2844  375 HOH   B O   
7162 O  O   . HOH   H .   ? 0.2205 0.4126 0.4514 0.0320  -0.0581 -0.0729 376 HOH   B O   
7163 O  O   . HOH   H .   ? 0.2810 0.4674 0.1999 0.0475  0.0173  0.0031  377 HOH   B O   
7164 O  O   . HOH   H .   ? 0.5700 0.7592 0.3706 -0.1375 0.0359  -0.1501 378 HOH   B O   
7165 O  O   . HOH   H .   ? 0.3444 0.5533 0.5249 0.0746  -0.0069 -0.0158 379 HOH   B O   
7166 O  O   . HOH   H .   ? 0.7156 0.3532 0.5062 -0.1222 -0.1182 -0.0065 380 HOH   B O   
7167 O  O   . HOH   H .   ? 0.6570 0.7095 0.6063 -0.0301 0.2808  0.1905  381 HOH   B O   
7168 O  O   . HOH   H .   ? 0.2920 0.2457 0.3116 0.0089  0.0246  0.0367  382 HOH   B O   
7169 O  O   . HOH   H .   ? 0.4706 0.7610 0.5622 -0.0047 0.2217  0.0461  383 HOH   B O   
7170 O  O   . HOH   H .   ? 0.5077 0.4831 0.4247 0.0332  -0.0567 -0.0302 384 HOH   B O   
7171 O  O   . HOH   H .   ? 0.7777 0.4032 0.4147 0.1456  0.0649  -0.0767 385 HOH   B O   
7172 O  O   . HOH   H .   ? 0.5957 0.4113 0.5185 -0.0888 0.0935  -0.0374 386 HOH   B O   
7173 O  O   . HOH   H .   ? 0.4519 0.3834 0.2958 0.0198  0.0569  0.0027  387 HOH   B O   
7174 O  O   . HOH   H .   ? 0.7523 0.5135 0.3801 0.1977  0.0248  0.0322  388 HOH   B O   
7175 O  O   . HOH   H .   ? 0.2343 0.4016 0.3637 -0.0641 -0.0839 -0.0090 389 HOH   B O   
7176 O  O   . HOH   H .   ? 0.3819 0.2011 0.3385 0.0656  -0.0361 0.0196  390 HOH   B O   
7177 O  O   . HOH   H .   ? 0.4654 0.4178 0.4301 0.0530  0.0956  0.1000  391 HOH   B O   
7178 O  O   . HOH   H .   ? 0.2465 0.4319 0.6814 -0.1190 -0.0666 -0.0318 392 HOH   B O   
7179 O  O   . HOH   H .   ? 0.4113 0.2270 0.4965 -0.0534 0.0805  0.0547  393 HOH   B O   
7180 O  O   . HOH   H .   ? 0.4275 0.4143 0.4257 0.0126  0.0873  0.0720  394 HOH   B O   
7181 O  O   . HOH   H .   ? 0.4538 0.5799 0.3629 0.0899  0.0257  -0.0816 395 HOH   B O   
7182 O  O   . HOH   H .   ? 0.3194 0.3618 0.3727 0.0388  0.0078  -0.0595 396 HOH   B O   
7183 O  O   . HOH   H .   ? 0.2207 0.2734 0.5816 -0.0581 -0.1052 -0.0013 397 HOH   B O   
7184 O  O   . HOH   H .   ? 0.5534 0.6742 0.6988 0.1150  -0.1112 0.3001  398 HOH   B O   
7185 O  O   . HOH   H .   ? 0.5765 0.4227 0.3071 -0.2231 -0.0314 0.1276  399 HOH   B O   
7186 O  O   . HOH   H .   ? 0.6200 0.6012 0.3664 0.2479  -0.0212 -0.0324 400 HOH   B O   
# 
