data_7HEV
# 
_entry.id   7HEV 
# 
_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   7HEV         pdb_00007hev 10.2210/pdb7hev/pdb 
WWPDB D_1001407385 ?            ?                   
# 
_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                        7HEV 
_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 '(2R)-3-(pyridin-2-yl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' 269.302   1   ? ? ? ? 
3 non-polymer syn '(2S)-3-(pyridin-2-yl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' 269.302   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                                35.453    1   ? ? ? ? 
5 water       nat water                                                                         18.015    426 ? ? ? ? 
# 
_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 '(2R)-3-(pyridin-2-yl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' A1BAD 
3 '(2S)-3-(pyridin-2-yl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' A1BAE 
4 'CHLORIDE ION'                                                                CL    
5 water                                                                         HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BAD non-polymer         . '(2R)-3-(pyridin-2-yl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' ? 'C14 H15 N5 O'   
269.302 
A1BAE non-polymer         . '(2S)-3-(pyridin-2-yl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' ? 'C14 H15 N5 O'   
269.302 
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 
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 A1BAD 1   201 201  A1BAD LA1 A . 
D 3 A1BAE 1   202 301  A1BAE LA2 A . 
E 4 CL    1   203 1    CL    CL  A . 
F 5 HOH   1   301 196  HOH   HOH A . 
F 5 HOH   2   302 292  HOH   HOH A . 
F 5 HOH   3   303 85   HOH   HOH A . 
F 5 HOH   4   304 153  HOH   HOH A . 
F 5 HOH   5   305 625  HOH   HOH A . 
F 5 HOH   6   306 1289 HOH   HOH A . 
F 5 HOH   7   307 109  HOH   HOH A . 
F 5 HOH   8   308 229  HOH   HOH A . 
F 5 HOH   9   309 86   HOH   HOH A . 
F 5 HOH   10  310 493  HOH   HOH A . 
F 5 HOH   11  311 148  HOH   HOH A . 
F 5 HOH   12  312 1301 HOH   HOH A . 
F 5 HOH   13  313 337  HOH   HOH A . 
F 5 HOH   14  314 93   HOH   HOH A . 
F 5 HOH   15  315 209  HOH   HOH A . 
F 5 HOH   16  316 10   HOH   HOH A . 
F 5 HOH   17  317 76   HOH   HOH A . 
F 5 HOH   18  318 136  HOH   HOH A . 
F 5 HOH   19  319 124  HOH   HOH A . 
F 5 HOH   20  320 1295 HOH   HOH A . 
F 5 HOH   21  321 151  HOH   HOH A . 
F 5 HOH   22  322 236  HOH   HOH A . 
F 5 HOH   23  323 57   HOH   HOH A . 
F 5 HOH   24  324 225  HOH   HOH A . 
F 5 HOH   25  325 36   HOH   HOH A . 
F 5 HOH   26  326 140  HOH   HOH A . 
F 5 HOH   27  327 964  HOH   HOH A . 
F 5 HOH   28  328 192  HOH   HOH A . 
F 5 HOH   29  329 1283 HOH   HOH A . 
F 5 HOH   30  330 662  HOH   HOH A . 
F 5 HOH   31  331 393  HOH   HOH A . 
F 5 HOH   32  332 1290 HOH   HOH A . 
F 5 HOH   33  333 199  HOH   HOH A . 
F 5 HOH   34  334 241  HOH   HOH A . 
F 5 HOH   35  335 21   HOH   HOH A . 
F 5 HOH   36  336 247  HOH   HOH A . 
F 5 HOH   37  337 320  HOH   HOH A . 
F 5 HOH   38  338 70   HOH   HOH A . 
F 5 HOH   39  339 105  HOH   HOH A . 
F 5 HOH   40  340 155  HOH   HOH A . 
F 5 HOH   41  341 14   HOH   HOH A . 
F 5 HOH   42  342 42   HOH   HOH A . 
F 5 HOH   43  343 164  HOH   HOH A . 
F 5 HOH   44  344 630  HOH   HOH A . 
F 5 HOH   45  345 92   HOH   HOH A . 
F 5 HOH   46  346 469  HOH   HOH A . 
F 5 HOH   47  347 165  HOH   HOH A . 
F 5 HOH   48  348 139  HOH   HOH A . 
F 5 HOH   49  349 195  HOH   HOH A . 
F 5 HOH   50  350 18   HOH   HOH A . 
F 5 HOH   51  351 354  HOH   HOH A . 
F 5 HOH   52  352 169  HOH   HOH A . 
F 5 HOH   53  353 102  HOH   HOH A . 
F 5 HOH   54  354 39   HOH   HOH A . 
F 5 HOH   55  355 409  HOH   HOH A . 
F 5 HOH   56  356 939  HOH   HOH A . 
F 5 HOH   57  357 8    HOH   HOH A . 
F 5 HOH   58  358 27   HOH   HOH A . 
F 5 HOH   59  359 66   HOH   HOH A . 
F 5 HOH   60  360 2    HOH   HOH A . 
F 5 HOH   61  361 162  HOH   HOH A . 
F 5 HOH   62  362 56   HOH   HOH A . 
F 5 HOH   63  363 396  HOH   HOH A . 
F 5 HOH   64  364 45   HOH   HOH A . 
F 5 HOH   65  365 33   HOH   HOH A . 
F 5 HOH   66  366 1300 HOH   HOH A . 
F 5 HOH   67  367 18   HOH   HOH A . 
F 5 HOH   68  368 19   HOH   HOH A . 
F 5 HOH   69  369 81   HOH   HOH A . 
F 5 HOH   70  370 5    HOH   HOH A . 
F 5 HOH   71  371 1    HOH   HOH A . 
F 5 HOH   72  372 17   HOH   HOH A . 
F 5 HOH   73  373 159  HOH   HOH A . 
F 5 HOH   74  374 296  HOH   HOH A . 
F 5 HOH   75  375 186  HOH   HOH A . 
F 5 HOH   76  376 16   HOH   HOH A . 
F 5 HOH   77  377 49   HOH   HOH A . 
F 5 HOH   78  378 138  HOH   HOH A . 
F 5 HOH   79  379 3    HOH   HOH A . 
F 5 HOH   80  380 218  HOH   HOH A . 
F 5 HOH   81  381 12   HOH   HOH A . 
F 5 HOH   82  382 461  HOH   HOH A . 
F 5 HOH   83  383 26   HOH   HOH A . 
F 5 HOH   84  384 24   HOH   HOH A . 
F 5 HOH   85  385 661  HOH   HOH A . 
F 5 HOH   86  386 134  HOH   HOH A . 
F 5 HOH   87  387 46   HOH   HOH A . 
F 5 HOH   88  388 11   HOH   HOH A . 
F 5 HOH   89  389 35   HOH   HOH A . 
F 5 HOH   90  390 34   HOH   HOH A . 
F 5 HOH   91  391 154  HOH   HOH A . 
F 5 HOH   92  392 58   HOH   HOH A . 
F 5 HOH   93  393 366  HOH   HOH A . 
F 5 HOH   94  394 333  HOH   HOH A . 
F 5 HOH   95  395 1310 HOH   HOH A . 
F 5 HOH   96  396 1308 HOH   HOH A . 
F 5 HOH   97  397 78   HOH   HOH A . 
F 5 HOH   98  398 4    HOH   HOH A . 
F 5 HOH   99  399 122  HOH   HOH A . 
F 5 HOH   100 400 74   HOH   HOH A . 
F 5 HOH   101 401 116  HOH   HOH A . 
F 5 HOH   102 402 351  HOH   HOH A . 
F 5 HOH   103 403 1275 HOH   HOH A . 
F 5 HOH   104 404 3    HOH   HOH A . 
F 5 HOH   105 405 121  HOH   HOH A . 
F 5 HOH   106 406 1315 HOH   HOH A . 
F 5 HOH   107 407 4    HOH   HOH A . 
F 5 HOH   108 408 132  HOH   HOH A . 
F 5 HOH   109 409 83   HOH   HOH A . 
F 5 HOH   110 410 67   HOH   HOH A . 
F 5 HOH   111 411 68   HOH   HOH A . 
F 5 HOH   112 412 303  HOH   HOH A . 
F 5 HOH   113 413 1313 HOH   HOH A . 
F 5 HOH   114 414 281  HOH   HOH A . 
F 5 HOH   115 415 1309 HOH   HOH A . 
F 5 HOH   116 416 25   HOH   HOH A . 
F 5 HOH   117 417 6    HOH   HOH A . 
F 5 HOH   118 418 7    HOH   HOH A . 
F 5 HOH   119 419 381  HOH   HOH A . 
F 5 HOH   120 420 123  HOH   HOH A . 
F 5 HOH   121 421 397  HOH   HOH A . 
F 5 HOH   122 422 13   HOH   HOH A . 
F 5 HOH   123 423 278  HOH   HOH A . 
F 5 HOH   124 424 95   HOH   HOH A . 
F 5 HOH   125 425 125  HOH   HOH A . 
F 5 HOH   126 426 582  HOH   HOH A . 
F 5 HOH   127 427 53   HOH   HOH A . 
F 5 HOH   128 428 405  HOH   HOH A . 
F 5 HOH   129 429 156  HOH   HOH A . 
F 5 HOH   130 430 51   HOH   HOH A . 
F 5 HOH   131 431 1279 HOH   HOH A . 
F 5 HOH   132 432 8    HOH   HOH A . 
F 5 HOH   133 433 1068 HOH   HOH A . 
F 5 HOH   134 434 96   HOH   HOH A . 
F 5 HOH   135 435 115  HOH   HOH A . 
F 5 HOH   136 436 1222 HOH   HOH A . 
F 5 HOH   137 437 1238 HOH   HOH A . 
F 5 HOH   138 438 188  HOH   HOH A . 
F 5 HOH   139 439 1286 HOH   HOH A . 
F 5 HOH   140 440 16   HOH   HOH A . 
F 5 HOH   141 441 15   HOH   HOH A . 
F 5 HOH   142 442 1296 HOH   HOH A . 
F 5 HOH   143 443 212  HOH   HOH A . 
F 5 HOH   144 444 73   HOH   HOH A . 
F 5 HOH   145 445 71   HOH   HOH A . 
F 5 HOH   146 446 80   HOH   HOH A . 
F 5 HOH   147 447 40   HOH   HOH A . 
F 5 HOH   148 448 944  HOH   HOH A . 
F 5 HOH   149 449 94   HOH   HOH A . 
F 5 HOH   150 450 19   HOH   HOH A . 
F 5 HOH   151 451 952  HOH   HOH A . 
F 5 HOH   152 452 1189 HOH   HOH A . 
F 5 HOH   153 453 97   HOH   HOH A . 
F 5 HOH   154 454 104  HOH   HOH A . 
F 5 HOH   155 455 576  HOH   HOH A . 
F 5 HOH   156 456 1094 HOH   HOH A . 
F 5 HOH   157 457 79   HOH   HOH A . 
F 5 HOH   158 458 330  HOH   HOH A . 
F 5 HOH   159 459 1119 HOH   HOH A . 
F 5 HOH   160 460 7    HOH   HOH A . 
F 5 HOH   161 461 1134 HOH   HOH A . 
F 5 HOH   162 462 107  HOH   HOH A . 
F 5 HOH   163 463 509  HOH   HOH A . 
F 5 HOH   164 464 1276 HOH   HOH A . 
F 5 HOH   165 465 163  HOH   HOH A . 
F 5 HOH   166 466 726  HOH   HOH A . 
F 5 HOH   167 467 408  HOH   HOH A . 
F 5 HOH   168 468 756  HOH   HOH A . 
F 5 HOH   169 469 319  HOH   HOH A . 
F 5 HOH   170 470 280  HOH   HOH A . 
F 5 HOH   171 471 361  HOH   HOH A . 
F 5 HOH   172 472 556  HOH   HOH A . 
F 5 HOH   173 473 126  HOH   HOH A . 
F 5 HOH   174 474 63   HOH   HOH A . 
F 5 HOH   175 475 17   HOH   HOH A . 
F 5 HOH   176 476 2    HOH   HOH A . 
F 5 HOH   177 477 801  HOH   HOH A . 
F 5 HOH   178 478 1307 HOH   HOH A . 
F 5 HOH   179 479 250  HOH   HOH A . 
F 5 HOH   180 480 342  HOH   HOH A . 
F 5 HOH   181 481 135  HOH   HOH A . 
F 5 HOH   182 482 370  HOH   HOH A . 
F 5 HOH   183 483 1306 HOH   HOH A . 
F 5 HOH   184 484 202  HOH   HOH A . 
F 5 HOH   185 485 1287 HOH   HOH A . 
F 5 HOH   186 486 224  HOH   HOH A . 
F 5 HOH   187 487 267  HOH   HOH A . 
F 5 HOH   188 488 1284 HOH   HOH A . 
F 5 HOH   189 489 674  HOH   HOH A . 
F 5 HOH   190 490 919  HOH   HOH A . 
F 5 HOH   191 491 695  HOH   HOH A . 
F 5 HOH   192 492 5    HOH   HOH A . 
F 5 HOH   193 493 318  HOH   HOH A . 
F 5 HOH   194 494 309  HOH   HOH A . 
F 5 HOH   195 495 315  HOH   HOH A . 
F 5 HOH   196 496 1299 HOH   HOH A . 
F 5 HOH   197 497 1314 HOH   HOH A . 
F 5 HOH   198 498 521  HOH   HOH A . 
F 5 HOH   199 499 12   HOH   HOH A . 
F 5 HOH   200 500 331  HOH   HOH A . 
F 5 HOH   201 501 263  HOH   HOH A . 
F 5 HOH   202 502 941  HOH   HOH A . 
F 5 HOH   203 503 152  HOH   HOH A . 
F 5 HOH   204 504 805  HOH   HOH A . 
F 5 HOH   205 505 711  HOH   HOH A . 
F 5 HOH   206 506 326  HOH   HOH A . 
F 5 HOH   207 507 208  HOH   HOH A . 
F 5 HOH   208 508 6    HOH   HOH A . 
F 5 HOH   209 509 981  HOH   HOH A . 
F 5 HOH   210 510 1071 HOH   HOH A . 
F 5 HOH   211 511 180  HOH   HOH A . 
F 5 HOH   212 512 350  HOH   HOH A . 
F 5 HOH   213 513 356  HOH   HOH A . 
F 5 HOH   214 514 9    HOH   HOH A . 
F 5 HOH   215 515 363  HOH   HOH A . 
F 5 HOH   216 516 313  HOH   HOH A . 
F 5 HOH   217 517 371  HOH   HOH A . 
F 5 HOH   218 518 185  HOH   HOH A . 
F 5 HOH   219 519 429  HOH   HOH A . 
F 5 HOH   220 520 772  HOH   HOH A . 
F 5 HOH   221 521 376  HOH   HOH A . 
F 5 HOH   222 522 1074 HOH   HOH A . 
F 5 HOH   223 523 346  HOH   HOH A . 
F 5 HOH   224 524 1292 HOH   HOH A . 
F 5 HOH   225 525 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 549  HOH   HOH B . 
G 5 HOH   3   203 358  HOH   HOH B . 
G 5 HOH   4   204 531  HOH   HOH B . 
G 5 HOH   5   205 398  HOH   HOH B . 
G 5 HOH   6   206 364  HOH   HOH B . 
G 5 HOH   7   207 1249 HOH   HOH B . 
G 5 HOH   8   208 758  HOH   HOH B . 
G 5 HOH   9   209 240  HOH   HOH B . 
G 5 HOH   10  210 900  HOH   HOH B . 
G 5 HOH   11  211 264  HOH   HOH B . 
G 5 HOH   12  212 743  HOH   HOH B . 
G 5 HOH   13  213 343  HOH   HOH B . 
G 5 HOH   14  214 120  HOH   HOH B . 
G 5 HOH   15  215 232  HOH   HOH B . 
G 5 HOH   16  216 353  HOH   HOH B . 
G 5 HOH   17  217 654  HOH   HOH B . 
G 5 HOH   18  218 452  HOH   HOH B . 
G 5 HOH   19  219 50   HOH   HOH B . 
G 5 HOH   20  220 15   HOH   HOH B . 
G 5 HOH   21  221 131  HOH   HOH B . 
G 5 HOH   22  222 1312 HOH   HOH B . 
G 5 HOH   23  223 444  HOH   HOH B . 
G 5 HOH   24  224 276  HOH   HOH B . 
G 5 HOH   25  225 723  HOH   HOH B . 
G 5 HOH   26  226 82   HOH   HOH B . 
G 5 HOH   27  227 1140 HOH   HOH B . 
G 5 HOH   28  228 54   HOH   HOH B . 
G 5 HOH   29  229 282  HOH   HOH B . 
G 5 HOH   30  230 166  HOH   HOH B . 
G 5 HOH   31  231 332  HOH   HOH B . 
G 5 HOH   32  232 75   HOH   HOH B . 
G 5 HOH   33  233 128  HOH   HOH B . 
G 5 HOH   34  234 60   HOH   HOH B . 
G 5 HOH   35  235 205  HOH   HOH B . 
G 5 HOH   36  236 127  HOH   HOH B . 
G 5 HOH   37  237 133  HOH   HOH B . 
G 5 HOH   38  238 1278 HOH   HOH B . 
G 5 HOH   39  239 325  HOH   HOH B . 
G 5 HOH   40  240 181  HOH   HOH B . 
G 5 HOH   41  241 272  HOH   HOH B . 
G 5 HOH   42  242 300  HOH   HOH B . 
G 5 HOH   43  243 1    HOH   HOH B . 
G 5 HOH   44  244 69   HOH   HOH B . 
G 5 HOH   45  245 110  HOH   HOH B . 
G 5 HOH   46  246 14   HOH   HOH B . 
G 5 HOH   47  247 9    HOH   HOH B . 
G 5 HOH   48  248 143  HOH   HOH B . 
G 5 HOH   49  249 30   HOH   HOH B . 
G 5 HOH   50  250 252  HOH   HOH B . 
G 5 HOH   51  251 129  HOH   HOH B . 
G 5 HOH   52  252 31   HOH   HOH B . 
G 5 HOH   53  253 144  HOH   HOH B . 
G 5 HOH   54  254 52   HOH   HOH B . 
G 5 HOH   55  255 41   HOH   HOH B . 
G 5 HOH   56  256 172  HOH   HOH B . 
G 5 HOH   57  257 231  HOH   HOH B . 
G 5 HOH   58  258 72   HOH   HOH B . 
G 5 HOH   59  259 10   HOH   HOH B . 
G 5 HOH   60  260 47   HOH   HOH B . 
G 5 HOH   61  261 221  HOH   HOH B . 
G 5 HOH   62  262 62   HOH   HOH B . 
G 5 HOH   63  263 150  HOH   HOH B . 
G 5 HOH   64  264 391  HOH   HOH B . 
G 5 HOH   65  265 103  HOH   HOH B . 
G 5 HOH   66  266 61   HOH   HOH B . 
G 5 HOH   67  267 271  HOH   HOH B . 
G 5 HOH   68  268 20   HOH   HOH B . 
G 5 HOH   69  269 117  HOH   HOH B . 
G 5 HOH   70  270 347  HOH   HOH B . 
G 5 HOH   71  271 302  HOH   HOH B . 
G 5 HOH   72  272 243  HOH   HOH B . 
G 5 HOH   73  273 1277 HOH   HOH B . 
G 5 HOH   74  274 84   HOH   HOH B . 
G 5 HOH   75  275 77   HOH   HOH B . 
G 5 HOH   76  276 11   HOH   HOH B . 
G 5 HOH   77  277 59   HOH   HOH B . 
G 5 HOH   78  278 114  HOH   HOH B . 
G 5 HOH   79  279 43   HOH   HOH B . 
G 5 HOH   80  280 175  HOH   HOH B . 
G 5 HOH   81  281 22   HOH   HOH B . 
G 5 HOH   82  282 242  HOH   HOH B . 
G 5 HOH   83  283 387  HOH   HOH B . 
G 5 HOH   84  284 147  HOH   HOH B . 
G 5 HOH   85  285 287  HOH   HOH B . 
G 5 HOH   86  286 235  HOH   HOH B . 
G 5 HOH   87  287 216  HOH   HOH B . 
G 5 HOH   88  288 106  HOH   HOH B . 
G 5 HOH   89  289 416  HOH   HOH B . 
G 5 HOH   90  290 1106 HOH   HOH B . 
G 5 HOH   91  291 13   HOH   HOH B . 
G 5 HOH   92  292 89   HOH   HOH B . 
G 5 HOH   93  293 88   HOH   HOH B . 
G 5 HOH   94  294 99   HOH   HOH B . 
G 5 HOH   95  295 160  HOH   HOH B . 
G 5 HOH   96  296 137  HOH   HOH B . 
G 5 HOH   97  297 1066 HOH   HOH B . 
G 5 HOH   98  298 297  HOH   HOH B . 
G 5 HOH   99  299 316  HOH   HOH B . 
G 5 HOH   100 300 112  HOH   HOH B . 
G 5 HOH   101 301 311  HOH   HOH B . 
G 5 HOH   102 302 142  HOH   HOH B . 
G 5 HOH   103 303 299  HOH   HOH B . 
G 5 HOH   104 304 32   HOH   HOH B . 
G 5 HOH   105 305 1305 HOH   HOH B . 
G 5 HOH   106 306 38   HOH   HOH B . 
G 5 HOH   107 307 141  HOH   HOH B . 
G 5 HOH   108 308 220  HOH   HOH B . 
G 5 HOH   109 309 635  HOH   HOH B . 
G 5 HOH   110 310 341  HOH   HOH B . 
G 5 HOH   111 311 101  HOH   HOH B . 
G 5 HOH   112 312 215  HOH   HOH B . 
G 5 HOH   113 313 91   HOH   HOH B . 
G 5 HOH   114 314 48   HOH   HOH B . 
G 5 HOH   115 315 37   HOH   HOH B . 
G 5 HOH   116 316 704  HOH   HOH B . 
G 5 HOH   117 317 1291 HOH   HOH B . 
G 5 HOH   118 318 170  HOH   HOH B . 
G 5 HOH   119 319 118  HOH   HOH B . 
G 5 HOH   120 320 177  HOH   HOH B . 
G 5 HOH   121 321 28   HOH   HOH B . 
G 5 HOH   122 322 23   HOH   HOH B . 
G 5 HOH   123 323 100  HOH   HOH B . 
G 5 HOH   124 324 1285 HOH   HOH B . 
G 5 HOH   125 325 1126 HOH   HOH B . 
G 5 HOH   126 326 44   HOH   HOH B . 
G 5 HOH   127 327 1274 HOH   HOH B . 
G 5 HOH   128 328 161  HOH   HOH B . 
G 5 HOH   129 329 197  HOH   HOH B . 
G 5 HOH   130 330 334  HOH   HOH B . 
G 5 HOH   131 331 29   HOH   HOH B . 
G 5 HOH   132 332 182  HOH   HOH B . 
G 5 HOH   133 333 55   HOH   HOH B . 
G 5 HOH   134 334 717  HOH   HOH B . 
G 5 HOH   135 335 98   HOH   HOH B . 
G 5 HOH   136 336 1294 HOH   HOH B . 
G 5 HOH   137 337 445  HOH   HOH B . 
G 5 HOH   138 338 207  HOH   HOH B . 
G 5 HOH   139 339 65   HOH   HOH B . 
G 5 HOH   140 340 619  HOH   HOH B . 
G 5 HOH   141 341 234  HOH   HOH B . 
G 5 HOH   142 342 1293 HOH   HOH B . 
G 5 HOH   143 343 339  HOH   HOH B . 
G 5 HOH   144 344 960  HOH   HOH B . 
G 5 HOH   145 345 362  HOH   HOH B . 
G 5 HOH   146 346 90   HOH   HOH B . 
G 5 HOH   147 347 463  HOH   HOH B . 
G 5 HOH   148 348 178  HOH   HOH B . 
G 5 HOH   149 349 1304 HOH   HOH B . 
G 5 HOH   150 350 191  HOH   HOH B . 
G 5 HOH   151 351 623  HOH   HOH B . 
G 5 HOH   152 352 335  HOH   HOH B . 
G 5 HOH   153 353 304  HOH   HOH B . 
G 5 HOH   154 354 1046 HOH   HOH B . 
G 5 HOH   155 355 1280 HOH   HOH B . 
G 5 HOH   156 356 203  HOH   HOH B . 
G 5 HOH   157 357 541  HOH   HOH B . 
G 5 HOH   158 358 290  HOH   HOH B . 
G 5 HOH   159 359 87   HOH   HOH B . 
G 5 HOH   160 360 479  HOH   HOH B . 
G 5 HOH   161 361 389  HOH   HOH B . 
G 5 HOH   162 362 1077 HOH   HOH B . 
G 5 HOH   163 363 718  HOH   HOH B . 
G 5 HOH   164 364 283  HOH   HOH B . 
G 5 HOH   165 365 1072 HOH   HOH B . 
G 5 HOH   166 366 373  HOH   HOH B . 
G 5 HOH   167 367 898  HOH   HOH B . 
G 5 HOH   168 368 1316 HOH   HOH B . 
G 5 HOH   169 369 291  HOH   HOH B . 
G 5 HOH   170 370 340  HOH   HOH B . 
G 5 HOH   171 371 1303 HOH   HOH B . 
G 5 HOH   172 372 615  HOH   HOH B . 
G 5 HOH   173 373 667  HOH   HOH B . 
G 5 HOH   174 374 190  HOH   HOH B . 
G 5 HOH   175 375 310  HOH   HOH B . 
G 5 HOH   176 376 431  HOH   HOH B . 
G 5 HOH   177 377 149  HOH   HOH B . 
G 5 HOH   178 378 1163 HOH   HOH B . 
G 5 HOH   179 379 1173 HOH   HOH B . 
G 5 HOH   180 380 183  HOH   HOH B . 
G 5 HOH   181 381 418  HOH   HOH B . 
G 5 HOH   182 382 1000 HOH   HOH B . 
G 5 HOH   183 383 176  HOH   HOH B . 
G 5 HOH   184 384 1311 HOH   HOH B . 
G 5 HOH   185 385 1298 HOH   HOH B . 
G 5 HOH   186 386 424  HOH   HOH B . 
G 5 HOH   187 387 491  HOH   HOH B . 
G 5 HOH   188 388 248  HOH   HOH B . 
G 5 HOH   189 389 265  HOH   HOH B . 
G 5 HOH   190 390 470  HOH   HOH B . 
G 5 HOH   191 391 184  HOH   HOH B . 
G 5 HOH   192 392 360  HOH   HOH B . 
G 5 HOH   193 393 410  HOH   HOH B . 
G 5 HOH   194 394 355  HOH   HOH B . 
G 5 HOH   195 395 566  HOH   HOH B . 
G 5 HOH   196 396 314  HOH   HOH B . 
G 5 HOH   197 397 274  HOH   HOH B . 
G 5 HOH   198 398 157  HOH   HOH B . 
G 5 HOH   199 399 792  HOH   HOH B . 
G 5 HOH   200 400 321  HOH   HOH B . 
G 5 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HEV 
_cell.length_a           88.716 
_cell.length_b           88.716 
_cell.length_c           39.527 
_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                         7HEV 
_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          7HEV 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.61 
_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                     7HEV 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.360 
_reflns.d_resolution_high            0.980 
_reflns.number_obs                   174590 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.100 
_reflns.pdbx_Rmerge_I_obs            0.034 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        19.100 
_reflns.B_iso_Wilson_estimate        11.650 
_reflns.pdbx_redundancy              6.300 
_reflns.pdbx_Rrim_I_all              0.037 
_reflns.pdbx_Rpim_I_all              0.015 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1092342 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 0.980 1.000  ? 27336 7645 ? 1.195 ? ? ? 3.600 ? 0.800  ? ? ? ? ? ? 88.300 1.398 0.705 0.515 
1 2 5.370 44.360 ? 8019  1164 ? 0.022 ? ? ? 6.900 ? 77.500 ? ? ? ? ? ? 99.700 0.024 0.009 1.000 
# 
_refine.entry_id                                 7HEV 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9800 
_refine.ls_d_res_low                             36.1100 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.0000 
_refine.ls_number_reflns_obs                     174501 
_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                          0.1433 
_refine.ls_R_factor_R_work                       0.1427 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1557 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  8417 
_refine.ls_number_reflns_R_work                  166084 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.1726 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1300 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                67.360 
_refine.B_iso_min                                8.280 
_refine.pdbx_overall_phase_error                 17.7200 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       0.9800 
_refine_hist.d_res_low                        36.1100 
_refine_hist.pdbx_number_atoms_ligand         71 
_refine_hist.number_atoms_solvent             426 
_refine_hist.number_atoms_total               3039 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           15.00 
_refine_hist.pdbx_B_iso_mean_solvent          29.45 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
0.9800 0.9900  30 86.0000  4811 . 0.4392 0.4340 . 256 0.0000 5067 . 'X-RAY DIFFRACTION' 
0.9900 1.0000  30 92.0000  5066 . 0.3826 0.3765 . 260 0.0000 5326 . 'X-RAY DIFFRACTION' 
1.0000 1.0200  30 95.0000  5277 . 0.3403 0.3151 . 256 0.0000 5533 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 98.0000  5501 . 0.2808 0.3039 . 246 0.0000 5747 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5568 . 0.2487 0.2490 . 305 0.0000 5873 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 5513 . 0.2054 0.1975 . 303 0.0000 5816 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 5554 . 0.1875 0.1969 . 307 0.0000 5861 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 100.0000 5531 . 0.1673 0.1859 . 257 0.0000 5788 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 100.0000 5605 . 0.1540 0.1656 . 286 0.0000 5891 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5571 . 0.1430 0.1632 . 288 0.0000 5859 . 'X-RAY DIFFRACTION' 
1.1200 1.1400  30 100.0000 5606 . 0.1427 0.1682 . 246 0.0000 5852 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5581 . 0.1364 0.1482 . 270 0.0000 5851 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 5557 . 0.1346 0.1526 . 287 0.0000 5844 . 'X-RAY DIFFRACTION' 
1.1800 1.2100  30 100.0000 5500 . 0.1320 0.1655 . 317 0.0000 5817 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5655 . 0.1275 0.1599 . 235 0.0000 5890 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5573 . 0.1264 0.1442 . 283 0.0000 5856 . 'X-RAY DIFFRACTION' 
1.2600 1.3000  30 100.0000 5541 . 0.1241 0.1383 . 288 0.0000 5829 . 'X-RAY DIFFRACTION' 
1.3000 1.3300  30 100.0000 5565 . 0.1198 0.1428 . 304 0.0000 5869 . 'X-RAY DIFFRACTION' 
1.3300 1.3700  30 100.0000 5595 . 0.1226 0.1458 . 298 0.0000 5893 . 'X-RAY DIFFRACTION' 
1.3700 1.4100  30 100.0000 5625 . 0.1182 0.1499 . 243 0.0000 5868 . 'X-RAY DIFFRACTION' 
1.4100 1.4600  30 100.0000 5551 . 0.1246 0.1297 . 306 0.0000 5857 . 'X-RAY DIFFRACTION' 
1.4600 1.5200  30 100.0000 5587 . 0.1243 0.1420 . 261 0.0000 5848 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 5612 . 0.1203 0.1334 . 309 0.0000 5921 . 'X-RAY DIFFRACTION' 
1.5900 1.6800  30 100.0000 5590 . 0.1192 0.1349 . 277 0.0000 5867 . 'X-RAY DIFFRACTION' 
1.6800 1.7800  30 100.0000 5626 . 0.1262 0.1392 . 262 0.0000 5888 . 'X-RAY DIFFRACTION' 
1.7800 1.9200  30 100.0000 5589 . 0.1320 0.1323 . 304 0.0000 5893 . 'X-RAY DIFFRACTION' 
1.9200 2.1100  30 100.0000 5645 . 0.1350 0.1424 . 284 0.0000 5929 . 'X-RAY DIFFRACTION' 
2.1100 2.4200  30 100.0000 5606 . 0.1346 0.1303 . 308 0.0000 5914 . 'X-RAY DIFFRACTION' 
2.4200 3.0400  30 100.0000 5692 . 0.1461 0.1667 . 292 0.0000 5984 . 'X-RAY DIFFRACTION' 
3.0400 36.1100 30 100.0000 5791 . 0.1474 0.1667 . 279 0.0000 6070 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HEV 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003696' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HEV 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HEV A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HEV 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 7HEV SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HEV MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HEV SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HEV MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F 
2 1 B,G       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O 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 ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HEV 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.59 
# 
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  ? ? 55.07 -133.39 
2 1 SER A 128 ? B 70.19 -6.71   
3 1 HIS B 86  ? ? 57.38 -127.85 
# 
_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 523 ? 5.91 . 
2 1 O ? A HOH 524 ? 6.04 . 
3 1 O ? A HOH 525 ? 7.60 . 
4 1 O ? B HOH 401 ? 6.19 . 
# 
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 
A1BAD N2   N  N N 1   
A1BAD C3   C  N N 2   
A1BAD C6   C  Y N 3   
A1BAD C9   C  Y N 4   
A1BAD C12  C  Y N 5   
A1BAD C14  C  Y N 6   
A1BAD C1   C  N N 7   
A1BAD C10  C  Y N 8   
A1BAD C11  C  Y N 9   
A1BAD C13  C  Y N 10  
A1BAD C2   C  N R 11  
A1BAD C4   C  Y N 12  
A1BAD C5   C  Y N 13  
A1BAD C7   C  Y N 14  
A1BAD C8   C  Y N 15  
A1BAD N1   N  Y N 16  
A1BAD N3   N  Y N 17  
A1BAD N4   N  Y N 18  
A1BAD N5   N  Y N 19  
A1BAD O1   O  N N 20  
A1BAD H11  H  N N 21  
A1BAD H5   H  N N 22  
A1BAD H6   H  N N 23  
A1BAD H8   H  N N 24  
A1BAD H14  H  N N 25  
A1BAD H3   H  N N 26  
A1BAD H4   H  N N 27  
A1BAD H12  H  N N 28  
A1BAD H13  H  N N 29  
A1BAD H1   H  N N 30  
A1BAD H7   H  N N 31  
A1BAD H9   H  N N 32  
A1BAD H10  H  N N 33  
A1BAD H15  H  N N 34  
A1BAD H2   H  N N 35  
A1BAE O1   O  N N 36  
A1BAE C1   C  N N 37  
A1BAE C2   C  N S 38  
A1BAE C3   C  N N 39  
A1BAE C4   C  Y N 40  
A1BAE C5   C  Y N 41  
A1BAE C6   C  Y N 42  
A1BAE C7   C  Y N 43  
A1BAE C8   C  Y N 44  
A1BAE C10  C  Y N 45  
A1BAE C11  C  Y N 46  
A1BAE C12  C  Y N 47  
A1BAE C13  C  Y N 48  
A1BAE C14  C  Y N 49  
A1BAE C9   C  Y N 50  
A1BAE N1   N  Y N 51  
A1BAE N2   N  N N 52  
A1BAE N3   N  Y N 53  
A1BAE N4   N  Y N 54  
A1BAE N5   N  Y N 55  
A1BAE H2   H  N N 56  
A1BAE H4   H  N N 57  
A1BAE H3   H  N N 58  
A1BAE H1   H  N N 59  
A1BAE H6   H  N N 60  
A1BAE H5   H  N N 61  
A1BAE H7   H  N N 62  
A1BAE H8   H  N N 63  
A1BAE H9   H  N N 64  
A1BAE H10  H  N N 65  
A1BAE H12  H  N N 66  
A1BAE H13  H  N N 67  
A1BAE H14  H  N N 68  
A1BAE H11  H  N N 69  
A1BAE H15  H  N N 70  
ALA   N    N  N N 71  
ALA   CA   C  N S 72  
ALA   C    C  N N 73  
ALA   O    O  N N 74  
ALA   CB   C  N N 75  
ALA   OXT  O  N N 76  
ALA   H    H  N N 77  
ALA   H2   H  N N 78  
ALA   HA   H  N N 79  
ALA   HB1  H  N N 80  
ALA   HB2  H  N N 81  
ALA   HB3  H  N N 82  
ALA   HXT  H  N N 83  
ARG   N    N  N N 84  
ARG   CA   C  N S 85  
ARG   C    C  N N 86  
ARG   O    O  N N 87  
ARG   CB   C  N N 88  
ARG   CG   C  N N 89  
ARG   CD   C  N N 90  
ARG   NE   N  N N 91  
ARG   CZ   C  N N 92  
ARG   NH1  N  N N 93  
ARG   NH2  N  N N 94  
ARG   OXT  O  N N 95  
ARG   H    H  N N 96  
ARG   H2   H  N N 97  
ARG   HA   H  N N 98  
ARG   HB2  H  N N 99  
ARG   HB3  H  N N 100 
ARG   HG2  H  N N 101 
ARG   HG3  H  N N 102 
ARG   HD2  H  N N 103 
ARG   HD3  H  N N 104 
ARG   HE   H  N N 105 
ARG   HH11 H  N N 106 
ARG   HH12 H  N N 107 
ARG   HH21 H  N N 108 
ARG   HH22 H  N N 109 
ARG   HXT  H  N N 110 
ASN   N    N  N N 111 
ASN   CA   C  N S 112 
ASN   C    C  N N 113 
ASN   O    O  N N 114 
ASN   CB   C  N N 115 
ASN   CG   C  N N 116 
ASN   OD1  O  N N 117 
ASN   ND2  N  N N 118 
ASN   OXT  O  N N 119 
ASN   H    H  N N 120 
ASN   H2   H  N N 121 
ASN   HA   H  N N 122 
ASN   HB2  H  N N 123 
ASN   HB3  H  N N 124 
ASN   HD21 H  N N 125 
ASN   HD22 H  N N 126 
ASN   HXT  H  N N 127 
ASP   N    N  N N 128 
ASP   CA   C  N S 129 
ASP   C    C  N N 130 
ASP   O    O  N N 131 
ASP   CB   C  N N 132 
ASP   CG   C  N N 133 
ASP   OD1  O  N N 134 
ASP   OD2  O  N N 135 
ASP   OXT  O  N N 136 
ASP   H    H  N N 137 
ASP   H2   H  N N 138 
ASP   HA   H  N N 139 
ASP   HB2  H  N N 140 
ASP   HB3  H  N N 141 
ASP   HD2  H  N N 142 
ASP   HXT  H  N N 143 
CL    CL   CL N N 144 
CYS   N    N  N N 145 
CYS   CA   C  N R 146 
CYS   C    C  N N 147 
CYS   O    O  N N 148 
CYS   CB   C  N N 149 
CYS   SG   S  N N 150 
CYS   OXT  O  N N 151 
CYS   H    H  N N 152 
CYS   H2   H  N N 153 
CYS   HA   H  N N 154 
CYS   HB2  H  N N 155 
CYS   HB3  H  N N 156 
CYS   HG   H  N N 157 
CYS   HXT  H  N N 158 
GLN   N    N  N N 159 
GLN   CA   C  N S 160 
GLN   C    C  N N 161 
GLN   O    O  N N 162 
GLN   CB   C  N N 163 
GLN   CG   C  N N 164 
GLN   CD   C  N N 165 
GLN   OE1  O  N N 166 
GLN   NE2  N  N N 167 
GLN   OXT  O  N N 168 
GLN   H    H  N N 169 
GLN   H2   H  N N 170 
GLN   HA   H  N N 171 
GLN   HB2  H  N N 172 
GLN   HB3  H  N N 173 
GLN   HG2  H  N N 174 
GLN   HG3  H  N N 175 
GLN   HE21 H  N N 176 
GLN   HE22 H  N N 177 
GLN   HXT  H  N N 178 
GLU   N    N  N N 179 
GLU   CA   C  N S 180 
GLU   C    C  N N 181 
GLU   O    O  N N 182 
GLU   CB   C  N N 183 
GLU   CG   C  N N 184 
GLU   CD   C  N N 185 
GLU   OE1  O  N N 186 
GLU   OE2  O  N N 187 
GLU   OXT  O  N N 188 
GLU   H    H  N N 189 
GLU   H2   H  N N 190 
GLU   HA   H  N N 191 
GLU   HB2  H  N N 192 
GLU   HB3  H  N N 193 
GLU   HG2  H  N N 194 
GLU   HG3  H  N N 195 
GLU   HE2  H  N N 196 
GLU   HXT  H  N N 197 
GLY   N    N  N N 198 
GLY   CA   C  N N 199 
GLY   C    C  N N 200 
GLY   O    O  N N 201 
GLY   OXT  O  N N 202 
GLY   H    H  N N 203 
GLY   H2   H  N N 204 
GLY   HA2  H  N N 205 
GLY   HA3  H  N N 206 
GLY   HXT  H  N N 207 
HIS   N    N  N N 208 
HIS   CA   C  N S 209 
HIS   C    C  N N 210 
HIS   O    O  N N 211 
HIS   CB   C  N N 212 
HIS   CG   C  Y N 213 
HIS   ND1  N  Y N 214 
HIS   CD2  C  Y N 215 
HIS   CE1  C  Y N 216 
HIS   NE2  N  Y N 217 
HIS   OXT  O  N N 218 
HIS   H    H  N N 219 
HIS   H2   H  N N 220 
HIS   HA   H  N N 221 
HIS   HB2  H  N N 222 
HIS   HB3  H  N N 223 
HIS   HD1  H  N N 224 
HIS   HD2  H  N N 225 
HIS   HE1  H  N N 226 
HIS   HE2  H  N N 227 
HIS   HXT  H  N N 228 
HOH   O    O  N N 229 
HOH   H1   H  N N 230 
HOH   H2   H  N N 231 
ILE   N    N  N N 232 
ILE   CA   C  N S 233 
ILE   C    C  N N 234 
ILE   O    O  N N 235 
ILE   CB   C  N S 236 
ILE   CG1  C  N N 237 
ILE   CG2  C  N N 238 
ILE   CD1  C  N N 239 
ILE   OXT  O  N N 240 
ILE   H    H  N N 241 
ILE   H2   H  N N 242 
ILE   HA   H  N N 243 
ILE   HB   H  N N 244 
ILE   HG12 H  N N 245 
ILE   HG13 H  N N 246 
ILE   HG21 H  N N 247 
ILE   HG22 H  N N 248 
ILE   HG23 H  N N 249 
ILE   HD11 H  N N 250 
ILE   HD12 H  N N 251 
ILE   HD13 H  N N 252 
ILE   HXT  H  N N 253 
LEU   N    N  N N 254 
LEU   CA   C  N S 255 
LEU   C    C  N N 256 
LEU   O    O  N N 257 
LEU   CB   C  N N 258 
LEU   CG   C  N N 259 
LEU   CD1  C  N N 260 
LEU   CD2  C  N N 261 
LEU   OXT  O  N N 262 
LEU   H    H  N N 263 
LEU   H2   H  N N 264 
LEU   HA   H  N N 265 
LEU   HB2  H  N N 266 
LEU   HB3  H  N N 267 
LEU   HG   H  N N 268 
LEU   HD11 H  N N 269 
LEU   HD12 H  N N 270 
LEU   HD13 H  N N 271 
LEU   HD21 H  N N 272 
LEU   HD22 H  N N 273 
LEU   HD23 H  N N 274 
LEU   HXT  H  N N 275 
LYS   N    N  N N 276 
LYS   CA   C  N S 277 
LYS   C    C  N N 278 
LYS   O    O  N N 279 
LYS   CB   C  N N 280 
LYS   CG   C  N N 281 
LYS   CD   C  N N 282 
LYS   CE   C  N N 283 
LYS   NZ   N  N N 284 
LYS   OXT  O  N N 285 
LYS   H    H  N N 286 
LYS   H2   H  N N 287 
LYS   HA   H  N N 288 
LYS   HB2  H  N N 289 
LYS   HB3  H  N N 290 
LYS   HG2  H  N N 291 
LYS   HG3  H  N N 292 
LYS   HD2  H  N N 293 
LYS   HD3  H  N N 294 
LYS   HE2  H  N N 295 
LYS   HE3  H  N N 296 
LYS   HZ1  H  N N 297 
LYS   HZ2  H  N N 298 
LYS   HZ3  H  N N 299 
LYS   HXT  H  N N 300 
MET   N    N  N N 301 
MET   CA   C  N S 302 
MET   C    C  N N 303 
MET   O    O  N N 304 
MET   CB   C  N N 305 
MET   CG   C  N N 306 
MET   SD   S  N N 307 
MET   CE   C  N N 308 
MET   OXT  O  N N 309 
MET   H    H  N N 310 
MET   H2   H  N N 311 
MET   HA   H  N N 312 
MET   HB2  H  N N 313 
MET   HB3  H  N N 314 
MET   HG2  H  N N 315 
MET   HG3  H  N N 316 
MET   HE1  H  N N 317 
MET   HE2  H  N N 318 
MET   HE3  H  N N 319 
MET   HXT  H  N N 320 
PHE   N    N  N N 321 
PHE   CA   C  N S 322 
PHE   C    C  N N 323 
PHE   O    O  N N 324 
PHE   CB   C  N N 325 
PHE   CG   C  Y N 326 
PHE   CD1  C  Y N 327 
PHE   CD2  C  Y N 328 
PHE   CE1  C  Y N 329 
PHE   CE2  C  Y N 330 
PHE   CZ   C  Y N 331 
PHE   OXT  O  N N 332 
PHE   H    H  N N 333 
PHE   H2   H  N N 334 
PHE   HA   H  N N 335 
PHE   HB2  H  N N 336 
PHE   HB3  H  N N 337 
PHE   HD1  H  N N 338 
PHE   HD2  H  N N 339 
PHE   HE1  H  N N 340 
PHE   HE2  H  N N 341 
PHE   HZ   H  N N 342 
PHE   HXT  H  N N 343 
PRO   N    N  N N 344 
PRO   CA   C  N S 345 
PRO   C    C  N N 346 
PRO   O    O  N N 347 
PRO   CB   C  N N 348 
PRO   CG   C  N N 349 
PRO   CD   C  N N 350 
PRO   OXT  O  N N 351 
PRO   H    H  N N 352 
PRO   HA   H  N N 353 
PRO   HB2  H  N N 354 
PRO   HB3  H  N N 355 
PRO   HG2  H  N N 356 
PRO   HG3  H  N N 357 
PRO   HD2  H  N N 358 
PRO   HD3  H  N N 359 
PRO   HXT  H  N N 360 
SER   N    N  N N 361 
SER   CA   C  N S 362 
SER   C    C  N N 363 
SER   O    O  N N 364 
SER   CB   C  N N 365 
SER   OG   O  N N 366 
SER   OXT  O  N N 367 
SER   H    H  N N 368 
SER   H2   H  N N 369 
SER   HA   H  N N 370 
SER   HB2  H  N N 371 
SER   HB3  H  N N 372 
SER   HG   H  N N 373 
SER   HXT  H  N N 374 
THR   N    N  N N 375 
THR   CA   C  N S 376 
THR   C    C  N N 377 
THR   O    O  N N 378 
THR   CB   C  N R 379 
THR   OG1  O  N N 380 
THR   CG2  C  N N 381 
THR   OXT  O  N N 382 
THR   H    H  N N 383 
THR   H2   H  N N 384 
THR   HA   H  N N 385 
THR   HB   H  N N 386 
THR   HG1  H  N N 387 
THR   HG21 H  N N 388 
THR   HG22 H  N N 389 
THR   HG23 H  N N 390 
THR   HXT  H  N N 391 
TYR   N    N  N N 392 
TYR   CA   C  N S 393 
TYR   C    C  N N 394 
TYR   O    O  N N 395 
TYR   CB   C  N N 396 
TYR   CG   C  Y N 397 
TYR   CD1  C  Y N 398 
TYR   CD2  C  Y N 399 
TYR   CE1  C  Y N 400 
TYR   CE2  C  Y N 401 
TYR   CZ   C  Y N 402 
TYR   OH   O  N N 403 
TYR   OXT  O  N N 404 
TYR   H    H  N N 405 
TYR   H2   H  N N 406 
TYR   HA   H  N N 407 
TYR   HB2  H  N N 408 
TYR   HB3  H  N N 409 
TYR   HD1  H  N N 410 
TYR   HD2  H  N N 411 
TYR   HE1  H  N N 412 
TYR   HE2  H  N N 413 
TYR   HH   H  N N 414 
TYR   HXT  H  N N 415 
VAL   N    N  N N 416 
VAL   CA   C  N S 417 
VAL   C    C  N N 418 
VAL   O    O  N N 419 
VAL   CB   C  N N 420 
VAL   CG1  C  N N 421 
VAL   CG2  C  N N 422 
VAL   OXT  O  N N 423 
VAL   H    H  N N 424 
VAL   H2   H  N N 425 
VAL   HA   H  N N 426 
VAL   HB   H  N N 427 
VAL   HG11 H  N N 428 
VAL   HG12 H  N N 429 
VAL   HG13 H  N N 430 
VAL   HG21 H  N N 431 
VAL   HG22 H  N N 432 
VAL   HG23 H  N N 433 
VAL   HXT  H  N N 434 
# 
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 
A1BAD C8  N1   doub Y N 1   
A1BAD C8  C7   sing Y N 2   
A1BAD N1  C4   sing Y N 3   
A1BAD C7  C6   doub Y N 4   
A1BAD C4  C3   sing N N 5   
A1BAD C4  C5   doub Y N 6   
A1BAD O1  C1   sing N N 7   
A1BAD C6  C5   sing Y N 8   
A1BAD C3  C2   sing N N 9   
A1BAD C2  C1   sing N N 10  
A1BAD C2  N2   sing N N 11  
A1BAD N2  C9   sing N N 12  
A1BAD C9  N3   doub Y N 13  
A1BAD C9  C12  sing Y N 14  
A1BAD C13 C12  sing Y N 15  
A1BAD C13 C14  doub Y N 16  
A1BAD N3  C10  sing Y N 17  
A1BAD C12 C11  doub Y N 18  
A1BAD C14 N5   sing Y N 19  
A1BAD C10 N4   doub Y N 20  
A1BAD C11 N5   sing Y N 21  
A1BAD C11 N4   sing Y N 22  
A1BAD N2  H11  sing N N 23  
A1BAD C3  H5   sing N N 24  
A1BAD C3  H6   sing N N 25  
A1BAD C6  H8   sing N N 26  
A1BAD C14 H14  sing N N 27  
A1BAD C1  H3   sing N N 28  
A1BAD C1  H4   sing N N 29  
A1BAD C10 H12  sing N N 30  
A1BAD C13 H13  sing N N 31  
A1BAD C2  H1   sing N N 32  
A1BAD C5  H7   sing N N 33  
A1BAD C7  H9   sing N N 34  
A1BAD C8  H10  sing N N 35  
A1BAD N5  H15  sing N N 36  
A1BAD O1  H2   sing N N 37  
A1BAE C8  N1   doub Y N 38  
A1BAE C8  C7   sing Y N 39  
A1BAE N1  C4   sing Y N 40  
A1BAE C7  C6   doub Y N 41  
A1BAE C4  C3   sing N N 42  
A1BAE C4  C5   doub Y N 43  
A1BAE C3  C2   sing N N 44  
A1BAE O1  C1   sing N N 45  
A1BAE C6  C5   sing Y N 46  
A1BAE C1  C2   sing N N 47  
A1BAE C2  N2   sing N N 48  
A1BAE N2  C9   sing N N 49  
A1BAE C9  C12  doub Y N 50  
A1BAE C9  N3   sing Y N 51  
A1BAE C13 C12  sing Y N 52  
A1BAE C13 C14  doub Y N 53  
A1BAE C12 C11  sing Y N 54  
A1BAE N3  C10  doub Y N 55  
A1BAE C14 N5   sing Y N 56  
A1BAE C11 N5   sing Y N 57  
A1BAE C11 N4   doub Y N 58  
A1BAE C10 N4   sing Y N 59  
A1BAE O1  H2   sing N N 60  
A1BAE C1  H4   sing N N 61  
A1BAE C1  H3   sing N N 62  
A1BAE C2  H1   sing N N 63  
A1BAE C3  H6   sing N N 64  
A1BAE C3  H5   sing N N 65  
A1BAE C5  H7   sing N N 66  
A1BAE C6  H8   sing N N 67  
A1BAE C7  H9   sing N N 68  
A1BAE C8  H10  sing N N 69  
A1BAE C10 H12  sing N N 70  
A1BAE C13 H13  sing N N 71  
A1BAE C14 H14  sing N N 72  
A1BAE N2  H11  sing N N 73  
A1BAE N5  H15  sing N N 74  
ALA   N   CA   sing N N 75  
ALA   N   H    sing N N 76  
ALA   N   H2   sing N N 77  
ALA   CA  C    sing N N 78  
ALA   CA  CB   sing N N 79  
ALA   CA  HA   sing N N 80  
ALA   C   O    doub N N 81  
ALA   C   OXT  sing N N 82  
ALA   CB  HB1  sing N N 83  
ALA   CB  HB2  sing N N 84  
ALA   CB  HB3  sing N N 85  
ALA   OXT HXT  sing N N 86  
ARG   N   CA   sing N N 87  
ARG   N   H    sing N N 88  
ARG   N   H2   sing N N 89  
ARG   CA  C    sing N N 90  
ARG   CA  CB   sing N N 91  
ARG   CA  HA   sing N N 92  
ARG   C   O    doub N N 93  
ARG   C   OXT  sing N N 94  
ARG   CB  CG   sing N N 95  
ARG   CB  HB2  sing N N 96  
ARG   CB  HB3  sing N N 97  
ARG   CG  CD   sing N N 98  
ARG   CG  HG2  sing N N 99  
ARG   CG  HG3  sing N N 100 
ARG   CD  NE   sing N N 101 
ARG   CD  HD2  sing N N 102 
ARG   CD  HD3  sing N N 103 
ARG   NE  CZ   sing N N 104 
ARG   NE  HE   sing N N 105 
ARG   CZ  NH1  sing N N 106 
ARG   CZ  NH2  doub N N 107 
ARG   NH1 HH11 sing N N 108 
ARG   NH1 HH12 sing N N 109 
ARG   NH2 HH21 sing N N 110 
ARG   NH2 HH22 sing N N 111 
ARG   OXT HXT  sing N N 112 
ASN   N   CA   sing N N 113 
ASN   N   H    sing N N 114 
ASN   N   H2   sing N N 115 
ASN   CA  C    sing N N 116 
ASN   CA  CB   sing N N 117 
ASN   CA  HA   sing N N 118 
ASN   C   O    doub N N 119 
ASN   C   OXT  sing N N 120 
ASN   CB  CG   sing N N 121 
ASN   CB  HB2  sing N N 122 
ASN   CB  HB3  sing N N 123 
ASN   CG  OD1  doub N N 124 
ASN   CG  ND2  sing N N 125 
ASN   ND2 HD21 sing N N 126 
ASN   ND2 HD22 sing N N 127 
ASN   OXT HXT  sing N N 128 
ASP   N   CA   sing N N 129 
ASP   N   H    sing N N 130 
ASP   N   H2   sing N N 131 
ASP   CA  C    sing N N 132 
ASP   CA  CB   sing N N 133 
ASP   CA  HA   sing N N 134 
ASP   C   O    doub N N 135 
ASP   C   OXT  sing N N 136 
ASP   CB  CG   sing N N 137 
ASP   CB  HB2  sing N N 138 
ASP   CB  HB3  sing N N 139 
ASP   CG  OD1  doub N N 140 
ASP   CG  OD2  sing N N 141 
ASP   OD2 HD2  sing N N 142 
ASP   OXT HXT  sing N N 143 
CYS   N   CA   sing N N 144 
CYS   N   H    sing N N 145 
CYS   N   H2   sing N N 146 
CYS   CA  C    sing N N 147 
CYS   CA  CB   sing N N 148 
CYS   CA  HA   sing N N 149 
CYS   C   O    doub N N 150 
CYS   C   OXT  sing N N 151 
CYS   CB  SG   sing N N 152 
CYS   CB  HB2  sing N N 153 
CYS   CB  HB3  sing N N 154 
CYS   SG  HG   sing N N 155 
CYS   OXT HXT  sing N N 156 
GLN   N   CA   sing N N 157 
GLN   N   H    sing N N 158 
GLN   N   H2   sing N N 159 
GLN   CA  C    sing N N 160 
GLN   CA  CB   sing N N 161 
GLN   CA  HA   sing N N 162 
GLN   C   O    doub N N 163 
GLN   C   OXT  sing N N 164 
GLN   CB  CG   sing N N 165 
GLN   CB  HB2  sing N N 166 
GLN   CB  HB3  sing N N 167 
GLN   CG  CD   sing N N 168 
GLN   CG  HG2  sing N N 169 
GLN   CG  HG3  sing N N 170 
GLN   CD  OE1  doub N N 171 
GLN   CD  NE2  sing N N 172 
GLN   NE2 HE21 sing N N 173 
GLN   NE2 HE22 sing N N 174 
GLN   OXT HXT  sing N N 175 
GLU   N   CA   sing N N 176 
GLU   N   H    sing N N 177 
GLU   N   H2   sing N N 178 
GLU   CA  C    sing N N 179 
GLU   CA  CB   sing N N 180 
GLU   CA  HA   sing N N 181 
GLU   C   O    doub N N 182 
GLU   C   OXT  sing N N 183 
GLU   CB  CG   sing N N 184 
GLU   CB  HB2  sing N N 185 
GLU   CB  HB3  sing N N 186 
GLU   CG  CD   sing N N 187 
GLU   CG  HG2  sing N N 188 
GLU   CG  HG3  sing N N 189 
GLU   CD  OE1  doub N N 190 
GLU   CD  OE2  sing N N 191 
GLU   OE2 HE2  sing N N 192 
GLU   OXT HXT  sing N N 193 
GLY   N   CA   sing N N 194 
GLY   N   H    sing N N 195 
GLY   N   H2   sing N N 196 
GLY   CA  C    sing N N 197 
GLY   CA  HA2  sing N N 198 
GLY   CA  HA3  sing N N 199 
GLY   C   O    doub N N 200 
GLY   C   OXT  sing N N 201 
GLY   OXT HXT  sing N N 202 
HIS   N   CA   sing N N 203 
HIS   N   H    sing N N 204 
HIS   N   H2   sing N N 205 
HIS   CA  C    sing N N 206 
HIS   CA  CB   sing N N 207 
HIS   CA  HA   sing N N 208 
HIS   C   O    doub N N 209 
HIS   C   OXT  sing N N 210 
HIS   CB  CG   sing N N 211 
HIS   CB  HB2  sing N N 212 
HIS   CB  HB3  sing N N 213 
HIS   CG  ND1  sing Y N 214 
HIS   CG  CD2  doub Y N 215 
HIS   ND1 CE1  doub Y N 216 
HIS   ND1 HD1  sing N N 217 
HIS   CD2 NE2  sing Y N 218 
HIS   CD2 HD2  sing N N 219 
HIS   CE1 NE2  sing Y N 220 
HIS   CE1 HE1  sing N N 221 
HIS   NE2 HE2  sing N N 222 
HIS   OXT HXT  sing N N 223 
HOH   O   H1   sing N N 224 
HOH   O   H2   sing N N 225 
ILE   N   CA   sing N N 226 
ILE   N   H    sing N N 227 
ILE   N   H2   sing N N 228 
ILE   CA  C    sing N N 229 
ILE   CA  CB   sing N N 230 
ILE   CA  HA   sing N N 231 
ILE   C   O    doub N N 232 
ILE   C   OXT  sing N N 233 
ILE   CB  CG1  sing N N 234 
ILE   CB  CG2  sing N N 235 
ILE   CB  HB   sing N N 236 
ILE   CG1 CD1  sing N N 237 
ILE   CG1 HG12 sing N N 238 
ILE   CG1 HG13 sing N N 239 
ILE   CG2 HG21 sing N N 240 
ILE   CG2 HG22 sing N N 241 
ILE   CG2 HG23 sing N N 242 
ILE   CD1 HD11 sing N N 243 
ILE   CD1 HD12 sing N N 244 
ILE   CD1 HD13 sing N N 245 
ILE   OXT HXT  sing N N 246 
LEU   N   CA   sing N N 247 
LEU   N   H    sing N N 248 
LEU   N   H2   sing N N 249 
LEU   CA  C    sing N N 250 
LEU   CA  CB   sing N N 251 
LEU   CA  HA   sing N N 252 
LEU   C   O    doub N N 253 
LEU   C   OXT  sing N N 254 
LEU   CB  CG   sing N N 255 
LEU   CB  HB2  sing N N 256 
LEU   CB  HB3  sing N N 257 
LEU   CG  CD1  sing N N 258 
LEU   CG  CD2  sing N N 259 
LEU   CG  HG   sing N N 260 
LEU   CD1 HD11 sing N N 261 
LEU   CD1 HD12 sing N N 262 
LEU   CD1 HD13 sing N N 263 
LEU   CD2 HD21 sing N N 264 
LEU   CD2 HD22 sing N N 265 
LEU   CD2 HD23 sing N N 266 
LEU   OXT HXT  sing N N 267 
LYS   N   CA   sing N N 268 
LYS   N   H    sing N N 269 
LYS   N   H2   sing N N 270 
LYS   CA  C    sing N N 271 
LYS   CA  CB   sing N N 272 
LYS   CA  HA   sing N N 273 
LYS   C   O    doub N N 274 
LYS   C   OXT  sing N N 275 
LYS   CB  CG   sing N N 276 
LYS   CB  HB2  sing N N 277 
LYS   CB  HB3  sing N N 278 
LYS   CG  CD   sing N N 279 
LYS   CG  HG2  sing N N 280 
LYS   CG  HG3  sing N N 281 
LYS   CD  CE   sing N N 282 
LYS   CD  HD2  sing N N 283 
LYS   CD  HD3  sing N N 284 
LYS   CE  NZ   sing N N 285 
LYS   CE  HE2  sing N N 286 
LYS   CE  HE3  sing N N 287 
LYS   NZ  HZ1  sing N N 288 
LYS   NZ  HZ2  sing N N 289 
LYS   NZ  HZ3  sing N N 290 
LYS   OXT HXT  sing N N 291 
MET   N   CA   sing N N 292 
MET   N   H    sing N N 293 
MET   N   H2   sing N N 294 
MET   CA  C    sing N N 295 
MET   CA  CB   sing N N 296 
MET   CA  HA   sing N N 297 
MET   C   O    doub N N 298 
MET   C   OXT  sing N N 299 
MET   CB  CG   sing N N 300 
MET   CB  HB2  sing N N 301 
MET   CB  HB3  sing N N 302 
MET   CG  SD   sing N N 303 
MET   CG  HG2  sing N N 304 
MET   CG  HG3  sing N N 305 
MET   SD  CE   sing N N 306 
MET   CE  HE1  sing N N 307 
MET   CE  HE2  sing N N 308 
MET   CE  HE3  sing N N 309 
MET   OXT HXT  sing N N 310 
PHE   N   CA   sing N N 311 
PHE   N   H    sing N N 312 
PHE   N   H2   sing N N 313 
PHE   CA  C    sing N N 314 
PHE   CA  CB   sing N N 315 
PHE   CA  HA   sing N N 316 
PHE   C   O    doub N N 317 
PHE   C   OXT  sing N N 318 
PHE   CB  CG   sing N N 319 
PHE   CB  HB2  sing N N 320 
PHE   CB  HB3  sing N N 321 
PHE   CG  CD1  doub Y N 322 
PHE   CG  CD2  sing Y N 323 
PHE   CD1 CE1  sing Y N 324 
PHE   CD1 HD1  sing N N 325 
PHE   CD2 CE2  doub Y N 326 
PHE   CD2 HD2  sing N N 327 
PHE   CE1 CZ   doub Y N 328 
PHE   CE1 HE1  sing N N 329 
PHE   CE2 CZ   sing Y N 330 
PHE   CE2 HE2  sing N N 331 
PHE   CZ  HZ   sing N N 332 
PHE   OXT HXT  sing N N 333 
PRO   N   CA   sing N N 334 
PRO   N   CD   sing N N 335 
PRO   N   H    sing N N 336 
PRO   CA  C    sing N N 337 
PRO   CA  CB   sing N N 338 
PRO   CA  HA   sing N N 339 
PRO   C   O    doub N N 340 
PRO   C   OXT  sing N N 341 
PRO   CB  CG   sing N N 342 
PRO   CB  HB2  sing N N 343 
PRO   CB  HB3  sing N N 344 
PRO   CG  CD   sing N N 345 
PRO   CG  HG2  sing N N 346 
PRO   CG  HG3  sing N N 347 
PRO   CD  HD2  sing N N 348 
PRO   CD  HD3  sing N N 349 
PRO   OXT HXT  sing N N 350 
SER   N   CA   sing N N 351 
SER   N   H    sing N N 352 
SER   N   H2   sing N N 353 
SER   CA  C    sing N N 354 
SER   CA  CB   sing N N 355 
SER   CA  HA   sing N N 356 
SER   C   O    doub N N 357 
SER   C   OXT  sing N N 358 
SER   CB  OG   sing N N 359 
SER   CB  HB2  sing N N 360 
SER   CB  HB3  sing N N 361 
SER   OG  HG   sing N N 362 
SER   OXT HXT  sing N N 363 
THR   N   CA   sing N N 364 
THR   N   H    sing N N 365 
THR   N   H2   sing N N 366 
THR   CA  C    sing N N 367 
THR   CA  CB   sing N N 368 
THR   CA  HA   sing N N 369 
THR   C   O    doub N N 370 
THR   C   OXT  sing N N 371 
THR   CB  OG1  sing N N 372 
THR   CB  CG2  sing N N 373 
THR   CB  HB   sing N N 374 
THR   OG1 HG1  sing N N 375 
THR   CG2 HG21 sing N N 376 
THR   CG2 HG22 sing N N 377 
THR   CG2 HG23 sing N N 378 
THR   OXT HXT  sing N N 379 
TYR   N   CA   sing N N 380 
TYR   N   H    sing N N 381 
TYR   N   H2   sing N N 382 
TYR   CA  C    sing N N 383 
TYR   CA  CB   sing N N 384 
TYR   CA  HA   sing N N 385 
TYR   C   O    doub N N 386 
TYR   C   OXT  sing N N 387 
TYR   CB  CG   sing N N 388 
TYR   CB  HB2  sing N N 389 
TYR   CB  HB3  sing N N 390 
TYR   CG  CD1  doub Y N 391 
TYR   CG  CD2  sing Y N 392 
TYR   CD1 CE1  sing Y N 393 
TYR   CD1 HD1  sing N N 394 
TYR   CD2 CE2  doub Y N 395 
TYR   CD2 HD2  sing N N 396 
TYR   CE1 CZ   doub Y N 397 
TYR   CE1 HE1  sing N N 398 
TYR   CE2 CZ   sing Y N 399 
TYR   CE2 HE2  sing N N 400 
TYR   CZ  OH   sing N N 401 
TYR   OH  HH   sing N N 402 
TYR   OXT HXT  sing N N 403 
VAL   N   CA   sing N N 404 
VAL   N   H    sing N N 405 
VAL   N   H2   sing N N 406 
VAL   CA  C    sing N N 407 
VAL   CA  CB   sing N N 408 
VAL   CA  HA   sing N N 409 
VAL   C   O    doub N N 410 
VAL   C   OXT  sing N N 411 
VAL   CB  CG1  sing N N 412 
VAL   CB  CG2  sing N N 413 
VAL   CB  HB   sing N N 414 
VAL   CG1 HG11 sing N N 415 
VAL   CG1 HG12 sing N N 416 
VAL   CG1 HG13 sing N N 417 
VAL   CG2 HG21 sing N N 418 
VAL   CG2 HG22 sing N N 419 
VAL   CG2 HG23 sing N N 420 
VAL   OXT HXT  sing N N 421 
# 
_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                    7HEV 
_atom_sites.fract_transf_matrix[1][1]   0.011272 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011272 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.025299 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    A VAL   A 1 3   ? 19.679 -16.227 22.273  0.60 52.52 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.614 -16.207 22.348  0.40 52.11 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.714 -15.148 22.445  0.60 52.26 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.678 -15.105 22.530  0.40 51.88 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.373 -13.802 22.164  0.60 51.03 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.354 -13.778 22.206  0.40 50.83 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.487 -13.538 22.619  0.60 51.37 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.462 -13.507 22.668  0.40 51.17 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.079 -15.184 23.850  0.60 53.01 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.093 -15.097 23.956  0.40 52.49 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.061 -14.062 24.006  0.60 53.20 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.107 -13.948 24.121  0.40 52.64 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.430 -16.537 24.106  0.60 53.18 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.424 -16.429 24.264  0.40 52.64 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.999 -15.262 21.803  0.60 62.69 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.939 -15.215 21.915  0.40 62.23 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.772 -15.055 24.516  0.60 63.59 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.811 -14.970 24.595  0.40 62.97 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.553 -14.208 24.820  0.60 63.82 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.619 -14.068 24.951  0.40 63.15 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.529 -13.214 24.057  0.60 63.82 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.596 -13.111 24.145  0.40 63.15 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.466 -14.068 23.240  0.60 63.82 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.490 -13.952 23.372  0.40 63.15 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.974 -16.512 24.962  0.60 63.79 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 16.997 -16.373 25.133  0.40 63.14 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.793 -16.720 23.397  0.60 63.79 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.761 -16.613 23.581  0.40 63.14 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.118 -17.221 24.118  0.60 63.79 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.097 -17.127 24.269  0.40 63.14 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.681 -12.956 21.403  1.00 49.20 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.149 -11.615 21.072  1.00 45.44 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 18.018 -10.620 21.317  1.00 41.84 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.901 -10.994 21.689  1.00 41.74 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.693 -11.531 19.639  1.00 44.85 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.668 -11.918 18.596  1.00 44.19 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.550 -11.402 18.583  1.00 44.05 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 19.046 -12.834 17.710  1.00 44.03 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.915 -13.146 21.059  0.60 59.01 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.931 -13.160 21.033  0.40 59.01 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.878 -11.388 21.666  1.00 54.50 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 19.971 -10.616 19.460  1.00 53.80 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.451 -12.128 19.552  1.00 53.80 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.503 -13.088 17.093  1.00 52.81 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.836 -13.173 17.753  1.00 52.81 ?  4   ASN   A HD22 1 
ATOM   46   N  N    . SER   A 1 5   ? 18.311 -9.338  21.098  1.00 37.97 ?  5   SER   A N    1 
ATOM   47   C  CA   . SER   A 1 5   ? 17.420 -8.255  21.494  1.00 33.79 ?  5   SER   A CA   1 
ATOM   48   C  C    . SER   A 1 5   ? 16.520 -7.761  20.365  1.00 28.76 ?  5   SER   A C    1 
ATOM   49   O  O    . SER   A 1 5   ? 15.835 -6.747  20.534  1.00 29.20 ?  5   SER   A O    1 
ATOM   50   C  CB   . SER   A 1 5   ? 18.223 -7.091  22.082  1.00 35.11 ?  5   SER   A CB   1 
ATOM   51   O  OG   . SER   A 1 5   ? 19.112 -6.544  21.124  1.00 35.57 ?  5   SER   A OG   1 
ATOM   52   H  H    . SER   A 1 5   ? 19.030 -9.071  20.707  1.00 45.54 ?  5   SER   A H    1 
ATOM   53   H  HA   . SER   A 1 5   ? 16.842 -8.580  22.197  1.00 40.52 ?  5   SER   A HA   1 
ATOM   54   H  HB2  . SER   A 1 5   ? 17.609 -6.398  22.374  1.00 42.11 ?  5   SER   A HB2  1 
ATOM   55   H  HB3  . SER   A 1 5   ? 18.739 -7.412  22.840  1.00 42.11 ?  5   SER   A HB3  1 
ATOM   56   H  HG   . SER   A 1 5   ? 19.545 -5.906  21.463  1.00 42.66 ?  5   SER   A HG   1 
ATOM   57   N  N    A PHE   A 1 6   ? 16.503 -8.455  19.228  0.60 25.10 ?  6   PHE   A N    1 
ATOM   58   N  N    B PHE   A 1 6   ? 16.499 -8.440  19.222  0.40 26.22 ?  6   PHE   A N    1 
ATOM   59   C  CA   A PHE   A 1 6   ? 15.599 -8.101  18.142  0.60 21.42 ?  6   PHE   A CA   1 
ATOM   60   C  CA   B PHE   A 1 6   ? 15.622 -8.016  18.137  0.40 23.62 ?  6   PHE   A CA   1 
ATOM   61   C  C    A PHE   A 1 6   ? 14.178 -8.514  18.503  0.60 21.01 ?  6   PHE   A C    1 
ATOM   62   C  C    B PHE   A 1 6   ? 14.164 -8.221  18.539  0.40 23.50 ?  6   PHE   A C    1 
ATOM   63   O  O    A PHE   A 1 6   ? 13.949 -9.632  18.970  0.60 21.88 ?  6   PHE   A O    1 
ATOM   64   O  O    B PHE   A 1 6   ? 13.789 -9.289  19.032  0.40 23.93 ?  6   PHE   A O    1 
ATOM   65   C  CB   A PHE   A 1 6   ? 16.025 -8.804  16.856  0.60 19.16 ?  6   PHE   A CB   1 
ATOM   66   C  CB   B PHE   A 1 6   ? 15.959 -8.784  16.861  0.40 21.81 ?  6   PHE   A CB   1 
ATOM   67   C  CG   A PHE   A 1 6   ? 17.276 -8.241  16.241  0.60 17.26 ?  6   PHE   A CG   1 
ATOM   68   C  CG   B PHE   A 1 6   ? 17.281 -8.389  16.252  0.40 20.33 ?  6   PHE   A CG   1 
ATOM   69   C  CD1  A PHE   A 1 6   ? 17.251 -7.025  15.580  0.60 16.51 ?  6   PHE   A CD1  1 
ATOM   70   C  CD1  B PHE   A 1 6   ? 17.377 -7.269  15.443  0.40 19.64 ?  6   PHE   A CD1  1 
ATOM   71   C  CD2  A PHE   A 1 6   ? 18.472 -8.936  16.313  0.60 17.18 ?  6   PHE   A CD2  1 
ATOM   72   C  CD2  B PHE   A 1 6   ? 18.425 -9.135  16.493  0.40 19.97 ?  6   PHE   A CD2  1 
ATOM   73   C  CE1  A PHE   A 1 6   ? 18.399 -6.508  15.010  0.60 16.60 ?  6   PHE   A CE1  1 
ATOM   74   C  CE1  B PHE   A 1 6   ? 18.589 -6.899  14.882  0.40 19.32 ?  6   PHE   A CE1  1 
ATOM   75   C  CE2  A PHE   A 1 6   ? 19.620 -8.428  15.746  0.60 17.08 ?  6   PHE   A CE2  1 
ATOM   76   C  CE2  B PHE   A 1 6   ? 19.639 -8.771  15.934  0.40 19.49 ?  6   PHE   A CE2  1 
ATOM   77   C  CZ   A PHE   A 1 6   ? 19.584 -7.212  15.092  0.60 16.84 ?  6   PHE   A CZ   1 
ATOM   78   C  CZ   B PHE   A 1 6   ? 19.720 -7.651  15.129  0.40 19.25 ?  6   PHE   A CZ   1 
ATOM   79   H  H    A PHE   A 1 6   ? 17.001 -9.137  19.067  0.60 30.10 ?  6   PHE   A H    1 
ATOM   80   H  H    B PHE   A 1 6   ? 16.975 -9.135  19.053  0.40 31.44 ?  6   PHE   A H    1 
ATOM   81   H  HA   A PHE   A 1 6   ? 15.615 -7.147  18.002  0.60 25.68 ?  6   PHE   A HA   1 
ATOM   82   H  HA   B PHE   A 1 6   ? 15.757 -7.073  17.973  0.40 28.32 ?  6   PHE   A HA   1 
ATOM   83   H  HB2  A PHE   A 1 6   ? 16.185 -9.742  17.052  0.60 22.97 ?  6   PHE   A HB2  1 
ATOM   84   H  HB2  B PHE   A 1 6   ? 15.994 -9.732  17.065  0.40 26.15 ?  6   PHE   A HB2  1 
ATOM   85   H  HB3  A PHE   A 1 6   ? 15.310 -8.723  16.207  0.60 22.97 ?  6   PHE   A HB3  1 
ATOM   86   H  HB3  B PHE   A 1 6   ? 15.265 -8.615  16.204  0.40 26.15 ?  6   PHE   A HB3  1 
ATOM   87   H  HD1  A PHE   A 1 6   ? 16.451 -6.547  15.524  0.60 19.79 ?  6   PHE   A HD1  1 
ATOM   88   H  HD1  B PHE   A 1 6   ? 16.619 -6.759  15.274  0.40 23.55 ?  6   PHE   A HD1  1 
ATOM   89   H  HD2  A PHE   A 1 6   ? 18.497 -9.755  16.755  0.60 20.60 ?  6   PHE   A HD2  1 
ATOM   90   H  HD2  B PHE   A 1 6   ? 18.378 -9.889  17.034  0.40 23.94 ?  6   PHE   A HD2  1 
ATOM   91   H  HE1  A PHE   A 1 6   ? 18.371 -5.686  14.570  0.60 19.90 ?  6   PHE   A HE1  1 
ATOM   92   H  HE1  B PHE   A 1 6   ? 18.642 -6.146  14.339  0.40 23.16 ?  6   PHE   A HE1  1 
ATOM   93   H  HE2  A PHE   A 1 6   ? 20.417 -8.900  15.803  0.60 20.48 ?  6   PHE   A HE2  1 
ATOM   94   H  HE2  B PHE   A 1 6   ? 20.402 -9.278  16.101  0.40 23.37 ?  6   PHE   A HE2  1 
ATOM   95   H  HZ   A PHE   A 1 6   ? 20.355 -6.863  14.709  0.60 20.18 ?  6   PHE   A HZ   1 
ATOM   96   H  HZ   B PHE   A 1 6   ? 20.535 -7.405  14.752  0.40 23.07 ?  6   PHE   A HZ   1 
ATOM   97   N  N    A SER   A 1 7   ? 13.220 -7.618  18.267  0.60 19.92 ?  7   SER   A N    1 
ATOM   98   N  N    B SER   A 1 7   ? 13.342 -7.194  18.327  0.40 23.00 ?  7   SER   A N    1 
ATOM   99   C  CA   A SER   A 1 7   ? 11.847 -7.790  18.725  0.60 19.82 ?  7   SER   A CA   1 
ATOM   100  C  CA   B SER   A 1 7   ? 12.011 -7.110  18.916  0.40 22.69 ?  7   SER   A CA   1 
ATOM   101  C  C    A SER   A 1 7   ? 10.865 -7.459  17.606  0.60 18.28 ?  7   SER   A C    1 
ATOM   102  C  C    B SER   A 1 7   ? 10.945 -7.187  17.832  0.40 21.35 ?  7   SER   A C    1 
ATOM   103  O  O    A SER   A 1 7   ? 11.107 -6.552  16.806  0.60 18.74 ?  7   SER   A O    1 
ATOM   104  O  O    B SER   A 1 7   ? 10.990 -6.435  16.854  0.40 21.44 ?  7   SER   A O    1 
ATOM   105  C  CB   A SER   A 1 7   ? 11.579 -6.870  19.924  0.60 21.41 ?  7   SER   A CB   1 
ATOM   106  C  CB   B SER   A 1 7   ? 11.854 -5.799  19.693  0.40 23.65 ?  7   SER   A CB   1 
ATOM   107  O  OG   A SER   A 1 7   ? 10.214 -6.890  20.292  0.60 22.87 ?  7   SER   A OG   1 
ATOM   108  O  OG   B SER   A 1 7   ? 10.902 -5.926  20.734  0.40 24.60 ?  7   SER   A OG   1 
ATOM   109  H  H    A SER   A 1 7   ? 13.348 -6.893  17.829  0.60 23.88 ?  7   SER   A H    1 
ATOM   110  H  H    B SER   A 1 7   ? 13.536 -6.520  17.826  0.40 27.58 ?  7   SER   A H    1 
ATOM   111  H  HA   A SER   A 1 7   ? 11.704 -8.710  19.001  0.60 23.76 ?  7   SER   A HA   1 
ATOM   112  H  HA   B SER   A 1 7   ? 11.877 -7.847  19.530  0.40 27.20 ?  7   SER   A HA   1 
ATOM   113  H  HB2  A SER   A 1 7   ? 12.111 -7.171  20.678  0.60 25.66 ?  7   SER   A HB2  1 
ATOM   114  H  HB2  B SER   A 1 7   ? 12.715 -5.551  20.068  0.40 28.36 ?  7   SER   A HB2  1 
ATOM   115  H  HB3  A SER   A 1 7   ? 11.827 -5.963  19.687  0.60 25.66 ?  7   SER   A HB3  1 
ATOM   116  H  HB3  B SER   A 1 7   ? 11.549 -5.103  19.089  0.40 28.36 ?  7   SER   A HB3  1 
ATOM   117  H  HG   A SER   A 1 7   ? 10.084 -6.382  20.947  0.60 27.42 ?  7   SER   A HG   1 
ATOM   118  H  HG   B SER   A 1 7   ? 10.852 -5.203  21.164  0.40 29.50 ?  7   SER   A HG   1 
ATOM   119  N  N    A GLY   A 1 8   ? 9.755  -8.199  17.551  0.60 16.87 ?  8   GLY   A N    1 
ATOM   120  N  N    B GLY   A 1 8   ? 9.991  -8.097  18.011  0.40 20.11 ?  8   GLY   A N    1 
ATOM   121  C  CA   A GLY   A 1 8   ? 8.688  -7.894  16.618  0.60 15.90 ?  8   GLY   A CA   1 
ATOM   122  C  CA   B GLY   A 1 8   ? 8.812  -8.121  17.168  0.40 18.68 ?  8   GLY   A CA   1 
ATOM   123  C  C    A GLY   A 1 8   ? 8.858  -8.436  15.215  0.60 14.99 ?  8   GLY   A C    1 
ATOM   124  C  C    B GLY   A 1 8   ? 9.043  -8.537  15.736  0.40 17.03 ?  8   GLY   A C    1 
ATOM   125  O  O    A GLY   A 1 8   ? 8.108  -8.030  14.319  0.60 15.29 ?  8   GLY   A O    1 
ATOM   126  O  O    B GLY   A 1 8   ? 8.274  -8.138  14.856  0.40 17.33 ?  8   GLY   A O    1 
ATOM   127  H  H    A GLY   A 1 8   ? 9.608  -8.884  18.045  0.60 20.22 ?  8   GLY   A H    1 
ATOM   128  H  H    B GLY   A 1 8   ? 10.008 -8.710  18.611  0.40 24.11 ?  8   GLY   A H    1 
ATOM   129  H  HA2  A GLY   A 1 8   ? 7.858  -8.241  16.979  0.60 19.06 ?  8   GLY   A HA2  1 
ATOM   130  H  HA2  B GLY   A 1 8   ? 8.169  -8.735  17.547  0.40 22.39 ?  8   GLY   A HA2  1 
ATOM   131  H  HA3  A GLY   A 1 8   ? 8.602  -6.929  16.551  0.60 19.06 ?  8   GLY   A HA3  1 
ATOM   132  H  HA3  B GLY   A 1 8   ? 8.419  -7.237  17.155  0.40 22.39 ?  8   GLY   A HA3  1 
ATOM   133  N  N    A TYR   A 1 9   ? 9.810  -9.335  14.987  0.60 13.66 ?  9   TYR   A N    1 
ATOM   134  N  N    B TYR   A 1 9   ? 10.073 -9.335  15.473  0.40 15.75 ?  9   TYR   A N    1 
ATOM   135  C  CA   A TYR   A 1 9   ? 10.058 -9.884  13.662  0.60 12.34 ?  9   TYR   A CA   1 
ATOM   136  C  CA   B TYR   A 1 9   ? 10.317 -9.810  14.120  0.40 14.49 ?  9   TYR   A CA   1 
ATOM   137  C  C    A TYR   A 1 9   ? 9.177  -11.099 13.395  0.60 12.31 ?  9   TYR   A C    1 
ATOM   138  C  C    B TYR   A 1 9   ? 9.479  -11.046 13.819  0.40 13.59 ?  9   TYR   A C    1 
ATOM   139  O  O    A TYR   A 1 9   ? 8.840  -11.868 14.302  0.60 13.57 ?  9   TYR   A O    1 
ATOM   140  O  O    B TYR   A 1 9   ? 9.311  -11.932 14.665  0.40 13.95 ?  9   TYR   A O    1 
ATOM   141  C  CB   A TYR   A 1 9   ? 11.524 -10.307 13.515  0.60 12.47 ?  9   TYR   A CB   1 
ATOM   142  C  CB   B TYR   A 1 9   ? 11.805 -10.112 13.919  0.40 14.11 ?  9   TYR   A CB   1 
ATOM   143  C  CG   A TYR   A 1 9   ? 12.476 -9.146  13.370  0.60 12.94 ?  9   TYR   A CG   1 
ATOM   144  C  CG   B TYR   A 1 9   ? 12.627 -8.865  13.679  0.40 13.41 ?  9   TYR   A CG   1 
ATOM   145  C  CD1  A TYR   A 1 9   ? 12.843 -8.388  14.471  0.60 13.32 ?  9   TYR   A CD1  1 
ATOM   146  C  CD1  B TYR   A 1 9   ? 12.896 -7.979  14.713  0.40 13.70 ?  9   TYR   A CD1  1 
ATOM   147  C  CD2  A TYR   A 1 9   ? 12.988 -8.795  12.129  0.60 13.30 ?  9   TYR   A CD2  1 
ATOM   148  C  CD2  B TYR   A 1 9   ? 13.113 -8.561  12.413  0.40 12.90 ?  9   TYR   A CD2  1 
ATOM   149  C  CE1  A TYR   A 1 9   ? 13.699 -7.312  14.346  0.60 13.74 ?  9   TYR   A CE1  1 
ATOM   150  C  CE1  B TYR   A 1 9   ? 13.634 -6.832  14.497  0.40 13.56 ?  9   TYR   A CE1  1 
ATOM   151  C  CE2  A TYR   A 1 9   ? 13.845 -7.724  11.992  0.60 13.68 ?  9   TYR   A CE2  1 
ATOM   152  C  CE2  B TYR   A 1 9   ? 13.851 -7.416  12.187  0.40 12.89 ?  9   TYR   A CE2  1 
ATOM   153  C  CZ   A TYR   A 1 9   ? 14.194 -6.984  13.102  0.60 14.27 ?  9   TYR   A CZ   1 
ATOM   154  C  CZ   B TYR   A 1 9   ? 14.107 -6.558  13.231  0.40 13.23 ?  9   TYR   A CZ   1 
ATOM   155  O  OH   A TYR   A 1 9   ? 15.044 -5.917  12.967  0.60 15.44 ?  9   TYR   A OH   1 
ATOM   156  O  OH   B TYR   A 1 9   ? 14.839 -5.417  13.001  0.40 13.53 ?  9   TYR   A OH   1 
ATOM   157  H  H    A TYR   A 1 9   ? 10.326 -9.648  15.592  0.60 16.37 ?  9   TYR   A H    1 
ATOM   158  H  H    B TYR   A 1 9   ? 10.647 -9.610  16.055  0.40 18.87 ?  9   TYR   A H    1 
ATOM   159  H  HA   A TYR   A 1 9   ? 9.864  -9.211  12.988  0.60 14.78 ?  9   TYR   A HA   1 
ATOM   160  H  HA   B TYR   A 1 9   ? 10.074 -9.115  13.490  0.40 17.37 ?  9   TYR   A HA   1 
ATOM   161  H  HB2  A TYR   A 1 9   ? 11.786 -10.818 14.296  0.60 14.95 ?  9   TYR   A HB2  1 
ATOM   162  H  HB2  B TYR   A 1 9   ? 12.156 -10.559 14.705  0.40 16.90 ?  9   TYR   A HB2  1 
ATOM   163  H  HB3  A TYR   A 1 9   ? 11.600 -10.857 12.719  0.60 14.95 ?  9   TYR   A HB3  1 
ATOM   164  H  HB3  B TYR   A 1 9   ? 11.902 -10.683 13.142  0.40 16.90 ?  9   TYR   A HB3  1 
ATOM   165  H  HD1  A TYR   A 1 9   ? 12.500 -8.607  15.310  0.60 15.96 ?  9   TYR   A HD1  1 
ATOM   166  H  HD1  B TYR   A 1 9   ? 12.576 -8.165  15.566  0.40 16.42 ?  9   TYR   A HD1  1 
ATOM   167  H  HD2  A TYR   A 1 9   ? 12.751 -9.295  11.378  0.60 15.94 ?  9   TYR   A HD2  1 
ATOM   168  H  HD2  B TYR   A 1 9   ? 12.943 -9.139  11.707  0.40 15.45 ?  9   TYR   A HD2  1 
ATOM   169  H  HE1  A TYR   A 1 9   ? 13.937 -6.815  15.094  0.60 16.46 ?  9   TYR   A HE1  1 
ATOM   170  H  HE1  B TYR   A 1 9   ? 13.809 -6.246  15.200  0.40 16.25 ?  9   TYR   A HE1  1 
ATOM   171  H  HE2  A TYR   A 1 9   ? 14.188 -7.505  11.156  0.60 16.39 ?  9   TYR   A HE2  1 
ATOM   172  H  HE2  B TYR   A 1 9   ? 14.176 -7.223  11.335  0.40 15.44 ?  9   TYR   A HE2  1 
ATOM   173  H  HH   A TYR   A 1 9   ? 15.175 -5.568  13.719  0.60 18.51 ?  9   TYR   A HH   1 
ATOM   174  H  HH   B TYR   A 1 9   ? 14.929 -4.976  13.712  0.40 16.21 ?  9   TYR   A HH   1 
ATOM   175  N  N    A LEU   A 1 10  ? 8.814  -11.264 12.125  0.60 12.01 ?  10  LEU   A N    1 
ATOM   176  N  N    B LEU   A 1 10  ? 8.940  -11.088 12.604  0.40 13.07 ?  10  LEU   A N    1 
ATOM   177  C  CA   A LEU   A 1 10  ? 8.220  -12.496 11.629  0.60 11.66 ?  10  LEU   A CA   1 
ATOM   178  C  CA   B LEU   A 1 10  ? 8.274  -12.276 12.093  0.40 12.82 ?  10  LEU   A CA   1 
ATOM   179  C  C    A LEU   A 1 10  ? 9.342  -13.429 11.189  0.60 11.44 ?  10  LEU   A C    1 
ATOM   180  C  C    B LEU   A 1 10  ? 9.334  -13.242 11.573  0.40 12.06 ?  10  LEU   A C    1 
ATOM   181  O  O    A LEU   A 1 10  ? 10.303 -13.000 10.545  0.60 11.64 ?  10  LEU   A O    1 
ATOM   182  O  O    B LEU   A 1 10  ? 10.193 -12.862 10.771  0.40 12.38 ?  10  LEU   A O    1 
ATOM   183  C  CB   A LEU   A 1 10  ? 7.322  -12.185 10.431  0.60 12.46 ?  10  LEU   A CB   1 
ATOM   184  C  CB   B LEU   A 1 10  ? 7.322  -11.881 10.962  0.40 13.26 ?  10  LEU   A CB   1 
ATOM   185  C  CG   A LEU   A 1 10  ? 6.661  -13.380 9.741   0.60 14.86 ?  10  LEU   A CG   1 
ATOM   186  C  CG   B LEU   A 1 10  ? 6.609  -13.032 10.249  0.40 14.44 ?  10  LEU   A CG   1 
ATOM   187  C  CD1  A LEU   A 1 10  ? 5.626  -14.018 10.648  0.60 16.09 ?  10  LEU   A CD1  1 
ATOM   188  C  CD1  B LEU   A 1 10  ? 5.595  -13.694 11.168  0.40 15.45 ?  10  LEU   A CD1  1 
ATOM   189  C  CD2  A LEU   A 1 10  ? 6.035  -12.967 8.421   0.60 16.16 ?  10  LEU   A CD2  1 
ATOM   190  C  CD2  B LEU   A 1 10  ? 5.946  -12.525 8.979   0.40 15.81 ?  10  LEU   A CD2  1 
ATOM   191  H  H    A LEU   A 1 10  ? 8.909  -10.666 11.511  0.60 14.39 ?  10  LEU   A H    1 
ATOM   192  H  H    B LEU   A 1 10  ? 8.952  -10.430 12.051  0.40 15.66 ?  10  LEU   A H    1 
ATOM   193  H  HA   A LEU   A 1 10  ? 7.693  -12.925 12.323  0.60 13.96 ?  10  LEU   A HA   1 
ATOM   194  H  HA   B LEU   A 1 10  ? 7.759  -12.702 12.798  0.40 15.37 ?  10  LEU   A HA   1 
ATOM   195  H  HB2  A LEU   A 1 10  ? 6.607  -11.603 10.726  0.60 14.93 ?  10  LEU   A HB2  1 
ATOM   196  H  HB2  B LEU   A 1 10  ? 6.632  -11.296 11.326  0.40 15.88 ?  10  LEU   A HB2  1 
ATOM   197  H  HB3  A LEU   A 1 10  ? 7.853  -11.733 9.760   0.60 14.93 ?  10  LEU   A HB3  1 
ATOM   198  H  HB3  B LEU   A 1 10  ? 7.827  -11.394 10.292  0.40 15.88 ?  10  LEU   A HB3  1 
ATOM   199  H  HG   A LEU   A 1 10  ? 7.334  -14.054 9.545   0.60 17.81 ?  10  LEU   A HG   1 
ATOM   200  H  HG   B LEU   A 1 10  ? 7.262  -13.701 9.996   0.40 17.30 ?  10  LEU   A HG   1 
ATOM   201  H  HD11 A LEU   A 1 10  ? 5.259  -14.803 10.211  0.60 19.28 ?  10  LEU   A HD11 1 
ATOM   202  H  HD11 B LEU   A 1 10  ? 5.224  -14.471 10.720  0.40 18.51 ?  10  LEU   A HD11 1 
ATOM   203  H  HD12 A LEU   A 1 10  ? 6.050  -14.273 11.482  0.60 19.28 ?  10  LEU   A HD12 1 
ATOM   204  H  HD12 B LEU   A 1 10  ? 6.038  -13.966 11.987  0.40 18.51 ?  10  LEU   A HD12 1 
ATOM   205  H  HD13 A LEU   A 1 10  ? 4.920  -13.375 10.820  0.60 19.28 ?  10  LEU   A HD13 1 
ATOM   206  H  HD13 B LEU   A 1 10  ? 4.890  -13.060 11.371  0.40 18.51 ?  10  LEU   A HD13 1 
ATOM   207  H  HD21 A LEU   A 1 10  ? 5.623  -13.743 8.009   0.60 19.36 ?  10  LEU   A HD21 1 
ATOM   208  H  HD21 B LEU   A 1 10  ? 5.488  -13.264 8.549   0.40 18.95 ?  10  LEU   A HD21 1 
ATOM   209  H  HD22 A LEU   A 1 10  ? 5.366  -12.287 8.592   0.60 19.36 ?  10  LEU   A HD22 1 
ATOM   210  H  HD22 B LEU   A 1 10  ? 5.312  -11.830 9.210   0.40 18.95 ?  10  LEU   A HD22 1 
ATOM   211  H  HD23 A LEU   A 1 10  ? 6.729  -12.614 7.843   0.60 19.36 ?  10  LEU   A HD23 1 
ATOM   212  H  HD23 B LEU   A 1 10  ? 6.629  -12.170 8.389   0.40 18.95 ?  10  LEU   A HD23 1 
ATOM   213  N  N    A LYS   A 1 11  ? 9.211  -14.708 11.527  0.60 11.32 ?  11  LYS   A N    1 
ATOM   214  N  N    B LYS   A 1 11  ? 9.287  -14.483 12.043  0.40 11.32 ?  11  LYS   A N    1 
ATOM   215  C  CA   A LYS   A 1 11  ? 10.219 -15.708 11.201  0.60 11.64 ?  11  LYS   A CA   1 
ATOM   216  C  CA   B LYS   A 1 11  ? 10.233 -15.497 11.595  0.40 11.53 ?  11  LYS   A CA   1 
ATOM   217  C  C    A LYS   A 1 11  ? 9.881  -16.313 9.845   0.60 11.61 ?  11  LYS   A C    1 
ATOM   218  C  C    B LYS   A 1 11  ? 9.816  -16.011 10.223  0.40 11.17 ?  11  LYS   A C    1 
ATOM   219  O  O    A LYS   A 1 11  ? 8.833  -16.943 9.695   0.60 13.17 ?  11  LYS   A O    1 
ATOM   220  O  O    B LYS   A 1 11  ? 8.674  -16.441 10.033  0.40 11.39 ?  11  LYS   A O    1 
ATOM   221  C  CB   A LYS   A 1 11  ? 10.227 -16.780 12.292  0.60 11.88 ?  11  LYS   A CB   1 
ATOM   222  C  CB   B LYS   A 1 11  ? 10.283 -16.647 12.602  0.40 11.94 ?  11  LYS   A CB   1 
ATOM   223  C  CG   A LYS   A 1 11  ? 11.268 -17.874 12.151  0.60 12.50 ?  11  LYS   A CG   1 
ATOM   224  C  CG   B LYS   A 1 11  ? 11.266 -17.763 12.253  0.40 12.78 ?  11  LYS   A CG   1 
ATOM   225  C  CD   A LYS   A 1 11  ? 11.334 -18.673 13.450  0.60 12.76 ?  11  LYS   A CD   1 
ATOM   226  C  CD   B LYS   A 1 11  ? 11.382 -18.763 13.402  0.40 13.45 ?  11  LYS   A CD   1 
ATOM   227  C  CE   A LYS   A 1 11  ? 12.331 -19.817 13.386  0.60 12.74 ?  11  LYS   A CE   1 
ATOM   228  C  CE   B LYS   A 1 11  ? 12.374 -19.888 13.115  0.40 13.90 ?  11  LYS   A CE   1 
ATOM   229  N  NZ   A LYS   A 1 11  ? 13.702 -19.341 13.091  0.60 13.00 ?  11  LYS   A NZ   1 
ATOM   230  N  NZ   B LYS   A 1 11  ? 13.774 -19.408 12.965  0.40 14.12 ?  11  LYS   A NZ   1 
ATOM   231  H  H    A LYS   A 1 11  ? 8.518  -15.037 11.931  0.60 13.56 ?  11  LYS   A H    1 
ATOM   232  H  H    B LYS   A 1 11  ? 8.716  -14.755 12.626  0.40 13.56 ?  11  LYS   A H    1 
ATOM   233  H  HA   A LYS   A 1 11  ? 11.088 -15.296 11.147  0.60 13.95 ?  11  LYS   A HA   1 
ATOM   234  H  HA   B LYS   A 1 11  ? 11.111 -15.097 11.518  0.40 13.82 ?  11  LYS   A HA   1 
ATOM   235  H  HB2  A LYS   A 1 11  ? 10.385 -16.338 13.140  0.60 14.24 ?  11  LYS   A HB2  1 
ATOM   236  H  HB2  B LYS   A 1 11  ? 10.541 -16.280 13.462  0.40 14.30 ?  11  LYS   A HB2  1 
ATOM   237  H  HB3  A LYS   A 1 11  ? 9.357  -17.208 12.308  0.60 14.24 ?  11  LYS   A HB3  1 
ATOM   238  H  HB3  B LYS   A 1 11  ? 9.397  -17.034 12.664  0.40 14.30 ?  11  LYS   A HB3  1 
ATOM   239  H  HG2  A LYS   A 1 11  ? 11.016 -18.473 11.429  0.60 14.97 ?  11  LYS   A HG2  1 
ATOM   240  H  HG2  B LYS   A 1 11  ? 10.948 -18.235 11.466  0.40 15.31 ?  11  LYS   A HG2  1 
ATOM   241  H  HG3  A LYS   A 1 11  ? 12.136 -17.479 11.982  0.60 14.97 ?  11  LYS   A HG3  1 
ATOM   242  H  HG3  B LYS   A 1 11  ? 12.141 -17.382 12.086  0.40 15.31 ?  11  LYS   A HG3  1 
ATOM   243  H  HD2  A LYS   A 1 11  ? 11.598 -18.081 14.171  0.60 15.29 ?  11  LYS   A HD2  1 
ATOM   244  H  HD2  B LYS   A 1 11  ? 11.680 -18.296 14.197  0.40 16.12 ?  11  LYS   A HD2  1 
ATOM   245  H  HD3  A LYS   A 1 11  ? 10.456 -19.048 13.635  0.60 15.29 ?  11  LYS   A HD3  1 
ATOM   246  H  HD3  B LYS   A 1 11  ? 10.513 -19.166 13.559  0.40 16.12 ?  11  LYS   A HD3  1 
ATOM   247  H  HE2  A LYS   A 1 11  ? 12.349 -20.275 14.242  0.60 15.26 ?  11  LYS   A HE2  1 
ATOM   248  H  HE2  B LYS   A 1 11  ? 12.355 -20.522 13.850  0.40 16.65 ?  11  LYS   A HE2  1 
ATOM   249  H  HE3  A LYS   A 1 11  ? 12.068 -20.433 12.684  0.60 15.26 ?  11  LYS   A HE3  1 
ATOM   250  H  HE3  B LYS   A 1 11  ? 12.122 -20.331 12.290  0.40 16.65 ?  11  LYS   A HE3  1 
ATOM   251  H  HZ1  A LYS   A 1 11  ? 14.260 -20.030 13.042  0.60 15.57 ?  11  LYS   A HZ1  1 
ATOM   252  H  HZ1  B LYS   A 1 11  ? 14.317 -20.095 12.801  0.40 16.92 ?  11  LYS   A HZ1  1 
ATOM   253  H  HZ2  A LYS   A 1 11  ? 13.711 -18.904 12.315  0.60 15.57 ?  11  LYS   A HZ2  1 
ATOM   254  H  HZ2  B LYS   A 1 11  ? 13.828 -18.831 12.290  0.40 16.92 ?  11  LYS   A HZ2  1 
ATOM   255  H  HZ3  A LYS   A 1 11  ? 13.977 -18.790 13.734  0.60 15.57 ?  11  LYS   A HZ3  1 
ATOM   256  H  HZ3  B LYS   A 1 11  ? 14.040 -19.004 13.713  0.40 16.92 ?  11  LYS   A HZ3  1 
ATOM   257  N  N    A LEU   A 1 12  ? 10.755 -16.126 8.856   0.60 10.84 ?  12  LEU   A N    1 
ATOM   258  N  N    B LEU   A 1 12  ? 10.735 -15.953 9.261   0.40 11.14 ?  12  LEU   A N    1 
ATOM   259  C  CA   A LEU   A 1 12  ? 10.504 -16.719 7.546   0.60 11.10 ?  12  LEU   A CA   1 
ATOM   260  C  CA   B LEU   A 1 12  ? 10.466 -16.454 7.917   0.40 11.48 ?  12  LEU   A CA   1 
ATOM   261  C  C    A LEU   A 1 12  ? 11.103 -18.112 7.417   0.60 11.48 ?  12  LEU   A C    1 
ATOM   262  C  C    B LEU   A 1 12  ? 11.022 -17.852 7.675   0.40 11.65 ?  12  LEU   A C    1 
ATOM   263  O  O    A LEU   A 1 12  ? 10.485 -18.997 6.816   0.60 11.67 ?  12  LEU   A O    1 
ATOM   264  O  O    B LEU   A 1 12  ? 10.341 -18.688 7.073   0.40 11.66 ?  12  LEU   A O    1 
ATOM   265  C  CB   A LEU   A 1 12  ? 11.055 -15.826 6.430   0.60 11.08 ?  12  LEU   A CB   1 
ATOM   266  C  CB   B LEU   A 1 12  ? 11.017 -15.489 6.861   0.40 11.96 ?  12  LEU   A CB   1 
ATOM   267  C  CG   A LEU   A 1 12  ? 10.412 -14.452 6.256   0.60 11.99 ?  12  LEU   A CG   1 
ATOM   268  C  CG   B LEU   A 1 12  ? 10.336 -14.122 6.781   0.40 12.56 ?  12  LEU   A CG   1 
ATOM   269  C  CD1  A LEU   A 1 12  ? 11.153 -13.701 5.169   0.60 12.79 ?  12  LEU   A CD1  1 
ATOM   270  C  CD1  B LEU   A 1 12  ? 10.922 -13.308 5.631   0.40 13.15 ?  12  LEU   A CD1  1 
ATOM   271  C  CD2  A LEU   A 1 12  ? 8.937  -14.581 5.913   0.60 12.38 ?  12  LEU   A CD2  1 
ATOM   272  C  CD2  B LEU   A 1 12  ? 8.829  -14.271 6.633   0.40 13.42 ?  12  LEU   A CD2  1 
ATOM   273  H  H    A LEU   A 1 12  ? 11.489 -15.677 8.913   0.60 12.98 ?  12  LEU   A H    1 
ATOM   274  H  H    B LEU   A 1 12  ? 11.522 -15.608 9.362   0.40 13.34 ?  12  LEU   A H    1 
ATOM   275  H  HA   A LEU   A 1 12  ? 9.548  -16.804 7.415   0.60 13.29 ?  12  LEU   A HA   1 
ATOM   276  H  HA   B LEU   A 1 12  ? 9.507  -16.499 7.796   0.40 13.76 ?  12  LEU   A HA   1 
ATOM   277  H  HB2  A LEU   A 1 12  ? 11.997 -15.685 6.597   0.60 13.27 ?  12  LEU   A HB2  1 
ATOM   278  H  HB2  B LEU   A 1 12  ? 11.956 -15.328 7.046   0.40 14.33 ?  12  LEU   A HB2  1 
ATOM   279  H  HB3  A LEU   A 1 12  ? 10.949 -16.301 5.587   0.60 13.27 ?  12  LEU   A HB3  1 
ATOM   280  H  HB3  B LEU   A 1 12  ? 10.926 -15.902 5.989   0.40 14.33 ?  12  LEU   A HB3  1 
ATOM   281  H  HG   A LEU   A 1 12  ? 10.493 -13.955 7.082   0.60 14.37 ?  12  LEU   A HG   1 
ATOM   282  H  HG   B LEU   A 1 12  ? 10.508 -13.633 7.603   0.40 15.04 ?  12  LEU   A HG   1 
ATOM   283  H  HD11 A LEU   A 1 12  ? 10.745 -12.830 5.056   0.60 15.33 ?  12  LEU   A HD11 1 
ATOM   284  H  HD11 B LEU   A 1 12  ? 10.482 -12.443 5.598   0.40 15.76 ?  12  LEU   A HD11 1 
ATOM   285  H  HD12 A LEU   A 1 12  ? 12.082 -13.603 5.431   0.60 15.33 ?  12  LEU   A HD12 1 
ATOM   286  H  HD12 B LEU   A 1 12  ? 11.873 -13.189 5.780   0.40 15.76 ?  12  LEU   A HD12 1 
ATOM   287  H  HD13 A LEU   A 1 12  ? 11.095 -14.206 4.341   0.60 15.33 ?  12  LEU   A HD13 1 
ATOM   288  H  HD13 B LEU   A 1 12  ? 10.774 -13.786 4.800   0.40 15.76 ?  12  LEU   A HD13 1 
ATOM   289  H  HD21 A LEU   A 1 12  ? 8.582  -13.703 5.710   0.60 14.83 ?  12  LEU   A HD21 1 
ATOM   290  H  HD21 B LEU   A 1 12  ? 8.453  -13.423 6.353   0.40 16.08 ?  12  LEU   A HD21 1 
ATOM   291  H  HD22 A LEU   A 1 12  ? 8.840  -15.163 5.142   0.60 14.83 ?  12  LEU   A HD22 1 
ATOM   292  H  HD22 B LEU   A 1 12  ? 8.647  -14.952 5.968   0.40 16.08 ?  12  LEU   A HD22 1 
ATOM   293  H  HD23 A LEU   A 1 12  ? 8.466  -14.961 6.673   0.60 14.83 ?  12  LEU   A HD23 1 
ATOM   294  H  HD23 B LEU   A 1 12  ? 8.455  -14.534 7.489   0.40 16.08 ?  12  LEU   A HD23 1 
ATOM   295  N  N    A THR   A 1 13  ? 12.313 -18.300 7.936   0.60 12.05 ?  13  THR   A N    1 
ATOM   296  N  N    B THR   A 1 13  ? 12.248 -18.121 8.116   0.40 11.72 ?  13  THR   A N    1 
ATOM   297  C  CA   A THR   A 1 13  ? 13.015 -19.577 7.908   0.60 12.27 ?  13  THR   A CA   1 
ATOM   298  C  CA   B THR   A 1 13  ? 12.895 -19.412 7.911   0.40 11.86 ?  13  THR   A CA   1 
ATOM   299  C  C    A THR   A 1 13  ? 13.763 -19.738 9.228   0.60 12.41 ?  13  THR   A C    1 
ATOM   300  C  C    B THR   A 1 13  ? 13.694 -19.747 9.164   0.40 12.21 ?  13  THR   A C    1 
ATOM   301  O  O    A THR   A 1 13  ? 13.650 -18.918 10.143  0.60 13.07 ?  13  THR   A O    1 
ATOM   302  O  O    B THR   A 1 13  ? 13.612 -19.057 10.185  0.40 12.20 ?  13  THR   A O    1 
ATOM   303  C  CB   A THR   A 1 13  ? 14.006 -19.659 6.738   0.60 12.88 ?  13  THR   A CB   1 
ATOM   304  C  CB   B THR   A 1 13  ? 13.829 -19.378 6.695   0.40 11.97 ?  13  THR   A CB   1 
ATOM   305  O  OG1  A THR   A 1 13  ? 15.077 -18.744 6.976   0.60 12.71 ?  13  THR   A OG1  1 
ATOM   306  O  OG1  B THR   A 1 13  ? 14.876 -18.435 6.939   0.40 12.29 ?  13  THR   A OG1  1 
ATOM   307  C  CG2  A THR   A 1 13  ? 13.351 -19.329 5.404   0.60 13.61 ?  13  THR   A CG2  1 
ATOM   308  C  CG2  B THR   A 1 13  ? 13.085 -19.006 5.418   0.40 12.53 ?  13  THR   A CG2  1 
ATOM   309  H  H    A THR   A 1 13  ? 12.768 -17.676 8.308   0.60 14.44 ?  13  THR   A H    1 
ATOM   310  H  H    B THR   A 1 13  ? 12.738 -17.553 8.538   0.40 14.04 ?  13  THR   A H    1 
ATOM   311  H  HA   A THR   A 1 13  ? 12.380 -20.299 7.819   0.60 14.70 ?  13  THR   A HA   1 
ATOM   312  H  HA   B THR   A 1 13  ? 12.225 -20.099 7.773   0.40 14.21 ?  13  THR   A HA   1 
ATOM   313  H  HB   A THR   A 1 13  ? 14.362 -20.565 6.676   0.60 15.43 ?  13  THR   A HB   1 
ATOM   314  H  HB   B THR   A 1 13  ? 14.220 -20.256 6.569   0.40 14.34 ?  13  THR   A HB   1 
ATOM   315  H  HG1  A THR   A 1 13  ? 15.649 -19.095 7.480   0.60 15.22 ?  13  THR   A HG1  1 
ATOM   316  H  HG1  B THR   A 1 13  ? 15.400 -18.405 6.283   0.40 14.73 ?  13  THR   A HG1  1 
ATOM   317  H  HG21 A THR   A 1 13  ? 13.970 -19.506 4.674   0.60 16.30 ?  13  THR   A HG21 1 
ATOM   318  H  HG21 B THR   A 1 13  ? 13.679 -19.090 4.653   0.40 15.01 ?  13  THR   A HG21 1 
ATOM   319  H  HG22 A THR   A 1 13  ? 12.560 -19.877 5.279   0.60 16.30 ?  13  THR   A HG22 1 
ATOM   320  H  HG22 B THR   A 1 13  ? 12.329 -19.601 5.290   0.40 15.01 ?  13  THR   A HG22 1 
ATOM   321  H  HG23 A THR   A 1 13  ? 13.097 -18.396 5.381   0.60 16.30 ?  13  THR   A HG23 1 
ATOM   322  H  HG23 B THR   A 1 13  ? 12.765 -18.094 5.470   0.40 15.01 ?  13  THR   A HG23 1 
ATOM   323  N  N    A ASP   A 1 14  ? 14.570 -20.794 9.301   0.60 12.47 ?  14  ASP   A N    1 
ATOM   324  N  N    B ASP   A 1 14  ? 14.501 -20.804 9.074   0.40 12.75 ?  14  ASP   A N    1 
ATOM   325  C  CA   A ASP   A 1 14  ? 15.398 -21.037 10.474  0.60 13.07 ?  14  ASP   A CA   1 
ATOM   326  C  CA   B ASP   A 1 14  ? 15.378 -21.143 10.186  0.40 13.06 ?  14  ASP   A CA   1 
ATOM   327  C  C    A ASP   A 1 14  ? 16.208 -19.805 10.869  0.60 12.25 ?  14  ASP   A C    1 
ATOM   328  C  C    B ASP   A 1 14  ? 16.262 -19.971 10.592  0.40 11.71 ?  14  ASP   A C    1 
ATOM   329  O  O    A ASP   A 1 14  ? 16.370 -19.517 12.061  0.60 12.98 ?  14  ASP   A O    1 
ATOM   330  O  O    B ASP   A 1 14  ? 16.615 -19.843 11.770  0.40 11.88 ?  14  ASP   A O    1 
ATOM   331  C  CB   A ASP   A 1 14  ? 16.342 -22.196 10.172  0.60 15.45 ?  14  ASP   A CB   1 
ATOM   332  C  CB   B ASP   A 1 14  ? 16.242 -22.354 9.831   0.40 15.46 ?  14  ASP   A CB   1 
ATOM   333  C  CG   A ASP   A 1 14  ? 17.192 -22.563 11.357  0.60 18.92 ?  14  ASP   A CG   1 
ATOM   334  C  CG   B ASP   A 1 14  ? 17.337 -22.595 10.840  0.40 18.00 ?  14  ASP   A CG   1 
ATOM   335  O  OD1  A ASP   A 1 14  ? 16.633 -23.103 12.334  0.60 19.60 ?  14  ASP   A OD1  1 
ATOM   336  O  OD1  B ASP   A 1 14  ? 17.017 -22.765 12.035  0.40 18.80 ?  14  ASP   A OD1  1 
ATOM   337  O  OD2  A ASP   A 1 14  ? 18.409 -22.295 11.317  0.60 20.90 -1 14  ASP   A OD2  1 
ATOM   338  O  OD2  B ASP   A 1 14  ? 18.519 -22.613 10.442  0.40 19.28 -1 14  ASP   A OD2  1 
ATOM   339  H  H    A ASP   A 1 14  ? 14.665 -21.376 8.682   0.60 14.94 ?  14  ASP   A H    1 
ATOM   340  H  H    B ASP   A 1 14  ? 14.558 -21.330 8.393   0.40 15.27 ?  14  ASP   A H    1 
ATOM   341  H  HA   A ASP   A 1 14  ? 14.834 -21.293 11.226  0.60 15.66 ?  14  ASP   A HA   1 
ATOM   342  H  HA   B ASP   A 1 14  ? 14.839 -21.382 10.951  0.40 15.65 ?  14  ASP   A HA   1 
ATOM   343  H  HB2  A ASP   A 1 14  ? 15.815 -22.974 9.914   0.60 18.51 ?  14  ASP   A HB2  1 
ATOM   344  H  HB2  B ASP   A 1 14  ? 15.686 -23.153 9.816   0.40 18.53 ?  14  ASP   A HB2  1 
ATOM   345  H  HB3  A ASP   A 1 14  ? 16.928 -21.944 9.439   0.60 18.51 ?  14  ASP   A HB3  1 
ATOM   346  H  HB3  B ASP   A 1 14  ? 16.649 -22.221 8.960   0.40 18.53 ?  14  ASP   A HB3  1 
ATOM   347  N  N    A ASN   A 1 15  ? 16.733 -19.069 9.885   0.60 12.06 ?  15  ASN   A N    1 
ATOM   348  N  N    B ASN   A 1 15  ? 16.621 -19.095 9.642   0.40 10.93 ?  15  ASN   A N    1 
ATOM   349  C  CA   A ASN   A 1 15  ? 17.706 -18.014 10.140  0.60 12.44 ?  15  ASN   A CA   1 
ATOM   350  C  CA   B ASN   A 1 15  ? 17.639 -18.090 9.929   0.40 11.44 ?  15  ASN   A CA   1 
ATOM   351  C  C    A ASN   A 1 15  ? 17.306 -16.635 9.632   0.60 12.18 ?  15  ASN   A C    1 
ATOM   352  C  C    B ASN   A 1 15  ? 17.322 -16.691 9.407   0.40 11.84 ?  15  ASN   A C    1 
ATOM   353  O  O    A ASN   A 1 15  ? 18.002 -15.667 9.959   0.60 11.70 ?  15  ASN   A O    1 
ATOM   354  O  O    B ASN   A 1 15  ? 18.222 -15.840 9.403   0.40 11.82 ?  15  ASN   A O    1 
ATOM   355  C  CB   A ASN   A 1 15  ? 19.073 -18.375 9.526   0.60 12.36 ?  15  ASN   A CB   1 
ATOM   356  C  CB   B ASN   A 1 15  ? 19.011 -18.542 9.402   0.40 11.39 ?  15  ASN   A CB   1 
ATOM   357  C  CG   A ASN   A 1 15  ? 19.013 -18.530 8.016   0.60 12.60 ?  15  ASN   A CG   1 
ATOM   358  C  CG   B ASN   A 1 15  ? 19.071 -18.564 7.892   0.40 11.68 ?  15  ASN   A CG   1 
ATOM   359  O  OD1  A ASN   A 1 15  ? 18.187 -19.281 7.489   0.60 12.91 ?  15  ASN   A OD1  1 
ATOM   360  O  OD1  B ASN   A 1 15  ? 18.493 -19.442 7.245   0.40 11.95 ?  15  ASN   A OD1  1 
ATOM   361  N  ND2  A ASN   A 1 15  ? 19.879 -17.801 7.307   0.60 12.91 ?  15  ASN   A ND2  1 
ATOM   362  N  ND2  B ASN   A 1 15  ? 19.765 -17.586 7.318   0.40 11.90 ?  15  ASN   A ND2  1 
ATOM   363  H  H    A ASN   A 1 15  ? 16.544 -19.172 9.062   0.60 14.44 ?  15  ASN   A H    1 
ATOM   364  H  H    B ASN   A 1 15  ? 16.292 -19.069 8.846   0.40 13.09 ?  15  ASN   A H    1 
ATOM   365  H  HA   A ASN   A 1 15  ? 17.842 -17.941 11.102  0.60 14.90 ?  15  ASN   A HA   1 
ATOM   366  H  HA   B ASN   A 1 15  ? 17.720 -18.009 10.884  0.40 13.70 ?  15  ASN   A HA   1 
ATOM   367  H  HB2  A ASN   A 1 15  ? 19.712 -17.669 9.734   0.60 14.81 ?  15  ASN   A HB2  1 
ATOM   368  H  HB2  B ASN   A 1 15  ? 19.695 -17.929 9.724   0.40 13.64 ?  15  ASN   A HB2  1 
ATOM   369  H  HB3  A ASN   A 1 15  ? 19.381 -19.215 9.899   0.60 14.81 ?  15  ASN   A HB3  1 
ATOM   370  H  HB3  B ASN   A 1 15  ? 19.200 -19.440 9.727   0.40 13.64 ?  15  ASN   A HB3  1 
ATOM   371  H  HD21 A ASN   A 1 15  ? 19.885 -17.850 6.447   0.60 15.47 ?  15  ASN   A HD21 1 
ATOM   372  H  HD21 B ASN   A 1 15  ? 19.832 -17.553 6.463   0.40 14.25 ?  15  ASN   A HD21 1 
ATOM   373  H  HD22 A ASN   A 1 15  ? 20.441 -17.282 7.706   0.60 15.47 ?  15  ASN   A HD22 1 
ATOM   374  H  HD22 B ASN   A 1 15  ? 20.150 -16.985 7.803   0.40 14.25 ?  15  ASN   A HD22 1 
ATOM   375  N  N    A VAL   A 1 16  ? 16.237 -16.513 8.841   0.60 11.57 ?  16  VAL   A N    1 
ATOM   376  N  N    B VAL   A 1 16  ? 16.085 -16.403 9.006   0.40 11.89 ?  16  VAL   A N    1 
ATOM   377  C  CA   A VAL   A 1 16  ? 15.817 -15.245 8.245   0.60 11.66 ?  16  VAL   A CA   1 
ATOM   378  C  CA   B VAL   A 1 16  ? 15.731 -15.100 8.454   0.40 12.01 ?  16  VAL   A CA   1 
ATOM   379  C  C    A VAL   A 1 16  ? 14.526 -14.760 8.901   0.60 11.00 ?  16  VAL   A C    1 
ATOM   380  C  C    B VAL   A 1 16  ? 14.486 -14.581 9.161   0.40 11.84 ?  16  VAL   A C    1 
ATOM   381  O  O    A VAL   A 1 16  ? 13.521 -15.484 8.947   0.60 10.61 ?  16  VAL   A O    1 
ATOM   382  O  O    B VAL   A 1 16  ? 13.505 -15.315 9.332   0.40 11.89 ?  16  VAL   A O    1 
ATOM   383  C  CB   A VAL   A 1 16  ? 15.659 -15.345 6.717   0.60 12.35 ?  16  VAL   A CB   1 
ATOM   384  C  CB   B VAL   A 1 16  ? 15.525 -15.152 6.927   0.40 11.98 ?  16  VAL   A CB   1 
ATOM   385  C  CG1  A VAL   A 1 16  ? 15.197 -14.005 6.143   0.60 13.33 ?  16  VAL   A CG1  1 
ATOM   386  C  CG1  B VAL   A 1 16  ? 15.159 -13.770 6.387   0.40 12.12 ?  16  VAL   A CG1  1 
ATOM   387  C  CG2  A VAL   A 1 16  ? 16.961 -15.786 6.064   0.60 13.02 ?  16  VAL   A CG2  1 
ATOM   388  C  CG2  B VAL   A 1 16  ? 16.772 -15.693 6.229   0.40 12.54 ?  16  VAL   A CG2  1 
ATOM   389  H  H    A VAL   A 1 16  ? 15.744 -17.180 8.623   0.60 13.86 ?  16  VAL   A H    1 
ATOM   390  H  H    B VAL   A 1 16  ? 15.417 -16.944 9.065   0.40 14.24 ?  16  VAL   A H    1 
ATOM   391  H  HA   A VAL   A 1 16  ? 16.506 -14.585 8.418   0.60 13.97 ?  16  VAL   A HA   1 
ATOM   392  H  HA   B VAL   A 1 16  ? 16.447 -14.472 8.636   0.40 14.39 ?  16  VAL   A HA   1 
ATOM   393  H  HB   A VAL   A 1 16  ? 14.985 -16.011 6.510   0.60 14.79 ?  16  VAL   A HB   1 
ATOM   394  H  HB   B VAL   A 1 16  ? 14.792 -15.750 6.733   0.40 14.35 ?  16  VAL   A HB   1 
ATOM   395  H  HG11 A VAL   A 1 16  ? 15.303 -14.021 5.179   0.60 15.98 ?  16  VAL   A HG11 1 
ATOM   396  H  HG11 B VAL   A 1 16  ? 15.217 -13.789 5.418   0.40 14.52 ?  16  VAL   A HG11 1 
ATOM   397  H  HG12 A VAL   A 1 16  ? 14.264 -13.868 6.369   0.60 15.98 ?  16  VAL   A HG12 1 
ATOM   398  H  HG12 B VAL   A 1 16  ? 14.252 -13.554 6.657   0.40 14.52 ?  16  VAL   A HG12 1 
ATOM   399  H  HG13 A VAL   A 1 16  ? 15.739 -13.296 6.522   0.60 15.98 ?  16  VAL   A HG13 1 
ATOM   400  H  HG13 B VAL   A 1 16  ? 15.778 -13.115 6.742   0.40 14.52 ?  16  VAL   A HG13 1 
ATOM   401  H  HG21 A VAL   A 1 16  ? 16.857 -15.755 5.099   0.60 15.60 ?  16  VAL   A HG21 1 
ATOM   402  H  HG21 B VAL   A 1 16  ? 16.640 -15.648 5.269   0.40 15.02 ?  16  VAL   A HG21 1 
ATOM   403  H  HG22 A VAL   A 1 16  ? 17.672 -15.186 6.337   0.60 15.60 ?  16  VAL   A HG22 1 
ATOM   404  H  HG22 B VAL   A 1 16  ? 17.538 -15.155 6.483   0.40 15.02 ?  16  VAL   A HG22 1 
ATOM   405  H  HG23 A VAL   A 1 16  ? 17.167 -16.691 6.344   0.60 15.60 ?  16  VAL   A HG23 1 
ATOM   406  H  HG23 B VAL   A 1 16  ? 16.911 -16.614 6.501   0.40 15.02 ?  16  VAL   A HG23 1 
ATOM   407  N  N    A TYR   A 1 17  ? 14.555 -13.506 9.354   0.60 11.12 ?  17  TYR   A N    1 
ATOM   408  N  N    B TYR   A 1 17  ? 14.529 -13.306 9.548   0.40 11.38 ?  17  TYR   A N    1 
ATOM   409  C  CA   A TYR   A 1 17  ? 13.453 -12.821 10.010  0.60 11.19 ?  17  TYR   A CA   1 
ATOM   410  C  CA   B TYR   A 1 17  ? 13.494 -12.646 10.327  0.40 10.69 ?  17  TYR   A CA   1 
ATOM   411  C  C    A TYR   A 1 17  ? 13.191 -11.507 9.280   0.60 10.81 ?  17  TYR   A C    1 
ATOM   412  C  C    B TYR   A 1 17  ? 13.225 -11.289 9.696   0.40 10.45 ?  17  TYR   A C    1 
ATOM   413  O  O    A TYR   A 1 17  ? 14.090 -10.954 8.644   0.60 10.58 ?  17  TYR   A O    1 
ATOM   414  O  O    B TYR   A 1 17  ? 14.132 -10.683 9.125   0.40 10.30 ?  17  TYR   A O    1 
ATOM   415  C  CB   A TYR   A 1 17  ? 13.824 -12.515 11.466  0.60 12.16 ?  17  TYR   A CB   1 
ATOM   416  C  CB   B TYR   A 1 17  ? 13.987 -12.474 11.765  0.40 11.10 ?  17  TYR   A CB   1 
ATOM   417  C  CG   A TYR   A 1 17  ? 13.965 -13.749 12.332  0.60 13.07 ?  17  TYR   A CG   1 
ATOM   418  C  CG   B TYR   A 1 17  ? 14.242 -13.791 12.466  0.40 11.32 ?  17  TYR   A CG   1 
ATOM   419  C  CD1  A TYR   A 1 17  ? 15.114 -14.533 12.288  0.60 14.00 ?  17  TYR   A CD1  1 
ATOM   420  C  CD1  B TYR   A 1 17  ? 15.443 -14.481 12.308  0.40 11.67 ?  17  TYR   A CD1  1 
ATOM   421  C  CD2  A TYR   A 1 17  ? 12.944 -14.137 13.191  0.60 13.14 ?  17  TYR   A CD2  1 
ATOM   422  C  CD2  B TYR   A 1 17  ? 13.274 -14.351 13.283  0.40 11.47 ?  17  TYR   A CD2  1 
ATOM   423  C  CE1  A TYR   A 1 17  ? 15.240 -15.674 13.074  0.60 13.98 ?  17  TYR   A CE1  1 
ATOM   424  C  CE1  B TYR   A 1 17  ? 15.661 -15.695 12.950  0.40 12.21 ?  17  TYR   A CE1  1 
ATOM   425  C  CE2  A TYR   A 1 17  ? 13.061 -15.283 13.983  0.60 13.59 ?  17  TYR   A CE2  1 
ATOM   426  C  CE2  B TYR   A 1 17  ? 13.482 -15.553 13.926  0.40 11.71 ?  17  TYR   A CE2  1 
ATOM   427  C  CZ   A TYR   A 1 17  ? 14.215 -16.046 13.922  0.60 13.53 ?  17  TYR   A CZ   1 
ATOM   428  C  CZ   B TYR   A 1 17  ? 14.671 -16.224 13.761  0.40 11.92 ?  17  TYR   A CZ   1 
ATOM   429  O  OH   A TYR   A 1 17  ? 14.342 -17.180 14.702  0.60 14.06 ?  17  TYR   A OH   1 
ATOM   430  O  OH   B TYR   A 1 17  ? 14.855 -17.422 14.416  0.40 12.18 ?  17  TYR   A OH   1 
ATOM   431  H  H    A TYR   A 1 17  ? 15.252 -13.015 9.277   0.60 13.32 ?  17  TYR   A H    1 
ATOM   432  H  H    B TYR   A 1 17  ? 15.183 -12.771 9.359   0.40 13.64 ?  17  TYR   A H    1 
ATOM   433  H  HA   A TYR   A 1 17  ? 12.656 -13.381 9.984   0.60 13.40 ?  17  TYR   A HA   1 
ATOM   434  H  HA   B TYR   A 1 17  ? 12.675 -13.163 10.324  0.40 12.81 ?  17  TYR   A HA   1 
ATOM   435  H  HB2  A TYR   A 1 17  ? 14.669 -12.046 11.478  0.60 14.57 ?  17  TYR   A HB2  1 
ATOM   436  H  HB2  B TYR   A 1 17  ? 14.819 -11.978 11.753  0.40 13.30 ?  17  TYR   A HB2  1 
ATOM   437  H  HB3  A TYR   A 1 17  ? 13.131 -11.962 11.847  0.60 14.57 ?  17  TYR   A HB3  1 
ATOM   438  H  HB3  B TYR   A 1 17  ? 13.321 -11.993 12.277  0.40 13.30 ?  17  TYR   A HB3  1 
ATOM   439  H  HD1  A TYR   A 1 17  ? 15.808 -14.293 11.718  0.60 16.78 ?  17  TYR   A HD1  1 
ATOM   440  H  HD1  B TYR   A 1 17  ? 16.109 -14.131 11.760  0.40 13.98 ?  17  TYR   A HD1  1 
ATOM   441  H  HD2  A TYR   A 1 17  ? 12.163 -13.630 13.235  0.60 15.75 ?  17  TYR   A HD2  1 
ATOM   442  H  HD2  B TYR   A 1 17  ? 12.468 -13.910 13.401  0.40 13.74 ?  17  TYR   A HD2  1 
ATOM   443  H  HE1  A TYR   A 1 17  ? 16.018 -16.186 13.031  0.60 16.75 ?  17  TYR   A HE1  1 
ATOM   444  H  HE1  B TYR   A 1 17  ? 16.470 -16.151 12.836  0.40 14.63 ?  17  TYR   A HE1  1 
ATOM   445  H  HE2  A TYR   A 1 17  ? 12.366 -15.525 14.554  0.60 16.28 ?  17  TYR   A HE2  1 
ATOM   446  H  HE2  B TYR   A 1 17  ? 12.823 -15.915 14.470  0.40 14.02 ?  17  TYR   A HE2  1 
ATOM   447  H  HH   A TYR   A 1 17  ? 13.586 -17.408 14.992  0.60 16.84 ?  17  TYR   A HH   1 
ATOM   448  H  HH   B TYR   A 1 17  ? 15.611 -17.741 14.225  0.40 14.59 ?  17  TYR   A HH   1 
ATOM   449  N  N    A ILE   A 1 18  ? 11.961 -10.989 9.385   0.60 11.27 ?  18  ILE   A N    1 
ATOM   450  N  N    B ILE   A 1 18  ? 11.983 -10.802 9.789   0.40 10.50 ?  18  ILE   A N    1 
ATOM   451  C  CA   A ILE   A 1 18  ? 11.571 -9.799  8.630   0.60 11.63 ?  18  ILE   A CA   1 
ATOM   452  C  CA   B ILE   A 1 18  ? 11.593 -9.598  9.062   0.40 10.00 ?  18  ILE   A CA   1 
ATOM   453  C  C    A ILE   A 1 18  ? 10.601 -8.949  9.445   0.60 12.34 ?  18  ILE   A C    1 
ATOM   454  C  C    B ILE   A 1 18  ? 10.663 -8.728  9.897   0.40 10.12 ?  18  ILE   A C    1 
ATOM   455  O  O    A ILE   A 1 18  ? 9.787  -9.469  10.212  0.60 12.36 ?  18  ILE   A O    1 
ATOM   456  O  O    B ILE   A 1 18  ? 9.841  -9.225  10.675  0.40 10.35 ?  18  ILE   A O    1 
ATOM   457  C  CB   A ILE   A 1 18  ? 11.013 -10.189 7.239   0.60 11.75 ?  18  ILE   A CB   1 
ATOM   458  C  CB   B ILE   A 1 18  ? 10.970 -9.944  7.691   0.40 9.78  ?  18  ILE   A CB   1 
ATOM   459  C  CG1  A ILE   A 1 18  ? 10.931 -8.969  6.323   0.60 12.35 ?  18  ILE   A CG1  1 
ATOM   460  C  CG1  B ILE   A 1 18  ? 10.958 -8.726  6.767   0.40 10.50 ?  18  ILE   A CG1  1 
ATOM   461  C  CG2  A ILE   A 1 18  ? 9.673  -10.909 7.371   0.60 11.65 ?  18  ILE   A CG2  1 
ATOM   462  C  CG2  B ILE   A 1 18  ? 9.575  -10.541 7.864   0.40 10.07 ?  18  ILE   A CG2  1 
ATOM   463  C  CD1  A ILE   A 1 18  ? 10.680 -9.328  4.877   0.60 14.07 ?  18  ILE   A CD1  1 
ATOM   464  C  CD1  B ILE   A 1 18  ? 10.693 -9.091  5.325   0.40 12.06 ?  18  ILE   A CD1  1 
ATOM   465  H  H    A ILE   A 1 18  ? 11.346 -11.317 9.892   0.60 13.49 ?  18  ILE   A H    1 
ATOM   466  H  H    B ILE   A 1 18  ? 11.355 -11.149 10.268  0.40 12.57 ?  18  ILE   A H    1 
ATOM   467  H  HA   A ILE   A 1 18  ? 12.366 -9.272  8.482   0.60 13.94 ?  18  ILE   A HA   1 
ATOM   468  H  HA   B ILE   A 1 18  ? 12.393 -9.077  8.895   0.40 11.98 ?  18  ILE   A HA   1 
ATOM   469  H  HB   A ILE   A 1 18  ? 11.638 -10.815 6.837   0.60 14.08 ?  18  ILE   A HB   1 
ATOM   470  H  HB   B ILE   A 1 18  ? 11.530 -10.614 7.284   0.40 11.71 ?  18  ILE   A HB   1 
ATOM   471  H  HG12 A ILE   A 1 18  ? 10.209 -8.401  6.623   0.60 14.80 ?  18  ILE   A HG12 1 
ATOM   472  H  HG12 B ILE   A 1 18  ? 10.266 -8.111  7.052   0.40 12.57 ?  18  ILE   A HG12 1 
ATOM   473  H  HG13 A ILE   A 1 18  ? 11.775 -8.490  6.369   0.60 14.80 ?  18  ILE   A HG13 1 
ATOM   474  H  HG13 B ILE   A 1 18  ? 11.826 -8.287  6.807   0.40 12.57 ?  18  ILE   A HG13 1 
ATOM   475  H  HG21 A ILE   A 1 18  ? 9.430  -11.281 6.505   0.60 13.96 ?  18  ILE   A HG21 1 
ATOM   476  H  HG21 B ILE   A 1 18  ? 9.289  -10.913 7.014   0.40 12.06 ?  18  ILE   A HG21 1 
ATOM   477  H  HG22 A ILE   A 1 18  ? 9.761  -11.623 8.021   0.60 13.96 ?  18  ILE   A HG22 1 
ATOM   478  H  HG22 B ILE   A 1 18  ? 9.610  -11.234 8.537   0.40 12.06 ?  18  ILE   A HG22 1 
ATOM   479  H  HG23 A ILE   A 1 18  ? 9.000  -10.277 7.659   0.60 13.96 ?  18  ILE   A HG23 1 
ATOM   480  H  HG23 B ILE   A 1 18  ? 8.959  -9.841  8.139   0.40 12.06 ?  18  ILE   A HG23 1 
ATOM   481  H  HD11 A ILE   A 1 18  ? 10.694 -8.515  4.346   0.60 16.86 ?  18  ILE   A HD11 1 
ATOM   482  H  HD11 B ILE   A 1 18  ? 10.781 -8.298  4.772   0.40 14.45 ?  18  ILE   A HD11 1 
ATOM   483  H  HD12 A ILE   A 1 18  ? 11.373 -9.933  4.574   0.60 16.86 ?  18  ILE   A HD12 1 
ATOM   484  H  HD12 B ILE   A 1 18  ? 11.337 -9.760  5.043   0.40 14.45 ?  18  ILE   A HD12 1 
ATOM   485  H  HD13 A ILE   A 1 18  ? 9.811  -9.754  4.804   0.60 16.86 ?  18  ILE   A HD13 1 
ATOM   486  H  HD13 B ILE   A 1 18  ? 9.794  -9.447  5.249   0.40 14.45 ?  18  ILE   A HD13 1 
ATOM   487  N  N    A LYS   A 1 19  ? 10.686 -7.628  9.259   0.60 12.81 ?  19  LYS   A N    1 
ATOM   488  N  N    B LYS   A 1 19  ? 10.797 -7.410  9.716   0.40 10.28 ?  19  LYS   A N    1 
ATOM   489  C  CA   A LYS   A 1 19  ? 9.885  -6.675  10.021  0.60 13.94 ?  19  LYS   A CA   1 
ATOM   490  C  CA   B LYS   A 1 19  ? 10.005 -6.440  10.459  0.40 11.72 ?  19  LYS   A CA   1 
ATOM   491  C  C    A LYS   A 1 19  ? 9.695  -5.405  9.204   0.60 14.22 ?  19  LYS   A C    1 
ATOM   492  C  C    B LYS   A 1 19  ? 9.785  -5.207  9.592   0.40 12.16 ?  19  LYS   A C    1 
ATOM   493  O  O    A LYS   A 1 19  ? 10.568 -5.020  8.422   0.60 13.66 ?  19  LYS   A O    1 
ATOM   494  O  O    B LYS   A 1 19  ? 10.691 -4.786  8.868   0.40 11.83 ?  19  LYS   A O    1 
ATOM   495  C  CB   A LYS   A 1 19  ? 10.612 -6.320  11.327  0.60 15.26 ?  19  LYS   A CB   1 
ATOM   496  C  CB   B LYS   A 1 19  ? 10.726 -6.047  11.755  0.40 12.53 ?  19  LYS   A CB   1 
ATOM   497  C  CG   A LYS   A 1 19  ? 9.917  -5.340  12.281  0.60 16.64 ?  19  LYS   A CG   1 
ATOM   498  C  CG   B LYS   A 1 19  ? 9.912  -5.180  12.678  0.40 14.06 ?  19  LYS   A CG   1 
ATOM   499  C  CD   A LYS   A 1 19  ? 10.811 -5.113  13.516  0.60 17.45 ?  19  LYS   A CD   1 
ATOM   500  C  CD   B LYS   A 1 19  ? 10.718 -4.809  13.896  0.40 15.58 ?  19  LYS   A CD   1 
ATOM   501  C  CE   A LYS   A 1 19  ? 10.216 -4.152  14.546  0.60 18.34 ?  19  LYS   A CE   1 
ATOM   502  C  CE   B LYS   A 1 19  ? 9.931  -3.895  14.804  0.40 16.57 ?  19  LYS   A CE   1 
ATOM   503  N  NZ   A LYS   A 1 19  ? 11.114 -3.984  15.738  0.60 18.35 ?  19  LYS   A NZ   1 
ATOM   504  N  NZ   B LYS   A 1 19  ? 10.761 -3.445  15.943  0.40 17.18 ?  19  LYS   A NZ   1 
ATOM   505  H  H    A LYS   A 1 19  ? 11.211 -7.266  8.687   0.60 15.34 ?  19  LYS   A H    1 
ATOM   506  H  H    B LYS   A 1 19  ? 11.353 -7.042  9.162   0.40 12.32 ?  19  LYS   A H    1 
ATOM   507  H  HA   A LYS   A 1 19  ? 9.016  -7.066  10.226  0.60 16.71 ?  19  LYS   A HA   1 
ATOM   508  H  HA   B LYS   A 1 19  ? 9.147  -6.821  10.691  0.40 14.05 ?  19  LYS   A HA   1 
ATOM   509  H  HB2  A LYS   A 1 19  ? 10.753 -7.142  11.816  0.60 18.28 ?  19  LYS   A HB2  1 
ATOM   510  H  HB2  B LYS   A 1 19  ? 10.955 -6.854  12.248  0.40 15.01 ?  19  LYS   A HB2  1 
ATOM   511  H  HB3  A LYS   A 1 19  ? 11.465 -5.933  11.089  0.60 18.28 ?  19  LYS   A HB3  1 
ATOM   512  H  HB3  B LYS   A 1 19  ? 11.536 -5.559  11.537  0.40 15.01 ?  19  LYS   A HB3  1 
ATOM   513  H  HG2  A LYS   A 1 19  ? 9.780  -4.487  11.839  0.60 19.94 ?  19  LYS   A HG2  1 
ATOM   514  H  HG2  B LYS   A 1 19  ? 9.659  -4.365  12.220  0.40 16.85 ?  19  LYS   A HG2  1 
ATOM   515  H  HG3  A LYS   A 1 19  ? 9.068  -5.710  12.576  0.60 19.94 ?  19  LYS   A HG3  1 
ATOM   516  H  HG3  B LYS   A 1 19  ? 9.124  -5.667  12.969  0.40 16.85 ?  19  LYS   A HG3  1 
ATOM   517  H  HD2  A LYS   A 1 19  ? 10.954 -5.964  13.960  0.60 20.91 ?  19  LYS   A HD2  1 
ATOM   518  H  HD2  B LYS   A 1 19  ? 10.943 -5.615  14.390  0.40 18.68 ?  19  LYS   A HD2  1 
ATOM   519  H  HD3  A LYS   A 1 19  ? 11.659 -4.746  13.228  0.60 20.91 ?  19  LYS   A HD3  1 
ATOM   520  H  HD3  B LYS   A 1 19  ? 11.525 -4.349  13.619  0.40 18.68 ?  19  LYS   A HD3  1 
ATOM   521  H  HE2  A LYS   A 1 19  ? 10.094 -3.279  14.141  0.60 21.98 ?  19  LYS   A HE2  1 
ATOM   522  H  HE2  B LYS   A 1 19  ? 9.644  -3.117  14.300  0.40 19.86 ?  19  LYS   A HE2  1 
ATOM   523  H  HE3  A LYS   A 1 19  ? 9.366  -4.497  14.860  0.60 21.98 ?  19  LYS   A HE3  1 
ATOM   524  H  HE3  B LYS   A 1 19  ? 9.162  -4.375  15.150  0.40 19.86 ?  19  LYS   A HE3  1 
ATOM   525  H  HZ1  A LYS   A 1 19  ? 10.760 -3.400  16.310  0.60 22.00 ?  19  LYS   A HZ1  1 
ATOM   526  H  HZ1  B LYS   A 1 19  ? 10.285 -2.908  16.468  0.40 20.59 ?  19  LYS   A HZ1  1 
ATOM   527  H  HZ2  A LYS   A 1 19  ? 11.218 -4.765  16.154  0.60 22.00 ?  19  LYS   A HZ2  1 
ATOM   528  H  HZ2  B LYS   A 1 19  ? 11.034 -4.148  16.415  0.40 20.59 ?  19  LYS   A HZ2  1 
ATOM   529  H  HZ3  A LYS   A 1 19  ? 11.912 -3.687  15.480  0.60 22.00 ?  19  LYS   A HZ3  1 
ATOM   530  H  HZ3  B LYS   A 1 19  ? 11.472 -3.003  15.642  0.40 20.59 ?  19  LYS   A HZ3  1 
ATOM   531  N  N    A ASN   A 1 20  ? 8.546  -4.751  9.394   0.60 15.17 ?  20  ASN   A N    1 
ATOM   532  N  N    B ASN   A 1 20  ? 8.578  -4.640  9.657   0.40 13.36 ?  20  ASN   A N    1 
ATOM   533  C  CA   A ASN   A 1 20  ? 8.330  -3.412  8.854   0.60 16.32 ?  20  ASN   A CA   1 
ATOM   534  C  CA   B ASN   A 1 20  ? 8.269  -3.375  8.984   0.40 14.57 ?  20  ASN   A CA   1 
ATOM   535  C  C    A ASN   A 1 20  ? 8.952  -2.421  9.828   0.60 16.76 ?  20  ASN   A C    1 
ATOM   536  C  C    B ASN   A 1 20  ? 8.850  -2.248  9.825   0.40 15.12 ?  20  ASN   A C    1 
ATOM   537  O  O    A ASN   A 1 20  ? 8.437  -2.216  10.931  0.60 17.00 ?  20  ASN   A O    1 
ATOM   538  O  O    B ASN   A 1 20  ? 8.220  -1.780  10.777  0.40 15.64 ?  20  ASN   A O    1 
ATOM   539  C  CB   A ASN   A 1 20  ? 6.840  -3.144  8.654   0.60 16.89 ?  20  ASN   A CB   1 
ATOM   540  C  CB   B ASN   A 1 20  ? 6.759  -3.213  8.823   0.40 15.20 ?  20  ASN   A CB   1 
ATOM   541  C  CG   A ASN   A 1 20  ? 6.533  -1.676  8.379   0.60 17.78 ?  20  ASN   A CG   1 
ATOM   542  C  CG   B ASN   A 1 20  ? 6.358  -1.937  8.068   0.40 15.79 ?  20  ASN   A CG   1 
ATOM   543  O  OD1  A ASN   A 1 20  ? 5.626  -1.101  8.982   0.60 19.37 ?  20  ASN   A OD1  1 
ATOM   544  O  OD1  B ASN   A 1 20  ? 5.210  -1.480  8.173   0.40 15.76 ?  20  ASN   A OD1  1 
ATOM   545  N  ND2  A ASN   A 1 20  ? 7.287  -1.067  7.471   0.60 17.51 ?  20  ASN   A ND2  1 
ATOM   546  N  ND2  B ASN   A 1 20  ? 7.289  -1.366  7.305   0.40 16.86 ?  20  ASN   A ND2  1 
ATOM   547  H  H    A ASN   A 1 20  ? 7.878  -5.063  9.843   0.60 18.18 ?  20  ASN   A H    1 
ATOM   548  H  H    B ASN   A 1 20  ? 7.912  -4.980  10.078  0.40 16.00 ?  20  ASN   A H    1 
ATOM   549  H  HA   A ASN   A 1 20  ? 8.776  -3.332  8.000   0.60 19.56 ?  20  ASN   A HA   1 
ATOM   550  H  HA   B ASN   A 1 20  ? 8.689  -3.366  8.110   0.40 17.45 ?  20  ASN   A HA   1 
ATOM   551  H  HB2  A ASN   A 1 20  ? 6.526  -3.665  7.897   0.60 20.24 ?  20  ASN   A HB2  1 
ATOM   552  H  HB2  B ASN   A 1 20  ? 6.408  -3.970  8.340   0.40 18.21 ?  20  ASN   A HB2  1 
ATOM   553  H  HB3  A ASN   A 1 20  ? 6.361  -3.407  9.456   0.60 20.24 ?  20  ASN   A HB3  1 
ATOM   554  H  HB3  B ASN   A 1 20  ? 6.357  -3.173  9.704   0.40 18.21 ?  20  ASN   A HB3  1 
ATOM   555  H  HD21 A ASN   A 1 20  ? 7.148  -0.243  7.284   0.60 20.98 ?  20  ASN   A HD21 1 
ATOM   556  H  HD21 B ASN   A 1 20  ? 7.104  -0.651  6.869   0.40 20.21 ?  20  ASN   A HD21 1 
ATOM   557  H  HD22 A ASN   A 1 20  ? 7.916  -1.502  7.074   0.60 20.98 ?  20  ASN   A HD22 1 
ATOM   558  H  HD22 B ASN   A 1 20  ? 8.078  -1.705  7.246   0.40 20.21 ?  20  ASN   A HD22 1 
ATOM   559  N  N    A ALA   A 1 21  ? 10.081 -1.834  9.444   0.60 16.90 ?  21  ALA   A N    1 
ATOM   560  N  N    B ALA   A 1 21  ? 10.058 -1.807  9.477   0.40 15.37 ?  21  ALA   A N    1 
ATOM   561  C  CA   A ALA   A 1 21  ? 10.783 -0.948  10.358  0.60 16.86 ?  21  ALA   A CA   1 
ATOM   562  C  CA   B ALA   A 1 21  ? 10.720 -0.761  10.241  0.40 15.57 ?  21  ALA   A CA   1 
ATOM   563  C  C    A ALA   A 1 21  ? 11.741 -0.068  9.576   0.60 16.65 ?  21  ALA   A C    1 
ATOM   564  C  C    B ALA   A 1 21  ? 11.823 -0.132  9.402   0.40 14.80 ?  21  ALA   A C    1 
ATOM   565  O  O    A ALA   A 1 21  ? 12.171 -0.411  8.472   0.60 16.50 ?  21  ALA   A O    1 
ATOM   566  O  O    B ALA   A 1 21  ? 12.368 -0.760  8.492   0.40 14.73 ?  21  ALA   A O    1 
ATOM   567  C  CB   A ALA   A 1 21  ? 11.545 -1.737  11.425  0.60 17.51 ?  21  ALA   A CB   1 
ATOM   568  C  CB   B ALA   A 1 21  ? 11.296 -1.307  11.554  0.40 16.62 ?  21  ALA   A CB   1 
ATOM   569  H  H    A ALA   A 1 21  ? 10.453 -1.934  8.674   0.60 20.25 ?  21  ALA   A H    1 
ATOM   570  H  H    B ALA   A 1 21  ? 10.510 -2.094  8.803   0.40 18.42 ?  21  ALA   A H    1 
ATOM   571  H  HA   A ALA   A 1 21  ? 10.136 -0.376  10.802  0.60 20.21 ?  21  ALA   A HA   1 
ATOM   572  H  HA   B ALA   A 1 21  ? 10.077 -0.070  10.460  0.40 18.66 ?  21  ALA   A HA   1 
ATOM   573  H  HB1  A ALA   A 1 21  ? 11.959 -1.109  12.034  0.60 20.99 ?  21  ALA   A HB1  1 
ATOM   574  H  HB1  B ALA   A 1 21  ? 11.726 -0.584  12.037  0.40 19.92 ?  21  ALA   A HB1  1 
ATOM   575  H  HB2  A ALA   A 1 21  ? 10.915 -2.299  11.904  0.60 20.99 ?  21  ALA   A HB2  1 
ATOM   576  H  HB2  B ALA   A 1 21  ? 10.572 -1.674  12.089  0.40 19.92 ?  21  ALA   A HB2  1 
ATOM   577  H  HB3  A ALA   A 1 21  ? 12.216 -2.282  10.992  0.60 20.99 ?  21  ALA   A HB3  1 
ATOM   578  H  HB3  B ALA   A 1 21  ? 11.942 -2.002  11.354  0.40 19.92 ?  21  ALA   A HB3  1 
ATOM   579  N  N    A ASP   A 1 22  ? 12.046 1.086   10.167  0.60 16.67 ?  22  ASP   A N    1 
ATOM   580  N  N    B ASP   A 1 22  ? 12.111 1.132   9.706   0.40 14.26 ?  22  ASP   A N    1 
ATOM   581  C  CA   A ASP   A 1 22  ? 13.089 1.978   9.677   0.60 16.70 ?  22  ASP   A CA   1 
ATOM   582  C  CA   B ASP   A 1 22  ? 13.280 1.817   9.168   0.40 14.08 ?  22  ASP   A CA   1 
ATOM   583  C  C    A ASP   A 1 22  ? 14.418 1.477   10.228  0.60 15.40 ?  22  ASP   A C    1 
ATOM   584  C  C    B ASP   A 1 22  ? 14.535 1.221   9.796   0.40 13.00 ?  22  ASP   A C    1 
ATOM   585  O  O    A ASP   A 1 22  ? 14.635 1.489   11.443  0.60 15.83 ?  22  ASP   A O    1 
ATOM   586  O  O    B ASP   A 1 22  ? 14.647 1.145   11.022  0.40 12.80 ?  22  ASP   A O    1 
ATOM   587  C  CB   A ASP   A 1 22  ? 12.798 3.397   10.158  0.60 18.05 ?  22  ASP   A CB   1 
ATOM   588  C  CB   B ASP   A 1 22  ? 13.168 3.304   9.526   0.40 15.17 ?  22  ASP   A CB   1 
ATOM   589  C  CG   A ASP   A 1 22  ? 13.811 4.418   9.658   0.60 19.43 ?  22  ASP   A CG   1 
ATOM   590  C  CG   B ASP   A 1 22  ? 14.231 4.169   8.868   0.40 16.06 ?  22  ASP   A CG   1 
ATOM   591  O  OD1  A ASP   A 1 22  ? 14.863 4.033   9.109   0.60 19.49 ?  22  ASP   A OD1  1 
ATOM   592  O  OD1  B ASP   A 1 22  ? 15.266 3.634   8.424   0.40 15.64 ?  22  ASP   A OD1  1 
ATOM   593  O  OD2  A ASP   A 1 22  ? 13.552 5.627   9.824   0.60 20.75 -1 22  ASP   A OD2  1 
ATOM   594  O  OD2  B ASP   A 1 22  ? 14.030 5.402   8.809   0.40 17.22 -1 22  ASP   A OD2  1 
ATOM   595  H  H    A ASP   A 1 22  ? 11.638 1.386   10.864  0.60 19.98 ?  22  ASP   A H    1 
ATOM   596  H  H    B ASP   A 1 22  ? 11.623 1.623   10.217  0.40 17.09 ?  22  ASP   A H    1 
ATOM   597  H  HA   A ASP   A 1 22  ? 13.116 1.962   8.706   0.60 20.02 ?  22  ASP   A HA   1 
ATOM   598  H  HA   B ASP   A 1 22  ? 13.317 1.714   8.203   0.40 16.87 ?  22  ASP   A HA   1 
ATOM   599  H  HB2  A ASP   A 1 22  ? 11.917 3.661   9.848   0.60 21.64 ?  22  ASP   A HB2  1 
ATOM   600  H  HB2  B ASP   A 1 22  ? 12.302 3.630   9.240   0.40 18.18 ?  22  ASP   A HB2  1 
ATOM   601  H  HB3  A ASP   A 1 22  ? 12.823 3.408   11.129  0.60 21.64 ?  22  ASP   A HB3  1 
ATOM   602  H  HB3  B ASP   A 1 22  ? 13.258 3.398   10.487  0.40 18.18 ?  22  ASP   A HB3  1 
ATOM   603  N  N    A ILE   A 1 23  ? 15.303 1.028   9.335   0.60 14.51 ?  23  ILE   A N    1 
ATOM   604  N  N    B ILE   A 1 23  ? 15.480 0.783   8.955   0.40 12.70 ?  23  ILE   A N    1 
ATOM   605  C  CA   A ILE   A 1 23  ? 16.572 0.442   9.762   0.60 13.79 ?  23  ILE   A CA   1 
ATOM   606  C  CA   B ILE   A 1 23  ? 16.705 0.170   9.471   0.40 12.14 ?  23  ILE   A CA   1 
ATOM   607  C  C    A ILE   A 1 23  ? 17.372 1.416   10.614  0.60 13.97 ?  23  ILE   A C    1 
ATOM   608  C  C    B ILE   A 1 23  ? 17.440 1.124   10.400  0.40 12.77 ?  23  ILE   A C    1 
ATOM   609  O  O    A ILE   A 1 23  ? 18.118 1.000   11.509  0.60 14.22 ?  23  ILE   A O    1 
ATOM   610  O  O    B ILE   A 1 23  ? 18.088 0.692   11.362  0.40 12.50 ?  23  ILE   A O    1 
ATOM   611  C  CB   A ILE   A 1 23  ? 17.365 -0.066  8.539   0.60 13.46 ?  23  ILE   A CB   1 
ATOM   612  C  CB   B ILE   A 1 23  ? 17.611 -0.346  8.327   0.40 11.62 ?  23  ILE   A CB   1 
ATOM   613  C  CG1  A ILE   A 1 23  ? 18.558 -0.912  8.989   0.60 13.78 ?  23  ILE   A CG1  1 
ATOM   614  C  CG1  B ILE   A 1 23  ? 18.677 -1.297  8.888   0.40 11.55 ?  23  ILE   A CG1  1 
ATOM   615  C  CG2  A ILE   A 1 23  ? 17.802 1.098   7.653   0.60 13.32 ?  23  ILE   A CG2  1 
ATOM   616  C  CG2  B ILE   A 1 23  ? 18.265 0.810   7.573   0.40 11.47 ?  23  ILE   A CG2  1 
ATOM   617  C  CD1  A ILE   A 1 23  ? 19.271 -1.603  7.851   0.60 13.82 ?  23  ILE   A CD1  1 
ATOM   618  C  CD1  B ILE   A 1 23  ? 19.556 -1.950  7.831   0.40 11.54 ?  23  ILE   A CD1  1 
ATOM   619  H  H    A ILE   A 1 23  ? 15.188 1.049   8.488   0.60 17.39 ?  23  ILE   A H    1 
ATOM   620  H  H    B ILE   A 1 23  ? 15.437 0.827   8.104   0.40 15.21 ?  23  ILE   A H    1 
ATOM   621  H  HA   A ILE   A 1 23  ? 16.379 -0.328  10.316  0.60 16.52 ?  23  ILE   A HA   1 
ATOM   622  H  HA   B ILE   A 1 23  ? 16.455 -0.603  9.998   0.40 14.55 ?  23  ILE   A HA   1 
ATOM   623  H  HB   A ILE   A 1 23  ? 16.776 -0.631  8.017   0.60 16.12 ?  23  ILE   A HB   1 
ATOM   624  H  HB   B ILE   A 1 23  ? 17.063 -0.847  7.703   0.40 13.92 ?  23  ILE   A HB   1 
ATOM   625  H  HG12 A ILE   A 1 23  ? 19.199 -0.340  9.437   0.60 16.51 ?  23  ILE   A HG12 1 
ATOM   626  H  HG12 B ILE   A 1 23  ? 19.259 -0.800  9.484   0.40 13.84 ?  23  ILE   A HG12 1 
ATOM   627  H  HG13 A ILE   A 1 23  ? 18.242 -1.597  9.599   0.60 16.51 ?  23  ILE   A HG13 1 
ATOM   628  H  HG13 B ILE   A 1 23  ? 18.237 -2.008  9.380   0.40 13.84 ?  23  ILE   A HG13 1 
ATOM   629  H  HG21 A ILE   A 1 23  ? 18.153 0.748   6.819   0.60 15.95 ?  23  ILE   A HG21 1 
ATOM   630  H  HG21 B ILE   A 1 23  ? 18.654 0.471   6.748   0.40 13.74 ?  23  ILE   A HG21 1 
ATOM   631  H  HG22 A ILE   A 1 23  ? 17.033 1.665   7.471   0.60 15.95 ?  23  ILE   A HG22 1 
ATOM   632  H  HG22 B ILE   A 1 23  ? 17.592 1.475   7.370   0.40 13.74 ?  23  ILE   A HG22 1 
ATOM   633  H  HG23 A ILE   A 1 23  ? 18.486 1.610   8.111   0.60 15.95 ?  23  ILE   A HG23 1 
ATOM   634  H  HG23 B ILE   A 1 23  ? 18.961 1.199   8.126   0.40 13.74 ?  23  ILE   A HG23 1 
ATOM   635  H  HD11 A ILE   A 1 23  ? 19.956 -2.183  8.217   0.60 16.55 ?  23  ILE   A HD11 1 
ATOM   636  H  HD11 B ILE   A 1 23  ? 20.143 -2.595  8.262   0.40 13.83 ?  23  ILE   A HD11 1 
ATOM   637  H  HD12 A ILE   A 1 23  ? 18.627 -2.125  7.348   0.60 16.55 ?  23  ILE   A HD12 1 
ATOM   638  H  HD12 B ILE   A 1 23  ? 18.992 -2.401  7.185   0.40 13.83 ?  23  ILE   A HD12 1 
ATOM   639  H  HD13 A ILE   A 1 23  ? 19.674 -0.932  7.279   0.60 16.55 ?  23  ILE   A HD13 1 
ATOM   640  H  HD13 B ILE   A 1 23  ? 20.085 -1.267  7.391   0.40 13.83 ?  23  ILE   A HD13 1 
ATOM   641  N  N    A VAL   A 1 24  ? 17.227 2.719   10.366  0.60 14.37 ?  24  VAL   A N    1 
ATOM   642  N  N    B VAL   A 1 24  ? 17.342 2.429   10.144  0.40 13.80 ?  24  VAL   A N    1 
ATOM   643  C  CA   A VAL   A 1 24  ? 17.902 3.712   11.200  0.60 15.42 ?  24  VAL   A CA   1 
ATOM   644  C  CA   B VAL   A 1 24  ? 18.001 3.408   11.002  0.40 14.95 ?  24  VAL   A CA   1 
ATOM   645  C  C    A VAL   A 1 24  ? 17.411 3.614   12.638  0.60 16.24 ?  24  VAL   A C    1 
ATOM   646  C  C    B VAL   A 1 24  ? 17.397 3.381   12.399  0.40 15.82 ?  24  VAL   A C    1 
ATOM   647  O  O    A VAL   A 1 24  ? 18.204 3.536   13.584  0.60 16.54 ?  24  VAL   A O    1 
ATOM   648  O  O    B VAL   A 1 24  ? 18.116 3.423   13.404  0.40 16.36 ?  24  VAL   A O    1 
ATOM   649  C  CB   A VAL   A 1 24  ? 17.695 5.125   10.625  0.60 16.07 ?  24  VAL   A CB   1 
ATOM   650  C  CB   B VAL   A 1 24  ? 17.922 4.806   10.362  0.40 15.70 ?  24  VAL   A CB   1 
ATOM   651  C  CG1  A VAL   A 1 24  ? 18.200 6.180   11.603  0.60 16.66 ?  24  VAL   A CG1  1 
ATOM   652  C  CG1  B VAL   A 1 24  ? 18.561 5.841   11.267  0.40 16.73 ?  24  VAL   A CG1  1 
ATOM   653  C  CG2  A VAL   A 1 24  ? 18.388 5.261   9.275   0.60 16.54 ?  24  VAL   A CG2  1 
ATOM   654  C  CG2  B VAL   A 1 24  ? 18.590 4.789   9.000   0.40 16.00 ?  24  VAL   A CG2  1 
ATOM   655  H  H    A VAL   A 1 24  ? 16.751 3.049   9.730   0.60 17.22 ?  24  VAL   A H    1 
ATOM   656  H  H    B VAL   A 1 24  ? 16.903 2.766   9.491   0.40 16.53 ?  24  VAL   A H    1 
ATOM   657  H  HA   A VAL   A 1 24  ? 18.853 3.531   11.198  0.60 18.48 ?  24  VAL   A HA   1 
ATOM   658  H  HA   B VAL   A 1 24  ? 18.937 3.174   11.083  0.40 17.91 ?  24  VAL   A HA   1 
ATOM   659  H  HB   A VAL   A 1 24  ? 16.747 5.276   10.486  0.60 19.26 ?  24  VAL   A HB   1 
ATOM   660  H  HB   B VAL   A 1 24  ? 16.990 5.046   10.237  0.40 18.82 ?  24  VAL   A HB   1 
ATOM   661  H  HG11 A VAL   A 1 24  ? 18.322 7.017   11.127  0.60 19.96 ?  24  VAL   A HG11 1 
ATOM   662  H  HG11 B VAL   A 1 24  ? 18.692 6.659   10.763  0.40 20.05 ?  24  VAL   A HG11 1 
ATOM   663  H  HG12 A VAL   A 1 24  ? 17.549 6.295   12.311  0.60 19.96 ?  24  VAL   A HG12 1 
ATOM   664  H  HG12 B VAL   A 1 24  ? 17.971 6.007   12.018  0.40 20.05 ?  24  VAL   A HG12 1 
ATOM   665  H  HG13 A VAL   A 1 24  ? 19.048 5.886   11.972  0.60 19.96 ?  24  VAL   A HG13 1 
ATOM   666  H  HG13 B VAL   A 1 24  ? 19.414 5.503   11.579  0.40 20.05 ?  24  VAL   A HG13 1 
ATOM   667  H  HG21 A VAL   A 1 24  ? 18.155 6.118   8.884   0.60 19.83 ?  24  VAL   A HG21 1 
ATOM   668  H  HG21 B VAL   A 1 24  ? 18.686 5.699   8.685   0.40 19.17 ?  24  VAL   A HG21 1 
ATOM   669  H  HG22 A VAL   A 1 24  ? 19.348 5.210   9.406   0.60 19.83 ?  24  VAL   A HG22 1 
ATOM   670  H  HG22 B VAL   A 1 24  ? 19.463 4.374   9.086   0.40 19.17 ?  24  VAL   A HG22 1 
ATOM   671  H  HG23 A VAL   A 1 24  ? 18.094 4.542   8.693   0.60 19.83 ?  24  VAL   A HG23 1 
ATOM   672  H  HG23 B VAL   A 1 24  ? 18.042 4.277   8.385   0.40 19.17 ?  24  VAL   A HG23 1 
ATOM   673  N  N    A GLU   A 1 25  ? 16.089 3.626   12.821  0.60 17.24 ?  25  GLU   A N    1 
ATOM   674  N  N    B GLU   A 1 25  ? 16.068 3.297   12.485  0.40 16.53 ?  25  GLU   A N    1 
ATOM   675  C  CA   A GLU   A 1 25  ? 15.528 3.553   14.166  0.60 18.69 ?  25  GLU   A CA   1 
ATOM   676  C  CA   B GLU   A 1 25  ? 15.416 3.246   13.790  0.40 17.69 ?  25  GLU   A CA   1 
ATOM   677  C  C    A GLU   A 1 25  ? 15.769 2.187   14.797  0.60 17.96 ?  25  GLU   A C    1 
ATOM   678  C  C    B GLU   A 1 25  ? 15.686 1.919   14.492  0.40 17.58 ?  25  GLU   A C    1 
ATOM   679  O  O    A GLU   A 1 25  ? 15.998 2.091   16.008  0.60 18.56 ?  25  GLU   A O    1 
ATOM   680  O  O    B GLU   A 1 25  ? 15.898 1.889   15.710  0.40 17.90 ?  25  GLU   A O    1 
ATOM   681  C  CB   A GLU   A 1 25  ? 14.038 3.901   14.131  0.60 20.99 ?  25  GLU   A CB   1 
ATOM   682  C  CB   B GLU   A 1 25  ? 13.917 3.511   13.639  0.40 19.10 ?  25  GLU   A CB   1 
ATOM   683  C  CG   A GLU   A 1 25  ? 13.770 5.351   13.749  0.60 23.44 ?  25  GLU   A CG   1 
ATOM   684  C  CG   B GLU   A 1 25  ? 13.601 4.896   13.091  0.40 21.25 ?  25  GLU   A CG   1 
ATOM   685  C  CD   A GLU   A 1 25  ? 14.544 6.335   14.613  0.60 25.61 ?  25  GLU   A CD   1 
ATOM   686  C  CD   B GLU   A 1 25  ? 14.118 6.004   13.983  0.40 23.18 ?  25  GLU   A CD   1 
ATOM   687  O  OE1  A GLU   A 1 25  ? 14.608 6.129   15.844  0.60 26.31 ?  25  GLU   A OE1  1 
ATOM   688  O  OE1  B GLU   A 1 25  ? 14.111 5.821   15.219  0.40 24.23 ?  25  GLU   A OE1  1 
ATOM   689  O  OE2  A GLU   A 1 25  ? 15.110 7.299   14.057  0.60 26.65 -1 25  GLU   A OE2  1 
ATOM   690  O  OE2  B GLU   A 1 25  ? 14.537 7.051   13.449  0.40 23.81 -1 25  GLU   A OE2  1 
ATOM   691  H  H    A GLU   A 1 25  ? 15.507 3.692   12.190  0.60 20.66 ?  25  GLU   A H    1 
ATOM   692  H  H    B GLU   A 1 25  ? 15.531 3.270   11.814  0.40 19.81 ?  25  GLU   A H    1 
ATOM   693  H  HA   A GLU   A 1 25  ? 15.973 4.207   14.722  0.60 22.40 ?  25  GLU   A HA   1 
ATOM   694  H  HA   B GLU   A 1 25  ? 15.785 3.946   14.347  0.40 21.20 ?  25  GLU   A HA   1 
ATOM   695  H  HB2  A GLU   A 1 25  ? 13.592 3.339   13.477  0.60 25.17 ?  25  GLU   A HB2  1 
ATOM   696  H  HB2  B GLU   A 1 25  ? 13.539 2.861   13.027  0.40 22.90 ?  25  GLU   A HB2  1 
ATOM   697  H  HB3  A GLU   A 1 25  ? 13.656 3.754   15.009  0.60 25.17 ?  25  GLU   A HB3  1 
ATOM   698  H  HB3  B GLU   A 1 25  ? 13.493 3.434   14.508  0.40 22.90 ?  25  GLU   A HB3  1 
ATOM   699  H  HG2  A GLU   A 1 25  ? 14.041 5.493   12.829  0.60 28.11 ?  25  GLU   A HG2  1 
ATOM   700  H  HG2  B GLU   A 1 25  ? 14.013 4.996   12.219  0.40 25.48 ?  25  GLU   A HG2  1 
ATOM   701  H  HG3  A GLU   A 1 25  ? 12.820 5.535   13.847  0.60 28.11 ?  25  GLU   A HG3  1 
ATOM   702  H  HG3  B GLU   A 1 25  ? 12.640 5.001   13.020  0.40 25.48 ?  25  GLU   A HG3  1 
ATOM   703  N  N    A GLU   A 1 26  ? 15.735 1.120   13.995  0.60 17.78 ?  26  GLU   A N    1 
ATOM   704  N  N    B GLU   A 1 26  ? 15.700 0.813   13.743  0.40 17.68 ?  26  GLU   A N    1 
ATOM   705  C  CA   A GLU   A 1 26  ? 16.039 -0.208  14.523  0.60 17.17 ?  26  GLU   A CA   1 
ATOM   706  C  CA   B GLU   A 1 26  ? 16.065 -0.470  14.335  0.40 17.84 ?  26  GLU   A CA   1 
ATOM   707  C  C    A GLU   A 1 26  ? 17.464 -0.267  15.057  0.60 16.24 ?  26  GLU   A C    1 
ATOM   708  C  C    B GLU   A 1 26  ? 17.496 -0.445  14.856  0.40 17.10 ?  26  GLU   A C    1 
ATOM   709  O  O    A GLU   A 1 26  ? 17.704 -0.745  16.171  0.60 16.25 ?  26  GLU   A O    1 
ATOM   710  O  O    B GLU   A 1 26  ? 17.796 -1.036  15.900  0.40 17.11 ?  26  GLU   A O    1 
ATOM   711  C  CB   A GLU   A 1 26  ? 15.850 -1.264  13.434  0.60 18.31 ?  26  GLU   A CB   1 
ATOM   712  C  CB   B GLU   A 1 26  ? 15.899 -1.594  13.311  0.40 19.03 ?  26  GLU   A CB   1 
ATOM   713  C  CG   A GLU   A 1 26  ? 14.444 -1.795  13.290  0.60 20.38 ?  26  GLU   A CG   1 
ATOM   714  C  CG   B GLU   A 1 26  ? 14.465 -2.006  13.075  0.40 20.10 ?  26  GLU   A CG   1 
ATOM   715  C  CD   A GLU   A 1 26  ? 13.999 -2.622  14.486  0.60 21.28 ?  26  GLU   A CD   1 
ATOM   716  C  CD   B GLU   A 1 26  ? 13.793 -2.515  14.326  0.40 20.51 ?  26  GLU   A CD   1 
ATOM   717  O  OE1  A GLU   A 1 26  ? 14.430 -3.792  14.638  0.60 21.41 ?  26  GLU   A OE1  1 
ATOM   718  O  OE1  B GLU   A 1 26  ? 14.379 -3.378  15.014  0.40 20.83 ?  26  GLU   A OE1  1 
ATOM   719  O  OE2  A GLU   A 1 26  ? 13.209 -2.091  15.283  0.60 22.05 -1 26  GLU   A OE2  1 
ATOM   720  O  OE2  B GLU   A 1 26  ? 12.683 -2.035  14.623  0.40 19.99 -1 26  GLU   A OE2  1 
ATOM   721  H  H    A GLU   A 1 26  ? 15.551 1.142   13.155  0.60 21.31 ?  26  GLU   A H    1 
ATOM   722  H  H    B GLU   A 1 26  ? 15.506 0.780   12.907  0.40 21.19 ?  26  GLU   A H    1 
ATOM   723  H  HA   A GLU   A 1 26  ? 15.433 -0.402  15.252  0.60 20.58 ?  26  GLU   A HA   1 
ATOM   724  H  HA   B GLU   A 1 26  ? 15.482 -0.652  15.086  0.40 21.38 ?  26  GLU   A HA   1 
ATOM   725  H  HB2  A GLU   A 1 26  ? 16.107 -0.876  12.582  0.60 21.94 ?  26  GLU   A HB2  1 
ATOM   726  H  HB2  B GLU   A 1 26  ? 16.263 -1.299  12.461  0.40 22.82 ?  26  GLU   A HB2  1 
ATOM   727  H  HB3  A GLU   A 1 26  ? 16.428 -2.015  13.636  0.60 21.94 ?  26  GLU   A HB3  1 
ATOM   728  H  HB3  B GLU   A 1 26  ? 16.386 -2.375  13.620  0.40 22.82 ?  26  GLU   A HB3  1 
ATOM   729  H  HG2  A GLU   A 1 26  ? 13.839 -1.041  13.190  0.60 24.43 ?  26  GLU   A HG2  1 
ATOM   730  H  HG2  B GLU   A 1 26  ? 13.962 -1.240  12.764  0.40 24.10 ?  26  GLU   A HG2  1 
ATOM   731  H  HG3  A GLU   A 1 26  ? 14.401 -2.359  12.504  0.60 24.43 ?  26  GLU   A HG3  1 
ATOM   732  H  HG3  B GLU   A 1 26  ? 14.441 -2.715  12.417  0.40 24.10 ?  26  GLU   A HG3  1 
ATOM   733  N  N    A ALA   A 1 27  ? 18.429 0.214   14.268  0.60 15.21 ?  27  ALA   A N    1 
ATOM   734  N  N    B ALA   A 1 27  ? 18.397 0.227   14.139  0.40 16.38 ?  27  ALA   A N    1 
ATOM   735  C  CA   A ALA   A 1 27  ? 19.826 0.152   14.689  0.60 15.03 ?  27  ALA   A CA   1 
ATOM   736  C  CA   B ALA   A 1 27  ? 19.776 0.320   14.603  0.40 16.13 ?  27  ALA   A CA   1 
ATOM   737  C  C    A ALA   A 1 27  ? 20.048 0.948   15.969  0.60 16.41 ?  27  ALA   A C    1 
ATOM   738  C  C    B ALA   A 1 27  ? 19.867 1.149   15.879  0.40 17.17 ?  27  ALA   A C    1 
ATOM   739  O  O    A ALA   A 1 27  ? 20.731 0.485   16.890  0.60 16.56 ?  27  ALA   A O    1 
ATOM   740  O  O    B ALA   A 1 27  ? 20.525 0.749   16.847  0.40 16.95 ?  27  ALA   A O    1 
ATOM   741  C  CB   A ALA   A 1 27  ? 20.737 0.661   13.568  0.60 14.59 ?  27  ALA   A CB   1 
ATOM   742  C  CB   B ALA   A 1 27  ? 20.661 0.911   13.505  0.40 15.45 ?  27  ALA   A CB   1 
ATOM   743  H  H    A ALA   A 1 27  ? 18.302 0.574   13.498  0.60 18.22 ?  27  ALA   A H    1 
ATOM   744  H  H    B ALA   A 1 27  ? 18.235 0.624   13.392  0.40 19.63 ?  27  ALA   A H    1 
ATOM   745  H  HA   A ALA   A 1 27  ? 20.059 -0.771  14.865  0.60 18.01 ?  27  ALA   A HA   1 
ATOM   746  H  HA   B ALA   A 1 27  ? 20.099 -0.570  14.800  0.40 19.33 ?  27  ALA   A HA   1 
ATOM   747  H  HB1  A ALA   A 1 27  ? 21.661 0.611   13.864  0.60 17.48 ?  27  ALA   A HB1  1 
ATOM   748  H  HB1  B ALA   A 1 27  ? 21.574 0.954   13.830  0.40 18.52 ?  27  ALA   A HB1  1 
ATOM   749  H  HB2  A ALA   A 1 27  ? 20.613 0.103   12.783  0.60 17.48 ?  27  ALA   A HB2  1 
ATOM   750  H  HB2  B ALA   A 1 27  ? 20.615 0.340   12.722  0.40 18.52 ?  27  ALA   A HB2  1 
ATOM   751  H  HB3  A ALA   A 1 27  ? 20.506 1.579   13.361  0.60 17.48 ?  27  ALA   A HB3  1 
ATOM   752  H  HB3  B ALA   A 1 27  ? 20.343 1.800   13.286  0.40 18.52 ?  27  ALA   A HB3  1 
ATOM   753  N  N    A LYS   A 1 28  ? 19.468 2.147   16.051  0.60 18.17 ?  28  LYS   A N    1 
ATOM   754  N  N    B LYS   A 1 28  ? 19.192 2.300   15.909  0.40 18.70 ?  28  LYS   A N    1 
ATOM   755  C  CA   A LYS   A 1 28  ? 19.612 2.956   17.258  0.60 20.92 ?  28  LYS   A CA   1 
ATOM   756  C  CA   B LYS   A 1 28  ? 19.266 3.175   17.074  0.40 20.76 ?  28  LYS   A CA   1 
ATOM   757  C  C    A LYS   A 1 28  ? 19.049 2.232   18.474  0.60 22.26 ?  28  LYS   A C    1 
ATOM   758  C  C    B LYS   A 1 28  ? 18.758 2.500   18.341  0.40 22.36 ?  28  LYS   A C    1 
ATOM   759  O  O    A LYS   A 1 28  ? 19.634 2.284   19.562  0.60 23.34 ?  28  LYS   A O    1 
ATOM   760  O  O    B LYS   A 1 28  ? 19.167 2.887   19.441  0.40 23.03 ?  28  LYS   A O    1 
ATOM   761  C  CB   A LYS   A 1 28  ? 18.936 4.316   17.064  0.60 22.33 ?  28  LYS   A CB   1 
ATOM   762  C  CB   B LYS   A 1 28  ? 18.474 4.459   16.818  0.40 21.36 ?  28  LYS   A CB   1 
ATOM   763  C  CG   A LYS   A 1 28  ? 19.734 5.281   16.198  0.60 23.67 ?  28  LYS   A CG   1 
ATOM   764  C  CG   B LYS   A 1 28  ? 19.096 5.375   15.778  0.40 22.03 ?  28  LYS   A CG   1 
ATOM   765  C  CD   A LYS   A 1 28  ? 19.210 6.707   16.289  0.60 25.36 ?  28  LYS   A CD   1 
ATOM   766  C  CD   B LYS   A 1 28  ? 18.259 6.626   15.572  0.40 23.17 ?  28  LYS   A CD   1 
ATOM   767  C  CE   A LYS   A 1 28  ? 17.884 6.866   15.569  0.60 26.64 ?  28  LYS   A CE   1 
ATOM   768  C  CE   B LYS   A 1 28  ? 18.884 7.552   14.541  0.40 24.19 ?  28  LYS   A CE   1 
ATOM   769  N  NZ   A LYS   A 1 28  ? 17.442 8.288   15.539  0.60 27.32 ?  28  LYS   A NZ   1 
ATOM   770  N  NZ   B LYS   A 1 28  ? 18.087 8.796   14.344  0.40 24.73 ?  28  LYS   A NZ   1 
ATOM   771  H  H    A LYS   A 1 28  ? 18.998 2.502   15.435  0.60 21.78 ?  28  LYS   A H    1 
ATOM   772  H  H    B LYS   A 1 28  ? 18.683 2.588   15.279  0.40 22.41 ?  28  LYS   A H    1 
ATOM   773  H  HA   A LYS   A 1 28  ? 20.553 3.115   17.425  0.60 25.08 ?  28  LYS   A HA   1 
ATOM   774  H  HA   B LYS   A 1 28  ? 20.189 3.425   17.221  0.40 24.89 ?  28  LYS   A HA   1 
ATOM   775  H  HB2  A LYS   A 1 28  ? 18.077 4.180   16.635  0.60 26.78 ?  28  LYS   A HB2  1 
ATOM   776  H  HB2  B LYS   A 1 28  ? 17.586 4.223   16.508  0.40 25.61 ?  28  LYS   A HB2  1 
ATOM   777  H  HB3  A LYS   A 1 28  ? 18.811 4.733   17.929  0.60 26.78 ?  28  LYS   A HB3  1 
ATOM   778  H  HB3  B LYS   A 1 28  ? 18.409 4.959   17.647  0.40 25.61 ?  28  LYS   A HB3  1 
ATOM   779  H  HG2  A LYS   A 1 28  ? 20.658 5.282   16.490  0.60 28.38 ?  28  LYS   A HG2  1 
ATOM   780  H  HG2  B LYS   A 1 28  ? 19.978 5.646   16.077  0.40 26.41 ?  28  LYS   A HG2  1 
ATOM   781  H  HG3  A LYS   A 1 28  ? 19.676 5.001   15.271  0.60 28.38 ?  28  LYS   A HG3  1 
ATOM   782  H  HG3  B LYS   A 1 28  ? 19.160 4.907   14.931  0.40 26.41 ?  28  LYS   A HG3  1 
ATOM   783  H  HD2  A LYS   A 1 28  ? 19.077 6.940   17.222  0.60 30.41 ?  28  LYS   A HD2  1 
ATOM   784  H  HD2  B LYS   A 1 28  ? 17.376 6.374   15.258  0.40 27.78 ?  28  LYS   A HD2  1 
ATOM   785  H  HD3  A LYS   A 1 28  ? 19.850 7.311   15.882  0.60 30.41 ?  28  LYS   A HD3  1 
ATOM   786  H  HD3  B LYS   A 1 28  ? 18.191 7.109   16.411  0.40 27.78 ?  28  LYS   A HD3  1 
ATOM   787  H  HE2  A LYS   A 1 28  ? 17.979 6.558   14.654  0.60 31.94 ?  28  LYS   A HE2  1 
ATOM   788  H  HE2  B LYS   A 1 28  ? 19.771 7.807   14.840  0.40 29.00 ?  28  LYS   A HE2  1 
ATOM   789  H  HE3  A LYS   A 1 28  ? 17.206 6.347   16.029  0.60 31.94 ?  28  LYS   A HE3  1 
ATOM   790  H  HE3  B LYS   A 1 28  ? 18.941 7.091   13.690  0.40 29.00 ?  28  LYS   A HE3  1 
ATOM   791  H  HZ1  A LYS   A 1 28  ? 16.665 8.357   15.112  0.60 32.76 ?  28  LYS   A HZ1  1 
ATOM   792  H  HZ1  B LYS   A 1 28  ? 18.478 9.315   13.736  0.40 29.65 ?  28  LYS   A HZ1  1 
ATOM   793  H  HZ2  A LYS   A 1 28  ? 17.345 8.594   16.369  0.60 32.76 ?  28  LYS   A HZ2  1 
ATOM   794  H  HZ2  B LYS   A 1 28  ? 17.267 8.591   14.065  0.40 29.65 ?  28  LYS   A HZ2  1 
ATOM   795  H  HZ3  A LYS   A 1 28  ? 18.049 8.786   15.117  0.60 32.76 ?  28  LYS   A HZ3  1 
ATOM   796  H  HZ3  B LYS   A 1 28  ? 18.028 9.243   15.111  0.40 29.65 ?  28  LYS   A HZ3  1 
ATOM   797  N  N    A LYS   A 1 29  ? 17.924 1.534   18.306  0.60 23.17 ?  29  LYS   A N    1 
ATOM   798  N  N    B LYS   A 1 29  ? 17.885 1.502   18.213  0.40 23.73 ?  29  LYS   A N    1 
ATOM   799  C  CA   A LYS   A 1 29  ? 17.316 0.824   19.428  0.60 25.12 ?  29  LYS   A CA   1 
ATOM   800  C  CA   B LYS   A 1 29  ? 17.299 0.829   19.368  0.40 25.58 ?  29  LYS   A CA   1 
ATOM   801  C  C    A LYS   A 1 29  ? 18.131 -0.407  19.809  0.60 24.63 ?  29  LYS   A C    1 
ATOM   802  C  C    B LYS   A 1 29  ? 18.103 -0.399  19.789  0.40 24.84 ?  29  LYS   A C    1 
ATOM   803  O  O    A LYS   A 1 29  ? 18.429 -0.626  20.990  0.60 25.29 ?  29  LYS   A O    1 
ATOM   804  O  O    B LYS   A 1 29  ? 18.368 -0.595  20.980  0.40 25.37 ?  29  LYS   A O    1 
ATOM   805  C  CB   A LYS   A 1 29  ? 15.883 0.426   19.075  0.60 27.90 ?  29  LYS   A CB   1 
ATOM   806  C  CB   B LYS   A 1 29  ? 15.858 0.419   19.046  0.40 28.01 ?  29  LYS   A CB   1 
ATOM   807  C  CG   A LYS   A 1 29  ? 15.132 -0.274  20.200  0.60 30.88 ?  29  LYS   A CG   1 
ATOM   808  C  CG   B LYS   A 1 29  ? 15.112 -0.232  20.201  0.40 30.49 ?  29  LYS   A CG   1 
ATOM   809  C  CD   A LYS   A 1 29  ? 14.800 0.688   21.330  0.60 33.52 ?  29  LYS   A CD   1 
ATOM   810  C  CD   B LYS   A 1 29  ? 14.750 0.783   21.271  0.40 32.60 ?  29  LYS   A CD   1 
ATOM   811  C  CE   A LYS   A 1 29  ? 13.937 0.021   22.391  0.60 35.24 ?  29  LYS   A CE   1 
ATOM   812  C  CE   B LYS   A 1 29  ? 13.910 0.153   22.370  0.40 33.98 ?  29  LYS   A CE   1 
ATOM   813  N  NZ   A LYS   A 1 29  ? 13.502 0.981   23.443  0.60 36.35 ?  29  LYS   A NZ   1 
ATOM   814  N  NZ   B LYS   A 1 29  ? 13.475 1.155   23.381  0.40 34.84 ?  29  LYS   A NZ   1 
ATOM   815  H  H    A LYS   A 1 29  ? 17.499 1.457   17.562  0.60 27.78 ?  29  LYS   A H    1 
ATOM   816  H  H    B LYS   A 1 29  ? 17.610 1.198   17.456  0.40 28.45 ?  29  LYS   A H    1 
ATOM   817  H  HA   A LYS   A 1 29  ? 17.282 1.414   20.197  0.60 30.12 ?  29  LYS   A HA   1 
ATOM   818  H  HA   B LYS   A 1 29  ? 17.277 1.444   20.115  0.40 30.67 ?  29  LYS   A HA   1 
ATOM   819  H  HB2  A LYS   A 1 29  ? 15.384 1.224   18.843  0.60 33.46 ?  29  LYS   A HB2  1 
ATOM   820  H  HB2  B LYS   A 1 29  ? 15.362 1.211   18.786  0.40 33.58 ?  29  LYS   A HB2  1 
ATOM   821  H  HB3  A LYS   A 1 29  ? 15.905 -0.178  18.317  0.60 33.46 ?  29  LYS   A HB3  1 
ATOM   822  H  HB3  B LYS   A 1 29  ? 15.871 -0.213  18.311  0.40 33.58 ?  29  LYS   A HB3  1 
ATOM   823  H  HG2  A LYS   A 1 29  ? 14.300 -0.631  19.853  0.60 37.03 ?  29  LYS   A HG2  1 
ATOM   824  H  HG2  B LYS   A 1 29  ? 14.291 -0.624  19.866  0.40 36.56 ?  29  LYS   A HG2  1 
ATOM   825  H  HG3  A LYS   A 1 29  ? 15.676 -0.992  20.561  0.60 37.03 ?  29  LYS   A HG3  1 
ATOM   826  H  HG3  B LYS   A 1 29  ? 15.667 -0.918  20.605  0.40 36.56 ?  29  LYS   A HG3  1 
ATOM   827  H  HD2  A LYS   A 1 29  ? 15.622 0.986   21.750  0.60 40.20 ?  29  LYS   A HD2  1 
ATOM   828  H  HD2  B LYS   A 1 29  ? 15.562 1.132   21.670  0.40 39.10 ?  29  LYS   A HD2  1 
ATOM   829  H  HD3  A LYS   A 1 29  ? 14.311 1.446   20.972  0.60 40.20 ?  29  LYS   A HD3  1 
ATOM   830  H  HD3  B LYS   A 1 29  ? 14.237 1.502   20.869  0.40 39.10 ?  29  LYS   A HD3  1 
ATOM   831  H  HE2  A LYS   A 1 29  ? 13.144 -0.347  21.971  0.60 42.26 ?  29  LYS   A HE2  1 
ATOM   832  H  HE2  B LYS   A 1 29  ? 13.117 -0.245  21.976  0.40 40.76 ?  29  LYS   A HE2  1 
ATOM   833  H  HE3  A LYS   A 1 29  ? 14.447 -0.685  22.819  0.60 42.26 ?  29  LYS   A HE3  1 
ATOM   834  H  HE3  B LYS   A 1 29  ? 14.435 -0.527  22.822  0.40 40.76 ?  29  LYS   A HE3  1 
ATOM   835  H  HZ1  A LYS   A 1 29  ? 12.999 0.562   24.047  0.60 43.60 ?  29  LYS   A HZ1  1 
ATOM   836  H  HZ1  B LYS   A 1 29  ? 12.986 0.759   24.011  0.40 41.79 ?  29  LYS   A HZ1  1 
ATOM   837  H  HZ2  A LYS   A 1 29  ? 14.212 1.331   23.849  0.60 43.60 ?  29  LYS   A HZ2  1 
ATOM   838  H  HZ2  B LYS   A 1 29  ? 14.186 1.532   23.761  0.40 41.79 ?  29  LYS   A HZ2  1 
ATOM   839  H  HZ3  A LYS   A 1 29  ? 13.025 1.638   23.077  0.60 43.60 ?  29  LYS   A HZ3  1 
ATOM   840  H  HZ3  B LYS   A 1 29  ? 12.986 1.788   22.991  0.40 41.79 ?  29  LYS   A HZ3  1 
ATOM   841  N  N    . VAL   A 1 30  ? 18.486 -1.234  18.824  1.00 23.62 ?  30  VAL   A N    1 
ATOM   842  C  CA   . VAL   A 1 30  ? 19.140 -2.502  19.129  1.00 22.35 ?  30  VAL   A CA   1 
ATOM   843  C  C    . VAL   A 1 30  ? 20.641 -2.338  19.356  1.00 21.13 ?  30  VAL   A C    1 
ATOM   844  O  O    . VAL   A 1 30  ? 21.231 -3.062  20.164  1.00 21.53 ?  30  VAL   A O    1 
ATOM   845  C  CB   . VAL   A 1 30  ? 18.846 -3.504  17.998  1.00 22.90 ?  30  VAL   A CB   1 
ATOM   846  C  CG1  . VAL   A 1 30  ? 19.611 -4.804  18.213  1.00 23.00 ?  30  VAL   A CG1  1 
ATOM   847  C  CG2  . VAL   A 1 30  ? 17.348 -3.771  17.897  1.00 23.68 ?  30  VAL   A CG2  1 
ATOM   848  H  H    A VAL   A 1 30  ? 18.356 -1.089  17.987  0.60 28.32 ?  30  VAL   A H    1 
ATOM   849  H  H    B VAL   A 1 30  ? 18.372 -1.091  17.985  0.40 28.32 ?  30  VAL   A H    1 
ATOM   850  H  HA   . VAL   A 1 30  ? 18.747 -2.863  19.941  1.00 26.80 ?  30  VAL   A HA   1 
ATOM   851  H  HB   . VAL   A 1 30  ? 19.137 -3.126  17.154  1.00 27.45 ?  30  VAL   A HB   1 
ATOM   852  H  HG11 . VAL   A 1 30  ? 19.243 -5.486  17.628  1.00 27.58 ?  30  VAL   A HG11 1 
ATOM   853  H  HG12 . VAL   A 1 30  ? 20.546 -4.660  18.003  1.00 27.58 ?  30  VAL   A HG12 1 
ATOM   854  H  HG13 . VAL   A 1 30  ? 19.513 -5.076  19.138  1.00 27.58 ?  30  VAL   A HG13 1 
ATOM   855  H  HG21 . VAL   A 1 30  ? 17.191 -4.443  17.213  1.00 28.39 ?  30  VAL   A HG21 1 
ATOM   856  H  HG22 . VAL   A 1 30  ? 17.026 -4.091  18.754  1.00 28.39 ?  30  VAL   A HG22 1 
ATOM   857  H  HG23 . VAL   A 1 30  ? 16.896 -2.947  17.660  1.00 28.39 ?  30  VAL   A HG23 1 
ATOM   858  N  N    . LYS   A 1 31  ? 21.277 -1.401  18.662  1.00 20.00 ?  31  LYS   A N    1 
ATOM   859  C  CA   . LYS   A 1 31  ? 22.731 -1.298  18.612  1.00 20.51 ?  31  LYS   A CA   1 
ATOM   860  C  C    . LYS   A 1 31  ? 23.342 -2.660  18.269  1.00 18.44 ?  31  LYS   A C    1 
ATOM   861  O  O    . LYS   A 1 31  ? 24.115 -3.219  19.053  1.00 19.61 ?  31  LYS   A O    1 
ATOM   862  C  CB   . LYS   A 1 31  ? 23.312 -0.742  19.904  1.00 25.02 ?  31  LYS   A CB   1 
ATOM   863  C  CG   . LYS   A 1 31  ? 22.638 0.537   20.378  1.00 31.04 ?  31  LYS   A CG   1 
ATOM   864  C  CD   . LYS   A 1 31  ? 23.649 1.547   20.899  1.00 35.32 ?  31  LYS   A CD   1 
ATOM   865  C  CE   . LYS   A 1 31  ? 22.991 2.588   21.793  1.00 38.47 ?  31  LYS   A CE   1 
ATOM   866  N  NZ   . LYS   A 1 31  ? 21.842 3.271   21.137  1.00 40.18 ?  31  LYS   A NZ   1 
ATOM   867  H  H    . LYS   A 1 31  ? 20.874 -0.799  18.202  1.00 23.97 ?  31  LYS   A H    1 
ATOM   868  H  HA   . LYS   A 1 31  ? 22.955 -0.685  17.902  1.00 24.59 ?  31  LYS   A HA   1 
ATOM   869  H  HB2  . LYS   A 1 31  ? 23.216 -1.406  20.600  1.00 30.01 ?  31  LYS   A HB2  1 
ATOM   870  H  HB3  . LYS   A 1 31  ? 24.253 -0.546  19.761  1.00 30.01 ?  31  LYS   A HB3  1 
ATOM   871  H  HG2  . LYS   A 1 31  ? 22.161 0.941   19.636  1.00 37.22 ?  31  LYS   A HG2  1 
ATOM   872  H  HG3  . LYS   A 1 31  ? 22.023 0.327   21.098  1.00 37.22 ?  31  LYS   A HG3  1 
ATOM   873  H  HD2  . LYS   A 1 31  ? 24.326 1.086   21.417  1.00 42.36 ?  31  LYS   A HD2  1 
ATOM   874  H  HD3  . LYS   A 1 31  ? 24.058 2.007   20.148  1.00 42.36 ?  31  LYS   A HD3  1 
ATOM   875  H  HE2  . LYS   A 1 31  ? 22.663 2.152   22.595  1.00 46.14 ?  31  LYS   A HE2  1 
ATOM   876  H  HE3  . LYS   A 1 31  ? 23.647 3.263   22.027  1.00 46.14 ?  31  LYS   A HE3  1 
ATOM   877  H  HZ1  . LYS   A 1 31  ? 21.500 3.884   21.685  1.00 48.19 ?  31  LYS   A HZ1  1 
ATOM   878  H  HZ2  . LYS   A 1 31  ? 22.111 3.670   20.389  1.00 48.19 ?  31  LYS   A HZ2  1 
ATOM   879  H  HZ3  . LYS   A 1 31  ? 21.208 2.678   20.938  1.00 48.19 ?  31  LYS   A HZ3  1 
ATOM   880  N  N    . PRO   A 1 32  ? 23.005 -3.216  17.111  1.00 16.23 ?  32  PRO   A N    1 
ATOM   881  C  CA   . PRO   A 1 32  ? 23.479 -4.555  16.766  1.00 16.31 ?  32  PRO   A CA   1 
ATOM   882  C  C    . PRO   A 1 32  ? 24.979 -4.569  16.554  1.00 16.19 ?  32  PRO   A C    1 
ATOM   883  O  O    . PRO   A 1 32  ? 25.621 -3.539  16.341  1.00 16.13 ?  32  PRO   A O    1 
ATOM   884  C  CB   . PRO   A 1 32  ? 22.748 -4.852  15.453  1.00 16.55 ?  32  PRO   A CB   1 
ATOM   885  C  CG   . PRO   A 1 32  ? 22.565 -3.496  14.838  1.00 15.07 ?  32  PRO   A CG   1 
ATOM   886  C  CD   . PRO   A 1 32  ? 22.266 -2.593  16.002  1.00 15.23 ?  32  PRO   A CD   1 
ATOM   887  H  HA   . PRO   A 1 32  ? 23.231 -5.203  17.443  1.00 19.54 ?  32  PRO   A HA   1 
ATOM   888  H  HB2  . PRO   A 1 32  ? 23.297 -5.422  14.888  1.00 19.84 ?  32  PRO   A HB2  1 
ATOM   889  H  HB3  . PRO   A 1 32  ? 21.892 -5.272  15.638  1.00 19.84 ?  32  PRO   A HB3  1 
ATOM   890  H  HG2  . PRO   A 1 32  ? 23.380 -3.234  14.387  1.00 18.05 ?  32  PRO   A HG2  1 
ATOM   891  H  HG3  . PRO   A 1 32  ? 21.819 -3.525  14.215  1.00 18.05 ?  32  PRO   A HG3  1 
ATOM   892  H  HD2  . PRO   A 1 32  ? 22.604 -1.703  15.817  1.00 18.25 ?  32  PRO   A HD2  1 
ATOM   893  H  HD3  . PRO   A 1 32  ? 21.316 -2.587  16.182  1.00 18.25 ?  32  PRO   A HD3  1 
ATOM   894  N  N    . THR   A 1 33  ? 25.535 -5.778  16.592  1.00 16.15 ?  33  THR   A N    1 
ATOM   895  C  CA   . THR   A 1 33  ? 26.945 -5.943  16.271  1.00 16.24 ?  33  THR   A CA   1 
ATOM   896  C  C    . THR   A 1 33  ? 27.236 -5.487  14.848  1.00 14.67 ?  33  THR   A C    1 
ATOM   897  O  O    . THR   A 1 33  ? 28.264 -4.842  14.592  1.00 14.68 ?  33  THR   A O    1 
ATOM   898  C  CB   . THR   A 1 33  ? 27.347 -7.402  16.477  1.00 18.09 ?  33  THR   A CB   1 
ATOM   899  O  OG1  . THR   A 1 33  ? 27.033 -7.788  17.818  1.00 19.65 ?  33  THR   A OG1  1 
ATOM   900  C  CG2  . THR   A 1 33  ? 28.837 -7.595  16.237  1.00 18.93 ?  33  THR   A CG2  1 
ATOM   901  H  H    . THR   A 1 33  ? 25.124 -6.505  16.791  1.00 19.35 ?  33  THR   A H    1 
ATOM   902  H  HA   . THR   A 1 33  ? 27.476 -5.399  16.874  1.00 19.46 ?  33  THR   A HA   1 
ATOM   903  H  HB   . THR   A 1 33  ? 26.859 -7.966  15.855  1.00 21.69 ?  33  THR   A HB   1 
ATOM   904  H  HG1  . THR   A 1 33  ? 27.451 -7.303  18.365  1.00 23.55 ?  33  THR   A HG1  1 
ATOM   905  H  HG21 . THR   A 1 33  ? 29.103 -8.488  16.513  1.00 22.69 ?  33  THR   A HG21 1 
ATOM   906  H  HG22 . THR   A 1 33  ? 29.043 -7.482  15.298  1.00 22.69 ?  33  THR   A HG22 1 
ATOM   907  H  HG23 . THR   A 1 33  ? 29.341 -6.947  16.754  1.00 22.69 ?  33  THR   A HG23 1 
ATOM   908  N  N    . VAL   A 1 34  ? 26.341 -5.802  13.910  1.00 13.37 ?  34  VAL   A N    1 
ATOM   909  C  CA   . VAL   A 1 34  ? 26.528 -5.465  12.504  1.00 12.02 ?  34  VAL   A CA   1 
ATOM   910  C  C    . VAL   A 1 34  ? 25.225 -4.906  11.945  1.00 11.36 ?  34  VAL   A C    1 
ATOM   911  O  O    . VAL   A 1 34  ? 24.188 -5.581  11.988  1.00 12.34 ?  34  VAL   A O    1 
ATOM   912  C  CB   . VAL   A 1 34  ? 26.977 -6.676  11.662  1.00 12.84 ?  34  VAL   A CB   1 
ATOM   913  C  CG1  . VAL   A 1 34  ? 27.154 -6.273  10.207  1.00 12.83 ?  34  VAL   A CG1  1 
ATOM   914  C  CG2  . VAL   A 1 34  ? 28.261 -7.297  12.222  1.00 13.93 ?  34  VAL   A CG2  1 
ATOM   915  H  H    . VAL   A 1 34  ? 25.605 -6.221  14.068  1.00 16.02 ?  34  VAL   A H    1 
ATOM   916  H  HA   . VAL   A 1 34  ? 27.206 -4.776  12.424  1.00 14.40 ?  34  VAL   A HA   1 
ATOM   917  H  HB   . VAL   A 1 34  ? 26.284 -7.352  11.697  1.00 15.38 ?  34  VAL   A HB   1 
ATOM   918  H  HG11 . VAL   A 1 34  ? 27.649 -6.968  9.745   1.00 15.37 ?  34  VAL   A HG11 1 
ATOM   919  H  HG12 . VAL   A 1 34  ? 26.284 -6.159  9.797   1.00 15.37 ?  34  VAL   A HG12 1 
ATOM   920  H  HG13 . VAL   A 1 34  ? 27.651 -5.438  10.168  1.00 15.37 ?  34  VAL   A HG13 1 
ATOM   921  H  HG21 . VAL   A 1 34  ? 28.532 -8.034  11.652  1.00 16.69 ?  34  VAL   A HG21 1 
ATOM   922  H  HG22 . VAL   A 1 34  ? 28.959 -6.622  12.242  1.00 16.69 ?  34  VAL   A HG22 1 
ATOM   923  H  HG23 . VAL   A 1 34  ? 28.091 -7.621  13.121  1.00 16.69 ?  34  VAL   A HG23 1 
ATOM   924  N  N    . VAL   A 1 35  ? 25.283 -3.692  11.390  1.00 10.66 ?  35  VAL   A N    1 
ATOM   925  C  CA   . VAL   A 1 35  ? 24.247 -3.179  10.503  1.00 10.30 ?  35  VAL   A CA   1 
ATOM   926  C  C    . VAL   A 1 35  ? 24.800 -3.183  9.086   1.00 9.70  ?  35  VAL   A C    1 
ATOM   927  O  O    . VAL   A 1 35  ? 25.946 -2.778  8.852   1.00 10.47 ?  35  VAL   A O    1 
ATOM   928  C  CB   . VAL   A 1 35  ? 23.723 -1.785  10.911  1.00 10.96 ?  35  VAL   A CB   1 
ATOM   929  C  CG1  . VAL   A 1 35  ? 24.796 -0.697  10.768  1.00 11.84 ?  35  VAL   A CG1  1 
ATOM   930  C  CG2  . VAL   A 1 35  ? 22.485 -1.432  10.097  1.00 11.41 ?  35  VAL   A CG2  1 
ATOM   931  H  H    . VAL   A 1 35  ? 25.927 -3.139  11.512  1.00 12.77 ?  35  VAL   A H    1 
ATOM   932  H  HA   . VAL   A 1 35  ? 23.489 -3.789  10.524  1.00 12.33 ?  35  VAL   A HA   1 
ATOM   933  H  HB   . VAL   A 1 35  ? 23.453 -1.813  11.839  1.00 13.12 ?  35  VAL   A HB   1 
ATOM   934  H  HG11 . VAL   A 1 35  ? 24.458 0.134   11.143  1.00 14.19 ?  35  VAL   A HG11 1 
ATOM   935  H  HG12 . VAL   A 1 35  ? 25.591 -0.975  11.247  1.00 14.19 ?  35  VAL   A HG12 1 
ATOM   936  H  HG13 . VAL   A 1 35  ? 25.003 -0.570  9.827   1.00 14.19 ?  35  VAL   A HG13 1 
ATOM   937  H  HG21 . VAL   A 1 35  ? 22.132 -0.584  10.402  1.00 13.67 ?  35  VAL   A HG21 1 
ATOM   938  H  HG22 . VAL   A 1 35  ? 22.729 -1.367  9.156   1.00 13.67 ?  35  VAL   A HG22 1 
ATOM   939  H  HG23 . VAL   A 1 35  ? 21.818 -2.129  10.212  1.00 13.67 ?  35  VAL   A HG23 1 
ATOM   940  N  N    . VAL   A 1 36  ? 23.981 -3.632  8.142   1.00 9.37  ?  36  VAL   A N    1 
ATOM   941  C  CA   . VAL   A 1 36  ? 24.354 -3.648  6.737   1.00 9.10  ?  36  VAL   A CA   1 
ATOM   942  C  C    . VAL   A 1 36  ? 23.894 -2.361  6.074   1.00 9.05  ?  36  VAL   A C    1 
ATOM   943  O  O    . VAL   A 1 36  ? 22.732 -1.954  6.216   1.00 9.94  ?  36  VAL   A O    1 
ATOM   944  C  CB   . VAL   A 1 36  ? 23.741 -4.862  6.020   1.00 9.13  ?  36  VAL   A CB   1 
ATOM   945  C  CG1  . VAL   A 1 36  ? 23.991 -4.783  4.532   1.00 9.98  ?  36  VAL   A CG1  1 
ATOM   946  C  CG2  . VAL   A 1 36  ? 24.280 -6.158  6.596   1.00 10.13 ?  36  VAL   A CG2  1 
ATOM   947  H  H    . VAL   A 1 36  ? 23.184 -3.936  8.290   1.00 11.21 ?  36  VAL   A H    1 
ATOM   948  H  HA   . VAL   A 1 36  ? 25.323 -3.711  6.661   1.00 10.90 ?  36  VAL   A HA   1 
ATOM   949  H  HB   . VAL   A 1 36  ? 22.784 -4.853  6.155   1.00 10.93 ?  36  VAL   A HB   1 
ATOM   950  H  HG11 . VAL   A 1 36  ? 23.862 -5.662  4.141   1.00 11.96 ?  36  VAL   A HG11 1 
ATOM   951  H  HG12 . VAL   A 1 36  ? 23.367 -4.153  4.134   1.00 11.96 ?  36  VAL   A HG12 1 
ATOM   952  H  HG13 . VAL   A 1 36  ? 24.903 -4.487  4.377   1.00 11.96 ?  36  VAL   A HG13 1 
ATOM   953  H  HG21 . VAL   A 1 36  ? 23.887 -6.907  6.119   1.00 12.13 ?  36  VAL   A HG21 1 
ATOM   954  H  HG22 . VAL   A 1 36  ? 25.246 -6.176  6.496   1.00 12.13 ?  36  VAL   A HG22 1 
ATOM   955  H  HG23 . VAL   A 1 36  ? 24.046 -6.208  7.537   1.00 12.13 ?  36  VAL   A HG23 1 
ATOM   956  N  N    A ASN   A 1 37  ? 24.805 -1.732  5.335   0.60 8.90  ?  37  ASN   A N    1 
ATOM   957  N  N    B ASN   A 1 37  ? 24.802 -1.718  5.345   0.40 8.62  ?  37  ASN   A N    1 
ATOM   958  C  CA   A ASN   A 1 37  ? 24.482 -0.597  4.487   0.60 8.94  ?  37  ASN   A CA   1 
ATOM   959  C  CA   B ASN   A 1 37  ? 24.452 -0.614  4.465   0.40 8.51  ?  37  ASN   A CA   1 
ATOM   960  C  C    A ASN   A 1 37  ? 24.310 -1.047  3.044   0.60 8.97  ?  37  ASN   A C    1 
ATOM   961  C  C    B ASN   A 1 37  ? 24.363 -1.114  3.031   0.40 8.61  ?  37  ASN   A C    1 
ATOM   962  O  O    A ASN   A 1 37  ? 25.058 -1.899  2.548   0.60 9.56  ?  37  ASN   A O    1 
ATOM   963  O  O    B ASN   A 1 37  ? 25.187 -1.921  2.589   0.40 8.56  ?  37  ASN   A O    1 
ATOM   964  C  CB   A ASN   A 1 37  ? 25.587 0.454   4.553   0.60 9.18  ?  37  ASN   A CB   1 
ATOM   965  C  CB   B ASN   A 1 37  ? 25.492 0.503   4.547   0.40 8.82  ?  37  ASN   A CB   1 
ATOM   966  C  CG   A ASN   A 1 37  ? 25.235 1.702   3.788   0.60 8.85  ?  37  ASN   A CG   1 
ATOM   967  C  CG   B ASN   A 1 37  ? 25.211 1.629   3.568   0.40 8.99  ?  37  ASN   A CG   1 
ATOM   968  O  OD1  A ASN   A 1 37  ? 24.059 2.040   3.650   0.60 8.84  ?  37  ASN   A OD1  1 
ATOM   969  O  OD1  B ASN   A 1 37  ? 24.053 1.954   3.291   0.40 9.00  ?  37  ASN   A OD1  1 
ATOM   970  N  ND2  A ASN   A 1 37  ? 26.246 2.397   3.283   0.60 8.68  ?  37  ASN   A ND2  1 
ATOM   971  N  ND2  B ASN   A 1 37  ? 26.267 2.221   3.028   0.40 8.76  ?  37  ASN   A ND2  1 
ATOM   972  H  H    A ASN   A 1 37  ? 25.641 -1.950  5.312   0.60 10.66 ?  37  ASN   A H    1 
ATOM   973  H  H    B ASN   A 1 37  ? 25.645 -1.907  5.344   0.40 10.32 ?  37  ASN   A H    1 
ATOM   974  H  HA   A ASN   A 1 37  ? 23.657 -0.194  4.786   0.60 10.71 ?  37  ASN   A HA   1 
ATOM   975  H  HA   B ASN   A 1 37  ? 23.593 -0.252  4.723   0.40 10.18 ?  37  ASN   A HA   1 
ATOM   976  H  HB2  A ASN   A 1 37  ? 25.731 0.705   5.478   0.60 10.99 ?  37  ASN   A HB2  1 
ATOM   977  H  HB2  B ASN   A 1 37  ? 25.490 0.875   5.446   0.40 10.56 ?  37  ASN   A HB2  1 
ATOM   978  H  HB3  A ASN   A 1 37  ? 26.405 0.087   4.177   0.60 10.99 ?  37  ASN   A HB3  1 
ATOM   979  H  HB3  B ASN   A 1 37  ? 26.369 0.139   4.344   0.40 10.56 ?  37  ASN   A HB3  1 
ATOM   980  H  HD21 A ASN   A 1 37  ? 26.094 3.116   2.836   0.60 10.40 ?  37  ASN   A HD21 1 
ATOM   981  H  HD21 B ASN   A 1 37  ? 26.160 2.857   2.466   0.40 10.49 ?  37  ASN   A HD21 1 
ATOM   982  H  HD22 A ASN   A 1 37  ? 27.052 2.135   3.400   0.60 10.40 ?  37  ASN   A HD22 1 
ATOM   983  H  HD22 B ASN   A 1 37  ? 27.057 1.963   3.236   0.40 10.49 ?  37  ASN   A HD22 1 
ATOM   984  N  N    A ALA   A 1 38  ? 23.310 -0.463  2.378   0.60 9.11  ?  38  ALA   A N    1 
ATOM   985  N  N    B ALA   A 1 38  ? 23.339 -0.645  2.316   0.40 9.06  ?  38  ALA   A N    1 
ATOM   986  C  CA   A ALA   A 1 38  ? 23.091 -0.614  0.939   0.60 8.84  ?  38  ALA   A CA   1 
ATOM   987  C  CA   B ALA   A 1 38  ? 23.194 -0.882  0.880   0.40 9.85  ?  38  ALA   A CA   1 
ATOM   988  C  C    A ALA   A 1 38  ? 24.024 0.359   0.218   0.60 8.76  ?  38  ALA   A C    1 
ATOM   989  C  C    B ALA   A 1 38  ? 24.009 0.184   0.150   0.40 10.06 ?  38  ALA   A C    1 
ATOM   990  O  O    A ALA   A 1 38  ? 23.639 1.450   -0.208  0.60 8.81  ?  38  ALA   A O    1 
ATOM   991  O  O    B ALA   A 1 38  ? 23.510 1.235   -0.261  0.40 10.18 ?  38  ALA   A O    1 
ATOM   992  C  CB   A ALA   A 1 38  ? 21.627 -0.352  0.599   0.60 9.43  ?  38  ALA   A CB   1 
ATOM   993  C  CB   B ALA   A 1 38  ? 21.724 -0.842  0.481   0.40 10.45 ?  38  ALA   A CB   1 
ATOM   994  H  H    A ALA   A 1 38  ? 22.735 0.049   2.754   0.60 10.91 ?  38  ALA   A H    1 
ATOM   995  H  H    B ALA   A 1 38  ? 22.706 -0.178  2.653   0.40 10.85 ?  38  ALA   A H    1 
ATOM   996  H  HA   A ALA   A 1 38  ? 23.317 -1.513  0.665   0.60 10.58 ?  38  ALA   A HA   1 
ATOM   997  H  HA   B ALA   A 1 38  ? 23.552 -1.762  0.659   0.40 11.80 ?  38  ALA   A HA   1 
ATOM   998  H  HB1  A ALA   A 1 38  ? 21.497 -0.457  -0.356  0.60 11.30 ?  38  ALA   A HB1  1 
ATOM   999  H  HB1  B ALA   A 1 38  ? 21.653 -1.003  -0.472  0.40 12.51 ?  38  ALA   A HB1  1 
ATOM   1000 H  HB2  A ALA   A 1 38  ? 21.072 -0.986  1.081   0.60 11.30 ?  38  ALA   A HB2  1 
ATOM   1001 H  HB2  B ALA   A 1 38  ? 21.241 -1.527  0.970   0.40 12.51 ?  38  ALA   A HB2  1 
ATOM   1002 H  HB3  A ALA   A 1 38  ? 21.395 0.554   0.865   0.60 11.30 ?  38  ALA   A HB3  1 
ATOM   1003 H  HB3  B ALA   A 1 38  ? 21.366 0.033   0.698   0.40 12.51 ?  38  ALA   A HB3  1 
ATOM   1004 N  N    A ALA   A 1 39  ? 25.284 -0.050  0.092   0.60 8.89  ?  39  ALA   A N    1 
ATOM   1005 N  N    B ALA   A 1 39  ? 25.297 -0.100  -0.006  0.40 10.42 ?  39  ALA   A N    1 
ATOM   1006 C  CA   A ALA   A 1 39  ? 26.356 0.805   -0.393  0.60 8.79  ?  39  ALA   A CA   1 
ATOM   1007 C  CA   B ALA   A 1 39  ? 26.252 0.877   -0.496  0.40 10.50 ?  39  ALA   A CA   1 
ATOM   1008 C  C    A ALA   A 1 39  ? 26.460 0.771   -1.917  0.60 8.74  ?  39  ALA   A C    1 
ATOM   1009 C  C    B ALA   A 1 39  ? 26.429 0.771   -2.009  0.40 9.99  ?  39  ALA   A C    1 
ATOM   1010 O  O    A ALA   A 1 39  ? 25.948 -0.132  -2.586  0.60 9.55  ?  39  ALA   A O    1 
ATOM   1011 O  O    B ALA   A 1 39  ? 26.004 -0.192  -2.653  0.40 10.28 ?  39  ALA   A O    1 
ATOM   1012 C  CB   A ALA   A 1 39  ? 27.678 0.351   0.230   0.60 9.01  ?  39  ALA   A CB   1 
ATOM   1013 C  CB   B ALA   A 1 39  ? 27.596 0.676   0.202   0.40 11.23 ?  39  ALA   A CB   1 
ATOM   1014 H  H    A ALA   A 1 39  ? 25.546 -0.845  0.292   0.60 10.65 ?  39  ALA   A H    1 
ATOM   1015 H  H    B ALA   A 1 39  ? 25.644 -0.869  0.170   0.40 12.49 ?  39  ALA   A H    1 
ATOM   1016 H  HA   A ALA   A 1 39  ? 26.189 1.722   -0.114  0.60 10.52 ?  39  ALA   A HA   1 
ATOM   1017 H  HA   B ALA   A 1 39  ? 25.930 1.768   -0.282  0.40 12.57 ?  39  ALA   A HA   1 
ATOM   1018 H  HB1  A ALA   A 1 39  ? 28.392 0.925   -0.090  0.60 10.78 ?  39  ALA   A HB1  1 
ATOM   1019 H  HB1  B ALA   A 1 39  ? 28.222 1.338   -0.128  0.40 13.45 ?  39  ALA   A HB1  1 
ATOM   1020 H  HB2  A ALA   A 1 39  ? 27.614 0.420   1.199   0.60 10.78 ?  39  ALA   A HB2  1 
ATOM   1021 H  HB2  B ALA   A 1 39  ? 27.476 0.782   1.160   0.40 13.45 ?  39  ALA   A HB2  1 
ATOM   1022 H  HB3  A ALA   A 1 39  ? 27.849 -0.567  -0.023  0.60 10.78 ?  39  ALA   A HB3  1 
ATOM   1023 H  HB3  B ALA   A 1 39  ? 27.921 -0.216  0.007   0.40 13.45 ?  39  ALA   A HB3  1 
ATOM   1024 N  N    A ASN   A 1 40  ? 27.157 1.770   -2.460  0.60 9.09  ?  40  ASN   A N    1 
ATOM   1025 N  N    B ASN   A 1 40  ? 27.075 1.785   -2.574  0.40 10.12 ?  40  ASN   A N    1 
ATOM   1026 C  CA   A ASN   A 1 40  ? 27.656 1.728   -3.828  0.60 9.55  ?  40  ASN   A CA   1 
ATOM   1027 C  CA   B ASN   A 1 40  ? 27.624 1.714   -3.918  0.40 10.49 ?  40  ASN   A CA   1 
ATOM   1028 C  C    A ASN   A 1 40  ? 29.180 1.620   -3.809  0.60 9.56  ?  40  ASN   A C    1 
ATOM   1029 C  C    B ASN   A 1 40  ? 29.144 1.612   -3.830  0.40 9.95  ?  40  ASN   A C    1 
ATOM   1030 O  O    A ASN   A 1 40  ? 29.811 1.720   -2.755  0.60 9.65  ?  40  ASN   A O    1 
ATOM   1031 O  O    B ASN   A 1 40  ? 29.737 1.722   -2.754  0.40 9.71  ?  40  ASN   A O    1 
ATOM   1032 C  CB   A ASN   A 1 40  ? 27.150 2.918   -4.661  0.60 10.10 ?  40  ASN   A CB   1 
ATOM   1033 C  CB   B ASN   A 1 40  ? 27.173 2.906   -4.777  0.40 11.07 ?  40  ASN   A CB   1 
ATOM   1034 C  CG   A ASN   A 1 40  ? 27.576 4.261   -4.108  0.60 11.23 ?  40  ASN   A CG   1 
ATOM   1035 C  CG   B ASN   A 1 40  ? 27.465 4.242   -4.131  0.40 11.86 ?  40  ASN   A CG   1 
ATOM   1036 O  OD1  A ASN   A 1 40  ? 28.752 4.481   -3.805  0.60 12.40 ?  40  ASN   A OD1  1 
ATOM   1037 O  OD1  B ASN   A 1 40  ? 28.625 4.609   -3.935  0.40 12.52 ?  40  ASN   A OD1  1 
ATOM   1038 N  ND2  A ASN   A 1 40  ? 26.615 5.178   -3.988  0.60 11.59 ?  40  ASN   A ND2  1 
ATOM   1039 N  ND2  B ASN   A 1 40  ? 26.410 4.991   -3.817  0.40 12.24 ?  40  ASN   A ND2  1 
ATOM   1040 H  H    A ASN   A 1 40  ? 27.370 2.488   -2.040  0.60 10.89 ?  40  ASN   A H    1 
ATOM   1041 H  H    B ASN   A 1 40  ? 27.216 2.534   -2.184  0.40 12.12 ?  40  ASN   A H    1 
ATOM   1042 H  HA   A ASN   A 1 40  ? 27.324 0.920   -4.247  0.60 11.44 ?  40  ASN   A HA   1 
ATOM   1043 H  HA   B ASN   A 1 40  ? 27.299 0.902   -4.346  0.40 12.56 ?  40  ASN   A HA   1 
ATOM   1044 H  HB2  A ASN   A 1 40  ? 27.500 2.835   -5.563  0.60 12.10 ?  40  ASN   A HB2  1 
ATOM   1045 H  HB2  B ASN   A 1 40  ? 27.638 2.874   -5.625  0.40 13.26 ?  40  ASN   A HB2  1 
ATOM   1046 H  HB3  A ASN   A 1 40  ? 26.184 2.893   -4.678  0.60 12.10 ?  40  ASN   A HB3  1 
ATOM   1047 H  HB3  B ASN   A 1 40  ? 26.214 2.841   -4.921  0.40 13.26 ?  40  ASN   A HB3  1 
ATOM   1048 H  HD21 A ASN   A 1 40  ? 26.801 5.963   -3.686  0.60 13.89 ?  40  ASN   A HD21 1 
ATOM   1049 H  HD21 B ASN   A 1 40  ? 26.522 5.759   -3.447  0.40 14.66 ?  40  ASN   A HD21 1 
ATOM   1050 H  HD22 A ASN   A 1 40  ? 25.806 4.983   -4.205  0.60 13.89 ?  40  ASN   A HD22 1 
ATOM   1051 H  HD22 B ASN   A 1 40  ? 25.612 4.706   -3.977  0.40 14.66 ?  40  ASN   A HD22 1 
ATOM   1052 N  N    . VAL   A 1 41  ? 29.774 1.376   -4.982  1.00 10.13 ?  41  VAL   A N    1 
ATOM   1053 C  CA   . VAL   A 1 41  ? 31.207 1.073   -5.020  1.00 11.05 ?  41  VAL   A CA   1 
ATOM   1054 C  C    . VAL   A 1 41  ? 32.070 2.222   -4.541  1.00 10.67 ?  41  VAL   A C    1 
ATOM   1055 O  O    . VAL   A 1 41  ? 33.212 1.997   -4.127  1.00 11.11 ?  41  VAL   A O    1 
ATOM   1056 C  CB   . VAL   A 1 41  ? 31.690 0.588   -6.407  1.00 12.00 ?  41  VAL   A CB   1 
ATOM   1057 C  CG1  . VAL   A 1 41  ? 31.005 -0.716  -6.788  1.00 12.48 ?  41  VAL   A CG1  1 
ATOM   1058 C  CG2  . VAL   A 1 41  ? 31.512 1.656   -7.480  1.00 12.39 ?  41  VAL   A CG2  1 
ATOM   1059 H  H    A VAL   A 1 41  ? 29.380 1.371   -5.748  0.60 12.13 ?  41  VAL   A H    1 
ATOM   1060 H  H    B VAL   A 1 41  ? 29.394 1.370   -5.755  0.40 12.13 ?  41  VAL   A H    1 
ATOM   1061 H  HA   . VAL   A 1 41  ? 31.368 0.339   -4.406  1.00 13.23 ?  41  VAL   A HA   1 
ATOM   1062 H  HB   . VAL   A 1 41  ? 32.640 0.394   -6.348  1.00 14.38 ?  41  VAL   A HB   1 
ATOM   1063 H  HG11 . VAL   A 1 41  ? 31.344 -1.018  -7.646  1.00 14.95 ?  41  VAL   A HG11 1 
ATOM   1064 H  HG12 . VAL   A 1 41  ? 31.193 -1.385  -6.107  1.00 14.95 ?  41  VAL   A HG12 1 
ATOM   1065 H  HG13 . VAL   A 1 41  ? 30.048 -0.567  -6.844  1.00 14.95 ?  41  VAL   A HG13 1 
ATOM   1066 H  HG21 . VAL   A 1 41  ? 31.750 1.277   -8.343  1.00 14.85 ?  41  VAL   A HG21 1 
ATOM   1067 H  HG22 . VAL   A 1 41  ? 30.590 1.944   -7.487  1.00 14.85 ?  41  VAL   A HG22 1 
ATOM   1068 H  HG23 . VAL   A 1 41  ? 32.096 2.402   -7.277  1.00 14.85 ?  41  VAL   A HG23 1 
ATOM   1069 N  N    . TYR   A 1 42  ? 31.566 3.455   -4.610  1.00 10.42 ?  42  TYR   A N    1 
ATOM   1070 C  CA   . TYR   A 1 42  ? 32.312 4.637   -4.191  1.00 10.72 ?  42  TYR   A CA   1 
ATOM   1071 C  C    . TYR   A 1 42  ? 32.044 5.011   -2.744  1.00 10.34 ?  42  TYR   A C    1 
ATOM   1072 O  O    . TYR   A 1 42  ? 32.608 6.001   -2.253  1.00 10.98 ?  42  TYR   A O    1 
ATOM   1073 C  CB   . TYR   A 1 42  ? 31.966 5.825   -5.107  1.00 11.35 ?  42  TYR   A CB   1 
ATOM   1074 C  CG   . TYR   A 1 42  ? 32.153 5.511   -6.576  1.00 12.24 ?  42  TYR   A CG   1 
ATOM   1075 C  CD1  . TYR   A 1 42  ? 33.418 5.317   -7.108  1.00 12.85 ?  42  TYR   A CD1  1 
ATOM   1076 C  CD2  . TYR   A 1 42  ? 31.064 5.380   -7.426  1.00 13.44 ?  42  TYR   A CD2  1 
ATOM   1077 C  CE1  . TYR   A 1 42  ? 33.594 5.010   -8.449  1.00 13.37 ?  42  TYR   A CE1  1 
ATOM   1078 C  CE2  . TYR   A 1 42  ? 31.233 5.086   -8.767  1.00 14.86 ?  42  TYR   A CE2  1 
ATOM   1079 C  CZ   . TYR   A 1 42  ? 32.499 4.899   -9.273  1.00 14.48 ?  42  TYR   A CZ   1 
ATOM   1080 O  OH   . TYR   A 1 42  ? 32.662 4.597   -10.604 1.00 16.16 ?  42  TYR   A OH   1 
ATOM   1081 H  H    . TYR   A 1 42  ? 30.777 3.635   -4.905  1.00 12.48 ?  42  TYR   A H    1 
ATOM   1082 H  HA   . TYR   A 1 42  ? 33.259 4.464   -4.286  1.00 12.84 ?  42  TYR   A HA   1 
ATOM   1083 H  HB2  . TYR   A 1 42  ? 31.038 6.074   -4.971  1.00 13.60 ?  42  TYR   A HB2  1 
ATOM   1084 H  HB3  . TYR   A 1 42  ? 32.544 6.575   -4.888  1.00 13.60 ?  42  TYR   A HB3  1 
ATOM   1085 H  HD1  . TYR   A 1 42  ? 34.162 5.387   -6.554  1.00 15.40 ?  42  TYR   A HD1  1 
ATOM   1086 H  HD2  . TYR   A 1 42  ? 30.207 5.512   -7.092  1.00 16.11 ?  42  TYR   A HD2  1 
ATOM   1087 H  HE1  . TYR   A 1 42  ? 34.452 4.882   -8.792  1.00 16.02 ?  42  TYR   A HE1  1 
ATOM   1088 H  HE2  . TYR   A 1 42  ? 30.494 5.009   -9.327  1.00 17.81 ?  42  TYR   A HE2  1 
ATOM   1089 H  HH   . TYR   A 1 42  ? 33.482 4.500   -10.782 1.00 19.37 ?  42  TYR   A HH   1 
ATOM   1090 N  N    A LEU   A 1 43  ? 31.201 4.247   -2.050  0.60 9.93  ?  43  LEU   A N    1 
ATOM   1091 N  N    B LEU   A 1 43  ? 31.187 4.251   -2.060  0.40 10.20 ?  43  LEU   A N    1 
ATOM   1092 C  CA   A LEU   A 1 43  ? 30.776 4.576   -0.689  0.60 9.51  ?  43  LEU   A CA   1 
ATOM   1093 C  CA   B LEU   A 1 43  ? 30.714 4.600   -0.722  0.40 10.01 ?  43  LEU   A CA   1 
ATOM   1094 C  C    A LEU   A 1 43  ? 30.293 6.020   -0.577  0.60 9.40  ?  43  LEU   A C    1 
ATOM   1095 C  C    B LEU   A 1 43  ? 30.238 6.049   -0.658  0.40 10.30 ?  43  LEU   A C    1 
ATOM   1096 O  O    A LEU   A 1 43  ? 30.524 6.702   0.426   0.60 10.48 ?  43  LEU   A O    1 
ATOM   1097 O  O    B LEU   A 1 43  ? 30.547 6.789   0.279   0.40 10.73 ?  43  LEU   A O    1 
ATOM   1098 C  CB   A LEU   A 1 43  ? 31.855 4.266   0.347   0.60 10.20 ?  43  LEU   A CB   1 
ATOM   1099 C  CB   B LEU   A 1 43  ? 31.754 4.301   0.355   0.40 9.89  ?  43  LEU   A CB   1 
ATOM   1100 C  CG   A LEU   A 1 43  ? 32.355 2.821   0.434   0.60 10.50 ?  43  LEU   A CG   1 
ATOM   1101 C  CG   B LEU   A 1 43  ? 32.220 2.845   0.442   0.40 9.96  ?  43  LEU   A CG   1 
ATOM   1102 C  CD1  A LEU   A 1 43  ? 33.430 2.724   1.504   0.60 11.16 ?  43  LEU   A CD1  1 
ATOM   1103 C  CD1  B LEU   A 1 43  ? 33.250 2.699   1.548   0.40 10.52 ?  43  LEU   A CD1  1 
ATOM   1104 C  CD2  A LEU   A 1 43  ? 31.234 1.834   0.716   0.60 10.79 ?  43  LEU   A CD2  1 
ATOM   1105 C  CD2  B LEU   A 1 43  ? 31.052 1.887   0.654   0.40 10.26 ?  43  LEU   A CD2  1 
ATOM   1106 H  H    A LEU   A 1 43  ? 30.851 3.515   -2.349  0.60 11.89 ?  43  LEU   A H    1 
ATOM   1107 H  H    B LEU   A 1 43  ? 30.854 3.511   -2.356  0.40 12.22 ?  43  LEU   A H    1 
ATOM   1108 H  HA   A LEU   A 1 43  ? 30.015 4.014   -0.475  0.60 11.39 ?  43  LEU   A HA   1 
ATOM   1109 H  HA   B LEU   A 1 43  ? 29.942 4.043   -0.530  0.40 11.99 ?  43  LEU   A HA   1 
ATOM   1110 H  HB2  A LEU   A 1 43  ? 32.624 4.824   0.160   0.60 12.21 ?  43  LEU   A HB2  1 
ATOM   1111 H  HB2  B LEU   A 1 43  ? 32.535 4.849   0.189   0.40 11.85 ?  43  LEU   A HB2  1 
ATOM   1112 H  HB3  A LEU   A 1 43  ? 31.499 4.489   1.220   0.60 12.21 ?  43  LEU   A HB3  1 
ATOM   1113 H  HB3  B LEU   A 1 43  ? 31.372 4.533   1.217   0.40 11.85 ?  43  LEU   A HB3  1 
ATOM   1114 H  HG   A LEU   A 1 43  ? 32.763 2.578   -0.413  0.60 12.58 ?  43  LEU   A HG   1 
ATOM   1115 H  HG   B LEU   A 1 43  ? 32.649 2.608   -0.394  0.40 11.92 ?  43  LEU   A HG   1 
ATOM   1116 H  HD11 A LEU   A 1 43  ? 33.744 1.807   1.554   0.60 13.36 ?  43  LEU   A HD11 1 
ATOM   1117 H  HD11 B LEU   A 1 43  ? 33.538 1.774   1.589   0.40 12.60 ?  43  LEU   A HD11 1 
ATOM   1118 H  HD12 A LEU   A 1 43  ? 34.164 3.313   1.272   0.60 13.36 ?  43  LEU   A HD12 1 
ATOM   1119 H  HD12 B LEU   A 1 43  ? 34.007 3.273   1.352   0.40 12.60 ?  43  LEU   A HD12 1 
ATOM   1120 H  HD13 A LEU   A 1 43  ? 33.050 2.988   2.357   0.60 13.36 ?  43  LEU   A HD13 1 
ATOM   1121 H  HD13 B LEU   A 1 43  ? 32.846 2.958   2.391   0.40 12.60 ?  43  LEU   A HD13 1 
ATOM   1122 H  HD21 A LEU   A 1 43  ? 31.617 0.951   0.835   0.60 12.92 ?  43  LEU   A HD21 1 
ATOM   1123 H  HD21 B LEU   A 1 43  ? 31.402 1.003   0.843   0.40 12.29 ?  43  LEU   A HD21 1 
ATOM   1124 H  HD22 A LEU   A 1 43  ? 30.773 2.109   1.523   0.60 12.92 ?  43  LEU   A HD22 1 
ATOM   1125 H  HD22 B LEU   A 1 43  ? 30.520 2.201   1.401   0.40 12.29 ?  43  LEU   A HD22 1 
ATOM   1126 H  HD23 A LEU   A 1 43  ? 30.623 1.834   -0.035  0.60 12.92 ?  43  LEU   A HD23 1 
ATOM   1127 H  HD23 B LEU   A 1 43  ? 30.513 1.865   -0.152  0.40 12.29 ?  43  LEU   A HD23 1 
ATOM   1128 N  N    A LYS   A 1 44  ? 29.585 6.480   -1.608  0.60 9.67  ?  44  LYS   A N    1 
ATOM   1129 N  N    B LYS   A 1 44  ? 29.467 6.454   -1.667  0.40 10.65 ?  44  LYS   A N    1 
ATOM   1130 C  CA   A LYS   A 1 44  ? 28.948 7.794   -1.591  0.60 10.15 ?  44  LYS   A CA   1 
ATOM   1131 C  CA   B LYS   A 1 44  ? 28.809 7.760   -1.674  0.40 11.39 ?  44  LYS   A CA   1 
ATOM   1132 C  C    A LYS   A 1 44  ? 27.516 7.613   -1.102  0.60 9.18  ?  44  LYS   A C    1 
ATOM   1133 C  C    B LYS   A 1 44  ? 27.399 7.573   -1.133  0.40 10.65 ?  44  LYS   A C    1 
ATOM   1134 O  O    A LYS   A 1 44  ? 26.660 7.092   -1.824  0.60 10.30 ?  44  LYS   A O    1 
ATOM   1135 O  O    B LYS   A 1 44  ? 26.505 7.096   -1.836  0.40 10.99 ?  44  LYS   A O    1 
ATOM   1136 C  CB   A LYS   A 1 44  ? 28.994 8.438   -2.972  0.60 12.04 ?  44  LYS   A CB   1 
ATOM   1137 C  CB   B LYS   A 1 44  ? 28.811 8.362   -3.076  0.40 13.50 ?  44  LYS   A CB   1 
ATOM   1138 C  CG   A LYS   A 1 44  ? 30.385 8.876   -3.407  0.60 15.02 ?  44  LYS   A CG   1 
ATOM   1139 C  CG   B LYS   A 1 44  ? 30.164 8.907   -3.520  0.40 16.31 ?  44  LYS   A CG   1 
ATOM   1140 C  CD   A LYS   A 1 44  ? 31.027 9.859   -2.426  0.60 19.96 ?  44  LYS   A CD   1 
ATOM   1141 C  CD   B LYS   A 1 44  ? 30.936 9.511   -2.352  0.40 19.80 ?  44  LYS   A CD   1 
ATOM   1142 C  CE   A LYS   A 1 44  ? 32.389 10.320  -2.917  0.60 23.26 ?  44  LYS   A CE   1 
ATOM   1143 C  CE   B LYS   A 1 44  ? 32.102 10.355  -2.820  0.40 21.74 ?  44  LYS   A CE   1 
ATOM   1144 N  NZ   A LYS   A 1 44  ? 33.145 11.051  -1.866  0.60 24.89 ?  44  LYS   A NZ   1 
ATOM   1145 N  NZ   B LYS   A 1 44  ? 33.033 10.677  -1.701  0.40 22.36 ?  44  LYS   A NZ   1 
ATOM   1146 H  H    A LYS   A 1 44  ? 29.463 6.045   -2.339  0.60 11.58 ?  44  LYS   A H    1 
ATOM   1147 H  H    B LYS   A 1 44  ? 29.312 5.987   -2.375  0.40 12.76 ?  44  LYS   A H    1 
ATOM   1148 H  HA   A LYS   A 1 44  ? 29.409 8.368   -0.957  0.60 12.16 ?  44  LYS   A HA   1 
ATOM   1149 H  HA   B LYS   A 1 44  ? 29.260 8.352   -1.055  0.40 13.64 ?  44  LYS   A HA   1 
ATOM   1150 H  HB2  A LYS   A 1 44  ? 28.667 7.803   -3.624  0.60 14.42 ?  44  LYS   A HB2  1 
ATOM   1151 H  HB2  B LYS   A 1 44  ? 28.550 7.677   -3.714  0.40 16.18 ?  44  LYS   A HB2  1 
ATOM   1152 H  HB3  A LYS   A 1 44  ? 28.428 9.227   -2.965  0.60 14.42 ?  44  LYS   A HB3  1 
ATOM   1153 H  HB3  B LYS   A 1 44  ? 28.176 9.095   -3.108  0.40 16.18 ?  44  LYS   A HB3  1 
ATOM   1154 H  HG2  A LYS   A 1 44  ? 30.960 8.097   -3.472  0.60 18.00 ?  44  LYS   A HG2  1 
ATOM   1155 H  HG2  B LYS   A 1 44  ? 30.693 8.187   -3.896  0.40 19.55 ?  44  LYS   A HG2  1 
ATOM   1156 H  HG3  A LYS   A 1 44  ? 30.326 9.316   -4.272  0.60 18.00 ?  44  LYS   A HG3  1 
ATOM   1157 H  HG3  B LYS   A 1 44  ? 30.028 9.604   -4.184  0.40 19.55 ?  44  LYS   A HG3  1 
ATOM   1158 H  HD2  A LYS   A 1 44  ? 30.448 10.629  -2.326  0.60 23.92 ?  44  LYS   A HD2  1 
ATOM   1159 H  HD2  B LYS   A 1 44  ? 30.338 10.076  -1.832  0.40 23.73 ?  44  LYS   A HD2  1 
ATOM   1160 H  HD3  A LYS   A 1 44  ? 31.150 9.416   -1.569  0.60 23.92 ?  44  LYS   A HD3  1 
ATOM   1161 H  HD3  B LYS   A 1 44  ? 31.285 8.794   -1.795  0.40 23.73 ?  44  LYS   A HD3  1 
ATOM   1162 H  HE2  A LYS   A 1 44  ? 32.907 9.544   -3.181  0.60 27.89 ?  44  LYS   A HE2  1 
ATOM   1163 H  HE2  B LYS   A 1 44  ? 32.597 9.868   -3.495  0.40 26.07 ?  44  LYS   A HE2  1 
ATOM   1164 H  HE3  A LYS   A 1 44  ? 32.264 10.913  -3.672  0.60 27.89 ?  44  LYS   A HE3  1 
ATOM   1165 H  HE3  B LYS   A 1 44  ? 31.765 11.188  -3.184  0.40 26.07 ?  44  LYS   A HE3  1 
ATOM   1166 H  HZ1  A LYS   A 1 44  ? 33.942 11.289  -2.179  0.60 29.84 ?  44  LYS   A HZ1  1 
ATOM   1167 H  HZ1  B LYS   A 1 44  ? 33.708 11.175  -2.002  0.40 26.81 ?  44  LYS   A HZ1  1 
ATOM   1168 H  HZ2  A LYS   A 1 44  ? 32.698 11.781  -1.623  0.60 29.84 ?  44  LYS   A HZ2  1 
ATOM   1169 H  HZ2  B LYS   A 1 44  ? 32.602 11.131  -1.067  0.40 26.81 ?  44  LYS   A HZ2  1 
ATOM   1170 H  HZ3  A LYS   A 1 44  ? 33.257 10.529  -1.153  0.60 29.84 ?  44  LYS   A HZ3  1 
ATOM   1171 H  HZ3  B LYS   A 1 44  ? 33.359 9.929   -1.350  0.40 26.81 ?  44  LYS   A HZ3  1 
ATOM   1172 N  N    A HIS   A 1 45  ? 27.268 8.017   0.137   0.60 8.64  ?  45  HIS   A N    1 
ATOM   1173 N  N    B HIS   A 1 45  ? 27.205 7.940   0.131   0.40 10.67 ?  45  HIS   A N    1 
ATOM   1174 C  CA   A HIS   A 1 45  ? 26.038 7.647   0.830   0.60 8.80  ?  45  HIS   A CA   1 
ATOM   1175 C  CA   B HIS   A 1 45  ? 25.958 7.653   0.837   0.40 10.91 ?  45  HIS   A CA   1 
ATOM   1176 C  C    A HIS   A 1 45  ? 24.994 8.753   0.676   0.60 9.64  ?  45  HIS   A C    1 
ATOM   1177 C  C    B HIS   A 1 45  ? 25.006 8.824   0.644   0.40 11.21 ?  45  HIS   A C    1 
ATOM   1178 O  O    A HIS   A 1 45  ? 24.618 9.441   1.625   0.60 10.24 ?  45  HIS   A O    1 
ATOM   1179 O  O    B HIS   A 1 45  ? 24.911 9.722   1.481   0.40 11.98 ?  45  HIS   A O    1 
ATOM   1180 C  CB   A HIS   A 1 45  ? 26.342 7.366   2.291   0.60 8.53  ?  45  HIS   A CB   1 
ATOM   1181 C  CB   B HIS   A 1 45  ? 26.236 7.407   2.310   0.40 10.79 ?  45  HIS   A CB   1 
ATOM   1182 C  CG   A HIS   A 1 45  ? 27.451 6.387   2.493   0.60 8.28  ?  45  HIS   A CG   1 
ATOM   1183 C  CG   B HIS   A 1 45  ? 27.375 6.474   2.560   0.40 10.05 ?  45  HIS   A CG   1 
ATOM   1184 N  ND1  A HIS   A 1 45  ? 27.422 5.105   1.982   0.60 8.83  ?  45  HIS   A ND1  1 
ATOM   1185 N  ND1  B HIS   A 1 45  ? 27.403 5.180   2.082   0.40 10.36 ?  45  HIS   A ND1  1 
ATOM   1186 C  CD2  A HIS   A 1 45  ? 28.629 6.512   3.147   0.60 9.11  ?  45  HIS   A CD2  1 
ATOM   1187 C  CD2  B HIS   A 1 45  ? 28.530 6.651   3.242   0.40 9.44  ?  45  HIS   A CD2  1 
ATOM   1188 C  CE1  A HIS   A 1 45  ? 28.538 4.482   2.326   0.60 9.07  ?  45  HIS   A CE1  1 
ATOM   1189 C  CE1  B HIS   A 1 45  ? 28.528 4.602   2.463   0.40 9.34  ?  45  HIS   A CE1  1 
ATOM   1190 N  NE2  A HIS   A 1 45  ? 29.287 5.313   3.032   0.60 9.53  ?  45  HIS   A NE2  1 
ATOM   1191 N  NE2  B HIS   A 1 45  ? 29.230 5.473   3.169   0.40 8.95  ?  45  HIS   A NE2  1 
ATOM   1192 H  H    A HIS   A 1 45  ? 27.794 8.522   0.604   0.60 10.34 ?  45  HIS   A H    1 
ATOM   1193 H  H    B HIS   A 1 45  ? 27.786 8.366   0.608   0.40 12.78 ?  45  HIS   A H    1 
ATOM   1194 H  HA   A HIS   A 1 45  ? 25.681 6.838   0.434   0.60 10.54 ?  45  HIS   A HA   1 
ATOM   1195 H  HA   B HIS   A 1 45  ? 25.549 6.863   0.459   0.40 13.06 ?  45  HIS   A HA   1 
ATOM   1196 H  HB2  A HIS   A 1 45  ? 26.592 8.194   2.728   0.60 10.22 ?  45  HIS   A HB2  1 
ATOM   1197 H  HB2  B HIS   A 1 45  ? 26.444 8.254   2.734   0.40 12.92 ?  45  HIS   A HB2  1 
ATOM   1198 H  HB3  A HIS   A 1 45  ? 25.544 7.001   2.712   0.60 10.22 ?  45  HIS   A HB3  1 
ATOM   1199 H  HB3  B HIS   A 1 45  ? 25.442 7.024   2.714   0.40 12.92 ?  45  HIS   A HB3  1 
ATOM   1200 H  HD2  A HIS   A 1 45  ? 28.939 7.271   3.591   0.60 10.91 ?  45  HIS   A HD2  1 
ATOM   1201 H  HD2  B HIS   A 1 45  ? 28.798 7.430   3.679   0.40 11.31 ?  45  HIS   A HD2  1 
ATOM   1202 H  HE1  A HIS   A 1 45  ? 28.758 3.600   2.120   0.60 10.86 ?  45  HIS   A HE1  1 
ATOM   1203 H  HE1  B HIS   A 1 45  ? 28.780 3.730   2.272   0.40 11.18 ?  45  HIS   A HE1  1 
ATOM   1204 H  HE2  A HIS   A 1 45  ? 30.062 5.133   3.365   0.60 11.41 ?  45  HIS   A HE2  1 
ATOM   1205 H  HE2  B HIS   A 1 45  ? 29.997 5.327   3.524   0.40 10.72 ?  45  HIS   A HE2  1 
ATOM   1206 N  N    A GLY   A 1 46  ? 24.514 8.905   -0.555  0.60 10.56 ?  46  GLY   A N    1 
ATOM   1207 N  N    B GLY   A 1 46  ? 24.276 8.808   -0.466  0.40 10.95 ?  46  GLY   A N    1 
ATOM   1208 C  CA   A GLY   A 1 46  ? 23.728 10.075  -0.907  0.60 11.32 ?  46  GLY   A CA   1 
ATOM   1209 C  CA   B GLY   A 1 46  ? 23.441 9.942   -0.814  0.40 10.99 ?  46  GLY   A CA   1 
ATOM   1210 C  C    A GLY   A 1 46  ? 22.235 9.952   -0.681  0.60 11.08 ?  46  GLY   A C    1 
ATOM   1211 C  C    B GLY   A 1 46  ? 21.986 9.810   -0.412  0.40 10.68 ?  46  GLY   A C    1 
ATOM   1212 O  O    A GLY   A 1 46  ? 21.562 10.951  -0.413  0.60 11.60 ?  46  GLY   A O    1 
ATOM   1213 O  O    B GLY   A 1 46  ? 21.377 10.779  0.052   0.40 11.14 ?  46  GLY   A O    1 
ATOM   1214 H  H    A GLY   A 1 46  ? 24.626 8.344   -1.197  0.60 12.65 ?  46  GLY   A H    1 
ATOM   1215 H  H    B GLY   A 1 46  ? 24.252 8.155   -1.025  0.40 13.12 ?  46  GLY   A H    1 
ATOM   1216 H  HA2  A GLY   A 1 46  ? 24.051 10.833  -0.390  0.60 13.56 ?  46  GLY   A HA2  1 
ATOM   1217 H  HA2  B GLY   A 1 46  ? 23.793 10.740  -0.388  0.40 13.16 ?  46  GLY   A HA2  1 
ATOM   1218 H  HA3  A GLY   A 1 46  ? 23.871 10.276  -1.845  0.60 13.56 ?  46  GLY   A HA3  1 
ATOM   1219 H  HA3  B GLY   A 1 46  ? 23.477 10.075  -1.772  0.40 13.16 ?  46  GLY   A HA3  1 
ATOM   1220 N  N    A GLY   A 1 47  ? 21.700 8.744   -0.810  0.60 10.91 ?  47  GLY   A N    1 
ATOM   1221 N  N    B GLY   A 1 47  ? 21.414 8.626   -0.589  0.40 10.68 ?  47  GLY   A N    1 
ATOM   1222 C  CA   A GLY   A 1 47  ? 20.265 8.537   -0.769  0.60 10.87 ?  47  GLY   A CA   1 
ATOM   1223 C  CA   B GLY   A 1 47  ? 19.998 8.441   -0.361  0.40 10.77 ?  47  GLY   A CA   1 
ATOM   1224 C  C    A GLY   A 1 47  ? 19.945 7.103   -0.409  0.60 10.07 ?  47  GLY   A C    1 
ATOM   1225 C  C    B GLY   A 1 47  ? 19.667 7.002   -0.043  0.40 9.94  ?  47  GLY   A C    1 
ATOM   1226 O  O    A GLY   A 1 47  ? 20.834 6.280   -0.182  0.60 10.56 ?  47  GLY   A O    1 
ATOM   1227 O  O    B GLY   A 1 47  ? 20.553 6.156   0.098   0.40 9.77  ?  47  GLY   A O    1 
ATOM   1228 H  H    A GLY   A 1 47  ? 22.157 8.030   -0.910  0.60 13.07 ?  47  GLY   A H    1 
ATOM   1229 H  H    B GLY   A 1 47  ? 21.829 7.913   -0.831  0.40 12.79 ?  47  GLY   A H    1 
ATOM   1230 H  HA2  A GLY   A 1 47  ? 19.863 9.137   -0.117  0.60 13.02 ?  47  GLY   A HA2  1 
ATOM   1231 H  HA2  B GLY   A 1 47  ? 19.707 8.986   0.385   0.40 12.90 ?  47  GLY   A HA2  1 
ATOM   1232 H  HA3  A GLY   A 1 47  ? 19.888 8.735   -1.644  0.60 13.02 ?  47  GLY   A HA3  1 
ATOM   1233 H  HA3  B GLY   A 1 47  ? 19.501 8.707   -1.152  0.40 12.90 ?  47  GLY   A HA3  1 
ATOM   1234 N  N    A GLY   A 1 48  ? 18.653 6.799   -0.377  0.60 9.98  ?  48  GLY   A N    1 
ATOM   1235 N  N    B GLY   A 1 48  ? 18.367 6.731   0.066   0.40 9.97  ?  48  GLY   A N    1 
ATOM   1236 C  CA   A GLY   A 1 48  ? 18.263 5.457   -0.008  0.60 10.25 ?  48  GLY   A CA   1 
ATOM   1237 C  CA   B GLY   A 1 48  ? 17.936 5.401   0.454   0.40 9.61  ?  48  GLY   A CA   1 
ATOM   1238 C  C    A GLY   A 1 48  ? 18.656 5.140   1.428   0.60 10.05 ?  48  GLY   A C    1 
ATOM   1239 C  C    B GLY   A 1 48  ? 18.531 5.012   1.790   0.40 9.44  ?  48  GLY   A C    1 
ATOM   1240 O  O    A GLY   A 1 48  ? 18.818 6.026   2.274   0.60 10.46 ?  48  GLY   A O    1 
ATOM   1241 O  O    B GLY   A 1 48  ? 18.685 5.837   2.698   0.40 9.83  ?  48  GLY   A O    1 
ATOM   1242 H  H    A GLY   A 1 48  ? 18.014 7.339   -0.560  0.60 11.95 ?  48  GLY   A H    1 
ATOM   1243 H  H    B GLY   A 1 48  ? 17.723 7.291   -0.074  0.40 11.94 ?  48  GLY   A H    1 
ATOM   1244 H  HA2  A GLY   A 1 48  ? 17.307 5.361   -0.097  0.60 12.28 ?  48  GLY   A HA2  1 
ATOM   1245 H  HA2  B GLY   A 1 48  ? 16.965 5.367   0.518   0.40 11.50 ?  48  GLY   A HA2  1 
ATOM   1246 H  HA3  A GLY   A 1 48  ? 18.702 4.818   -0.589  0.60 12.28 ?  48  GLY   A HA3  1 
ATOM   1247 H  HA3  B GLY   A 1 48  ? 18.221 4.751   -0.210  0.40 11.50 ?  48  GLY   A HA3  1 
ATOM   1248 N  N    A VAL   A 1 49  ? 18.821 3.841   1.694   0.60 10.38 ?  49  VAL   A N    1 
ATOM   1249 N  N    B VAL   A 1 49  ? 18.878 3.732   1.911   0.40 9.49  ?  49  VAL   A N    1 
ATOM   1250 C  CA   A VAL   A 1 49  ? 19.261 3.405   3.016   0.60 10.31 ?  49  VAL   A CA   1 
ATOM   1251 C  CA   B VAL   A 1 49  ? 19.475 3.224   3.142   0.40 9.50  ?  49  VAL   A CA   1 
ATOM   1252 C  C    A VAL   A 1 49  ? 20.586 4.064   3.388   0.60 9.71  ?  49  VAL   A C    1 
ATOM   1253 C  C    B VAL   A 1 49  ? 20.745 3.993   3.482   0.40 8.74  ?  49  VAL   A C    1 
ATOM   1254 O  O    A VAL   A 1 49  ? 20.781 4.490   4.532   0.60 10.02 ?  49  VAL   A O    1 
ATOM   1255 O  O    B VAL   A 1 49  ? 20.951 4.410   4.627   0.40 8.88  ?  49  VAL   A O    1 
ATOM   1256 C  CB   A VAL   A 1 49  ? 19.347 1.866   3.070   0.60 11.66 ?  49  VAL   A CB   1 
ATOM   1257 C  CB   B VAL   A 1 49  ? 19.752 1.716   3.010   0.40 9.70  ?  49  VAL   A CB   1 
ATOM   1258 C  CG1  A VAL   A 1 49  ? 20.087 1.409   4.326   0.60 12.30 ?  49  VAL   A CG1  1 
ATOM   1259 C  CG1  B VAL   A 1 49  ? 20.586 1.237   4.187   0.40 9.24  ?  49  VAL   A CG1  1 
ATOM   1260 C  CG2  A VAL   A 1 49  ? 17.955 1.249   3.011   0.60 13.24 ?  49  VAL   A CG2  1 
ATOM   1261 C  CG2  B VAL   A 1 49  ? 18.448 0.935   2.896   0.40 9.99  ?  49  VAL   A CG2  1 
ATOM   1262 H  H    A VAL   A 1 49  ? 18.684 3.201   1.137   0.60 12.43 ?  49  VAL   A H    1 
ATOM   1263 H  H    B VAL   A 1 49  ? 18.781 3.140   1.300   0.40 11.37 ?  49  VAL   A H    1 
ATOM   1264 H  HA   A VAL   A 1 49  ? 18.602 3.679   3.673   0.60 12.35 ?  49  VAL   A HA   1 
ATOM   1265 H  HA   B VAL   A 1 49  ? 18.855 3.349   3.874   0.40 11.38 ?  49  VAL   A HA   1 
ATOM   1266 H  HB   A VAL   A 1 49  ? 19.848 1.548   2.302   0.60 13.97 ?  49  VAL   A HB   1 
ATOM   1267 H  HB   B VAL   A 1 49  ? 20.263 1.561   2.200   0.40 11.61 ?  49  VAL   A HB   1 
ATOM   1268 H  HG11 A VAL   A 1 49  ? 19.895 0.470   4.481   0.60 14.74 ?  49  VAL   A HG11 1 
ATOM   1269 H  HG11 B VAL   A 1 49  ? 20.496 0.275   4.264   0.40 11.06 ?  49  VAL   A HG11 1 
ATOM   1270 H  HG12 A VAL   A 1 49  ? 21.039 1.535   4.201   0.60 14.74 ?  49  VAL   A HG12 1 
ATOM   1271 H  HG12 B VAL   A 1 49  ? 21.517 1.469   4.034   0.40 11.06 ?  49  VAL   A HG12 1 
ATOM   1272 H  HG13 A VAL   A 1 49  ? 19.777 1.935   5.083   0.60 14.74 ?  49  VAL   A HG13 1 
ATOM   1273 H  HG13 B VAL   A 1 49  ? 20.265 1.664   4.997   0.40 11.06 ?  49  VAL   A HG13 1 
ATOM   1274 H  HG21 A VAL   A 1 49  ? 18.036 0.282   3.042   0.60 15.87 ?  49  VAL   A HG21 1 
ATOM   1275 H  HG21 B VAL   A 1 49  ? 18.651 -0.005  2.778   0.40 11.96 ?  49  VAL   A HG21 1 
ATOM   1276 H  HG22 A VAL   A 1 49  ? 17.440 1.561   3.771   0.60 15.87 ?  49  VAL   A HG22 1 
ATOM   1277 H  HG22 B VAL   A 1 49  ? 17.931 1.063   3.708   0.40 11.96 ?  49  VAL   A HG22 1 
ATOM   1278 H  HG23 A VAL   A 1 49  ? 17.527 1.519   2.185   0.60 15.87 ?  49  VAL   A HG23 1 
ATOM   1279 H  HG23 B VAL   A 1 49  ? 17.947 1.264   2.132   0.40 11.96 ?  49  VAL   A HG23 1 
ATOM   1280 N  N    A ALA   A 1 50  ? 21.523 4.132   2.440   0.60 9.48  ?  50  ALA   A N    1 
ATOM   1281 N  N    B ALA   A 1 50  ? 21.633 4.158   2.498   0.40 8.43  ?  50  ALA   A N    1 
ATOM   1282 C  CA   A ALA   A 1 50  ? 22.846 4.677   2.734   0.60 9.43  ?  50  ALA   A CA   1 
ATOM   1283 C  CA   B ALA   A 1 50  ? 22.941 4.741   2.776   0.40 8.71  ?  50  ALA   A CA   1 
ATOM   1284 C  C    A ALA   A 1 50  ? 22.766 6.139   3.140   0.60 9.50  ?  50  ALA   A C    1 
ATOM   1285 C  C    B ALA   A 1 50  ? 22.815 6.180   3.253   0.40 8.59  ?  50  ALA   A C    1 
ATOM   1286 O  O    A ALA   A 1 50  ? 23.407 6.564   4.108   0.60 9.83  ?  50  ALA   A O    1 
ATOM   1287 O  O    B ALA   A 1 50  ? 23.436 6.574   4.247   0.40 8.47  ?  50  ALA   A O    1 
ATOM   1288 C  CB   A ALA   A 1 50  ? 23.749 4.519   1.514   0.60 9.45  ?  50  ALA   A CB   1 
ATOM   1289 C  CB   B ALA   A 1 50  ? 23.829 4.654   1.534   0.40 8.60  ?  50  ALA   A CB   1 
ATOM   1290 H  H    A ALA   A 1 50  ? 21.418 3.873   1.629   0.60 11.35 ?  50  ALA   A H    1 
ATOM   1291 H  H    B ALA   A 1 50  ? 21.501 3.944   1.675   0.40 10.09 ?  50  ALA   A H    1 
ATOM   1292 H  HA   A ALA   A 1 50  ? 23.238 4.186   3.473   0.60 11.29 ?  50  ALA   A HA   1 
ATOM   1293 H  HA   B ALA   A 1 50  ? 23.367 4.236   3.483   0.40 10.42 ?  50  ALA   A HA   1 
ATOM   1294 H  HB1  A ALA   A 1 50  ? 24.623 4.886   1.721   0.60 11.32 ?  50  ALA   A HB1  1 
ATOM   1295 H  HB1  B ALA   A 1 50  ? 24.696 5.042   1.738   0.40 10.30 ?  50  ALA   A HB1  1 
ATOM   1296 H  HB2  A ALA   A 1 50  ? 23.824 3.580   1.297   0.60 11.32 ?  50  ALA   A HB2  1 
ATOM   1297 H  HB2  B ALA   A 1 50  ? 23.936 3.722   1.287   0.40 10.30 ?  50  ALA   A HB2  1 
ATOM   1298 H  HB3  A ALA   A 1 50  ? 23.356 5.004   0.770   0.60 11.32 ?  50  ALA   A HB3  1 
ATOM   1299 H  HB3  B ALA   A 1 50  ? 23.411 5.143   0.809   0.40 10.30 ?  50  ALA   A HB3  1 
ATOM   1300 N  N    A GLY   A 1 51  ? 22.004 6.934   2.393   0.60 9.70  ?  51  GLY   A N    1 
ATOM   1301 N  N    B GLY   A 1 51  ? 22.017 6.985   2.552   0.40 8.96  ?  51  GLY   A N    1 
ATOM   1302 C  CA   A GLY   A 1 51  ? 21.864 8.331   2.749   0.60 9.53  ?  51  GLY   A CA   1 
ATOM   1303 C  CA   B GLY   A 1 51  ? 21.820 8.356   2.987   0.40 9.27  ?  51  GLY   A CA   1 
ATOM   1304 C  C    A GLY   A 1 51  ? 21.254 8.510   4.125   0.60 9.04  ?  51  GLY   A C    1 
ATOM   1305 C  C    B GLY   A 1 51  ? 21.204 8.432   4.369   0.40 9.86  ?  51  GLY   A C    1 
ATOM   1306 O  O    A GLY   A 1 51  ? 21.652 9.401   4.882   0.60 9.49  ?  51  GLY   A O    1 
ATOM   1307 O  O    B GLY   A 1 51  ? 21.558 9.299   5.174   0.40 10.00 ?  51  GLY   A O    1 
ATOM   1308 H  H    A GLY   A 1 51  ? 21.583 6.691   1.684   0.60 11.62 ?  51  GLY   A H    1 
ATOM   1309 H  H    B GLY   A 1 51  ? 21.592 6.764   1.837   0.40 10.72 ?  51  GLY   A H    1 
ATOM   1310 H  HA2  A GLY   A 1 51  ? 22.736 8.758   2.745   0.60 11.41 ?  51  GLY   A HA2  1 
ATOM   1311 H  HA2  B GLY   A 1 51  ? 22.673 8.818   3.001   0.40 11.10 ?  51  GLY   A HA2  1 
ATOM   1312 H  HA3  A GLY   A 1 51  ? 21.302 8.778   2.096   0.60 11.41 ?  51  GLY   A HA3  1 
ATOM   1313 H  HA3  B GLY   A 1 51  ? 21.235 8.812   2.359   0.40 11.10 ?  51  GLY   A HA3  1 
ATOM   1314 N  N    A ALA   A 1 52  ? 20.276 7.668   4.466   0.60 9.11  ?  52  ALA   A N    1 
ATOM   1315 N  N    B ALA   A 1 52  ? 20.277 7.518   4.664   0.40 10.23 ?  52  ALA   A N    1 
ATOM   1316 C  CA   A ALA   A 1 52  ? 19.624 7.768   5.768   0.60 9.60  ?  52  ALA   A CA   1 
ATOM   1317 C  CA   B ALA   A 1 52  ? 19.620 7.510   5.965   0.40 9.98  ?  52  ALA   A CA   1 
ATOM   1318 C  C    A ALA   A 1 52  ? 20.555 7.336   6.899   0.60 9.10  ?  52  ALA   A C    1 
ATOM   1319 C  C    B ALA   A 1 52  ? 20.591 7.117   7.073   0.40 9.58  ?  52  ALA   A C    1 
ATOM   1320 O  O    A ALA   A 1 52  ? 20.637 8.004   7.937   0.60 10.23 ?  52  ALA   A O    1 
ATOM   1321 O  O    B ALA   A 1 52  ? 20.652 7.772   8.121   0.40 9.98  ?  52  ALA   A O    1 
ATOM   1322 C  CB   A ALA   A 1 52  ? 18.335 6.947   5.771   0.60 10.44 ?  52  ALA   A CB   1 
ATOM   1323 C  CB   B ALA   A 1 52  ? 18.418 6.567   5.926   0.40 10.66 ?  52  ALA   A CB   1 
ATOM   1324 H  H    A ALA   A 1 52  ? 19.983 7.032   3.962   0.60 10.90 ?  52  ALA   A H    1 
ATOM   1325 H  H    B ALA   A 1 52  ? 20.020 6.892   4.129   0.40 12.25 ?  52  ALA   A H    1 
ATOM   1326 H  HA   A ALA   A 1 52  ? 19.383 8.694   5.915   0.60 11.50 ?  52  ALA   A HA   1 
ATOM   1327 H  HA   B ALA   A 1 52  ? 19.297 8.398   6.157   0.40 11.96 ?  52  ALA   A HA   1 
ATOM   1328 H  HB1  A ALA   A 1 52  ? 17.914 7.028   6.642   0.60 12.51 ?  52  ALA   A HB1  1 
ATOM   1329 H  HB1  B ALA   A 1 52  ? 17.955 6.610   6.777   0.40 12.77 ?  52  ALA   A HB1  1 
ATOM   1330 H  HB2  A ALA   A 1 52  ? 17.738 7.288   5.085   0.60 12.51 ?  52  ALA   A HB2  1 
ATOM   1331 H  HB2  B ALA   A 1 52  ? 17.822 6.849   5.213   0.40 12.77 ?  52  ALA   A HB2  1 
ATOM   1332 H  HB3  A ALA   A 1 52  ? 18.548 6.018   5.592   0.60 12.51 ?  52  ALA   A HB3  1 
ATOM   1333 H  HB3  B ALA   A 1 52  ? 18.726 5.663   5.758   0.40 12.77 ?  52  ALA   A HB3  1 
ATOM   1334 N  N    A LEU   A 1 53  ? 21.261 6.214   6.727   0.60 9.04  ?  53  LEU   A N    1 
ATOM   1335 N  N    B LEU   A 1 53  ? 21.352 6.039   6.872   0.40 9.20  ?  53  LEU   A N    1 
ATOM   1336 C  CA   A LEU   A 1 53  ? 22.206 5.783   7.757   0.60 9.71  ?  53  LEU   A CA   1 
ATOM   1337 C  CA   B LEU   A 1 53  ? 22.371 5.680   7.854   0.40 9.14  ?  53  LEU   A CA   1 
ATOM   1338 C  C    A LEU   A 1 53  ? 23.296 6.825   7.963   0.60 9.69  ?  53  LEU   A C    1 
ATOM   1339 C  C    B LEU   A 1 53  ? 23.365 6.819   8.040   0.40 9.23  ?  53  LEU   A C    1 
ATOM   1340 O  O    A LEU   A 1 53  ? 23.664 7.139   9.100   0.60 10.52 ?  53  LEU   A O    1 
ATOM   1341 O  O    B LEU   A 1 53  ? 23.654 7.231   9.169   0.40 9.83  ?  53  LEU   A O    1 
ATOM   1342 C  CB   A LEU   A 1 53  ? 22.833 4.438   7.382   0.60 10.32 ?  53  LEU   A CB   1 
ATOM   1343 C  CB   B LEU   A 1 53  ? 23.097 4.399   7.435   0.40 8.85  ?  53  LEU   A CB   1 
ATOM   1344 C  CG   A LEU   A 1 53  ? 21.939 3.194   7.437   0.60 10.66 ?  53  LEU   A CG   1 
ATOM   1345 C  CG   B LEU   A 1 53  ? 22.319 3.083   7.503   0.40 8.99  ?  53  LEU   A CG   1 
ATOM   1346 C  CD1  A LEU   A 1 53  ? 22.666 1.989   6.856   0.60 10.73 ?  53  LEU   A CD1  1 
ATOM   1347 C  CD1  B LEU   A 1 53  ? 23.134 1.967   6.868   0.40 9.44  ?  53  LEU   A CD1  1 
ATOM   1348 C  CD2  A LEU   A 1 53  ? 21.491 2.903   8.860   0.60 11.51 ?  53  LEU   A CD2  1 
ATOM   1349 C  CD2  B LEU   A 1 53  ? 21.962 2.724   8.938   0.40 9.16  ?  53  LEU   A CD2  1 
ATOM   1350 H  H    A LEU   A 1 53  ? 21.216 5.701   6.042   0.60 10.83 ?  53  LEU   A H    1 
ATOM   1351 H  H    B LEU   A 1 53  ? 21.299 5.504   6.192   0.40 11.02 ?  53  LEU   A H    1 
ATOM   1352 H  HA   A LEU   A 1 53  ? 21.733 5.672   8.598   0.60 11.63 ?  53  LEU   A HA   1 
ATOM   1353 H  HA   B LEU   A 1 53  ? 21.942 5.513   8.705   0.40 10.94 ?  53  LEU   A HA   1 
ATOM   1354 H  HB2  A LEU   A 1 53  ? 23.166 4.507   6.474   0.60 12.36 ?  53  LEU   A HB2  1 
ATOM   1355 H  HB2  B LEU   A 1 53  ? 23.394 4.503   6.518   0.40 10.60 ?  53  LEU   A HB2  1 
ATOM   1356 H  HB3  A LEU   A 1 53  ? 23.577 4.275   7.982   0.60 12.36 ?  53  LEU   A HB3  1 
ATOM   1357 H  HB3  B LEU   A 1 53  ? 23.875 4.292   8.009   0.40 10.60 ?  53  LEU   A HB3  1 
ATOM   1358 H  HG   A LEU   A 1 53  ? 21.145 3.353   6.899   0.60 12.77 ?  53  LEU   A HG   1 
ATOM   1359 H  HG   B LEU   A 1 53  ? 21.497 3.172   6.998   0.40 10.76 ?  53  LEU   A HG   1 
ATOM   1360 H  HD11 A LEU   A 1 53  ? 22.080 1.217   6.902   0.60 12.85 ?  53  LEU   A HD11 1 
ATOM   1361 H  HD11 B LEU   A 1 53  ? 22.632 1.138   6.919   0.40 11.31 ?  53  LEU   A HD11 1 
ATOM   1362 H  HD12 A LEU   A 1 53  ? 22.899 2.174   5.934   0.60 12.85 ?  53  LEU   A HD12 1 
ATOM   1363 H  HD12 B LEU   A 1 53  ? 23.309 2.191   5.941   0.40 11.31 ?  53  LEU   A HD12 1 
ATOM   1364 H  HD13 A LEU   A 1 53  ? 23.468 1.827   7.376   0.60 12.85 ?  53  LEU   A HD13 1 
ATOM   1365 H  HD13 B LEU   A 1 53  ? 23.972 1.875   7.350   0.40 11.31 ?  53  LEU   A HD13 1 
ATOM   1366 H  HD21 A LEU   A 1 53  ? 20.984 2.078   8.867   0.60 13.79 ?  53  LEU   A HD21 1 
ATOM   1367 H  HD21 B LEU   A 1 53  ? 21.429 1.912   8.938   0.40 10.97 ?  53  LEU   A HD21 1 
ATOM   1368 H  HD22 A LEU   A 1 53  ? 22.276 2.816   9.423   0.60 13.79 ?  53  LEU   A HD22 1 
ATOM   1369 H  HD22 B LEU   A 1 53  ? 22.777 2.584   9.442   0.40 10.97 ?  53  LEU   A HD22 1 
ATOM   1370 H  HD23 A LEU   A 1 53  ? 20.939 3.635   9.174   0.60 13.79 ?  53  LEU   A HD23 1 
ATOM   1371 H  HD23 B LEU   A 1 53  ? 21.452 3.451   9.329   0.40 10.97 ?  53  LEU   A HD23 1 
ATOM   1372 N  N    A ASN   A 1 54  ? 23.826 7.373   6.875   0.60 9.18  ?  54  ASN   A N    1 
ATOM   1373 N  N    B ASN   A 1 54  ? 23.894 7.350   6.938   0.40 9.14  ?  54  ASN   A N    1 
ATOM   1374 C  CA   A ASN   A 1 54  ? 24.889 8.357   7.023   0.60 9.19  ?  54  ASN   A CA   1 
ATOM   1375 C  CA   B ASN   A 1 54  ? 24.923 8.376   7.058   0.40 9.16  ?  54  ASN   A CA   1 
ATOM   1376 C  C    A ASN   A 1 54  ? 24.391 9.601   7.752   0.60 9.59  ?  54  ASN   A C    1 
ATOM   1377 C  C    B ASN   A 1 54  ? 24.394 9.619   7.766   0.40 9.46  ?  54  ASN   A C    1 
ATOM   1378 O  O    A ASN   A 1 54  ? 25.086 10.145  8.619   0.60 10.30 ?  54  ASN   A O    1 
ATOM   1379 O  O    B ASN   A 1 54  ? 25.074 10.184  8.632   0.40 9.73  ?  54  ASN   A O    1 
ATOM   1380 C  CB   A ASN   A 1 54  ? 25.457 8.725   5.664   0.60 9.37  ?  54  ASN   A CB   1 
ATOM   1381 C  CB   B ASN   A 1 54  ? 25.493 8.737   5.693   0.40 9.53  ?  54  ASN   A CB   1 
ATOM   1382 C  CG   A ASN   A 1 54  ? 26.502 9.796   5.779   0.60 9.49  ?  54  ASN   A CG   1 
ATOM   1383 C  CG   B ASN   A 1 54  ? 26.464 9.889   5.781   0.40 9.73  ?  54  ASN   A CG   1 
ATOM   1384 O  OD1  A ASN   A 1 54  ? 27.481 9.638   6.513   0.60 9.16  ?  54  ASN   A OD1  1 
ATOM   1385 O  OD1  B ASN   A 1 54  ? 27.518 9.769   6.406   0.40 9.84  ?  54  ASN   A OD1  1 
ATOM   1386 N  ND2  A ASN   A 1 54  ? 26.301 10.905  5.090   0.60 10.28 ?  54  ASN   A ND2  1 
ATOM   1387 N  ND2  B ASN   A 1 54  ? 26.107 11.022  5.191   0.40 10.31 ?  54  ASN   A ND2  1 
ATOM   1388 H  H    A ASN   A 1 54  ? 23.587 7.199   6.070   0.60 10.99 ?  54  ASN   A H    1 
ATOM   1389 H  H    B ASN   A 1 54  ? 23.675 7.138   6.134   0.40 10.94 ?  54  ASN   A H    1 
ATOM   1390 H  HA   A ASN   A 1 54  ? 25.598 7.965   7.550   0.60 11.00 ?  54  ASN   A HA   1 
ATOM   1391 H  HA   B ASN   A 1 54  ? 25.643 8.023   7.595   0.40 10.96 ?  54  ASN   A HA   1 
ATOM   1392 H  HB2  A ASN   A 1 54  ? 25.866 7.932   5.269   0.60 11.21 ?  54  ASN   A HB2  1 
ATOM   1393 H  HB2  B ASN   A 1 54  ? 25.968 7.965   5.337   0.40 11.41 ?  54  ASN   A HB2  1 
ATOM   1394 H  HB3  A ASN   A 1 54  ? 24.744 9.047   5.094   0.60 11.21 ?  54  ASN   A HB3  1 
ATOM   1395 H  HB3  B ASN   A 1 54  ? 24.772 8.987   5.098   0.40 11.41 ?  54  ASN   A HB3  1 
ATOM   1396 H  HD21 A ASN   A 1 54  ? 26.876 11.541  5.133   0.60 12.31 ?  54  ASN   A HD21 1 
ATOM   1397 H  HD21 B ASN   A 1 54  ? 26.630 11.706  5.224   0.40 12.35 ?  54  ASN   A HD21 1 
ATOM   1398 H  HD22 A ASN   A 1 54  ? 25.600 10.984  4.602   0.60 12.31 ?  54  ASN   A HD22 1 
ATOM   1399 H  HD22 B ASN   A 1 54  ? 25.360 11.071  4.772   0.40 12.35 ?  54  ASN   A HD22 1 
ATOM   1400 N  N    . LYS   A 1 55  ? 23.181 10.059  7.417   1.00 9.92  ?  55  LYS   A N    1 
ATOM   1401 C  CA   . LYS   A 1 55  ? 22.601 11.213  8.091   1.00 10.52 ?  55  LYS   A CA   1 
ATOM   1402 C  C    . LYS   A 1 55  ? 22.512 10.975  9.592   1.00 10.76 ?  55  LYS   A C    1 
ATOM   1403 O  O    . LYS   A 1 55  ? 22.794 11.878  10.389  1.00 11.38 ?  55  LYS   A O    1 
ATOM   1404 C  CB   . LYS   A 1 55  ? 21.228 11.514  7.487   1.00 11.31 ?  55  LYS   A CB   1 
ATOM   1405 C  CG   . LYS   A 1 55  ? 20.491 12.685  8.113   1.00 13.03 ?  55  LYS   A CG   1 
ATOM   1406 C  CD   . LYS   A 1 55  ? 19.162 12.920  7.391   1.00 14.51 ?  55  LYS   A CD   1 
ATOM   1407 C  CE   . LYS   A 1 55  ? 18.324 14.002  8.055   1.00 16.60 ?  55  LYS   A CE   1 
ATOM   1408 N  NZ   . LYS   A 1 55  ? 16.991 14.147  7.405   1.00 17.56 ?  55  LYS   A NZ   1 
ATOM   1409 H  H    A LYS   A 1 55  ? 22.675 9.716   6.810   0.60 11.88 ?  55  LYS   A H    1 
ATOM   1410 H  H    B LYS   A 1 55  ? 22.675 9.702   6.818   0.40 11.88 ?  55  LYS   A H    1 
ATOM   1411 H  HA   . LYS   A 1 55  ? 23.166 11.982  7.947   1.00 12.60 ?  55  LYS   A HA   1 
ATOM   1412 H  HB2  . LYS   A 1 55  ? 21.342 11.717  6.546   1.00 13.55 ?  55  LYS   A HB2  1 
ATOM   1413 H  HB3  . LYS   A 1 55  ? 20.663 10.732  7.585   1.00 13.55 ?  55  LYS   A HB3  1 
ATOM   1414 H  HG2  . LYS   A 1 55  ? 20.298 12.489  9.045   1.00 15.62 ?  55  LYS   A HG2  1 
ATOM   1415 H  HG3  . LYS   A 1 55  ? 21.027 13.487  8.038   1.00 15.62 ?  55  LYS   A HG3  1 
ATOM   1416 H  HD2  . LYS   A 1 55  ? 19.346 13.195  6.478   1.00 17.39 ?  55  LYS   A HD2  1 
ATOM   1417 H  HD3  . LYS   A 1 55  ? 18.651 12.095  7.392   1.00 17.39 ?  55  LYS   A HD3  1 
ATOM   1418 H  HE2  . LYS   A 1 55  ? 18.183 13.767  8.985   1.00 19.90 ?  55  LYS   A HE2  1 
ATOM   1419 H  HE3  . LYS   A 1 55  ? 18.788 14.849  7.988   1.00 19.90 ?  55  LYS   A HE3  1 
ATOM   1420 H  HZ1  . LYS   A 1 55  ? 16.431 14.570  7.953   1.00 21.05 ?  55  LYS   A HZ1  1 
ATOM   1421 H  HZ2  . LYS   A 1 55  ? 17.067 14.618  6.653   1.00 21.05 ?  55  LYS   A HZ2  1 
ATOM   1422 H  HZ3  . LYS   A 1 55  ? 16.654 13.345  7.213   1.00 21.05 ?  55  LYS   A HZ3  1 
ATOM   1423 N  N    . ALA   A 1 56  ? 22.125 9.764   9.996   1.00 11.04 ?  56  ALA   A N    1 
ATOM   1424 C  CA   . ALA   A 1 56  ? 22.009 9.432   11.411  1.00 11.63 ?  56  ALA   A CA   1 
ATOM   1425 C  C    . ALA   A 1 56  ? 23.351 9.460   12.134  1.00 11.42 ?  56  ALA   A C    1 
ATOM   1426 O  O    . ALA   A 1 56  ? 23.375 9.642   13.353  1.00 12.82 ?  56  ALA   A O    1 
ATOM   1427 C  CB   . ALA   A 1 56  ? 21.331 8.068   11.575  1.00 12.67 ?  56  ALA   A CB   1 
ATOM   1428 H  H    . ALA   A 1 56  ? 21.928 9.119   9.467   1.00 13.22 ?  56  ALA   A H    1 
ATOM   1429 H  HA   . ALA   A 1 56  ? 21.443 10.085  11.837  1.00 13.93 ?  56  ALA   A HA   1 
ATOM   1430 H  HB1  . ALA   A 1 56  ? 21.263 7.857   12.522  1.00 15.18 ?  56  ALA   A HB1  1 
ATOM   1431 H  HB2  . ALA   A 1 56  ? 20.443 8.106   11.185  1.00 15.18 ?  56  ALA   A HB2  1 
ATOM   1432 H  HB3  . ALA   A 1 56  ? 21.859 7.388   11.126  1.00 15.18 ?  56  ALA   A HB3  1 
ATOM   1433 N  N    . THR   A 1 57  ? 24.463 9.284   11.415  1.00 10.70 ?  57  THR   A N    1 
ATOM   1434 C  CA   . THR   A 1 57  ? 25.804 9.410   11.990  1.00 10.67 ?  57  THR   A CA   1 
ATOM   1435 C  C    . THR   A 1 57  ? 26.354 10.828  11.911  1.00 11.22 ?  57  THR   A C    1 
ATOM   1436 O  O    . THR   A 1 57  ? 27.537 11.039  12.202  1.00 11.75 ?  57  THR   A O    1 
ATOM   1437 C  CB   . THR   A 1 57  ? 26.817 8.464   11.316  1.00 10.59 ?  57  THR   A CB   1 
ATOM   1438 O  OG1  . THR   A 1 57  ? 27.197 8.964   10.019  1.00 10.54 ?  57  THR   A OG1  1 
ATOM   1439 C  CG2  . THR   A 1 57  ? 26.284 7.047   11.203  1.00 10.89 ?  57  THR   A CG2  1 
ATOM   1440 H  H    . THR   A 1 57  ? 24.467 9.075   10.578  1.00 12.81 ?  57  THR   A H    1 
ATOM   1441 H  HA   . THR   A 1 57  ? 25.757 9.153   12.930  1.00 12.78 ?  57  THR   A HA   1 
ATOM   1442 H  HB   . THR   A 1 57  ? 27.614 8.419   11.875  1.00 12.69 ?  57  THR   A HB   1 
ATOM   1443 H  HG1  . THR   A 1 57  ? 26.515 9.028   9.534   1.00 12.62 ?  57  THR   A HG1  1 
ATOM   1444 H  HG21 . THR   A 1 57  ? 26.972 6.454   10.856  1.00 13.05 ?  57  THR   A HG21 1 
ATOM   1445 H  HG22 . THR   A 1 57  ? 26.001 6.720   12.072  1.00 13.05 ?  57  THR   A HG22 1 
ATOM   1446 H  HG23 . THR   A 1 57  ? 25.524 7.023   10.600  1.00 13.05 ?  57  THR   A HG23 1 
ATOM   1447 N  N    . ASN   A 1 58  ? 25.541 11.802  11.511  1.00 11.46 ?  58  ASN   A N    1 
ATOM   1448 C  CA   . ASN   A 1 58  ? 26.004 13.182  11.412  1.00 12.51 ?  58  ASN   A CA   1 
ATOM   1449 C  C    . ASN   A 1 58  ? 27.152 13.310  10.407  1.00 11.75 ?  58  ASN   A C    1 
ATOM   1450 O  O    . ASN   A 1 58  ? 28.051 14.141  10.569  1.00 12.24 ?  58  ASN   A O    1 
ATOM   1451 C  CB   . ASN   A 1 58  ? 26.372 13.721  12.808  1.00 15.21 ?  58  ASN   A CB   1 
ATOM   1452 C  CG   . ASN   A 1 58  ? 26.788 15.177  12.803  1.00 19.19 ?  58  ASN   A CG   1 
ATOM   1453 O  OD1  . ASN   A 1 58  ? 26.166 16.007  12.148  1.00 20.59 ?  58  ASN   A OD1  1 
ATOM   1454 N  ND2  . ASN   A 1 58  ? 27.847 15.498  13.551  1.00 20.50 ?  58  ASN   A ND2  1 
ATOM   1455 H  H    . ASN   A 1 58  ? 24.718 11.680  11.287  1.00 13.73 ?  58  ASN   A H    1 
ATOM   1456 H  HA   . ASN   A 1 58  ? 25.266 13.714  11.082  1.00 14.99 ?  58  ASN   A HA   1 
ATOM   1457 H  HB2  . ASN   A 1 58  ? 25.595 13.631  13.394  1.00 18.22 ?  58  ASN   A HB2  1 
ATOM   1458 H  HB3  . ASN   A 1 58  ? 27.108 13.207  13.167  1.00 18.22 ?  58  ASN   A HB3  1 
ATOM   1459 H  HD21 . ASN   A 1 58  ? 28.117 16.314  13.585  1.00 24.58 ?  58  ASN   A HD21 1 
ATOM   1460 H  HD22 . ASN   A 1 58  ? 28.254 14.890  13.998  1.00 24.58 ?  58  ASN   A HD22 1 
ATOM   1461 N  N    . ASN   A 1 59  ? 27.124 12.493  9.350   1.00 10.60 ?  59  ASN   A N    1 
ATOM   1462 C  CA   . ASN   A 1 59  ? 28.099 12.468  8.251   1.00 10.39 ?  59  ASN   A CA   1 
ATOM   1463 C  C    . ASN   A 1 59  ? 29.418 11.787  8.633   1.00 10.01 ?  59  ASN   A C    1 
ATOM   1464 O  O    . ASN   A 1 59  ? 30.336 11.750  7.803   1.00 10.48 ?  59  ASN   A O    1 
ATOM   1465 C  CB   . ASN   A 1 59  ? 28.379 13.857  7.644   1.00 10.43 ?  59  ASN   A CB   1 
ATOM   1466 C  CG   . ASN   A 1 59  ? 28.748 13.791  6.179   1.00 10.67 ?  59  ASN   A CG   1 
ATOM   1467 O  OD1  . ASN   A 1 59  ? 28.044 13.165  5.383   1.00 10.93 ?  59  ASN   A OD1  1 
ATOM   1468 N  ND2  . ASN   A 1 59  ? 29.836 14.457  5.805   1.00 11.27 ?  59  ASN   A ND2  1 
ATOM   1469 H  H    . ASN   A 1 59  ? 26.508 11.901  9.239   1.00 12.69 ?  59  ASN   A H    1 
ATOM   1470 H  HA   . ASN   A 1 59  ? 27.714 11.936  7.541   1.00 12.45 ?  59  ASN   A HA   1 
ATOM   1471 H  HB2  . ASN   A 1 59  ? 27.581 14.405  7.718   1.00 12.50 ?  59  ASN   A HB2  1 
ATOM   1472 H  HB3  . ASN   A 1 59  ? 29.114 14.272  8.114   1.00 12.50 ?  59  ASN   A HB3  1 
ATOM   1473 H  HD21 . ASN   A 1 59  ? 30.092 14.450  4.984   1.00 13.49 ?  59  ASN   A HD21 1 
ATOM   1474 H  HD22 . ASN   A 1 59  ? 30.306 14.883  6.393   1.00 13.49 ?  59  ASN   A HD22 1 
ATOM   1475 N  N    . ALA   A 1 60  ? 29.551 11.242  9.844   1.00 9.93  ?  60  ALA   A N    1 
ATOM   1476 C  CA   . ALA   A 1 60  ? 30.790 10.556  10.198  1.00 10.39 ?  60  ALA   A CA   1 
ATOM   1477 C  C    . ALA   A 1 60  ? 31.012 9.322   9.333   1.00 10.12 ?  60  ALA   A C    1 
ATOM   1478 O  O    . ALA   A 1 60  ? 32.159 9.006   8.990   1.00 10.67 ?  60  ALA   A O    1 
ATOM   1479 C  CB   . ALA   A 1 60  ? 30.785 10.186  11.680  1.00 11.04 ?  60  ALA   A CB   1 
ATOM   1480 H  H    . ALA   A 1 60  ? 28.955 11.256  10.463  1.00 11.89 ?  60  ALA   A H    1 
ATOM   1481 H  HA   . ALA   A 1 60  ? 31.535 11.162  10.048  1.00 12.44 ?  60  ALA   A HA   1 
ATOM   1482 H  HB1  . ALA   A 1 60  ? 31.614 9.735   11.897  1.00 13.23 ?  60  ALA   A HB1  1 
ATOM   1483 H  HB2  . ALA   A 1 60  ? 30.703 11.000  12.207  1.00 13.23 ?  60  ALA   A HB2  1 
ATOM   1484 H  HB3  . ALA   A 1 60  ? 30.031 9.604   11.857  1.00 13.23 ?  60  ALA   A HB3  1 
ATOM   1485 N  N    . MET   A 1 61  ? 29.937 8.630   8.953   1.00 9.85  ?  61  MET   A N    1 
ATOM   1486 C  CA   . MET   A 1 61  ? 30.074 7.494   8.048   1.00 9.59  ?  61  MET   A CA   1 
ATOM   1487 C  C    . MET   A 1 61  ? 30.704 7.920   6.724   1.00 9.77  ?  61  MET   A C    1 
ATOM   1488 O  O    . MET   A 1 61  ? 31.598 7.241   6.206   1.00 10.04 ?  61  MET   A O    1 
ATOM   1489 C  CB   . MET   A 1 61  ? 28.710 6.839   7.834   1.00 9.53  ?  61  MET   A CB   1 
ATOM   1490 C  CG   . MET   A 1 61  ? 28.721 5.682   6.854   1.00 10.53 ?  61  MET   A CG   1 
ATOM   1491 S  SD   . MET   A 1 61  ? 27.101 4.929   6.647   1.00 11.28 ?  61  MET   A SD   1 
ATOM   1492 C  CE   . MET   A 1 61  ? 26.963 4.017   8.186   1.00 12.25 ?  61  MET   A CE   1 
ATOM   1493 H  H    . MET   A 1 61  ? 29.130 8.796   9.205   1.00 11.79 ?  61  MET   A H    1 
ATOM   1494 H  HA   . MET   A 1 61  ? 30.651 6.840   8.464   1.00 11.49 ?  61  MET   A HA   1 
ATOM   1495 H  HB2  . MET   A 1 61  ? 28.395 6.499   8.685   1.00 11.41 ?  61  MET   A HB2  1 
ATOM   1496 H  HB3  . MET   A 1 61  ? 28.092 7.504   7.499   1.00 11.41 ?  61  MET   A HB3  1 
ATOM   1497 H  HG2  . MET   A 1 61  ? 29.002 5.995   5.983   1.00 12.61 ?  61  MET   A HG2  1 
ATOM   1498 H  HG3  . MET   A 1 61  ? 29.318 4.992   7.173   1.00 12.61 ?  61  MET   A HG3  1 
ATOM   1499 H  HE1  . MET   A 1 61  ? 26.124 3.527   8.194   1.00 14.68 ?  61  MET   A HE1  1 
ATOM   1500 H  HE2  . MET   A 1 61  ? 27.706 3.396   8.254   1.00 14.68 ?  61  MET   A HE2  1 
ATOM   1501 H  HE3  . MET   A 1 61  ? 26.985 4.642   8.928   1.00 14.68 ?  61  MET   A HE3  1 
ATOM   1502 N  N    . GLN   A 1 62  ? 30.259 9.049   6.167   1.00 9.62  ?  62  GLN   A N    1 
ATOM   1503 C  CA   . GLN   A 1 62  ? 30.819 9.527   4.906   1.00 9.91  ?  62  GLN   A CA   1 
ATOM   1504 C  C    . GLN   A 1 62  ? 32.289 9.907   5.049   1.00 9.75  ?  62  GLN   A C    1 
ATOM   1505 O  O    . GLN   A 1 62  ? 33.098 9.596   4.169   1.00 10.31 ?  62  GLN   A O    1 
ATOM   1506 C  CB   . GLN   A 1 62  ? 30.012 10.711  4.379   1.00 9.74  ?  62  GLN   A CB   1 
ATOM   1507 C  CG   . GLN   A 1 62  ? 30.389 11.082  2.957   1.00 9.74  ?  62  GLN   A CG   1 
ATOM   1508 C  CD   . GLN   A 1 62  ? 30.061 9.952   2.003   1.00 10.14 ?  62  GLN   A CD   1 
ATOM   1509 O  OE1  . GLN   A 1 62  ? 28.885 9.641   1.793   1.00 10.73 ?  62  GLN   A OE1  1 
ATOM   1510 N  NE2  . GLN   A 1 62  ? 31.084 9.285   1.479   1.00 10.93 ?  62  GLN   A NE2  1 
ATOM   1511 H  H    . GLN   A 1 62  ? 29.638 9.545   6.494   1.00 11.52 ?  62  GLN   A H    1 
ATOM   1512 H  HA   . GLN   A 1 62  ? 30.764 8.809   4.256   1.00 11.87 ?  62  GLN   A HA   1 
ATOM   1513 H  HB2  . GLN   A 1 62  ? 29.069 10.487  4.392   1.00 11.66 ?  62  GLN   A HB2  1 
ATOM   1514 H  HB3  . GLN   A 1 62  ? 30.177 11.484  4.944   1.00 11.66 ?  62  GLN   A HB3  1 
ATOM   1515 H  HG2  . GLN   A 1 62  ? 29.883 11.864  2.684   1.00 11.66 ?  62  GLN   A HG2  1 
ATOM   1516 H  HG3  . GLN   A 1 62  ? 31.340 11.261  2.907   1.00 11.66 ?  62  GLN   A HG3  1 
ATOM   1517 H  HE21 . GLN   A 1 62  ? 31.890 9.521   1.663   1.00 13.09 ?  62  GLN   A HE21 1 
ATOM   1518 H  HE22 . GLN   A 1 62  ? 30.938 8.631   0.941   1.00 13.09 ?  62  GLN   A HE22 1 
ATOM   1519 N  N    . VAL   A 1 63  ? 32.650 10.594  6.136   1.00 10.34 ?  63  VAL   A N    1 
ATOM   1520 C  CA   . VAL   A 1 63  ? 34.041 10.985  6.346   1.00 11.13 ?  63  VAL   A CA   1 
ATOM   1521 C  C    . VAL   A 1 63  ? 34.938 9.751   6.404   1.00 10.57 ?  63  VAL   A C    1 
ATOM   1522 O  O    . VAL   A 1 63  ? 35.991 9.690   5.755   1.00 10.91 ?  63  VAL   A O    1 
ATOM   1523 C  CB   . VAL   A 1 63  ? 34.157 11.858  7.608   1.00 12.59 ?  63  VAL   A CB   1 
ATOM   1524 C  CG1  . VAL   A 1 63  ? 35.604 12.106  7.955   1.00 14.55 ?  63  VAL   A CG1  1 
ATOM   1525 C  CG2  . VAL   A 1 63  ? 33.424 13.187  7.405   1.00 12.94 ?  63  VAL   A CG2  1 
ATOM   1526 H  H    . VAL   A 1 63  ? 32.107 10.840  6.762   1.00 12.38 ?  63  VAL   A H    1 
ATOM   1527 H  HA   . VAL   A 1 63  ? 34.322 11.522  5.594   1.00 13.33 ?  63  VAL   A HA   1 
ATOM   1528 H  HB   . VAL   A 1 63  ? 33.745 11.399  8.357   1.00 15.08 ?  63  VAL   A HB   1 
ATOM   1529 H  HG11 . VAL   A 1 63  ? 35.657 12.844  8.584   1.00 17.43 ?  63  VAL   A HG11 1 
ATOM   1530 H  HG12 . VAL   A 1 63  ? 35.980 11.306  8.354   1.00 17.43 ?  63  VAL   A HG12 1 
ATOM   1531 H  HG13 . VAL   A 1 63  ? 36.089 12.332  7.144   1.00 17.43 ?  63  VAL   A HG13 1 
ATOM   1532 H  HG21 . VAL   A 1 63  ? 33.520 13.728  8.205   1.00 15.51 ?  63  VAL   A HG21 1 
ATOM   1533 H  HG22 . VAL   A 1 63  ? 33.813 13.649  6.645   1.00 15.51 ?  63  VAL   A HG22 1 
ATOM   1534 H  HG23 . VAL   A 1 63  ? 32.486 13.008  7.238   1.00 15.51 ?  63  VAL   A HG23 1 
ATOM   1535 N  N    . GLU   A 1 64  ? 34.522 8.744   7.175   1.00 10.56 ?  64  GLU   A N    1 
ATOM   1536 C  CA   . GLU   A 1 64  ? 35.287 7.506   7.267   1.00 10.62 ?  64  GLU   A CA   1 
ATOM   1537 C  C    . GLU   A 1 64  ? 35.370 6.816   5.912   1.00 10.16 ?  64  GLU   A C    1 
ATOM   1538 O  O    . GLU   A 1 64  ? 36.421 6.276   5.531   1.00 10.72 ?  64  GLU   A O    1 
ATOM   1539 C  CB   . GLU   A 1 64  ? 34.607 6.596   8.290   1.00 11.27 ?  64  GLU   A CB   1 
ATOM   1540 C  CG   . GLU   A 1 64  ? 35.258 5.248   8.445   1.00 11.76 ?  64  GLU   A CG   1 
ATOM   1541 C  CD   . GLU   A 1 64  ? 34.379 4.251   9.173   1.00 12.00 ?  64  GLU   A CD   1 
ATOM   1542 O  OE1  . GLU   A 1 64  ? 33.141 4.343   9.039   1.00 12.88 ?  64  GLU   A OE1  1 
ATOM   1543 O  OE2  . GLU   A 1 64  ? 34.931 3.353   9.854   1.00 12.56 -1 64  GLU   A OE2  1 
ATOM   1544 H  H    . GLU   A 1 64  ? 33.800 8.751   7.643   1.00 12.65 ?  64  GLU   A H    1 
ATOM   1545 H  HA   . GLU   A 1 64  ? 36.185 7.707   7.575   1.00 12.73 ?  64  GLU   A HA   1 
ATOM   1546 H  HB2  . GLU   A 1 64  ? 34.630 7.039   9.158   1.00 13.50 ?  64  GLU   A HB2  1 
ATOM   1547 H  HB3  . GLU   A 1 64  ? 33.688 6.462   8.019   1.00 13.50 ?  64  GLU   A HB3  1 
ATOM   1548 H  HG2  . GLU   A 1 64  ? 35.460 4.880   7.567   1.00 14.09 ?  64  GLU   A HG2  1 
ATOM   1549 H  HG3  . GLU   A 1 64  ? 36.079 5.351   8.951   1.00 14.09 ?  64  GLU   A HG3  1 
ATOM   1550 N  N    . SER   A 1 65  ? 34.252 6.807   5.181   1.00 9.81  ?  65  SER   A N    1 
ATOM   1551 C  CA   . SER   A 1 65  ? 34.198 6.151   3.879   1.00 9.81  ?  65  SER   A CA   1 
ATOM   1552 C  C    . SER   A 1 65  ? 35.119 6.821   2.871   1.00 10.05 ?  65  SER   A C    1 
ATOM   1553 O  O    . SER   A 1 65  ? 35.760 6.143   2.061   1.00 10.97 ?  65  SER   A O    1 
ATOM   1554 C  CB   . SER   A 1 65  ? 32.768 6.160   3.349   1.00 9.88  ?  65  SER   A CB   1 
ATOM   1555 O  OG   . SER   A 1 65  ? 31.923 5.341   4.141   1.00 10.50 ?  65  SER   A OG   1 
ATOM   1556 H  H    . SER   A 1 65  ? 33.513 7.179   5.416   1.00 11.75 ?  65  SER   A H    1 
ATOM   1557 H  HA   . SER   A 1 65  ? 34.481 5.230   3.974   1.00 11.75 ?  65  SER   A HA   1 
ATOM   1558 H  HB2  . SER   A 1 65  ? 32.430 7.069   3.366   1.00 11.83 ?  65  SER   A HB2  1 
ATOM   1559 H  HB3  . SER   A 1 65  ? 32.771 5.826   2.439   1.00 11.83 ?  65  SER   A HB3  1 
ATOM   1560 H  HG   . SER   A 1 65  ? 31.920 5.621   4.938   1.00 12.57 ?  65  SER   A HG   1 
ATOM   1561 N  N    . ASP   A 1 66  ? 35.196 8.154   2.896   1.00 10.42 ?  66  ASP   A N    1 
ATOM   1562 C  CA   . ASP   A 1 66  ? 36.053 8.856   1.948   1.00 11.11 ?  66  ASP   A CA   1 
ATOM   1563 C  C    . ASP   A 1 66  ? 37.517 8.499   2.178   1.00 10.68 ?  66  ASP   A C    1 
ATOM   1564 O  O    . ASP   A 1 66  ? 38.284 8.331   1.221   1.00 11.93 ?  66  ASP   A O    1 
ATOM   1565 C  CB   . ASP   A 1 66  ? 35.838 10.364  2.062   1.00 12.31 ?  66  ASP   A CB   1 
ATOM   1566 C  CG   . ASP   A 1 66  ? 34.500 10.827  1.479   1.00 14.09 ?  66  ASP   A CG   1 
ATOM   1567 O  OD1  . ASP   A 1 66  ? 33.779 10.033  0.834   1.00 14.32 ?  66  ASP   A OD1  1 
ATOM   1568 O  OD2  . ASP   A 1 66  ? 34.195 12.024  1.654   1.00 17.17 -1 66  ASP   A OD2  1 
ATOM   1569 H  H    . ASP   A 1 66  ? 34.764 8.666   3.439   1.00 12.48 ?  66  ASP   A H    1 
ATOM   1570 H  HA   . ASP   A 1 66  ? 35.816 8.586   1.048   1.00 13.31 ?  66  ASP   A HA   1 
ATOM   1571 H  HB2  . ASP   A 1 66  ? 35.852 10.617  2.998   1.00 14.74 ?  66  ASP   A HB2  1 
ATOM   1572 H  HB3  . ASP   A 1 66  ? 36.551 10.821  1.585   1.00 14.74 ?  66  ASP   A HB3  1 
ATOM   1573 N  N    . ASP   A 1 67  ? 37.921 8.368   3.442   1.00 11.03 ?  67  ASP   A N    1 
ATOM   1574 C  CA   . ASP   A 1 67  ? 39.274 7.916   3.739   1.00 12.04 ?  67  ASP   A CA   1 
ATOM   1575 C  C    . ASP   A 1 67  ? 39.491 6.482   3.266   1.00 11.92 ?  67  ASP   A C    1 
ATOM   1576 O  O    . ASP   A 1 67  ? 40.547 6.159   2.711   1.00 12.69 ?  67  ASP   A O    1 
ATOM   1577 C  CB   . ASP   A 1 67  ? 39.546 8.044   5.234   1.00 13.34 ?  67  ASP   A CB   1 
ATOM   1578 C  CG   . ASP   A 1 67  ? 40.845 7.387   5.645   1.00 14.49 ?  67  ASP   A CG   1 
ATOM   1579 O  OD1  . ASP   A 1 67  ? 41.915 8.018   5.495   1.00 17.18 ?  67  ASP   A OD1  1 
ATOM   1580 O  OD2  . ASP   A 1 67  ? 40.795 6.228   6.118   1.00 14.04 -1 67  ASP   A OD2  1 
ATOM   1581 H  H    . ASP   A 1 67  ? 37.439 8.534   4.132   1.00 13.21 ?  67  ASP   A H    1 
ATOM   1582 H  HA   . ASP   A 1 67  ? 39.907 8.480   3.268   1.00 14.42 ?  67  ASP   A HA   1 
ATOM   1583 H  HB2  . ASP   A 1 67  ? 39.596 8.980   5.463   1.00 15.98 ?  67  ASP   A HB2  1 
ATOM   1584 H  HB3  . ASP   A 1 67  ? 38.823 7.615   5.721   1.00 15.98 ?  67  ASP   A HB3  1 
ATOM   1585 N  N    . TYR   A 1 68  ? 38.495 5.607   3.463   1.00 11.28 ?  68  TYR   A N    1 
ATOM   1586 C  CA   . TYR   A 1 68  ? 38.613 4.228   2.987   1.00 11.55 ?  68  TYR   A CA   1 
ATOM   1587 C  C    . TYR   A 1 68  ? 38.854 4.182   1.480   1.00 11.29 ?  68  TYR   A C    1 
ATOM   1588 O  O    . TYR   A 1 68  ? 39.730 3.447   1.003   1.00 11.96 ?  68  TYR   A O    1 
ATOM   1589 C  CB   . TYR   A 1 68  ? 37.359 3.408   3.360   1.00 11.67 ?  68  TYR   A CB   1 
ATOM   1590 C  CG   . TYR   A 1 68  ? 37.383 2.023   2.730   1.00 12.80 ?  68  TYR   A CG   1 
ATOM   1591 C  CD1  . TYR   A 1 68  ? 36.927 1.831   1.429   1.00 13.96 ?  68  TYR   A CD1  1 
ATOM   1592 C  CD2  . TYR   A 1 68  ? 37.923 0.938   3.398   1.00 14.53 ?  68  TYR   A CD2  1 
ATOM   1593 C  CE1  . TYR   A 1 68  ? 36.997 0.617   0.814   1.00 15.49 ?  68  TYR   A CE1  1 
ATOM   1594 C  CE2  . TYR   A 1 68  ? 37.986 -0.319  2.784   1.00 15.01 ?  68  TYR   A CE2  1 
ATOM   1595 C  CZ   . TYR   A 1 68  ? 37.529 -0.454  1.492   1.00 15.60 ?  68  TYR   A CZ   1 
ATOM   1596 O  OH   . TYR   A 1 68  ? 37.611 -1.667  0.866   1.00 16.71 ?  68  TYR   A OH   1 
ATOM   1597 H  H    . TYR   A 1 68  ? 37.751 5.782   3.864   1.00 13.51 ?  68  TYR   A H    1 
ATOM   1598 H  HA   . TYR   A 1 68  ? 39.372 3.813   3.419   1.00 13.84 ?  68  TYR   A HA   1 
ATOM   1599 H  HB2  . TYR   A 1 68  ? 37.322 3.298   4.322   1.00 13.98 ?  68  TYR   A HB2  1 
ATOM   1600 H  HB3  . TYR   A 1 68  ? 36.566 3.869   3.043   1.00 13.98 ?  68  TYR   A HB3  1 
ATOM   1601 H  HD1  . TYR   A 1 68  ? 36.580 2.558   0.960   1.00 16.73 ?  68  TYR   A HD1  1 
ATOM   1602 H  HD2  . TYR   A 1 68  ? 38.251 1.045   4.259   1.00 17.41 ?  68  TYR   A HD2  1 
ATOM   1603 H  HE1  . TYR   A 1 68  ? 36.677 0.513   -0.054  1.00 18.57 ?  68  TYR   A HE1  1 
ATOM   1604 H  HE2  . TYR   A 1 68  ? 38.352 -1.047  3.229   1.00 17.98 ?  68  TYR   A HE2  1 
ATOM   1605 H  HH   . TYR   A 1 68  ? 37.936 -2.238  1.392   1.00 20.03 ?  68  TYR   A HH   1 
ATOM   1606 N  N    . ILE   A 1 69  ? 38.064 4.940   0.710   1.00 10.86 ?  69  ILE   A N    1 
ATOM   1607 C  CA   . ILE   A 1 69  ? 38.198 4.937   -0.744  1.00 10.99 ?  69  ILE   A CA   1 
ATOM   1608 C  C    . ILE   A 1 69  ? 39.533 5.541   -1.168  1.00 10.96 ?  69  ILE   A C    1 
ATOM   1609 O  O    . ILE   A 1 69  ? 40.175 5.055   -2.104  1.00 11.53 ?  69  ILE   A O    1 
ATOM   1610 C  CB   . ILE   A 1 69  ? 37.007 5.661   -1.402  1.00 11.80 ?  69  ILE   A CB   1 
ATOM   1611 C  CG1  . ILE   A 1 69  ? 35.688 4.929   -1.134  1.00 12.59 ?  69  ILE   A CG1  1 
ATOM   1612 C  CG2  . ILE   A 1 69  ? 37.251 5.853   -2.901  1.00 13.39 ?  69  ILE   A CG2  1 
ATOM   1613 C  CD1  . ILE   A 1 69  ? 35.534 3.626   -1.883  1.00 13.14 ?  69  ILE   A CD1  1 
ATOM   1614 H  H    . ILE   A 1 69  ? 37.453 5.465   1.008   1.00 13.01 ?  69  ILE   A H    1 
ATOM   1615 H  HA   . ILE   A 1 69  ? 38.188 4.018   -1.051  1.00 13.17 ?  69  ILE   A HA   1 
ATOM   1616 H  HB   . ILE   A 1 69  ? 36.940 6.541   -1.002  1.00 14.14 ?  69  ILE   A HB   1 
ATOM   1617 H  HG12 . ILE   A 1 69  ? 35.634 4.732   -0.183  1.00 15.08 ?  69  ILE   A HG12 1 
ATOM   1618 H  HG13 . ILE   A 1 69  ? 34.955 5.508   -1.388  1.00 15.08 ?  69  ILE   A HG13 1 
ATOM   1619 H  HG21 . ILE   A 1 69  ? 36.407 6.063   -3.334  1.00 16.05 ?  69  ILE   A HG21 1 
ATOM   1620 H  HG22 . ILE   A 1 69  ? 37.874 6.590   -3.031  1.00 16.05 ?  69  ILE   A HG22 1 
ATOM   1621 H  HG23 . ILE   A 1 69  ? 37.618 5.039   -3.272  1.00 16.05 ?  69  ILE   A HG23 1 
ATOM   1622 H  HD11 . ILE   A 1 69  ? 34.714 3.197   -1.596  1.00 15.74 ?  69  ILE   A HD11 1 
ATOM   1623 H  HD12 . ILE   A 1 69  ? 35.493 3.811   -2.834  1.00 15.74 ?  69  ILE   A HD12 1 
ATOM   1624 H  HD13 . ILE   A 1 69  ? 36.291 3.054   -1.688  1.00 15.74 ?  69  ILE   A HD13 1 
ATOM   1625 N  N    . ALA   A 1 70  ? 39.955 6.621   -0.510  1.00 11.42 ?  70  ALA   A N    1 
ATOM   1626 C  CA   . ALA   A 1 70  ? 41.233 7.227   -0.868  1.00 12.21 ?  70  ALA   A CA   1 
ATOM   1627 C  C    . ALA   A 1 70  ? 42.380 6.240   -0.703  1.00 12.74 ?  70  ALA   A C    1 
ATOM   1628 O  O    . ALA   A 1 70  ? 43.345 6.271   -1.473  1.00 14.42 ?  70  ALA   A O    1 
ATOM   1629 C  CB   . ALA   A 1 70  ? 41.478 8.480   -0.025  1.00 12.90 ?  70  ALA   A CB   1 
ATOM   1630 H  H    . ALA   A 1 70  ? 39.529 7.017   0.121   1.00 13.68 ?  70  ALA   A H    1 
ATOM   1631 H  HA   . ALA   A 1 70  ? 41.205 7.503   -1.799  1.00 14.63 ?  70  ALA   A HA   1 
ATOM   1632 H  HB1  . ALA   A 1 70  ? 42.337 8.867   -0.276  1.00 15.45 ?  70  ALA   A HB1  1 
ATOM   1633 H  HB2  . ALA   A 1 70  ? 40.771 9.119   -0.187  1.00 15.45 ?  70  ALA   A HB2  1 
ATOM   1634 H  HB3  . ALA   A 1 70  ? 41.496 8.231   0.913   1.00 15.45 ?  70  ALA   A HB3  1 
ATOM   1635 N  N    . THR   A 1 71  ? 42.280 5.346   0.277   1.00 12.27 ?  71  THR   A N    1 
ATOM   1636 C  CA   . THR   A 1 71  ? 43.330 4.367   0.527   1.00 13.60 ?  71  THR   A CA   1 
ATOM   1637 C  C    . THR   A 1 71  ? 43.206 3.147   -0.374  1.00 13.84 ?  71  THR   A C    1 
ATOM   1638 O  O    . THR   A 1 71  ? 44.215 2.649   -0.888  1.00 15.77 ?  71  THR   A O    1 
ATOM   1639 C  CB   . THR   A 1 71  ? 43.259 3.920   1.982   1.00 15.39 ?  71  THR   A CB   1 
ATOM   1640 O  OG1  . THR   A 1 71  ? 43.506 5.047   2.830   1.00 16.55 ?  71  THR   A OG1  1 
ATOM   1641 C  CG2  . THR   A 1 71  ? 44.273 2.817   2.271   1.00 17.03 ?  71  THR   A CG2  1 
ATOM   1642 H  H    . THR   A 1 71  ? 41.608 5.280   0.807   1.00 14.69 ?  71  THR   A H    1 
ATOM   1643 H  HA   . THR   A 1 71  ? 44.196 4.773   0.367   1.00 16.29 ?  71  THR   A HA   1 
ATOM   1644 H  HB   . THR   A 1 71  ? 42.371 3.563   2.158   1.00 18.45 ?  71  THR   A HB   1 
ATOM   1645 H  HG1  . THR   A 1 71  ? 43.461 4.802   3.633   1.00 19.84 ?  71  THR   A HG1  1 
ATOM   1646 H  HG21 . THR   A 1 71  ? 44.400 2.734   3.229   1.00 20.41 ?  71  THR   A HG21 1 
ATOM   1647 H  HG22 . THR   A 1 71  ? 43.962 1.969   1.921   1.00 20.41 ?  71  THR   A HG22 1 
ATOM   1648 H  HG23 . THR   A 1 71  ? 45.125 3.037   1.861   1.00 20.41 ?  71  THR   A HG23 1 
ATOM   1649 N  N    . ASN   A 1 72  ? 41.983 2.642   -0.560  1.00 12.69 ?  72  ASN   A N    1 
ATOM   1650 C  CA   . ASN   A 1 72  ? 41.767 1.317   -1.123  1.00 12.94 ?  72  ASN   A CA   1 
ATOM   1651 C  C    . ASN   A 1 72  ? 41.141 1.307   -2.505  1.00 13.10 ?  72  ASN   A C    1 
ATOM   1652 O  O    . ASN   A 1 72  ? 41.155 0.253   -3.157  1.00 14.35 ?  72  ASN   A O    1 
ATOM   1653 C  CB   . ASN   A 1 72  ? 40.880 0.492   -0.183  1.00 13.83 ?  72  ASN   A CB   1 
ATOM   1654 C  CG   . ASN   A 1 72  ? 41.491 0.337   1.183   1.00 14.88 ?  72  ASN   A CG   1 
ATOM   1655 O  OD1  . ASN   A 1 72  ? 41.029 0.933   2.157   1.00 16.57 ?  72  ASN   A OD1  1 
ATOM   1656 N  ND2  . ASN   A 1 72  ? 42.550 -0.443  1.263   1.00 15.57 ?  72  ASN   A ND2  1 
ATOM   1657 H  H    . ASN   A 1 72  ? 41.253 3.059   -0.364  1.00 15.21 ?  72  ASN   A H    1 
ATOM   1658 H  HA   . ASN   A 1 72  ? 42.621 0.868   -1.191  1.00 15.50 ?  72  ASN   A HA   1 
ATOM   1659 H  HB2  . ASN   A 1 72  ? 40.023 0.933   -0.085  1.00 16.57 ?  72  ASN   A HB2  1 
ATOM   1660 H  HB3  . ASN   A 1 72  ? 40.759 -0.394  -0.561  1.00 16.57 ?  72  ASN   A HB3  1 
ATOM   1661 H  HD21 . ASN   A 1 72  ? 42.941 -0.557  2.022   1.00 18.66 ?  72  ASN   A HD21 1 
ATOM   1662 H  HD22 . ASN   A 1 72  ? 42.853 -0.833  0.561   1.00 18.66 ?  72  ASN   A HD22 1 
ATOM   1663 N  N    . GLY   A 1 73  ? 40.587 2.423   -2.965  1.00 12.60 ?  73  GLY   A N    1 
ATOM   1664 C  CA   . GLY   A 1 73  ? 39.851 2.435   -4.203  1.00 12.38 ?  73  GLY   A CA   1 
ATOM   1665 C  C    . GLY   A 1 73  ? 38.460 1.857   -4.036  1.00 11.84 ?  73  GLY   A C    1 
ATOM   1666 O  O    . GLY   A 1 73  ? 38.073 1.400   -2.954  1.00 12.51 ?  73  GLY   A O    1 
ATOM   1667 H  H    . GLY   A 1 73  ? 40.629 3.194   -2.575  1.00 15.10 ?  73  GLY   A H    1 
ATOM   1668 H  HA2  . GLY   A 1 73  ? 39.777 3.351   -4.525  1.00 14.83 ?  73  GLY   A HA2  1 
ATOM   1669 H  HA3  . GLY   A 1 73  ? 40.328 1.916   -4.870  1.00 14.83 ?  73  GLY   A HA3  1 
ATOM   1670 N  N    . PRO   A 1 74  ? 37.683 1.874   -5.115  1.00 12.24 ?  74  PRO   A N    1 
ATOM   1671 C  CA   . PRO   A 1 74  ? 36.286 1.444   -5.033  1.00 12.37 ?  74  PRO   A CA   1 
ATOM   1672 C  C    . PRO   A 1 74  ? 36.140 -0.040  -4.721  1.00 11.71 ?  74  PRO   A C    1 
ATOM   1673 O  O    . PRO   A 1 74  ? 37.008 -0.871  -5.011  1.00 12.59 ?  74  PRO   A O    1 
ATOM   1674 C  CB   . PRO   A 1 74  ? 35.737 1.755   -6.430  1.00 13.97 ?  74  PRO   A CB   1 
ATOM   1675 C  CG   . PRO   A 1 74  ? 36.690 2.739   -7.029  1.00 16.79 ?  74  PRO   A CG   1 
ATOM   1676 C  CD   . PRO   A 1 74  ? 38.026 2.390   -6.451  1.00 14.30 ?  74  PRO   A CD   1 
ATOM   1677 H  HA   . PRO   A 1 74  ? 35.804 1.968   -4.371  1.00 14.82 ?  74  PRO   A HA   1 
ATOM   1678 H  HB2  . PRO   A 1 74  ? 35.707 0.941   -6.955  1.00 16.73 ?  74  PRO   A HB2  1 
ATOM   1679 H  HB3  . PRO   A 1 74  ? 34.850 2.144   -6.352  1.00 16.73 ?  74  PRO   A HB3  1 
ATOM   1680 H  HG2  . PRO   A 1 74  ? 36.702 2.641   -7.994  1.00 20.12 ?  74  PRO   A HG2  1 
ATOM   1681 H  HG3  . PRO   A 1 74  ? 36.436 3.639   -6.778  1.00 20.12 ?  74  PRO   A HG3  1 
ATOM   1682 H  HD2  . PRO   A 1 74  ? 38.459 1.698   -6.979  1.00 17.14 ?  74  PRO   A HD2  1 
ATOM   1683 H  HD3  . PRO   A 1 74  ? 38.582 3.185   -6.389  1.00 17.14 ?  74  PRO   A HD3  1 
ATOM   1684 N  N    . LEU   A 1 75  ? 35.000 -0.362  -4.122  1.00 10.94 ?  75  LEU   A N    1 
ATOM   1685 C  CA   . LEU   A 1 75  ? 34.601 -1.751  -3.970  1.00 10.99 ?  75  LEU   A CA   1 
ATOM   1686 C  C    . LEU   A 1 75  ? 34.210 -2.329  -5.327  1.00 11.34 ?  75  LEU   A C    1 
ATOM   1687 O  O    . LEU   A 1 75  ? 34.086 -1.614  -6.327  1.00 12.91 ?  75  LEU   A O    1 
ATOM   1688 C  CB   . LEU   A 1 75  ? 33.411 -1.870  -3.017  1.00 11.17 ?  75  LEU   A CB   1 
ATOM   1689 C  CG   . LEU   A 1 75  ? 33.633 -1.454  -1.564  1.00 12.82 ?  75  LEU   A CG   1 
ATOM   1690 C  CD1  . LEU   A 1 75  ? 32.342 -1.609  -0.770  1.00 14.73 ?  75  LEU   A CD1  1 
ATOM   1691 C  CD2  . LEU   A 1 75  ? 34.757 -2.209  -0.907  1.00 15.62 ?  75  LEU   A CD2  1 
ATOM   1692 H  H    . LEU   A 1 75  ? 34.440 0.208   -3.800  1.00 13.11 ?  75  LEU   A H    1 
ATOM   1693 H  HA   . LEU   A 1 75  ? 35.341 -2.263  -3.618  1.00 13.16 ?  75  LEU   A HA   1 
ATOM   1694 H  HB2  . LEU   A 1 75  ? 32.691 -1.322  -3.363  1.00 13.37 ?  75  LEU   A HB2  1 
ATOM   1695 H  HB3  . LEU   A 1 75  ? 33.130 -2.799  -3.008  1.00 13.37 ?  75  LEU   A HB3  1 
ATOM   1696 H  HG   . LEU   A 1 75  ? 33.875 -0.515  -1.550  1.00 15.36 ?  75  LEU   A HG   1 
ATOM   1697 H  HD11 . LEU   A 1 75  ? 32.506 -1.336  0.147   1.00 17.65 ?  75  LEU   A HD11 1 
ATOM   1698 H  HD12 . LEU   A 1 75  ? 31.664 -1.041  -1.168  1.00 17.65 ?  75  LEU   A HD12 1 
ATOM   1699 H  HD13 . LEU   A 1 75  ? 32.065 -2.534  -0.799  1.00 17.65 ?  75  LEU   A HD13 1 
ATOM   1700 H  HD21 . LEU   A 1 75  ? 34.815 -1.947  0.025   1.00 18.72 ?  75  LEU   A HD21 1 
ATOM   1701 H  HD22 . LEU   A 1 75  ? 34.584 -3.161  -0.973  1.00 18.72 ?  75  LEU   A HD22 1 
ATOM   1702 H  HD23 . LEU   A 1 75  ? 35.593 -1.996  -1.359  1.00 18.72 ?  75  LEU   A HD23 1 
ATOM   1703 N  N    . LYS   A 1 76  ? 34.028 -3.647  -5.347  1.00 11.63 ?  76  LYS   A N    1 
ATOM   1704 C  CA   . LYS   A 1 76  ? 33.428 -4.360  -6.467  1.00 12.08 ?  76  LYS   A CA   1 
ATOM   1705 C  C    . LYS   A 1 76  ? 31.917 -4.444  -6.272  1.00 10.93 ?  76  LYS   A C    1 
ATOM   1706 O  O    . LYS   A 1 76  ? 31.436 -4.578  -5.150  1.00 10.90 ?  76  LYS   A O    1 
ATOM   1707 C  CB   . LYS   A 1 76  ? 33.971 -5.798  -6.526  1.00 14.10 ?  76  LYS   A CB   1 
ATOM   1708 C  CG   . LYS   A 1 76  ? 35.484 -5.908  -6.690  1.00 15.99 ?  76  LYS   A CG   1 
ATOM   1709 C  CD   . LYS   A 1 76  ? 35.998 -7.317  -6.483  1.00 17.46 ?  76  LYS   A CD   1 
ATOM   1710 C  CE   . LYS   A 1 76  ? 37.490 -7.380  -6.719  1.00 19.94 ?  76  LYS   A CE   1 
ATOM   1711 N  NZ   . LYS   A 1 76  ? 38.021 -8.738  -6.519  1.00 20.89 ?  76  LYS   A NZ   1 
ATOM   1712 H  H    . LYS   A 1 76  ? 34.254 -4.166  -4.698  1.00 13.94 ?  76  LYS   A H    1 
ATOM   1713 H  HA   . LYS   A 1 76  ? 33.626 -3.908  -7.304  1.00 14.47 ?  76  LYS   A HA   1 
ATOM   1714 H  HB2  . LYS   A 1 76  ? 33.734 -6.252  -5.703  1.00 16.90 ?  76  LYS   A HB2  1 
ATOM   1715 H  HB3  . LYS   A 1 76  ? 33.563 -6.252  -7.279  1.00 16.90 ?  76  LYS   A HB3  1 
ATOM   1716 H  HG2  . LYS   A 1 76  ? 35.726 -5.630  -7.588  1.00 19.16 ?  76  LYS   A HG2  1 
ATOM   1717 H  HG3  . LYS   A 1 76  ? 35.917 -5.333  -6.038  1.00 19.16 ?  76  LYS   A HG3  1 
ATOM   1718 H  HD2  . LYS   A 1 76  ? 35.819 -7.597  -5.570  1.00 20.93 ?  76  LYS   A HD2  1 
ATOM   1719 H  HD3  . LYS   A 1 76  ? 35.561 -7.917  -7.110  1.00 20.93 ?  76  LYS   A HD3  1 
ATOM   1720 H  HE2  . LYS   A 1 76  ? 37.679 -7.111  -7.631  1.00 23.91 ?  76  LYS   A HE2  1 
ATOM   1721 H  HE3  . LYS   A 1 76  ? 37.936 -6.787  -6.095  1.00 23.91 ?  76  LYS   A HE3  1 
ATOM   1722 H  HZ1  . LYS   A 1 76  ? 38.898 -8.753  -6.665  1.00 25.05 ?  76  LYS   A HZ1  1 
ATOM   1723 H  HZ2  . LYS   A 1 76  ? 37.862 -9.013  -5.686  1.00 25.05 ?  76  LYS   A HZ2  1 
ATOM   1724 H  HZ3  . LYS   A 1 76  ? 37.628 -9.308  -7.085  1.00 25.05 ?  76  LYS   A HZ3  1 
ATOM   1725 N  N    . VAL   A 1 77  ? 31.163 -4.411  -7.376  1.00 11.46 ?  77  VAL   A N    1 
ATOM   1726 C  CA   . VAL   A 1 77  ? 29.756 -4.804  -7.289  1.00 11.30 ?  77  VAL   A CA   1 
ATOM   1727 C  C    . VAL   A 1 77  ? 29.693 -6.258  -6.846  1.00 10.91 ?  77  VAL   A C    1 
ATOM   1728 O  O    . VAL   A 1 77  ? 30.345 -7.130  -7.432  1.00 11.34 ?  77  VAL   A O    1 
ATOM   1729 C  CB   . VAL   A 1 77  ? 29.031 -4.586  -8.625  1.00 12.47 ?  77  VAL   A CB   1 
ATOM   1730 C  CG1  . VAL   A 1 77  ? 27.578 -5.042  -8.520  1.00 13.15 ?  77  VAL   A CG1  1 
ATOM   1731 C  CG2  . VAL   A 1 77  ? 29.102 -3.126  -9.037  1.00 13.76 ?  77  VAL   A CG2  1 
ATOM   1732 H  H    . VAL   A 1 77  ? 31.436 -4.168  -8.155  1.00 13.72 ?  77  VAL   A H    1 
ATOM   1733 H  HA   . VAL   A 1 77  ? 29.320 -4.265  -6.615  1.00 13.53 ?  77  VAL   A HA   1 
ATOM   1734 H  HB   . VAL   A 1 77  ? 29.465 -5.114  -9.314  1.00 14.94 ?  77  VAL   A HB   1 
ATOM   1735 H  HG11 . VAL   A 1 77  ? 27.097 -4.739  -9.302  1.00 15.75 ?  77  VAL   A HG11 1 
ATOM   1736 H  HG12 . VAL   A 1 77  ? 27.554 -6.011  -8.470  1.00 15.75 ?  77  VAL   A HG12 1 
ATOM   1737 H  HG13 . VAL   A 1 77  ? 27.188 -4.659  -7.719  1.00 15.75 ?  77  VAL   A HG13 1 
ATOM   1738 H  HG21 . VAL   A 1 77  ? 28.593 -3.006  -9.854  1.00 16.49 ?  77  VAL   A HG21 1 
ATOM   1739 H  HG22 . VAL   A 1 77  ? 28.724 -2.581  -8.329  1.00 16.49 ?  77  VAL   A HG22 1 
ATOM   1740 H  HG23 . VAL   A 1 77  ? 30.028 -2.883  -9.185  1.00 16.49 ?  77  VAL   A HG23 1 
ATOM   1741 N  N    . GLY   A 1 78  ? 28.910 -6.527  -5.800  1.00 10.78 ?  78  GLY   A N    1 
ATOM   1742 C  CA   . GLY   A 1 78  ? 28.892 -7.817  -5.143  1.00 10.69 ?  78  GLY   A CA   1 
ATOM   1743 C  C    . GLY   A 1 78  ? 29.813 -7.911  -3.947  1.00 10.31 ?  78  GLY   A C    1 
ATOM   1744 O  O    . GLY   A 1 78  ? 29.752 -8.912  -3.215  1.00 10.88 ?  78  GLY   A O    1 
ATOM   1745 H  H    . GLY   A 1 78  ? 28.359 -5.957  -5.459  1.00 12.91 ?  78  GLY   A H    1 
ATOM   1746 H  HA2  . GLY   A 1 78  ? 27.989 -8.005  -4.846  1.00 12.80 ?  78  GLY   A HA2  1 
ATOM   1747 H  HA3  . GLY   A 1 78  ? 29.150 -8.499  -5.781  1.00 12.80 ?  78  GLY   A HA3  1 
ATOM   1748 N  N    . GLY   A 1 79  ? 30.664 -6.905  -3.726  1.00 10.26 ?  79  GLY   A N    1 
ATOM   1749 C  CA   . GLY   A 1 79  ? 31.631 -6.921  -2.653  1.00 10.51 ?  79  GLY   A CA   1 
ATOM   1750 C  C    . GLY   A 1 79  ? 31.189 -6.126  -1.438  1.00 10.03 ?  79  GLY   A C    1 
ATOM   1751 O  O    . GLY   A 1 79  ? 30.068 -5.620  -1.356  1.00 10.66 ?  79  GLY   A O    1 
ATOM   1752 H  H    . GLY   A 1 79  ? 30.699 -6.189  -4.202  1.00 12.28 ?  79  GLY   A H    1 
ATOM   1753 H  HA2  . GLY   A 1 79  ? 31.785 -7.847  -2.379  1.00 12.59 ?  79  GLY   A HA2  1 
ATOM   1754 H  HA3  . GLY   A 1 79  ? 32.471 -6.562  -2.970  1.00 12.59 ?  79  GLY   A HA3  1 
ATOM   1755 N  N    . SER   A 1 80  ? 32.102 -6.030  -0.471  1.00 10.68 ?  80  SER   A N    1 
ATOM   1756 C  CA   . SER   A 1 80  ? 31.786 -5.404  0.802   1.00 10.27 ?  80  SER   A CA   1 
ATOM   1757 C  C    . SER   A 1 80  ? 33.057 -4.956  1.501   1.00 10.22 ?  80  SER   A C    1 
ATOM   1758 O  O    . SER   A 1 80  ? 34.166 -5.385  1.164   1.00 11.73 ?  80  SER   A O    1 
ATOM   1759 C  CB   . SER   A 1 80  ? 31.029 -6.368  1.724   1.00 11.27 ?  80  SER   A CB   1 
ATOM   1760 O  OG   . SER   A 1 80  ? 31.859 -7.414  2.203   1.00 12.90 ?  80  SER   A OG   1 
ATOM   1761 H  H    . SER   A 1 80  ? 32.910 -6.316  -0.536  1.00 12.79 ?  80  SER   A H    1 
ATOM   1762 H  HA   . SER   A 1 80  ? 31.233 -4.625  0.631   1.00 12.30 ?  80  SER   A HA   1 
ATOM   1763 H  HB2  . SER   A 1 80  ? 30.691 -5.867  2.481   1.00 13.50 ?  80  SER   A HB2  1 
ATOM   1764 H  HB3  . SER   A 1 80  ? 30.292 -6.753  1.227   1.00 13.50 ?  80  SER   A HB3  1 
ATOM   1765 H  HG   . SER   A 1 80  ? 32.161 -7.859  1.552   1.00 15.45 ?  80  SER   A HG   1 
ATOM   1766 N  N    . CYS   A 1 81  ? 32.872 -4.104  2.508   1.00 9.92  ?  81  CYS   A N    1 
ATOM   1767 C  CA   . CYS   A 1 81  ? 33.924 -3.819  3.468   1.00 9.96  ?  81  CYS   A CA   1 
ATOM   1768 C  C    . CYS   A 1 81  ? 33.283 -3.583  4.826   1.00 9.76  ?  81  CYS   A C    1 
ATOM   1769 O  O    . CYS   A 1 81  ? 32.115 -3.186  4.923   1.00 11.01 ?  81  CYS   A O    1 
ATOM   1770 C  CB   . CYS   A 1 81  ? 34.794 -2.625  3.050   1.00 11.14 ?  81  CYS   A CB   1 
ATOM   1771 S  SG   . CYS   A 1 81  ? 33.894 -1.056  3.070   1.00 11.23 ?  81  CYS   A SG   1 
ATOM   1772 H  H    . CYS   A 1 81  ? 32.137 -3.677  2.658   1.00 11.88 ?  81  CYS   A H    1 
ATOM   1773 H  HA   . CYS   A 1 81  ? 34.502 -4.594  3.539   1.00 11.92 ?  81  CYS   A HA   1 
ATOM   1774 H  HB2  . CYS   A 1 81  ? 35.547 -2.553  3.662   1.00 13.34 ?  81  CYS   A HB2  1 
ATOM   1775 H  HB3  . CYS   A 1 81  ? 35.125 -2.776  2.146   1.00 13.34 ?  81  CYS   A HB3  1 
ATOM   1776 H  HG   . CYS   A 1 81  ? 34.636 -0.173  2.733   1.00 13.45 ?  81  CYS   A HG   1 
ATOM   1777 N  N    . VAL   A 1 82  ? 34.055 -3.843  5.874   1.00 10.09 ?  82  VAL   A N    1 
ATOM   1778 C  CA   . VAL   A 1 82  ? 33.631 -3.600  7.245   1.00 10.51 ?  82  VAL   A CA   1 
ATOM   1779 C  C    . VAL   A 1 82  ? 34.233 -2.288  7.712   1.00 10.91 ?  82  VAL   A C    1 
ATOM   1780 O  O    . VAL   A 1 82  ? 35.458 -2.114  7.689   1.00 11.83 ?  82  VAL   A O    1 
ATOM   1781 C  CB   . VAL   A 1 82  ? 34.052 -4.739  8.184   1.00 12.16 ?  82  VAL   A CB   1 
ATOM   1782 C  CG1  . VAL   A 1 82  ? 33.595 -4.441  9.606   1.00 13.52 ?  82  VAL   A CG1  1 
ATOM   1783 C  CG2  . VAL   A 1 82  ? 33.500 -6.069  7.707   1.00 13.25 ?  82  VAL   A CG2  1 
ATOM   1784 H  H    . VAL   A 1 82  ? 34.852 -4.173  5.817   1.00 12.08 ?  82  VAL   A H    1 
ATOM   1785 H  HA   . VAL   A 1 82  ? 32.664 -3.519  7.273   1.00 12.59 ?  82  VAL   A HA   1 
ATOM   1786 H  HB   . VAL   A 1 82  ? 35.018 -4.796  8.193   1.00 14.56 ?  82  VAL   A HB   1 
ATOM   1787 H  HG11 . VAL   A 1 82  ? 33.678 -5.247  10.140  1.00 16.20 ?  82  VAL   A HG11 1 
ATOM   1788 H  HG12 . VAL   A 1 82  ? 34.149 -3.739  9.984   1.00 16.20 ?  82  VAL   A HG12 1 
ATOM   1789 H  HG13 . VAL   A 1 82  ? 32.666 -4.155  9.589   1.00 16.20 ?  82  VAL   A HG13 1 
ATOM   1790 H  HG21 . VAL   A 1 82  ? 33.745 -6.757  8.345   1.00 15.88 ?  82  VAL   A HG21 1 
ATOM   1791 H  HG22 . VAL   A 1 82  ? 32.535 -6.005  7.641   1.00 15.88 ?  82  VAL   A HG22 1 
ATOM   1792 H  HG23 . VAL   A 1 82  ? 33.880 -6.272  6.839   1.00 15.88 ?  82  VAL   A HG23 1 
ATOM   1793 N  N    . LEU   A 1 83  ? 33.377 -1.369  8.145   1.00 10.37 ?  83  LEU   A N    1 
ATOM   1794 C  CA   . LEU   A 1 83  ? 33.794 -0.102  8.720   1.00 10.46 ?  83  LEU   A CA   1 
ATOM   1795 C  C    . LEU   A 1 83  ? 33.083 0.078   10.056  1.00 10.60 ?  83  LEU   A C    1 
ATOM   1796 O  O    . LEU   A 1 83  ? 32.366 -0.812  10.527  1.00 11.17 ?  83  LEU   A O    1 
ATOM   1797 C  CB   . LEU   A 1 83  ? 33.549 1.055   7.739   1.00 11.23 ?  83  LEU   A CB   1 
ATOM   1798 C  CG   . LEU   A 1 83  ? 34.446 1.052   6.496   1.00 11.76 ?  83  LEU   A CG   1 
ATOM   1799 C  CD1  . LEU   A 1 83  ? 33.996 2.108   5.507   1.00 12.47 ?  83  LEU   A CD1  1 
ATOM   1800 C  CD2  . LEU   A 1 83  ? 35.909 1.265   6.875   1.00 12.54 ?  83  LEU   A CD2  1 
ATOM   1801 H  H    . LEU   A 1 83  ? 32.522 -1.460  8.106   1.00 12.42 ?  83  LEU   A H    1 
ATOM   1802 H  HA   . LEU   A 1 83  ? 34.743 -0.136  8.898   1.00 12.53 ?  83  LEU   A HA   1 
ATOM   1803 H  HB2  . LEU   A 1 83  ? 32.630 1.014   7.430   1.00 13.46 ?  83  LEU   A HB2  1 
ATOM   1804 H  HB3  . LEU   A 1 83  ? 33.696 1.894   8.202   1.00 13.46 ?  83  LEU   A HB3  1 
ATOM   1805 H  HG   . LEU   A 1 83  ? 34.378 0.189   6.063   1.00 14.09 ?  83  LEU   A HG   1 
ATOM   1806 H  HD11 . LEU   A 1 83  ? 34.582 2.079   4.731   1.00 14.94 ?  83  LEU   A HD11 1 
ATOM   1807 H  HD12 . LEU   A 1 83  ? 33.085 1.918   5.240   1.00 14.94 ?  83  LEU   A HD12 1 
ATOM   1808 H  HD13 . LEU   A 1 83  ? 34.049 2.978   5.928   1.00 14.94 ?  83  LEU   A HD13 1 
ATOM   1809 H  HD21 . LEU   A 1 83  ? 36.428 1.413   6.066   1.00 15.02 ?  83  LEU   A HD21 1 
ATOM   1810 H  HD22 . LEU   A 1 83  ? 35.980 2.040   7.455   1.00 15.02 ?  83  LEU   A HD22 1 
ATOM   1811 H  HD23 . LEU   A 1 83  ? 36.239 0.477   7.335   1.00 15.02 ?  83  LEU   A HD23 1 
ATOM   1812 N  N    . SER   A 1 84  ? 33.297 1.228   10.687  1.00 11.20 ?  84  SER   A N    1 
ATOM   1813 C  CA   . SER   A 1 84  ? 32.654 1.483   11.966  1.00 11.32 ?  84  SER   A CA   1 
ATOM   1814 C  C    . SER   A 1 84  ? 31.135 1.568   11.820  1.00 11.24 ?  84  SER   A C    1 
ATOM   1815 O  O    . SER   A 1 84  ? 30.607 2.031   10.808  1.00 11.43 ?  84  SER   A O    1 
ATOM   1816 C  CB   . SER   A 1 84  ? 33.158 2.802   12.543  1.00 12.48 ?  84  SER   A CB   1 
ATOM   1817 O  OG   . SER   A 1 84  ? 32.521 3.088   13.775  1.00 13.34 ?  84  SER   A OG   1 
ATOM   1818 H  H    . SER   A 1 84  ? 33.801 1.867   10.394  1.00 13.42 ?  84  SER   A H    1 
ATOM   1819 H  HA   . SER   A 1 84  ? 32.875 0.771   12.581  1.00 13.55 ?  84  SER   A HA   1 
ATOM   1820 H  HB2  . SER   A 1 84  ? 34.118 2.742   12.686  1.00 14.95 ?  84  SER   A HB2  1 
ATOM   1821 H  HB3  . SER   A 1 84  ? 32.967 3.519   11.914  1.00 14.95 ?  84  SER   A HB3  1 
ATOM   1822 H  HG   . SER   A 1 84  ? 32.808 3.815   14.085  1.00 15.98 ?  84  SER   A HG   1 
ATOM   1823 N  N    . GLY   A 1 85  ? 30.432 1.148   12.869  1.00 11.81 ?  85  GLY   A N    1 
ATOM   1824 C  CA   . GLY   A 1 85  ? 29.009 1.383   12.968  1.00 12.45 ?  85  GLY   A CA   1 
ATOM   1825 C  C    . GLY   A 1 85  ? 28.642 2.699   13.613  1.00 12.20 ?  85  GLY   A C    1 
ATOM   1826 O  O    . GLY   A 1 85  ? 27.452 3.012   13.736  1.00 12.70 ?  85  GLY   A O    1 
ATOM   1827 H  H    . GLY   A 1 85  ? 30.771 0.721   13.539  1.00 14.15 ?  85  GLY   A H    1 
ATOM   1828 H  HA2  . GLY   A 1 85  ? 28.630 1.363   12.076  1.00 14.92 ?  85  GLY   A HA2  1 
ATOM   1829 H  HA3  . GLY   A 1 85  ? 28.610 0.672   13.484  1.00 14.92 ?  85  GLY   A HA3  1 
ATOM   1830 N  N    . HIS   A 1 86  ? 29.633 3.474   14.044  1.00 12.00 ?  86  HIS   A N    1 
ATOM   1831 C  CA   . HIS   A 1 86  ? 29.412 4.807   14.615  1.00 12.67 ?  86  HIS   A CA   1 
ATOM   1832 C  C    . HIS   A 1 86  ? 28.428 4.679   15.772  1.00 13.11 ?  86  HIS   A C    1 
ATOM   1833 O  O    . HIS   A 1 86  ? 28.611 3.794   16.624  1.00 14.15 ?  86  HIS   A O    1 
ATOM   1834 C  CB   . HIS   A 1 86  ? 29.029 5.788   13.513  1.00 12.78 ?  86  HIS   A CB   1 
ATOM   1835 C  CG   . HIS   A 1 86  ? 30.079 5.889   12.467  1.00 12.55 ?  86  HIS   A CG   1 
ATOM   1836 N  ND1  . HIS   A 1 86  ? 31.161 6.733   12.588  1.00 13.53 ?  86  HIS   A ND1  1 
ATOM   1837 C  CD2  . HIS   A 1 86  ? 30.261 5.196   11.322  1.00 12.46 ?  86  HIS   A CD2  1 
ATOM   1838 C  CE1  . HIS   A 1 86  ? 31.952 6.572   11.543  1.00 13.35 ?  86  HIS   A CE1  1 
ATOM   1839 N  NE2  . HIS   A 1 86  ? 31.434 5.639   10.766  1.00 12.64 ?  86  HIS   A NE2  1 
ATOM   1840 H  H    . HIS   A 1 86  ? 30.460 3.254   14.024  1.00 14.37 ?  86  HIS   A H    1 
ATOM   1841 H  HA   . HIS   A 1 86  ? 30.249 5.124   14.987  1.00 15.17 ?  86  HIS   A HA   1 
ATOM   1842 H  HB2  . HIS   A 1 86  ? 28.207 5.496   13.089  1.00 15.31 ?  86  HIS   A HB2  1 
ATOM   1843 H  HB3  . HIS   A 1 86  ? 28.904 6.676   13.896  1.00 15.31 ?  86  HIS   A HB3  1 
ATOM   1844 H  HD2  . HIS   A 1 86  ? 29.703 4.533   10.979  1.00 14.93 ?  86  HIS   A HD2  1 
ATOM   1845 H  HE1  . HIS   A 1 86  ? 32.739 7.040   11.370  1.00 16.00 ?  86  HIS   A HE1  1 
ATOM   1846 H  HE2  . HIS   A 1 86  ? 31.767 5.364   10.015  1.00 15.14 ?  86  HIS   A HE2  1 
ATOM   1847 N  N    . ASN   A 1 87  ? 27.417 5.532   15.852  1.00 14.08 ?  87  ASN   A N    1 
ATOM   1848 C  CA   . ASN   A 1 87  ? 26.433 5.512   16.917  1.00 15.10 ?  87  ASN   A CA   1 
ATOM   1849 C  C    . ASN   A 1 87  ? 25.317 4.512   16.672  1.00 16.35 ?  87  ASN   A C    1 
ATOM   1850 O  O    . ASN   A 1 87  ? 24.407 4.423   17.500  1.00 18.62 ?  87  ASN   A O    1 
ATOM   1851 C  CB   . ASN   A 1 87  ? 25.825 6.910   17.088  1.00 15.98 ?  87  ASN   A CB   1 
ATOM   1852 C  CG   . ASN   A 1 87  ? 25.318 7.496   15.775  1.00 16.95 ?  87  ASN   A CG   1 
ATOM   1853 O  OD1  . ASN   A 1 87  ? 25.964 7.387   14.735  1.00 17.50 ?  87  ASN   A OD1  1 
ATOM   1854 N  ND2  . ASN   A 1 87  ? 24.157 8.125   15.824  1.00 18.07 ?  87  ASN   A ND2  1 
ATOM   1855 H  H    . ASN   A 1 87  ? 27.274 6.154   15.280  1.00 16.87 ?  87  ASN   A H    1 
ATOM   1856 H  HA   . ASN   A 1 87  ? 26.864 5.268   17.754  1.00 18.09 ?  87  ASN   A HA   1 
ATOM   1857 H  HB2  . ASN   A 1 87  ? 25.072 6.855   17.707  1.00 19.15 ?  87  ASN   A HB2  1 
ATOM   1858 H  HB3  . ASN   A 1 87  ? 26.499 7.504   17.448  1.00 19.15 ?  87  ASN   A HB3  1 
ATOM   1859 H  HD21 . ASN   A 1 87  ? 23.832 8.471   15.110  1.00 21.65 ?  87  ASN   A HD21 1 
ATOM   1860 H  HD22 . ASN   A 1 87  ? 23.732 8.189   16.569  1.00 21.65 ?  87  ASN   A HD22 1 
ATOM   1861 N  N    . LEU   A 1 88  ? 25.366 3.753   15.581  1.00 15.21 ?  88  LEU   A N    1 
ATOM   1862 C  CA   . LEU   A 1 88  ? 24.255 2.890   15.193  1.00 15.36 ?  88  LEU   A CA   1 
ATOM   1863 C  C    . LEU   A 1 88  ? 24.478 1.415   15.495  1.00 14.81 ?  88  LEU   A C    1 
ATOM   1864 O  O    . LEU   A 1 88  ? 23.503 0.681   15.671  1.00 15.83 ?  88  LEU   A O    1 
ATOM   1865 C  CB   . LEU   A 1 88  ? 23.988 3.043   13.695  1.00 15.86 ?  88  LEU   A CB   1 
ATOM   1866 C  CG   . LEU   A 1 88  ? 23.690 4.467   13.223  1.00 17.53 ?  88  LEU   A CG   1 
ATOM   1867 C  CD1  . LEU   A 1 88  ? 23.506 4.496   11.717  1.00 17.84 ?  88  LEU   A CD1  1 
ATOM   1868 C  CD2  . LEU   A 1 88  ? 22.463 5.034   13.928  1.00 19.04 ?  88  LEU   A CD2  1 
ATOM   1869 H  H    . LEU   A 1 88  ? 26.041 3.712   15.052  1.00 18.23 ?  88  LEU   A H    1 
ATOM   1870 H  HA   . LEU   A 1 88  ? 23.458 3.174   15.670  1.00 18.40 ?  88  LEU   A HA   1 
ATOM   1871 H  HB2  . LEU   A 1 88  ? 24.767 2.737   13.209  1.00 19.01 ?  88  LEU   A HB2  1 
ATOM   1872 H  HB3  . LEU   A 1 88  ? 23.222 2.497   13.461  1.00 19.01 ?  88  LEU   A HB3  1 
ATOM   1873 H  HG   . LEU   A 1 88  ? 24.444 5.036   13.438  1.00 21.01 ?  88  LEU   A HG   1 
ATOM   1874 H  HD11 . LEU   A 1 88  ? 23.321 5.408   11.438  1.00 21.39 ?  88  LEU   A HD11 1 
ATOM   1875 H  HD12 . LEU   A 1 88  ? 24.320 4.180   11.294  1.00 21.39 ?  88  LEU   A HD12 1 
ATOM   1876 H  HD13 . LEU   A 1 88  ? 22.763 3.921   11.477  1.00 21.39 ?  88  LEU   A HD13 1 
ATOM   1877 H  HD21 . LEU   A 1 88  ? 22.228 5.880   13.517  1.00 22.82 ?  88  LEU   A HD21 1 
ATOM   1878 H  HD22 . LEU   A 1 88  ? 21.732 4.406   13.839  1.00 22.82 ?  88  LEU   A HD22 1 
ATOM   1879 H  HD23 . LEU   A 1 88  ? 22.676 5.168   14.864  1.00 22.82 ?  88  LEU   A HD23 1 
ATOM   1880 N  N    . ALA   A 1 89  ? 25.727 0.968   15.547  1.00 13.92 ?  89  ALA   A N    1 
ATOM   1881 C  CA   . ALA   A 1 89  ? 26.068 -0.444  15.648  1.00 13.72 ?  89  ALA   A CA   1 
ATOM   1882 C  C    . ALA   A 1 89  ? 27.555 -0.509  15.954  1.00 14.16 ?  89  ALA   A C    1 
ATOM   1883 O  O    . ALA   A 1 89  ? 28.267 0.489   15.835  1.00 14.66 ?  89  ALA   A O    1 
ATOM   1884 C  CB   . ALA   A 1 89  ? 25.777 -1.162  14.331  1.00 13.17 ?  89  ALA   A CB   1 
ATOM   1885 H  H    . ALA   A 1 89  ? 26.414 1.483   15.515  1.00 16.68 ?  89  ALA   A H    1 
ATOM   1886 H  HA   . ALA   A 1 89  ? 25.566 -0.861  16.367  1.00 16.44 ?  89  ALA   A HA   1 
ATOM   1887 H  HB1  . ALA   A 1 89  ? 26.032 -2.097  14.418  1.00 15.78 ?  89  ALA   A HB1  1 
ATOM   1888 H  HB2  . ALA   A 1 89  ? 24.826 -1.101  14.136  1.00 15.78 ?  89  ALA   A HB2  1 
ATOM   1889 H  HB3  . ALA   A 1 89  ? 26.287 -0.747  13.621  1.00 15.78 ?  89  ALA   A HB3  1 
ATOM   1890 N  N    . LYS   A 1 90  ? 28.034 -1.688  16.337  1.00 14.65 ?  90  LYS   A N    1 
ATOM   1891 C  CA   . LYS   A 1 90  ? 29.478 -1.836  16.482  1.00 15.15 ?  90  LYS   A CA   1 
ATOM   1892 C  C    . LYS   A 1 90  ? 30.174 -1.647  15.137  1.00 14.12 ?  90  LYS   A C    1 
ATOM   1893 O  O    . LYS   A 1 90  ? 31.105 -0.835  15.006  1.00 15.27 ?  90  LYS   A O    1 
ATOM   1894 C  CB   . LYS   A 1 90  ? 29.817 -3.194  17.099  1.00 18.07 ?  90  LYS   A CB   1 
ATOM   1895 C  CG   . LYS   A 1 90  ? 31.291 -3.338  17.436  1.00 22.94 ?  90  LYS   A CG   1 
ATOM   1896 C  CD   . LYS   A 1 90  ? 31.551 -4.575  18.278  1.00 27.86 ?  90  LYS   A CD   1 
ATOM   1897 C  CE   . LYS   A 1 90  ? 32.960 -4.577  18.855  1.00 31.65 ?  90  LYS   A CE   1 
ATOM   1898 N  NZ   . LYS   A 1 90  ? 34.001 -4.836  17.825  1.00 34.47 ?  90  LYS   A NZ   1 
ATOM   1899 H  H    . LYS   A 1 90  ? 27.563 -2.383  16.516  1.00 17.55 ?  90  LYS   A H    1 
ATOM   1900 H  HA   . LYS   A 1 90  ? 29.803 -1.148  17.081  1.00 18.15 ?  90  LYS   A HA   1 
ATOM   1901 H  HB2  . LYS   A 1 90  ? 29.309 -3.302  17.921  1.00 21.66 ?  90  LYS   A HB2  1 
ATOM   1902 H  HB3  . LYS   A 1 90  ? 29.582 -3.895  16.473  1.00 21.66 ?  90  LYS   A HB3  1 
ATOM   1903 H  HG2  . LYS   A 1 90  ? 31.801 -3.415  16.616  1.00 27.50 ?  90  LYS   A HG2  1 
ATOM   1904 H  HG3  . LYS   A 1 90  ? 31.581 -2.560  17.940  1.00 27.50 ?  90  LYS   A HG3  1 
ATOM   1905 H  HD2  . LYS   A 1 90  ? 30.921 -4.600  19.016  1.00 33.40 ?  90  LYS   A HD2  1 
ATOM   1906 H  HD3  . LYS   A 1 90  ? 31.449 -5.366  17.725  1.00 33.40 ?  90  LYS   A HD3  1 
ATOM   1907 H  HE2  . LYS   A 1 90  ? 33.140 -3.711  19.253  1.00 37.96 ?  90  LYS   A HE2  1 
ATOM   1908 H  HE3  . LYS   A 1 90  ? 33.025 -5.271  19.530  1.00 37.96 ?  90  LYS   A HE3  1 
ATOM   1909 H  HZ1  . LYS   A 1 90  ? 34.808 -4.836  18.202  1.00 41.34 ?  90  LYS   A HZ1  1 
ATOM   1910 H  HZ2  . LYS   A 1 90  ? 33.862 -5.629  17.445  1.00 41.34 ?  90  LYS   A HZ2  1 
ATOM   1911 H  HZ3  . LYS   A 1 90  ? 33.974 -4.206  17.199  1.00 41.34 ?  90  LYS   A HZ3  1 
ATOM   1912 N  N    . HIS   A 1 91  ? 29.702 -2.364  14.118  1.00 12.54 ?  91  HIS   A N    1 
ATOM   1913 C  CA   . HIS   A 1 91  ? 30.276 -2.352  12.788  1.00 11.87 ?  91  HIS   A CA   1 
ATOM   1914 C  C    . HIS   A 1 91  ? 29.188 -2.076  11.769  1.00 10.85 ?  91  HIS   A C    1 
ATOM   1915 O  O    . HIS   A 1 91  ? 28.024 -2.437  11.968  1.00 11.51 ?  91  HIS   A O    1 
ATOM   1916 C  CB   . HIS   A 1 91  ? 30.867 -3.722  12.429  1.00 14.35 ?  91  HIS   A CB   1 
ATOM   1917 C  CG   . HIS   A 1 91  ? 31.850 -4.243  13.427  1.00 18.41 ?  91  HIS   A CG   1 
ATOM   1918 N  ND1  . HIS   A 1 91  ? 33.131 -3.749  13.535  1.00 20.68 ?  91  HIS   A ND1  1 
ATOM   1919 C  CD2  . HIS   A 1 91  ? 31.745 -5.224  14.354  1.00 20.31 ?  91  HIS   A CD2  1 
ATOM   1920 C  CE1  . HIS   A 1 91  ? 33.773 -4.401  14.489  1.00 21.49 ?  91  HIS   A CE1  1 
ATOM   1921 N  NE2  . HIS   A 1 91  ? 32.954 -5.302  15.002  1.00 21.60 ?  91  HIS   A NE2  1 
ATOM   1922 H  H    . HIS   A 1 91  ? 29.021 -2.899  14.188  1.00 15.02 ?  91  HIS   A H    1 
ATOM   1923 H  HA   . HIS   A 1 91  ? 30.963 -1.679  12.721  1.00 14.21 ?  91  HIS   A HA   1 
ATOM   1924 H  HB2  . HIS   A 1 91  ? 30.145 -4.371  12.364  1.00 17.20 ?  91  HIS   A HB2  1 
ATOM   1925 H  HB3  . HIS   A 1 91  ? 31.321 -3.654  11.575  1.00 17.20 ?  91  HIS   A HB3  1 
ATOM   1926 H  HD1  . HIS   A 1 91  ? 33.463 -3.116  13.055  1.00 24.79 ?  91  HIS   A HD1  1 
ATOM   1927 H  HD2  . HIS   A 1 91  ? 30.999 -5.749  14.521  1.00 24.35 ?  91  HIS   A HD2  1 
ATOM   1928 H  HE1  . HIS   A 1 91  ? 34.654 -4.246  14.752  1.00 25.76 ?  91  HIS   A HE1  1 
ATOM   1929 N  N    . CYS   A 1 92  ? 29.588 -1.474  10.653  1.00 10.40 ?  92  CYS   A N    1 
ATOM   1930 C  CA   . CYS   A 1 92  ? 28.749 -1.399  9.466   1.00 10.31 ?  92  CYS   A CA   1 
ATOM   1931 C  C    . CYS   A 1 92  ? 29.395 -2.219  8.359   1.00 9.84  ?  92  CYS   A C    1 
ATOM   1932 O  O    . CYS   A 1 92  ? 30.553 -1.972  7.990   1.00 10.53 ?  92  CYS   A O    1 
ATOM   1933 C  CB   . CYS   A 1 92  ? 28.540 0.042   9.001   1.00 10.71 ?  92  CYS   A CB   1 
ATOM   1934 S  SG   . CYS   A 1 92  ? 27.517 0.150   7.507   1.00 10.35 ?  92  CYS   A SG   1 
ATOM   1935 H  H    . CYS   A 1 92  ? 30.355 -1.094  10.556  1.00 12.45 ?  92  CYS   A H    1 
ATOM   1936 H  HA   . CYS   A 1 92  ? 27.879 -1.781  9.663   1.00 12.34 ?  92  CYS   A HA   1 
ATOM   1937 H  HB2  . CYS   A 1 92  ? 28.093 0.541   9.704   1.00 12.83 ?  92  CYS   A HB2  1 
ATOM   1938 H  HB3  . CYS   A 1 92  ? 29.401 0.441   8.806   1.00 12.83 ?  92  CYS   A HB3  1 
ATOM   1939 H  HG   . CYS   A 1 92  ? 27.380 1.301   7.204   1.00 12.40 ?  92  CYS   A HG   1 
ATOM   1940 N  N    . LEU   A 1 93  ? 28.653 -3.204  7.857   1.00 9.79  ?  93  LEU   A N    1 
ATOM   1941 C  CA   . LEU   A 1 93  ? 29.052 -3.964  6.679   1.00 9.29  ?  93  LEU   A CA   1 
ATOM   1942 C  C    . LEU   A 1 93  ? 28.454 -3.271  5.462   1.00 9.01  ?  93  LEU   A C    1 
ATOM   1943 O  O    . LEU   A 1 93  ? 27.239 -3.326  5.241   1.00 9.33  ?  93  LEU   A O    1 
ATOM   1944 C  CB   . LEU   A 1 93  ? 28.571 -5.408  6.791   1.00 9.99  ?  93  LEU   A CB   1 
ATOM   1945 C  CG   . LEU   A 1 93  ? 28.954 -6.307  5.620   1.00 10.13 ?  93  LEU   A CG   1 
ATOM   1946 C  CD1  . LEU   A 1 93  ? 30.453 -6.570  5.612   1.00 11.39 ?  93  LEU   A CD1  1 
ATOM   1947 C  CD2  . LEU   A 1 93  ? 28.177 -7.620  5.658   1.00 10.93 ?  93  LEU   A CD2  1 
ATOM   1948 H  H    . LEU   A 1 93  ? 27.896 -3.452  8.191   1.00 11.72 ?  93  LEU   A H    1 
ATOM   1949 H  HA   . LEU   A 1 93  ? 30.015 -3.956  6.602   1.00 11.12 ?  93  LEU   A HA   1 
ATOM   1950 H  HB2  . LEU   A 1 93  ? 28.954 -5.794  7.597   1.00 11.96 ?  93  LEU   A HB2  1 
ATOM   1951 H  HB3  . LEU   A 1 93  ? 27.606 -5.409  6.858   1.00 11.96 ?  93  LEU   A HB3  1 
ATOM   1952 H  HG   . LEU   A 1 93  ? 28.735 -5.859  4.795   1.00 12.14 ?  93  LEU   A HG   1 
ATOM   1953 H  HD11 . LEU   A 1 93  ? 30.669 -7.190  4.898   1.00 13.65 ?  93  LEU   A HD11 1 
ATOM   1954 H  HD12 . LEU   A 1 93  ? 30.929 -5.735  5.479   1.00 13.65 ?  93  LEU   A HD12 1 
ATOM   1955 H  HD13 . LEU   A 1 93  ? 30.717 -6.960  6.469   1.00 13.65 ?  93  LEU   A HD13 1 
ATOM   1956 H  HD21 . LEU   A 1 93  ? 28.446 -8.172  4.902   1.00 13.09 ?  93  LEU   A HD21 1 
ATOM   1957 H  HD22 . LEU   A 1 93  ? 28.373 -8.088  6.487   1.00 13.09 ?  93  LEU   A HD22 1 
ATOM   1958 H  HD23 . LEU   A 1 93  ? 27.227 -7.431  5.603   1.00 13.09 ?  93  LEU   A HD23 1 
ATOM   1959 N  N    . HIS   A 1 94  ? 29.302 -2.583  4.703   1.00 8.93  ?  94  HIS   A N    1 
ATOM   1960 C  CA   . HIS   A 1 94  ? 28.883 -1.907  3.481   1.00 8.84  ?  94  HIS   A CA   1 
ATOM   1961 C  C    . HIS   A 1 94  ? 28.885 -2.934  2.366   1.00 9.14  ?  94  HIS   A C    1 
ATOM   1962 O  O    . HIS   A 1 94  ? 29.948 -3.445  2.011   1.00 10.38 ?  94  HIS   A O    1 
ATOM   1963 C  CB   . HIS   A 1 94  ? 29.840 -0.761  3.150   1.00 9.18  ?  94  HIS   A CB   1 
ATOM   1964 C  CG   . HIS   A 1 94  ? 29.827 0.336   4.161   1.00 9.16  ?  94  HIS   A CG   1 
ATOM   1965 N  ND1  . HIS   A 1 94  ? 28.952 1.399   4.103   1.00 9.34  ?  94  HIS   A ND1  1 
ATOM   1966 C  CD2  . HIS   A 1 94  ? 30.559 0.502   5.284   1.00 9.75  ?  94  HIS   A CD2  1 
ATOM   1967 C  CE1  . HIS   A 1 94  ? 29.163 2.178   5.146   1.00 9.54  ?  94  HIS   A CE1  1 
ATOM   1968 N  NE2  . HIS   A 1 94  ? 30.134 1.659   5.877   1.00 9.68  ?  94  HIS   A NE2  1 
ATOM   1969 H  H    . HIS   A 1 94  ? 30.140 -2.485  4.880   1.00 10.69 ?  94  HIS   A H    1 
ATOM   1970 H  HA   . HIS   A 1 94  ? 27.984 -1.554  3.584   1.00 10.58 ?  94  HIS   A HA   1 
ATOM   1971 H  HB2  . HIS   A 1 94  ? 30.740 -1.108  3.100   1.00 10.99 ?  94  HIS   A HB2  1 
ATOM   1972 H  HB3  . HIS   A 1 94  ? 29.583 -0.376  2.295   1.00 10.99 ?  94  HIS   A HB3  1 
ATOM   1973 H  HD2  . HIS   A 1 94  ? 31.231 -0.053  5.595   1.00 11.68 ?  94  HIS   A HD2  1 
ATOM   1974 H  HE1  . HIS   A 1 94  ? 28.695 2.965   5.331   1.00 11.43 ?  94  HIS   A HE1  1 
ATOM   1975 H  HE2  . HIS   A 1 94  ? 30.441 2.003   6.602   1.00 11.59 ?  94  HIS   A HE2  1 
ATOM   1976 N  N    . VAL   A 1 95  ? 27.711 -3.256  1.825   1.00 8.49  ?  95  VAL   A N    1 
ATOM   1977 C  CA   . VAL   A 1 95  ? 27.568 -4.291  0.803   1.00 8.92  ?  95  VAL   A CA   1 
ATOM   1978 C  C    . VAL   A 1 95  ? 27.020 -3.655  -0.460  1.00 8.54  ?  95  VAL   A C    1 
ATOM   1979 O  O    . VAL   A 1 95  ? 26.019 -2.929  -0.408  1.00 9.50  ?  95  VAL   A O    1 
ATOM   1980 C  CB   . VAL   A 1 95  ? 26.642 -5.436  1.254   1.00 9.69  ?  95  VAL   A CB   1 
ATOM   1981 C  CG1  . VAL   A 1 95  ? 26.544 -6.481  0.160   1.00 10.39 ?  95  VAL   A CG1  1 
ATOM   1982 C  CG2  . VAL   A 1 95  ? 27.145 -6.059  2.538   1.00 9.74  ?  95  VAL   A CG2  1 
ATOM   1983 H  H    . VAL   A 1 95  ? 26.963 -2.882  2.037   1.00 10.17 ?  95  VAL   A H    1 
ATOM   1984 H  HA   . VAL   A 1 95  ? 28.436 -4.667  0.601   1.00 10.67 ?  95  VAL   A HA   1 
ATOM   1985 H  HB   . VAL   A 1 95  ? 25.756 -5.087  1.421   1.00 11.61 ?  95  VAL   A HB   1 
ATOM   1986 H  HG11 . VAL   A 1 95  ? 26.159 -7.294  0.528   1.00 12.45 ?  95  VAL   A HG11 1 
ATOM   1987 H  HG12 . VAL   A 1 95  ? 25.982 -6.146  -0.555  1.00 12.45 ?  95  VAL   A HG12 1 
ATOM   1988 H  HG13 . VAL   A 1 95  ? 27.436 -6.671  -0.181  1.00 12.45 ?  95  VAL   A HG13 1 
ATOM   1989 H  HG21 . VAL   A 1 95  ? 26.582 -6.815  2.764   1.00 11.67 ?  95  VAL   A HG21 1 
ATOM   1990 H  HG22 . VAL   A 1 95  ? 28.061 -6.355  2.408   1.00 11.67 ?  95  VAL   A HG22 1 
ATOM   1991 H  HG23 . VAL   A 1 95  ? 27.109 -5.396  3.245   1.00 11.67 ?  95  VAL   A HG23 1 
ATOM   1992 N  N    . VAL   A 1 96  ? 27.649 -3.947  -1.593  1.00 8.74  ?  96  VAL   A N    1 
ATOM   1993 C  CA   . VAL   A 1 96  ? 27.240 -3.392  -2.878  1.00 9.49  ?  96  VAL   A CA   1 
ATOM   1994 C  C    . VAL   A 1 96  ? 26.434 -4.438  -3.641  1.00 9.69  ?  96  VAL   A C    1 
ATOM   1995 O  O    . VAL   A 1 96  ? 26.989 -5.382  -4.210  1.00 10.73 ?  96  VAL   A O    1 
ATOM   1996 C  CB   . VAL   A 1 96  ? 28.431 -2.910  -3.709  1.00 9.84  ?  96  VAL   A CB   1 
ATOM   1997 C  CG1  . VAL   A 1 96  ? 27.925 -2.278  -4.992  1.00 10.03 ?  96  VAL   A CG1  1 
ATOM   1998 C  CG2  . VAL   A 1 96  ? 29.285 -1.931  -2.920  1.00 10.46 ?  96  VAL   A CG2  1 
ATOM   1999 H  H    . VAL   A 1 96  ? 28.338 -4.466  -1.645  1.00 10.47 ?  96  VAL   A H    1 
ATOM   2000 H  HA   . VAL   A 1 96  ? 26.664 -2.628  -2.721  1.00 11.36 ?  96  VAL   A HA   1 
ATOM   2001 H  HB   . VAL   A 1 96  ? 28.985 -3.666  -3.945  1.00 11.78 ?  96  VAL   A HB   1 
ATOM   2002 H  HG11 . VAL   A 1 96  ? 28.659 -1.799  -5.415  1.00 12.02 ?  96  VAL   A HG11 1 
ATOM   2003 H  HG12 . VAL   A 1 96  ? 27.604 -2.973  -5.584  1.00 12.02 ?  96  VAL   A HG12 1 
ATOM   2004 H  HG13 . VAL   A 1 96  ? 27.210 -1.659  -4.780  1.00 12.02 ?  96  VAL   A HG13 1 
ATOM   2005 H  HG21 . VAL   A 1 96  ? 29.990 -1.588  -3.491  1.00 12.53 ?  96  VAL   A HG21 1 
ATOM   2006 H  HG22 . VAL   A 1 96  ? 28.726 -1.195  -2.614  1.00 12.53 ?  96  VAL   A HG22 1 
ATOM   2007 H  HG23 . VAL   A 1 96  ? 29.670 -2.388  -2.156  1.00 12.53 ?  96  VAL   A HG23 1 
ATOM   2008 N  N    A GLY   A 1 97  ? 25.116 -4.278  -3.653  0.60 9.96  ?  97  GLY   A N    1 
ATOM   2009 N  N    B GLY   A 1 97  ? 25.118 -4.264  -3.689  0.40 9.80  ?  97  GLY   A N    1 
ATOM   2010 C  CA   A GLY   A 1 97  ? 24.287 -5.028  -4.560  0.60 10.60 ?  97  GLY   A CA   1 
ATOM   2011 C  CA   B GLY   A 1 97  ? 24.301 -5.046  -4.583  0.40 10.24 ?  97  GLY   A CA   1 
ATOM   2012 C  C    A GLY   A 1 97  ? 24.271 -4.346  -5.912  0.60 10.43 ?  97  GLY   A C    1 
ATOM   2013 C  C    B GLY   A 1 97  ? 24.316 -4.445  -5.974  0.40 10.49 ?  97  GLY   A C    1 
ATOM   2014 O  O    A GLY   A 1 97  ? 24.578 -3.155  -6.028  0.60 11.25 ?  97  GLY   A O    1 
ATOM   2015 O  O    B GLY   A 1 97  ? 24.557 -3.246  -6.147  0.40 10.82 ?  97  GLY   A O    1 
ATOM   2016 H  H    A GLY   A 1 97  ? 24.684 -3.733  -3.141  0.60 11.93 ?  97  GLY   A H    1 
ATOM   2017 H  H    B GLY   A 1 97  ? 24.679 -3.698  -3.208  0.40 11.74 ?  97  GLY   A H    1 
ATOM   2018 H  HA2  A GLY   A 1 97  ? 24.640 -5.925  -4.655  0.60 12.69 ?  97  GLY   A HA2  1 
ATOM   2019 H  HA2  B GLY   A 1 97  ? 24.644 -5.954  -4.617  0.40 12.26 ?  97  GLY   A HA2  1 
ATOM   2020 H  HA3  A GLY   A 1 97  ? 23.381 -5.081  -4.211  0.60 12.69 ?  97  GLY   A HA3  1 
ATOM   2021 H  HA3  B GLY   A 1 97  ? 23.387 -5.071  -4.258  0.40 12.26 ?  97  GLY   A HA3  1 
ATOM   2022 N  N    A PRO   A 1 98  ? 23.912 -5.077  -6.962  0.60 10.13 ?  98  PRO   A N    1 
ATOM   2023 N  N    B PRO   A 1 98  ? 24.061 -5.260  -6.996  0.40 11.29 ?  98  PRO   A N    1 
ATOM   2024 C  CA   A PRO   A 1 98  ? 23.793 -4.446  -8.280  0.60 10.60 ?  98  PRO   A CA   1 
ATOM   2025 C  CA   B PRO   A 1 98  ? 23.987 -4.718  -8.357  0.40 12.09 ?  98  PRO   A CA   1 
ATOM   2026 C  C    A PRO   A 1 98  ? 22.679 -3.408  -8.299  0.60 10.91 ?  98  PRO   A C    1 
ATOM   2027 C  C    B PRO   A 1 98  ? 22.860 -3.704  -8.479  0.40 12.43 ?  98  PRO   A C    1 
ATOM   2028 O  O    A PRO   A 1 98  ? 21.611 -3.597  -7.712  0.60 10.73 ?  98  PRO   A O    1 
ATOM   2029 O  O    B PRO   A 1 98  ? 21.778 -3.871  -7.912  0.40 12.94 ?  98  PRO   A O    1 
ATOM   2030 C  CB   A PRO   A 1 98  ? 23.482 -5.625  -9.208  0.60 10.95 ?  98  PRO   A CB   1 
ATOM   2031 C  CB   B PRO   A 1 98  ? 23.722 -5.959  -9.218  0.40 11.97 ?  98  PRO   A CB   1 
ATOM   2032 C  CG   A PRO   A 1 98  ? 22.844 -6.654  -8.317  0.60 10.98 ?  98  PRO   A CG   1 
ATOM   2033 C  CG   B PRO   A 1 98  ? 23.113 -6.954  -8.279  0.40 12.24 ?  98  PRO   A CG   1 
ATOM   2034 C  CD   A PRO   A 1 98  ? 23.567 -6.511  -6.998  0.60 10.49 ?  98  PRO   A CD   1 
ATOM   2035 C  CD   B PRO   A 1 98  ? 23.802 -6.709  -6.968  0.40 11.68 ?  98  PRO   A CD   1 
ATOM   2036 H  HA   A PRO   A 1 98  ? 24.631 -4.036  -8.532  0.60 12.70 ?  98  PRO   A HA   1 
ATOM   2037 H  HA   B PRO   A 1 98  ? 24.831 -4.313  -8.611  0.40 14.48 ?  98  PRO   A HA   1 
ATOM   2038 H  HB2  A PRO   A 1 98  ? 22.864 -5.343  -9.897  0.60 13.11 ?  98  PRO   A HB2  1 
ATOM   2039 H  HB2  B PRO   A 1 98  ? 23.103 -5.734  -9.930  0.40 14.34 ?  98  PRO   A HB2  1 
ATOM   2040 H  HB3  A PRO   A 1 98  ? 24.303 -5.965  -9.591  0.60 13.11 ?  98  PRO   A HB3  1 
ATOM   2041 H  HB3  B PRO   A 1 98  ? 24.557 -6.292  -9.578  0.40 14.34 ?  98  PRO   A HB3  1 
ATOM   2042 H  HG2  A PRO   A 1 98  ? 21.901 -6.464  -8.213  0.60 13.15 ?  98  PRO   A HG2  1 
ATOM   2043 H  HG2  B PRO   A 1 98  ? 22.159 -6.790  -8.201  0.40 14.67 ?  98  PRO   A HG2  1 
ATOM   2044 H  HG3  A PRO   A 1 98  ? 22.982 -7.540  -8.687  0.60 13.15 ?  98  PRO   A HG3  1 
ATOM   2045 H  HG3  B PRO   A 1 98  ? 23.284 -7.853  -8.598  0.40 14.67 ?  98  PRO   A HG3  1 
ATOM   2046 H  HD2  A PRO   A 1 98  ? 22.978 -6.745  -6.259  0.60 12.56 ?  98  PRO   A HD2  1 
ATOM   2047 H  HD2  B PRO   A 1 98  ? 23.218 -6.941  -6.229  0.40 13.99 ?  98  PRO   A HD2  1 
ATOM   2048 H  HD3  A PRO   A 1 98  ? 24.375 -7.051  -6.987  0.60 12.56 ?  98  PRO   A HD3  1 
ATOM   2049 H  HD3  B PRO   A 1 98  ? 24.639 -7.202  -6.928  0.40 13.99 ?  98  PRO   A HD3  1 
ATOM   2050 N  N    A ASN   A 1 99  ? 22.944 -2.296  -8.981  0.60 11.84 ?  99  ASN   A N    1 
ATOM   2051 N  N    B ASN   A 1 99  ? 23.127 -2.636  -9.222  0.40 12.77 ?  99  ASN   A N    1 
ATOM   2052 C  CA   A ASN   A 1 99  ? 21.968 -1.228  -9.175  0.60 12.71 ?  99  ASN   A CA   1 
ATOM   2053 C  CA   B ASN   A 1 99  ? 22.134 -1.603  -9.485  0.40 13.59 ?  99  ASN   A CA   1 
ATOM   2054 C  C    A ASN   A 1 99  ? 21.417 -1.359  -10.592 0.60 13.85 ?  99  ASN   A C    1 
ATOM   2055 C  C    B ASN   A 1 99  ? 21.549 -1.859  -10.869 0.40 14.65 ?  99  ASN   A C    1 
ATOM   2056 O  O    A ASN   A 1 99  ? 22.100 -1.025  -11.568 0.60 14.38 ?  99  ASN   A O    1 
ATOM   2057 O  O    B ASN   A 1 99  ? 22.245 -1.740  -11.884 0.40 14.30 ?  99  ASN   A O    1 
ATOM   2058 C  CB   A ASN   A 1 99  ? 22.617 0.138   -8.952  0.60 13.18 ?  99  ASN   A CB   1 
ATOM   2059 C  CB   B ASN   A 1 99  ? 22.750 -0.212  -9.382  0.40 14.84 ?  99  ASN   A CB   1 
ATOM   2060 C  CG   A ASN   A 1 99  ? 21.610 1.281   -8.966  0.60 13.43 ?  99  ASN   A CG   1 
ATOM   2061 C  CG   B ASN   A 1 99  ? 21.720 0.887   -9.508  0.40 16.45 ?  99  ASN   A CG   1 
ATOM   2062 O  OD1  A ASN   A 1 99  ? 20.602 1.229   -9.674  0.60 13.09 ?  99  ASN   A OD1  1 
ATOM   2063 O  OD1  B ASN   A 1 99  ? 20.913 0.886   -10.435 0.40 16.32 ?  99  ASN   A OD1  1 
ATOM   2064 N  ND2  A ASN   A 1 99  ? 21.887 2.323   -8.183  0.60 13.44 ?  99  ASN   A ND2  1 
ATOM   2065 N  ND2  B ASN   A 1 99  ? 21.725 1.820   -8.559  0.40 17.41 ?  99  ASN   A ND2  1 
ATOM   2066 H  H    A ASN   A 1 99  ? 23.705 -2.134  -9.335  0.60 14.19 ?  99  ASN   A H    1 
ATOM   2067 H  H    B ASN   A 1 99  ? 23.892 -2.483  -9.584  0.40 15.30 ?  99  ASN   A H    1 
ATOM   2068 H  HA   A ASN   A 1 99  ? 21.238 -1.334  -8.537  0.60 15.22 ?  99  ASN   A HA   1 
ATOM   2069 H  HA   B ASN   A 1 99  ? 21.418 -1.673  -8.829  0.40 16.28 ?  99  ASN   A HA   1 
ATOM   2070 H  HB2  A ASN   A 1 99  ? 23.066 0.140   -8.091  0.60 15.79 ?  99  ASN   A HB2  1 
ATOM   2071 H  HB2  B ASN   A 1 99  ? 23.186 -0.122  -8.521  0.40 17.79 ?  99  ASN   A HB2  1 
ATOM   2072 H  HB3  A ASN   A 1 99  ? 23.261 0.296   -9.660  0.60 15.79 ?  99  ASN   A HB3  1 
ATOM   2073 H  HB3  B ASN   A 1 99  ? 23.392 -0.106  -10.095 0.40 17.79 ?  99  ASN   A HB3  1 
ATOM   2074 H  HD21 A ASN   A 1 99  ? 21.352 2.994   -8.155  0.60 16.10 ?  99  ASN   A HD21 1 
ATOM   2075 H  HD21 B ASN   A 1 99  ? 21.156 2.465   -8.579  0.40 20.87 ?  99  ASN   A HD21 1 
ATOM   2076 H  HD22 A ASN   A 1 99  ? 22.602 2.321   -7.703  0.60 16.10 ?  99  ASN   A HD22 1 
ATOM   2077 H  HD22 B ASN   A 1 99  ? 22.298 1.776   -7.916  0.40 20.87 ?  99  ASN   A HD22 1 
ATOM   2078 N  N    A VAL   A 1 100 ? 20.179 -1.857  -10.696 0.60 14.49 ?  100 VAL   A N    1 
ATOM   2079 N  N    B VAL   A 1 100 ? 20.265 -2.212  -10.897 0.40 16.59 ?  100 VAL   A N    1 
ATOM   2080 C  CA   A VAL   A 1 100 ? 19.555 -2.074  -11.999 0.60 15.68 ?  100 VAL   A CA   1 
ATOM   2081 C  CA   B VAL   A 1 100 ? 19.614 -2.572  -12.151 0.40 19.09 ?  100 VAL   A CA   1 
ATOM   2082 C  C    A VAL   A 1 100 ? 19.428 -0.764  -12.767 0.60 15.98 ?  100 VAL   A C    1 
ATOM   2083 C  C    B VAL   A 1 100 ? 19.523 -1.366  -13.067 0.40 20.42 ?  100 VAL   A C    1 
ATOM   2084 O  O    A VAL   A 1 100 ? 19.497 -0.745  -14.002 0.60 16.72 ?  100 VAL   A O    1 
ATOM   2085 O  O    B VAL   A 1 100 ? 19.579 -1.505  -14.295 0.40 20.78 ?  100 VAL   A O    1 
ATOM   2086 C  CB   A VAL   A 1 100 ? 18.202 -2.799  -11.822 0.60 17.08 ?  100 VAL   A CB   1 
ATOM   2087 C  CB   B VAL   A 1 100 ? 18.227 -3.170  -11.868 0.40 20.75 ?  100 VAL   A CB   1 
ATOM   2088 C  CG1  A VAL   A 1 100 ? 17.461 -2.918  -13.148 0.60 17.30 ?  100 VAL   A CG1  1 
ATOM   2089 C  CG1  B VAL   A 1 100 ? 17.783 -4.040  -13.028 0.40 21.28 ?  100 VAL   A CG1  1 
ATOM   2090 C  CG2  A VAL   A 1 100 ? 18.424 -4.183  -11.219 0.60 17.24 ?  100 VAL   A CG2  1 
ATOM   2091 C  CG2  B VAL   A 1 100 ? 18.257 -3.957  -10.577 0.40 21.53 ?  100 VAL   A CG2  1 
ATOM   2092 H  H    A VAL   A 1 100 ? 19.684 -2.081  -10.022 0.60 17.36 ?  100 VAL   A H    1 
ATOM   2093 H  H    B VAL   A 1 100 ? 19.760 -2.241  -10.201 0.40 19.89 ?  100 VAL   A H    1 
ATOM   2094 H  HA   A VAL   A 1 100 ? 20.126 -2.660  -12.515 0.60 18.79 ?  100 VAL   A HA   1 
ATOM   2095 H  HA   B VAL   A 1 100 ? 20.144 -3.247  -12.603 0.40 22.89 ?  100 VAL   A HA   1 
ATOM   2096 H  HB   A VAL   A 1 100 ? 17.644 -2.296  -11.209 0.60 20.48 ?  100 VAL   A HB   1 
ATOM   2097 H  HB   B VAL   A 1 100 ? 17.586 -2.445  -11.769 0.40 24.87 ?  100 VAL   A HB   1 
ATOM   2098 H  HG11 A VAL   A 1 100 ? 16.726 -3.544  -13.044 0.60 20.73 ?  100 VAL   A HG11 1 
ATOM   2099 H  HG11 B VAL   A 1 100 ? 16.898 -4.388  -12.838 0.40 25.51 ?  100 VAL   A HG11 1 
ATOM   2100 H  HG12 A VAL   A 1 100 ? 17.119 -2.047  -13.399 0.60 20.73 ?  100 VAL   A HG12 1 
ATOM   2101 H  HG12 B VAL   A 1 100 ? 17.764 -3.506  -13.836 0.40 25.51 ?  100 VAL   A HG12 1 
ATOM   2102 H  HG13 A VAL   A 1 100 ? 18.076 -3.243  -13.825 0.60 20.73 ?  100 VAL   A HG13 1 
ATOM   2103 H  HG13 B VAL   A 1 100 ? 18.413 -4.772  -13.128 0.40 25.51 ?  100 VAL   A HG13 1 
ATOM   2104 H  HG21 A VAL   A 1 100 ? 17.571 -4.639  -11.148 0.60 20.66 ?  100 VAL   A HG21 1 
ATOM   2105 H  HG21 B VAL   A 1 100 ? 17.531 -4.588  -10.585 0.40 25.81 ?  100 VAL   A HG21 1 
ATOM   2106 H  HG22 A VAL   A 1 100 ? 19.021 -4.686  -11.796 0.60 20.66 ?  100 VAL   A HG22 1 
ATOM   2107 H  HG22 B VAL   A 1 100 ? 19.107 -4.422  -10.515 0.40 25.81 ?  100 VAL   A HG22 1 
ATOM   2108 H  HG23 A VAL   A 1 100 ? 18.821 -4.086  -10.339 0.60 20.66 ?  100 VAL   A HG23 1 
ATOM   2109 H  HG23 B VAL   A 1 100 ? 18.159 -3.343  -9.831  0.40 25.81 ?  100 VAL   A HG23 1 
ATOM   2110 N  N    A ASN   A 1 101 ? 19.253 0.349   -12.063 0.60 17.03 ?  101 ASN   A N    1 
ATOM   2111 N  N    B ASN   A 1 101 ? 19.370 -0.170  -12.494 0.40 21.63 ?  101 ASN   A N    1 
ATOM   2112 C  CA   A ASN   A 1 101 ? 19.183 1.630   -12.752 0.60 18.39 ?  101 ASN   A CA   1 
ATOM   2113 C  CA   B ASN   A 1 101 ? 19.335 1.051   -13.286 0.40 23.06 ?  101 ASN   A CA   1 
ATOM   2114 C  C    A ASN   A 1 101 ? 20.534 2.080   -13.305 0.60 20.79 ?  101 ASN   A C    1 
ATOM   2115 C  C    B ASN   A 1 101 ? 20.704 1.429   -13.832 0.40 24.45 ?  101 ASN   A C    1 
ATOM   2116 O  O    A ASN   A 1 101 ? 20.599 3.141   -13.938 0.60 22.38 ?  101 ASN   A O    1 
ATOM   2117 O  O    B ASN   A 1 101 ? 20.780 2.281   -14.724 0.40 24.69 ?  101 ASN   A O    1 
ATOM   2118 C  CB   A ASN   A 1 101 ? 18.555 2.670   -11.828 0.60 17.94 ?  101 ASN   A CB   1 
ATOM   2119 C  CB   B ASN   A 1 101 ? 18.739 2.192   -12.454 0.40 23.06 ?  101 ASN   A CB   1 
ATOM   2120 C  CG   A ASN   A 1 101 ? 17.197 2.222   -11.304 0.60 17.25 ?  101 ASN   A CG   1 
ATOM   2121 C  CG   B ASN   A 1 101 ? 17.391 1.833   -11.855 0.40 23.27 ?  101 ASN   A CG   1 
ATOM   2122 O  OD1  A ASN   A 1 101 ? 16.367 1.704   -12.059 0.60 17.19 ?  101 ASN   A OD1  1 
ATOM   2123 O  OD1  B ASN   A 1 101 ? 16.619 1.076   -12.443 0.40 23.52 ?  101 ASN   A OD1  1 
ATOM   2124 N  ND2  A ASN   A 1 101 ? 16.976 2.392   -10.008 0.60 16.43 ?  101 ASN   A ND2  1 
ATOM   2125 N  ND2  B ASN   A 1 101 ? 17.104 2.374   -10.676 0.40 23.30 ?  101 ASN   A ND2  1 
ATOM   2126 H  H    A ASN   A 1 101 ? 19.167 0.389   -11.210 0.60 20.41 ?  101 ASN   A H    1 
ATOM   2127 H  H    B ASN   A 1 101 ? 19.285 -0.041  -11.645 0.40 25.94 ?  101 ASN   A H    1 
ATOM   2128 H  HA   A ASN   A 1 101 ? 18.589 1.529   -13.510 0.60 22.04 ?  101 ASN   A HA   1 
ATOM   2129 H  HA   B ASN   A 1 101 ? 18.760 0.915   -14.047 0.40 27.65 ?  101 ASN   A HA   1 
ATOM   2130 H  HB2  A ASN   A 1 101 ? 19.142 2.822   -11.073 0.60 21.50 ?  101 ASN   A HB2  1 
ATOM   2131 H  HB2  B ASN   A 1 101 ? 19.338 2.410   -11.724 0.40 27.64 ?  101 ASN   A HB2  1 
ATOM   2132 H  HB3  A ASN   A 1 101 ? 18.432 3.499   -12.325 0.60 21.50 ?  101 ASN   A HB3  1 
ATOM   2133 H  HB3  B ASN   A 1 101 ? 18.610 2.970   -13.021 0.40 27.64 ?  101 ASN   A HB3  1 
ATOM   2134 H  HD21 A ASN   A 1 101 ? 16.225 2.152   -9.666  0.60 19.70 ?  101 ASN   A HD21 1 
ATOM   2135 H  HD21 B ASN   A 1 101 ? 16.351 2.201   -10.296 0.40 27.93 ?  101 ASN   A HD21 1 
ATOM   2136 H  HD22 A ASN   A 1 101 ? 17.578 2.754   -9.511  0.60 19.70 ?  101 ASN   A HD22 1 
ATOM   2137 H  HD22 B ASN   A 1 101 ? 17.666 2.901   -10.296 0.40 27.93 ?  101 ASN   A HD22 1 
ATOM   2138 N  N    A LYS   A 1 102 ? 21.597 1.296   -13.093 0.60 22.99 ?  102 LYS   A N    1 
ATOM   2139 N  N    B LYS   A 1 102 ? 21.774 0.806   -13.337 0.40 25.71 ?  102 LYS   A N    1 
ATOM   2140 C  CA   A LYS   A 1 102 ? 22.874 1.474   -13.773 0.60 25.08 ?  102 LYS   A CA   1 
ATOM   2141 C  CA   B LYS   A 1 102 ? 23.119 1.015   -13.855 0.40 26.59 ?  102 LYS   A CA   1 
ATOM   2142 C  C    A LYS   A 1 102 ? 23.157 0.379   -14.793 0.60 25.19 ?  102 LYS   A C    1 
ATOM   2143 C  C    B LYS   A 1 102 ? 23.543 -0.086  -14.821 0.40 26.37 ?  102 LYS   A C    1 
ATOM   2144 O  O    A LYS   A 1 102 ? 24.206 0.420   -15.445 0.60 25.67 ?  102 LYS   A O    1 
ATOM   2145 O  O    B LYS   A 1 102 ? 24.705 -0.119  -15.237 0.40 26.23 ?  102 LYS   A O    1 
ATOM   2146 C  CB   A LYS   A 1 102 ? 24.026 1.512   -12.760 0.60 27.16 ?  102 LYS   A CB   1 
ATOM   2147 C  CB   B LYS   A 1 102 ? 24.128 1.113   -12.705 0.40 27.85 ?  102 LYS   A CB   1 
ATOM   2148 C  CG   A LYS   A 1 102 ? 23.946 2.631   -11.740 0.60 28.97 ?  102 LYS   A CG   1 
ATOM   2149 C  CG   B LYS   A 1 102 ? 23.982 2.362   -11.843 0.40 28.84 ?  102 LYS   A CG   1 
ATOM   2150 C  CD   A LYS   A 1 102 ? 25.141 2.582   -10.798 0.60 30.57 ?  102 LYS   A CD   1 
ATOM   2151 C  CD   B LYS   A 1 102 ? 24.951 2.358   -10.663 0.40 29.78 ?  102 LYS   A CD   1 
ATOM   2152 C  CE   A LYS   A 1 102 ? 25.077 3.679   -9.749  0.60 31.88 ?  102 LYS   A CE   1 
ATOM   2153 C  CE   B LYS   A 1 102 ? 24.784 3.607   -9.805  0.40 30.65 ?  102 LYS   A CE   1 
ATOM   2154 N  NZ   A LYS   A 1 102 ? 26.215 3.592   -8.789  0.60 32.37 ?  102 LYS   A NZ   1 
ATOM   2155 N  NZ   B LYS   A 1 102 ? 25.552 3.531   -8.529  0.40 30.99 ?  102 LYS   A NZ   1 
ATOM   2156 H  H    A LYS   A 1 102 ? 21.601 0.635   -12.541 0.60 27.56 ?  102 LYS   A H    1 
ATOM   2157 H  H    B LYS   A 1 102 ? 21.739 0.234   -12.694 0.40 30.83 ?  102 LYS   A H    1 
ATOM   2158 H  HA   A LYS   A 1 102 ? 22.867 2.314   -14.249 0.60 30.07 ?  102 LYS   A HA   1 
ATOM   2159 H  HA   B LYS   A 1 102 ? 23.137 1.862   -14.329 0.40 31.88 ?  102 LYS   A HA   1 
ATOM   2160 H  HB2  A LYS   A 1 102 ? 24.040 0.673   -12.274 0.60 32.56 ?  102 LYS   A HB2  1 
ATOM   2161 H  HB2  B LYS   A 1 102 ? 24.023 0.340   -12.130 0.40 33.40 ?  102 LYS   A HB2  1 
ATOM   2162 H  HB3  A LYS   A 1 102 ? 24.861 1.619   -13.245 0.60 32.56 ?  102 LYS   A HB3  1 
ATOM   2163 H  HB3  B LYS   A 1 102 ? 25.023 1.120   -13.079 0.40 33.40 ?  102 LYS   A HB3  1 
ATOM   2164 H  HG2  A LYS   A 1 102 ? 23.949 3.486   -12.198 0.60 34.73 ?  102 LYS   A HG2  1 
ATOM   2165 H  HG2  B LYS   A 1 102 ? 24.169 3.146   -12.383 0.40 34.58 ?  102 LYS   A HG2  1 
ATOM   2166 H  HG3  A LYS   A 1 102 ? 23.136 2.530   -11.216 0.60 34.73 ?  102 LYS   A HG3  1 
ATOM   2167 H  HG3  B LYS   A 1 102 ? 23.079 2.404   -11.492 0.40 34.58 ?  102 LYS   A HG3  1 
ATOM   2168 H  HD2  A LYS   A 1 102 ? 25.153 1.725   -10.342 0.60 36.65 ?  102 LYS   A HD2  1 
ATOM   2169 H  HD2  B LYS   A 1 102 ? 24.781 1.583   -10.105 0.40 35.71 ?  102 LYS   A HD2  1 
ATOM   2170 H  HD3  A LYS   A 1 102 ? 25.956 2.699   -11.311 0.60 36.65 ?  102 LYS   A HD3  1 
ATOM   2171 H  HD3  B LYS   A 1 102 ? 25.862 2.337   -10.996 0.40 35.71 ?  102 LYS   A HD3  1 
ATOM   2172 H  HE2  A LYS   A 1 102 ? 25.114 4.543   -10.189 0.60 38.23 ?  102 LYS   A HE2  1 
ATOM   2173 H  HE2  B LYS   A 1 102 ? 25.103 4.377   -10.302 0.40 36.75 ?  102 LYS   A HE2  1 
ATOM   2174 H  HE3  A LYS   A 1 102 ? 24.250 3.594   -9.249  0.60 38.23 ?  102 LYS   A HE3  1 
ATOM   2175 H  HE3  B LYS   A 1 102 ? 23.846 3.719   -9.586  0.40 36.75 ?  102 LYS   A HE3  1 
ATOM   2176 H  HZ1  A LYS   A 1 102 ? 26.155 4.244   -8.187  0.60 38.82 ?  102 LYS   A HZ1  1 
ATOM   2177 H  HZ1  B LYS   A 1 102 ? 25.315 4.200   -7.990  0.40 37.16 ?  102 LYS   A HZ1  1 
ATOM   2178 H  HZ2  A LYS   A 1 102 ? 26.199 2.807   -8.370  0.60 38.82 ?  102 LYS   A HZ2  1 
ATOM   2179 H  HZ2  B LYS   A 1 102 ? 25.384 2.758   -8.121  0.40 37.16 ?  102 LYS   A HZ2  1 
ATOM   2180 H  HZ3  A LYS   A 1 102 ? 26.987 3.672   -9.226  0.60 38.82 ?  102 LYS   A HZ3  1 
ATOM   2181 H  HZ3  B LYS   A 1 102 ? 26.424 3.586   -8.694  0.40 37.16 ?  102 LYS   A HZ3  1 
ATOM   2182 N  N    A GLY   A 1 103 ? 22.266 -0.601  -14.942 0.60 25.76 ?  103 GLY   A N    1 
ATOM   2183 N  N    B GLY   A 1 103 ? 22.634 -0.993  -15.175 0.40 26.22 ?  103 GLY   A N    1 
ATOM   2184 C  CA   A GLY   A 1 103 ? 22.484 -1.690  -15.876 0.60 25.81 ?  103 GLY   A CA   1 
ATOM   2185 C  CA   B GLY   A 1 103 ? 22.965 -2.066  -16.091 0.40 25.68 ?  103 GLY   A CA   1 
ATOM   2186 C  C    A GLY   A 1 103 ? 23.321 -2.831  -15.346 0.60 25.84 ?  103 GLY   A C    1 
ATOM   2187 C  C    B GLY   A 1 103 ? 23.747 -3.207  -15.482 0.40 24.90 ?  103 GLY   A C    1 
ATOM   2188 O  O    A GLY   A 1 103 ? 23.834 -3.625  -16.140 0.60 26.78 ?  103 GLY   A O    1 
ATOM   2189 O  O    B GLY   A 1 103 ? 24.344 -3.998  -16.219 0.40 25.46 ?  103 GLY   A O    1 
ATOM   2190 H  H    A GLY   A 1 103 ? 21.527 -0.657  -14.513 0.60 30.89 ?  103 GLY   A H    1 
ATOM   2191 H  H    B GLY   A 1 103 ? 21.820 -1.006  -14.896 0.40 31.44 ?  103 GLY   A H    1 
ATOM   2192 H  HA2  A GLY   A 1 103 ? 21.625 -2.052  -16.147 0.60 30.95 ?  103 GLY   A HA2  1 
ATOM   2193 H  HA2  B GLY   A 1 103 ? 22.147 -2.423  -16.468 0.40 30.80 ?  103 GLY   A HA2  1 
ATOM   2194 H  HA3  A GLY   A 1 103 ? 22.925 -1.345  -16.669 0.60 30.95 ?  103 GLY   A HA3  1 
ATOM   2195 H  HA3  B GLY   A 1 103 ? 23.495 -1.696  -16.816 0.40 30.80 ?  103 GLY   A HA3  1 
ATOM   2196 N  N    A GLU   A 1 104 ? 23.466 -2.950  -14.030 0.60 24.27 ?  104 GLU   A N    1 
ATOM   2197 N  N    B GLU   A 1 104 ? 23.756 -3.326  -14.160 0.40 23.07 ?  104 GLU   A N    1 
ATOM   2198 C  CA   A GLU   A 1 104 ? 24.357 -3.947  -13.452 0.60 22.94 ?  104 GLU   A CA   1 
ATOM   2199 C  CA   B GLU   A 1 104 ? 24.606 -4.294  -13.484 0.40 21.43 ?  104 GLU   A CA   1 
ATOM   2200 C  C    A GLU   A 1 104 ? 23.681 -5.313  -13.355 0.60 23.66 ?  104 GLU   A C    1 
ATOM   2201 C  C    B GLU   A 1 104 ? 23.899 -5.640  -13.332 0.40 21.00 ?  104 GLU   A C    1 
ATOM   2202 O  O    A GLU   A 1 104 ? 22.459 -5.424  -13.214 0.60 24.10 ?  104 GLU   A O    1 
ATOM   2203 O  O    B GLU   A 1 104 ? 22.680 -5.713  -13.145 0.40 21.22 ?  104 GLU   A O    1 
ATOM   2204 C  CB   A GLU   A 1 104 ? 24.869 -3.467  -12.091 0.60 21.03 ?  104 GLU   A CB   1 
ATOM   2205 C  CB   B GLU   A 1 104 ? 25.056 -3.733  -12.132 0.40 20.81 ?  104 GLU   A CB   1 
ATOM   2206 C  CG   A GLU   A 1 104 ? 25.865 -2.314  -12.243 0.60 20.04 ?  104 GLU   A CG   1 
ATOM   2207 C  CG   B GLU   A 1 104 ? 25.794 -2.397  -12.281 0.40 21.01 ?  104 GLU   A CG   1 
ATOM   2208 C  CD   A GLU   A 1 104 ? 26.212 -1.583  -10.961 0.60 18.64 ?  104 GLU   A CD   1 
ATOM   2209 C  CD   B GLU   A 1 104 ? 26.067 -1.688  -10.968 0.40 21.07 ?  104 GLU   A CD   1 
ATOM   2210 O  OE1  A GLU   A 1 104 ? 25.581 -1.834  -9.914  0.60 16.77 ?  104 GLU   A OE1  1 
ATOM   2211 O  OE1  B GLU   A 1 104 ? 25.645 -2.185  -9.905  0.40 20.85 ?  104 GLU   A OE1  1 
ATOM   2212 O  OE2  A GLU   A 1 104 ? 27.130 -0.731  -11.021 0.60 19.46 -1 104 GLU   A OE2  1 
ATOM   2213 O  OE2  B GLU   A 1 104 ? 26.703 -0.613  -11.008 0.40 21.44 -1 104 GLU   A OE2  1 
ATOM   2214 H  H    A GLU   A 1 104 ? 23.062 -2.461  -13.454 0.60 29.10 ?  104 GLU   A H    1 
ATOM   2215 H  H    B GLU   A 1 104 ? 23.278 -2.846  -13.629 0.40 27.66 ?  104 GLU   A H    1 
ATOM   2216 H  HA   A GLU   A 1 104 ? 25.125 -4.043  -14.033 0.60 27.51 ?  104 GLU   A HA   1 
ATOM   2217 H  HA   B GLU   A 1 104 ? 25.402 -4.432  -14.021 0.40 25.69 ?  104 GLU   A HA   1 
ATOM   2218 H  HB2  A GLU   A 1 104 ? 24.120 -3.157  -11.558 0.60 25.22 ?  104 GLU   A HB2  1 
ATOM   2219 H  HB2  B GLU   A 1 104 ? 24.281 -3.587  -11.570 0.40 24.95 ?  104 GLU   A HB2  1 
ATOM   2220 H  HB3  A GLU   A 1 104 ? 25.318 -4.201  -11.643 0.60 25.22 ?  104 GLU   A HB3  1 
ATOM   2221 H  HB3  B GLU   A 1 104 ? 25.663 -4.364  -11.712 0.40 24.95 ?  104 GLU   A HB3  1 
ATOM   2222 H  HG2  A GLU   A 1 104 ? 26.691 -2.666  -12.600 0.60 24.02 ?  104 GLU   A HG2  1 
ATOM   2223 H  HG2  B GLU   A 1 104 ? 26.646 -2.554  -12.718 0.40 25.19 ?  104 GLU   A HG2  1 
ATOM   2224 H  HG3  A GLU   A 1 104 ? 25.490 -1.663  -12.854 0.60 24.02 ?  104 GLU   A HG3  1 
ATOM   2225 H  HG3  B GLU   A 1 104 ? 25.257 -1.796  -12.822 0.40 25.19 ?  104 GLU   A HG3  1 
ATOM   2226 N  N    A ASP   A 1 105 ? 24.503 -6.359  -13.435 0.60 24.29 ?  105 ASP   A N    1 
ATOM   2227 N  N    B ASP   A 1 105 ? 24.689 -6.710  -13.419 0.40 21.07 ?  105 ASP   A N    1 
ATOM   2228 C  CA   A ASP   A 1 105 ? 24.018 -7.729  -13.563 0.60 25.34 ?  105 ASP   A CA   1 
ATOM   2229 C  CA   B ASP   A 1 105 ? 24.165 -8.070  -13.508 0.40 21.42 ?  105 ASP   A CA   1 
ATOM   2230 C  C    A ASP   A 1 105 ? 23.333 -8.175  -12.276 0.60 23.45 ?  105 ASP   A C    1 
ATOM   2231 C  C    B ASP   A 1 105 ? 23.451 -8.460  -12.218 0.40 19.91 ?  105 ASP   A C    1 
ATOM   2232 O  O    A ASP   A 1 105 ? 23.955 -8.197  -11.211 0.60 22.11 ?  105 ASP   A O    1 
ATOM   2233 O  O    B ASP   A 1 105 ? 24.072 -8.536  -11.154 0.40 17.87 ?  105 ASP   A O    1 
ATOM   2234 C  CB   A ASP   A 1 105 ? 25.201 -8.644  -13.872 0.60 28.01 ?  105 ASP   A CB   1 
ATOM   2235 C  CB   B ASP   A 1 105 ? 25.331 -9.019  -13.781 0.40 23.29 ?  105 ASP   A CB   1 
ATOM   2236 C  CG   A ASP   A 1 105 ? 24.778 -10.062 -14.177 0.60 30.31 ?  105 ASP   A CG   1 
ATOM   2237 C  CG   B ASP   A 1 105 ? 24.916 -10.477 -13.829 0.40 25.00 ?  105 ASP   A CG   1 
ATOM   2238 O  OD1  A ASP   A 1 105 ? 23.559 -10.309 -14.278 0.60 30.85 ?  105 ASP   A OD1  1 
ATOM   2239 O  OD1  B ASP   A 1 105 ? 23.705 -10.764 -13.927 0.40 25.03 ?  105 ASP   A OD1  1 
ATOM   2240 O  OD2  A ASP   A 1 105 ? 25.669 -10.928 -14.323 0.60 31.55 -1 105 ASP   A OD2  1 
ATOM   2241 O  OD2  B ASP   A 1 105 ? 25.818 -11.341 -13.762 0.40 26.28 -1 105 ASP   A OD2  1 
ATOM   2242 H  H    A ASP   A 1 105 ? 25.362 -6.298  -13.419 0.60 29.12 ?  105 ASP   A H    1 
ATOM   2243 H  H    B ASP   A 1 105 ? 25.549 -6.669  -13.431 0.40 25.26 ?  105 ASP   A H    1 
ATOM   2244 H  HA   A ASP   A 1 105 ? 23.382 -7.788  -14.291 0.60 30.38 ?  105 ASP   A HA   1 
ATOM   2245 H  HA   B ASP   A 1 105 ? 23.531 -8.125  -14.237 0.40 25.68 ?  105 ASP   A HA   1 
ATOM   2246 H  HB2  A ASP   A 1 105 ? 25.670 -8.307  -14.651 0.60 33.58 ?  105 ASP   A HB2  1 
ATOM   2247 H  HB2  B ASP   A 1 105 ? 25.728 -8.785  -14.634 0.40 27.93 ?  105 ASP   A HB2  1 
ATOM   2248 H  HB3  A ASP   A 1 105 ? 25.800 -8.658  -13.106 0.60 33.58 ?  105 ASP   A HB3  1 
ATOM   2249 H  HB3  B ASP   A 1 105 ? 25.984 -8.925  -13.073 0.40 27.93 ?  105 ASP   A HB3  1 
ATOM   2250 N  N    A ILE   A 1 106 ? 22.059 -8.564  -12.380 0.60 22.94 ?  106 ILE   A N    1 
ATOM   2251 N  N    B ILE   A 1 106 ? 22.147 -8.732  -12.315 0.40 20.60 ?  106 ILE   A N    1 
ATOM   2252 C  CA   A ILE   A 1 106 ? 21.303 -8.969  -11.200 0.60 22.11 ?  106 ILE   A CA   1 
ATOM   2253 C  CA   B ILE   A 1 106 ? 21.372 -9.118  -11.141 0.40 21.14 ?  106 ILE   A CA   1 
ATOM   2254 C  C    A ILE   A 1 106 ? 21.842 -10.257 -10.593 0.60 20.63 ?  106 ILE   A C    1 
ATOM   2255 C  C    B ILE   A 1 106 ? 21.891 -10.413 -10.534 0.40 20.80 ?  106 ILE   A C    1 
ATOM   2256 O  O    A ILE   A 1 106 ? 21.615 -10.516 -9.406  0.60 19.88 ?  106 ILE   A O    1 
ATOM   2257 O  O    B ILE   A 1 106 ? 21.692 -10.656 -9.339  0.40 20.50 ?  106 ILE   A O    1 
ATOM   2258 C  CB   A ILE   A 1 106 ? 19.799 -9.071  -11.527 0.60 23.45 ?  106 ILE   A CB   1 
ATOM   2259 C  CB   B ILE   A 1 106 ? 19.863 -9.186  -11.476 0.40 22.46 ?  106 ILE   A CB   1 
ATOM   2260 C  CG1  A ILE   A 1 106 ? 18.964 -9.118  -10.244 0.60 23.99 ?  106 ILE   A CG1  1 
ATOM   2261 C  CG1  B ILE   A 1 106 ? 19.024 -9.296  -10.199 0.40 23.03 ?  106 ILE   A CG1  1 
ATOM   2262 C  CG2  A ILE   A 1 106 ? 19.516 -10.299 -12.377 0.60 24.05 ?  106 ILE   A CG2  1 
ATOM   2263 C  CG2  B ILE   A 1 106 ? 19.568 -10.364 -12.385 0.40 22.92 ?  106 ILE   A CG2  1 
ATOM   2264 C  CD1  A ILE   A 1 106 ? 19.110 -7.890  -9.371  0.60 24.46 ?  106 ILE   A CD1  1 
ATOM   2265 C  CD1  B ILE   A 1 106 ? 19.147 -8.104  -9.273  0.40 23.31 ?  106 ILE   A CD1  1 
ATOM   2266 H  H    A ILE   A 1 106 ? 21.619 -8.598  -13.114 0.60 27.50 ?  106 ILE   A H    1 
ATOM   2267 H  H    B ILE   A 1 106 ? 21.698 -8.696  -13.042 0.40 24.69 ?  106 ILE   A H    1 
ATOM   2268 H  HA   A ILE   A 1 106 ? 21.412 -8.282  -10.532 0.60 26.50 ?  106 ILE   A HA   1 
ATOM   2269 H  HA   B ILE   A 1 106 ? 21.488 -8.434  -10.470 0.40 25.35 ?  106 ILE   A HA   1 
ATOM   2270 H  HB   A ILE   A 1 106 ? 19.542 -8.284  -12.031 0.60 28.11 ?  106 ILE   A HB   1 
ATOM   2271 H  HB   B ILE   A 1 106 ? 19.613 -8.368  -11.937 0.40 26.93 ?  106 ILE   A HB   1 
ATOM   2272 H  HG12 A ILE   A 1 106 ? 18.028 -9.197  -10.483 0.60 28.77 ?  106 ILE   A HG12 1 
ATOM   2273 H  HG12 B ILE   A 1 106 ? 18.090 -9.378  -10.447 0.40 27.61 ?  106 ILE   A HG12 1 
ATOM   2274 H  HG13 A ILE   A 1 106 ? 19.235 -9.887  -9.720  0.60 28.77 ?  106 ILE   A HG13 1 
ATOM   2275 H  HG13 B ILE   A 1 106 ? 19.302 -10.083 -9.707  0.40 27.61 ?  106 ILE   A HG13 1 
ATOM   2276 H  HG21 A ILE   A 1 106 ? 18.625 -10.221 -12.752 0.60 28.83 ?  106 ILE   A HG21 1 
ATOM   2277 H  HG21 B ILE   A 1 106 ? 18.665 -10.277 -12.727 0.40 27.48 ?  106 ILE   A HG21 1 
ATOM   2278 H  HG22 A ILE   A 1 106 ? 20.173 -10.344 -13.088 0.60 28.83 ?  106 ILE   A HG22 1 
ATOM   2279 H  HG22 B ILE   A 1 106 ? 20.203 -10.360 -13.116 0.40 27.48 ?  106 ILE   A HG22 1 
ATOM   2280 H  HG23 A ILE   A 1 106 ? 19.574 -11.090 -11.820 0.60 28.83 ?  106 ILE   A HG23 1 
ATOM   2281 H  HG23 B ILE   A 1 106 ? 19.652 -11.184 -11.875 0.40 27.48 ?  106 ILE   A HG23 1 
ATOM   2282 H  HD11 A ILE   A 1 106 ? 18.371 -7.859  -8.747  0.60 29.32 ?  106 ILE   A HD11 1 
ATOM   2283 H  HD11 B ILE   A 1 106 ? 18.432 -8.139  -8.619  0.40 27.95 ?  106 ILE   A HD11 1 
ATOM   2284 H  HD12 A ILE   A 1 106 ? 19.950 -7.944  -8.887  0.60 29.32 ?  106 ILE   A HD12 1 
ATOM   2285 H  HD12 B ILE   A 1 106 ? 20.007 -8.138  -8.824  0.40 27.95 ?  106 ILE   A HD12 1 
ATOM   2286 H  HD13 A ILE   A 1 106 ? 19.102 -7.101  -9.935  0.60 29.32 ?  106 ILE   A HD13 1 
ATOM   2287 H  HD13 B ILE   A 1 106 ? 19.077 -7.290  -9.795  0.40 27.95 ?  106 ILE   A HD13 1 
ATOM   2288 N  N    A GLN   A 1 107 ? 22.565 -11.069 -11.373 0.60 21.31 ?  107 GLN   A N    1 
ATOM   2289 N  N    B GLN   A 1 107 ? 22.568 -11.250 -11.328 0.40 21.22 ?  107 GLN   A N    1 
ATOM   2290 C  CA   A GLN   A 1 107 ? 23.143 -12.299 -10.837 0.60 22.80 ?  107 GLN   A CA   1 
ATOM   2291 C  CA   B GLN   A 1 107 ? 23.217 -12.432 -10.776 0.40 22.00 ?  107 GLN   A CA   1 
ATOM   2292 C  C    A GLN   A 1 107 ? 24.111 -12.009 -9.697  0.60 20.48 ?  107 GLN   A C    1 
ATOM   2293 C  C    B GLN   A 1 107 ? 24.254 -12.073 -9.722  0.40 20.02 ?  107 GLN   A C    1 
ATOM   2294 O  O    A GLN   A 1 107 ? 24.294 -12.847 -8.806  0.60 21.37 ?  107 GLN   A O    1 
ATOM   2295 O  O    B GLN   A 1 107 ? 24.635 -12.935 -8.923  0.40 20.97 ?  107 GLN   A O    1 
ATOM   2296 C  CB   A GLN   A 1 107 ? 23.846 -13.072 -11.957 0.60 26.75 ?  107 GLN   A CB   1 
ATOM   2297 C  CB   B GLN   A 1 107 ? 23.862 -13.255 -11.895 0.40 24.60 ?  107 GLN   A CB   1 
ATOM   2298 C  CG   A GLN   A 1 107 ? 22.987 -13.276 -13.200 0.60 30.63 ?  107 GLN   A CG   1 
ATOM   2299 C  CG   B GLN   A 1 107 ? 22.859 -13.920 -12.826 0.40 27.09 ?  107 GLN   A CG   1 
ATOM   2300 C  CD   A GLN   A 1 107 ? 21.713 -14.044 -12.909 0.60 33.98 ?  107 GLN   A CD   1 
ATOM   2301 C  CD   B GLN   A 1 107 ? 21.971 -14.918 -12.107 0.40 29.42 ?  107 GLN   A CD   1 
ATOM   2302 O  OE1  A GLN   A 1 107 ? 21.739 -15.096 -12.271 0.60 35.31 ?  107 GLN   A OE1  1 
ATOM   2303 O  OE1  B GLN   A 1 107 ? 22.458 -15.815 -11.417 0.40 29.93 ?  107 GLN   A OE1  1 
ATOM   2304 N  NE2  A GLN   A 1 107 ? 20.586 -13.516 -13.371 0.60 34.93 ?  107 GLN   A NE2  1 
ATOM   2305 N  NE2  B GLN   A 1 107 ? 20.660 -14.762 -12.257 0.40 30.09 ?  107 GLN   A NE2  1 
ATOM   2306 H  H    A GLN   A 1 107 ? 22.741 -10.925 -12.200 0.60 25.55 ?  107 GLN   A H    1 
ATOM   2307 H  H    B GLN   A 1 107 ? 22.664 -11.154 -12.176 0.40 25.43 ?  107 GLN   A H    1 
ATOM   2308 H  HA   A GLN   A 1 107 ? 22.437 -12.860 -10.488 0.60 27.33 ?  107 GLN   A HA   1 
ATOM   2309 H  HA   B GLN   A 1 107 ? 22.547 -12.987 -10.353 0.40 26.38 ?  107 GLN   A HA   1 
ATOM   2310 H  HB2  A GLN   A 1 107 ? 24.642 -12.587 -12.227 0.60 32.08 ?  107 GLN   A HB2  1 
ATOM   2311 H  HB2  B GLN   A 1 107 ? 24.424 -12.675 -12.431 0.40 29.49 ?  107 GLN   A HB2  1 
ATOM   2312 H  HB3  A GLN   A 1 107 ? 24.095 -13.951 -11.629 0.60 32.08 ?  107 GLN   A HB3  1 
ATOM   2313 H  HB3  B GLN   A 1 107 ? 24.402 -13.956 -11.498 0.40 29.49 ?  107 GLN   A HB3  1 
ATOM   2314 H  HG2  A GLN   A 1 107 ? 22.741 -12.412 -13.566 0.60 36.73 ?  107 GLN   A HG2  1 
ATOM   2315 H  HG2  B GLN   A 1 107 ? 22.292 -13.239 -13.219 0.40 32.48 ?  107 GLN   A HG2  1 
ATOM   2316 H  HG3  A GLN   A 1 107 ? 23.497 -13.776 -13.856 0.60 36.73 ?  107 GLN   A HG3  1 
ATOM   2317 H  HG3  B GLN   A 1 107 ? 23.340 -14.393 -13.524 0.40 32.48 ?  107 GLN   A HG3  1 
ATOM   2318 H  HE21 A GLN   A 1 107 ? 20.605 -12.778 -13.811 0.60 41.89 ?  107 GLN   A HE21 1 
ATOM   2319 H  HE21 B GLN   A 1 107 ? 20.356 -14.123 -12.745 0.40 36.08 ?  107 GLN   A HE21 1 
ATOM   2320 H  HE22 A GLN   A 1 107 ? 19.838 -13.915 -13.230 0.60 41.89 ?  107 GLN   A HE22 1 
ATOM   2321 H  HE22 B GLN   A 1 107 ? 20.115 -15.302 -11.868 0.40 36.08 ?  107 GLN   A HE22 1 
ATOM   2322 N  N    . LEU   A 1 108 ? 24.720 -10.820 -9.694  1.00 17.33 ?  108 LEU   A N    1 
ATOM   2323 C  CA   . LEU   A 1 108 ? 25.633 -10.406 -8.641  1.00 14.84 ?  108 LEU   A CA   1 
ATOM   2324 C  C    . LEU   A 1 108 ? 24.934 -10.233 -7.303  1.00 12.94 ?  108 LEU   A C    1 
ATOM   2325 O  O    . LEU   A 1 108 ? 25.618 -10.076 -6.289  1.00 13.13 ?  108 LEU   A O    1 
ATOM   2326 C  CB   . LEU   A 1 108 ? 26.365 -9.119  -9.041  1.00 14.42 ?  108 LEU   A CB   1 
ATOM   2327 C  CG   . LEU   A 1 108 ? 27.353 -9.321  -10.191 1.00 16.09 ?  108 LEU   A CG   1 
ATOM   2328 C  CD1  . LEU   A 1 108 ? 27.836 -7.990  -10.745 1.00 17.00 ?  108 LEU   A CD1  1 
ATOM   2329 C  CD2  . LEU   A 1 108 ? 28.538 -10.159 -9.734  1.00 17.99 ?  108 LEU   A CD2  1 
ATOM   2330 H  H    A LEU   A 1 108 ? 24.611 -10.229 -10.303 0.60 20.77 ?  108 LEU   A H    1 
ATOM   2331 H  H    B LEU   A 1 108 ? 24.533 -10.215 -10.268 0.40 20.77 ?  108 LEU   A H    1 
ATOM   2332 H  HA   . LEU   A 1 108 ? 26.300 -11.098 -8.520  1.00 17.79 ?  108 LEU   A HA   1 
ATOM   2333 H  HB2  . LEU   A 1 108 ? 25.713 -8.459  -9.321  1.00 17.28 ?  108 LEU   A HB2  1 
ATOM   2334 H  HB3  . LEU   A 1 108 ? 26.863 -8.790  -8.277  1.00 17.28 ?  108 LEU   A HB3  1 
ATOM   2335 H  HG   . LEU   A 1 108 ? 26.908 -9.800  -10.909 1.00 19.29 ?  108 LEU   A HG   1 
ATOM   2336 H  HD11 . LEU   A 1 108 ? 28.422 -8.157  -11.502 1.00 20.37 ?  108 LEU   A HD11 1 
ATOM   2337 H  HD12 . LEU   A 1 108 ? 27.071 -7.468  -11.029 1.00 20.37 ?  108 LEU   A HD12 1 
ATOM   2338 H  HD13 . LEU   A 1 108 ? 28.322 -7.517  -10.051 1.00 20.37 ?  108 LEU   A HD13 1 
ATOM   2339 H  HD21 . LEU   A 1 108 ? 29.229 -10.119 -10.410 1.00 21.57 ?  108 LEU   A HD21 1 
ATOM   2340 H  HD22 . LEU   A 1 108 ? 28.869 -9.800  -8.897  1.00 21.57 ?  108 LEU   A HD22 1 
ATOM   2341 H  HD23 . LEU   A 1 108 ? 28.246 -11.075 -9.610  1.00 21.57 ?  108 LEU   A HD23 1 
ATOM   2342 N  N    . LEU   A 1 109 ? 23.599 -10.279 -7.267  1.00 12.18 ?  109 LEU   A N    1 
ATOM   2343 C  CA   . LEU   A 1 109 ? 22.904 -10.155 -5.994  1.00 11.30 ?  109 LEU   A CA   1 
ATOM   2344 C  C    . LEU   A 1 109 ? 23.249 -11.309 -5.063  1.00 10.68 ?  109 LEU   A C    1 
ATOM   2345 O  O    . LEU   A 1 109 ? 23.392 -11.114 -3.850  1.00 11.43 ?  109 LEU   A O    1 
ATOM   2346 C  CB   . LEU   A 1 109 ? 21.400 -10.068 -6.238  1.00 12.13 ?  109 LEU   A CB   1 
ATOM   2347 C  CG   . LEU   A 1 109 ? 20.521 -9.775  -5.026  1.00 12.55 ?  109 LEU   A CG   1 
ATOM   2348 C  CD1  . LEU   A 1 109 ? 20.983 -8.513  -4.315  1.00 12.81 ?  109 LEU   A CD1  1 
ATOM   2349 C  CD2  . LEU   A 1 109 ? 19.067 -9.641  -5.447  1.00 13.77 ?  109 LEU   A CD2  1 
ATOM   2350 H  H    . LEU   A 1 109 ? 23.084 -10.374 -7.949  1.00 14.59 ?  109 LEU   A H    1 
ATOM   2351 H  HA   . LEU   A 1 109 ? 23.188 -9.332  -5.564  1.00 13.53 ?  109 LEU   A HA   1 
ATOM   2352 H  HB2  . LEU   A 1 109 ? 21.240 -9.361  -6.884  1.00 14.53 ?  109 LEU   A HB2  1 
ATOM   2353 H  HB3  . LEU   A 1 109 ? 21.104 -10.912 -6.607  1.00 14.53 ?  109 LEU   A HB3  1 
ATOM   2354 H  HG   . LEU   A 1 109 ? 20.584 -10.511 -4.402  1.00 15.04 ?  109 LEU   A HG   1 
ATOM   2355 H  HD11 . LEU   A 1 109 ? 20.307 -8.237  -3.681  1.00 15.35 ?  109 LEU   A HD11 1 
ATOM   2356 H  HD12 . LEU   A 1 109 ? 21.817 -8.697  -3.853  1.00 15.35 ?  109 LEU   A HD12 1 
ATOM   2357 H  HD13 . LEU   A 1 109 ? 21.122 -7.811  -4.975  1.00 15.35 ?  109 LEU   A HD13 1 
ATOM   2358 H  HD21 . LEU   A 1 109 ? 18.541 -9.353  -4.683  1.00 16.50 ?  109 LEU   A HD21 1 
ATOM   2359 H  HD22 . LEU   A 1 109 ? 19.000 -8.983  -6.158  1.00 16.50 ?  109 LEU   A HD22 1 
ATOM   2360 H  HD23 . LEU   A 1 109 ? 18.746 -10.500 -5.763  1.00 16.50 ?  109 LEU   A HD23 1 
ATOM   2361 N  N    . LYS   A 1 110 ? 23.394 -12.520 -5.604  1.00 10.83 ?  110 LYS   A N    1 
ATOM   2362 C  CA   . LYS   A 1 110 ? 23.773 -13.639 -4.747  1.00 10.91 ?  110 LYS   A CA   1 
ATOM   2363 C  C    . LYS   A 1 110 ? 25.157 -13.418 -4.144  1.00 10.45 ?  110 LYS   A C    1 
ATOM   2364 O  O    . LYS   A 1 110 ? 25.355 -13.612 -2.940  1.00 10.70 ?  110 LYS   A O    1 
ATOM   2365 C  CB   . LYS   A 1 110 ? 23.689 -14.962 -5.508  1.00 11.99 ?  110 LYS   A CB   1 
ATOM   2366 C  CG   . LYS   A 1 110 ? 23.910 -16.174 -4.605  1.00 11.91 ?  110 LYS   A CG   1 
ATOM   2367 C  CD   . LYS   A 1 110 ? 23.674 -17.492 -5.318  1.00 12.64 ?  110 LYS   A CD   1 
ATOM   2368 C  CE   . LYS   A 1 110 ? 23.773 -18.670 -4.365  1.00 13.24 ?  110 LYS   A CE   1 
ATOM   2369 N  NZ   . LYS   A 1 110 ? 22.591 -18.801 -3.480  1.00 13.59 ?  110 LYS   A NZ   1 
ATOM   2370 H  H    . LYS   A 1 110 ? 23.283 -12.715 -6.434  1.00 12.97 ?  110 LYS   A H    1 
ATOM   2371 H  HA   . LYS   A 1 110 ? 23.137 -13.689 -4.012  1.00 13.07 ?  110 LYS   A HA   1 
ATOM   2372 H  HB2  . LYS   A 1 110 ? 22.808 -15.043 -5.906  1.00 14.37 ?  110 LYS   A HB2  1 
ATOM   2373 H  HB3  . LYS   A 1 110 ? 24.369 -14.972 -6.196  1.00 14.37 ?  110 LYS   A HB3  1 
ATOM   2374 H  HG2  . LYS   A 1 110 ? 24.826 -16.166 -4.282  1.00 14.27 ?  110 LYS   A HG2  1 
ATOM   2375 H  HG3  . LYS   A 1 110 ? 23.297 -16.127 -3.854  1.00 14.27 ?  110 LYS   A HG3  1 
ATOM   2376 H  HD2  . LYS   A 1 110 ? 22.792 -17.492 -5.708  1.00 15.15 ?  110 LYS   A HD2  1 
ATOM   2377 H  HD3  . LYS   A 1 110 ? 24.352 -17.606 -6.004  1.00 15.15 ?  110 LYS   A HD3  1 
ATOM   2378 H  HE2  . LYS   A 1 110 ? 23.852 -19.487 -4.878  1.00 15.86 ?  110 LYS   A HE2  1 
ATOM   2379 H  HE3  . LYS   A 1 110 ? 24.554 -18.557 -3.798  1.00 15.86 ?  110 LYS   A HE3  1 
ATOM   2380 H  HZ1  . LYS   A 1 110 ? 22.684 -19.500 -2.941  1.00 16.28 ?  110 LYS   A HZ1  1 
ATOM   2381 H  HZ2  . LYS   A 1 110 ? 22.494 -18.064 -2.987  1.00 16.28 ?  110 LYS   A HZ2  1 
ATOM   2382 H  HZ3  . LYS   A 1 110 ? 21.854 -18.912 -3.973  1.00 16.28 ?  110 LYS   A HZ3  1 
ATOM   2383 N  N    . SER   A 1 111 ? 26.116 -12.977 -4.961  1.00 10.46 ?  111 SER   A N    1 
ATOM   2384 C  CA   . SER   A 1 111 ? 27.449 -12.672 -4.448  1.00 10.70 ?  111 SER   A CA   1 
ATOM   2385 C  C    . SER   A 1 111 ? 27.385 -11.625 -3.340  1.00 10.20 ?  111 SER   A C    1 
ATOM   2386 O  O    . SER   A 1 111 ? 28.084 -11.733 -2.325  1.00 10.73 ?  111 SER   A O    1 
ATOM   2387 C  CB   . SER   A 1 111 ? 28.336 -12.184 -5.591  1.00 12.01 ?  111 SER   A CB   1 
ATOM   2388 O  OG   . SER   A 1 111 ? 28.442 -13.174 -6.602  1.00 14.21 ?  111 SER   A OG   1 
ATOM   2389 H  H    . SER   A 1 111 ? 26.014 -12.847 -5.805  1.00 12.53 ?  111 SER   A H    1 
ATOM   2390 H  HA   . SER   A 1 111 ? 27.840 -13.481 -4.084  1.00 12.82 ?  111 SER   A HA   1 
ATOM   2391 H  HB2  . SER   A 1 111 ? 27.940 -11.385 -5.978  1.00 14.38 ?  111 SER   A HB2  1 
ATOM   2392 H  HB3  . SER   A 1 111 ? 29.216 -11.978 -5.240  1.00 14.38 ?  111 SER   A HB3  1 
ATOM   2393 H  HG   . SER   A 1 111 ? 28.948 -12.889 -7.219  1.00 17.03 ?  111 SER   A HG   1 
ATOM   2394 N  N    . ALA   A 1 112 ? 26.543 -10.607 -3.518  1.00 10.32 ?  112 ALA   A N    1 
ATOM   2395 C  CA   . ALA   A 1 112 ? 26.394 -9.573  -2.498  1.00 10.18 ?  112 ALA   A CA   1 
ATOM   2396 C  C    . ALA   A 1 112 ? 25.918 -10.172 -1.180  1.00 9.86  ?  112 ALA   A C    1 
ATOM   2397 O  O    . ALA   A 1 112 ? 26.470 -9.881  -0.113  1.00 10.20 ?  112 ALA   A O    1 
ATOM   2398 C  CB   . ALA   A 1 112 ? 25.436 -8.485  -2.990  1.00 10.77 ?  112 ALA   A CB   1 
ATOM   2399 H  H    . ALA   A 1 112 ? 26.055 -10.489 -4.214  1.00 12.35 ?  112 ALA   A H    1 
ATOM   2400 H  HA   . ALA   A 1 112 ? 27.252 -9.153  -2.340  1.00 12.20 ?  112 ALA   A HA   1 
ATOM   2401 H  HB1  . ALA   A 1 112 ? 25.359 -7.793  -2.306  1.00 12.90 ?  112 ALA   A HB1  1 
ATOM   2402 H  HB2  . ALA   A 1 112 ? 25.786 -8.094  -3.806  1.00 12.90 ?  112 ALA   A HB2  1 
ATOM   2403 H  HB3  . ALA   A 1 112 ? 24.564 -8.874  -3.157  1.00 12.90 ?  112 ALA   A HB3  1 
ATOM   2404 N  N    . TYR   A 1 113 ? 24.882 -11.012 -1.229  1.00 10.00 ?  113 TYR   A N    1 
ATOM   2405 C  CA   . TYR   A 1 113 ? 24.375 -11.621 -0.002  1.00 9.93  ?  113 TYR   A CA   1 
ATOM   2406 C  C    . TYR   A 1 113 ? 25.379 -12.575 0.643   1.00 9.51  ?  113 TYR   A C    1 
ATOM   2407 O  O    . TYR   A 1 113 ? 25.344 -12.759 1.862   1.00 10.22 ?  113 TYR   A O    1 
ATOM   2408 C  CB   . TYR   A 1 113 ? 23.055 -12.342 -0.273  1.00 10.25 ?  113 TYR   A CB   1 
ATOM   2409 C  CG   . TYR   A 1 113 ? 21.842 -11.443 -0.183  1.00 10.28 ?  113 TYR   A CG   1 
ATOM   2410 C  CD1  . TYR   A 1 113 ? 21.483 -10.844 1.023   1.00 10.47 ?  113 TYR   A CD1  1 
ATOM   2411 C  CD2  . TYR   A 1 113 ? 21.034 -11.215 -1.291  1.00 10.49 ?  113 TYR   A CD2  1 
ATOM   2412 C  CE1  . TYR   A 1 113 ? 20.361 -10.041 1.122   1.00 10.72 ?  113 TYR   A CE1  1 
ATOM   2413 C  CE2  . TYR   A 1 113 ? 19.891 -10.411 -1.198  1.00 10.63 ?  113 TYR   A CE2  1 
ATOM   2414 C  CZ   . TYR   A 1 113 ? 19.570 -9.827  0.009   1.00 10.67 ?  113 TYR   A CZ   1 
ATOM   2415 O  OH   . TYR   A 1 113 ? 18.453 -9.030  0.136   1.00 11.50 ?  113 TYR   A OH   1 
ATOM   2416 H  H    . TYR   A 1 113 ? 24.466 -11.238 -1.946  1.00 11.97 ?  113 TYR   A H    1 
ATOM   2417 H  HA   . TYR   A 1 113 ? 24.198 -10.914 0.637   1.00 11.89 ?  113 TYR   A HA   1 
ATOM   2418 H  HB2  . TYR   A 1 113 ? 23.078 -12.713 -1.170  1.00 12.27 ?  113 TYR   A HB2  1 
ATOM   2419 H  HB3  . TYR   A 1 113 ? 22.946 -13.052 0.375   1.00 12.27 ?  113 TYR   A HB3  1 
ATOM   2420 H  HD1  . TYR   A 1 113 ? 22.014 -10.990 1.775   1.00 12.55 ?  113 TYR   A HD1  1 
ATOM   2421 H  HD2  . TYR   A 1 113 ? 21.242 -11.615 -2.103  1.00 12.57 ?  113 TYR   A HD2  1 
ATOM   2422 H  HE1  . TYR   A 1 113 ? 20.143 -9.647  1.934   1.00 12.84 ?  113 TYR   A HE1  1 
ATOM   2423 H  HE2  . TYR   A 1 113 ? 19.352 -10.261 -1.945  1.00 12.73 ?  113 TYR   A HE2  1 
ATOM   2424 H  HH   . TYR   A 1 113 ? 18.058 -8.976  -0.609  1.00 13.77 ?  113 TYR   A HH   1 
ATOM   2425 N  N    . GLU   A 1 114 ? 26.279 -13.185 -0.143  1.00 9.90  ?  114 GLU   A N    1 
ATOM   2426 C  CA   . GLU   A 1 114 ? 27.272 -14.085 0.447   1.00 10.02 ?  114 GLU   A CA   1 
ATOM   2427 C  C    . GLU   A 1 114 ? 28.128 -13.378 1.496   1.00 10.17 ?  114 GLU   A C    1 
ATOM   2428 O  O    . GLU   A 1 114 ? 28.601 -14.014 2.447   1.00 10.55 ?  114 GLU   A O    1 
ATOM   2429 C  CB   . GLU   A 1 114 ? 28.137 -14.722 -0.648  1.00 10.28 ?  114 GLU   A CB   1 
ATOM   2430 C  CG   . GLU   A 1 114 ? 27.372 -15.780 -1.426  1.00 10.69 ?  114 GLU   A CG   1 
ATOM   2431 C  CD   . GLU   A 1 114 ? 28.082 -16.309 -2.666  1.00 10.96 ?  114 GLU   A CD   1 
ATOM   2432 O  OE1  . GLU   A 1 114 ? 29.040 -15.681 -3.169  1.00 11.38 ?  114 GLU   A OE1  1 
ATOM   2433 O  OE2  . GLU   A 1 114 ? 27.639 -17.371 -3.157  1.00 12.38 -1 114 GLU   A OE2  1 
ATOM   2434 H  H    . GLU   A 1 114 ? 26.337 -13.086 -1.003  1.00 11.85 ?  114 GLU   A H    1 
ATOM   2435 H  HA   . GLU   A 1 114 ? 26.800 -14.799 0.890   1.00 12.00 ?  114 GLU   A HA   1 
ATOM   2436 H  HB2  . GLU   A 1 114 ? 28.423 -14.039 -1.276  1.00 12.31 ?  114 GLU   A HB2  1 
ATOM   2437 H  HB3  . GLU   A 1 114 ? 28.906 -15.148 -0.242  1.00 12.31 ?  114 GLU   A HB3  1 
ATOM   2438 H  HG2  . GLU   A 1 114 ? 27.203 -16.534 -0.839  1.00 12.81 ?  114 GLU   A HG2  1 
ATOM   2439 H  HG3  . GLU   A 1 114 ? 26.523 -15.400 -1.713  1.00 12.81 ?  114 GLU   A HG3  1 
ATOM   2440 N  N    . ASN   A 1 115 ? 28.306 -12.059 1.369   1.00 9.78  ?  115 ASN   A N    1 
ATOM   2441 C  CA   . ASN   A 1 115 ? 29.077 -11.334 2.372   1.00 10.15 ?  115 ASN   A CA   1 
ATOM   2442 C  C    . ASN   A 1 115 ? 28.466 -11.470 3.759   1.00 9.74  ?  115 ASN   A C    1 
ATOM   2443 O  O    . ASN   A 1 115 ? 29.179 -11.395 4.765   1.00 10.36 ?  115 ASN   A O    1 
ATOM   2444 C  CB   . ASN   A 1 115 ? 29.181 -9.858  1.995   1.00 10.42 ?  115 ASN   A CB   1 
ATOM   2445 C  CG   . ASN   A 1 115 ? 29.979 -9.641  0.732   1.00 11.28 ?  115 ASN   A CG   1 
ATOM   2446 O  OD1  . ASN   A 1 115 ? 31.199 -9.748  0.740   1.00 14.61 ?  115 ASN   A OD1  1 
ATOM   2447 N  ND2  . ASN   A 1 115 ? 29.300 -9.333  -0.358  1.00 10.71 ?  115 ASN   A ND2  1 
ATOM   2448 H  H    . ASN   A 1 115 ? 28.001 -11.571 0.724   1.00 11.72 ?  115 ASN   A H    1 
ATOM   2449 H  HA   . ASN   A 1 115 ? 29.972 -11.698 2.406   1.00 12.15 ?  115 ASN   A HA   1 
ATOM   2450 H  HB2  . ASN   A 1 115 ? 28.287 -9.502  1.863   1.00 12.48 ?  115 ASN   A HB2  1 
ATOM   2451 H  HB3  . ASN   A 1 115 ? 29.620 -9.380  2.720   1.00 12.48 ?  115 ASN   A HB3  1 
ATOM   2452 H  HD21 . ASN   A 1 115 ? 29.712 -9.198  -1.098  1.00 12.83 ?  115 ASN   A HD21 1 
ATOM   2453 H  HD22 . ASN   A 1 115 ? 28.439 -9.284  -0.329  1.00 12.83 ?  115 ASN   A HD22 1 
ATOM   2454 N  N    . PHE   A 1 116 ? 27.142 -11.632 3.838   1.00 10.05 ?  116 PHE   A N    1 
ATOM   2455 C  CA   . PHE   A 1 116 ? 26.494 -11.730 5.142   1.00 10.03 ?  116 PHE   A CA   1 
ATOM   2456 C  C    . PHE   A 1 116 ? 26.967 -12.963 5.911   1.00 10.25 ?  116 PHE   A C    1 
ATOM   2457 O  O    . PHE   A 1 116 ? 26.892 -12.982 7.141   1.00 10.88 ?  116 PHE   A O    1 
ATOM   2458 C  CB   . PHE   A 1 116 ? 24.967 -11.860 5.002   1.00 10.28 ?  116 PHE   A CB   1 
ATOM   2459 C  CG   . PHE   A 1 116 ? 24.210 -10.614 4.550   1.00 9.79  ?  116 PHE   A CG   1 
ATOM   2460 C  CD1  . PHE   A 1 116 ? 24.778 -9.596  3.796   1.00 10.05 ?  116 PHE   A CD1  1 
ATOM   2461 C  CD2  . PHE   A 1 116 ? 22.858 -10.507 4.878   1.00 10.61 ?  116 PHE   A CD2  1 
ATOM   2462 C  CE1  . PHE   A 1 116 ? 24.011 -8.512  3.385   1.00 10.44 ?  116 PHE   A CE1  1 
ATOM   2463 C  CE2  . PHE   A 1 116 ? 22.091 -9.432  4.472   1.00 10.74 ?  116 PHE   A CE2  1 
ATOM   2464 C  CZ   . PHE   A 1 116 ? 22.662 -8.433  3.725   1.00 10.33 ?  116 PHE   A CZ   1 
ATOM   2465 H  H    . PHE   A 1 116 ? 26.603 -11.678 3.164   1.00 12.03 ?  116 PHE   A H    1 
ATOM   2466 H  HA   . PHE   A 1 116 ? 26.688 -10.937 5.668   1.00 12.01 ?  116 PHE   A HA   1 
ATOM   2467 H  HB2  . PHE   A 1 116 ? 24.783 -12.561 4.354   1.00 12.32 ?  116 PHE   A HB2  1 
ATOM   2468 H  HB3  . PHE   A 1 116 ? 24.606 -12.123 5.864   1.00 12.32 ?  116 PHE   A HB3  1 
ATOM   2469 H  HD1  . PHE   A 1 116 ? 25.671 -9.655  3.556   1.00 12.04 ?  116 PHE   A HD1  1 
ATOM   2470 H  HD2  . PHE   A 1 116 ? 22.458 -11.193 5.374   1.00 12.71 ?  116 PHE   A HD2  1 
ATOM   2471 H  HE1  . PHE   A 1 116 ? 24.403 -7.835  2.885   1.00 12.50 ?  116 PHE   A HE1  1 
ATOM   2472 H  HE2  . PHE   A 1 116 ? 21.192 -9.388  4.711   1.00 12.86 ?  116 PHE   A HE2  1 
ATOM   2473 H  HZ   . PHE   A 1 116 ? 22.156 -7.698  3.463   1.00 12.37 ?  116 PHE   A HZ   1 
ATOM   2474 N  N    . ASN   A 1 117 ? 27.406 -14.017 5.209   1.00 10.48 ?  117 ASN   A N    1 
ATOM   2475 C  CA   . ASN   A 1 117 ? 27.777 -15.263 5.875   1.00 10.64 ?  117 ASN   A CA   1 
ATOM   2476 C  C    . ASN   A 1 117 ? 29.040 -15.144 6.708   1.00 11.16 ?  117 ASN   A C    1 
ATOM   2477 O  O    . ASN   A 1 117 ? 29.340 -16.064 7.476   1.00 12.07 ?  117 ASN   A O    1 
ATOM   2478 C  CB   . ASN   A 1 117 ? 27.890 -16.380 4.848   1.00 10.82 ?  117 ASN   A CB   1 
ATOM   2479 C  CG   . ASN   A 1 117 ? 26.532 -16.764 4.314   1.00 10.83 ?  117 ASN   A CG   1 
ATOM   2480 O  OD1  . ASN   A 1 117 ? 25.560 -16.793 5.068   1.00 11.88 ?  117 ASN   A OD1  1 
ATOM   2481 N  ND2  . ASN   A 1 117 ? 26.443 -17.022 3.022   1.00 10.96 ?  117 ASN   A ND2  1 
ATOM   2482 H  H    . ASN   A 1 117 ? 27.480 -14.032 4.348   1.00 12.55 ?  117 ASN   A H    1 
ATOM   2483 H  HA   . ASN   A 1 117 ? 27.056 -15.498 6.477   1.00 12.75 ?  117 ASN   A HA   1 
ATOM   2484 H  HB2  . ASN   A 1 117 ? 28.441 -16.083 4.107   1.00 12.96 ?  117 ASN   A HB2  1 
ATOM   2485 H  HB3  . ASN   A 1 117 ? 28.282 -17.159 5.270   1.00 12.96 ?  117 ASN   A HB3  1 
ATOM   2486 H  HD21 . ASN   A 1 117 ? 25.687 -17.239 2.682   1.00 13.13 ?  117 ASN   A HD21 1 
ATOM   2487 H  HD22 . ASN   A 1 117 ? 27.145 -16.978 2.527   1.00 13.13 ?  117 ASN   A HD22 1 
ATOM   2488 N  N    . GLN   A 1 118 ? 29.769 -14.033 6.587   1.00 10.99 ?  118 GLN   A N    1 
ATOM   2489 C  CA   . GLN   A 1 118 ? 30.948 -13.798 7.405   1.00 11.51 ?  118 GLN   A CA   1 
ATOM   2490 C  C    . GLN   A 1 118 ? 30.609 -13.225 8.776   1.00 11.54 ?  118 GLN   A C    1 
ATOM   2491 O  O    . GLN   A 1 118 ? 31.526 -12.934 9.554   1.00 12.96 ?  118 GLN   A O    1 
ATOM   2492 C  CB   . GLN   A 1 118 ? 31.932 -12.891 6.660   1.00 11.89 ?  118 GLN   A CB   1 
ATOM   2493 C  CG   . GLN   A 1 118 ? 32.409 -13.472 5.338   1.00 11.70 ?  118 GLN   A CG   1 
ATOM   2494 C  CD   . GLN   A 1 118 ? 33.226 -14.735 5.516   1.00 11.98 ?  118 GLN   A CD   1 
ATOM   2495 O  OE1  . GLN   A 1 118 ? 34.089 -14.808 6.400   1.00 12.84 ?  118 GLN   A OE1  1 
ATOM   2496 N  NE2  . GLN   A 1 118 ? 32.976 -15.729 4.667   1.00 12.34 ?  118 GLN   A NE2  1 
ATOM   2497 H  H    . GLN   A 1 118 ? 29.587 -13.389 6.036   1.00 13.16 ?  118 GLN   A H    1 
ATOM   2498 H  HA   . GLN   A 1 118 ? 31.381 -14.654 7.547   1.00 13.79 ?  118 GLN   A HA   1 
ATOM   2499 H  HB2  . GLN   A 1 118 ? 31.501 -12.046 6.478   1.00 14.24 ?  118 GLN   A HB2  1 
ATOM   2500 H  HB3  . GLN   A 1 118 ? 32.709 -12.756 7.224   1.00 14.24 ?  118 GLN   A HB3  1 
ATOM   2501 H  HG2  . GLN   A 1 118 ? 31.643 -13.682 4.783   1.00 14.01 ?  118 GLN   A HG2  1 
ATOM   2502 H  HG3  . GLN   A 1 118 ? 32.971 -12.816 4.890   1.00 14.01 ?  118 GLN   A HG3  1 
ATOM   2503 H  HE21 . GLN   A 1 118 ? 32.361 -15.638 4.062   1.00 14.78 ?  118 GLN   A HE21 1 
ATOM   2504 H  HE22 . GLN   A 1 118 ? 33.407 -16.469 4.723   1.00 14.78 ?  118 GLN   A HE22 1 
ATOM   2505 N  N    . HIS   A 1 119 ? 29.320 -13.071 9.093   1.00 11.31 ?  119 HIS   A N    1 
ATOM   2506 C  CA   . HIS   A 1 119 ? 28.873 -12.461 10.340  1.00 11.90 ?  119 HIS   A CA   1 
ATOM   2507 C  C    . HIS   A 1 119 ? 27.734 -13.284 10.911  1.00 11.96 ?  119 HIS   A C    1 
ATOM   2508 O  O    . HIS   A 1 119 ? 26.787 -13.616 10.195  1.00 12.42 ?  119 HIS   A O    1 
ATOM   2509 C  CB   . HIS   A 1 119 ? 28.412 -11.029 10.067  1.00 12.59 ?  119 HIS   A CB   1 
ATOM   2510 C  CG   . HIS   A 1 119 ? 29.490 -10.213 9.458   1.00 13.89 ?  119 HIS   A CG   1 
ATOM   2511 N  ND1  . HIS   A 1 119 ? 30.470 -9.618  10.217  1.00 16.06 ?  119 HIS   A ND1  1 
ATOM   2512 C  CD2  . HIS   A 1 119 ? 29.834 -10.013 8.166   1.00 14.85 ?  119 HIS   A CD2  1 
ATOM   2513 C  CE1  . HIS   A 1 119 ? 31.339 -9.028  9.417   1.00 16.16 ?  119 HIS   A CE1  1 
ATOM   2514 N  NE2  . HIS   A 1 119 ? 30.986 -9.265  8.167   1.00 15.88 ?  119 HIS   A NE2  1 
ATOM   2515 H  H    . HIS   A 1 119 ? 28.668 -13.323 8.588   1.00 13.55 ?  119 HIS   A H    1 
ATOM   2516 H  HA   . HIS   A 1 119 ? 29.605 -12.446 10.980  1.00 14.26 ?  119 HIS   A HA   1 
ATOM   2517 H  HB2  . HIS   A 1 119 ? 27.659 -11.053 9.456   1.00 15.09 ?  119 HIS   A HB2  1 
ATOM   2518 H  HB3  . HIS   A 1 119 ? 28.152 -10.619 10.906  1.00 15.09 ?  119 HIS   A HB3  1 
ATOM   2519 H  HD1  . HIS   A 1 119 ? 30.497 -9.611  11.075  1.00 19.25 ?  119 HIS   A HD1  1 
ATOM   2520 H  HD2  . HIS   A 1 119 ? 29.373 -10.319 7.416   1.00 17.80 ?  119 HIS   A HD2  1 
ATOM   2521 H  HE1  . HIS   A 1 119 ? 32.077 -8.533  9.688   1.00 19.37 ?  119 HIS   A HE1  1 
ATOM   2522 N  N    . GLU   A 1 120 ? 27.823 -13.600 12.203  1.00 12.85 ?  120 GLU   A N    1 
ATOM   2523 C  CA   . GLU   A 1 120 ? 26.868 -14.531 12.800  1.00 15.20 ?  120 GLU   A CA   1 
ATOM   2524 C  C    . GLU   A 1 120 ? 25.452 -13.965 12.863  1.00 13.53 ?  120 GLU   A C    1 
ATOM   2525 O  O    . GLU   A 1 120 ? 24.479 -14.729 12.758  1.00 13.74 ?  120 GLU   A O    1 
ATOM   2526 C  CB   . GLU   A 1 120 ? 27.334 -14.933 14.200  1.00 20.18 ?  120 GLU   A CB   1 
ATOM   2527 C  CG   . GLU   A 1 120 ? 28.524 -15.876 14.206  1.00 28.32 ?  120 GLU   A CG   1 
ATOM   2528 C  CD   . GLU   A 1 120 ? 28.700 -16.576 15.538  1.00 37.12 ?  120 GLU   A CD   1 
ATOM   2529 O  OE1  . GLU   A 1 120 ? 28.163 -16.076 16.550  1.00 38.58 ?  120 GLU   A OE1  1 
ATOM   2530 O  OE2  . GLU   A 1 120 ? 29.372 -17.628 15.573  1.00 41.25 -1 120 GLU   A OE2  1 
ATOM   2531 H  H    . GLU   A 1 120 ? 28.425 -13.306 12.747  1.00 15.40 ?  120 GLU   A H    1 
ATOM   2532 H  HA   . GLU   A 1 120 ? 26.837 -15.335 12.264  1.00 18.22 ?  120 GLU   A HA   1 
ATOM   2533 H  HB2  . GLU   A 1 120 ? 27.592 -14.138 14.692  1.00 24.19 ?  120 GLU   A HB2  1 
ATOM   2534 H  HB3  . GLU   A 1 120 ? 26.605 -15.381 14.661  1.00 24.19 ?  120 GLU   A HB3  1 
ATOM   2535 H  HG2  . GLU   A 1 120 ? 28.404 -16.546 13.514  1.00 33.97 ?  120 GLU   A HG2  1 
ATOM   2536 H  HG3  . GLU   A 1 120 ? 29.334 -15.371 14.045  1.00 33.97 ?  120 GLU   A HG3  1 
ATOM   2537 N  N    . VAL   A 1 121 ? 25.317 -12.653 13.074  1.00 12.70 ?  121 VAL   A N    1 
ATOM   2538 C  CA   . VAL   A 1 121 ? 24.025 -11.986 13.206  1.00 12.82 ?  121 VAL   A CA   1 
ATOM   2539 C  C    . VAL   A 1 121 ? 24.135 -10.605 12.570  1.00 12.06 ?  121 VAL   A C    1 
ATOM   2540 O  O    . VAL   A 1 121 ? 25.104 -9.879  12.815  1.00 12.55 ?  121 VAL   A O    1 
ATOM   2541 C  CB   . VAL   A 1 121 ? 23.594 -11.840 14.684  1.00 15.90 ?  121 VAL   A CB   1 
ATOM   2542 C  CG1  . VAL   A 1 121 ? 22.217 -11.187 14.786  1.00 16.45 ?  121 VAL   A CG1  1 
ATOM   2543 C  CG2  . VAL   A 1 121 ? 23.595 -13.174 15.403  1.00 18.33 ?  121 VAL   A CG2  1 
ATOM   2544 H  H    . VAL   A 1 121 ? 25.983 -12.109 13.146  1.00 15.22 ?  121 VAL   A H    1 
ATOM   2545 H  HA   . VAL   A 1 121 ? 23.348 -12.496 12.735  1.00 15.36 ?  121 VAL   A HA   1 
ATOM   2546 H  HB   . VAL   A 1 121 ? 24.225 -11.264 15.137  1.00 19.06 ?  121 VAL   A HB   1 
ATOM   2547 H  HG11 . VAL   A 1 121 ? 21.904 -11.250 15.702  1.00 19.71 ?  121 VAL   A HG11 1 
ATOM   2548 H  HG12 . VAL   A 1 121 ? 22.288 -10.254 14.526  1.00 19.71 ?  121 VAL   A HG12 1 
ATOM   2549 H  HG13 . VAL   A 1 121 ? 21.602 -11.649 14.195  1.00 19.71 ?  121 VAL   A HG13 1 
ATOM   2550 H  HG21 . VAL   A 1 121 ? 23.251 -13.048 16.306  1.00 21.97 ?  121 VAL   A HG21 1 
ATOM   2551 H  HG22 . VAL   A 1 121 ? 23.023 -13.796 14.924  1.00 21.97 ?  121 VAL   A HG22 1 
ATOM   2552 H  HG23 . VAL   A 1 121 ? 24.499 -13.516 15.442  1.00 21.97 ?  121 VAL   A HG23 1 
ATOM   2553 N  N    . LEU   A 1 122 ? 23.122 -10.220 11.785  1.00 11.68 ?  122 LEU   A N    1 
ATOM   2554 C  CA   . LEU   A 1 122 ? 23.126 -8.922  11.114  1.00 11.44 ?  122 LEU   A CA   1 
ATOM   2555 C  C    . LEU   A 1 122 ? 21.727 -8.332  11.090  1.00 11.01 ?  122 LEU   A C    1 
ATOM   2556 O  O    . LEU   A 1 122 ? 20.740 -9.054  10.949  1.00 12.02 ?  122 LEU   A O    1 
ATOM   2557 C  CB   . LEU   A 1 122 ? 23.542 -9.015  9.641   1.00 12.72 ?  122 LEU   A CB   1 
ATOM   2558 C  CG   . LEU   A 1 122 ? 24.753 -9.865  9.283   1.00 12.55 ?  122 LEU   A CG   1 
ATOM   2559 C  CD1  . LEU   A 1 122 ? 24.362 -11.315 9.053   1.00 13.49 ?  122 LEU   A CD1  1 
ATOM   2560 C  CD2  . LEU   A 1 122 ? 25.430 -9.295  8.053   1.00 12.25 ?  122 LEU   A CD2  1 
ATOM   2561 H  H    . LEU   A 1 122 ? 22.419 -10.692 11.624  1.00 13.99 ?  122 LEU   A H    1 
ATOM   2562 H  HA   . LEU   A 1 122 ? 23.725 -8.310  11.570  1.00 13.71 ?  122 LEU   A HA   1 
ATOM   2563 H  HB2  . LEU   A 1 122 ? 22.798 -9.378  9.140   1.00 15.24 ?  122 LEU   A HB2  1 
ATOM   2564 H  HB3  . LEU   A 1 122 ? 23.732 -8.120  9.324   1.00 15.24 ?  122 LEU   A HB3  1 
ATOM   2565 H  HG   . LEU   A 1 122 ? 25.398 -9.839  10.009  1.00 15.04 ?  122 LEU   A HG   1 
ATOM   2566 H  HD11 . LEU   A 1 122 ? 25.145 -11.821 8.784   1.00 16.16 ?  122 LEU   A HD11 1 
ATOM   2567 H  HD12 . LEU   A 1 122 ? 24.003 -11.678 9.878   1.00 16.16 ?  122 LEU   A HD12 1 
ATOM   2568 H  HD13 . LEU   A 1 122 ? 23.689 -11.353 8.355   1.00 16.16 ?  122 LEU   A HD13 1 
ATOM   2569 H  HD21 . LEU   A 1 122 ? 26.176 -9.866  7.800   1.00 14.67 ?  122 LEU   A HD21 1 
ATOM   2570 H  HD22 . LEU   A 1 122 ? 24.789 -9.253  7.327   1.00 14.67 ?  122 LEU   A HD22 1 
ATOM   2571 H  HD23 . LEU   A 1 122 ? 25.758 -8.402  8.254   1.00 14.67 ?  122 LEU   A HD23 1 
ATOM   2572 N  N    . LEU   A 1 123 ? 21.668 -7.002  11.189  1.00 10.67 ?  123 LEU   A N    1 
ATOM   2573 C  CA   . LEU   A 1 123 ? 20.497 -6.204  10.829  1.00 10.64 ?  123 LEU   A CA   1 
ATOM   2574 C  C    . LEU   A 1 123 ? 20.737 -5.677  9.420   1.00 10.18 ?  123 LEU   A C    1 
ATOM   2575 O  O    . LEU   A 1 123 ? 21.786 -5.083  9.165   1.00 10.66 ?  123 LEU   A O    1 
ATOM   2576 C  CB   . LEU   A 1 123 ? 20.380 -5.024  11.794  1.00 11.44 ?  123 LEU   A CB   1 
ATOM   2577 C  CG   . LEU   A 1 123 ? 19.328 -3.966  11.456  1.00 12.15 ?  123 LEU   A CG   1 
ATOM   2578 C  CD1  . LEU   A 1 123 ? 17.930 -4.563  11.463  1.00 13.04 ?  123 LEU   A CD1  1 
ATOM   2579 C  CD2  . LEU   A 1 123 ? 19.423 -2.792  12.416  1.00 12.71 ?  123 LEU   A CD2  1 
ATOM   2580 H  H    . LEU   A 1 123 ? 22.322 -6.518  11.471  1.00 12.78 ?  123 LEU   A H    1 
ATOM   2581 H  HA   . LEU   A 1 123 ? 19.685 -6.740  10.855  1.00 12.74 ?  123 LEU   A HA   1 
ATOM   2582 H  HB2  . LEU   A 1 123 ? 20.159 -5.368  12.674  1.00 13.70 ?  123 LEU   A HB2  1 
ATOM   2583 H  HB3  . LEU   A 1 123 ? 21.233 -4.571  11.828  1.00 13.70 ?  123 LEU   A HB3  1 
ATOM   2584 H  HG   . LEU   A 1 123 ? 19.491 -3.619  10.565  1.00 14.56 ?  123 LEU   A HG   1 
ATOM   2585 H  HD11 . LEU   A 1 123 ? 17.280 -3.864  11.300  1.00 15.62 ?  123 LEU   A HD11 1 
ATOM   2586 H  HD12 . LEU   A 1 123 ? 17.872 -5.239  10.767  1.00 15.62 ?  123 LEU   A HD12 1 
ATOM   2587 H  HD13 . LEU   A 1 123 ? 17.766 -4.971  12.330  1.00 15.62 ?  123 LEU   A HD13 1 
ATOM   2588 H  HD21 . LEU   A 1 123 ? 18.745 -2.137  12.187  1.00 15.23 ?  123 LEU   A HD21 1 
ATOM   2589 H  HD22 . LEU   A 1 123 ? 19.270 -3.118  13.321  1.00 15.23 ?  123 LEU   A HD22 1 
ATOM   2590 H  HD23 . LEU   A 1 123 ? 20.303 -2.402  12.350  1.00 15.23 ?  123 LEU   A HD23 1 
ATOM   2591 N  N    A ALA   A 1 124 ? 19.769 -5.855  8.522   0.60 9.72  ?  124 ALA   A N    1 
ATOM   2592 N  N    B ALA   A 1 124 ? 19.794 -5.911  8.507   0.40 10.40 ?  124 ALA   A N    1 
ATOM   2593 C  CA   A ALA   A 1 124 ? 20.033 -5.540  7.126   0.60 9.44  ?  124 ALA   A CA   1 
ATOM   2594 C  CA   B ALA   A 1 124 ? 20.094 -5.679  7.101   0.40 10.77 ?  124 ALA   A CA   1 
ATOM   2595 C  C    A ALA   A 1 124 ? 18.775 -5.044  6.430   0.60 9.16  ?  124 ALA   A C    1 
ATOM   2596 C  C    B ALA   A 1 124 ? 18.874 -5.229  6.310   0.40 10.16 ?  124 ALA   A C    1 
ATOM   2597 O  O    A ALA   A 1 124 ? 17.653 -5.366  6.843   0.60 9.82  ?  124 ALA   A O    1 
ATOM   2598 O  O    B ALA   A 1 124 ? 17.738 -5.576  6.657   0.40 10.51 ?  124 ALA   A O    1 
ATOM   2599 C  CB   A ALA   A 1 124 ? 20.575 -6.759  6.372   0.60 9.57  ?  124 ALA   A CB   1 
ATOM   2600 C  CB   B ALA   A 1 124 ? 20.691 -6.940  6.459   0.40 11.29 ?  124 ALA   A CB   1 
ATOM   2601 H  H    A ALA   A 1 124 ? 18.978 -6.154  8.690   0.60 11.64 ?  124 ALA   A H    1 
ATOM   2602 H  H    B ALA   A 1 124 ? 19.005 -6.206  8.665   0.40 12.46 ?  124 ALA   A H    1 
ATOM   2603 H  HA   A ALA   A 1 124 ? 20.707 -4.844  7.094   0.60 11.31 ?  124 ALA   A HA   1 
ATOM   2604 H  HA   B ALA   A 1 124 ? 20.754 -4.979  7.043   0.40 12.90 ?  124 ALA   A HA   1 
ATOM   2605 H  HB1  A ALA   A 1 124 ? 20.743 -6.509  5.448   0.60 11.46 ?  124 ALA   A HB1  1 
ATOM   2606 H  HB1  B ALA   A 1 124 ? 20.881 -6.764  5.525   0.40 13.53 ?  124 ALA   A HB1  1 
ATOM   2607 H  HB2  A ALA   A 1 124 ? 21.404 -7.047  6.789   0.60 11.46 ?  124 ALA   A HB2  1 
ATOM   2608 H  HB2  B ALA   A 1 124 ? 21.513 -7.168  6.925   0.40 13.53 ?  124 ALA   A HB2  1 
ATOM   2609 H  HB3  A ALA   A 1 124 ? 19.921 -7.472  6.409   0.60 11.46 ?  124 ALA   A HB3  1 
ATOM   2610 H  HB3  B ALA   A 1 124 ? 20.056 -7.668  6.538   0.40 13.53 ?  124 ALA   A HB3  1 
ATOM   2611 N  N    A PRO   A 1 125 ? 18.936 -4.275  5.354   0.60 9.61  ?  125 PRO   A N    1 
ATOM   2612 N  N    B PRO   A 1 125 ? 19.085 -4.479  5.231   0.40 9.05  ?  125 PRO   A N    1 
ATOM   2613 C  CA   A PRO   A 1 125 ? 17.857 -4.044  4.393   0.60 10.50 ?  125 PRO   A CA   1 
ATOM   2614 C  CA   B PRO   A 1 125 ? 18.005 -4.132  4.310   0.40 9.45  ?  125 PRO   A CA   1 
ATOM   2615 C  C    A PRO   A 1 125 ? 17.922 -5.115  3.308   0.60 10.00 ?  125 PRO   A C    1 
ATOM   2616 C  C    B PRO   A 1 125 ? 17.958 -5.149  3.175   0.40 9.92  ?  125 PRO   A C    1 
ATOM   2617 O  O    A PRO   A 1 125 ? 18.872 -5.896  3.228   0.60 10.34 ?  125 PRO   A O    1 
ATOM   2618 O  O    B PRO   A 1 125 ? 18.840 -5.996  3.024   0.40 10.17 ?  125 PRO   A O    1 
ATOM   2619 C  CB   A PRO   A 1 125 ? 18.253 -2.685  3.800   0.60 10.81 ?  125 PRO   A CB   1 
ATOM   2620 C  CB   B PRO   A 1 125 ? 18.493 -2.790  3.760   0.40 8.83  ?  125 PRO   A CB   1 
ATOM   2621 C  CG   A PRO   A 1 125 ? 19.759 -2.787  3.721   0.60 11.08 ?  125 PRO   A CG   1 
ATOM   2622 C  CG   B PRO   A 1 125 ? 19.977 -3.019  3.605   0.40 8.28  ?  125 PRO   A CG   1 
ATOM   2623 C  CD   A PRO   A 1 125 ? 20.170 -3.565  4.962   0.60 10.43 ?  125 PRO   A CD   1 
ATOM   2624 C  CD   B PRO   A 1 125 ? 20.370 -3.904  4.786   0.40 8.28  ?  125 PRO   A CD   1 
ATOM   2625 H  HA   A PRO   A 1 125 ? 16.984 -4.013  4.813   0.60 12.58 ?  125 PRO   A HA   1 
ATOM   2626 H  HA   B PRO   A 1 125 ? 17.142 -4.048  4.761   0.40 11.32 ?  125 PRO   A HA   1 
ATOM   2627 H  HB2  A PRO   A 1 125 ? 17.859 -2.576  2.919   0.60 12.95 ?  125 PRO   A HB2  1 
ATOM   2628 H  HB2  B PRO   A 1 125 ? 18.073 -2.616  2.905   0.40 10.58 ?  125 PRO   A HB2  1 
ATOM   2629 H  HB3  A PRO   A 1 125 ? 17.980 -1.970  4.397   0.60 12.95 ?  125 PRO   A HB3  1 
ATOM   2630 H  HB3  B PRO   A 1 125 ? 18.312 -2.087  4.397   0.40 10.58 ?  125 PRO   A HB3  1 
ATOM   2631 H  HG2  A PRO   A 1 125 ? 20.014 -3.268  2.915   0.60 13.27 ?  125 PRO   A HG2  1 
ATOM   2632 H  HG2  B PRO   A 1 125 ? 20.151 -3.472  2.762   0.40 9.92  ?  125 PRO   A HG2  1 
ATOM   2633 H  HG3  A PRO   A 1 125 ? 20.149 -1.898  3.724   0.60 13.27 ?  125 PRO   A HG3  1 
ATOM   2634 H  HG3  B PRO   A 1 125 ? 20.440 -2.169  3.637   0.40 9.92  ?  125 PRO   A HG3  1 
ATOM   2635 H  HD2  A PRO   A 1 125 ? 20.880 -4.190  4.749   0.60 12.49 ?  125 PRO   A HD2  1 
ATOM   2636 H  HD2  B PRO   A 1 125 ? 20.984 -4.604  4.496   0.40 9.92  ?  125 PRO   A HD2  1 
ATOM   2637 H  HD3  A PRO   A 1 125 ? 20.441 -2.951  5.667   0.60 12.49 ?  125 PRO   A HD3  1 
ATOM   2638 H  HD3  B PRO   A 1 125 ? 20.768 -3.364  5.492   0.40 9.92  ?  125 PRO   A HD3  1 
ATOM   2639 N  N    A LEU   A 1 126 ? 16.900 -5.129  2.454   0.60 10.29 ?  126 LEU   A N    1 
ATOM   2640 N  N    B LEU   A 1 126 ? 16.922 -5.027  2.353   0.40 11.16 ?  126 LEU   A N    1 
ATOM   2641 C  CA   A LEU   A 1 126 ? 16.945 -5.985  1.276   0.60 10.48 ?  126 LEU   A CA   1 
ATOM   2642 C  CA   B LEU   A 1 126 ? 16.825 -5.810  1.127   0.40 11.62 ?  126 LEU   A CA   1 
ATOM   2643 C  C    A LEU   A 1 126 ? 17.887 -5.389  0.238   0.60 10.71 ?  126 LEU   A C    1 
ATOM   2644 C  C    B LEU   A 1 126 ? 17.766 -5.223  0.082   0.40 10.74 ?  126 LEU   A C    1 
ATOM   2645 O  O    A LEU   A 1 126 ? 17.707 -4.249  -0.199  0.60 11.50 ?  126 LEU   A O    1 
ATOM   2646 O  O    B LEU   A 1 126 ? 17.516 -4.136  -0.449  0.40 11.16 ?  126 LEU   A O    1 
ATOM   2647 C  CB   A LEU   A 1 126 ? 15.552 -6.162  0.686   0.60 10.57 ?  126 LEU   A CB   1 
ATOM   2648 C  CB   B LEU   A 1 126 ? 15.390 -5.804  0.613   0.40 13.18 ?  126 LEU   A CB   1 
ATOM   2649 C  CG   A LEU   A 1 126 ? 14.653 -7.115  1.470   0.60 11.32 ?  126 LEU   A CG   1 
ATOM   2650 C  CG   B LEU   A 1 126 ? 14.441 -6.844  1.199   0.40 14.69 ?  126 LEU   A CG   1 
ATOM   2651 C  CD1  A LEU   A 1 126 ? 13.216 -6.956  1.017   0.60 11.70 ?  126 LEU   A CD1  1 
ATOM   2652 C  CD1  B LEU   A 1 126 ? 13.157 -6.834  0.399   0.40 15.30 ?  126 LEU   A CD1  1 
ATOM   2653 C  CD2  A LEU   A 1 126 ? 15.114 -8.558  1.299   0.60 12.01 ?  126 LEU   A CD2  1 
ATOM   2654 C  CD2  B LEU   A 1 126 ? 15.056 -8.237  1.198   0.40 15.16 ?  126 LEU   A CD2  1 
ATOM   2655 H  H    A LEU   A 1 126 ? 16.186 -4.649  2.520   0.60 12.32 ?  126 LEU   A H    1 
ATOM   2656 H  H    B LEU   A 1 126 ? 16.261 -4.495  2.487   0.40 13.36 ?  126 LEU   A H    1 
ATOM   2657 H  HA   A LEU   A 1 126 ? 17.286 -6.855  1.524   0.60 12.55 ?  126 LEU   A HA   1 
ATOM   2658 H  HA   B LEU   A 1 126 ? 17.102 -6.720  1.308   0.40 13.92 ?  126 LEU   A HA   1 
ATOM   2659 H  HB2  A LEU   A 1 126 ? 15.111 -5.300  0.662   0.60 12.66 ?  126 LEU   A HB2  1 
ATOM   2660 H  HB2  B LEU   A 1 126 ? 15.005 -4.930  0.801   0.40 15.79 ?  126 LEU   A HB2  1 
ATOM   2661 H  HB3  A LEU   A 1 126 ? 15.633 -6.514  -0.214  0.60 12.66 ?  126 LEU   A HB3  1 
ATOM   2662 H  HB3  B LEU   A 1 126 ? 15.412 -5.941  -0.343  0.40 15.79 ?  126 LEU   A HB3  1 
ATOM   2663 H  HG   A LEU   A 1 126 ? 14.694 -6.895  2.413   0.60 13.56 ?  126 LEU   A HG   1 
ATOM   2664 H  HG   B LEU   A 1 126 ? 14.226 -6.605  2.115   0.40 17.60 ?  126 LEU   A HG   1 
ATOM   2665 H  HD11 A LEU   A 1 126 ? 12.656 -7.573  1.515   0.60 14.02 ?  126 LEU   A HD11 1 
ATOM   2666 H  HD11 B LEU   A 1 126 ? 12.542 -7.479  0.781   0.40 18.34 ?  126 LEU   A HD11 1 
ATOM   2667 H  HD12 A LEU   A 1 126 ? 12.932 -6.044  1.181   0.60 14.02 ?  126 LEU   A HD12 1 
ATOM   2668 H  HD12 B LEU   A 1 126 ? 12.771 -5.946  0.432   0.40 18.34 ?  126 LEU   A HD12 1 
ATOM   2669 H  HD13 A LEU   A 1 126 ? 13.161 -7.154  0.068   0.60 14.02 ?  126 LEU   A HD13 1 
ATOM   2670 H  HD13 B LEU   A 1 126 ? 13.359 -7.074  -0.520  0.40 18.34 ?  126 LEU   A HD13 1 
ATOM   2671 H  HD21 A LEU   A 1 126 ? 14.463 -9.150  1.705   0.60 14.39 ?  126 LEU   A HD21 1 
ATOM   2672 H  HD21 B LEU   A 1 126 ? 14.352 -8.894  1.285   0.40 18.17 ?  126 LEU   A HD21 1 
ATOM   2673 H  HD22 A LEU   A 1 126 ? 15.195 -8.753  0.352   0.60 14.39 ?  126 LEU   A HD22 1 
ATOM   2674 H  HD22 B LEU   A 1 126 ? 15.534 -8.368  0.363   0.40 18.17 ?  126 LEU   A HD22 1 
ATOM   2675 H  HD23 A LEU   A 1 126 ? 15.976 -8.667  1.733   0.60 14.39 ?  126 LEU   A HD23 1 
ATOM   2676 H  HD23 B LEU   A 1 126 ? 15.673 -8.309  1.944   0.40 18.17 ?  126 LEU   A HD23 1 
ATOM   2677 N  N    A LEU   A 1 127 ? 18.898 -6.160  -0.152  0.60 11.27 ?  127 LEU   A N    1 
ATOM   2678 N  N    B LEU   A 1 127 ? 18.836 -5.947  -0.232  0.40 10.21 ?  127 LEU   A N    1 
ATOM   2679 C  CA   A LEU   A 1 127 ? 19.881 -5.678  -1.108  0.60 10.93 ?  127 LEU   A CA   1 
ATOM   2680 C  CA   B LEU   A 1 127 ? 19.832 -5.431  -1.161  0.40 10.36 ?  127 LEU   A CA   1 
ATOM   2681 C  C    A LEU   A 1 127 ? 19.245 -5.457  -2.472  0.60 10.23 ?  127 LEU   A C    1 
ATOM   2682 C  C    B LEU   A 1 127 ? 19.283 -5.361  -2.586  0.40 10.56 ?  127 LEU   A C    1 
ATOM   2683 O  O    A LEU   A 1 127 ? 18.396 -6.232  -2.925  0.60 10.58 ?  127 LEU   A O    1 
ATOM   2684 O  O    B LEU   A 1 127 ? 18.444 -6.165  -3.005  0.40 10.42 ?  127 LEU   A O    1 
ATOM   2685 C  CB   A LEU   A 1 127 ? 21.031 -6.675  -1.231  0.60 10.79 ?  127 LEU   A CB   1 
ATOM   2686 C  CB   B LEU   A 1 127 ? 21.094 -6.296  -1.129  0.40 10.90 ?  127 LEU   A CB   1 
ATOM   2687 C  CG   A LEU   A 1 127 ? 21.849 -6.898  0.039   0.60 10.36 ?  127 LEU   A CG   1 
ATOM   2688 C  CG   B LEU   A 1 127 ? 21.885 -6.276  0.182   0.40 11.48 ?  127 LEU   A CG   1 
ATOM   2689 C  CD1  A LEU   A 1 127 ? 22.962 -7.879  -0.251  0.60 10.55 ?  127 LEU   A CD1  1 
ATOM   2690 C  CD1  B LEU   A 1 127 ? 23.045 -7.247  0.112   0.40 12.22 ?  127 LEU   A CD1  1 
ATOM   2691 C  CD2  A LEU   A 1 127 ? 22.416 -5.595  0.569   0.60 10.68 ?  127 LEU   A CD2  1 
ATOM   2692 C  CD2  B LEU   A 1 127 ? 22.385 -4.867  0.498   0.40 12.01 ?  127 LEU   A CD2  1 
ATOM   2693 H  H    A LEU   A 1 127 ? 19.036 -6.966  0.123   0.60 13.50 ?  127 LEU   A H    1 
ATOM   2694 H  H    B LEU   A 1 127 ? 19.004 -6.734  0.087   0.40 12.22 ?  127 LEU   A H    1 
ATOM   2695 H  HA   A LEU   A 1 127 ? 20.239 -4.835  -0.803  0.60 13.09 ?  127 LEU   A HA   1 
ATOM   2696 H  HA   B LEU   A 1 127 ? 20.078 -4.535  -0.880  0.40 12.41 ?  127 LEU   A HA   1 
ATOM   2697 H  HB2  A LEU   A 1 127 ? 20.668 -7.536  -1.494  0.60 12.93 ?  127 LEU   A HB2  1 
ATOM   2698 H  HB2  B LEU   A 1 127 ? 20.843 -7.216  -1.300  0.40 13.06 ?  127 LEU   A HB2  1 
ATOM   2699 H  HB3  A LEU   A 1 127 ? 21.643 -6.360  -1.915  0.60 12.93 ?  127 LEU   A HB3  1 
ATOM   2700 H  HB3  B LEU   A 1 127 ? 21.691 -5.987  -1.828  0.40 13.06 ?  127 LEU   A HB3  1 
ATOM   2701 H  HG   A LEU   A 1 127 ? 21.277 -7.281  0.725   0.60 12.41 ?  127 LEU   A HG   1 
ATOM   2702 H  HG   B LEU   A 1 127 ? 21.304 -6.557  0.907   0.40 13.75 ?  127 LEU   A HG   1 
ATOM   2703 H  HD11 A LEU   A 1 127 ? 23.456 -8.047  0.568   0.60 12.64 ?  127 LEU   A HD11 1 
ATOM   2704 H  HD11 B LEU   A 1 127 ? 23.558 -7.183  0.933   0.40 14.64 ?  127 LEU   A HD11 1 
ATOM   2705 H  HD12 A LEU   A 1 127 ? 22.577 -8.706  -0.580  0.60 12.64 ?  127 LEU   A HD12 1 
ATOM   2706 H  HD12 B LEU   A 1 127 ? 22.697 -8.146  0.008   0.40 14.64 ?  127 LEU   A HD12 1 
ATOM   2707 H  HD13 A LEU   A 1 127 ? 23.550 -7.497  -0.920  0.60 12.64 ?  127 LEU   A HD13 1 
ATOM   2708 H  HD13 B LEU   A 1 127 ? 23.602 -7.015  -0.646  0.40 14.64 ?  127 LEU   A HD13 1 
ATOM   2709 H  HD21 A LEU   A 1 127 ? 23.060 -5.791  1.264   0.60 12.79 ?  127 LEU   A HD21 1 
ATOM   2710 H  HD21 B LEU   A 1 127 ? 23.012 -4.912  1.237   0.40 14.39 ?  127 LEU   A HD21 1 
ATOM   2711 H  HD22 A LEU   A 1 127 ? 22.848 -5.123  -0.161  0.60 12.79 ?  127 LEU   A HD22 1 
ATOM   2712 H  HD22 B LEU   A 1 127 ? 22.825 -4.506  -0.288  0.40 14.39 ?  127 LEU   A HD22 1 
ATOM   2713 H  HD23 A LEU   A 1 127 ? 21.692 -5.058  0.927   0.60 12.79 ?  127 LEU   A HD23 1 
ATOM   2714 H  HD23 B LEU   A 1 127 ? 21.629 -4.310  0.739   0.40 14.39 ?  127 LEU   A HD23 1 
ATOM   2715 N  N    A SER   A 1 128 ? 19.674 -4.383  -3.125  0.60 10.03 ?  128 SER   A N    1 
ATOM   2716 N  N    B SER   A 1 128 ? 19.777 -4.366  -3.324  0.40 11.12 ?  128 SER   A N    1 
ATOM   2717 C  CA   A SER   A 1 128 ? 19.254 -3.980  -4.462  0.60 10.18 ?  128 SER   A CA   1 
ATOM   2718 C  CA   B SER   A 1 128 ? 19.454 -4.118  -4.727  0.40 11.19 ?  128 SER   A CA   1 
ATOM   2719 C  C    A SER   A 1 128 ? 17.793 -3.551  -4.538  0.60 10.44 ?  128 SER   A C    1 
ATOM   2720 C  C    B SER   A 1 128 ? 18.031 -3.620  -4.963  0.40 11.35 ?  128 SER   A C    1 
ATOM   2721 O  O    A SER   A 1 128 ? 17.295 -3.295  -5.637  0.60 11.58 ?  128 SER   A O    1 
ATOM   2722 O  O    B SER   A 1 128 ? 17.696 -3.230  -6.086  0.40 11.61 ?  128 SER   A O    1 
ATOM   2723 C  CB   A SER   A 1 128 ? 19.592 -5.013  -5.544  0.60 9.93  ?  128 SER   A CB   1 
ATOM   2724 C  CB   B SER   A 1 128 ? 19.777 -5.330  -5.607  0.40 11.61 ?  128 SER   A CB   1 
ATOM   2725 O  OG   A SER   A 1 128 ? 20.997 -5.207  -5.620  0.60 10.31 ?  128 SER   A OG   1 
ATOM   2726 O  OG   B SER   A 1 128 ? 21.180 -5.495  -5.737  0.40 11.77 ?  128 SER   A OG   1 
ATOM   2727 H  H    A SER   A 1 128 ? 20.252 -3.832  -2.789  0.60 12.02 ?  128 SER   A H    1 
ATOM   2728 H  H    B SER   A 1 128 ? 20.343 -3.799  -3.014  0.40 13.32 ?  128 SER   A H    1 
ATOM   2729 H  HA   A SER   A 1 128 ? 19.772 -3.196  -4.682  0.60 12.19 ?  128 SER   A HA   1 
ATOM   2730 H  HA   B SER   A 1 128 ? 20.033 -3.407  -5.026  0.40 13.40 ?  128 SER   A HA   1 
ATOM   2731 H  HB2  A SER   A 1 128 ? 19.163 -5.853  -5.328  0.60 11.89 ?  128 SER   A HB2  1 
ATOM   2732 H  HB2  B SER   A 1 128 ? 19.402 -6.129  -5.213  0.40 13.91 ?  128 SER   A HB2  1 
ATOM   2733 H  HB3  A SER   A 1 128 ? 19.272 -4.685  -6.402  0.60 11.89 ?  128 SER   A HB3  1 
ATOM   2734 H  HB3  B SER   A 1 128 ? 19.403 -5.185  -6.491  0.40 13.91 ?  128 SER   A HB3  1 
ATOM   2735 H  HG   A SER   A 1 128 ? 21.379 -4.480  -5.799  0.60 12.35 ?  128 SER   A HG   1 
ATOM   2736 H  HG   B SER   A 1 128 ? 21.521 -4.801  -6.070  0.40 14.10 ?  128 SER   A HG   1 
ATOM   2737 N  N    A ALA   A 1 129 ? 17.102 -3.437  -3.405  0.60 10.47 ?  129 ALA   A N    1 
ATOM   2738 N  N    B ALA   A 1 129 ? 17.200 -3.592  -3.926  0.40 11.97 ?  129 ALA   A N    1 
ATOM   2739 C  CA   A ALA   A 1 129 ? 15.742 -2.927  -3.395  0.60 10.40 ?  129 ALA   A CA   1 
ATOM   2740 C  CA   B ALA   A 1 129 ? 15.836 -3.107  -4.066  0.40 12.70 ?  129 ALA   A CA   1 
ATOM   2741 C  C    A ALA   A 1 129 ? 15.765 -1.400  -3.421  0.60 10.74 ?  129 ALA   A C    1 
ATOM   2742 C  C    B ALA   A 1 129 ? 15.796 -1.596  -3.820  0.40 12.61 ?  129 ALA   A C    1 
ATOM   2743 O  O    A ALA   A 1 129 ? 16.822 -0.767  -3.516  0.60 11.24 ?  129 ALA   A O    1 
ATOM   2744 O  O    B ALA   A 1 129 ? 16.826 -0.917  -3.808  0.40 12.40 ?  129 ALA   A O    1 
ATOM   2745 C  CB   A ALA   A 1 129 ? 14.976 -3.484  -2.194  0.60 11.11 ?  129 ALA   A CB   1 
ATOM   2746 C  CB   B ALA   A 1 129 ? 14.898 -3.909  -3.166  0.40 13.43 ?  129 ALA   A CB   1 
ATOM   2747 H  H    A ALA   A 1 129 ? 17.402 -3.650  -2.625  0.60 12.54 ?  129 ALA   A H    1 
ATOM   2748 H  H    B ALA   A 1 129 ? 17.403 -3.851  -3.128  0.40 14.34 ?  129 ALA   A H    1 
ATOM   2749 H  HA   A ALA   A 1 129 ? 15.290 -3.222  -4.194  0.60 12.45 ?  129 ALA   A HA   1 
ATOM   2750 H  HA   B ALA   A 1 129 ? 15.555 -3.261  -4.979  0.40 15.21 ?  129 ALA   A HA   1 
ATOM   2751 H  HB1  A ALA   A 1 129 ? 14.068 -3.138  -2.207  0.60 13.31 ?  129 ALA   A HB1  1 
ATOM   2752 H  HB1  B ALA   A 1 129 ? 13.992 -3.590  -3.296  0.40 16.10 ?  129 ALA   A HB1  1 
ATOM   2753 H  HB2  A ALA   A 1 129 ? 14.959 -4.453  -2.253  0.60 13.31 ?  129 ALA   A HB2  1 
ATOM   2754 H  HB2  B ALA   A 1 129 ? 14.954 -4.848  -3.411  0.40 16.10 ?  129 ALA   A HB2  1 
ATOM   2755 H  HB3  A ALA   A 1 129 ? 15.420 -3.212  -1.375  0.60 13.31 ?  129 ALA   A HB3  1 
ATOM   2756 H  HB3  B ALA   A 1 129 ? 15.165 -3.791  -2.244  0.40 16.10 ?  129 ALA   A HB3  1 
ATOM   2757 N  N    A GLY   A 1 130 ? 14.583 -0.798  -3.352  0.60 11.66 ?  130 GLY   A N    1 
ATOM   2758 N  N    B GLY   A 1 130 ? 14.596 -1.053  -3.639  0.40 12.78 ?  130 GLY   A N    1 
ATOM   2759 C  CA   A GLY   A 1 130 ? 14.519 0.654   -3.345  0.60 12.86 ?  130 GLY   A CA   1 
ATOM   2760 C  CA   B GLY   A 1 130 ? 14.458 0.379   -3.458  0.40 13.17 ?  130 GLY   A CA   1 
ATOM   2761 C  C    A GLY   A 1 130 ? 15.163 1.238   -4.585  0.60 12.74 ?  130 GLY   A C    1 
ATOM   2762 C  C    B GLY   A 1 130 ? 14.971 1.116   -4.676  0.40 12.85 ?  130 GLY   A C    1 
ATOM   2763 O  O    A GLY   A 1 130 ? 14.930 0.779   -5.709  0.60 13.08 ?  130 GLY   A O    1 
ATOM   2764 O  O    B GLY   A 1 130 ? 14.719 0.724   -5.821  0.40 13.08 ?  130 GLY   A O    1 
ATOM   2765 H  H    A GLY   A 1 130 ? 13.819 -1.196  -3.309  0.60 13.97 ?  130 GLY   A H    1 
ATOM   2766 H  H    B GLY   A 1 130 ? 13.862 -1.491  -3.626  0.40 15.31 ?  130 GLY   A H    1 
ATOM   2767 H  HA2  A GLY   A 1 130 ? 13.592 0.944   -3.317  0.60 15.40 ?  130 GLY   A HA2  1 
ATOM   2768 H  HA2  B GLY   A 1 130 ? 13.519 0.597   -3.308  0.40 15.78 ?  130 GLY   A HA2  1 
ATOM   2769 H  HA3  A GLY   A 1 130 ? 14.976 1.002   -2.564  0.60 15.40 ?  130 GLY   A HA3  1 
ATOM   2770 H  HA3  B GLY   A 1 130 ? 14.968 0.667   -2.688  0.40 15.78 ?  130 GLY   A HA3  1 
ATOM   2771 N  N    A ILE   A 1 131 ? 16.001 2.260   -4.383  0.60 12.25 ?  131 ILE   A N    1 
ATOM   2772 N  N    B ILE   A 1 131 ? 15.717 2.195   -4.436  0.40 12.77 ?  131 ILE   A N    1 
ATOM   2773 C  CA   A ILE   A 1 131 ? 16.570 3.012   -5.498  0.60 11.79 ?  131 ILE   A CA   1 
ATOM   2774 C  CA   B ILE   A 1 131 ? 16.254 3.002   -5.529  0.40 12.78 ?  131 ILE   A CA   1 
ATOM   2775 C  C    A ILE   A 1 131 ? 17.553 2.211   -6.337  0.60 11.77 ?  131 ILE   A C    1 
ATOM   2776 C  C    B ILE   A 1 131 ? 17.351 2.279   -6.309  0.40 13.03 ?  131 ILE   A C    1 
ATOM   2777 O  O    A ILE   A 1 131 ? 17.925 2.670   -7.425  0.60 12.75 ?  131 ILE   A O    1 
ATOM   2778 O  O    B ILE   A 1 131 ? 17.851 2.805   -7.309  0.40 13.41 ?  131 ILE   A O    1 
ATOM   2779 C  CB   A ILE   A 1 131 ? 17.181 4.353   -5.038  0.60 12.81 ?  131 ILE   A CB   1 
ATOM   2780 C  CB   B ILE   A 1 131 ? 16.711 4.398   -5.061  0.40 13.50 ?  131 ILE   A CB   1 
ATOM   2781 C  CG1  A ILE   A 1 131 ? 18.436 4.134   -4.185  0.60 13.82 ?  131 ILE   A CG1  1 
ATOM   2782 C  CG1  B ILE   A 1 131 ? 17.865 4.312   -4.064  0.40 14.58 ?  131 ILE   A CG1  1 
ATOM   2783 C  CG2  A ILE   A 1 131 ? 16.142 5.174   -4.277  0.60 13.29 ?  131 ILE   A CG2  1 
ATOM   2784 C  CG2  B ILE   A 1 131 ? 15.549 5.167   -4.446  0.40 13.56 ?  131 ILE   A CG2  1 
ATOM   2785 C  CD1  A ILE   A 1 131 ? 19.091 5.436   -3.719  0.60 14.97 ?  131 ILE   A CD1  1 
ATOM   2786 C  CD1  B ILE   A 1 131 ? 18.344 5.680   -3.614  0.40 15.67 ?  131 ILE   A CD1  1 
ATOM   2787 H  H    A ILE   A 1 131 ? 16.255 2.536   -3.610  0.60 14.68 ?  131 ILE   A H    1 
ATOM   2788 H  H    B ILE   A 1 131 ? 15.896 2.493   -3.647  0.40 15.29 ?  131 ILE   A H    1 
ATOM   2789 H  HA   A ILE   A 1 131 ? 15.850 3.238   -6.094  0.60 14.13 ?  131 ILE   A HA   1 
ATOM   2790 H  HA   B ILE   A 1 131 ? 15.534 3.148   -6.152  0.40 15.32 ?  131 ILE   A HA   1 
ATOM   2791 H  HB   A ILE   A 1 131 ? 17.439 4.858   -5.826  0.60 15.35 ?  131 ILE   A HB   1 
ATOM   2792 H  HB   B ILE   A 1 131 ? 17.019 4.887   -5.839  0.40 16.17 ?  131 ILE   A HB   1 
ATOM   2793 H  HG12 A ILE   A 1 131 ? 18.198 3.627   -3.397  0.60 16.56 ?  131 ILE   A HG12 1 
ATOM   2794 H  HG12 B ILE   A 1 131 ? 17.570 3.824   -3.278  0.40 17.47 ?  131 ILE   A HG12 1 
ATOM   2795 H  HG13 A ILE   A 1 131 ? 19.095 3.652   -4.706  0.60 16.56 ?  131 ILE   A HG13 1 
ATOM   2796 H  HG13 B ILE   A 1 131 ? 18.612 3.855   -4.479  0.40 17.47 ?  131 ILE   A HG13 1 
ATOM   2797 H  HG21 A ILE   A 1 131 ? 16.473 6.080   -4.163  0.60 15.92 ?  131 ILE   A HG21 1 
ATOM   2798 H  HG21 B ILE   A 1 131 ? 15.802 6.098   -4.341  0.40 16.24 ?  131 ILE   A HG21 1 
ATOM   2799 H  HG22 A ILE   A 1 131 ? 15.319 5.186   -4.787  0.60 15.92 ?  131 ILE   A HG22 1 
ATOM   2800 H  HG22 B ILE   A 1 131 ? 14.782 5.101   -5.033  0.40 16.24 ?  131 ILE   A HG22 1 
ATOM   2801 H  HG23 A ILE   A 1 131 ? 15.991 4.765   -3.411  0.60 15.92 ?  131 ILE   A HG23 1 
ATOM   2802 H  HG23 B ILE   A 1 131 ? 15.338 4.780   -3.582  0.40 16.24 ?  131 ILE   A HG23 1 
ATOM   2803 H  HD11 A ILE   A 1 131 ? 19.948 5.233   -3.309  0.60 17.94 ?  131 ILE   A HD11 1 
ATOM   2804 H  HD11 B ILE   A 1 131 ? 19.305 5.667   -3.514  0.40 18.78 ?  131 ILE   A HD11 1 
ATOM   2805 H  HD12 A ILE   A 1 131 ? 19.225 6.019   -4.485  0.60 17.94 ?  131 ILE   A HD12 1 
ATOM   2806 H  HD12 B ILE   A 1 131 ? 18.091 6.337   -4.285  0.40 18.78 ?  131 ILE   A HD12 1 
ATOM   2807 H  HD13 A ILE   A 1 131 ? 18.513 5.873   -3.072  0.60 17.94 ?  131 ILE   A HD13 1 
ATOM   2808 H  HD13 B ILE   A 1 131 ? 17.921 5.901   -2.768  0.40 18.78 ?  131 ILE   A HD13 1 
ATOM   2809 N  N    A PHE   A 1 132 ? 17.981 1.031   -5.876  0.60 11.18 ?  132 PHE   A N    1 
ATOM   2810 N  N    B PHE   A 1 132 ? 17.730 1.069   -5.878  0.40 12.91 ?  132 PHE   A N    1 
ATOM   2811 C  CA   A PHE   A 1 132 ? 18.802 0.160   -6.712  0.60 11.30 ?  132 PHE   A CA   1 
ATOM   2812 C  CA   B PHE   A 1 132 ? 18.677 0.279   -6.660  0.40 13.10 ?  132 PHE   A CA   1 
ATOM   2813 C  C    A PHE   A 1 132 ? 17.981 -0.604  -7.749  0.60 11.84 ?  132 PHE   A C    1 
ATOM   2814 C  C    B PHE   A 1 132 ? 18.022 -0.432  -7.842  0.40 13.66 ?  132 PHE   A C    1 
ATOM   2815 O  O    A PHE   A 1 132 ? 18.566 -1.280  -8.600  0.60 12.09 ?  132 PHE   A O    1 
ATOM   2816 O  O    B PHE   A 1 132 ? 18.736 -0.884  -8.743  0.40 14.06 ?  132 PHE   A O    1 
ATOM   2817 C  CB   A PHE   A 1 132 ? 19.626 -0.816  -5.859  0.60 10.79 ?  132 PHE   A CB   1 
ATOM   2818 C  CB   B PHE   A 1 132 ? 19.401 -0.738  -5.775  0.40 12.83 ?  132 PHE   A CB   1 
ATOM   2819 C  CG   A PHE   A 1 132 ? 20.849 -0.200  -5.201  0.60 10.74 ?  132 PHE   A CG   1 
ATOM   2820 C  CG   B PHE   A 1 132 ? 20.613 -0.190  -5.065  0.40 12.65 ?  132 PHE   A CG   1 
ATOM   2821 C  CD1  A PHE   A 1 132 ? 20.730 0.840   -4.291  0.60 11.21 ?  132 PHE   A CD1  1 
ATOM   2822 C  CD1  B PHE   A 1 132 ? 20.483 0.743   -4.050  0.40 12.96 ?  132 PHE   A CD1  1 
ATOM   2823 C  CD2  A PHE   A 1 132 ? 22.118 -0.709  -5.458  0.60 11.88 ?  132 PHE   A CD2  1 
ATOM   2824 C  CD2  B PHE   A 1 132 ? 21.881 -0.643  -5.391  0.40 12.78 ?  132 PHE   A CD2  1 
ATOM   2825 C  CE1  A PHE   A 1 132 ? 21.855 1.381   -3.678  0.60 11.13 ?  132 PHE   A CE1  1 
ATOM   2826 C  CE1  B PHE   A 1 132 ? 21.598 1.231   -3.391  0.40 12.68 ?  132 PHE   A CE1  1 
ATOM   2827 C  CE2  A PHE   A 1 132 ? 23.242 -0.172  -4.849  0.60 12.55 ?  132 PHE   A CE2  1 
ATOM   2828 C  CE2  B PHE   A 1 132 ? 22.999 -0.160  -4.736  0.40 12.90 ?  132 PHE   A CE2  1 
ATOM   2829 C  CZ   A PHE   A 1 132 ? 23.108 0.873   -3.956  0.60 11.90 ?  132 PHE   A CZ   1 
ATOM   2830 C  CZ   B PHE   A 1 132 ? 22.856 0.780   -3.734  0.40 12.52 ?  132 PHE   A CZ   1 
ATOM   2831 H  H    A PHE   A 1 132 ? 17.819 0.718   -5.089  0.60 13.39 ?  132 PHE   A H    1 
ATOM   2832 H  H    B PHE   A 1 132 ? 17.473 0.690   -5.149  0.40 15.47 ?  132 PHE   A H    1 
ATOM   2833 H  HA   A PHE   A 1 132 ? 19.436 0.710   -7.193  0.60 13.53 ?  132 PHE   A HA   1 
ATOM   2834 H  HA   B PHE   A 1 132 ? 19.348 0.880   -7.018  0.40 15.70 ?  132 PHE   A HA   1 
ATOM   2835 H  HB2  A PHE   A 1 132 ? 19.065 -1.165  -5.152  0.60 12.93 ?  132 PHE   A HB2  1 
ATOM   2836 H  HB2  B PHE   A 1 132 ? 18.790 -1.055  -5.099  0.40 15.37 ?  132 PHE   A HB2  1 
ATOM   2837 H  HB3  A PHE   A 1 132 ? 19.936 -1.548  -6.423  0.60 12.93 ?  132 PHE   A HB3  1 
ATOM   2838 H  HB3  B PHE   A 1 132 ? 19.697 -1.477  -6.327  0.40 15.37 ?  132 PHE   A HB3  1 
ATOM   2839 H  HD1  A PHE   A 1 132 ? 19.895 1.186   -4.096  0.60 13.43 ?  132 PHE   A HD1  1 
ATOM   2840 H  HD1  B PHE   A 1 132 ? 19.638 1.052   -3.814  0.40 15.53 ?  132 PHE   A HD1  1 
ATOM   2841 H  HD2  A PHE   A 1 132 ? 22.221 -1.413  -6.059  0.60 14.24 ?  132 PHE   A HD2  1 
ATOM   2842 H  HD2  B PHE   A 1 132 ? 21.984 -1.273  -6.069  0.40 15.31 ?  132 PHE   A HD2  1 
ATOM   2843 H  HE1  A PHE   A 1 132 ? 21.768 2.087   -3.075  0.60 13.33 ?  132 PHE   A HE1  1 
ATOM   2844 H  HE1  B PHE   A 1 132 ? 21.498 1.861   -2.714  0.40 15.19 ?  132 PHE   A HE1  1 
ATOM   2845 H  HE2  A PHE   A 1 132 ? 24.087 -0.515  -5.041  0.60 15.04 ?  132 PHE   A HE2  1 
ATOM   2846 H  HE2  B PHE   A 1 132 ? 23.845 -0.467  -4.972  0.40 15.46 ?  132 PHE   A HE2  1 
ATOM   2847 H  HZ   A PHE   A 1 132 ? 23.864 1.239   -3.547  0.60 14.25 ?  132 PHE   A HZ   1 
ATOM   2848 H  HZ   B PHE   A 1 132 ? 23.605 1.106   -3.290  0.40 15.00 ?  132 PHE   A HZ   1 
ATOM   2849 N  N    A GLY   A 1 133 ? 16.651 -0.530  -7.692  0.60 12.24 ?  133 GLY   A N    1 
ATOM   2850 N  N    B GLY   A 1 133 ? 16.694 -0.561  -7.859  0.40 13.53 ?  133 GLY   A N    1 
ATOM   2851 C  CA   A GLY   A 1 133 ? 15.819 -0.900  -8.820  0.60 13.01 ?  133 GLY   A CA   1 
ATOM   2852 C  CA   B GLY   A 1 133 ? 15.976 -0.925  -9.064  0.40 13.36 ?  133 GLY   A CA   1 
ATOM   2853 C  C    A GLY   A 1 133 ? 15.531 -2.371  -9.019  0.60 13.54 ?  133 GLY   A C    1 
ATOM   2854 C  C    B GLY   A 1 133 ? 15.460 -2.349  -9.145  0.40 13.39 ?  133 GLY   A C    1 
ATOM   2855 O  O    A GLY   A 1 133 ? 14.921 -2.716  -10.037 0.60 15.03 ?  133 GLY   A O    1 
ATOM   2856 O  O    B GLY   A 1 133 ? 14.614 -2.622  -10.005 0.40 14.28 ?  133 GLY   A O    1 
ATOM   2857 H  H    A GLY   A 1 133 ? 16.208 -0.268  -7.004  0.60 14.67 ?  133 GLY   A H    1 
ATOM   2858 H  H    B GLY   A 1 133 ? 16.190 -0.441  -7.173  0.40 16.21 ?  133 GLY   A H    1 
ATOM   2859 H  HA2  A GLY   A 1 133 ? 14.967 -0.444  -8.736  0.60 15.58 ?  133 GLY   A HA2  1 
ATOM   2860 H  HA2  B GLY   A 1 133 ? 15.205 -0.349  -9.147  0.40 16.01 ?  133 GLY   A HA2  1 
ATOM   2861 H  HA3  A GLY   A 1 133 ? 16.241 -0.590  -9.634  0.60 15.58 ?  133 GLY   A HA3  1 
ATOM   2862 H  HA3  B GLY   A 1 133 ? 16.551 -0.763  -9.830  0.40 16.01 ?  133 GLY   A HA3  1 
ATOM   2863 N  N    A ALA   A 1 134 ? 15.945 -3.253  -8.113  0.60 13.04 ?  134 ALA   A N    1 
ATOM   2864 N  N    B ALA   A 1 134 ? 15.922 -3.259  -8.289  0.40 12.78 ?  134 ALA   A N    1 
ATOM   2865 C  CA   A ALA   A 1 134 ? 15.597 -4.657  -8.271  0.60 13.76 ?  134 ALA   A CA   1 
ATOM   2866 C  CA   B ALA   A 1 134 ? 15.532 -4.654  -8.431  0.40 12.97 ?  134 ALA   A CA   1 
ATOM   2867 C  C    A ALA   A 1 134 ? 14.241 -4.951  -7.629  0.60 14.38 ?  134 ALA   A C    1 
ATOM   2868 C  C    B ALA   A 1 134 ? 14.194 -4.919  -7.745  0.40 13.23 ?  134 ALA   A C    1 
ATOM   2869 O  O    A ALA   A 1 134 ? 13.719 -4.173  -6.827  0.60 15.51 ?  134 ALA   A O    1 
ATOM   2870 O  O    B ALA   A 1 134 ? 13.682 -4.106  -6.969  0.40 14.11 ?  134 ALA   A O    1 
ATOM   2871 C  CB   A ALA   A 1 134 ? 16.678 -5.564  -7.679  0.60 14.52 ?  134 ALA   A CB   1 
ATOM   2872 C  CB   B ALA   A 1 134 ? 16.614 -5.585  -7.882  0.40 13.50 ?  134 ALA   A CB   1 
ATOM   2873 H  H    A ALA   A 1 134 ? 16.436 -3.072  -7.419  0.60 15.62 ?  134 ALA   A H    1 
ATOM   2874 H  H    B ALA   A 1 134 ? 16.446 -3.093  -7.624  0.40 15.31 ?  134 ALA   A H    1 
ATOM   2875 H  HA   A ALA   A 1 134 ? 15.539 -4.854  -9.219  0.60 16.49 ?  134 ALA   A HA   1 
ATOM   2876 H  HA   B ALA   A 1 134 ? 15.417 -4.854  -9.367  0.40 15.54 ?  134 ALA   A HA   1 
ATOM   2877 H  HB1  A ALA   A 1 134 ? 16.429 -6.488  -7.833  0.60 17.40 ?  134 ALA   A HB1  1 
ATOM   2878 H  HB1  B ALA   A 1 134 ? 16.330 -6.505  -8.004  0.40 16.17 ?  134 ALA   A HB1  1 
ATOM   2879 H  HB2  A ALA   A 1 134 ? 17.524 -5.373  -8.118  0.60 17.40 ?  134 ALA   A HB2  1 
ATOM   2880 H  HB2  B ALA   A 1 134 ? 17.439 -5.428  -8.369  0.40 16.17 ?  134 ALA   A HB2  1 
ATOM   2881 H  HB3  A ALA   A 1 134 ? 16.752 -5.391  -6.730  0.60 17.40 ?  134 ALA   A HB3  1 
ATOM   2882 H  HB3  B ALA   A 1 134 ? 16.747 -5.402  -6.940  0.40 16.17 ?  134 ALA   A HB3  1 
ATOM   2883 N  N    A ASP   A 1 135 ? 13.676 -6.093  -8.004  0.60 15.10 ?  135 ASP   A N    1 
ATOM   2884 N  N    B ASP   A 1 135 ? 13.619 -6.078  -8.056  0.40 14.03 ?  135 ASP   A N    1 
ATOM   2885 C  CA   A ASP   A 1 135 ? 12.413 -6.562  -7.437  0.60 16.23 ?  135 ASP   A CA   1 
ATOM   2886 C  CA   B ASP   A 1 135 ? 12.370 -6.490  -7.433  0.40 15.29 ?  135 ASP   A CA   1 
ATOM   2887 C  C    A ASP   A 1 135 ? 12.647 -6.999  -5.995  0.60 15.50 ?  135 ASP   A C    1 
ATOM   2888 C  C    B ASP   A 1 135 ? 12.645 -6.965  -6.011  0.40 15.04 ?  135 ASP   A C    1 
ATOM   2889 O  O    A ASP   A 1 135 ? 13.412 -7.946  -5.769  0.60 15.19 ?  135 ASP   A O    1 
ATOM   2890 O  O    B ASP   A 1 135 ? 13.428 -7.903  -5.822  0.40 14.68 ?  135 ASP   A O    1 
ATOM   2891 C  CB   A ASP   A 1 135 ? 11.958 -7.754  -8.279  0.60 18.06 ?  135 ASP   A CB   1 
ATOM   2892 C  CB   B ASP   A 1 135 ? 11.719 -7.608  -8.232  0.40 16.71 ?  135 ASP   A CB   1 
ATOM   2893 C  CG   A ASP   A 1 135 ? 10.709 -8.444  -7.733  0.60 19.76 ?  135 ASP   A CG   1 
ATOM   2894 C  CG   B ASP   A 1 135 ? 10.301 -7.907  -7.773  0.40 17.89 ?  135 ASP   A CG   1 
ATOM   2895 O  OD1  A ASP   A 1 135 ? 10.120 -7.971  -6.738  0.60 19.96 ?  135 ASP   A OD1  1 
ATOM   2896 O  OD1  B ASP   A 1 135 ? 9.907  -7.440  -6.683  0.40 18.50 ?  135 ASP   A OD1  1 
ATOM   2897 O  OD2  A ASP   A 1 135 ? 10.319 -9.481  -8.311  0.60 21.68 -1 135 ASP   A OD2  1 
ATOM   2898 O  OD2  B ASP   A 1 135 ? 9.576  -8.608  -8.509  0.40 18.54 -1 135 ASP   A OD2  1 
ATOM   2899 H  H    A ASP   A 1 135 ? 14.006 -6.623  -8.595  0.60 18.09 ?  135 ASP   A H    1 
ATOM   2900 H  H    B ASP   A 1 135 ? 13.925 -6.636  -8.632  0.40 16.81 ?  135 ASP   A H    1 
ATOM   2901 H  HA   A ASP   A 1 135 ? 11.740 -5.859  -7.481  0.60 19.45 ?  135 ASP   A HA   1 
ATOM   2902 H  HA   B ASP   A 1 135 ? 11.759 -5.737  -7.421  0.40 18.33 ?  135 ASP   A HA   1 
ATOM   2903 H  HB2  A ASP   A 1 135 ? 11.780 -7.448  -9.185  0.60 21.64 ?  135 ASP   A HB2  1 
ATOM   2904 H  HB2  B ASP   A 1 135 ? 11.697 -7.358  -9.170  0.40 20.02 ?  135 ASP   A HB2  1 
ATOM   2905 H  HB3  A ASP   A 1 135 ? 12.667 -8.414  -8.290  0.60 21.64 ?  135 ASP   A HB3  1 
ATOM   2906 H  HB3  B ASP   A 1 135 ? 12.229 -8.423  -8.119  0.40 20.02 ?  135 ASP   A HB3  1 
ATOM   2907 N  N    . PRO   A 1 136 ? 12.040 -6.349  -4.994  1.00 15.21 ?  136 PRO   A N    1 
ATOM   2908 C  CA   . PRO   A 1 136 ? 12.287 -6.787  -3.609  1.00 15.26 ?  136 PRO   A CA   1 
ATOM   2909 C  C    . PRO   A 1 136 ? 11.857 -8.215  -3.315  1.00 14.14 ?  136 PRO   A C    1 
ATOM   2910 O  O    . PRO   A 1 136 ? 12.453 -8.857  -2.444  1.00 13.57 ?  136 PRO   A O    1 
ATOM   2911 C  CB   . PRO   A 1 136 ? 11.504 -5.763  -2.774  1.00 16.55 ?  136 PRO   A CB   1 
ATOM   2912 C  CG   . PRO   A 1 136 ? 10.495 -5.184  -3.722  1.00 17.77 ?  136 PRO   A CG   1 
ATOM   2913 C  CD   . PRO   A 1 136 ? 11.151 -5.175  -5.054  1.00 16.83 ?  136 PRO   A CD   1 
ATOM   2914 H  HA   . PRO   A 1 136 ? 13.234 -6.700  -3.398  1.00 18.29 ?  136 PRO   A HA   1 
ATOM   2915 H  HB2  . PRO   A 1 136 ? 11.065 -6.214  -2.035  1.00 19.84 ?  136 PRO   A HB2  1 
ATOM   2916 H  HB3  . PRO   A 1 136 ? 12.108 -5.077  -2.448  1.00 19.84 ?  136 PRO   A HB3  1 
ATOM   2917 H  HG2  . PRO   A 1 136 ? 9.708  -5.747  -3.743  1.00 21.30 ?  136 PRO   A HG2  1 
ATOM   2918 H  HG3  . PRO   A 1 136 ? 10.272 -4.284  -3.451  1.00 21.30 ?  136 PRO   A HG3  1 
ATOM   2919 H  HD2  . PRO   A 1 136 ? 10.487 -5.287  -5.754  1.00 20.17 ?  136 PRO   A HD2  1 
ATOM   2920 H  HD3  . PRO   A 1 136 ? 11.668 -4.360  -5.183  1.00 20.17 ?  136 PRO   A HD3  1 
ATOM   2921 N  N    A ILE   A 1 137 ? 10.828 -8.728  -3.993  0.60 14.22 ?  137 ILE   A N    1 
ATOM   2922 N  N    B ILE   A 1 137 ? 10.823 -8.718  -3.993  0.40 14.43 ?  137 ILE   A N    1 
ATOM   2923 C  CA   A ILE   A 1 137 ? 10.445 -10.123 -3.792  0.60 14.62 ?  137 ILE   A CA   1 
ATOM   2924 C  CA   B ILE   A 1 137 ? 10.438 -10.119 -3.832  0.40 14.96 ?  137 ILE   A CA   1 
ATOM   2925 C  C    A ILE   A 1 137 ? 11.585 -11.046 -4.204  0.60 14.26 ?  137 ILE   A C    1 
ATOM   2926 C  C    B ILE   A 1 137 ? 11.610 -11.021 -4.191  0.40 14.57 ?  137 ILE   A C    1 
ATOM   2927 O  O    A ILE   A 1 137 ? 11.879 -12.042 -3.529  0.60 14.28 ?  137 ILE   A O    1 
ATOM   2928 O  O    B ILE   A 1 137 ? 11.935 -11.977 -3.475  0.40 14.64 ?  137 ILE   A O    1 
ATOM   2929 C  CB   A ILE   A 1 137 ? 9.139  -10.434 -4.547  0.60 15.75 ?  137 ILE   A CB   1 
ATOM   2930 C  CB   B ILE   A 1 137 ? 9.205  -10.440 -4.698  0.40 16.24 ?  137 ILE   A CB   1 
ATOM   2931 C  CG1  A ILE   A 1 137 ? 7.968  -9.639  -3.954  0.60 16.92 ?  137 ILE   A CG1  1 
ATOM   2932 C  CG1  B ILE   A 1 137 ? 8.061  -9.461  -4.426  0.40 17.39 ?  137 ILE   A CG1  1 
ATOM   2933 C  CG2  A ILE   A 1 137 ? 8.849  -11.931 -4.516  0.60 16.97 ?  137 ILE   A CG2  1 
ATOM   2934 C  CG2  B ILE   A 1 137 ? 8.750  -11.874 -4.456  0.40 16.97 ?  137 ILE   A CG2  1 
ATOM   2935 C  CD1  A ILE   A 1 137 ? 6.666  -9.805  -4.708  0.60 18.14 ?  137 ILE   A CD1  1 
ATOM   2936 C  CD1  B ILE   A 1 137 ? 6.843  -9.717  -5.293  0.40 18.39 ?  137 ILE   A CD1  1 
ATOM   2937 H  H    A ILE   A 1 137 ? 10.350 -8.297  -4.563  0.60 17.04 ?  137 ILE   A H    1 
ATOM   2938 H  H    B ILE   A 1 137 ? 10.341 -8.271  -4.546  0.40 17.29 ?  137 ILE   A H    1 
ATOM   2939 H  HA   A ILE   A 1 137 ? 10.282 -10.266 -2.850  0.60 17.52 ?  137 ILE   A HA   1 
ATOM   2940 H  HA   B ILE   A 1 137 ? 10.205 -10.281 -2.906  0.40 17.93 ?  137 ILE   A HA   1 
ATOM   2941 H  HB   A ILE   A 1 137 ? 9.246  -10.162 -5.469  0.60 18.88 ?  137 ILE   A HB   1 
ATOM   2942 H  HB   B ILE   A 1 137 ? 9.456  -10.355 -5.629  0.40 19.47 ?  137 ILE   A HB   1 
ATOM   2943 H  HG12 A ILE   A 1 137 ? 7.819  -9.926  -3.040  0.60 20.28 ?  137 ILE   A HG12 1 
ATOM   2944 H  HG12 B ILE   A 1 137 ? 7.792  -9.538  -3.498  0.40 20.85 ?  137 ILE   A HG12 1 
ATOM   2945 H  HG13 A ILE   A 1 137 ? 8.194  -8.691  -3.964  0.60 20.28 ?  137 ILE   A HG13 1 
ATOM   2946 H  HG13 B ILE   A 1 137 ? 8.362  -8.555  -4.608  0.40 20.85 ?  137 ILE   A HG13 1 
ATOM   2947 H  HG21 A ILE   A 1 137 ? 8.027  -12.111 -4.998  0.60 20.34 ?  137 ILE   A HG21 1 
ATOM   2948 H  HG21 B ILE   A 1 137 ? 8.052  -12.103 -5.089  0.40 20.34 ?  137 ILE   A HG21 1 
ATOM   2949 H  HG22 A ILE   A 1 137 ? 9.572  -12.407 -4.944  0.60 20.34 ?  137 ILE   A HG22 1 
ATOM   2950 H  HG22 B ILE   A 1 137 ? 9.501  -12.472 -4.578  0.40 20.34 ?  137 ILE   A HG22 1 
ATOM   2951 H  HG23 A ILE   A 1 137 ? 8.758  -12.213 -3.594  0.60 20.34 ?  137 ILE   A HG23 1 
ATOM   2952 H  HG23 B ILE   A 1 137 ? 8.413  -11.945 -3.551  0.40 20.34 ?  137 ILE   A HG23 1 
ATOM   2953 H  HD11 A ILE   A 1 137 ? 5.961  -9.434  -4.165  0.60 21.75 ?  137 ILE   A HD11 1 
ATOM   2954 H  HD11 B ILE   A 1 137 ? 6.097  -9.967  -4.724  0.40 22.04 ?  137 ILE   A HD11 1 
ATOM   2955 H  HD12 A ILE   A 1 137 ? 6.725  -9.332  -5.555  0.60 21.75 ?  137 ILE   A HD12 1 
ATOM   2956 H  HD12 B ILE   A 1 137 ? 6.635  -8.911  -5.785  0.40 22.04 ?  137 ILE   A HD12 1 
ATOM   2957 H  HD13 A ILE   A 1 137 ? 6.489  -10.744 -4.866  0.60 21.75 ?  137 ILE   A HD13 1 
ATOM   2958 H  HD13 B ILE   A 1 137 ? 7.037  -10.432 -5.919  0.40 22.04 ?  137 ILE   A HD13 1 
ATOM   2959 N  N    A HIS   A 1 138 ? 12.239 -10.730 -5.323  0.60 14.21 ?  138 HIS   A N    1 
ATOM   2960 N  N    B HIS   A 1 138 ? 12.251 -10.730 -5.323  0.40 14.29 ?  138 HIS   A N    1 
ATOM   2961 C  CA   A HIS   A 1 138 ? 13.402 -11.502 -5.744  0.60 14.27 ?  138 HIS   A CA   1 
ATOM   2962 C  CA   B HIS   A 1 138 ? 13.409 -11.502 -5.751  0.40 14.10 ?  138 HIS   A CA   1 
ATOM   2963 C  C    A HIS   A 1 138 ? 14.547 -11.363 -4.748  0.60 13.22 ?  138 HIS   A C    1 
ATOM   2964 C  C    B HIS   A 1 138 ? 14.561 -11.360 -4.764  0.40 13.29 ?  138 HIS   A C    1 
ATOM   2965 O  O    A HIS   A 1 138 ? 15.202 -12.353 -4.402  0.60 13.31 ?  138 HIS   A O    1 
ATOM   2966 O  O    B HIS   A 1 138 ? 15.235 -12.345 -4.440  0.40 13.38 ?  138 HIS   A O    1 
ATOM   2967 C  CB   A HIS   A 1 138 ? 13.833 -11.068 -7.144  0.60 15.09 ?  138 HIS   A CB   1 
ATOM   2968 C  CB   B HIS   A 1 138 ? 13.824 -11.049 -7.150  0.40 14.62 ?  138 HIS   A CB   1 
ATOM   2969 C  CG   A HIS   A 1 138 ? 15.078 -11.743 -7.620  0.60 16.08 ?  138 HIS   A CG   1 
ATOM   2970 C  CG   B HIS   A 1 138 ? 15.118 -11.635 -7.612  0.40 15.28 ?  138 HIS   A CG   1 
ATOM   2971 N  ND1  A HIS   A 1 138 ? 15.149 -13.101 -7.846  0.60 17.26 ?  138 HIS   A ND1  1 
ATOM   2972 N  ND1  B HIS   A 1 138 ? 15.266 -12.972 -7.913  0.40 16.13 ?  138 HIS   A ND1  1 
ATOM   2973 C  CD2  A HIS   A 1 138 ? 16.307 -11.249 -7.901  0.60 16.28 ?  138 HIS   A CD2  1 
ATOM   2974 C  CD2  B HIS   A 1 138 ? 16.327 -11.065 -7.821  0.40 15.35 ?  138 HIS   A CD2  1 
ATOM   2975 C  CE1  A HIS   A 1 138 ? 16.366 -13.413 -8.254  0.60 17.54 ?  138 HIS   A CE1  1 
ATOM   2976 C  CE1  B HIS   A 1 138 ? 16.511 -13.199 -8.291  0.40 16.16 ?  138 HIS   A CE1  1 
ATOM   2977 N  NE2  A HIS   A 1 138 ? 17.089 -12.308 -8.295  0.60 16.83 ?  138 HIS   A NE2  1 
ATOM   2978 N  NE2  B HIS   A 1 138 ? 17.176 -12.059 -8.243  0.40 15.75 ?  138 HIS   A NE2  1 
ATOM   2979 H  H    A HIS   A 1 138 ? 12.029 -10.079 -5.852  0.60 17.02 ?  138 HIS   A H    1 
ATOM   2980 H  H    B HIS   A 1 138 ? 12.031 -10.090 -5.858  0.40 17.13 ?  138 HIS   A H    1 
ATOM   2981 H  HA   A HIS   A 1 138 ? 13.154 -12.436 -5.792  0.60 17.09 ?  138 HIS   A HA   1 
ATOM   2982 H  HA   B HIS   A 1 138 ? 13.164 -12.438 -5.800  0.40 16.90 ?  138 HIS   A HA   1 
ATOM   2983 H  HB2  A HIS   A 1 138 ? 13.122 -11.281 -7.775  0.60 18.08 ?  138 HIS   A HB2  1 
ATOM   2984 H  HB2  B HIS   A 1 138 ? 13.135 -11.316 -7.783  0.40 17.52 ?  138 HIS   A HB2  1 
ATOM   2985 H  HB3  A HIS   A 1 138 ? 13.993 -10.112 -7.146  0.60 18.08 ?  138 HIS   A HB3  1 
ATOM   2986 H  HB3  B HIS   A 1 138 ? 13.915 -10.084 -7.155  0.40 17.52 ?  138 HIS   A HB3  1 
ATOM   2987 H  HD1  A HIS   A 1 138 ? 14.501 -13.657 -7.744  0.60 20.69 ?  138 HIS   A HD1  1 
ATOM   2988 H  HD2  A HIS   A 1 138 ? 16.571 -10.359 -7.841  0.60 19.52 ?  138 HIS   A HD2  1 
ATOM   2989 H  HD2  B HIS   A 1 138 ? 16.541 -10.168 -7.701  0.40 18.40 ?  138 HIS   A HD2  1 
ATOM   2990 H  HE1  A HIS   A 1 138 ? 16.665 -14.266 -8.472  0.60 21.02 ?  138 HIS   A HE1  1 
ATOM   2991 H  HE1  B HIS   A 1 138 ? 16.860 -14.023 -8.545  0.40 19.37 ?  138 HIS   A HE1  1 
ATOM   2992 H  HE2  B HIS   A 1 138 ? 18.005 -11.956 -8.442  0.40 18.88 ?  138 HIS   A HE2  1 
ATOM   2993 N  N    . SER   A 1 139 ? 14.796 -10.145 -4.267  1.00 12.82 ?  139 SER   A N    1 
ATOM   2994 C  CA   . SER   A 1 139 ? 15.875 -9.950  -3.308  1.00 12.37 ?  139 SER   A CA   1 
ATOM   2995 C  C    . SER   A 1 139 ? 15.660 -10.787 -2.054  1.00 11.74 ?  139 SER   A C    1 
ATOM   2996 O  O    . SER   A 1 139 ? 16.609 -11.378 -1.527  1.00 11.89 ?  139 SER   A O    1 
ATOM   2997 C  CB   . SER   A 1 139 ? 16.006 -8.471  -2.957  1.00 12.40 ?  139 SER   A CB   1 
ATOM   2998 O  OG   . SER   A 1 139 ? 17.094 -8.302  -2.073  1.00 12.62 ?  139 SER   A OG   1 
ATOM   2999 H  H    A SER   A 1 139 ? 14.361 -9.432  -4.476  0.60 15.36 ?  139 SER   A H    1 
ATOM   3000 H  H    B SER   A 1 139 ? 14.352 -9.435  -4.467  0.40 15.36 ?  139 SER   A H    1 
ATOM   3001 H  HA   . SER   A 1 139 ? 16.709 -10.230 -3.715  1.00 14.83 ?  139 SER   A HA   1 
ATOM   3002 H  HB2  . SER   A 1 139 ? 16.158 -7.956  -3.769  1.00 14.85 ?  139 SER   A HB2  1 
ATOM   3003 H  HB3  . SER   A 1 139 ? 15.191 -8.168  -2.520  1.00 14.85 ?  139 SER   A HB3  1 
ATOM   3004 H  HG   . SER   A 1 139 ? 17.184 -7.489  -1.878  1.00 15.12 ?  139 SER   A HG   1 
ATOM   3005 N  N    . LEU   A 1 140 ? 14.422 -10.845 -1.561  1.00 11.71 ?  140 LEU   A N    1 
ATOM   3006 C  CA   . LEU   A 1 140 ? 14.145 -11.654 -0.380  1.00 11.63 ?  140 LEU   A CA   1 
ATOM   3007 C  C    . LEU   A 1 140 ? 14.414 -13.131 -0.654  1.00 11.68 ?  140 LEU   A C    1 
ATOM   3008 O  O    . LEU   A 1 140 ? 14.963 -13.842 0.198   1.00 12.24 ?  140 LEU   A O    1 
ATOM   3009 C  CB   . LEU   A 1 140 ? 12.702 -11.433 0.070   1.00 11.82 ?  140 LEU   A CB   1 
ATOM   3010 C  CG   . LEU   A 1 140 ? 12.247 -12.279 1.255   1.00 12.50 ?  140 LEU   A CG   1 
ATOM   3011 C  CD1  . LEU   A 1 140 ? 13.154 -12.111 2.464   1.00 12.97 ?  140 LEU   A CD1  1 
ATOM   3012 C  CD2  . LEU   A 1 140 ? 10.799 -11.963 1.620   1.00 13.53 ?  140 LEU   A CD2  1 
ATOM   3013 H  H    . LEU   A 1 140 ? 13.739 -10.430 -1.885  1.00 14.02 ?  140 LEU   A H    1 
ATOM   3014 H  HA   . LEU   A 1 140 ? 14.726 -11.372 0.339   1.00 13.93 ?  140 LEU   A HA   1 
ATOM   3015 H  HB2  . LEU   A 1 140 ? 12.594 -10.507 0.323   1.00 14.16 ?  140 LEU   A HB2  1 
ATOM   3016 H  HB3  . LEU   A 1 140 ? 12.112 -11.639 -0.673  1.00 14.16 ?  140 LEU   A HB3  1 
ATOM   3017 H  HG   . LEU   A 1 140 ? 12.269 -13.217 0.997   1.00 14.97 ?  140 LEU   A HG   1 
ATOM   3018 H  HD11 . LEU   A 1 140 ? 12.768 -12.587 3.216   1.00 15.54 ?  140 LEU   A HD11 1 
ATOM   3019 H  HD12 . LEU   A 1 140 ? 14.025 -12.486 2.251   1.00 15.54 ?  140 LEU   A HD12 1 
ATOM   3020 H  HD13 . LEU   A 1 140 ? 13.234 -11.172 2.667   1.00 15.54 ?  140 LEU   A HD13 1 
ATOM   3021 H  HD21 . LEU   A 1 140 ? 10.532 -12.520 2.374   1.00 16.21 ?  140 LEU   A HD21 1 
ATOM   3022 H  HD22 . LEU   A 1 140 ? 10.728 -11.029 1.861   1.00 16.21 ?  140 LEU   A HD22 1 
ATOM   3023 H  HD23 . LEU   A 1 140 ? 10.228 -12.155 0.858   1.00 16.21 ?  140 LEU   A HD23 1 
ATOM   3024 N  N    . ARG   A 1 141 ? 14.023 -13.610 -1.839  1.00 12.56 ?  141 ARG   A N    1 
ATOM   3025 C  CA   . ARG   A 1 141 ? 14.259 -15.000 -2.209  1.00 13.54 ?  141 ARG   A CA   1 
ATOM   3026 C  C    . ARG   A 1 141 ? 15.752 -15.309 -2.236  1.00 12.63 ?  141 ARG   A C    1 
ATOM   3027 O  O    . ARG   A 1 141 ? 16.202 -16.322 -1.686  1.00 12.76 ?  141 ARG   A O    1 
ATOM   3028 C  CB   . ARG   A 1 141 ? 13.621 -15.250 -3.577  1.00 15.61 ?  141 ARG   A CB   1 
ATOM   3029 C  CG   . ARG   A 1 141 ? 13.604 -16.690 -4.028  1.00 18.55 ?  141 ARG   A CG   1 
ATOM   3030 C  CD   . ARG   A 1 141 ? 12.569 -17.458 -3.273  1.00 20.66 ?  141 ARG   A CD   1 
ATOM   3031 N  NE   . ARG   A 1 141 ? 13.176 -18.263 -2.227  1.00 21.34 ?  141 ARG   A NE   1 
ATOM   3032 C  CZ   . ARG   A 1 141 ? 12.496 -18.826 -1.237  1.00 22.30 ?  141 ARG   A CZ   1 
ATOM   3033 N  NH1  . ARG   A 1 141 ? 11.208 -18.584 -1.058  1.00 22.05 ?  141 ARG   A NH1  1 
ATOM   3034 N  NH2  . ARG   A 1 141 ? 13.127 -19.644 -0.401  1.00 23.16 ?  141 ARG   A NH2  1 
ATOM   3035 H  H    . ARG   A 1 141 ? 13.622 -13.147 -2.445  1.00 15.05 ?  141 ARG   A H    1 
ATOM   3036 H  HA   . ARG   A 1 141 ? 13.838 -15.583 -1.561  1.00 16.23 ?  141 ARG   A HA   1 
ATOM   3037 H  HB2  . ARG   A 1 141 ? 12.706 -14.931 -3.555  1.00 18.71 ?  141 ARG   A HB2  1 
ATOM   3038 H  HB3  . ARG   A 1 141 ? 14.120 -14.744 -4.240  1.00 18.71 ?  141 ARG   A HB3  1 
ATOM   3039 H  HG2  . ARG   A 1 141 ? 13.391 -16.730 -4.975  1.00 22.23 ?  141 ARG   A HG2  1 
ATOM   3040 H  HG3  . ARG   A 1 141 ? 14.472 -17.095 -3.863  1.00 22.23 ?  141 ARG   A HG3  1 
ATOM   3041 H  HD2  . ARG   A 1 141 ? 11.948 -16.841 -2.851  1.00 24.77 ?  141 ARG   A HD2  1 
ATOM   3042 H  HD3  . ARG   A 1 141 ? 12.092 -18.043 -3.883  1.00 24.77 ?  141 ARG   A HD3  1 
ATOM   3043 H  HE   . ARG   A 1 141 ? 13.999 -18.488 -2.323  1.00 25.59 ?  141 ARG   A HE   1 
ATOM   3044 H  HH11 . ARG   A 1 141 ? 10.782 -18.067 -1.598  1.00 26.43 ?  141 ARG   A HH11 1 
ATOM   3045 H  HH12 . ARG   A 1 141 ? 10.786 -18.959 -0.407  1.00 26.43 ?  141 ARG   A HH12 1 
ATOM   3046 H  HH21 . ARG   A 1 141 ? 13.964 -19.806 -0.507  1.00 27.77 ?  141 ARG   A HH21 1 
ATOM   3047 H  HH22 . ARG   A 1 141 ? 12.699 -20.007 0.253   1.00 27.77 ?  141 ARG   A HH22 1 
ATOM   3048 N  N    . VAL   A 1 142 ? 16.540 -14.444 -2.877  1.00 12.03 ?  142 VAL   A N    1 
ATOM   3049 C  CA   . VAL   A 1 142 ? 17.985 -14.657 -2.914  1.00 12.03 ?  142 VAL   A CA   1 
ATOM   3050 C  C    . VAL   A 1 142 ? 18.559 -14.636 -1.504  1.00 11.41 ?  142 VAL   A C    1 
ATOM   3051 O  O    . VAL   A 1 142 ? 19.425 -15.448 -1.159  1.00 11.78 ?  142 VAL   A O    1 
ATOM   3052 C  CB   . VAL   A 1 142 ? 18.677 -13.640 -3.840  1.00 12.19 ?  142 VAL   A CB   1 
ATOM   3053 C  CG1  . VAL   A 1 142 ? 20.189 -13.864 -3.822  1.00 12.32 ?  142 VAL   A CG1  1 
ATOM   3054 C  CG2  . VAL   A 1 142 ? 18.153 -13.758 -5.262  1.00 13.81 ?  142 VAL   A CG2  1 
ATOM   3055 H  H    . VAL   A 1 142 ? 16.270 -13.731 -3.288  1.00 14.41 ?  142 VAL   A H    1 
ATOM   3056 H  HA   . VAL   A 1 142 ? 18.152 -15.532 -3.287  1.00 14.41 ?  142 VAL   A HA   1 
ATOM   3057 H  HB   . VAL   A 1 142 ? 18.506 -12.734 -3.526  1.00 14.60 ?  142 VAL   A HB   1 
ATOM   3058 H  HG11 . VAL   A 1 142 ? 20.593 -13.376 -4.558  1.00 14.76 ?  142 VAL   A HG11 1 
ATOM   3059 H  HG12 . VAL   A 1 142 ? 20.551 -13.542 -2.979  1.00 14.76 ?  142 VAL   A HG12 1 
ATOM   3060 H  HG13 . VAL   A 1 142 ? 20.367 -14.812 -3.918  1.00 14.76 ?  142 VAL   A HG13 1 
ATOM   3061 H  HG21 . VAL   A 1 142 ? 18.615 -13.112 -5.822  1.00 16.54 ?  142 VAL   A HG21 1 
ATOM   3062 H  HG22 . VAL   A 1 142 ? 18.330 -14.656 -5.582  1.00 16.54 ?  142 VAL   A HG22 1 
ATOM   3063 H  HG23 . VAL   A 1 142 ? 17.205 -13.581 -5.262  1.00 16.54 ?  142 VAL   A HG23 1 
ATOM   3064 N  N    . CYS   A 1 143 ? 18.095 -13.710 -0.668  1.00 11.31 ?  143 CYS   A N    1 
ATOM   3065 C  CA   . CYS   A 1 143 ? 18.562 -13.666 0.713   1.00 11.42 ?  143 CYS   A CA   1 
ATOM   3066 C  C    . CYS   A 1 143 ? 18.337 -15.004 1.408   1.00 11.69 ?  143 CYS   A C    1 
ATOM   3067 O  O    . CYS   A 1 143 ? 19.259 -15.587 1.987   1.00 11.61 ?  143 CYS   A O    1 
ATOM   3068 C  CB   . CYS   A 1 143 ? 17.833 -12.552 1.461   1.00 11.83 ?  143 CYS   A CB   1 
ATOM   3069 S  SG   . CYS   A 1 143 ? 18.331 -12.369 3.182   1.00 12.36 ?  143 CYS   A SG   1 
ATOM   3070 H  H    . CYS   A 1 143 ? 17.518 -13.109 -0.876  1.00 13.54 ?  143 CYS   A H    1 
ATOM   3071 H  HA   . CYS   A 1 143 ? 19.510 -13.476 0.721   1.00 13.68 ?  143 CYS   A HA   1 
ATOM   3072 H  HB2  . CYS   A 1 143 ? 18.001 -11.710 1.009   1.00 14.17 ?  143 CYS   A HB2  1 
ATOM   3073 H  HB3  . CYS   A 1 143 ? 16.883 -12.740 1.448   1.00 14.17 ?  143 CYS   A HB3  1 
ATOM   3074 H  HG   . CYS   A 1 143 ? 17.776 -11.417 3.648   1.00 14.81 ?  143 CYS   A HG   1 
ATOM   3075 N  N    . VAL   A 1 144 ? 17.107 -15.505 1.357   1.00 12.09 ?  144 VAL   A N    1 
ATOM   3076 C  CA   . VAL   A 1 144 ? 16.770 -16.736 2.062   1.00 13.29 ?  144 VAL   A CA   1 
ATOM   3077 C  C    . VAL   A 1 144 ? 17.576 -17.910 1.527   1.00 12.89 ?  144 VAL   A C    1 
ATOM   3078 O  O    . VAL   A 1 144 ? 17.951 -18.819 2.280   1.00 13.54 ?  144 VAL   A O    1 
ATOM   3079 C  CB   . VAL   A 1 144 ? 15.252 -16.970 1.954   1.00 16.31 ?  144 VAL   A CB   1 
ATOM   3080 C  CG1  . VAL   A 1 144 ? 14.889 -18.399 2.288   1.00 18.13 ?  144 VAL   A CG1  1 
ATOM   3081 C  CG2  . VAL   A 1 144 ? 14.514 -15.968 2.844   1.00 16.51 ?  144 VAL   A CG2  1 
ATOM   3082 H  H    . VAL   A 1 144 ? 16.451 -15.153 0.916   1.00 14.48 ?  144 VAL   A H    1 
ATOM   3083 H  HA   . VAL   A 1 144 ? 16.984 -16.625 2.995   1.00 15.93 ?  144 VAL   A HA   1 
ATOM   3084 H  HB   . VAL   A 1 144 ? 14.974 -16.802 1.038   1.00 19.55 ?  144 VAL   A HB   1 
ATOM   3085 H  HG11 . VAL   A 1 144 ? 13.934 -18.446 2.469   1.00 21.73 ?  144 VAL   A HG11 1 
ATOM   3086 H  HG12 . VAL   A 1 144 ? 15.105 -18.968 1.534   1.00 21.73 ?  144 VAL   A HG12 1 
ATOM   3087 H  HG13 . VAL   A 1 144 ? 15.385 -18.676 3.072   1.00 21.73 ?  144 VAL   A HG13 1 
ATOM   3088 H  HG21 . VAL   A 1 144 ? 13.556 -16.122 2.774   1.00 19.79 ?  144 VAL   A HG21 1 
ATOM   3089 H  HG22 . VAL   A 1 144 ? 14.800 -16.083 3.762   1.00 19.79 ?  144 VAL   A HG22 1 
ATOM   3090 H  HG23 . VAL   A 1 144 ? 14.718 -15.064 2.546   1.00 19.79 ?  144 VAL   A HG23 1 
ATOM   3091 N  N    . ASP   A 1 145 ? 17.846 -17.920 0.224   1.00 13.07 ?  145 ASP   A N    1 
ATOM   3092 C  CA   . ASP   A 1 145 ? 18.548 -19.027 -0.413  1.00 13.77 ?  145 ASP   A CA   1 
ATOM   3093 C  C    . ASP   A 1 145 ? 20.067 -18.885 -0.377  1.00 13.17 ?  145 ASP   A C    1 
ATOM   3094 O  O    . ASP   A 1 145 ? 20.768 -19.780 -0.862  1.00 15.18 ?  145 ASP   A O    1 
ATOM   3095 C  CB   . ASP   A 1 145 ? 18.093 -19.165 -1.869  1.00 15.63 ?  145 ASP   A CB   1 
ATOM   3096 C  CG   . ASP   A 1 145 ? 16.647 -19.605 -1.994  1.00 17.67 ?  145 ASP   A CG   1 
ATOM   3097 O  OD1  . ASP   A 1 145 ? 16.091 -20.152 -1.017  1.00 17.97 ?  145 ASP   A OD1  1 
ATOM   3098 O  OD2  . ASP   A 1 145 ? 16.068 -19.402 -3.079  1.00 19.07 -1 145 ASP   A OD2  1 
ATOM   3099 H  H    . ASP   A 1 145 ? 17.616 -17.295 -0.322  1.00 15.66 ?  145 ASP   A H    1 
ATOM   3100 H  HA   . ASP   A 1 145 ? 18.313 -19.849 0.045   1.00 16.50 ?  145 ASP   A HA   1 
ATOM   3101 H  HB2  . ASP   A 1 145 ? 18.195 -18.308 -2.314  1.00 18.73 ?  145 ASP   A HB2  1 
ATOM   3102 H  HB3  . ASP   A 1 145 ? 18.638 -19.835 -2.308  1.00 18.73 ?  145 ASP   A HB3  1 
ATOM   3103 N  N    . THR   A 1 146 ? 20.593 -17.802 0.182   1.00 11.86 ?  146 THR   A N    1 
ATOM   3104 C  CA   . THR   A 1 146 ? 22.033 -17.556 0.194   1.00 11.36 ?  146 THR   A CA   1 
ATOM   3105 C  C    . THR   A 1 146 ? 22.599 -17.370 1.590   1.00 11.34 ?  146 THR   A C    1 
ATOM   3106 O  O    . THR   A 1 146 ? 23.679 -17.898 1.896   1.00 12.24 ?  146 THR   A O    1 
ATOM   3107 C  CB   . THR   A 1 146 ? 22.358 -16.304 -0.646  1.00 11.31 ?  146 THR   A CB   1 
ATOM   3108 O  OG1  . THR   A 1 146 ? 21.828 -16.461 -1.963  1.00 11.93 ?  146 THR   A OG1  1 
ATOM   3109 C  CG2  . THR   A 1 146 ? 23.856 -16.073 -0.738  1.00 11.83 ?  146 THR   A CG2  1 
ATOM   3110 H  H    . THR   A 1 146 ? 20.132 -17.182 0.563   1.00 14.20 ?  146 THR   A H    1 
ATOM   3111 H  HA   . THR   A 1 146 ? 22.488 -18.306 -0.210  1.00 13.61 ?  146 THR   A HA   1 
ATOM   3112 H  HB   . THR   A 1 146 ? 21.960 -15.524 -0.229  1.00 13.54 ?  146 THR   A HB   1 
ATOM   3113 H  HG1  . THR   A 1 146 ? 20.991 -16.535 -1.927  1.00 14.29 ?  146 THR   A HG1  1 
ATOM   3114 H  HG21 . THR   A 1 146 ? 24.047 -15.410 -1.419  1.00 14.18 ?  146 THR   A HG21 1 
ATOM   3115 H  HG22 . THR   A 1 146 ? 24.199 -15.758 0.112   1.00 14.18 ?  146 THR   A HG22 1 
ATOM   3116 H  HG23 . THR   A 1 146 ? 24.304 -16.902 -0.973  1.00 14.18 ?  146 THR   A HG23 1 
ATOM   3117 N  N    . VAL   A 1 147 ? 21.920 -16.595 2.429   1.00 11.06 ?  147 VAL   A N    1 
ATOM   3118 C  CA   . VAL   A 1 147 ? 22.412 -16.298 3.764   1.00 11.36 ?  147 VAL   A CA   1 
ATOM   3119 C  C    . VAL   A 1 147 ? 22.091 -17.467 4.681   1.00 11.51 ?  147 VAL   A C    1 
ATOM   3120 O  O    . VAL   A 1 147 ? 20.946 -17.937 4.734   1.00 12.31 ?  147 VAL   A O    1 
ATOM   3121 C  CB   . VAL   A 1 147 ? 21.797 -14.991 4.288   1.00 11.50 ?  147 VAL   A CB   1 
ATOM   3122 C  CG1  . VAL   A 1 147 ? 22.343 -14.679 5.659   1.00 12.74 ?  147 VAL   A CG1  1 
ATOM   3123 C  CG2  . VAL   A 1 147 ? 22.050 -13.843 3.321   1.00 11.70 ?  147 VAL   A CG2  1 
ATOM   3124 H  H    . VAL   A 1 147 ? 21.159 -16.231 2.246   1.00 13.25 ?  147 VAL   A H    1 
ATOM   3125 H  HA   . VAL   A 1 147 ? 23.372 -16.188 3.730   1.00 13.61 ?  147 VAL   A HA   1 
ATOM   3126 H  HB   . VAL   A 1 147 ? 20.837 -15.105 4.373   1.00 13.78 ?  147 VAL   A HB   1 
ATOM   3127 H  HG11 . VAL   A 1 147 ? 22.097 -13.775 5.898   1.00 15.27 ?  147 VAL   A HG11 1 
ATOM   3128 H  HG12 . VAL   A 1 147 ? 21.962 -15.305 6.301   1.00 15.27 ?  147 VAL   A HG12 1 
ATOM   3129 H  HG13 . VAL   A 1 147 ? 23.307 -14.771 5.643   1.00 15.27 ?  147 VAL   A HG13 1 
ATOM   3130 H  HG21 . VAL   A 1 147 ? 21.717 -13.019 3.718   1.00 14.02 ?  147 VAL   A HG21 1 
ATOM   3131 H  HG22 . VAL   A 1 147 ? 22.999 -13.771 3.157   1.00 14.02 ?  147 VAL   A HG22 1 
ATOM   3132 H  HG23 . VAL   A 1 147 ? 21.578 -14.021 2.493   1.00 14.02 ?  147 VAL   A HG23 1 
ATOM   3133 N  N    . ARG   A 1 148 ? 23.114 -17.938 5.396   1.00 11.72 ?  148 ARG   A N    1 
ATOM   3134 C  CA   . ARG   A 1 148 ? 22.988 -19.018 6.358   1.00 11.75 ?  148 ARG   A CA   1 
ATOM   3135 C  C    . ARG   A 1 148 ? 23.120 -18.547 7.794   1.00 12.05 ?  148 ARG   A C    1 
ATOM   3136 O  O    . ARG   A 1 148 ? 22.715 -19.270 8.712   1.00 13.69 ?  148 ARG   A O    1 
ATOM   3137 C  CB   . ARG   A 1 148 ? 24.028 -20.109 6.070   1.00 12.46 ?  148 ARG   A CB   1 
ATOM   3138 C  CG   . ARG   A 1 148 ? 23.856 -20.740 4.704   1.00 13.67 ?  148 ARG   A CG   1 
ATOM   3139 C  CD   . ARG   A 1 148 ? 24.925 -21.784 4.405   1.00 14.90 ?  148 ARG   A CD   1 
ATOM   3140 N  NE   . ARG   A 1 148 ? 26.266 -21.211 4.420   1.00 14.54 ?  148 ARG   A NE   1 
ATOM   3141 C  CZ   . ARG   A 1 148 ? 26.774 -20.469 3.445   1.00 14.13 ?  148 ARG   A CZ   1 
ATOM   3142 N  NH1  . ARG   A 1 148 ? 26.094 -20.229 2.334   1.00 14.41 ?  148 ARG   A NH1  1 
ATOM   3143 N  NH2  . ARG   A 1 148 ? 27.992 -19.944 3.591   1.00 14.49 ?  148 ARG   A NH2  1 
ATOM   3144 H  H    . ARG   A 1 148 ? 23.921 -17.633 5.324   1.00 14.04 ?  148 ARG   A H    1 
ATOM   3145 H  HA   . ARG   A 1 148 ? 22.115 -19.418 6.256   1.00 14.08 ?  148 ARG   A HA   1 
ATOM   3146 H  HB2  . ARG   A 1 148 ? 24.917 -19.727 6.112   1.00 14.93 ?  148 ARG   A HB2  1 
ATOM   3147 H  HB3  . ARG   A 1 148 ? 23.939 -20.814 6.734   1.00 14.93 ?  148 ARG   A HB3  1 
ATOM   3148 H  HG2  . ARG   A 1 148 ? 22.989 -21.172 4.664   1.00 16.38 ?  148 ARG   A HG2  1 
ATOM   3149 H  HG3  . ARG   A 1 148 ? 23.915 -20.047 4.029   1.00 16.38 ?  148 ARG   A HG3  1 
ATOM   3150 H  HD2  . ARG   A 1 148 ? 24.889 -22.482 5.079   1.00 17.86 ?  148 ARG   A HD2  1 
ATOM   3151 H  HD3  . ARG   A 1 148 ? 24.763 -22.165 3.525   1.00 17.86 ?  148 ARG   A HD3  1 
ATOM   3152 H  HE   . ARG   A 1 148 ? 26.759 -21.363 5.101   1.00 17.42 ?  148 ARG   A HE   1 
ATOM   3153 H  HH11 . ARG   A 1 148 ? 25.306 -20.556 2.229   1.00 17.27 ?  148 ARG   A HH11 1 
ATOM   3154 H  HH12 . ARG   A 1 148 ? 26.440 -19.740 1.715   1.00 17.27 ?  148 ARG   A HH12 1 
ATOM   3155 H  HH21 . ARG   A 1 148 ? 28.435 -20.085 4.310   1.00 17.37 ?  148 ARG   A HH21 1 
ATOM   3156 H  HH22 . ARG   A 1 148 ? 28.327 -19.454 2.965   1.00 17.37 ?  148 ARG   A HH22 1 
ATOM   3157 N  N    . THR   A 1 149 ? 23.663 -17.356 8.005   1.00 12.07 ?  149 THR   A N    1 
ATOM   3158 C  CA   . THR   A 1 149 ? 23.744 -16.761 9.324   1.00 12.43 ?  149 THR   A CA   1 
ATOM   3159 C  C    . THR   A 1 149 ? 22.421 -16.063 9.633   1.00 11.77 ?  149 THR   A C    1 
ATOM   3160 O  O    . THR   A 1 149 ? 21.486 -16.058 8.824   1.00 12.53 ?  149 THR   A O    1 
ATOM   3161 C  CB   . THR   A 1 149 ? 24.946 -15.826 9.386   1.00 12.43 ?  149 THR   A CB   1 
ATOM   3162 O  OG1  . THR   A 1 149 ? 24.823 -14.890 8.316   1.00 12.62 ?  149 THR   A OG1  1 
ATOM   3163 C  CG2  . THR   A 1 149 ? 26.253 -16.618 9.260   1.00 13.29 ?  149 THR   A CG2  1 
ATOM   3164 H  H    . THR   A 1 149 ? 24.001 -16.862 7.383   1.00 14.46 ?  149 THR   A H    1 
ATOM   3165 H  HA   . THR   A 1 149 ? 23.870 -17.465 9.979   1.00 14.89 ?  149 THR   A HA   1 
ATOM   3166 H  HB   . THR   A 1 149 ? 24.942 -15.358 10.232  1.00 14.90 ?  149 THR   A HB   1 
ATOM   3167 H  HG1  . THR   A 1 149 ? 25.476 -14.362 8.320   1.00 15.12 ?  149 THR   A HG1  1 
ATOM   3168 H  HG21 . THR   A 1 149 ? 27.011 -16.015 9.316   1.00 15.93 ?  149 THR   A HG21 1 
ATOM   3169 H  HG22 . THR   A 1 149 ? 26.319 -17.272 9.976   1.00 15.93 ?  149 THR   A HG22 1 
ATOM   3170 H  HG23 . THR   A 1 149 ? 26.284 -17.083 8.408   1.00 15.93 ?  149 THR   A HG23 1 
ATOM   3171 N  N    . ASN   A 1 150 ? 22.305 -15.522 10.836  1.00 12.24 ?  150 ASN   A N    1 
ATOM   3172 C  CA   . ASN   A 1 150 ? 21.024 -15.010 11.317  1.00 12.68 ?  150 ASN   A CA   1 
ATOM   3173 C  C    . ASN   A 1 150 ? 20.842 -13.570 10.863  1.00 12.04 ?  150 ASN   A C    1 
ATOM   3174 O  O    . ASN   A 1 150 ? 21.599 -12.682 11.274  1.00 13.51 ?  150 ASN   A O    1 
ATOM   3175 C  CB   . ASN   A 1 150 ? 20.963 -15.120 12.836  1.00 15.26 ?  150 ASN   A CB   1 
ATOM   3176 C  CG   . ASN   A 1 150 ? 20.850 -16.550 13.296  1.00 19.36 ?  150 ASN   A CG   1 
ATOM   3177 O  OD1  . ASN   A 1 150 ? 20.250 -17.377 12.610  1.00 20.51 ?  150 ASN   A OD1  1 
ATOM   3178 N  ND2  . ASN   A 1 150 ? 21.440 -16.862 14.446  1.00 21.85 ?  150 ASN   A ND2  1 
ATOM   3179 H  H    . ASN   A 1 150 ? 22.949 -15.437 11.397  1.00 14.66 ?  150 ASN   A H    1 
ATOM   3180 H  HA   . ASN   A 1 150 ? 20.300 -15.545 10.950  1.00 15.19 ?  150 ASN   A HA   1 
ATOM   3181 H  HB2  . ASN   A 1 150 ? 21.770 -14.746 13.218  1.00 18.29 ?  150 ASN   A HB2  1 
ATOM   3182 H  HB3  . ASN   A 1 150 ? 20.184 -14.642 13.164  1.00 18.29 ?  150 ASN   A HB3  1 
ATOM   3183 H  HD21 . ASN   A 1 150 ? 21.407 -17.670 14.751  1.00 26.19 ?  150 ASN   A HD21 1 
ATOM   3184 H  HD22 . ASN   A 1 150 ? 21.854 -16.256 14.896  1.00 26.19 ?  150 ASN   A HD22 1 
ATOM   3185 N  N    . VAL   A 1 151 ? 19.846 -13.335 10.014  1.00 11.53 ?  151 VAL   A N    1 
ATOM   3186 C  CA   . VAL   A 1 151 ? 19.639 -12.026 9.417   1.00 11.58 ?  151 VAL   A CA   1 
ATOM   3187 C  C    . VAL   A 1 151 ? 18.252 -11.511 9.782   1.00 11.53 ?  151 VAL   A C    1 
ATOM   3188 O  O    . VAL   A 1 151 ? 17.246 -12.225 9.646   1.00 12.93 ?  151 VAL   A O    1 
ATOM   3189 C  CB   . VAL   A 1 151 ? 19.926 -12.021 7.901   1.00 13.08 ?  151 VAL   A CB   1 
ATOM   3190 C  CG1  . VAL   A 1 151 ? 19.100 -13.048 7.161   1.00 14.50 ?  151 VAL   A CG1  1 
ATOM   3191 C  CG2  . VAL   A 1 151 ? 19.726 -10.623 7.317   1.00 13.14 ?  151 VAL   A CG2  1 
ATOM   3192 H  H    . VAL   A 1 151 ? 19.272 -13.929 9.767   1.00 13.82 ?  151 VAL   A H    1 
ATOM   3193 H  HA   . VAL   A 1 151 ? 20.280 -11.416 9.813   1.00 13.87 ?  151 VAL   A HA   1 
ATOM   3194 H  HB   . VAL   A 1 151 ? 20.861 -12.256 7.763   1.00 15.68 ?  151 VAL   A HB   1 
ATOM   3195 H  HG11 . VAL   A 1 151 ? 19.297 -12.996 6.212   1.00 17.37 ?  151 VAL   A HG11 1 
ATOM   3196 H  HG12 . VAL   A 1 151 ? 19.326 -13.936 7.492   1.00 17.37 ?  151 VAL   A HG12 1 
ATOM   3197 H  HG13 . VAL   A 1 151 ? 18.160 -12.871 7.314   1.00 17.37 ?  151 VAL   A HG13 1 
ATOM   3198 H  HG21 . VAL   A 1 151 ? 20.049 -10.615 6.401   1.00 15.74 ?  151 VAL   A HG21 1 
ATOM   3199 H  HG22 . VAL   A 1 151 ? 18.782 -10.405 7.336   1.00 15.74 ?  151 VAL   A HG22 1 
ATOM   3200 H  HG23 . VAL   A 1 151 ? 20.228 -9.986  7.848   1.00 15.74 ?  151 VAL   A HG23 1 
ATOM   3201 N  N    . TYR   A 1 152 ? 18.235 -10.271 10.268  1.00 11.54 ?  152 TYR   A N    1 
ATOM   3202 C  CA   . TYR   A 1 152 ? 17.044 -9.538  10.660  1.00 11.13 ?  152 TYR   A CA   1 
ATOM   3203 C  C    . TYR   A 1 152 ? 16.849 -8.438  9.630   1.00 11.04 ?  152 TYR   A C    1 
ATOM   3204 O  O    . TYR   A 1 152 ? 17.629 -7.478  9.577   1.00 11.35 ?  152 TYR   A O    1 
ATOM   3205 C  CB   . TYR   A 1 152 ? 17.231 -8.994  12.073  1.00 11.91 ?  152 TYR   A CB   1 
ATOM   3206 C  CG   . TYR   A 1 152 ? 17.197 -10.123 13.072  1.00 12.92 ?  152 TYR   A CG   1 
ATOM   3207 C  CD1  . TYR   A 1 152 ? 18.325 -10.887 13.332  1.00 14.32 ?  152 TYR   A CD1  1 
ATOM   3208 C  CD2  . TYR   A 1 152 ? 16.020 -10.468 13.711  1.00 13.26 ?  152 TYR   A CD2  1 
ATOM   3209 C  CE1  . TYR   A 1 152 ? 18.290 -11.947 14.218  1.00 15.52 ?  152 TYR   A CE1  1 
ATOM   3210 C  CE2  . TYR   A 1 152 ? 15.970 -11.536 14.601  1.00 14.61 ?  152 TYR   A CE2  1 
ATOM   3211 C  CZ   . TYR   A 1 152 ? 17.111 -12.268 14.852  1.00 15.64 ?  152 TYR   A CZ   1 
ATOM   3212 O  OH   . TYR   A 1 152 ? 17.071 -13.330 15.733  1.00 18.08 ?  152 TYR   A OH   1 
ATOM   3213 H  H    . TYR   A 1 152 ? 18.957 -9.800  10.366  1.00 13.82 ?  152 TYR   A H    1 
ATOM   3214 H  HA   . TYR   A 1 152 ? 16.277 -10.131 10.642  1.00 13.33 ?  152 TYR   A HA   1 
ATOM   3215 H  HB2  . TYR   A 1 152 ? 18.090 -8.555  12.139  1.00 14.27 ?  152 TYR   A HB2  1 
ATOM   3216 H  HB3  . TYR   A 1 152 ? 16.514 -8.377  12.278  1.00 14.27 ?  152 TYR   A HB3  1 
ATOM   3217 H  HD1  . TYR   A 1 152 ? 19.120 -10.675 12.900  1.00 17.16 ?  152 TYR   A HD1  1 
ATOM   3218 H  HD2  . TYR   A 1 152 ? 15.242 -9.977  13.542  1.00 15.89 ?  152 TYR   A HD2  1 
ATOM   3219 H  HE1  . TYR   A 1 152 ? 19.058 -12.437 14.384  1.00 18.60 ?  152 TYR   A HE1  1 
ATOM   3220 H  HE2  . TYR   A 1 152 ? 15.171 -11.746 15.034  1.00 17.51 ?  152 TYR   A HE2  1 
ATOM   3221 H  HH   . TYR   A 1 152 ? 16.297 -13.404 16.054  1.00 21.67 ?  152 TYR   A HH   1 
ATOM   3222 N  N    A LEU   A 1 153 ? 15.846 -8.620  8.777   0.60 11.13 ?  153 LEU   A N    1 
ATOM   3223 N  N    B LEU   A 1 153 ? 15.805 -8.567  8.817   0.40 11.55 ?  153 LEU   A N    1 
ATOM   3224 C  CA   A LEU   A 1 153 ? 15.571 -7.718  7.671   0.60 10.90 ?  153 LEU   A CA   1 
ATOM   3225 C  CA   B LEU   A 1 153 ? 15.549 -7.648  7.716   0.40 11.57 ?  153 LEU   A CA   1 
ATOM   3226 C  C    A LEU   A 1 153 ? 14.581 -6.645  8.092   0.60 11.27 ?  153 LEU   A C    1 
ATOM   3227 C  C    B LEU   A 1 153 ? 14.554 -6.575  8.145   0.40 11.89 ?  153 LEU   A C    1 
ATOM   3228 O  O    A LEU   A 1 153 ? 13.530 -6.947  8.674   0.60 11.97 ?  153 LEU   A O    1 
ATOM   3229 O  O    B LEU   A 1 153 ? 13.399 -6.883  8.465   0.40 12.38 ?  153 LEU   A O    1 
ATOM   3230 C  CB   A LEU   A 1 153 ? 14.993 -8.495  6.488   0.60 11.05 ?  153 LEU   A CB   1 
ATOM   3231 C  CB   B LEU   A 1 153 ? 15.016 -8.402  6.499   0.40 11.77 ?  153 LEU   A CB   1 
ATOM   3232 C  CG   A LEU   A 1 153 ? 15.930 -9.477  5.791   0.60 11.12 ?  153 LEU   A CG   1 
ATOM   3233 C  CG   B LEU   A 1 153 ? 15.938 -9.472  5.912   0.40 11.87 ?  153 LEU   A CG   1 
ATOM   3234 C  CD1  A LEU   A 1 153 ? 15.138 -10.395 4.875   0.60 11.67 ?  153 LEU   A CD1  1 
ATOM   3235 C  CD1  B LEU   A 1 153 ? 15.199 -10.281 4.853   0.40 12.38 ?  153 LEU   A CD1  1 
ATOM   3236 C  CD2  A LEU   A 1 153 ? 16.984 -8.716  5.005   0.60 11.01 ?  153 LEU   A CD2  1 
ATOM   3237 C  CD2  B LEU   A 1 153 ? 17.201 -8.843  5.333   0.40 11.75 ?  153 LEU   A CD2  1 
ATOM   3238 H  H    A LEU   A 1 153 ? 15.293 -9.283  8.823   0.60 13.33 ?  153 LEU   A H    1 
ATOM   3239 H  H    B LEU   A 1 153 ? 15.216 -9.192  8.887   0.40 13.83 ?  153 LEU   A H    1 
ATOM   3240 H  HA   A LEU   A 1 153 ? 16.395 -7.296  7.390   0.60 13.05 ?  153 LEU   A HA   1 
ATOM   3241 H  HA   B LEU   A 1 153 ? 16.376 -7.214  7.470   0.40 13.85 ?  153 LEU   A HA   1 
ATOM   3242 H  HB2  A LEU   A 1 153 ? 14.226 -9.002  6.801   0.60 13.23 ?  153 LEU   A HB2  1 
ATOM   3243 H  HB2  B LEU   A 1 153 ? 14.189 -8.841  6.753   0.40 14.10 ?  153 LEU   A HB2  1 
ATOM   3244 H  HB3  A LEU   A 1 153 ? 14.700 -7.854  5.820   0.60 13.23 ?  153 LEU   A HB3  1 
ATOM   3245 H  HB3  B LEU   A 1 153 ? 14.836 -7.757  5.798   0.40 14.10 ?  153 LEU   A HB3  1 
ATOM   3246 H  HG   A LEU   A 1 153 ? 16.382 -10.020 6.459   0.60 13.32 ?  153 LEU   A HG   1 
ATOM   3247 H  HG   B LEU   A 1 153 ? 16.206 -10.077 6.621   0.40 14.22 ?  153 LEU   A HG   1 
ATOM   3248 H  HD11 A LEU   A 1 153 ? 15.740 -11.056 4.498   0.60 13.97 ?  153 LEU   A HD11 1 
ATOM   3249 H  HD11 B LEU   A 1 153 ? 15.763 -11.019 4.572   0.40 14.83 ?  153 LEU   A HD11 1 
ATOM   3250 H  HD12 A LEU   A 1 153 ? 14.448 -10.833 5.393   0.60 13.97 ?  153 LEU   A HD12 1 
ATOM   3251 H  HD12 B LEU   A 1 153 ? 14.376 -10.621 5.235   0.40 14.83 ?  153 LEU   A HD12 1 
ATOM   3252 H  HD13 A LEU   A 1 153 ? 14.742 -9.864  4.169   0.60 13.97 ?  153 LEU   A HD13 1 
ATOM   3253 H  HD13 B LEU   A 1 153 ? 15.003 -9.706  4.098   0.40 14.83 ?  153 LEU   A HD13 1 
ATOM   3254 H  HD21 A LEU   A 1 153 ? 17.549 -9.351  4.545   0.60 13.18 ?  153 LEU   A HD21 1 
ATOM   3255 H  HD21 B LEU   A 1 153 ? 17.744 -9.539  4.933   0.40 14.08 ?  153 LEU   A HD21 1 
ATOM   3256 H  HD22 A LEU   A 1 153 ? 16.535 -8.141  4.366   0.60 13.18 ?  153 LEU   A HD22 1 
ATOM   3257 H  HD22 B LEU   A 1 153 ? 16.949 -8.191  4.661   0.40 14.08 ?  153 LEU   A HD22 1 
ATOM   3258 H  HD23 A LEU   A 1 153 ? 17.508 -8.183  5.621   0.60 13.18 ?  153 LEU   A HD23 1 
ATOM   3259 H  HD23 B LEU   A 1 153 ? 17.695 -8.409  6.047   0.40 14.08 ?  153 LEU   A HD23 1 
ATOM   3260 N  N    A ALA   A 1 154 ? 14.912 -5.399  7.776   0.60 10.76 ?  154 ALA   A N    1 
ATOM   3261 N  N    B ALA   A 1 154 ? 15.002 -5.321  8.134   0.40 11.43 ?  154 ALA   A N    1 
ATOM   3262 C  CA   A ALA   A 1 154 ? 14.040 -4.256  8.003   0.60 11.29 ?  154 ALA   A CA   1 
ATOM   3263 C  CA   B ALA   A 1 154 ? 14.145 -4.172  8.399   0.40 11.83 ?  154 ALA   A CA   1 
ATOM   3264 C  C    A ALA   A 1 154 ? 13.567 -3.742  6.653   0.60 11.59 ?  154 ALA   A C    1 
ATOM   3265 C  C    B ALA   A 1 154 ? 13.643 -3.620  7.069   0.40 11.76 ?  154 ALA   A C    1 
ATOM   3266 O  O    A ALA   A 1 154 ? 14.386 -3.397  5.793   0.60 12.27 ?  154 ALA   A O    1 
ATOM   3267 O  O    B ALA   A 1 154 ? 14.443 -3.225  6.212   0.40 11.80 ?  154 ALA   A O    1 
ATOM   3268 C  CB   A ALA   A 1 154 ? 14.780 -3.150  8.750   0.60 12.38 ?  154 ALA   A CB   1 
ATOM   3269 C  CB   B ALA   A 1 154 ? 14.910 -3.098  9.175   0.40 11.98 ?  154 ALA   A CB   1 
ATOM   3270 H  H    A ALA   A 1 154 ? 15.661 -5.189  7.410   0.60 12.89 ?  154 ALA   A H    1 
ATOM   3271 H  H    B ALA   A 1 154 ? 15.816 -5.106  7.968   0.40 13.69 ?  154 ALA   A H    1 
ATOM   3272 H  HA   A ALA   A 1 154 ? 13.267 -4.530  8.523   0.60 13.53 ?  154 ALA   A HA   1 
ATOM   3273 H  HA   B ALA   A 1 154 ? 13.380 -4.442  8.928   0.40 14.17 ?  154 ALA   A HA   1 
ATOM   3274 H  HB1  A ALA   A 1 154 ? 14.174 -2.406  8.883   0.60 14.83 ?  154 ALA   A HB1  1 
ATOM   3275 H  HB1  B ALA   A 1 154 ? 14.322 -2.342  9.341   0.40 14.35 ?  154 ALA   A HB1  1 
ATOM   3276 H  HB2  A ALA   A 1 154 ? 15.080 -3.494  9.603   0.60 14.83 ?  154 ALA   A HB2  1 
ATOM   3277 H  HB2  B ALA   A 1 154 ? 15.211 -3.470  10.021  0.40 14.35 ?  154 ALA   A HB2  1 
ATOM   3278 H  HB3  A ALA   A 1 154 ? 15.540 -2.869  8.217   0.60 14.83 ?  154 ALA   A HB3  1 
ATOM   3279 H  HB3  B ALA   A 1 154 ? 15.676 -2.810  8.653   0.40 14.35 ?  154 ALA   A HB3  1 
ATOM   3280 N  N    A VAL   A 1 155 ? 12.251 -3.693  6.473   0.60 12.08 ?  155 VAL   A N    1 
ATOM   3281 N  N    B VAL   A 1 155 ? 12.323 -3.596  6.899   0.40 12.43 ?  155 VAL   A N    1 
ATOM   3282 C  CA   A VAL   A 1 155 ? 11.620 -3.202  5.255   0.60 13.42 ?  155 VAL   A CA   1 
ATOM   3283 C  CA   B VAL   A 1 155 ? 11.672 -3.160  5.666   0.40 13.21 ?  155 VAL   A CA   1 
ATOM   3284 C  C    A VAL   A 1 155 ? 10.846 -1.944  5.635   0.60 14.40 ?  155 VAL   A C    1 
ATOM   3285 C  C    B VAL   A 1 155 ? 11.003 -1.818  5.925   0.40 14.41 ?  155 VAL   A C    1 
ATOM   3286 O  O    A VAL   A 1 155 ? 9.864  -2.016  6.385   0.60 14.14 ?  155 VAL   A O    1 
ATOM   3287 O  O    B VAL   A 1 155 ? 10.116 -1.711  6.780   0.40 14.10 ?  155 VAL   A O    1 
ATOM   3288 C  CB   A VAL   A 1 155 ? 10.714 -4.268  4.620   0.60 13.60 ?  155 VAL   A CB   1 
ATOM   3289 C  CB   B VAL   A 1 155 ? 10.644 -4.190  5.175   0.40 13.51 ?  155 VAL   A CB   1 
ATOM   3290 C  CG1  A VAL   A 1 155 ? 10.034 -3.730  3.371   0.60 14.21 ?  155 VAL   A CG1  1 
ATOM   3291 C  CG1  B VAL   A 1 155 ? 9.854  -3.629  3.996   0.40 13.94 ?  155 VAL   A CG1  1 
ATOM   3292 C  CG2  A VAL   A 1 155 ? 11.537 -5.512  4.279   0.60 13.96 ?  155 VAL   A CG2  1 
ATOM   3293 C  CG2  B VAL   A 1 155 ? 11.330 -5.494  4.801   0.40 14.17 ?  155 VAL   A CG2  1 
ATOM   3294 H  H    A VAL   A 1 155 ? 11.681 -3.956  7.064   0.60 14.47 ?  155 VAL   A H    1 
ATOM   3295 H  H    B VAL   A 1 155 ? 11.770 -3.837  7.506   0.40 14.90 ?  155 VAL   A H    1 
ATOM   3296 H  HA   A VAL   A 1 155 ? 12.301 -2.962  4.608   0.60 16.08 ?  155 VAL   A HA   1 
ATOM   3297 H  HA   B VAL   A 1 155 ? 12.342 -3.037  4.973   0.40 15.83 ?  155 VAL   A HA   1 
ATOM   3298 H  HB   A VAL   A 1 155 ? 10.026 -4.528  5.254   0.60 16.29 ?  155 VAL   A HB   1 
ATOM   3299 H  HB   B VAL   A 1 155 ? 10.021 -4.372  5.895   0.40 16.18 ?  155 VAL   A HB   1 
ATOM   3300 H  HG11 A VAL   A 1 155 ? 9.593  -4.464  2.911   0.60 17.03 ?  155 VAL   A HG11 1 
ATOM   3301 H  HG11 B VAL   A 1 155 ? 9.476  -4.365  3.492   0.40 16.71 ?  155 VAL   A HG11 1 
ATOM   3302 H  HG12 A VAL   A 1 155 ? 9.379  -3.064  3.629   0.60 17.03 ?  155 VAL   A HG12 1 
ATOM   3303 H  HG12 B VAL   A 1 155 ? 9.143  -3.059  4.332   0.40 16.71 ?  155 VAL   A HG12 1 
ATOM   3304 H  HG13 A VAL   A 1 155 ? 10.704 -3.335  2.793   0.60 17.03 ?  155 VAL   A HG13 1 
ATOM   3305 H  HG13 B VAL   A 1 155 ? 10.449 -3.113  3.431   0.40 16.71 ?  155 VAL   A HG13 1 
ATOM   3306 H  HG21 A VAL   A 1 155 ? 10.969 -6.159  3.831   0.60 16.73 ?  155 VAL   A HG21 1 
ATOM   3307 H  HG21 B VAL   A 1 155 ? 10.674 -6.093  4.415   0.40 16.98 ?  155 VAL   A HG21 1 
ATOM   3308 H  HG22 A VAL   A 1 155 ? 12.270 -5.256  3.696   0.60 16.73 ?  155 VAL   A HG22 1 
ATOM   3309 H  HG22 B VAL   A 1 155 ? 12.030 -5.309  4.155   0.40 16.98 ?  155 VAL   A HG22 1 
ATOM   3310 H  HG23 A VAL   A 1 155 ? 11.889 -5.896  5.099   0.60 16.73 ?  155 VAL   A HG23 1 
ATOM   3311 H  HG23 B VAL   A 1 155 ? 11.714 -5.891  5.599   0.40 16.98 ?  155 VAL   A HG23 1 
ATOM   3312 N  N    A PHE   A 1 156 ? 11.299 -0.786  5.135   0.60 16.08 ?  156 PHE   A N    1 
ATOM   3313 N  N    B PHE   A 1 156 ? 11.408 -0.805  5.155   0.40 15.69 ?  156 PHE   A N    1 
ATOM   3314 C  CA   A PHE   A 1 156 ? 10.755 0.505   5.566   0.60 17.75 ?  156 PHE   A CA   1 
ATOM   3315 C  CA   B PHE   A 1 156 ? 10.916 0.556   5.350   0.40 16.88 ?  156 PHE   A CA   1 
ATOM   3316 C  C    A PHE   A 1 156 ? 9.296  0.681   5.158   0.60 18.07 ?  156 PHE   A C    1 
ATOM   3317 C  C    B PHE   A 1 156 ? 9.454  0.684   4.947   0.40 17.86 ?  156 PHE   A C    1 
ATOM   3318 O  O    A PHE   A 1 156 ? 8.502  1.257   5.912   0.60 18.98 ?  156 PHE   A O    1 
ATOM   3319 O  O    B PHE   A 1 156 ? 8.631  1.210   5.707   0.40 18.66 ?  156 PHE   A O    1 
ATOM   3320 C  CB   A PHE   A 1 156 ? 11.615 1.632   4.985   0.60 19.66 ?  156 PHE   A CB   1 
ATOM   3321 C  CB   B PHE   A 1 156 ? 11.776 1.504   4.511   0.40 16.82 ?  156 PHE   A CB   1 
ATOM   3322 C  CG   A PHE   A 1 156 ? 11.113 3.019   5.294   0.60 21.41 ?  156 PHE   A CG   1 
ATOM   3323 C  CG   B PHE   A 1 156 ? 11.445 2.960   4.689   0.40 16.41 ?  156 PHE   A CG   1 
ATOM   3324 C  CD1  A PHE   A 1 156 ? 11.052 3.472   6.600   0.60 22.32 ?  156 PHE   A CD1  1 
ATOM   3325 C  CD1  B PHE   A 1 156 ? 12.054 3.700   5.691   0.40 16.54 ?  156 PHE   A CD1  1 
ATOM   3326 C  CD2  A PHE   A 1 156 ? 10.735 3.880   4.272   0.60 22.61 ?  156 PHE   A CD2  1 
ATOM   3327 C  CD2  B PHE   A 1 156 ? 10.553 3.597   3.839   0.40 16.96 ?  156 PHE   A CD2  1 
ATOM   3328 C  CE1  A PHE   A 1 156 ? 10.604 4.752   6.885   0.60 23.32 ?  156 PHE   A CE1  1 
ATOM   3329 C  CE1  B PHE   A 1 156 ? 11.765 5.041   5.858   0.40 16.72 ?  156 PHE   A CE1  1 
ATOM   3330 C  CE2  A PHE   A 1 156 ? 10.285 5.160   4.550   0.60 23.33 ?  156 PHE   A CE2  1 
ATOM   3331 C  CE2  B PHE   A 1 156 ? 10.259 4.941   4.002   0.40 17.15 ?  156 PHE   A CE2  1 
ATOM   3332 C  CZ   A PHE   A 1 156 ? 10.223 5.597   5.858   0.60 23.59 ?  156 PHE   A CZ   1 
ATOM   3333 C  CZ   B PHE   A 1 156 ? 10.871 5.664   5.013   0.40 16.84 ?  156 PHE   A CZ   1 
ATOM   3334 H  H    A PHE   A 1 156 ? 11.932 -0.725  4.554   0.60 19.28 ?  156 PHE   A H    1 
ATOM   3335 H  H    B PHE   A 1 156 ? 11.969 -0.882  4.510   0.40 18.81 ?  156 PHE   A H    1 
ATOM   3336 H  HA   A PHE   A 1 156 ? 10.808 0.560   6.531   0.60 21.27 ?  156 PHE   A HA   1 
ATOM   3337 H  HA   B PHE   A 1 156 ? 11.004 0.806   6.281   0.40 20.23 ?  156 PHE   A HA   1 
ATOM   3338 H  HB2  A PHE   A 1 156 ? 12.513 1.560   5.346   0.60 23.56 ?  156 PHE   A HB2  1 
ATOM   3339 H  HB2  B PHE   A 1 156 ? 12.704 1.383   4.759   0.40 20.15 ?  156 PHE   A HB2  1 
ATOM   3340 H  HB3  A PHE   A 1 156 ? 11.643 1.539   4.020   0.60 23.56 ?  156 PHE   A HB3  1 
ATOM   3341 H  HB3  B PHE   A 1 156 ? 11.658 1.285   3.572   0.40 20.15 ?  156 PHE   A HB3  1 
ATOM   3342 H  HD1  A PHE   A 1 156 ? 11.308 2.910   7.294   0.60 26.76 ?  156 PHE   A HD1  1 
ATOM   3343 H  HD1  B PHE   A 1 156 ? 12.657 3.283   6.265   0.40 19.83 ?  156 PHE   A HD1  1 
ATOM   3344 H  HD2  A PHE   A 1 156 ? 10.777 3.588   3.389   0.60 27.10 ?  156 PHE   A HD2  1 
ATOM   3345 H  HD2  B PHE   A 1 156 ? 10.141 3.115   3.159   0.40 20.33 ?  156 PHE   A HD2  1 
ATOM   3346 H  HE1  A PHE   A 1 156 ? 10.562 5.046   7.767   0.60 27.96 ?  156 PHE   A HE1  1 
ATOM   3347 H  HE1  B PHE   A 1 156 ? 12.175 5.522   6.540   0.40 20.04 ?  156 PHE   A HE1  1 
ATOM   3348 H  HE2  A PHE   A 1 156 ? 10.030 5.725   3.855   0.60 27.97 ?  156 PHE   A HE2  1 
ATOM   3349 H  HE2  B PHE   A 1 156 ? 9.655  5.357   3.432   0.40 20.55 ?  156 PHE   A HE2  1 
ATOM   3350 H  HZ   A PHE   A 1 156 ? 9.921  6.458   6.047   0.60 28.28 ?  156 PHE   A HZ   1 
ATOM   3351 H  HZ   B PHE   A 1 156 ? 10.673 6.565   5.127   0.40 20.18 ?  156 PHE   A HZ   1 
ATOM   3352 N  N    A ASP   A 1 157 ? 8.929  0.211   3.971   0.60 17.98 ?  157 ASP   A N    1 
ATOM   3353 N  N    B ASP   A 1 157 ? 9.118  0.223   3.748   0.40 18.16 ?  157 ASP   A N    1 
ATOM   3354 C  CA   A ASP   A 1 157 ? 7.614  0.465   3.393   0.60 19.32 ?  157 ASP   A CA   1 
ATOM   3355 C  CA   B ASP   A 1 157 ? 7.817  0.489   3.154   0.40 18.44 ?  157 ASP   A CA   1 
ATOM   3356 C  C    A ASP   A 1 157 ? 6.624  -0.593  3.874   0.60 19.51 ?  157 ASP   A C    1 
ATOM   3357 C  C    B ASP   A 1 157 ? 6.779  -0.493  3.687   0.40 18.49 ?  157 ASP   A C    1 
ATOM   3358 O  O    A ASP   A 1 157 ? 6.795  -1.784  3.591   0.60 19.06 ?  157 ASP   A O    1 
ATOM   3359 O  O    B ASP   A 1 157 ? 6.959  -1.712  3.596   0.40 18.18 ?  157 ASP   A O    1 
ATOM   3360 C  CB   A ASP   A 1 157 ? 7.722  0.440   1.870   0.60 20.88 ?  157 ASP   A CB   1 
ATOM   3361 C  CB   B ASP   A 1 157 ? 7.934  0.365   1.638   0.40 18.74 ?  157 ASP   A CB   1 
ATOM   3362 C  CG   A ASP   A 1 157 ? 6.458  0.918   1.186   0.60 22.70 ?  157 ASP   A CG   1 
ATOM   3363 C  CG   B ASP   A 1 157 ? 6.716  0.883   0.920   0.40 18.95 ?  157 ASP   A CG   1 
ATOM   3364 O  OD1  A ASP   A 1 157 ? 6.168  2.132   1.236   0.60 23.90 ?  157 ASP   A OD1  1 
ATOM   3365 O  OD1  B ASP   A 1 157 ? 5.617  0.327   1.140   0.40 19.37 ?  157 ASP   A OD1  1 
ATOM   3366 O  OD2  A ASP   A 1 157 ? 5.749  0.073   0.598   0.60 23.06 -1 157 ASP   A OD2  1 
ATOM   3367 O  OD2  B ASP   A 1 157 ? 6.857  1.857   0.151   0.40 18.57 -1 157 ASP   A OD2  1 
ATOM   3368 H  H    A ASP   A 1 157 ? 9.441  -0.266  3.471   0.60 21.55 ?  157 ASP   A H    1 
ATOM   3369 H  H    B ASP   A 1 157 ? 9.639  -0.247  3.250   0.40 21.77 ?  157 ASP   A H    1 
ATOM   3370 H  HA   A ASP   A 1 157 ? 7.299  1.338   3.672   0.60 23.16 ?  157 ASP   A HA   1 
ATOM   3371 H  HA   B ASP   A 1 157 ? 7.535  1.394   3.367   0.40 22.11 ?  157 ASP   A HA   1 
ATOM   3372 H  HB2  A ASP   A 1 157 ? 8.475  0.996   1.602   0.60 25.03 ?  157 ASP   A HB2  1 
ATOM   3373 H  HB2  B ASP   A 1 157 ? 8.702  0.875   1.338   0.40 22.47 ?  157 ASP   A HB2  1 
ATOM   3374 H  HB3  A ASP   A 1 157 ? 7.870  -0.472  1.579   0.60 25.03 ?  157 ASP   A HB3  1 
ATOM   3375 H  HB3  B ASP   A 1 157 ? 8.059  -0.568  1.404   0.40 22.47 ?  157 ASP   A HB3  1 
ATOM   3376 N  N    A LYS   A 1 158 ? 5.585  -0.154  4.592   0.60 20.80 ?  158 LYS   A N    1 
ATOM   3377 N  N    B LYS   A 1 158 ? 5.687  0.041   4.238   0.40 19.30 ?  158 LYS   A N    1 
ATOM   3378 C  CA   A LYS   A 1 158 ? 4.624  -1.095  5.163   0.60 22.05 ?  158 LYS   A CA   1 
ATOM   3379 C  CA   B LYS   A 1 158 ? 4.673  -0.818  4.841   0.40 20.13 ?  158 LYS   A CA   1 
ATOM   3380 C  C    A LYS   A 1 158 ? 3.887  -1.865  4.074   0.60 21.63 ?  158 LYS   A C    1 
ATOM   3381 C  C    B LYS   A 1 158 ? 3.989  -1.683  3.789   0.40 20.05 ?  158 LYS   A C    1 
ATOM   3382 O  O    A LYS   A 1 158 ? 3.675  -3.078  4.194   0.60 21.54 ?  158 LYS   A O    1 
ATOM   3383 O  O    B LYS   A 1 158 ? 3.831  -2.896  3.974   0.40 20.13 ?  158 LYS   A O    1 
ATOM   3384 C  CB   A LYS   A 1 158 ? 3.642  -0.349  6.069   0.60 23.28 ?  158 LYS   A CB   1 
ATOM   3385 C  CB   B LYS   A 1 158 ? 3.643  0.024   5.597   0.40 20.90 ?  158 LYS   A CB   1 
ATOM   3386 C  CG   A LYS   A 1 158 ? 2.423  -1.159  6.505   0.60 24.73 ?  158 LYS   A CG   1 
ATOM   3387 C  CG   B LYS   A 1 158 ? 2.432  -0.783  6.039   0.40 21.81 ?  158 LYS   A CG   1 
ATOM   3388 C  CD   A LYS   A 1 158 ? 2.802  -2.394  7.313   0.60 25.73 ?  158 LYS   A CD   1 
ATOM   3389 C  CD   B LYS   A 1 158 ? 1.419  0.059   6.780   0.40 22.54 ?  158 LYS   A CD   1 
ATOM   3390 C  CE   A LYS   A 1 158 ? 1.554  -3.104  7.826   0.60 26.26 ?  158 LYS   A CE   1 
ATOM   3391 C  CE   B LYS   A 1 158 ? 0.243  -0.788  7.242   0.40 22.88 ?  158 LYS   A CE   1 
ATOM   3392 N  NZ   A LYS   A 1 158 ? 1.852  -4.426  8.443   0.60 26.48 ?  158 LYS   A NZ   1 
ATOM   3393 N  NZ   B LYS   A 1 158 ? -0.423 -1.495  6.110   0.40 23.06 ?  158 LYS   A NZ   1 
ATOM   3394 H  H    A LYS   A 1 158 ? 5.421  0.672   4.757   0.60 24.93 ?  158 LYS   A H    1 
ATOM   3395 H  H    B LYS   A 1 158 ? 5.513  0.883   4.270   0.40 23.14 ?  158 LYS   A H    1 
ATOM   3396 H  HA   A LYS   A 1 158 ? 5.101  -1.736  5.710   0.60 26.43 ?  158 LYS   A HA   1 
ATOM   3397 H  HA   B LYS   A 1 158 ? 5.101  -1.406  5.483   0.40 24.13 ?  158 LYS   A HA   1 
ATOM   3398 H  HB2  A LYS   A 1 158 ? 4.110  -0.073  6.874   0.60 27.91 ?  158 LYS   A HB2  1 
ATOM   3399 H  HB2  B LYS   A 1 158 ? 4.060  0.398   6.393   0.40 25.05 ?  158 LYS   A HB2  1 
ATOM   3400 H  HB3  A LYS   A 1 158 ? 3.319  0.437   5.599   0.60 27.91 ?  158 LYS   A HB3  1 
ATOM   3401 H  HB3  B LYS   A 1 158 ? 3.334  0.740   5.021   0.40 25.05 ?  158 LYS   A HB3  1 
ATOM   3402 H  HG2  A LYS   A 1 158 ? 1.861  -0.600  7.064   0.60 29.65 ?  158 LYS   A HG2  1 
ATOM   3403 H  HG2  B LYS   A 1 158 ? 1.987  -1.151  5.260   0.40 26.15 ?  158 LYS   A HG2  1 
ATOM   3404 H  HG3  A LYS   A 1 158 ? 1.922  -1.445  5.724   0.60 29.65 ?  158 LYS   A HG3  1 
ATOM   3405 H  HG3  B LYS   A 1 158 ? 2.725  -1.498  6.626   0.40 26.15 ?  158 LYS   A HG3  1 
ATOM   3406 H  HD2  A LYS   A 1 158 ? 3.296  -3.009  6.751   0.60 30.86 ?  158 LYS   A HD2  1 
ATOM   3407 H  HD2  B LYS   A 1 158 ? 1.838  0.453   7.560   0.40 27.03 ?  158 LYS   A HD2  1 
ATOM   3408 H  HD3  A LYS   A 1 158 ? 3.339  -2.126  8.077   0.60 30.86 ?  158 LYS   A HD3  1 
ATOM   3409 H  HD3  B LYS   A 1 158 ? 1.085  0.753   6.189   0.40 27.03 ?  158 LYS   A HD3  1 
ATOM   3410 H  HE2  A LYS   A 1 158 ? 1.125  -2.550  8.497   0.60 31.49 ?  158 LYS   A HE2  1 
ATOM   3411 H  HE2  B LYS   A 1 158 ? 0.560  -1.456  7.869   0.40 27.43 ?  158 LYS   A HE2  1 
ATOM   3412 H  HE3  A LYS   A 1 158 ? 0.949  -3.251  7.084   0.60 31.49 ?  158 LYS   A HE3  1 
ATOM   3413 H  HE3  B LYS   A 1 158 ? -0.413 -0.214  7.667   0.40 27.43 ?  158 LYS   A HE3  1 
ATOM   3414 H  HZ1  A LYS   A 1 158 ? 1.099  -4.806  8.728   0.60 31.76 ?  158 LYS   A HZ1  1 
ATOM   3415 H  HZ1  B LYS   A 1 158 ? -1.145 -1.926  6.403   0.40 27.65 ?  158 LYS   A HZ1  1 
ATOM   3416 H  HZ2  A LYS   A 1 158 ? 2.236  -4.961  7.844   0.60 31.76 ?  158 LYS   A HZ2  1 
ATOM   3417 H  HZ2  B LYS   A 1 158 ? -0.671 -0.908  5.487   0.40 27.65 ?  158 LYS   A HZ2  1 
ATOM   3418 H  HZ3  A LYS   A 1 158 ? 2.403  -4.323  9.134   0.60 31.76 ?  158 LYS   A HZ3  1 
ATOM   3419 H  HZ3  B LYS   A 1 158 ? 0.136  -2.083  5.745   0.40 27.65 ?  158 LYS   A HZ3  1 
ATOM   3420 N  N    A ASN   A 1 159 ? 3.479  -1.178  3.006   0.60 21.91 ?  159 ASN   A N    1 
ATOM   3421 N  N    B ASN   A 1 159 ? 3.555  -1.074  2.685   0.40 20.48 ?  159 ASN   A N    1 
ATOM   3422 C  CA   A ASN   A 1 159 ? 2.808  -1.872  1.913   0.60 22.11 ?  159 ASN   A CA   1 
ATOM   3423 C  CA   B ASN   A 1 159 ? 2.895  -1.850  1.642   0.40 21.16 ?  159 ASN   A CA   1 
ATOM   3424 C  C    A ASN   A 1 159 ? 3.710  -2.948  1.315   0.60 20.64 ?  159 ASN   A C    1 
ATOM   3425 C  C    B ASN   A 1 159 ? 3.829  -2.897  1.054   0.40 20.27 ?  159 ASN   A C    1 
ATOM   3426 O  O    A ASN   A 1 159 ? 3.277  -4.085  1.094   0.60 19.75 ?  159 ASN   A O    1 
ATOM   3427 O  O    B ASN   A 1 159 ? 3.376  -3.962  0.621   0.40 20.00 ?  159 ASN   A O    1 
ATOM   3428 C  CB   A ASN   A 1 159 ? 2.340  -0.860  0.864   0.60 23.90 ?  159 ASN   A CB   1 
ATOM   3429 C  CB   B ASN   A 1 159 ? 2.362  -0.921  0.550   0.40 22.90 ?  159 ASN   A CB   1 
ATOM   3430 C  CG   A ASN   A 1 159 ? 1.132  -0.058  1.328   0.60 25.87 ?  159 ASN   A CG   1 
ATOM   3431 C  CG   B ASN   A 1 159 ? 1.264  -0.002  1.054   0.40 24.64 ?  159 ASN   A CG   1 
ATOM   3432 O  OD1  A ASN   A 1 159 ? 0.278  -0.574  2.047   0.60 26.90 ?  159 ASN   A OD1  1 
ATOM   3433 O  OD1  B ASN   A 1 159 ? 1.272  1.202   0.788   0.40 25.64 ?  159 ASN   A OD1  1 
ATOM   3434 N  ND2  A ASN   A 1 159 ? 1.057  1.208   0.918   0.60 26.89 ?  159 ASN   A ND2  1 
ATOM   3435 N  ND2  B ASN   A 1 159 ? 0.314  -0.567  1.790   0.40 25.25 ?  159 ASN   A ND2  1 
ATOM   3436 H  H    A ASN   A 1 159 ? 3.580  -0.330  2.895   0.60 26.26 ?  159 ASN   A H    1 
ATOM   3437 H  H    B ASN   A 1 159 ? 3.630  -0.234  2.523   0.40 24.56 ?  159 ASN   A H    1 
ATOM   3438 H  HA   A ASN   A 1 159 ? 2.018  -2.309  2.264   0.60 26.51 ?  159 ASN   A HA   1 
ATOM   3439 H  HA   B ASN   A 1 159 ? 2.142  -2.319  2.032   0.40 25.36 ?  159 ASN   A HA   1 
ATOM   3440 H  HB2  A ASN   A 1 159 ? 3.054  -0.231  0.678   0.60 28.65 ?  159 ASN   A HB2  1 
ATOM   3441 H  HB2  B ASN   A 1 159 ? 3.086  -0.367  0.222   0.40 27.46 ?  159 ASN   A HB2  1 
ATOM   3442 H  HB3  A ASN   A 1 159 ? 2.089  -1.329  0.053   0.60 28.65 ?  159 ASN   A HB3  1 
ATOM   3443 H  HB3  B ASN   A 1 159 ? 1.997  -1.457  -0.171  0.40 27.46 ?  159 ASN   A HB3  1 
ATOM   3444 H  HD21 A ASN   A 1 159 ? 0.392  1.701   1.154   0.60 32.24 ?  159 ASN   A HD21 1 
ATOM   3445 H  HD21 B ASN   A 1 159 ? -0.329 -0.089  2.099   0.40 30.28 ?  159 ASN   A HD21 1 
ATOM   3446 H  HD22 A ASN   A 1 159 ? 1.677  1.535   0.420   0.60 32.24 ?  159 ASN   A HD22 1 
ATOM   3447 H  HD22 B ASN   A 1 159 ? 0.339  -1.411  1.957   0.40 30.28 ?  159 ASN   A HD22 1 
ATOM   3448 N  N    A LEU   A 1 160 ? 4.982  -2.623  1.088   0.60 19.58 ?  160 LEU   A N    1 
ATOM   3449 N  N    B LEU   A 1 160 ? 5.132  -2.621  1.037   0.40 19.39 ?  160 LEU   A N    1 
ATOM   3450 C  CA   A LEU   A 1 160 ? 5.895  -3.617  0.534   0.60 18.89 ?  160 LEU   A CA   1 
ATOM   3451 C  CA   B LEU   A 1 160 ? 6.085  -3.625  0.582   0.40 18.58 ?  160 LEU   A CA   1 
ATOM   3452 C  C    A LEU   A 1 160 ? 6.102  -4.773  1.502   0.60 18.02 ?  160 LEU   A C    1 
ATOM   3453 C  C    B LEU   A 1 160 ? 6.207  -4.757  1.595   0.40 17.64 ?  160 LEU   A C    1 
ATOM   3454 O  O    A LEU   A 1 160 ? 6.144  -5.937  1.088   0.60 18.39 ?  160 LEU   A O    1 
ATOM   3455 O  O    B LEU   A 1 160 ? 6.178  -5.937  1.230   0.40 17.96 ?  160 LEU   A O    1 
ATOM   3456 C  CB   A LEU   A 1 160 ? 7.230  -2.969  0.181   0.60 18.70 ?  160 LEU   A CB   1 
ATOM   3457 C  CB   B LEU   A 1 160 ? 7.445  -2.980  0.328   0.40 18.69 ?  160 LEU   A CB   1 
ATOM   3458 C  CG   A LEU   A 1 160 ? 8.291  -3.961  -0.290  0.60 18.97 ?  160 LEU   A CG   1 
ATOM   3459 C  CG   B LEU   A 1 160 ? 8.546  -3.979  -0.021  0.40 18.91 ?  160 LEU   A CG   1 
ATOM   3460 C  CD1  A LEU   A 1 160 ? 7.797  -4.713  -1.510  0.60 19.23 ?  160 LEU   A CD1  1 
ATOM   3461 C  CD1  B LEU   A 1 160 ? 8.131  -4.808  -1.221  0.40 18.83 ?  160 LEU   A CD1  1 
ATOM   3462 C  CD2  A LEU   A 1 160 ? 9.598  -3.251  -0.585  0.60 19.08 ?  160 LEU   A CD2  1 
ATOM   3463 C  CD2  B LEU   A 1 160 ? 9.864  -3.273  -0.279  0.40 18.95 ?  160 LEU   A CD2  1 
ATOM   3464 H  H    A LEU   A 1 160 ? 5.335  -1.857  1.257   0.60 23.47 ?  160 LEU   A H    1 
ATOM   3465 H  H    B LEU   A 1 160 ? 5.479  -1.873  1.280   0.40 23.25 ?  160 LEU   A H    1 
ATOM   3466 H  HA   A LEU   A 1 160 ? 5.509  -3.973  -0.277  0.60 22.65 ?  160 LEU   A HA   1 
ATOM   3467 H  HA   B LEU   A 1 160 ? 5.766  -3.997  -0.253  0.40 22.28 ?  160 LEU   A HA   1 
ATOM   3468 H  HB2  A LEU   A 1 160 ? 7.089  -2.320  -0.531  0.60 22.41 ?  160 LEU   A HB2  1 
ATOM   3469 H  HB2  B LEU   A 1 160 ? 7.369  -2.335  -0.401  0.40 22.41 ?  160 LEU   A HB2  1 
ATOM   3470 H  HB3  A LEU   A 1 160 ? 7.578  -2.520  0.967   0.60 22.41 ?  160 LEU   A HB3  1 
ATOM   3471 H  HB3  B LEU   A 1 160 ? 7.717  -2.532  1.140   0.40 22.41 ?  160 LEU   A HB3  1 
ATOM   3472 H  HG   A LEU   A 1 160 ? 8.463  -4.606  0.413   0.60 22.74 ?  160 LEU   A HG   1 
ATOM   3473 H  HG   B LEU   A 1 160 ? 8.677  -4.578  0.730   0.40 22.67 ?  160 LEU   A HG   1 
ATOM   3474 H  HD11 A LEU   A 1 160 ? 8.522  -5.249  -1.861  0.60 23.05 ?  160 LEU   A HD11 1 
ATOM   3475 H  HD11 B LEU   A 1 160 ? 8.893  -5.320  -1.523  0.40 22.57 ?  160 LEU   A HD11 1 
ATOM   3476 H  HD12 A LEU   A 1 160 ? 7.059  -5.287  -1.252  0.60 23.05 ?  160 LEU   A HD12 1 
ATOM   3477 H  HD12 B LEU   A 1 160 ? 7.412  -5.406  -0.960  0.40 22.57 ?  160 LEU   A HD12 1 
ATOM   3478 H  HD13 A LEU   A 1 160 ? 7.503  -4.073  -2.177  0.60 23.05 ?  160 LEU   A HD13 1 
ATOM   3479 H  HD13 B LEU   A 1 160 ? 7.828  -4.212  -1.925  0.40 22.57 ?  160 LEU   A HD13 1 
ATOM   3480 H  HD21 A LEU   A 1 160 ? 10.253 -3.905  -0.879  0.60 22.87 ?  160 LEU   A HD21 1 
ATOM   3481 H  HD21 B LEU   A 1 160 ? 10.539 -3.937  -0.491  0.40 22.71 ?  160 LEU   A HD21 1 
ATOM   3482 H  HD22 A LEU   A 1 160 ? 9.451  -2.594  -1.283  0.60 22.87 ?  160 LEU   A HD22 1 
ATOM   3483 H  HD22 B LEU   A 1 160 ? 9.754  -2.662  -1.025  0.40 22.71 ?  160 LEU   A HD22 1 
ATOM   3484 H  HD23 A LEU   A 1 160 ? 9.910  -2.812  0.222   0.60 22.87 ?  160 LEU   A HD23 1 
ATOM   3485 H  HD23 B LEU   A 1 160 ? 10.121 -2.781  0.517   0.40 22.71 ?  160 LEU   A HD23 1 
ATOM   3486 N  N    A TYR   A 1 161 ? 6.234  -4.472  2.794   0.60 17.21 ?  161 TYR   A N    1 
ATOM   3487 N  N    B TYR   A 1 161 ? 6.350  -4.413  2.878   0.40 16.69 ?  161 TYR   A N    1 
ATOM   3488 C  CA   A TYR   A 1 161 ? 6.377  -5.526  3.791   0.60 16.80 ?  161 TYR   A CA   1 
ATOM   3489 C  CA   B TYR   A 1 161 ? 6.419  -5.438  3.915   0.40 16.21 ?  161 TYR   A CA   1 
ATOM   3490 C  C    A TYR   A 1 161 ? 5.235  -6.534  3.697   0.60 17.14 ?  161 TYR   A C    1 
ATOM   3491 C  C    B TYR   A 1 161 ? 5.217  -6.369  3.846   0.40 16.66 ?  161 TYR   A C    1 
ATOM   3492 O  O    A TYR   A 1 161 ? 5.462  -7.747  3.626   0.60 16.81 ?  161 TYR   A O    1 
ATOM   3493 O  O    B TYR   A 1 161 ? 5.359  -7.594  3.944   0.40 16.53 ?  161 TYR   A O    1 
ATOM   3494 C  CB   A TYR   A 1 161 ? 6.442  -4.910  5.189   0.60 16.92 ?  161 TYR   A CB   1 
ATOM   3495 C  CB   B TYR   A 1 161 ? 6.505  -4.780  5.294   0.40 15.89 ?  161 TYR   A CB   1 
ATOM   3496 C  CG   A TYR   A 1 161 ? 6.353  -5.941  6.279   0.60 16.30 ?  161 TYR   A CG   1 
ATOM   3497 C  CG   B TYR   A 1 161 ? 6.392  -5.757  6.447   0.40 15.13 ?  161 TYR   A CG   1 
ATOM   3498 C  CD1  A TYR   A 1 161 ? 7.473  -6.662  6.666   0.60 16.28 ?  161 TYR   A CD1  1 
ATOM   3499 C  CD1  B TYR   A 1 161 ? 7.509  -6.431  6.927   0.40 15.01 ?  161 TYR   A CD1  1 
ATOM   3500 C  CD2  A TYR   A 1 161 ? 5.147  -6.208  6.914   0.60 16.18 ?  161 TYR   A CD2  1 
ATOM   3501 C  CD2  B TYR   A 1 161 ? 5.169  -5.995  7.065   0.40 15.07 ?  161 TYR   A CD2  1 
ATOM   3502 C  CE1  A TYR   A 1 161 ? 7.397  -7.616  7.652   0.60 16.14 ?  161 TYR   A CE1  1 
ATOM   3503 C  CE1  B TYR   A 1 161 ? 7.410  -7.321  7.982   0.40 15.27 ?  161 TYR   A CE1  1 
ATOM   3504 C  CE2  A TYR   A 1 161 ? 5.060  -7.163  7.904   0.60 15.89 ?  161 TYR   A CE2  1 
ATOM   3505 C  CE2  B TYR   A 1 161 ? 5.061  -6.885  8.121   0.40 15.22 ?  161 TYR   A CE2  1 
ATOM   3506 C  CZ   A TYR   A 1 161 ? 6.190  -7.862  8.269   0.60 16.17 ?  161 TYR   A CZ   1 
ATOM   3507 C  CZ   B TYR   A 1 161 ? 6.184  -7.543  8.575   0.40 15.71 ?  161 TYR   A CZ   1 
ATOM   3508 O  OH   A TYR   A 1 161 ? 6.129  -8.816  9.255   0.60 16.59 ?  161 TYR   A OH   1 
ATOM   3509 O  OH   B TYR   A 1 161 ? 6.086  -8.428  9.625   0.40 16.83 ?  161 TYR   A OH   1 
ATOM   3510 H  H    A TYR   A 1 161 ? 6.231  -3.677  3.117   0.60 20.63 ?  161 TYR   A H    1 
ATOM   3511 H  H    B TYR   A 1 161 ? 6.401  -3.606  3.165   0.40 20.01 ?  161 TYR   A H    1 
ATOM   3512 H  HA   A TYR   A 1 161 ? 7.204  -6.002  3.637   0.60 20.14 ?  161 TYR   A HA   1 
ATOM   3513 H  HA   B TYR   A 1 161 ? 7.220  -5.966  3.786   0.40 19.43 ?  161 TYR   A HA   1 
ATOM   3514 H  HB2  A TYR   A 1 161 ? 7.286  -4.443  5.290   0.60 20.28 ?  161 TYR   A HB2  1 
ATOM   3515 H  HB2  B TYR   A 1 161 ? 7.360  -4.329  5.373   0.40 19.05 ?  161 TYR   A HB2  1 
ATOM   3516 H  HB3  A TYR   A 1 161 ? 5.703  -4.292  5.302   0.60 20.28 ?  161 TYR   A HB3  1 
ATOM   3517 H  HB3  B TYR   A 1 161 ? 5.785  -4.135  5.380   0.40 19.05 ?  161 TYR   A HB3  1 
ATOM   3518 H  HD1  A TYR   A 1 161 ? 8.287  -6.501  6.250   0.60 19.52 ?  161 TYR   A HD1  1 
ATOM   3519 H  HD1  B TYR   A 1 161 ? 8.337  -6.284  6.532   0.40 17.98 ?  161 TYR   A HD1  1 
ATOM   3520 H  HD2  A TYR   A 1 161 ? 4.381  -5.739  6.670   0.60 19.39 ?  161 TYR   A HD2  1 
ATOM   3521 H  HD2  B TYR   A 1 161 ? 4.407  -5.553  6.765   0.40 18.06 ?  161 TYR   A HD2  1 
ATOM   3522 H  HE1  A TYR   A 1 161 ? 8.156  -8.094  7.902   0.60 19.35 ?  161 TYR   A HE1  1 
ATOM   3523 H  HE1  B TYR   A 1 161 ? 8.166  -7.767  8.292   0.40 18.30 ?  161 TYR   A HE1  1 
ATOM   3524 H  HE2  A TYR   A 1 161 ? 4.244  -7.335  8.326   0.60 19.05 ?  161 TYR   A HE2  1 
ATOM   3525 H  HE2  B TYR   A 1 161 ? 4.234  -7.036  8.525   0.40 18.24 ?  161 TYR   A HE2  1 
ATOM   3526 H  HH   A TYR   A 1 161 ? 5.338  -8.876  9.552   0.60 19.88 ?  161 TYR   A HH   1 
ATOM   3527 H  HH   B TYR   A 1 161 ? 5.286  -8.473  9.894   0.40 20.17 ?  161 TYR   A HH   1 
ATOM   3528 N  N    A ASP   A 1 162 ? 3.993  -6.045  3.693   0.60 17.94 ?  162 ASP   A N    1 
ATOM   3529 N  N    B ASP   A 1 162 ? 4.019  -5.803  3.681   0.40 17.35 ?  162 ASP   A N    1 
ATOM   3530 C  CA   A ASP   A 1 162 ? 2.844  -6.946  3.626   0.60 18.62 ?  162 ASP   A CA   1 
ATOM   3531 C  CA   B ASP   A 1 162 ? 2.818  -6.626  3.574   0.40 18.35 ?  162 ASP   A CA   1 
ATOM   3532 C  C    A ASP   A 1 162 ? 2.889  -7.792  2.361   0.60 18.66 ?  162 ASP   A C    1 
ATOM   3533 C  C    B ASP   A 1 162 ? 2.895  -7.565  2.374   0.40 18.92 ?  162 ASP   A C    1 
ATOM   3534 O  O    A ASP   A 1 162 ? 2.555  -8.984  2.388   0.60 19.12 ?  162 ASP   A O    1 
ATOM   3535 O  O    B ASP   A 1 162 ? 2.516  -8.739  2.469   0.40 19.33 ?  162 ASP   A O    1 
ATOM   3536 C  CB   A ASP   A 1 162 ? 1.541  -6.146  3.679   0.60 19.63 ?  162 ASP   A CB   1 
ATOM   3537 C  CB   B ASP   A 1 162 ? 1.577  -5.735  3.472   0.40 19.05 ?  162 ASP   A CB   1 
ATOM   3538 C  CG   A ASP   A 1 162 ? 1.250  -5.577  5.052   0.60 20.87 ?  162 ASP   A CG   1 
ATOM   3539 C  CG   B ASP   A 1 162 ? 1.318  -4.933  4.740   0.40 19.32 ?  162 ASP   A CG   1 
ATOM   3540 O  OD1  A ASP   A 1 162 ? 1.915  -5.979  6.028   0.60 21.60 ?  162 ASP   A OD1  1 
ATOM   3541 O  OD1  B ASP   A 1 162 ? 1.841  -5.310  5.809   0.40 19.45 ?  162 ASP   A OD1  1 
ATOM   3542 O  OD2  A ASP   A 1 162 ? 0.341  -4.724  5.151   0.60 21.43 -1 162 ASP   A OD2  1 
ATOM   3543 O  OD2  B ASP   A 1 162 ? 0.571  -3.932  4.670   0.40 19.48 -1 162 ASP   A OD2  1 
ATOM   3544 H  H    A ASP   A 1 162 ? 3.789  -5.214  3.722   0.60 21.50 ?  162 ASP   A H    1 
ATOM   3545 H  H    B ASP   A 1 162 ? 3.880  -4.956  3.639   0.40 20.80 ?  162 ASP   A H    1 
ATOM   3546 H  HA   A ASP   A 1 162 ? 2.857  -7.550  4.383   0.60 22.32 ?  162 ASP   A HA   1 
ATOM   3547 H  HA   B ASP   A 1 162 ? 2.731  -7.166  4.374   0.40 21.99 ?  162 ASP   A HA   1 
ATOM   3548 H  HB2  A ASP   A 1 162 ? 1.596  -5.404  3.059   0.60 23.53 ?  162 ASP   A HB2  1 
ATOM   3549 H  HB2  B ASP   A 1 162 ? 1.691  -5.115  2.734   0.40 22.84 ?  162 ASP   A HB2  1 
ATOM   3550 H  HB3  A ASP   A 1 162 ? 0.798  -6.724  3.445   0.60 23.53 ?  162 ASP   A HB3  1 
ATOM   3551 H  HB3  B ASP   A 1 162 ? 0.798  -6.292  3.320   0.40 22.84 ?  162 ASP   A HB3  1 
ATOM   3552 N  N    A LYS   A 1 163 ? 3.297  -7.193  1.242   0.60 19.31 ?  163 LYS   A N    1 
ATOM   3553 N  N    B LYS   A 1 163 ? 3.380  -7.065  1.235   0.40 19.70 ?  163 LYS   A N    1 
ATOM   3554 C  CA   A LYS   A 1 163 ? 3.422  -7.958  0.008   0.60 20.13 ?  163 LYS   A CA   1 
ATOM   3555 C  CA   B LYS   A 1 163 ? 3.441  -7.891  0.031   0.40 20.35 ?  163 LYS   A CA   1 
ATOM   3556 C  C    A LYS   A 1 163 ? 4.534  -8.994  0.114   0.60 19.73 ?  163 LYS   A C    1 
ATOM   3557 C  C    B LYS   A 1 163 ? 4.511  -8.972  0.148   0.40 19.64 ?  163 LYS   A C    1 
ATOM   3558 O  O    A LYS   A 1 163 ? 4.400  -10.108 -0.403  0.60 20.15 ?  163 LYS   A O    1 
ATOM   3559 O  O    B LYS   A 1 163 ? 4.318  -10.098 -0.322  0.40 19.90 ?  163 LYS   A O    1 
ATOM   3560 C  CB   A LYS   A 1 163 ? 3.667  -7.023  -1.176  0.60 22.48 ?  163 LYS   A CB   1 
ATOM   3561 C  CB   B LYS   A 1 163 ? 3.694  -7.006  -1.192  0.40 22.34 ?  163 LYS   A CB   1 
ATOM   3562 C  CG   A LYS   A 1 163 ? 3.690  -7.739  -2.517  0.60 24.82 ?  163 LYS   A CG   1 
ATOM   3563 C  CG   B LYS   A 1 163 ? 3.804  -7.765  -2.507  0.40 24.30 ?  163 LYS   A CG   1 
ATOM   3564 C  CD   A LYS   A 1 163 ? 4.086  -6.805  -3.647  0.60 27.12 ?  163 LYS   A CD   1 
ATOM   3565 C  CD   B LYS   A 1 163 ? 3.799  -6.818  -3.702  0.40 26.33 ?  163 LYS   A CD   1 
ATOM   3566 C  CE   A LYS   A 1 163 ? 3.961  -7.496  -4.997  0.60 28.73 ?  163 LYS   A CE   1 
ATOM   3567 C  CE   B LYS   A 1 163 ? 5.171  -6.714  -4.348  0.40 27.46 ?  163 LYS   A CE   1 
ATOM   3568 N  NZ   A LYS   A 1 163 ? 4.542  -6.685  -6.099  0.60 29.62 ?  163 LYS   A NZ   1 
ATOM   3569 N  NZ   B LYS   A 1 163 ? 5.157  -5.887  -5.589  0.40 28.23 ?  163 LYS   A NZ   1 
ATOM   3570 H  H    A LYS   A 1 163 ? 3.500  -6.358  1.173   0.60 23.15 ?  163 LYS   A H    1 
ATOM   3571 H  H    B LYS   A 1 163 ? 3.671  -6.260  1.135   0.40 23.61 ?  163 LYS   A H    1 
ATOM   3572 H  HA   A LYS   A 1 163 ? 2.589  -8.427  -0.155  0.60 24.14 ?  163 LYS   A HA   1 
ATOM   3573 H  HA   B LYS   A 1 163 ? 2.585  -8.329  -0.092  0.40 24.40 ?  163 LYS   A HA   1 
ATOM   3574 H  HB2  A LYS   A 1 163 ? 2.957  -6.360  -1.208  0.60 26.95 ?  163 LYS   A HB2  1 
ATOM   3575 H  HB2  B LYS   A 1 163 ? 2.957  -6.378  -1.279  0.40 26.79 ?  163 LYS   A HB2  1 
ATOM   3576 H  HB3  A LYS   A 1 163 ? 4.522  -6.583  -1.060  0.60 26.95 ?  163 LYS   A HB3  1 
ATOM   3577 H  HB3  B LYS   A 1 163 ? 4.522  -6.520  -1.063  0.40 26.79 ?  163 LYS   A HB3  1 
ATOM   3578 H  HG2  A LYS   A 1 163 ? 4.335  -8.462  -2.485  0.60 29.76 ?  163 LYS   A HG2  1 
ATOM   3579 H  HG2  B LYS   A 1 163 ? 4.637  -8.264  -2.521  0.40 29.14 ?  163 LYS   A HG2  1 
ATOM   3580 H  HG3  A LYS   A 1 163 ? 2.804  -8.088  -2.707  0.60 29.76 ?  163 LYS   A HG3  1 
ATOM   3581 H  HG3  B LYS   A 1 163 ? 3.050  -8.368  -2.596  0.40 29.14 ?  163 LYS   A HG3  1 
ATOM   3582 H  HD2  A LYS   A 1 163 ? 3.498  -6.032  -3.645  0.60 32.52 ?  163 LYS   A HD2  1 
ATOM   3583 H  HD2  B LYS   A 1 163 ? 3.176  -7.146  -4.368  0.40 31.57 ?  163 LYS   A HD2  1 
ATOM   3584 H  HD3  A LYS   A 1 163 ? 5.007  -6.529  -3.527  0.60 32.52 ?  163 LYS   A HD3  1 
ATOM   3585 H  HD3  B LYS   A 1 163 ? 3.538  -5.931  -3.409  0.40 31.57 ?  163 LYS   A HD3  1 
ATOM   3586 H  HE2  A LYS   A 1 163 ? 4.417  -8.350  -4.972  0.60 34.45 ?  163 LYS   A HE2  1 
ATOM   3587 H  HE2  B LYS   A 1 163 ? 5.791  -6.308  -3.723  0.40 32.93 ?  163 LYS   A HE2  1 
ATOM   3588 H  HE3  A LYS   A 1 163 ? 3.023  -7.634  -5.191  0.60 34.45 ?  163 LYS   A HE3  1 
ATOM   3589 H  HE3  B LYS   A 1 163 ? 5.472  -7.603  -4.582  0.40 32.93 ?  163 LYS   A HE3  1 
ATOM   3590 H  HZ1  A LYS   A 1 163 ? 4.455  -7.117  -6.872  0.60 35.52 ?  163 LYS   A HZ1  1 
ATOM   3591 H  HZ1  B LYS   A 1 163 ? 5.974  -5.849  -5.941  0.40 33.86 ?  163 LYS   A HZ1  1 
ATOM   3592 H  HZ2  A LYS   A 1 163 ? 4.120  -5.904  -6.155  0.60 35.52 ?  163 LYS   A HZ2  1 
ATOM   3593 H  HZ2  B LYS   A 1 163 ? 4.602  -6.245  -6.187  0.40 33.86 ?  163 LYS   A HZ2  1 
ATOM   3594 H  HZ3  A LYS   A 1 163 ? 5.406  -6.536  -5.946  0.60 35.52 ?  163 LYS   A HZ3  1 
ATOM   3595 H  HZ3  B LYS   A 1 163 ? 4.885  -5.061  -5.400  0.40 33.86 ?  163 LYS   A HZ3  1 
ATOM   3596 N  N    . LEU   A 1 164 ? 5.647  -8.644  0.768   1.00 18.48 ?  164 LEU   A N    1 
ATOM   3597 C  CA   . LEU   A 1 164 ? 6.734  -9.611  0.919   1.00 17.33 ?  164 LEU   A CA   1 
ATOM   3598 C  C    . LEU   A 1 164 ? 6.301  -10.796 1.771   1.00 17.29 ?  164 LEU   A C    1 
ATOM   3599 O  O    . LEU   A 1 164 ? 6.610  -11.949 1.449   1.00 17.86 ?  164 LEU   A O    1 
ATOM   3600 C  CB   . LEU   A 1 164 ? 7.940  -8.926  1.549   1.00 16.77 ?  164 LEU   A CB   1 
ATOM   3601 C  CG   . LEU   A 1 164 ? 8.715  -7.966  0.649   1.00 17.06 ?  164 LEU   A CG   1 
ATOM   3602 C  CD1  . LEU   A 1 164 ? 9.641  -7.105  1.489   1.00 17.08 ?  164 LEU   A CD1  1 
ATOM   3603 C  CD2  . LEU   A 1 164 ? 9.507  -8.717  -0.413  1.00 17.34 ?  164 LEU   A CD2  1 
ATOM   3604 H  H    A LEU   A 1 164 ? 5.792  -7.872  1.124   0.60 22.15 ?  164 LEU   A H    1 
ATOM   3605 H  H    B LEU   A 1 164 ? 5.810  -7.869  1.110   0.40 22.15 ?  164 LEU   A H    1 
ATOM   3606 H  HA   . LEU   A 1 164 ? 6.989  -9.939  0.045   1.00 20.77 ?  164 LEU   A HA   1 
ATOM   3607 H  HB2  . LEU   A 1 164 ? 7.638  -8.414  2.314   1.00 20.10 ?  164 LEU   A HB2  1 
ATOM   3608 H  HB3  . LEU   A 1 164 ? 8.562  -9.607  1.838   1.00 20.10 ?  164 LEU   A HB3  1 
ATOM   3609 H  HG   . LEU   A 1 164 ? 8.094  -7.374  0.197   1.00 20.44 ?  164 LEU   A HG   1 
ATOM   3610 H  HD11 . LEU   A 1 164 ? 10.127 -6.497  0.909   1.00 20.47 ?  164 LEU   A HD11 1 
ATOM   3611 H  HD12 . LEU   A 1 164 ? 9.112  -6.600  2.127   1.00 20.47 ?  164 LEU   A HD12 1 
ATOM   3612 H  HD13 . LEU   A 1 164 ? 10.266 -7.679  1.962   1.00 20.47 ?  164 LEU   A HD13 1 
ATOM   3613 H  HD21 . LEU   A 1 164 ? 10.027 -8.079  -0.931  1.00 20.79 ?  164 LEU   A HD21 1 
ATOM   3614 H  HD22 . LEU   A 1 164 ? 10.100 -9.348  0.022   1.00 20.79 ?  164 LEU   A HD22 1 
ATOM   3615 H  HD23 . LEU   A 1 164 ? 8.888  -9.185  -0.993  1.00 20.79 ?  164 LEU   A HD23 1 
ATOM   3616 N  N    . VAL   A 1 165 ? 5.598  -10.525 2.871   1.00 16.90 ?  165 VAL   A N    1 
ATOM   3617 C  CA   . VAL   A 1 165 ? 5.116  -11.597 3.735   1.00 17.41 ?  165 VAL   A CA   1 
ATOM   3618 C  C    . VAL   A 1 165 ? 4.087  -12.444 3.002   1.00 17.42 ?  165 VAL   A C    1 
ATOM   3619 O  O    . VAL   A 1 165 ? 4.181  -13.677 2.962   1.00 17.47 ?  165 VAL   A O    1 
ATOM   3620 C  CB   . VAL   A 1 165 ? 4.541  -11.003 5.035   1.00 18.14 ?  165 VAL   A CB   1 
ATOM   3621 C  CG1  . VAL   A 1 165 ? 3.783  -12.061 5.822   1.00 18.36 ?  165 VAL   A CG1  1 
ATOM   3622 C  CG2  . VAL   A 1 165 ? 5.653  -10.383 5.870   1.00 18.80 ?  165 VAL   A CG2  1 
ATOM   3623 H  H    . VAL   A 1 165 ? 5.392  -9.733  3.137   1.00 20.26 ?  165 VAL   A H    1 
ATOM   3624 H  HA   . VAL   A 1 165 ? 5.861  -12.168 3.974   1.00 20.86 ?  165 VAL   A HA   1 
ATOM   3625 H  HB   . VAL   A 1 165 ? 3.919  -10.294 4.808   1.00 21.74 ?  165 VAL   A HB   1 
ATOM   3626 H  HG11 . VAL   A 1 165 ? 3.665  -11.749 6.733   1.00 22.01 ?  165 VAL   A HG11 1 
ATOM   3627 H  HG12 . VAL   A 1 165 ? 2.914  -12.198 5.409   1.00 22.01 ?  165 VAL   A HG12 1 
ATOM   3628 H  HG13 . VAL   A 1 165 ? 4.290  -12.883 5.816   1.00 22.01 ?  165 VAL   A HG13 1 
ATOM   3629 H  HG21 . VAL   A 1 165 ? 5.276  -10.039 6.696   1.00 22.53 ?  165 VAL   A HG21 1 
ATOM   3630 H  HG22 . VAL   A 1 165 ? 6.318  -11.061 6.068   1.00 22.53 ?  165 VAL   A HG22 1 
ATOM   3631 H  HG23 . VAL   A 1 165 ? 6.062  -9.658  5.368   1.00 22.53 ?  165 VAL   A HG23 1 
ATOM   3632 N  N    . SER   A 1 166 ? 3.089  -11.793 2.406   1.00 18.17 ?  166 SER   A N    1 
ATOM   3633 C  CA   . SER   A 1 166 ? 1.970  -12.530 1.833   1.00 19.79 ?  166 SER   A CA   1 
ATOM   3634 C  C    . SER   A 1 166 ? 2.387  -13.371 0.638   1.00 20.22 ?  166 SER   A C    1 
ATOM   3635 O  O    . SER   A 1 166 ? 1.731  -14.376 0.337   1.00 22.05 ?  166 SER   A O    1 
ATOM   3636 C  CB   . SER   A 1 166 ? 0.860  -11.566 1.416   1.00 22.51 ?  166 SER   A CB   1 
ATOM   3637 O  OG   . SER   A 1 166 ? 0.284  -10.922 2.538   1.00 25.26 ?  166 SER   A OG   1 
ATOM   3638 H  H    . SER   A 1 166 ? 3.030  -10.939 2.335   1.00 21.78 ?  166 SER   A H    1 
ATOM   3639 H  HA   . SER   A 1 166 ? 1.603  -13.127 2.501   1.00 23.72 ?  166 SER   A HA   1 
ATOM   3640 H  HB2  . SER   A 1 166 ? 1.222  -10.907 0.805   1.00 26.99 ?  166 SER   A HB2  1 
ATOM   3641 H  HB3  . SER   A 1 166 ? 0.151  -12.066 0.977   1.00 26.99 ?  166 SER   A HB3  1 
ATOM   3642 H  HG   . SER   A 1 166 ? -0.299 -10.368 2.290   1.00 30.29 ?  166 SER   A HG   1 
ATOM   3643 N  N    . SER   A 1 167 ? 3.451  -12.979 -0.062  1.00 19.43 ?  167 SER   A N    1 
ATOM   3644 C  CA   . SER   A 1 167 ? 3.902  -13.700 -1.243  1.00 20.18 ?  167 SER   A CA   1 
ATOM   3645 C  C    . SER   A 1 167 ? 5.056  -14.652 -0.956  1.00 20.11 ?  167 SER   A C    1 
ATOM   3646 O  O    . SER   A 1 167 ? 5.561  -15.289 -1.887  1.00 20.77 ?  167 SER   A O    1 
ATOM   3647 C  CB   . SER   A 1 167 ? 4.304  -12.716 -2.352  1.00 20.87 ?  167 SER   A CB   1 
ATOM   3648 O  OG   . SER   A 1 167 ? 5.407  -11.917 -1.952  1.00 21.28 ?  167 SER   A OG   1 
ATOM   3649 H  H    . SER   A 1 167 ? 3.932  -12.283 0.131   1.00 23.29 ?  167 SER   A H    1 
ATOM   3650 H  HA   . SER   A 1 167 ? 3.162  -14.222 -1.579  1.00 24.19 ?  167 SER   A HA   1 
ATOM   3651 H  HB2  . SER   A 1 167 ? 4.551  -13.220 -3.143  1.00 25.02 ?  167 SER   A HB2  1 
ATOM   3652 H  HB3  . SER   A 1 167 ? 3.541  -12.143 -2.558  1.00 25.02 ?  167 SER   A HB3  1 
ATOM   3653 H  HG   . SER   A 1 167 ? 5.189  -11.453 -1.283  1.00 25.51 ?  167 SER   A HG   1 
ATOM   3654 N  N    . PHE   A 1 168 ? 5.485  -14.767 0.298   1.00 19.77 ?  168 PHE   A N    1 
ATOM   3655 C  CA   . PHE   A 1 168 ? 6.663  -15.569 0.602   1.00 20.25 ?  168 PHE   A CA   1 
ATOM   3656 C  C    . PHE   A 1 168 ? 6.351  -17.054 0.497   1.00 22.74 ?  168 PHE   A C    1 
ATOM   3657 O  O    . PHE   A 1 168 ? 5.381  -17.542 1.086   1.00 23.57 ?  168 PHE   A O    1 
ATOM   3658 C  CB   . PHE   A 1 168 ? 7.175  -15.274 2.007   1.00 19.07 ?  168 PHE   A CB   1 
ATOM   3659 C  CG   . PHE   A 1 168 ? 8.445  -16.008 2.332   1.00 17.84 ?  168 PHE   A CG   1 
ATOM   3660 C  CD1  . PHE   A 1 168 ? 9.629  -15.628 1.740   1.00 17.91 ?  168 PHE   A CD1  1 
ATOM   3661 C  CD2  . PHE   A 1 168 ? 8.458  -17.094 3.197   1.00 17.20 ?  168 PHE   A CD2  1 
ATOM   3662 C  CE1  . PHE   A 1 168 ? 10.804 -16.297 2.011   1.00 17.52 ?  168 PHE   A CE1  1 
ATOM   3663 C  CE2  . PHE   A 1 168 ? 9.641  -17.764 3.475   1.00 17.28 ?  168 PHE   A CE2  1 
ATOM   3664 C  CZ   . PHE   A 1 168 ? 10.810 -17.362 2.880   1.00 17.21 ?  168 PHE   A CZ   1 
ATOM   3665 H  H    . PHE   A 1 168 ? 5.126  -14.380 0.977   1.00 23.70 ?  168 PHE   A H    1 
ATOM   3666 H  HA   . PHE   A 1 168 ? 7.370  -15.354 -0.033  1.00 24.27 ?  168 PHE   A HA   1 
ATOM   3667 H  HB2  . PHE   A 1 168 ? 7.349  -14.323 2.089   1.00 22.86 ?  168 PHE   A HB2  1 
ATOM   3668 H  HB3  . PHE   A 1 168 ? 6.500  -15.544 2.648   1.00 22.86 ?  168 PHE   A HB3  1 
ATOM   3669 H  HD1  . PHE   A 1 168 ? 9.642  -14.906 1.153   1.00 21.47 ?  168 PHE   A HD1  1 
ATOM   3670 H  HD2  . PHE   A 1 168 ? 7.667  -17.368 3.603   1.00 20.62 ?  168 PHE   A HD2  1 
ATOM   3671 H  HE1  . PHE   A 1 168 ? 11.603 -16.024 1.612   1.00 21.00 ?  168 PHE   A HE1  1 
ATOM   3672 H  HE2  . PHE   A 1 168 ? 9.639  -18.487 4.061   1.00 20.72 ?  168 PHE   A HE2  1 
ATOM   3673 H  HZ   . PHE   A 1 168 ? 11.608 -17.809 3.062   1.00 20.63 ?  168 PHE   A HZ   1 
ATOM   3674 N  N    . LEU   A 1 169 ? 7.201  -17.780 -0.222  1.00 26.91 ?  169 LEU   A N    1 
ATOM   3675 C  CA   . LEU   A 1 169 ? 7.008  -19.210 -0.380  1.00 33.15 ?  169 LEU   A CA   1 
ATOM   3676 C  C    . LEU   A 1 169 ? 7.888  -19.955 0.612   1.00 35.14 ?  169 LEU   A C    1 
ATOM   3677 O  O    . LEU   A 1 169 ? 7.400  -20.446 1.631   1.00 35.92 ?  169 LEU   A O    1 
ATOM   3678 C  CB   . LEU   A 1 169 ? 7.317  -19.642 -1.816  1.00 35.98 ?  169 LEU   A CB   1 
ATOM   3679 C  CG   . LEU   A 1 169 ? 7.005  -21.099 -2.166  1.00 38.64 ?  169 LEU   A CG   1 
ATOM   3680 C  CD1  . LEU   A 1 169 ? 5.599  -21.476 -1.723  1.00 39.47 ?  169 LEU   A CD1  1 
ATOM   3681 C  CD2  . LEU   A 1 169 ? 7.173  -21.334 -3.660  1.00 39.57 ?  169 LEU   A CD2  1 
ATOM   3682 O  OXT  . LEU   A 1 169 ? 9.102  -20.067 0.431   1.00 35.17 -1 169 LEU   A OXT  1 
ATOM   3683 H  H    . LEU   A 1 169 ? 7.897  -17.467 -0.620  1.00 32.26 ?  169 LEU   A H    1 
ATOM   3684 H  HA   . LEU   A 1 169 ? 6.083  -19.422 -0.188  1.00 39.76 ?  169 LEU   A HA   1 
ATOM   3685 H  HB2  . LEU   A 1 169 ? 6.798  -19.086 -2.417  1.00 43.15 ?  169 LEU   A HB2  1 
ATOM   3686 H  HB3  . LEU   A 1 169 ? 8.261  -19.503 -1.980  1.00 43.15 ?  169 LEU   A HB3  1 
ATOM   3687 H  HG   . LEU   A 1 169 ? 7.630  -21.677 -1.702  1.00 46.35 ?  169 LEU   A HG   1 
ATOM   3688 H  HD11 . LEU   A 1 169 ? 5.355  -22.319 -2.135  1.00 47.34 ?  169 LEU   A HD11 1 
ATOM   3689 H  HD12 . LEU   A 1 169 ? 5.584  -21.564 -0.757  1.00 47.34 ?  169 LEU   A HD12 1 
ATOM   3690 H  HD13 . LEU   A 1 169 ? 4.983  -20.781 -2.004  1.00 47.34 ?  169 LEU   A HD13 1 
ATOM   3691 H  HD21 . LEU   A 1 169 ? 6.977  -22.264 -3.858  1.00 47.46 ?  169 LEU   A HD21 1 
ATOM   3692 H  HD22 . LEU   A 1 169 ? 6.557  -20.758 -4.141  1.00 47.46 ?  169 LEU   A HD22 1 
ATOM   3693 H  HD23 . LEU   A 1 169 ? 8.086  -21.126 -3.912  1.00 47.46 ?  169 LEU   A HD23 1 
ATOM   3694 N  N    A SER   B 1 1   ? 50.713 -9.183  -23.691 0.60 30.41 ?  1   SER   B N    1 
ATOM   3695 N  N    B SER   B 1 1   ? 50.708 -9.224  -23.706 0.40 27.82 ?  1   SER   B N    1 
ATOM   3696 C  CA   A SER   B 1 1   ? 51.235 -10.257 -22.823 0.60 30.39 ?  1   SER   B CA   1 
ATOM   3697 C  CA   B SER   B 1 1   ? 51.179 -10.234 -22.735 0.40 27.76 ?  1   SER   B CA   1 
ATOM   3698 C  C    A SER   B 1 1   ? 50.170 -11.313 -22.575 0.60 28.82 ?  1   SER   B C    1 
ATOM   3699 C  C    B SER   B 1 1   ? 50.103 -11.282 -22.489 0.40 26.59 ?  1   SER   B C    1 
ATOM   3700 O  O    A SER   B 1 1   ? 48.979 -11.106 -22.835 0.60 28.28 ?  1   SER   B O    1 
ATOM   3701 O  O    B SER   B 1 1   ? 48.939 -11.112 -22.870 0.40 25.96 ?  1   SER   B O    1 
ATOM   3702 C  CB   A SER   B 1 1   ? 51.713 -9.689  -21.490 0.60 31.10 ?  1   SER   B CB   1 
ATOM   3703 C  CB   B SER   B 1 1   ? 51.564 -9.572  -21.415 0.40 28.20 ?  1   SER   B CB   1 
ATOM   3704 O  OG   A SER   B 1 1   ? 50.616 -9.312  -20.680 0.60 32.63 ?  1   SER   B OG   1 
ATOM   3705 O  OG   B SER   B 1 1   ? 50.441 -9.478  -20.559 0.40 29.28 ?  1   SER   B OG   1 
ATOM   3706 H  H1   A SER   B 1 1   ? 50.501 -9.527  -24.482 0.60 36.47 ?  1   SER   B H1   1 
ATOM   3707 H  H1   B SER   B 1 1   ? 51.406 -8.762  -24.003 0.40 33.36 ?  1   SER   B H1   1 
ATOM   3708 H  H2   A SER   B 1 1   ? 49.995 -8.828  -23.312 0.60 36.47 ?  1   SER   B H2   1 
ATOM   3709 H  H2   B SER   B 1 1   ? 50.312 -9.638  -24.384 0.40 33.36 ?  1   SER   B H2   1 
ATOM   3710 H  H3   A SER   B 1 1   ? 51.342 -8.564  -23.790 0.60 36.47 ?  1   SER   B H3   1 
ATOM   3711 H  H3   B SER   B 1 1   ? 50.135 -8.682  -23.304 0.40 33.36 ?  1   SER   B H3   1 
ATOM   3712 H  HA   A SER   B 1 1   ? 51.986 -10.671 -23.269 0.60 36.45 ?  1   SER   B HA   1 
ATOM   3713 H  HA   B SER   B 1 1   ? 51.962 -10.667 -23.103 0.40 33.29 ?  1   SER   B HA   1 
ATOM   3714 H  HB2  A SER   B 1 1   ? 52.231 -10.370 -21.034 0.60 37.29 ?  1   SER   B HB2  1 
ATOM   3715 H  HB2  B SER   B 1 1   ? 52.251 -10.107 -20.991 0.40 33.82 ?  1   SER   B HB2  1 
ATOM   3716 H  HB3  A SER   B 1 1   ? 52.262 -8.908  -21.657 0.60 37.29 ?  1   SER   B HB3  1 
ATOM   3717 H  HB3  B SER   B 1 1   ? 51.900 -8.679  -21.593 0.40 33.82 ?  1   SER   B HB3  1 
ATOM   3718 H  HG   A SER   B 1 1   ? 50.881 -8.816  -20.057 0.60 39.13 ?  1   SER   B HG   1 
ATOM   3719 H  HG   B SER   B 1 1   ? 50.526 -8.816  -20.052 0.40 35.11 ?  1   SER   B HG   1 
ATOM   3720 N  N    A MET   B 1 2   ? 50.620 -12.445 -22.052 0.60 27.41 ?  2   MET   B N    1 
ATOM   3721 N  N    B MET   B 1 2   ? 50.505 -12.362 -21.830 0.40 25.78 ?  2   MET   B N    1 
ATOM   3722 C  CA   A MET   B 1 2   ? 49.795 -13.631 -21.881 0.60 26.66 ?  2   MET   B CA   1 
ATOM   3723 C  CA   B MET   B 1 2   ? 49.690 -13.565 -21.686 0.40 25.28 ?  2   MET   B CA   1 
ATOM   3724 C  C    A MET   B 1 2   ? 49.563 -13.828 -20.391 0.60 23.18 ?  2   MET   B C    1 
ATOM   3725 C  C    B MET   B 1 2   ? 49.412 -13.793 -20.205 0.40 23.12 ?  2   MET   B C    1 
ATOM   3726 O  O    A MET   B 1 2   ? 50.512 -14.062 -19.636 0.60 22.70 ?  2   MET   B O    1 
ATOM   3727 O  O    B MET   B 1 2   ? 50.281 -14.275 -19.471 0.40 23.47 ?  2   MET   B O    1 
ATOM   3728 C  CB   A MET   B 1 2   ? 50.507 -14.830 -22.495 0.60 30.31 ?  2   MET   B CB   1 
ATOM   3729 C  CB   B MET   B 1 2   ? 50.441 -14.740 -22.289 0.40 27.47 ?  2   MET   B CB   1 
ATOM   3730 C  CG   A MET   B 1 2   ? 49.654 -16.078 -22.639 0.60 33.61 ?  2   MET   B CG   1 
ATOM   3731 C  CG   B MET   B 1 2   ? 49.576 -15.906 -22.736 0.40 29.35 ?  2   MET   B CG   1 
ATOM   3732 S  SD   A MET   B 1 2   ? 50.494 -17.336 -23.617 0.60 36.58 ?  2   MET   B SD   1 
ATOM   3733 S  SD   B MET   B 1 2   ? 50.494 -17.016 -23.813 0.40 31.29 ?  2   MET   B SD   1 
ATOM   3734 C  CE   A MET   B 1 2   ? 51.061 -16.325 -24.982 0.60 37.01 ?  2   MET   B CE   1 
ATOM   3735 C  CE   B MET   B 1 2   ? 51.388 -15.833 -24.806 0.40 31.54 ?  2   MET   B CE   1 
ATOM   3736 H  H    A MET   B 1 2   ? 51.427 -12.554 -21.774 0.60 32.87 ?  2   MET   B H    1 
ATOM   3737 H  H    B MET   B 1 2   ? 51.277 -12.429 -21.457 0.40 30.92 ?  2   MET   B H    1 
ATOM   3738 H  HA   A MET   B 1 2   ? 48.948 -13.519 -22.336 0.60 31.96 ?  2   MET   B HA   1 
ATOM   3739 H  HA   B MET   B 1 2   ? 48.858 -13.457 -22.173 0.40 30.31 ?  2   MET   B HA   1 
ATOM   3740 H  HB2  A MET   B 1 2   ? 50.808 -14.551 -23.371 0.60 36.35 ?  2   MET   B HB2  1 
ATOM   3741 H  HB2  B MET   B 1 2   ? 50.924 -14.380 -23.042 0.40 32.94 ?  2   MET   B HB2  1 
ATOM   3742 H  HB3  A MET   B 1 2   ? 51.271 -15.070 -21.951 0.60 36.35 ?  2   MET   B HB3  1 
ATOM   3743 H  HB3  B MET   B 1 2   ? 51.069 -15.095 -21.646 0.40 32.94 ?  2   MET   B HB3  1 
ATOM   3744 H  HG2  A MET   B 1 2   ? 49.474 -16.442 -21.756 0.60 40.30 ?  2   MET   B HG2  1 
ATOM   3745 H  HG2  B MET   B 1 2   ? 49.283 -16.407 -21.956 0.40 35.20 ?  2   MET   B HG2  1 
ATOM   3746 H  HG3  A MET   B 1 2   ? 48.825 -15.856 -23.089 0.60 40.30 ?  2   MET   B HG3  1 
ATOM   3747 H  HG3  B MET   B 1 2   ? 48.811 -15.584 -23.230 0.40 35.20 ?  2   MET   B HG3  1 
ATOM   3748 H  HE1  A MET   B 1 2   ? 51.236 -16.895 -25.735 0.60 44.39 ?  2   MET   B HE1  1 
ATOM   3749 H  HE1  B MET   B 1 2   ? 51.661 -16.273 -25.606 0.40 37.83 ?  2   MET   B HE1  1 
ATOM   3750 H  HE2  A MET   B 1 2   ? 50.364 -15.682 -25.200 0.60 44.39 ?  2   MET   B HE2  1 
ATOM   3751 H  HE2  B MET   B 1 2   ? 50.798 -15.088 -25.018 0.40 37.83 ?  2   MET   B HE2  1 
ATOM   3752 H  HE3  A MET   B 1 2   ? 51.873 -15.851 -24.724 0.60 44.39 ?  2   MET   B HE3  1 
ATOM   3753 H  HE3  B MET   B 1 2   ? 52.166 -15.515 -24.311 0.40 37.83 ?  2   MET   B HE3  1 
ATOM   3754 N  N    A VAL   B 1 3   ? 48.307 -13.704 -19.968 0.60 20.77 ?  3   VAL   B N    1 
ATOM   3755 N  N    B VAL   B 1 3   ? 48.206 -13.447 -19.767 0.40 20.93 ?  3   VAL   B N    1 
ATOM   3756 C  CA   A VAL   B 1 3   ? 47.907 -13.959 -18.592 0.60 19.60 ?  3   VAL   B CA   1 
ATOM   3757 C  CA   B VAL   B 1 3   ? 47.763 -13.720 -18.406 0.40 19.35 ?  3   VAL   B CA   1 
ATOM   3758 C  C    A VAL   B 1 3   ? 46.667 -14.841 -18.608 0.60 17.74 ?  3   VAL   B C    1 
ATOM   3759 C  C    B VAL   B 1 3   ? 46.516 -14.591 -18.456 0.40 17.45 ?  3   VAL   B C    1 
ATOM   3760 O  O    A VAL   B 1 3   ? 45.964 -14.951 -19.615 0.60 17.75 ?  3   VAL   B O    1 
ATOM   3761 O  O    B VAL   B 1 3   ? 45.684 -14.478 -19.360 0.40 17.19 ?  3   VAL   B O    1 
ATOM   3762 C  CB   A VAL   B 1 3   ? 47.632 -12.659 -17.807 0.60 21.06 ?  3   VAL   B CB   1 
ATOM   3763 C  CB   B VAL   B 1 3   ? 47.508 -12.441 -17.577 0.40 19.91 ?  3   VAL   B CB   1 
ATOM   3764 C  CG1  A VAL   B 1 3   ? 48.894 -11.810 -17.720 0.60 21.79 ?  3   VAL   B CG1  1 
ATOM   3765 C  CG1  B VAL   B 1 3   ? 48.782 -11.616 -17.459 0.40 20.23 ?  3   VAL   B CG1  1 
ATOM   3766 C  CG2  A VAL   B 1 3   ? 46.497 -11.880 -18.454 0.60 21.79 ?  3   VAL   B CG2  1 
ATOM   3767 C  CG2  B VAL   B 1 3   ? 46.381 -11.623 -18.183 0.40 20.08 ?  3   VAL   B CG2  1 
ATOM   3768 H  H    A VAL   B 1 3   ? 47.659 -13.463 -20.475 0.60 24.90 ?  3   VAL   B H    1 
ATOM   3769 H  H    B VAL   B 1 3   ? 47.620 -13.048 -20.254 0.40 25.09 ?  3   VAL   B H    1 
ATOM   3770 H  HA   A VAL   B 1 3   ? 48.619 -14.441 -18.137 0.60 23.49 ?  3   VAL   B HA   1 
ATOM   3771 H  HA   B VAL   B 1 3   ? 48.452 -14.225 -17.953 0.40 23.20 ?  3   VAL   B HA   1 
ATOM   3772 H  HB   A VAL   B 1 3   ? 47.363 -12.891 -16.904 0.60 25.25 ?  3   VAL   B HB   1 
ATOM   3773 H  HB   B VAL   B 1 3   ? 47.241 -12.699 -16.682 0.40 23.87 ?  3   VAL   B HB   1 
ATOM   3774 H  HG11 A VAL   B 1 3   ? 48.699 -11.009 -17.210 0.60 26.12 ?  3   VAL   B HG11 1 
ATOM   3775 H  HG11 B VAL   B 1 3   ? 48.600 -10.830 -16.921 0.40 24.25 ?  3   VAL   B HG11 1 
ATOM   3776 H  HG12 A VAL   B 1 3   ? 49.589 -12.323 -17.277 0.60 26.12 ?  3   VAL   B HG12 1 
ATOM   3777 H  HG12 B VAL   B 1 3   ? 49.469 -12.155 -17.036 0.40 24.25 ?  3   VAL   B HG12 1 
ATOM   3778 H  HG13 A VAL   B 1 3   ? 49.177 -11.573 -18.616 0.60 26.12 ?  3   VAL   B HG13 1 
ATOM   3779 H  HG13 B VAL   B 1 3   ? 49.069 -11.350 -18.347 0.40 24.25 ?  3   VAL   B HG13 1 
ATOM   3780 H  HG21 A VAL   B 1 3   ? 46.438 -11.008 -18.037 0.60 26.12 ?  3   VAL   B HG21 1 
ATOM   3781 H  HG21 B VAL   B 1 3   ? 46.348 -10.760 -17.743 0.40 24.08 ?  3   VAL   B HG21 1 
ATOM   3782 H  HG22 A VAL   B 1 3   ? 46.680 -11.783 -19.401 0.60 26.12 ?  3   VAL   B HG22 1 
ATOM   3783 H  HG22 B VAL   B 1 3   ? 46.549 -11.507 -19.130 0.40 24.08 ?  3   VAL   B HG22 1 
ATOM   3784 H  HG23 A VAL   B 1 3   ? 45.666 -12.365 -18.326 0.60 26.12 ?  3   VAL   B HG23 1 
ATOM   3785 H  HG23 B VAL   B 1 3   ? 45.543 -12.094 -18.050 0.40 24.08 ?  3   VAL   B HG23 1 
ATOM   3786 N  N    . ASN   B 1 4   ? 46.398 -15.471 -17.464 1.00 16.30 ?  4   ASN   B N    1 
ATOM   3787 C  CA   . ASN   B 1 4   ? 45.267 -16.391 -17.347 1.00 15.10 ?  4   ASN   B CA   1 
ATOM   3788 C  C    . ASN   B 1 4   ? 45.217 -17.356 -18.530 1.00 15.40 ?  4   ASN   B C    1 
ATOM   3789 O  O    . ASN   B 1 4   ? 44.157 -17.622 -19.093 1.00 16.23 ?  4   ASN   B O    1 
ATOM   3790 C  CB   . ASN   B 1 4   ? 43.939 -15.648 -17.182 1.00 14.33 ?  4   ASN   B CB   1 
ATOM   3791 C  CG   . ASN   B 1 4   ? 43.892 -14.820 -15.917 1.00 13.80 ?  4   ASN   B CG   1 
ATOM   3792 O  OD1  . ASN   B 1 4   ? 44.178 -15.314 -14.830 1.00 13.67 ?  4   ASN   B OD1  1 
ATOM   3793 N  ND2  . ASN   B 1 4   ? 43.546 -13.546 -16.054 1.00 14.45 ?  4   ASN   B ND2  1 
ATOM   3794 H  H    A ASN   B 1 4   ? 46.852 -15.376 -16.743 0.60 19.54 ?  4   ASN   B H    1 
ATOM   3795 H  H    B ASN   B 1 4   ? 46.978 -15.558 -16.838 0.40 19.54 ?  4   ASN   B H    1 
ATOM   3796 H  HA   . ASN   B 1 4   ? 45.400 -16.922 -16.545 1.00 18.10 ?  4   ASN   B HA   1 
ATOM   3797 H  HB2  . ASN   B 1 4   ? 43.807 -15.056 -17.934 1.00 17.17 ?  4   ASN   B HB2  1 
ATOM   3798 H  HB3  . ASN   B 1 4   ? 43.218 -16.300 -17.141 1.00 17.17 ?  4   ASN   B HB3  1 
ATOM   3799 H  HD21 . ASN   B 1 4   ? 43.506 -13.033 -15.362 1.00 17.32 ?  4   ASN   B HD21 1 
ATOM   3800 H  HD22 . ASN   B 1 4   ? 43.355 -13.231 -16.831 1.00 17.32 ?  4   ASN   B HD22 1 
ATOM   3801 N  N    . SER   B 1 5   ? 46.379 -17.880 -18.912 1.00 16.61 ?  5   SER   B N    1 
ATOM   3802 C  CA   . SER   B 1 5   ? 46.480 -18.793 -20.049 1.00 18.94 ?  5   SER   B CA   1 
ATOM   3803 C  C    . SER   B 1 5   ? 46.470 -20.229 -19.535 1.00 20.31 ?  5   SER   B C    1 
ATOM   3804 O  O    . SER   B 1 5   ? 47.480 -20.927 -19.504 1.00 22.78 ?  5   SER   B O    1 
ATOM   3805 C  CB   . SER   B 1 5   ? 47.732 -18.489 -20.865 1.00 20.15 ?  5   SER   B CB   1 
ATOM   3806 O  OG   . SER   B 1 5   ? 48.902 -18.697 -20.094 1.00 22.71 ?  5   SER   B OG   1 
ATOM   3807 H  H    . SER   B 1 5   ? 47.132 -17.726 -18.525 1.00 19.91 ?  5   SER   B H    1 
ATOM   3808 H  HA   . SER   B 1 5   ? 45.712 -18.676 -20.623 1.00 22.70 ?  5   SER   B HA   1 
ATOM   3809 H  HB2  . SER   B 1 5   ? 47.748 -19.064 -21.648 1.00 24.15 ?  5   SER   B HB2  1 
ATOM   3810 H  HB3  . SER   B 1 5   ? 47.689 -17.561 -21.142 1.00 24.15 ?  5   SER   B HB3  1 
ATOM   3811 H  HG   . SER   B 1 5   ? 48.968 -19.508 -19.884 1.00 27.23 ?  5   SER   B HG   1 
ATOM   3812 N  N    . PHE   B 1 6   ? 45.286 -20.647 -19.104 1.00 20.34 ?  6   PHE   B N    1 
ATOM   3813 C  CA   . PHE   B 1 6   ? 45.088 -21.993 -18.593 1.00 19.98 ?  6   PHE   B CA   1 
ATOM   3814 C  C    . PHE   B 1 6   ? 45.017 -22.974 -19.753 1.00 23.21 ?  6   PHE   B C    1 
ATOM   3815 O  O    . PHE   B 1 6   ? 44.362 -22.708 -20.765 1.00 25.59 ?  6   PHE   B O    1 
ATOM   3816 C  CB   . PHE   B 1 6   ? 43.795 -22.046 -17.781 1.00 17.70 ?  6   PHE   B CB   1 
ATOM   3817 C  CG   . PHE   B 1 6   ? 43.818 -21.190 -16.545 1.00 15.80 ?  6   PHE   B CG   1 
ATOM   3818 C  CD1  . PHE   B 1 6   ? 44.339 -21.682 -15.362 1.00 14.60 ?  6   PHE   B CD1  1 
ATOM   3819 C  CD2  . PHE   B 1 6   ? 43.327 -19.891 -16.566 1.00 15.39 ?  6   PHE   B CD2  1 
ATOM   3820 C  CE1  . PHE   B 1 6   ? 44.355 -20.904 -14.217 1.00 14.29 ?  6   PHE   B CE1  1 
ATOM   3821 C  CE2  . PHE   B 1 6   ? 43.349 -19.102 -15.429 1.00 15.78 ?  6   PHE   B CE2  1 
ATOM   3822 C  CZ   . PHE   B 1 6   ? 43.869 -19.602 -14.257 1.00 14.61 ?  6   PHE   B CZ   1 
ATOM   3823 H  H    . PHE   B 1 6   ? 44.574 -20.171 -19.104 1.00 24.38 ?  6   PHE   B H    1 
ATOM   3824 H  HA   . PHE   B 1 6   ? 45.826 -22.243 -18.017 1.00 23.95 ?  6   PHE   B HA   1 
ATOM   3825 H  HB2  . PHE   B 1 6   ? 43.062 -21.738 -18.337 1.00 21.21 ?  6   PHE   B HB2  1 
ATOM   3826 H  HB3  . PHE   B 1 6   ? 43.632 -22.960 -17.501 1.00 21.21 ?  6   PHE   B HB3  1 
ATOM   3827 H  HD1  . PHE   B 1 6   ? 44.677 -22.548 -15.334 1.00 17.49 ?  6   PHE   B HD1  1 
ATOM   3828 H  HD2  . PHE   B 1 6   ? 42.971 -19.549 -17.355 1.00 18.44 ?  6   PHE   B HD2  1 
ATOM   3829 H  HE1  . PHE   B 1 6   ? 44.720 -21.241 -13.428 1.00 17.12 ?  6   PHE   B HE1  1 
ATOM   3830 H  HE2  . PHE   B 1 6   ? 43.011 -18.236 -15.455 1.00 18.91 ?  6   PHE   B HE2  1 
ATOM   3831 H  HZ   . PHE   B 1 6   ? 43.884 -19.077 -13.489 1.00 17.51 ?  6   PHE   B HZ   1 
ATOM   3832 N  N    . SER   B 1 7   ? 45.710 -24.104 -19.610 1.00 24.38 ?  7   SER   B N    1 
ATOM   3833 C  CA   . SER   B 1 7   ? 45.796 -25.096 -20.671 1.00 26.47 ?  7   SER   B CA   1 
ATOM   3834 C  C    . SER   B 1 7   ? 45.737 -26.495 -20.078 1.00 25.51 ?  7   SER   B C    1 
ATOM   3835 O  O    . SER   B 1 7   ? 46.312 -26.757 -19.018 1.00 26.44 ?  7   SER   B O    1 
ATOM   3836 C  CB   . SER   B 1 7   ? 47.097 -24.933 -21.469 1.00 29.43 ?  7   SER   B CB   1 
ATOM   3837 O  OG   . SER   B 1 7   ? 47.139 -25.824 -22.569 1.00 31.55 ?  7   SER   B OG   1 
ATOM   3838 H  H    . SER   B 1 7   ? 46.146 -24.321 -18.896 1.00 29.24 ?  7   SER   B H    1 
ATOM   3839 H  HA   . SER   B 1 7   ? 45.050 -24.994 -21.278 1.00 31.73 ?  7   SER   B HA   1 
ATOM   3840 H  HB2  . SER   B 1 7   ? 47.149 -24.022 -21.800 1.00 35.29 ?  7   SER   B HB2  1 
ATOM   3841 H  HB3  . SER   B 1 7   ? 47.851 -25.115 -20.885 1.00 35.29 ?  7   SER   B HB3  1 
ATOM   3842 H  HG   . SER   B 1 7   ? 47.856 -25.723 -22.995 1.00 37.83 ?  7   SER   B HG   1 
ATOM   3843 N  N    . GLY   B 1 8   ? 45.038 -27.390 -20.772 1.00 25.53 ?  8   GLY   B N    1 
ATOM   3844 C  CA   . GLY   B 1 8   ? 45.003 -28.782 -20.382 1.00 24.69 ?  8   GLY   B CA   1 
ATOM   3845 C  C    . GLY   B 1 8   ? 44.053 -29.106 -19.259 1.00 23.22 ?  8   GLY   B C    1 
ATOM   3846 O  O    . GLY   B 1 8   ? 44.192 -30.166 -18.636 1.00 24.57 ?  8   GLY   B O    1 
ATOM   3847 H  H    . GLY   B 1 8   ? 44.580 -27.209 -21.475 1.00 30.61 ?  8   GLY   B H    1 
ATOM   3848 H  HA2  . GLY   B 1 8   ? 44.748 -29.317 -21.150 1.00 29.61 ?  8   GLY   B HA2  1 
ATOM   3849 H  HA3  . GLY   B 1 8   ? 45.887 -29.057 -20.103 1.00 29.61 ?  8   GLY   B HA3  1 
ATOM   3850 N  N    . TYR   B 1 9   ? 43.076 -28.244 -18.986 1.00 21.30 ?  9   TYR   B N    1 
ATOM   3851 C  CA   . TYR   B 1 9   ? 42.114 -28.513 -17.930 1.00 19.06 ?  9   TYR   B CA   1 
ATOM   3852 C  C    . TYR   B 1 9   ? 40.935 -29.309 -18.456 1.00 18.44 ?  9   TYR   B C    1 
ATOM   3853 O  O    . TYR   B 1 9   ? 40.520 -29.168 -19.610 1.00 20.70 ?  9   TYR   B O    1 
ATOM   3854 C  CB   . TYR   B 1 9   ? 41.602 -27.223 -17.297 1.00 18.59 ?  9   TYR   B CB   1 
ATOM   3855 C  CG   . TYR   B 1 9   ? 42.617 -26.595 -16.379 1.00 17.84 ?  9   TYR   B CG   1 
ATOM   3856 C  CD1  . TYR   B 1 9   ? 43.706 -25.912 -16.895 1.00 18.42 ?  9   TYR   B CD1  1 
ATOM   3857 C  CD2  . TYR   B 1 9   ? 42.506 -26.707 -15.002 1.00 17.16 ?  9   TYR   B CD2  1 
ATOM   3858 C  CE1  . TYR   B 1 9   ? 44.655 -25.348 -16.065 1.00 18.45 ?  9   TYR   B CE1  1 
ATOM   3859 C  CE2  . TYR   B 1 9   ? 43.450 -26.147 -14.162 1.00 17.49 ?  9   TYR   B CE2  1 
ATOM   3860 C  CZ   . TYR   B 1 9   ? 44.523 -25.466 -14.701 1.00 18.14 ?  9   TYR   B CZ   1 
ATOM   3861 O  OH   . TYR   B 1 9   ? 45.468 -24.912 -13.872 1.00 19.20 ?  9   TYR   B OH   1 
ATOM   3862 H  H    . TYR   B 1 9   ? 42.936 -27.509 -19.411 1.00 25.54 ?  9   TYR   B H    1 
ATOM   3863 H  HA   . TYR   B 1 9   ? 42.538 -29.036 -17.237 1.00 22.85 ?  9   TYR   B HA   1 
ATOM   3864 H  HB2  . TYR   B 1 9   ? 41.380 -26.579 -17.991 1.00 22.29 ?  9   TYR   B HB2  1 
ATOM   3865 H  HB3  . TYR   B 1 9   ? 40.817 -27.430 -16.772 1.00 22.29 ?  9   TYR   B HB3  1 
ATOM   3866 H  HD1  . TYR   B 1 9   ? 43.799 -25.830 -17.817 1.00 22.07 ?  9   TYR   B HD1  1 
ATOM   3867 H  HD2  . TYR   B 1 9   ? 41.782 -27.168 -14.636 1.00 20.57 ?  9   TYR   B HD2  1 
ATOM   3868 H  HE1  . TYR   B 1 9   ? 45.374 -24.892 -16.427 1.00 22.11 ?  9   TYR   B HE1  1 
ATOM   3869 H  HE2  . TYR   B 1 9   ? 43.354 -26.232 -13.240 1.00 20.96 ?  9   TYR   B HE2  1 
ATOM   3870 H  HH   . TYR   B 1 9   ? 46.055 -24.533 -14.329 1.00 23.01 ?  9   TYR   B HH   1 
ATOM   3871 N  N    . LEU   B 1 10  ? 40.403 -30.156 -17.584 1.00 16.49 ?  10  LEU   B N    1 
ATOM   3872 C  CA   . LEU   B 1 10  ? 39.200 -30.917 -17.857 1.00 16.35 ?  10  LEU   B CA   1 
ATOM   3873 C  C    . LEU   B 1 10  ? 38.008 -30.157 -17.290 1.00 15.75 ?  10  LEU   B C    1 
ATOM   3874 O  O    . LEU   B 1 10  ? 38.023 -29.740 -16.128 1.00 15.78 ?  10  LEU   B O    1 
ATOM   3875 C  CB   . LEU   B 1 10  ? 39.312 -32.289 -17.195 1.00 17.23 ?  10  LEU   B CB   1 
ATOM   3876 C  CG   . LEU   B 1 10  ? 38.160 -33.236 -17.512 1.00 19.30 ?  10  LEU   B CG   1 
ATOM   3877 C  CD1  . LEU   B 1 10  ? 38.277 -33.762 -18.936 1.00 20.98 ?  10  LEU   B CD1  1 
ATOM   3878 C  CD2  . LEU   B 1 10  ? 38.097 -34.373 -16.511 1.00 20.50 ?  10  LEU   B CD2  1 
ATOM   3879 H  H    . LEU   B 1 10  ? 40.731 -30.308 -16.799 1.00 19.77 ?  10  LEU   B H    1 
ATOM   3880 H  HA   . LEU   B 1 10  ? 39.083 -31.034 -18.811 1.00 19.59 ?  10  LEU   B HA   1 
ATOM   3881 H  HB2  . LEU   B 1 10  ? 40.134 -32.716 -17.495 1.00 20.66 ?  10  LEU   B HB2  1 
ATOM   3882 H  HB3  . LEU   B 1 10  ? 39.341 -32.173 -16.232 1.00 20.66 ?  10  LEU   B HB3  1 
ATOM   3883 H  HG   . LEU   B 1 10  ? 37.326 -32.746 -17.449 1.00 23.14 ?  10  LEU   B HG   1 
ATOM   3884 H  HD11 . LEU   B 1 10  ? 37.557 -34.393 -19.098 1.00 25.16 ?  10  LEU   B HD11 1 
ATOM   3885 H  HD12 . LEU   B 1 10  ? 38.206 -33.017 -19.554 1.00 25.16 ?  10  LEU   B HD12 1 
ATOM   3886 H  HD13 . LEU   B 1 10  ? 39.133 -34.201 -19.042 1.00 25.16 ?  10  LEU   B HD13 1 
ATOM   3887 H  HD21 . LEU   B 1 10  ? 37.358 -34.954 -16.746 1.00 24.58 ?  10  LEU   B HD21 1 
ATOM   3888 H  HD22 . LEU   B 1 10  ? 38.931 -34.862 -16.541 1.00 24.58 ?  10  LEU   B HD22 1 
ATOM   3889 H  HD23 . LEU   B 1 10  ? 37.959 -34.000 -15.627 1.00 24.58 ?  10  LEU   B HD23 1 
ATOM   3890 N  N    . LYS   B 1 11  ? 36.984 -29.977 -18.113 1.00 16.93 ?  11  LYS   B N    1 
ATOM   3891 C  CA   . LYS   B 1 11  ? 35.789 -29.257 -17.699 1.00 19.14 ?  11  LYS   B CA   1 
ATOM   3892 C  C    . LYS   B 1 11  ? 34.905 -30.178 -16.866 1.00 18.39 ?  11  LYS   B C    1 
ATOM   3893 O  O    . LYS   B 1 11  ? 34.511 -31.255 -17.328 1.00 20.14 ?  11  LYS   B O    1 
ATOM   3894 C  CB   . LYS   B 1 11  ? 35.046 -28.777 -18.944 1.00 22.93 ?  11  LYS   B CB   1 
ATOM   3895 C  CG   . LYS   B 1 11  ? 33.908 -27.808 -18.684 1.00 26.49 ?  11  LYS   B CG   1 
ATOM   3896 C  CD   . LYS   B 1 11  ? 33.169 -27.497 -19.981 1.00 29.46 ?  11  LYS   B CD   1 
ATOM   3897 C  CE   . LYS   B 1 11  ? 32.143 -26.394 -19.797 1.00 31.58 ?  11  LYS   B CE   1 
ATOM   3898 N  NZ   . LYS   B 1 11  ? 32.785 -25.076 -19.554 1.00 32.65 ?  11  LYS   B NZ   1 
ATOM   3899 H  H    . LYS   B 1 11  ? 36.952 -30.274 -18.920 1.00 20.29 ?  11  LYS   B H    1 
ATOM   3900 H  HA   . LYS   B 1 11  ? 36.037 -28.490 -17.162 1.00 22.94 ?  11  LYS   B HA   1 
ATOM   3901 H  HB2  . LYS   B 1 11  ? 35.682 -28.332 -19.527 1.00 27.49 ?  11  LYS   B HB2  1 
ATOM   3902 H  HB3  . LYS   B 1 11  ? 34.675 -29.549 -19.399 1.00 27.49 ?  11  LYS   B HB3  1 
ATOM   3903 H  HG2  . LYS   B 1 11  ? 33.280 -28.205 -18.061 1.00 31.76 ?  11  LYS   B HG2  1 
ATOM   3904 H  HG3  . LYS   B 1 11  ? 34.263 -26.979 -18.327 1.00 31.76 ?  11  LYS   B HG3  1 
ATOM   3905 H  HD2  . LYS   B 1 11  ? 33.809 -27.208 -20.651 1.00 35.32 ?  11  LYS   B HD2  1 
ATOM   3906 H  HD3  . LYS   B 1 11  ? 32.707 -28.295 -20.284 1.00 35.32 ?  11  LYS   B HD3  1 
ATOM   3907 H  HE2  . LYS   B 1 11  ? 31.602 -26.325 -20.600 1.00 37.87 ?  11  LYS   B HE2  1 
ATOM   3908 H  HE3  . LYS   B 1 11  ? 31.584 -26.609 -19.035 1.00 37.87 ?  11  LYS   B HE3  1 
ATOM   3909 H  HZ1  . LYS   B 1 11  ? 32.162 -24.446 -19.470 1.00 39.15 ?  11  LYS   B HZ1  1 
ATOM   3910 H  HZ2  . LYS   B 1 11  ? 33.270 -25.106 -18.809 1.00 39.15 ?  11  LYS   B HZ2  1 
ATOM   3911 H  HZ3  . LYS   B 1 11  ? 33.316 -24.866 -20.237 1.00 39.15 ?  11  LYS   B HZ3  1 
ATOM   3912 N  N    . LEU   B 1 12  ? 34.586 -29.758 -15.642 1.00 16.85 ?  12  LEU   B N    1 
ATOM   3913 C  CA   . LEU   B 1 12  ? 33.627 -30.469 -14.803 1.00 16.67 ?  12  LEU   B CA   1 
ATOM   3914 C  C    . LEU   B 1 12  ? 32.235 -29.864 -14.892 1.00 16.60 ?  12  LEU   B C    1 
ATOM   3915 O  O    . LEU   B 1 12  ? 31.250 -30.583 -15.065 1.00 16.97 ?  12  LEU   B O    1 
ATOM   3916 C  CB   . LEU   B 1 12  ? 34.085 -30.490 -13.342 1.00 15.98 ?  12  LEU   B CB   1 
ATOM   3917 C  CG   . LEU   B 1 12  ? 35.427 -31.164 -13.071 1.00 15.93 ?  12  LEU   B CG   1 
ATOM   3918 C  CD1  . LEU   B 1 12  ? 35.757 -31.115 -11.590 1.00 16.02 ?  12  LEU   B CD1  1 
ATOM   3919 C  CD2  . LEU   B 1 12  ? 35.424 -32.597 -13.575 1.00 16.41 ?  12  LEU   B CD2  1 
ATOM   3920 H  H    . LEU   B 1 12  ? 34.909 -29.051 -15.275 1.00 20.19 ?  12  LEU   B H    1 
ATOM   3921 H  HA   . LEU   B 1 12  ? 33.558 -31.384 -15.110 1.00 19.98 ?  12  LEU   B HA   1 
ATOM   3922 H  HB2  . LEU   B 1 12  ? 34.150 -29.578 -13.029 1.00 19.15 ?  12  LEU   B HB2  1 
ATOM   3923 H  HB3  . LEU   B 1 12  ? 33.414 -30.964 -12.821 1.00 19.15 ?  12  LEU   B HB3  1 
ATOM   3924 H  HG   . LEU   B 1 12  ? 36.121 -30.683 -13.546 1.00 19.10 ?  12  LEU   B HG   1 
ATOM   3925 H  HD11 . LEU   B 1 12  ? 36.616 -31.547 -11.444 1.00 19.20 ?  12  LEU   B HD11 1 
ATOM   3926 H  HD12 . LEU   B 1 12  ? 35.801 -30.190 -11.305 1.00 19.20 ?  12  LEU   B HD12 1 
ATOM   3927 H  HD13 . LEU   B 1 12  ? 35.067 -31.584 -11.095 1.00 19.20 ?  12  LEU   B HD13 1 
ATOM   3928 H  HD21 . LEU   B 1 12  ? 36.224 -33.044 -13.259 1.00 19.66 ?  12  LEU   B HD21 1 
ATOM   3929 H  HD22 . LEU   B 1 12  ? 34.635 -33.048 -13.238 1.00 19.66 ?  12  LEU   B HD22 1 
ATOM   3930 H  HD23 . LEU   B 1 12  ? 35.411 -32.589 -14.546 1.00 19.66 ?  12  LEU   B HD23 1 
ATOM   3931 N  N    . THR   B 1 13  ? 32.143 -28.546 -14.772 1.00 16.29 ?  13  THR   B N    1 
ATOM   3932 C  CA   . THR   B 1 13  ? 30.915 -27.795 -14.969 1.00 16.19 ?  13  THR   B CA   1 
ATOM   3933 C  C    . THR   B 1 13  ? 31.248 -26.596 -15.849 1.00 18.30 ?  13  THR   B C    1 
ATOM   3934 O  O    . THR   B 1 13  ? 32.393 -26.404 -16.275 1.00 19.03 ?  13  THR   B O    1 
ATOM   3935 C  CB   . THR   B 1 13  ? 30.324 -27.323 -13.635 1.00 15.75 ?  13  THR   B CB   1 
ATOM   3936 O  OG1  . THR   B 1 13  ? 31.173 -26.309 -13.083 1.00 15.69 ?  13  THR   B OG1  1 
ATOM   3937 C  CG2  . THR   B 1 13  ? 30.205 -28.481 -12.649 1.00 16.57 ?  13  THR   B CG2  1 
ATOM   3938 H  H    . THR   B 1 13  ? 32.812 -28.043 -14.568 1.00 19.53 ?  13  THR   B H    1 
ATOM   3939 H  HA   . THR   B 1 13  ? 30.261 -28.349 -15.417 1.00 19.40 ?  13  THR   B HA   1 
ATOM   3940 H  HB   . THR   B 1 13  ? 29.434 -26.956 -13.782 1.00 18.88 ?  13  THR   B HB   1 
ATOM   3941 H  HG1  . THR   B 1 13  ? 30.885 -25.546 -13.291 1.00 18.80 ?  13  THR   B HG1  1 
ATOM   3942 H  HG21 . THR   B 1 13  ? 29.700 -28.205 -11.868 1.00 19.85 ?  13  THR   B HG21 1 
ATOM   3943 H  HG22 . THR   B 1 13  ? 29.748 -29.227 -13.069 1.00 19.85 ?  13  THR   B HG22 1 
ATOM   3944 H  HG23 . THR   B 1 13  ? 31.087 -28.770 -12.368 1.00 19.85 ?  13  THR   B HG23 1 
ATOM   3945 N  N    A ASP   B 1 14  ? 30.234 -25.770 -16.107 0.60 19.33 ?  14  ASP   B N    1 
ATOM   3946 N  N    B ASP   B 1 14  ? 30.238 -25.760 -16.102 0.40 19.12 ?  14  ASP   B N    1 
ATOM   3947 C  CA   A ASP   B 1 14  ? 30.442 -24.608 -16.963 0.60 20.65 ?  14  ASP   B CA   1 
ATOM   3948 C  CA   B ASP   B 1 14  ? 30.435 -24.602 -16.970 0.40 20.08 ?  14  ASP   B CA   1 
ATOM   3949 C  C    A ASP   B 1 14  ? 31.548 -23.703 -16.433 0.60 18.68 ?  14  ASP   B C    1 
ATOM   3950 C  C    B ASP   B 1 14  ? 31.437 -23.602 -16.408 0.40 18.24 ?  14  ASP   B C    1 
ATOM   3951 O  O    A ASP   B 1 14  ? 32.226 -23.034 -17.222 0.60 19.77 ?  14  ASP   B O    1 
ATOM   3952 O  O    B ASP   B 1 14  ? 31.892 -22.726 -17.152 0.40 18.69 ?  14  ASP   B O    1 
ATOM   3953 C  CB   A ASP   B 1 14  ? 29.134 -23.831 -17.122 0.60 24.19 ?  14  ASP   B CB   1 
ATOM   3954 C  CB   B ASP   B 1 14  ? 29.109 -23.884 -17.215 0.40 23.03 ?  14  ASP   B CB   1 
ATOM   3955 C  CG   A ASP   B 1 14  ? 28.158 -24.510 -18.060 0.60 27.60 ?  14  ASP   B CG   1 
ATOM   3956 C  CG   B ASP   B 1 14  ? 28.219 -24.626 -18.193 0.40 25.77 ?  14  ASP   B CG   1 
ATOM   3957 O  OD1  A ASP   B 1 14  ? 28.506 -25.557 -18.649 0.60 28.60 ?  14  ASP   B OD1  1 
ATOM   3958 O  OD1  B ASP   B 1 14  ? 28.760 -25.298 -19.096 0.40 26.65 ?  14  ASP   B OD1  1 
ATOM   3959 O  OD2  A ASP   B 1 14  ? 27.033 -23.990 -18.205 0.60 28.86 -1 14  ASP   B OD2  1 
ATOM   3960 O  OD2  B ASP   B 1 14  ? 26.980 -24.541 -18.060 0.40 26.66 -1 14  ASP   B OD2  1 
ATOM   3961 H  H    A ASP   B 1 14  ? 29.438 -25.849 -15.792 0.60 23.17 ?  14  ASP   B H    1 
ATOM   3962 H  H    B ASP   B 1 14  ? 29.443 -25.839 -15.785 0.40 22.91 ?  14  ASP   B H    1 
ATOM   3963 H  HA   A ASP   B 1 14  ? 30.715 -24.908 -17.840 0.60 24.76 ?  14  ASP   B HA   1 
ATOM   3964 H  HA   B ASP   B 1 14  ? 30.767 -24.911 -17.827 0.40 24.08 ?  14  ASP   B HA   1 
ATOM   3965 H  HB2  A ASP   B 1 14  ? 28.694 -23.759 -16.263 0.60 29.00 ?  14  ASP   B HB2  1 
ATOM   3966 H  HB2  B ASP   B 1 14  ? 28.634 -23.803 -16.373 0.40 27.61 ?  14  ASP   B HB2  1 
ATOM   3967 H  HB3  A ASP   B 1 14  ? 29.323 -22.951 -17.479 0.60 29.00 ?  14  ASP   B HB3  1 
ATOM   3968 H  HB3  B ASP   B 1 14  ? 29.295 -22.998 -17.574 0.40 27.61 ?  14  ASP   B HB3  1 
ATOM   3969 N  N    . ASN   B 1 15  ? 31.763 -23.683 -15.115 1.00 16.40 ?  15  ASN   B N    1 
ATOM   3970 C  CA   . ASN   B 1 15  ? 32.722 -22.763 -14.513 1.00 14.26 ?  15  ASN   B CA   1 
ATOM   3971 C  C    . ASN   B 1 15  ? 33.816 -23.420 -13.679 1.00 13.34 ?  15  ASN   B C    1 
ATOM   3972 O  O    . ASN   B 1 15  ? 34.662 -22.696 -13.147 1.00 13.33 ?  15  ASN   B O    1 
ATOM   3973 C  CB   . ASN   B 1 15  ? 32.007 -21.715 -13.646 1.00 14.66 ?  15  ASN   B CB   1 
ATOM   3974 C  CG   . ASN   B 1 15  ? 31.388 -22.319 -12.408 1.00 14.33 ?  15  ASN   B CG   1 
ATOM   3975 O  OD1  . ASN   B 1 15  ? 30.445 -23.112 -12.498 1.00 15.75 ?  15  ASN   B OD1  1 
ATOM   3976 N  ND2  . ASN   B 1 15  ? 31.913 -21.974 -11.248 1.00 13.47 ?  15  ASN   B ND2  1 
ATOM   3977 H  H    A ASN   B 1 15  ? 31.367 -24.201 -14.551 0.60 19.66 ?  15  ASN   B H    1 
ATOM   3978 H  H    B ASN   B 1 15  ? 31.414 -24.243 -14.561 0.40 19.66 ?  15  ASN   B H    1 
ATOM   3979 H  HA   . ASN   B 1 15  ? 33.166 -22.279 -15.218 1.00 17.09 ?  15  ASN   B HA   1 
ATOM   3980 H  HB2  . ASN   B 1 15  ? 32.652 -21.040 -13.366 1.00 17.56 ?  15  ASN   B HB2  1 
ATOM   3981 H  HB3  . ASN   B 1 15  ? 31.300 -21.295 -14.164 1.00 17.56 ?  15  ASN   B HB3  1 
ATOM   3982 H  HD21 . ASN   B 1 15  ? 31.593 -22.291 -10.513 1.00 16.14 ?  15  ASN   B HD21 1 
ATOM   3983 H  HD22 . ASN   B 1 15  ? 32.577 -21.422 -11.216 1.00 16.14 ?  15  ASN   B HD22 1 
ATOM   3984 N  N    . VAL   B 1 16  ? 33.830 -24.745 -13.536 1.00 13.22 ?  16  VAL   B N    1 
ATOM   3985 C  CA   . VAL   B 1 16  ? 34.831 -25.437 -12.727 1.00 12.72 ?  16  VAL   B CA   1 
ATOM   3986 C  C    . VAL   B 1 16  ? 35.629 -26.376 -13.619 1.00 13.00 ?  16  VAL   B C    1 
ATOM   3987 O  O    . VAL   B 1 16  ? 35.054 -27.254 -14.281 1.00 14.05 ?  16  VAL   B O    1 
ATOM   3988 C  CB   . VAL   B 1 16  ? 34.203 -26.205 -11.549 1.00 13.23 ?  16  VAL   B CB   1 
ATOM   3989 C  CG1  . VAL   B 1 16  ? 35.289 -26.934 -10.758 1.00 13.25 ?  16  VAL   B CG1  1 
ATOM   3990 C  CG2  . VAL   B 1 16  ? 33.411 -25.259 -10.654 1.00 14.02 ?  16  VAL   B CG2  1 
ATOM   3991 H  H    . VAL   B 1 16  ? 33.253 -25.274 -13.898 1.00 15.85 ?  16  VAL   B H    1 
ATOM   3992 H  HA   . VAL   B 1 16  ? 35.444 -24.781 -12.358 1.00 15.24 ?  16  VAL   B HA   1 
ATOM   3993 H  HB   . VAL   B 1 16  ? 33.592 -26.871 -11.899 1.00 15.85 ?  16  VAL   B HB   1 
ATOM   3994 H  HG11 . VAL   B 1 16  ? 34.916 -27.230 -9.913  1.00 15.88 ?  16  VAL   B HG11 1 
ATOM   3995 H  HG12 . VAL   B 1 16  ? 35.600 -27.696 -11.267 1.00 15.88 ?  16  VAL   B HG12 1 
ATOM   3996 H  HG13 . VAL   B 1 16  ? 36.025 -26.320 -10.594 1.00 15.88 ?  16  VAL   B HG13 1 
ATOM   3997 H  HG21 . VAL   B 1 16  ? 33.070 -25.756 -9.895  1.00 16.80 ?  16  VAL   B HG21 1 
ATOM   3998 H  HG22 . VAL   B 1 16  ? 33.995 -24.548 -10.351 1.00 16.80 ?  16  VAL   B HG22 1 
ATOM   3999 H  HG23 . VAL   B 1 16  ? 32.674 -24.887 -11.164 1.00 16.80 ?  16  VAL   B HG23 1 
ATOM   4000 N  N    . TYR   B 1 17  ? 36.953 -26.207 -13.595 1.00 12.98 ?  17  TYR   B N    1 
ATOM   4001 C  CA   . TYR   B 1 17  ? 37.899 -26.953 -14.410 1.00 13.51 ?  17  TYR   B CA   1 
ATOM   4002 C  C    . TYR   B 1 17  ? 38.948 -27.564 -13.494 1.00 12.74 ?  17  TYR   B C    1 
ATOM   4003 O  O    . TYR   B 1 17  ? 39.219 -27.039 -12.412 1.00 12.91 ?  17  TYR   B O    1 
ATOM   4004 C  CB   . TYR   B 1 17  ? 38.606 -26.022 -15.403 1.00 16.09 ?  17  TYR   B CB   1 
ATOM   4005 C  CG   . TYR   B 1 17  ? 37.676 -25.252 -16.305 1.00 18.92 ?  17  TYR   B CG   1 
ATOM   4006 C  CD1  . TYR   B 1 17  ? 37.080 -24.070 -15.881 1.00 20.36 ?  17  TYR   B CD1  1 
ATOM   4007 C  CD2  . TYR   B 1 17  ? 37.395 -25.706 -17.585 1.00 20.99 ?  17  TYR   B CD2  1 
ATOM   4008 C  CE1  . TYR   B 1 17  ? 36.225 -23.362 -16.709 1.00 21.84 ?  17  TYR   B CE1  1 
ATOM   4009 C  CE2  . TYR   B 1 17  ? 36.546 -25.008 -18.420 1.00 22.66 ?  17  TYR   B CE2  1 
ATOM   4010 C  CZ   . TYR   B 1 17  ? 35.962 -23.838 -17.978 1.00 23.32 ?  17  TYR   B CZ   1 
ATOM   4011 O  OH   . TYR   B 1 17  ? 35.117 -23.142 -18.810 1.00 24.79 ?  17  TYR   B OH   1 
ATOM   4012 H  H    . TYR   B 1 17  ? 37.349 -25.633 -13.084 1.00 15.55 ?  17  TYR   B H    1 
ATOM   4013 H  HA   . TYR   B 1 17  ? 37.443 -27.661 -14.895 1.00 16.19 ?  17  TYR   B HA   1 
ATOM   4014 H  HB2  . TYR   B 1 17  ? 39.143 -25.383 -14.911 1.00 19.28 ?  17  TYR   B HB2  1 
ATOM   4015 H  HB3  . TYR   B 1 17  ? 39.173 -26.558 -15.973 1.00 19.28 ?  17  TYR   B HB3  1 
ATOM   4016 H  HD1  . TYR   B 1 17  ? 37.256 -23.748 -15.027 1.00 24.40 ?  17  TYR   B HD1  1 
ATOM   4017 H  HD2  . TYR   B 1 17  ? 37.782 -26.494 -17.888 1.00 25.16 ?  17  TYR   B HD2  1 
ATOM   4018 H  HE1  . TYR   B 1 17  ? 35.832 -22.571 -16.414 1.00 26.19 ?  17  TYR   B HE1  1 
ATOM   4019 H  HE2  . TYR   B 1 17  ? 36.362 -25.325 -19.277 1.00 27.16 ?  17  TYR   B HE2  1 
ATOM   4020 H  HH   . TYR   B 1 17  ? 35.040 -23.537 -19.548 1.00 29.72 ?  17  TYR   B HH   1 
ATOM   4021 N  N    . ILE   B 1 18  ? 39.558 -28.668 -13.928 1.00 12.75 ?  18  ILE   B N    1 
ATOM   4022 C  CA   . ILE   B 1 18  ? 40.489 -29.391 -13.068 1.00 12.90 ?  18  ILE   B CA   1 
ATOM   4023 C  C    . ILE   B 1 18  ? 41.650 -29.938 -13.888 1.00 13.20 ?  18  ILE   B C    1 
ATOM   4024 O  O    . ILE   B 1 18  ? 41.488 -30.336 -15.047 1.00 14.46 ?  18  ILE   B O    1 
ATOM   4025 C  CB   . ILE   B 1 18  ? 39.740 -30.491 -12.270 1.00 13.50 ?  18  ILE   B CB   1 
ATOM   4026 C  CG1  . ILE   B 1 18  ? 40.597 -31.033 -11.122 1.00 14.04 ?  18  ILE   B CG1  1 
ATOM   4027 C  CG2  . ILE   B 1 18  ? 39.238 -31.603 -13.195 1.00 13.70 ?  18  ILE   B CG2  1 
ATOM   4028 C  CD1  . ILE   B 1 18  ? 39.782 -31.828 -10.104 1.00 15.53 ?  18  ILE   B CD1  1 
ATOM   4029 H  H    . ILE   B 1 18  ? 39.451 -29.018 -14.707 1.00 15.27 ?  18  ILE   B H    1 
ATOM   4030 H  HA   . ILE   B 1 18  ? 40.854 -28.775 -12.419 1.00 15.46 ?  18  ILE   B HA   1 
ATOM   4031 H  HB   . ILE   B 1 18  ? 38.959 -30.082 -11.870 1.00 16.18 ?  18  ILE   B HB   1 
ATOM   4032 H  HG12 . ILE   B 1 18  ? 41.280 -31.616 -11.480 1.00 16.83 ?  18  ILE   B HG12 1 
ATOM   4033 H  HG13 . ILE   B 1 18  ? 41.006 -30.284 -10.656 1.00 16.83 ?  18  ILE   B HG13 1 
ATOM   4034 H  HG21 . ILE   B 1 18  ? 38.653 -32.192 -12.692 1.00 16.42 ?  18  ILE   B HG21 1 
ATOM   4035 H  HG22 . ILE   B 1 18  ? 38.748 -31.199 -13.928 1.00 16.42 ?  18  ILE   B HG22 1 
ATOM   4036 H  HG23 . ILE   B 1 18  ? 39.996 -32.100 -13.534 1.00 16.42 ?  18  ILE   B HG23 1 
ATOM   4037 H  HD11 . ILE   B 1 18  ? 40.366 -32.104 -9.380  1.00 18.61 ?  18  ILE   B HD11 1 
ATOM   4038 H  HD12 . ILE   B 1 18  ? 39.071 -31.264 -9.758  1.00 18.61 ?  18  ILE   B HD12 1 
ATOM   4039 H  HD13 . ILE   B 1 18  ? 39.405 -32.606 -10.541 1.00 18.61 ?  18  ILE   B HD13 1 
ATOM   4040 N  N    . LYS   B 1 19  ? 42.831 -29.969 -13.265 1.00 13.66 ?  19  LYS   B N    1 
ATOM   4041 C  CA   . LYS   B 1 19  ? 44.041 -30.443 -13.920 1.00 14.57 ?  19  LYS   B CA   1 
ATOM   4042 C  C    . LYS   B 1 19  ? 44.938 -31.124 -12.900 1.00 14.47 ?  19  LYS   B C    1 
ATOM   4043 O  O    . LYS   B 1 19  ? 45.022 -30.691 -11.748 1.00 13.95 ?  19  LYS   B O    1 
ATOM   4044 C  CB   . LYS   B 1 19  ? 44.812 -29.274 -14.549 1.00 15.86 ?  19  LYS   B CB   1 
ATOM   4045 C  CG   . LYS   B 1 19  ? 46.021 -29.679 -15.373 1.00 17.72 ?  19  LYS   B CG   1 
ATOM   4046 C  CD   . LYS   B 1 19  ? 46.736 -28.444 -15.906 1.00 19.32 ?  19  LYS   B CD   1 
ATOM   4047 C  CE   . LYS   B 1 19  ? 47.900 -28.813 -16.803 1.00 21.32 ?  19  LYS   B CE   1 
ATOM   4048 N  NZ   . LYS   B 1 19  ? 48.619 -27.612 -17.296 1.00 22.09 ?  19  LYS   B NZ   1 
ATOM   4049 H  H    . LYS   B 1 19  ? 42.951 -29.716 -12.449 1.00 16.37 ?  19  LYS   B H    1 
ATOM   4050 H  HA   . LYS   B 1 19  ? 43.809 -31.080 -14.614 1.00 17.46 ?  19  LYS   B HA   1 
ATOM   4051 H  HB2  . LYS   B 1 19  ? 44.209 -28.790 -15.134 1.00 19.01 ?  19  LYS   B HB2  1 
ATOM   4052 H  HB3  . LYS   B 1 19  ? 45.117 -28.688 -13.837 1.00 19.01 ?  19  LYS   B HB3  1 
ATOM   4053 H  HG2  . LYS   B 1 19  ? 46.637 -30.179 -14.817 1.00 21.24 ?  19  LYS   B HG2  1 
ATOM   4054 H  HG3  . LYS   B 1 19  ? 45.727 -30.218 -16.125 1.00 21.24 ?  19  LYS   B HG3  1 
ATOM   4055 H  HD2  . LYS   B 1 19  ? 46.108 -27.911 -16.420 1.00 23.16 ?  19  LYS   B HD2  1 
ATOM   4056 H  HD3  . LYS   B 1 19  ? 47.076 -27.928 -15.157 1.00 23.16 ?  19  LYS   B HD3  1 
ATOM   4057 H  HE2  . LYS   B 1 19  ? 48.525 -29.361 -16.302 1.00 25.56 ?  19  LYS   B HE2  1 
ATOM   4058 H  HE3  . LYS   B 1 19  ? 47.565 -29.305 -17.570 1.00 25.56 ?  19  LYS   B HE3  1 
ATOM   4059 H  HZ1  . LYS   B 1 19  ? 49.266 -27.855 -17.858 1.00 26.49 ?  19  LYS   B HZ1  1 
ATOM   4060 H  HZ2  . LYS   B 1 19  ? 48.055 -27.071 -17.721 1.00 26.49 ?  19  LYS   B HZ2  1 
ATOM   4061 H  HZ3  . LYS   B 1 19  ? 48.982 -27.173 -16.612 1.00 26.49 ?  19  LYS   B HZ3  1 
ATOM   4062 N  N    . ASN   B 1 20  ? 45.620 -32.180 -13.334 1.00 15.39 ?  20  ASN   B N    1 
ATOM   4063 C  CA   . ASN   B 1 20  ? 46.653 -32.811 -12.518 1.00 16.58 ?  20  ASN   B CA   1 
ATOM   4064 C  C    . ASN   B 1 20  ? 47.924 -31.988 -12.700 1.00 16.77 ?  20  ASN   B C    1 
ATOM   4065 O  O    . ASN   B 1 20  ? 48.573 -32.055 -13.748 1.00 18.59 ?  20  ASN   B O    1 
ATOM   4066 C  CB   . ASN   B 1 20  ? 46.829 -34.261 -12.959 1.00 18.52 ?  20  ASN   B CB   1 
ATOM   4067 C  CG   . ASN   B 1 20  ? 47.986 -34.963 -12.276 1.00 20.04 ?  20  ASN   B CG   1 
ATOM   4068 O  OD1  . ASN   B 1 20  ? 48.649 -35.808 -12.884 1.00 22.07 ?  20  ASN   B OD1  1 
ATOM   4069 N  ND2  . ASN   B 1 20  ? 48.230 -34.639 -11.015 1.00 19.43 ?  20  ASN   B ND2  1 
ATOM   4070 H  H    . ASN   B 1 20  ? 45.505 -32.549 -14.102 1.00 18.44 ?  20  ASN   B H    1 
ATOM   4071 H  HA   . ASN   B 1 20  ? 46.381 -32.794 -11.585 1.00 19.87 ?  20  ASN   B HA   1 
ATOM   4072 H  HB2  . ASN   B 1 20  ? 46.018 -34.754 -12.751 1.00 22.20 ?  20  ASN   B HB2  1 
ATOM   4073 H  HB3  . ASN   B 1 20  ? 46.988 -34.278 -13.914 1.00 22.20 ?  20  ASN   B HB3  1 
ATOM   4074 H  HD21 . ASN   B 1 20  ? 48.881 -35.010 -10.595 1.00 23.29 ?  20  ASN   B HD21 1 
ATOM   4075 H  HD22 . ASN   B 1 20  ? 47.746 -34.048 -10.617 1.00 23.29 ?  20  ASN   B HD22 1 
ATOM   4076 N  N    . ALA   B 1 21  ? 48.274 -31.188 -11.690 1.00 16.30 ?  21  ALA   B N    1 
ATOM   4077 C  CA   . ALA   B 1 21  ? 49.378 -30.254 -11.838 1.00 16.89 ?  21  ALA   B CA   1 
ATOM   4078 C  C    . ALA   B 1 21  ? 49.840 -29.765 -10.474 1.00 15.81 ?  21  ALA   B C    1 
ATOM   4079 O  O    . ALA   B 1 21  ? 49.098 -29.797 -9.488  1.00 15.69 ?  21  ALA   B O    1 
ATOM   4080 C  CB   . ALA   B 1 21  ? 48.975 -29.070 -12.718 1.00 18.24 ?  21  ALA   B CB   1 
ATOM   4081 H  H    . ALA   B 1 21  ? 47.885 -31.170 -10.917 1.00 19.54 ?  21  ALA   B H    1 
ATOM   4082 H  HA   . ALA   B 1 21  ? 50.118 -30.712 -12.261 1.00 20.24 ?  21  ALA   B HA   1 
ATOM   4083 H  HB1  . ALA   B 1 21  ? 49.755 -28.521 -12.866 1.00 21.87 ?  21  ALA   B HB1  1 
ATOM   4084 H  HB2  . ALA   B 1 21  ? 48.640 -29.412 -13.561 1.00 21.87 ?  21  ALA   B HB2  1 
ATOM   4085 H  HB3  . ALA   B 1 21  ? 48.282 -28.563 -12.266 1.00 21.87 ?  21  ALA   B HB3  1 
ATOM   4086 N  N    . ASP   B 1 22  ? 51.097 -29.321 -10.452 1.00 15.32 ?  22  ASP   B N    1 
ATOM   4087 C  CA   . ASP   B 1 22  ? 51.711 -28.626 -9.325  1.00 14.87 ?  22  ASP   B CA   1 
ATOM   4088 C  C    . ASP   B 1 22  ? 51.304 -27.157 -9.409  1.00 13.51 ?  22  ASP   B C    1 
ATOM   4089 O  O    . ASP   B 1 22  ? 51.613 -26.484 -10.397 1.00 13.61 ?  22  ASP   B O    1 
ATOM   4090 C  CB   . ASP   B 1 22  ? 53.228 -28.799 -9.479  1.00 16.41 ?  22  ASP   B CB   1 
ATOM   4091 C  CG   . ASP   B 1 22  ? 54.050 -28.046 -8.439  1.00 18.08 ?  22  ASP   B CG   1 
ATOM   4092 O  OD1  . ASP   B 1 22  ? 53.678 -26.932 -8.035  1.00 18.16 ?  22  ASP   B OD1  1 
ATOM   4093 O  OD2  . ASP   B 1 22  ? 55.125 -28.562 -8.057  1.00 20.57 -1 22  ASP   B OD2  1 
ATOM   4094 H  H    . ASP   B 1 22  ? 51.642 -29.421 -11.116 1.00 18.36 ?  22  ASP   B H    1 
ATOM   4095 H  HA   . ASP   B 1 22  ? 51.421 -29.011 -8.482  1.00 17.82 ?  22  ASP   B HA   1 
ATOM   4096 H  HB2  . ASP   B 1 22  ? 53.452 -29.737 -9.407  1.00 19.67 ?  22  ASP   B HB2  1 
ATOM   4097 H  HB3  . ASP   B 1 22  ? 53.495 -28.460 -10.348 1.00 19.67 ?  22  ASP   B HB3  1 
ATOM   4098 N  N    . ILE   B 1 23  ? 50.592 -26.664 -8.388  1.00 13.01 ?  23  ILE   B N    1 
ATOM   4099 C  CA   . ILE   B 1 23  ? 50.001 -25.325 -8.459  1.00 12.34 ?  23  ILE   B CA   1 
ATOM   4100 C  C    . ILE   B 1 23  ? 51.059 -24.235 -8.599  1.00 12.23 ?  23  ILE   B C    1 
ATOM   4101 O  O    . ILE   B 1 23  ? 50.796 -23.192 -9.206  1.00 11.60 ?  23  ILE   B O    1 
ATOM   4102 C  CB   . ILE   B 1 23  ? 49.059 -25.081 -7.264  1.00 12.56 ?  23  ILE   B CB   1 
ATOM   4103 C  CG1  . ILE   B 1 23  ? 48.238 -23.806 -7.468  1.00 13.26 ?  23  ILE   B CG1  1 
ATOM   4104 C  CG2  . ILE   B 1 23  ? 49.823 -25.042 -5.957  1.00 13.60 ?  23  ILE   B CG2  1 
ATOM   4105 C  CD1  . ILE   B 1 23  ? 47.116 -23.641 -6.457  1.00 13.82 ?  23  ILE   B CD1  1 
ATOM   4106 H  H    . ILE   B 1 23  ? 50.441 -27.086 -7.654  1.00 15.59 ?  23  ILE   B H    1 
ATOM   4107 H  HA   . ILE   B 1 23  ? 49.457 -25.287 -9.258  1.00 14.78 ?  23  ILE   B HA   1 
ATOM   4108 H  HB   . ILE   B 1 23  ? 48.435 -25.824 -7.224  1.00 15.05 ?  23  ILE   B HB   1 
ATOM   4109 H  HG12 . ILE   B 1 23  ? 48.827 -23.037 -7.388  1.00 15.89 ?  23  ILE   B HG12 1 
ATOM   4110 H  HG13 . ILE   B 1 23  ? 47.843 -23.822 -8.356  1.00 15.89 ?  23  ILE   B HG13 1 
ATOM   4111 H  HG21 . ILE   B 1 23  ? 49.190 -25.041 -5.222  1.00 16.30 ?  23  ILE   B HG21 1 
ATOM   4112 H  HG22 . ILE   B 1 23  ? 50.392 -25.825 -5.903  1.00 16.30 ?  23  ILE   B HG22 1 
ATOM   4113 H  HG23 . ILE   B 1 23  ? 50.363 -24.237 -5.931  1.00 16.30 ?  23  ILE   B HG23 1 
ATOM   4114 H  HD11 . ILE   B 1 23  ? 46.587 -22.865 -6.696  1.00 16.56 ?  23  ILE   B HD11 1 
ATOM   4115 H  HD12 . ILE   B 1 23  ? 46.561 -24.438 -6.475  1.00 16.56 ?  23  ILE   B HD12 1 
ATOM   4116 H  HD13 . ILE   B 1 23  ? 47.500 -23.525 -5.576  1.00 16.56 ?  23  ILE   B HD13 1 
ATOM   4117 N  N    . VAL   B 1 24  ? 52.253 -24.443 -8.042  1.00 12.28 ?  24  VAL   B N    1 
ATOM   4118 C  CA   . VAL   B 1 24  ? 53.327 -23.463 -8.206  1.00 12.90 ?  24  VAL   B CA   1 
ATOM   4119 C  C    . VAL   B 1 24  ? 53.780 -23.412 -9.659  1.00 13.00 ?  24  VAL   B C    1 
ATOM   4120 O  O    . VAL   B 1 24  ? 53.921 -22.334 -10.253 1.00 13.59 ?  24  VAL   B O    1 
ATOM   4121 C  CB   . VAL   B 1 24  ? 54.503 -23.788 -7.262  1.00 13.93 ?  24  VAL   B CB   1 
ATOM   4122 C  CG1  . VAL   B 1 24  ? 55.711 -22.908 -7.575  1.00 14.66 ?  24  VAL   B CG1  1 
ATOM   4123 C  CG2  . VAL   B 1 24  ? 54.082 -23.621 -5.821  1.00 15.08 ?  24  VAL   B CG2  1 
ATOM   4124 H  H    . VAL   B 1 24  ? 52.463 -25.129 -7.569  1.00 14.71 ?  24  VAL   B H    1 
ATOM   4125 H  HA   . VAL   B 1 24  ? 52.996 -22.587 -7.967  1.00 15.46 ?  24  VAL   B HA   1 
ATOM   4126 H  HB   . VAL   B 1 24  ? 54.768 -24.715 -7.386  1.00 16.69 ?  24  VAL   B HB   1 
ATOM   4127 H  HG11 . VAL   B 1 24  ? 56.299 -22.896 -6.802  1.00 17.57 ?  24  VAL   B HG11 1 
ATOM   4128 H  HG12 . VAL   B 1 24  ? 56.179 -23.278 -8.338  1.00 17.57 ?  24  VAL   B HG12 1 
ATOM   4129 H  HG13 . VAL   B 1 24  ? 55.404 -22.010 -7.769  1.00 17.57 ?  24  VAL   B HG13 1 
ATOM   4130 H  HG21 . VAL   B 1 24  ? 54.809 -23.899 -5.242  1.00 18.07 ?  24  VAL   B HG21 1 
ATOM   4131 H  HG22 . VAL   B 1 24  ? 53.872 -22.688 -5.661  1.00 18.07 ?  24  VAL   B HG22 1 
ATOM   4132 H  HG23 . VAL   B 1 24  ? 53.299 -24.170 -5.652  1.00 18.07 ?  24  VAL   B HG23 1 
ATOM   4133 N  N    . GLU   B 1 25  ? 54.041 -24.582 -10.247 1.00 13.88 ?  25  GLU   B N    1 
ATOM   4134 C  CA   . GLU   B 1 25  ? 54.432 -24.619 -11.650 1.00 15.46 ?  25  GLU   B CA   1 
ATOM   4135 C  C    . GLU   B 1 25  ? 53.324 -24.074 -12.537 1.00 14.36 ?  25  GLU   B C    1 
ATOM   4136 O  O    . GLU   B 1 25  ? 53.592 -23.354 -13.507 1.00 15.24 ?  25  GLU   B O    1 
ATOM   4137 C  CB   . GLU   B 1 25  ? 54.823 -26.042 -12.045 1.00 19.23 ?  25  GLU   B CB   1 
ATOM   4138 C  CG   . GLU   B 1 25  ? 56.116 -26.498 -11.388 1.00 24.92 ?  25  GLU   B CG   1 
ATOM   4139 C  CD   . GLU   B 1 25  ? 57.229 -25.462 -11.478 1.00 30.19 ?  25  GLU   B CD   1 
ATOM   4140 O  OE1  . GLU   B 1 25  ? 57.607 -25.088 -12.608 1.00 32.25 ?  25  GLU   B OE1  1 
ATOM   4141 O  OE2  . GLU   B 1 25  ? 57.714 -25.006 -10.417 1.00 32.06 -1 25  GLU   B OE2  1 
ATOM   4142 H  H    . GLU   B 1 25  ? 53.992 -25.352 -9.863  1.00 16.63 ?  25  GLU   B H    1 
ATOM   4143 H  HA   . GLU   B 1 25  ? 55.191 -24.037 -11.775 1.00 18.52 ?  25  GLU   B HA   1 
ATOM   4144 H  HB2  . GLU   B 1 25  ? 54.120 -26.655 -11.772 1.00 23.05 ?  25  GLU   B HB2  1 
ATOM   4145 H  HB3  . GLU   B 1 25  ? 54.942 -26.084 -13.007 1.00 23.05 ?  25  GLU   B HB3  1 
ATOM   4146 H  HG2  . GLU   B 1 25  ? 55.955 -26.661 -10.451 1.00 29.88 ?  25  GLU   B HG2  1 
ATOM   4147 H  HG3  . GLU   B 1 25  ? 56.425 -27.305 -11.827 1.00 29.88 ?  25  GLU   B HG3  1 
ATOM   4148 N  N    . GLU   B 1 26  ? 52.070 -24.390 -12.207 1.00 13.61 ?  26  GLU   B N    1 
ATOM   4149 C  CA   . GLU   B 1 26  ? 50.947 -23.859 -12.969 1.00 14.13 ?  26  GLU   B CA   1 
ATOM   4150 C  C    . GLU   B 1 26  ? 50.902 -22.341 -12.886 1.00 13.25 ?  26  GLU   B C    1 
ATOM   4151 O  O    . GLU   B 1 26  ? 50.710 -21.661 -13.898 1.00 14.46 ?  26  GLU   B O    1 
ATOM   4152 C  CB   . GLU   B 1 26  ? 49.635 -24.440 -12.444 1.00 16.26 ?  26  GLU   B CB   1 
ATOM   4153 C  CG   . GLU   B 1 26  ? 49.185 -25.714 -13.126 1.00 19.97 ?  26  GLU   B CG   1 
ATOM   4154 C  CD   . GLU   B 1 26  ? 48.943 -25.554 -14.624 1.00 21.07 ?  26  GLU   B CD   1 
ATOM   4155 O  OE1  . GLU   B 1 26  ? 47.965 -24.899 -15.042 1.00 20.99 ?  26  GLU   B OE1  1 
ATOM   4156 O  OE2  . GLU   B 1 26  ? 49.736 -26.117 -15.390 1.00 23.64 -1 26  GLU   B OE2  1 
ATOM   4157 H  H    . GLU   B 1 26  ? 51.845 -24.907 -11.553 1.00 16.31 ?  26  GLU   B H    1 
ATOM   4158 H  HA   . GLU   B 1 26  ? 51.045 -24.108 -13.899 1.00 16.93 ?  26  GLU   B HA   1 
ATOM   4159 H  HB2  . GLU   B 1 26  ? 49.736 -24.636 -11.498 1.00 19.49 ?  26  GLU   B HB2  1 
ATOM   4160 H  HB3  . GLU   B 1 26  ? 48.933 -23.779 -12.562 1.00 19.49 ?  26  GLU   B HB3  1 
ATOM   4161 H  HG2  . GLU   B 1 26  ? 49.874 -26.378 -13.010 1.00 23.94 ?  26  GLU   B HG2  1 
ATOM   4162 H  HG3  . GLU   B 1 26  ? 48.355 -26.010 -12.720 1.00 23.94 ?  26  GLU   B HG3  1 
ATOM   4163 N  N    . ALA   B 1 27  ? 51.047 -21.791 -11.678 1.00 12.39 ?  27  ALA   B N    1 
ATOM   4164 C  CA   . ALA   B 1 27  ? 51.010 -20.342 -11.528 1.00 12.86 ?  27  ALA   B CA   1 
ATOM   4165 C  C    . ALA   B 1 27  ? 52.084 -19.682 -12.381 1.00 13.81 ?  27  ALA   B C    1 
ATOM   4166 O  O    . ALA   B 1 27  ? 51.826 -18.679 -13.061 1.00 14.24 ?  27  ALA   B O    1 
ATOM   4167 C  CB   . ALA   B 1 27  ? 51.167 -19.964 -10.056 1.00 13.09 ?  27  ALA   B CB   1 
ATOM   4168 H  H    . ALA   B 1 27  ? 51.162 -22.230 -10.943 1.00 14.85 ?  27  ALA   B H    1 
ATOM   4169 H  HA   . ALA   B 1 27  ? 50.153 -20.015 -11.828 1.00 15.41 ?  27  ALA   B HA   1 
ATOM   4170 H  HB1  . ALA   B 1 27  ? 51.134 -18.998 -9.973  1.00 15.68 ?  27  ALA   B HB1  1 
ATOM   4171 H  HB2  . ALA   B 1 27  ? 50.437 -20.362 -9.551  1.00 15.68 ?  27  ALA   B HB2  1 
ATOM   4172 H  HB3  . ALA   B 1 27  ? 52.014 -20.298 -9.729  1.00 15.68 ?  27  ALA   B HB3  1 
ATOM   4173 N  N    . LYS   B 1 28  ? 53.298 -20.232 -12.369 1.00 15.22 ?  28  LYS   B N    1 
ATOM   4174 C  CA   . LYS   B 1 28  ? 54.375 -19.615 -13.137 1.00 17.49 ?  28  LYS   B CA   1 
ATOM   4175 C  C    . LYS   B 1 28  ? 54.115 -19.694 -14.637 1.00 18.30 ?  28  LYS   B C    1 
ATOM   4176 O  O    . LYS   B 1 28  ? 54.528 -18.797 -15.383 1.00 19.37 ?  28  LYS   B O    1 
ATOM   4177 C  CB   . LYS   B 1 28  ? 55.731 -20.219 -12.750 1.00 20.84 ?  28  LYS   B CB   1 
ATOM   4178 C  CG   . LYS   B 1 28  ? 56.132 -19.887 -11.317 1.00 24.48 ?  28  LYS   B CG   1 
ATOM   4179 C  CD   . LYS   B 1 28  ? 57.556 -20.310 -10.982 1.00 29.14 ?  28  LYS   B CD   1 
ATOM   4180 C  CE   . LYS   B 1 28  ? 57.639 -21.778 -10.629 1.00 33.69 ?  28  LYS   B CE   1 
ATOM   4181 N  NZ   . LYS   B 1 28  ? 58.991 -22.140 -10.115 1.00 35.76 ?  28  LYS   B NZ   1 
ATOM   4182 H  H    . LYS   B 1 28  ? 53.522 -20.942 -11.937 1.00 18.24 ?  28  LYS   B H    1 
ATOM   4183 H  HA   . LYS   B 1 28  ? 54.410 -18.675 -12.909 1.00 20.96 ?  28  LYS   B HA   1 
ATOM   4184 H  HB2  . LYS   B 1 28  ? 55.691 -21.182 -12.831 1.00 24.98 ?  28  LYS   B HB2  1 
ATOM   4185 H  HB3  . LYS   B 1 28  ? 56.419 -19.864 -13.339 1.00 24.98 ?  28  LYS   B HB3  1 
ATOM   4186 H  HG2  . LYS   B 1 28  ? 56.066 -18.926 -11.189 1.00 29.35 ?  28  LYS   B HG2  1 
ATOM   4187 H  HG3  . LYS   B 1 28  ? 55.531 -20.344 -10.711 1.00 29.35 ?  28  LYS   B HG3  1 
ATOM   4188 H  HD2  . LYS   B 1 28  ? 58.124 -20.148 -11.751 1.00 34.94 ?  28  LYS   B HD2  1 
ATOM   4189 H  HD3  . LYS   B 1 28  ? 57.867 -19.794 -10.222 1.00 34.94 ?  28  LYS   B HD3  1 
ATOM   4190 H  HE2  . LYS   B 1 28  ? 56.987 -21.977 -9.938  1.00 40.40 ?  28  LYS   B HE2  1 
ATOM   4191 H  HE3  . LYS   B 1 28  ? 57.461 -22.309 -11.420 1.00 40.40 ?  28  LYS   B HE3  1 
ATOM   4192 H  HZ1  . LYS   B 1 28  ? 59.018 -23.006 -9.912  1.00 42.89 ?  28  LYS   B HZ1  1 
ATOM   4193 H  HZ2  . LYS   B 1 28  ? 59.607 -21.968 -10.733 1.00 42.89 ?  28  LYS   B HZ2  1 
ATOM   4194 H  HZ3  . LYS   B 1 28  ? 59.175 -21.667 -9.383  1.00 42.89 ?  28  LYS   B HZ3  1 
ATOM   4195 N  N    . LYS   B 1 29  ? 53.414 -20.735 -15.093 1.00 19.41 ?  29  LYS   B N    1 
ATOM   4196 C  CA   . LYS   B 1 29  ? 53.129 -20.868 -16.518 1.00 22.08 ?  29  LYS   B CA   1 
ATOM   4197 C  C    . LYS   B 1 29  ? 51.888 -20.086 -16.941 1.00 20.65 ?  29  LYS   B C    1 
ATOM   4198 O  O    . LYS   B 1 29  ? 51.890 -19.448 -17.999 1.00 21.50 ?  29  LYS   B O    1 
ATOM   4199 C  CB   . LYS   B 1 29  ? 52.974 -22.344 -16.881 1.00 26.59 ?  29  LYS   B CB   1 
ATOM   4200 C  CG   . LYS   B 1 29  ? 52.845 -22.610 -18.370 1.00 31.12 ?  29  LYS   B CG   1 
ATOM   4201 C  CD   . LYS   B 1 29  ? 53.111 -24.072 -18.696 1.00 34.68 ?  29  LYS   B CD   1 
ATOM   4202 C  CE   . LYS   B 1 29  ? 52.045 -24.990 -18.117 1.00 37.13 ?  29  LYS   B CE   1 
ATOM   4203 N  NZ   . LYS   B 1 29  ? 52.317 -26.422 -18.433 1.00 38.86 ?  29  LYS   B NZ   1 
ATOM   4204 H  H    . LYS   B 1 29  ? 53.107 -21.373 -14.599 1.00 23.27 ?  29  LYS   B H    1 
ATOM   4205 H  HA   . LYS   B 1 29  ? 53.876 -20.515 -17.014 1.00 26.48 ?  29  LYS   B HA   1 
ATOM   4206 H  HB2  . LYS   B 1 29  ? 53.756 -22.823 -16.564 1.00 31.88 ?  29  LYS   B HB2  1 
ATOM   4207 H  HB3  . LYS   B 1 29  ? 52.179 -22.691 -16.452 1.00 31.88 ?  29  LYS   B HB3  1 
ATOM   4208 H  HG2  . LYS   B 1 29  ? 51.945 -22.393 -18.658 1.00 37.32 ?  29  LYS   B HG2  1 
ATOM   4209 H  HG3  . LYS   B 1 29  ? 53.492 -22.069 -18.850 1.00 37.32 ?  29  LYS   B HG3  1 
ATOM   4210 H  HD2  . LYS   B 1 29  ? 53.119 -24.186 -19.659 1.00 41.59 ?  29  LYS   B HD2  1 
ATOM   4211 H  HD3  . LYS   B 1 29  ? 53.969 -24.330 -18.322 1.00 41.59 ?  29  LYS   B HD3  1 
ATOM   4212 H  HE2  . LYS   B 1 29  ? 52.025 -24.893 -17.152 1.00 44.53 ?  29  LYS   B HE2  1 
ATOM   4213 H  HE3  . LYS   B 1 29  ? 51.182 -24.755 -18.494 1.00 44.53 ?  29  LYS   B HE3  1 
ATOM   4214 H  HZ1  . LYS   B 1 29  ? 51.680 -26.937 -18.084 1.00 46.61 ?  29  LYS   B HZ1  1 
ATOM   4215 H  HZ2  . LYS   B 1 29  ? 52.335 -26.541 -19.315 1.00 46.61 ?  29  LYS   B HZ2  1 
ATOM   4216 H  HZ3  . LYS   B 1 29  ? 53.103 -26.664 -18.093 1.00 46.61 ?  29  LYS   B HZ3  1 
ATOM   4217 N  N    . VAL   B 1 30  ? 50.820 -20.140 -16.139 1.00 18.95 ?  30  VAL   B N    1 
ATOM   4218 C  CA   . VAL   B 1 30  ? 49.530 -19.552 -16.510 1.00 19.20 ?  30  VAL   B CA   1 
ATOM   4219 C  C    . VAL   B 1 30  ? 49.526 -18.039 -16.352 1.00 18.35 ?  30  VAL   B C    1 
ATOM   4220 O  O    . VAL   B 1 30  ? 48.786 -17.332 -17.055 1.00 18.98 ?  30  VAL   B O    1 
ATOM   4221 C  CB   . VAL   B 1 30  ? 48.422 -20.180 -15.642 1.00 20.42 ?  30  VAL   B CB   1 
ATOM   4222 C  CG1  . VAL   B 1 30  ? 47.127 -19.383 -15.738 1.00 20.69 ?  30  VAL   B CG1  1 
ATOM   4223 C  CG2  . VAL   B 1 30  ? 48.197 -21.633 -16.029 1.00 21.29 ?  30  VAL   B CG2  1 
ATOM   4224 H  H    . VAL   B 1 30  ? 50.806 -20.541 -15.368 1.00 22.72 ?  30  VAL   B H    1 
ATOM   4225 H  HA   . VAL   B 1 30  ? 49.339 -19.773 -17.435 1.00 23.02 ?  30  VAL   B HA   1 
ATOM   4226 H  HB   . VAL   B 1 30  ? 48.705 -20.171 -14.714 1.00 24.48 ?  30  VAL   B HB   1 
ATOM   4227 H  HG11 . VAL   B 1 30  ? 46.385 -19.974 -15.531 1.00 24.81 ?  30  VAL   B HG11 1 
ATOM   4228 H  HG12 . VAL   B 1 30  ? 47.151 -18.655 -15.100 1.00 24.81 ?  30  VAL   B HG12 1 
ATOM   4229 H  HG13 . VAL   B 1 30  ? 47.025 -19.046 -16.637 1.00 24.81 ?  30  VAL   B HG13 1 
ATOM   4230 H  HG21 . VAL   B 1 30  ? 47.506 -22.009 -15.456 1.00 25.53 ?  30  VAL   B HG21 1 
ATOM   4231 H  HG22 . VAL   B 1 30  ? 47.910 -21.671 -16.955 1.00 25.53 ?  30  VAL   B HG22 1 
ATOM   4232 H  HG23 . VAL   B 1 30  ? 49.023 -22.123 -15.914 1.00 25.53 ?  30  VAL   B HG23 1 
ATOM   4233 N  N    . LYS   B 1 31  ? 50.305 -17.535 -15.410 1.00 17.82 ?  31  LYS   B N    1 
ATOM   4234 C  CA   . LYS   B 1 31  ? 50.333 -16.128 -15.043 1.00 18.56 ?  31  LYS   B CA   1 
ATOM   4235 C  C    . LYS   B 1 31  ? 48.928 -15.665 -14.662 1.00 16.12 ?  31  LYS   B C    1 
ATOM   4236 O  O    . LYS   B 1 31  ? 48.382 -14.751 -15.292 1.00 17.30 ?  31  LYS   B O    1 
ATOM   4237 C  CB   . LYS   B 1 31  ? 50.962 -15.306 -16.173 1.00 22.17 ?  31  LYS   B CB   1 
ATOM   4238 C  CG   . LYS   B 1 31  ? 52.381 -15.764 -16.522 1.00 25.54 ?  31  LYS   B CG   1 
ATOM   4239 C  CD   . LYS   B 1 31  ? 52.965 -14.967 -17.675 1.00 29.09 ?  31  LYS   B CD   1 
ATOM   4240 C  CE   . LYS   B 1 31  ? 54.451 -15.228 -17.837 1.00 31.99 ?  31  LYS   B CE   1 
ATOM   4241 N  NZ   . LYS   B 1 31  ? 55.196 -14.825 -16.613 1.00 33.75 ?  31  LYS   B NZ   1 
ATOM   4242 H  H    . LYS   B 1 31  ? 50.844 -18.024 -14.958 1.00 21.36 ?  31  LYS   B H    1 
ATOM   4243 H  HA   . LYS   B 1 31  ? 50.885 -16.044 -14.262 1.00 22.25 ?  31  LYS   B HA   1 
ATOM   4244 H  HB2  . LYS   B 1 31  ? 50.418 -15.388 -16.972 1.00 26.58 ?  31  LYS   B HB2  1 
ATOM   4245 H  HB3  . LYS   B 1 31  ? 51.007 -14.382 -15.893 1.00 26.58 ?  31  LYS   B HB3  1 
ATOM   4246 H  HG2  . LYS   B 1 31  ? 52.947 -15.648 -15.743 1.00 30.62 ?  31  LYS   B HG2  1 
ATOM   4247 H  HG3  . LYS   B 1 31  ? 52.359 -16.702 -16.778 1.00 30.62 ?  31  LYS   B HG3  1 
ATOM   4248 H  HD2  . LYS   B 1 31  ? 52.517 -15.226 -18.495 1.00 34.88 ?  31  LYS   B HD2  1 
ATOM   4249 H  HD3  . LYS   B 1 31  ? 52.835 -14.023 -17.502 1.00 34.88 ?  31  LYS   B HD3  1 
ATOM   4250 H  HE2  . LYS   B 1 31  ? 54.602 -16.175 -17.988 1.00 38.37 ?  31  LYS   B HE2  1 
ATOM   4251 H  HE3  . LYS   B 1 31  ? 54.790 -14.709 -18.584 1.00 38.37 ?  31  LYS   B HE3  1 
ATOM   4252 H  HZ1  . LYS   B 1 31  ? 56.071 -14.855 -16.765 1.00 40.47 ?  31  LYS   B HZ1  1 
ATOM   4253 H  HZ2  . LYS   B 1 31  ? 54.971 -13.996 -16.381 1.00 40.47 ?  31  LYS   B HZ2  1 
ATOM   4254 H  HZ3  . LYS   B 1 31  ? 54.999 -15.376 -15.942 1.00 40.47 ?  31  LYS   B HZ3  1 
ATOM   4255 N  N    . PRO   B 1 32  ? 48.317 -16.271 -13.637 1.00 13.74 ?  32  PRO   B N    1 
ATOM   4256 C  CA   . PRO   B 1 32  ? 46.938 -15.916 -13.280 1.00 12.78 ?  32  PRO   B CA   1 
ATOM   4257 C  C    . PRO   B 1 32  ? 46.856 -14.567 -12.585 1.00 12.92 ?  32  PRO   B C    1 
ATOM   4258 O  O    . PRO   B 1 32  ? 47.778 -14.141 -11.882 1.00 14.01 ?  32  PRO   B O    1 
ATOM   4259 C  CB   . PRO   B 1 32  ? 46.538 -17.034 -12.311 1.00 12.84 ?  32  PRO   B CB   1 
ATOM   4260 C  CG   . PRO   B 1 32  ? 47.840 -17.363 -11.623 1.00 13.32 ?  32  PRO   B CG   1 
ATOM   4261 C  CD   . PRO   B 1 32  ? 48.891 -17.255 -12.696 1.00 13.56 ?  32  PRO   B CD   1 
ATOM   4262 H  HA   . PRO   B 1 32  ? 46.357 -15.932 -14.059 1.00 15.31 ?  32  PRO   B HA   1 
ATOM   4263 H  HB2  . PRO   B 1 32  ? 45.882 -16.707 -11.674 1.00 15.38 ?  32  PRO   B HB2  1 
ATOM   4264 H  HB3  . PRO   B 1 32  ? 46.202 -17.800 -12.799 1.00 15.38 ?  32  PRO   B HB3  1 
ATOM   4265 H  HG2  . PRO   B 1 32  ? 48.009 -16.717 -10.915 1.00 15.96 ?  32  PRO   B HG2  1 
ATOM   4266 H  HG3  . PRO   B 1 32  ? 47.808 -18.261 -11.264 1.00 15.96 ?  32  PRO   B HG3  1 
ATOM   4267 H  HD2  . PRO   B 1 32  ? 49.720 -16.920 -12.321 1.00 16.25 ?  32  PRO   B HD2  1 
ATOM   4268 H  HD3  . PRO   B 1 32  ? 49.012 -18.111 -13.130 1.00 16.25 ?  32  PRO   B HD3  1 
ATOM   4269 N  N    . THR   B 1 33  ? 45.706 -13.914 -12.758 1.00 12.47 ?  33  THR   B N    1 
ATOM   4270 C  CA   . THR   B 1 33  ? 45.406 -12.738 -11.952 1.00 12.62 ?  33  THR   B CA   1 
ATOM   4271 C  C    . THR   B 1 33  ? 45.362 -13.090 -10.470 1.00 12.29 ?  33  THR   B C    1 
ATOM   4272 O  O    . THR   B 1 33  ? 45.841 -12.316 -9.629  1.00 13.30 ?  33  THR   B O    1 
ATOM   4273 C  CB   . THR   B 1 33  ? 44.088 -12.108 -12.407 1.00 13.29 ?  33  THR   B CB   1 
ATOM   4274 O  OG1  . THR   B 1 33  ? 44.140 -11.852 -13.814 1.00 13.38 ?  33  THR   B OG1  1 
ATOM   4275 C  CG2  . THR   B 1 33  ? 43.829 -10.807 -11.667 1.00 14.42 ?  33  THR   B CG2  1 
ATOM   4276 H  H    . THR   B 1 33  ? 45.087 -14.133 -13.322 1.00 14.94 ?  33  THR   B H    1 
ATOM   4277 H  HA   . THR   B 1 33  ? 46.105 -12.084 -12.082 1.00 15.12 ?  33  THR   B HA   1 
ATOM   4278 H  HB   . THR   B 1 33  ? 43.352 -12.718 -12.218 1.00 15.93 ?  33  THR   B HB   1 
ATOM   4279 H  HG1  . THR   B 1 33  ? 43.418 -11.494 -14.072 1.00 16.03 ?  33  THR   B HG1  1 
ATOM   4280 H  HG21 . THR   B 1 33  ? 43.070 -10.350 -12.058 1.00 17.28 ?  33  THR   B HG21 1 
ATOM   4281 H  HG22 . THR   B 1 33  ? 43.643 -10.987 -10.733 1.00 17.28 ?  33  THR   B HG22 1 
ATOM   4282 H  HG23 . THR   B 1 33  ? 44.610 -10.235 -11.731 1.00 17.28 ?  33  THR   B HG23 1 
ATOM   4283 N  N    . VAL   B 1 34  ? 44.804 -14.255 -10.128 1.00 11.43 ?  34  VAL   B N    1 
ATOM   4284 C  CA   . VAL   B 1 34  ? 44.619 -14.661 -8.739  1.00 10.87 ?  34  VAL   B CA   1 
ATOM   4285 C  C    . VAL   B 1 34  ? 45.055 -16.109 -8.577  1.00 10.01 ?  34  VAL   B C    1 
ATOM   4286 O  O    . VAL   B 1 34  ? 44.533 -16.996 -9.261  1.00 10.89 ?  34  VAL   B O    1 
ATOM   4287 C  CB   . VAL   B 1 34  ? 43.150 -14.522 -8.287  1.00 12.02 ?  34  VAL   B CB   1 
ATOM   4288 C  CG1  . VAL   B 1 34  ? 42.999 -14.972 -6.839  1.00 12.36 ?  34  VAL   B CG1  1 
ATOM   4289 C  CG2  . VAL   B 1 34  ? 42.646 -13.099 -8.475  1.00 13.13 ?  34  VAL   B CG2  1 
ATOM   4290 H  H    . VAL   B 1 34  ? 44.527 -14.845 -10.696 1.00 13.69 ?  34  VAL   B H    1 
ATOM   4291 H  HA   . VAL   B 1 34  ? 45.175 -14.107 -8.163  1.00 13.02 ?  34  VAL   B HA   1 
ATOM   4292 H  HB   . VAL   B 1 34  ? 42.603 -15.104 -8.833  1.00 14.40 ?  34  VAL   B HB   1 
ATOM   4293 H  HG11 . VAL   B 1 34  ? 42.141 -14.664 -6.499  1.00 14.81 ?  34  VAL   B HG11 1 
ATOM   4294 H  HG12 . VAL   B 1 34  ? 43.034 -15.942 -6.797  1.00 14.81 ?  34  VAL   B HG12 1 
ATOM   4295 H  HG13 . VAL   B 1 34  ? 43.716 -14.592 -6.307  1.00 14.81 ?  34  VAL   B HG13 1 
ATOM   4296 H  HG21 . VAL   B 1 34  ? 41.732 -13.042 -8.154  1.00 15.73 ?  34  VAL   B HG21 1 
ATOM   4297 H  HG22 . VAL   B 1 34  ? 43.211 -12.492 -7.973  1.00 15.73 ?  34  VAL   B HG22 1 
ATOM   4298 H  HG23 . VAL   B 1 34  ? 42.677 -12.876 -9.420  1.00 15.73 ?  34  VAL   B HG23 1 
ATOM   4299 N  N    . VAL   B 1 35  ? 45.966 -16.357 -7.639  1.00 9.71  ?  35  VAL   B N    1 
ATOM   4300 C  CA   . VAL   B 1 35  ? 46.195 -17.699 -7.121  1.00 9.56  ?  35  VAL   B CA   1 
ATOM   4301 C  C    . VAL   B 1 35  ? 45.660 -17.752 -5.699  1.00 9.30  ?  35  VAL   B C    1 
ATOM   4302 O  O    . VAL   B 1 35  ? 45.886 -16.832 -4.908  1.00 9.87  ?  35  VAL   B O    1 
ATOM   4303 C  CB   . VAL   B 1 35  ? 47.680 -18.120 -7.205  1.00 10.32 ?  35  VAL   B CB   1 
ATOM   4304 C  CG1  . VAL   B 1 35  ? 48.580 -17.283 -6.283  1.00 11.16 ?  35  VAL   B CG1  1 
ATOM   4305 C  CG2  . VAL   B 1 35  ? 47.829 -19.612 -6.893  1.00 10.99 ?  35  VAL   B CG2  1 
ATOM   4306 H  H    . VAL   B 1 35  ? 46.475 -15.757 -7.289  1.00 11.62 ?  35  VAL   B H    1 
ATOM   4307 H  HA   . VAL   B 1 35  ? 45.684 -18.331 -7.650  1.00 11.44 ?  35  VAL   B HA   1 
ATOM   4308 H  HB   . VAL   B 1 35  ? 47.988 -17.989 -8.116  1.00 12.36 ?  35  VAL   B HB   1 
ATOM   4309 H  HG11 . VAL   B 1 35  ? 49.506 -17.509 -6.457  1.00 13.37 ?  35  VAL   B HG11 1 
ATOM   4310 H  HG12 . VAL   B 1 35  ? 48.423 -16.346 -6.462  1.00 13.37 ?  35  VAL   B HG12 1 
ATOM   4311 H  HG13 . VAL   B 1 35  ? 48.359 -17.488 -5.359  1.00 13.37 ?  35  VAL   B HG13 1 
ATOM   4312 H  HG21 . VAL   B 1 35  ? 48.758 -19.871 -6.995  1.00 13.16 ?  35  VAL   B HG21 1 
ATOM   4313 H  HG22 . VAL   B 1 35  ? 47.539 -19.779 -5.980  1.00 13.16 ?  35  VAL   B HG22 1 
ATOM   4314 H  HG23 . VAL   B 1 35  ? 47.276 -20.126 -7.508  1.00 13.16 ?  35  VAL   B HG23 1 
ATOM   4315 N  N    . VAL   B 1 36  ? 44.940 -18.827 -5.383  1.00 9.46  ?  36  VAL   B N    1 
ATOM   4316 C  CA   . VAL   B 1 36  ? 44.397 -19.037 -4.051  1.00 9.01  ?  36  VAL   B CA   1 
ATOM   4317 C  C    . VAL   B 1 36  ? 45.409 -19.794 -3.200  1.00 8.80  ?  36  VAL   B C    1 
ATOM   4318 O  O    . VAL   B 1 36  ? 45.952 -20.825 -3.622  1.00 10.07 ?  36  VAL   B O    1 
ATOM   4319 C  CB   . VAL   B 1 36  ? 43.064 -19.800 -4.129  1.00 9.45  ?  36  VAL   B CB   1 
ATOM   4320 C  CG1  . VAL   B 1 36  ? 42.565 -20.172 -2.744  1.00 10.24 ?  36  VAL   B CG1  1 
ATOM   4321 C  CG2  . VAL   B 1 36  ? 42.032 -18.966 -4.869  1.00 10.12 ?  36  VAL   B CG2  1 
ATOM   4322 H  H    . VAL   B 1 36  ? 44.761 -19.463 -5.934  1.00 11.32 ?  36  VAL   B H    1 
ATOM   4323 H  HA   . VAL   B 1 36  ? 44.228 -18.176 -3.635  1.00 10.78 ?  36  VAL   B HA   1 
ATOM   4324 H  HB   . VAL   B 1 36  ? 43.199 -20.618 -4.631  1.00 11.32 ?  36  VAL   B HB   1 
ATOM   4325 H  HG11 . VAL   B 1 36  ? 41.628 -20.414 -2.802  1.00 12.26 ?  36  VAL   B HG11 1 
ATOM   4326 H  HG12 . VAL   B 1 36  ? 43.080 -20.921 -2.411  1.00 12.26 ?  36  VAL   B HG12 1 
ATOM   4327 H  HG13 . VAL   B 1 36  ? 42.671 -19.406 -2.156  1.00 12.26 ?  36  VAL   B HG13 1 
ATOM   4328 H  HG21 . VAL   B 1 36  ? 41.192 -19.448 -4.890  1.00 12.12 ?  36  VAL   B HG21 1 
ATOM   4329 H  HG22 . VAL   B 1 36  ? 41.919 -18.121 -4.406  1.00 12.12 ?  36  VAL   B HG22 1 
ATOM   4330 H  HG23 . VAL   B 1 36  ? 42.344 -18.806 -5.775  1.00 12.12 ?  36  VAL   B HG23 1 
ATOM   4331 N  N    . ASN   B 1 37  ? 45.625 -19.305 -1.982  1.00 9.28  ?  37  ASN   B N    1 
ATOM   4332 C  CA   . ASN   B 1 37  ? 46.383 -20.031 -0.981  1.00 9.65  ?  37  ASN   B CA   1 
ATOM   4333 C  C    . ASN   B 1 37  ? 45.437 -20.704 0.004   1.00 9.45  ?  37  ASN   B C    1 
ATOM   4334 O  O    . ASN   B 1 37  ? 44.423 -20.128 0.412   1.00 10.13 ?  37  ASN   B O    1 
ATOM   4335 C  CB   . ASN   B 1 37  ? 47.313 -19.081 -0.226  1.00 9.43  ?  37  ASN   B CB   1 
ATOM   4336 C  CG   . ASN   B 1 37  ? 48.168 -19.799 0.791   1.00 9.83  ?  37  ASN   B CG   1 
ATOM   4337 O  OD1  . ASN   B 1 37  ? 48.502 -20.976 0.620   1.00 10.58 ?  37  ASN   B OD1  1 
ATOM   4338 N  ND2  . ASN   B 1 37  ? 48.516 -19.101 1.864   1.00 9.87  ?  37  ASN   B ND2  1 
ATOM   4339 H  H    . ASN   B 1 37  ? 45.335 -18.541 -1.706  1.00 11.11 ?  37  ASN   B H    1 
ATOM   4340 H  HA   . ASN   B 1 37  ? 46.918 -20.719 -1.406  1.00 11.56 ?  37  ASN   B HA   1 
ATOM   4341 H  HB2  . ASN   B 1 37  ? 47.906 -18.653 -0.861  1.00 11.29 ?  37  ASN   B HB2  1 
ATOM   4342 H  HB3  . ASN   B 1 37  ? 46.787 -18.422 0.244   1.00 11.29 ?  37  ASN   B HB3  1 
ATOM   4343 H  HD21 . ASN   B 1 37  ? 49.006 -19.464 2.475   1.00 11.82 ?  37  ASN   B HD21 1 
ATOM   4344 H  HD22 . ASN   B 1 37  ? 48.265 -18.290 1.952   1.00 11.82 ?  37  ASN   B HD22 1 
ATOM   4345 N  N    . ALA   B 1 38  ? 45.793 -21.932 0.383   1.00 9.64  ?  38  ALA   B N    1 
ATOM   4346 C  CA   . ALA   B 1 38  ? 45.135 -22.678 1.454   1.00 10.18 ?  38  ALA   B CA   1 
ATOM   4347 C  C    . ALA   B 1 38  ? 45.722 -22.198 2.780   1.00 9.88  ?  38  ALA   B C    1 
ATOM   4348 O  O    . ALA   B 1 38  ? 46.625 -22.808 3.363   1.00 10.85 ?  38  ALA   B O    1 
ATOM   4349 C  CB   . ALA   B 1 38  ? 45.350 -24.172 1.259   1.00 11.19 ?  38  ALA   B CB   1 
ATOM   4350 H  H    . ALA   B 1 38  ? 46.446 -22.365 0.030   1.00 11.55 ?  38  ALA   B H    1 
ATOM   4351 H  HA   . ALA   B 1 38  ? 44.183 -22.493 1.449   1.00 12.19 ?  38  ALA   B HA   1 
ATOM   4352 H  HB1  . ALA   B 1 38  ? 44.901 -24.652 1.980   1.00 13.40 ?  38  ALA   B HB1  1 
ATOM   4353 H  HB2  . ALA   B 1 38  ? 44.966 -24.437 0.407   1.00 13.40 ?  38  ALA   B HB2  1 
ATOM   4354 H  HB3  . ALA   B 1 38  ? 46.295 -24.365 1.275   1.00 13.40 ?  38  ALA   B HB3  1 
ATOM   4355 N  N    . ALA   B 1 39  ? 45.208 -21.059 3.242   1.00 9.84  ?  39  ALA   B N    1 
ATOM   4356 C  CA   . ALA   B 1 39  ? 45.753 -20.326 4.375   1.00 10.33 ?  39  ALA   B CA   1 
ATOM   4357 C  C    . ALA   B 1 39  ? 45.134 -20.776 5.695   1.00 10.04 ?  39  ALA   B C    1 
ATOM   4358 O  O    . ALA   B 1 39  ? 44.107 -21.454 5.739   1.00 11.07 ?  39  ALA   B O    1 
ATOM   4359 C  CB   . ALA   B 1 39  ? 45.507 -18.826 4.187   1.00 11.01 ?  39  ALA   B CB   1 
ATOM   4360 H  H    . ALA   B 1 39  ? 44.513 -20.687 2.897   1.00 11.78 ?  39  ALA   B H    1 
ATOM   4361 H  HA   . ALA   B 1 39  ? 46.706 -20.473 4.420   1.00 12.37 ?  39  ALA   B HA   1 
ATOM   4362 H  HB1  . ALA   B 1 39  ? 45.875 -18.348 4.947   1.00 13.19 ?  39  ALA   B HB1  1 
ATOM   4363 H  HB2  . ALA   B 1 39  ? 45.944 -18.533 3.371   1.00 13.19 ?  39  ALA   B HB2  1 
ATOM   4364 H  HB3  . ALA   B 1 39  ? 44.552 -18.664 4.125   1.00 13.19 ?  39  ALA   B HB3  1 
ATOM   4365 N  N    . ASN   B 1 40  ? 45.776 -20.360 6.783   1.00 11.26 ?  40  ASN   B N    1 
ATOM   4366 C  CA   . ASN   B 1 40  ? 45.212 -20.408 8.124   1.00 11.60 ?  40  ASN   B CA   1 
ATOM   4367 C  C    . ASN   B 1 40  ? 45.038 -18.981 8.653   1.00 11.26 ?  40  ASN   B C    1 
ATOM   4368 O  O    . ASN   B 1 40  ? 45.448 -18.002 8.020   1.00 11.33 ?  40  ASN   B O    1 
ATOM   4369 C  CB   . ASN   B 1 40  ? 46.063 -21.284 9.058   1.00 12.60 ?  40  ASN   B CB   1 
ATOM   4370 C  CG   . ASN   B 1 40  ? 47.520 -20.876 9.083   1.00 13.62 ?  40  ASN   B CG   1 
ATOM   4371 O  OD1  . ASN   B 1 40  ? 47.836 -19.693 9.149   1.00 15.32 ?  40  ASN   B OD1  1 
ATOM   4372 N  ND2  . ASN   B 1 40  ? 48.417 -21.851 9.035   1.00 13.20 ?  40  ASN   B ND2  1 
ATOM   4373 H  H    . ASN   B 1 40  ? 46.575 -20.041 6.762   1.00 13.49 ?  40  ASN   B H    1 
ATOM   4374 H  HA   . ASN   B 1 40  ? 44.331 -20.803 8.075   1.00 13.90 ?  40  ASN   B HA   1 
ATOM   4375 H  HB2  . ASN   B 1 40  ? 45.716 -21.211 9.961   1.00 15.10 ?  40  ASN   B HB2  1 
ATOM   4376 H  HB3  . ASN   B 1 40  ? 46.013 -22.204 8.756   1.00 15.10 ?  40  ASN   B HB3  1 
ATOM   4377 H  HD21 . ASN   B 1 40  ? 49.257 -21.666 9.047   1.00 15.81 ?  40  ASN   B HD21 1 
ATOM   4378 H  HD22 . ASN   B 1 40  ? 48.159 -22.671 8.988   1.00 15.81 ?  40  ASN   B HD22 1 
ATOM   4379 N  N    . VAL   B 1 41  ? 44.390 -18.853 9.813   1.00 11.80 ?  41  VAL   B N    1 
ATOM   4380 C  CA   . VAL   B 1 41  ? 43.932 -17.533 10.254  1.00 12.59 ?  41  VAL   B CA   1 
ATOM   4381 C  C    . VAL   B 1 41  ? 45.083 -16.581 10.551  1.00 12.26 ?  41  VAL   B C    1 
ATOM   4382 O  O    . VAL   B 1 41  ? 44.907 -15.361 10.465  1.00 12.37 ?  41  VAL   B O    1 
ATOM   4383 C  CB   . VAL   B 1 41  ? 42.950 -17.608 11.440  1.00 14.07 ?  41  VAL   B CB   1 
ATOM   4384 C  CG1  . VAL   B 1 41  ? 41.659 -18.290 11.023  1.00 14.77 ?  41  VAL   B CG1  1 
ATOM   4385 C  CG2  . VAL   B 1 41  ? 43.587 -18.302 12.634  1.00 15.13 ?  41  VAL   B CG2  1 
ATOM   4386 H  H    . VAL   B 1 41  ? 44.211 -19.496 10.349  1.00 14.14 ?  41  VAL   B H    1 
ATOM   4387 H  HA   . VAL   B 1 41  ? 43.438 -17.137 9.523   1.00 15.08 ?  41  VAL   B HA   1 
ATOM   4388 H  HB   . VAL   B 1 41  ? 42.725 -16.706 11.715  1.00 16.86 ?  41  VAL   B HB   1 
ATOM   4389 H  HG11 . VAL   B 1 41  ? 41.045 -18.295 11.777  1.00 17.70 ?  41  VAL   B HG11 1 
ATOM   4390 H  HG12 . VAL   B 1 41  ? 41.267 -17.802 10.282  1.00 17.70 ?  41  VAL   B HG12 1 
ATOM   4391 H  HG13 . VAL   B 1 41  ? 41.855 -19.201 10.753  1.00 17.70 ?  41  VAL   B HG13 1 
ATOM   4392 H  HG21 . VAL   B 1 41  ? 42.949 -18.319 13.364  1.00 18.14 ?  41  VAL   B HG21 1 
ATOM   4393 H  HG22 . VAL   B 1 41  ? 43.826 -19.208 12.383  1.00 18.14 ?  41  VAL   B HG22 1 
ATOM   4394 H  HG23 . VAL   B 1 41  ? 44.379 -17.811 12.899  1.00 18.14 ?  41  VAL   B HG23 1 
ATOM   4395 N  N    . TYR   B 1 42  ? 46.252 -17.095 10.930  1.00 12.74 ?  42  TYR   B N    1 
ATOM   4396 C  CA   . TYR   B 1 42  ? 47.404 -16.244 11.200  1.00 13.27 ?  42  TYR   B CA   1 
ATOM   4397 C  C    . TYR   B 1 42  ? 48.366 -16.165 10.020  1.00 12.30 ?  42  TYR   B C    1 
ATOM   4398 O  O    . TYR   B 1 42  ? 49.458 -15.596 10.153  1.00 13.12 ?  42  TYR   B O    1 
ATOM   4399 C  CB   . TYR   B 1 42  ? 48.105 -16.647 12.503  1.00 15.28 ?  42  TYR   B CB   1 
ATOM   4400 C  CG   . TYR   B 1 42  ? 47.497 -15.968 13.725  1.00 15.72 ?  42  TYR   B CG   1 
ATOM   4401 C  CD1  . TYR   B 1 42  ? 47.710 -14.611 13.965  1.00 15.08 ?  42  TYR   B CD1  1 
ATOM   4402 C  CD2  . TYR   B 1 42  ? 46.708 -16.670 14.622  1.00 17.80 ?  42  TYR   B CD2  1 
ATOM   4403 C  CE1  . TYR   B 1 42  ? 47.159 -13.979 15.061  1.00 16.50 ?  42  TYR   B CE1  1 
ATOM   4404 C  CE2  . TYR   B 1 42  ? 46.153 -16.044 15.727  1.00 18.33 ?  42  TYR   B CE2  1 
ATOM   4405 C  CZ   . TYR   B 1 42  ? 46.380 -14.696 15.940  1.00 18.75 ?  42  TYR   B CZ   1 
ATOM   4406 O  OH   . TYR   B 1 42  ? 45.835 -14.068 17.039  1.00 21.56 ?  42  TYR   B OH   1 
ATOM   4407 H  H    . TYR   B 1 42  ? 46.400 -17.940 11.029  1.00 15.27 ?  42  TYR   B H    1 
ATOM   4408 H  HA   . TYR   B 1 42  ? 47.073 -15.347 11.336  1.00 15.90 ?  42  TYR   B HA   1 
ATOM   4409 H  HB2  . TYR   B 1 42  ? 48.029 -17.605 12.624  1.00 18.31 ?  42  TYR   B HB2  1 
ATOM   4410 H  HB3  . TYR   B 1 42  ? 49.039 -16.391 12.450  1.00 18.31 ?  42  TYR   B HB3  1 
ATOM   4411 H  HD1  . TYR   B 1 42  ? 48.238 -14.125 13.368  1.00 18.07 ?  42  TYR   B HD1  1 
ATOM   4412 H  HD2  . TYR   B 1 42  ? 46.549 -17.576 14.477  1.00 21.33 ?  42  TYR   B HD2  1 
ATOM   4413 H  HE1  . TYR   B 1 42  ? 47.319 -13.075 15.203  1.00 19.77 ?  42  TYR   B HE1  1 
ATOM   4414 H  HE2  . TYR   B 1 42  ? 45.625 -16.528 16.319  1.00 21.98 ?  42  TYR   B HE2  1 
ATOM   4415 H  HH   . TYR   B 1 42  ? 46.058 -13.261 17.044  1.00 25.84 ?  42  TYR   B HH   1 
ATOM   4416 N  N    . LEU   B 1 43  ? 47.965 -16.680 8.860   1.00 11.24 ?  43  LEU   B N    1 
ATOM   4417 C  CA   . LEU   B 1 43  ? 48.774 -16.613 7.648   1.00 11.32 ?  43  LEU   B CA   1 
ATOM   4418 C  C    . LEU   B 1 43  ? 50.187 -17.124 7.896   1.00 11.70 ?  43  LEU   B C    1 
ATOM   4419 O  O    . LEU   B 1 43  ? 51.166 -16.534 7.441   1.00 12.18 ?  43  LEU   B O    1 
ATOM   4420 C  CB   . LEU   B 1 43  ? 48.793 -15.209 7.043   1.00 11.27 ?  43  LEU   B CB   1 
ATOM   4421 C  CG   . LEU   B 1 43  ? 47.439 -14.597 6.668   1.00 11.48 ?  43  LEU   B CG   1 
ATOM   4422 C  CD1  . LEU   B 1 43  ? 47.651 -13.203 6.079   1.00 12.95 ?  43  LEU   B CD1  1 
ATOM   4423 C  CD2  . LEU   B 1 43  ? 46.679 -15.494 5.692   1.00 11.61 ?  43  LEU   B CD2  1 
ATOM   4424 H  H    . LEU   B 1 43  ? 47.217 -17.089 8.745   1.00 13.47 ?  43  LEU   B H    1 
ATOM   4425 H  HA   . LEU   B 1 43  ? 48.375 -17.202 6.984   1.00 13.56 ?  43  LEU   B HA   1 
ATOM   4426 H  HB2  . LEU   B 1 43  ? 49.211 -14.613 7.682   1.00 13.50 ?  43  LEU   B HB2  1 
ATOM   4427 H  HB3  . LEU   B 1 43  ? 49.327 -15.239 6.234   1.00 13.50 ?  43  LEU   B HB3  1 
ATOM   4428 H  HG   . LEU   B 1 43  ? 46.902 -14.504 7.467   1.00 13.75 ?  43  LEU   B HG   1 
ATOM   4429 H  HD11 . LEU   B 1 43  ? 46.790 -12.822 5.844   1.00 15.51 ?  43  LEU   B HD11 1 
ATOM   4430 H  HD12 . LEU   B 1 43  ? 48.089 -12.643 6.742   1.00 15.51 ?  43  LEU   B HD12 1 
ATOM   4431 H  HD13 . LEU   B 1 43  ? 48.209 -13.271 5.288   1.00 15.51 ?  43  LEU   B HD13 1 
ATOM   4432 H  HD21 . LEU   B 1 43  ? 45.882 -15.029 5.392   1.00 13.90 ?  43  LEU   B HD21 1 
ATOM   4433 H  HD22 . LEU   B 1 43  ? 47.250 -15.695 4.936   1.00 13.90 ?  43  LEU   B HD22 1 
ATOM   4434 H  HD23 . LEU   B 1 43  ? 46.430 -16.314 6.147   1.00 13.90 ?  43  LEU   B HD23 1 
ATOM   4435 N  N    . LYS   B 1 44  ? 50.288 -18.242 8.613   1.00 11.46 ?  44  LYS   B N    1 
ATOM   4436 C  CA   . LYS   B 1 44  ? 51.554 -18.926 8.847   1.00 12.23 ?  44  LYS   B CA   1 
ATOM   4437 C  C    . LYS   B 1 44  ? 51.674 -20.037 7.816   1.00 11.86 ?  44  LYS   B C    1 
ATOM   4438 O  O    . LYS   B 1 44  ? 50.981 -21.056 7.902   1.00 12.82 ?  44  LYS   B O    1 
ATOM   4439 C  CB   . LYS   B 1 44  ? 51.610 -19.451 10.280  1.00 14.03 ?  44  LYS   B CB   1 
ATOM   4440 C  CG   . LYS   B 1 44  ? 51.804 -18.345 11.309  1.00 16.69 ?  44  LYS   B CG   1 
ATOM   4441 C  CD   . LYS   B 1 44  ? 53.013 -17.489 10.925  1.00 19.95 ?  44  LYS   B CD   1 
ATOM   4442 C  CE   . LYS   B 1 44  ? 53.477 -16.582 12.035  1.00 22.29 ?  44  LYS   B CE   1 
ATOM   4443 N  NZ   . LYS   B 1 44  ? 54.676 -15.792 11.656  1.00 23.27 ?  44  LYS   B NZ   1 
ATOM   4444 H  H    . LYS   B 1 44  ? 49.616 -18.628 8.986   1.00 13.73 ?  44  LYS   B H    1 
ATOM   4445 H  HA   . LYS   B 1 44  ? 52.285 -18.311 8.688   1.00 14.65 ?  44  LYS   B HA   1 
ATOM   4446 H  HB2  . LYS   B 1 44  ? 50.770 -19.901 10.483  1.00 16.81 ?  44  LYS   B HB2  1 
ATOM   4447 H  HB3  . LYS   B 1 44  ? 52.345 -20.071 10.363  1.00 16.81 ?  44  LYS   B HB3  1 
ATOM   4448 H  HG2  . LYS   B 1 44  ? 51.016 -17.784 11.335  1.00 20.00 ?  44  LYS   B HG2  1 
ATOM   4449 H  HG3  . LYS   B 1 44  ? 51.969 -18.745 12.180  1.00 20.00 ?  44  LYS   B HG3  1 
ATOM   4450 H  HD2  . LYS   B 1 44  ? 53.744 -18.081 10.669  1.00 23.92 ?  44  LYS   B HD2  1 
ATOM   4451 H  HD3  . LYS   B 1 44  ? 52.767 -16.927 10.173  1.00 23.92 ?  44  LYS   B HD3  1 
ATOM   4452 H  HE2  . LYS   B 1 44  ? 52.769 -15.956 12.225  1.00 26.73 ?  44  LYS   B HE2  1 
ATOM   4453 H  HE3  . LYS   B 1 44  ? 53.688 -17.115 12.818  1.00 26.73 ?  44  LYS   B HE3  1 
ATOM   4454 H  HZ1  . LYS   B 1 44  ? 54.917 -15.267 12.333  1.00 27.89 ?  44  LYS   B HZ1  1 
ATOM   4455 H  HZ2  . LYS   B 1 44  ? 55.351 -16.333 11.453  1.00 27.89 ?  44  LYS   B HZ2  1 
ATOM   4456 H  HZ3  . LYS   B 1 44  ? 54.492 -15.281 10.948  1.00 27.89 ?  44  LYS   B HZ3  1 
ATOM   4457 N  N    . HIS   B 1 45  ? 52.527 -19.817 6.819   1.00 11.53 ?  45  HIS   B N    1 
ATOM   4458 C  CA   . HIS   B 1 45  ? 52.548 -20.647 5.618   1.00 11.59 ?  45  HIS   B CA   1 
ATOM   4459 C  C    . HIS   B 1 45  ? 53.568 -21.770 5.777   1.00 13.69 ?  45  HIS   B C    1 
ATOM   4460 O  O    . HIS   B 1 45  ? 54.628 -21.786 5.158   1.00 15.86 ?  45  HIS   B O    1 
ATOM   4461 C  CB   . HIS   B 1 45  ? 52.859 -19.792 4.403   1.00 11.56 ?  45  HIS   B CB   1 
ATOM   4462 C  CG   . HIS   B 1 45  ? 51.987 -18.590 4.296   1.00 11.41 ?  45  HIS   B CG   1 
ATOM   4463 N  ND1  . HIS   B 1 45  ? 50.611 -18.670 4.265   1.00 11.52 ?  45  HIS   B ND1  1 
ATOM   4464 C  CD2  . HIS   B 1 45  ? 52.302 -17.276 4.228   1.00 12.20 ?  45  HIS   B CD2  1 
ATOM   4465 C  CE1  . HIS   B 1 45  ? 50.120 -17.448 4.168   1.00 11.34 ?  45  HIS   B CE1  1 
ATOM   4466 N  NE2  . HIS   B 1 45  ? 51.121 -16.584 4.142   1.00 11.76 ?  45  HIS   B NE2  1 
ATOM   4467 H  H    . HIS   B 1 45  ? 53.105 -19.179 6.810   1.00 13.81 ?  45  HIS   B H    1 
ATOM   4468 H  HA   . HIS   B 1 45  ? 51.669 -21.045 5.490   1.00 13.88 ?  45  HIS   B HA   1 
ATOM   4469 H  HB2  . HIS   B 1 45  ? 53.779 -19.496 4.453   1.00 13.85 ?  45  HIS   B HB2  1 
ATOM   4470 H  HB3  . HIS   B 1 45  ? 52.730 -20.330 3.600   1.00 13.85 ?  45  HIS   B HB3  1 
ATOM   4471 H  HD2  . HIS   B 1 45  ? 53.159 -16.911 4.235   1.00 14.62 ?  45  HIS   B HD2  1 
ATOM   4472 H  HE1  . HIS   B 1 45  ? 49.219 -17.232 4.116   1.00 13.58 ?  45  HIS   B HE1  1 
ATOM   4473 H  HE2  . HIS   B 1 45  ? 51.046 -15.730 4.091   1.00 14.09 ?  45  HIS   B HE2  1 
ATOM   4474 N  N    A GLY   B 1 46  ? 53.207 -22.742 6.610   0.60 14.54 ?  46  GLY   B N    1 
ATOM   4475 N  N    B GLY   B 1 46  ? 53.217 -22.728 6.626   0.40 14.44 ?  46  GLY   B N    1 
ATOM   4476 C  CA   A GLY   B 1 46  ? 54.134 -23.795 6.985   0.60 16.17 ?  46  GLY   B CA   1 
ATOM   4477 C  CA   B GLY   B 1 46  ? 54.139 -23.794 6.961   0.40 15.69 ?  46  GLY   B CA   1 
ATOM   4478 C  C    A GLY   B 1 46  ? 54.182 -25.015 6.087   0.60 17.86 ?  46  GLY   B C    1 
ATOM   4479 C  C    B GLY   B 1 46  ? 54.165 -24.941 5.973   0.40 17.16 ?  46  GLY   B C    1 
ATOM   4480 O  O    A GLY   B 1 46  ? 55.263 -25.443 5.671   0.60 20.54 ?  46  GLY   B O    1 
ATOM   4481 O  O    B GLY   B 1 46  ? 55.198 -25.223 5.357   0.40 18.38 ?  46  GLY   B O    1 
ATOM   4482 H  H    A GLY   B 1 46  ? 52.431 -22.799 6.985   0.60 17.43 ?  46  GLY   B H    1 
ATOM   4483 H  H    B GLY   B 1 46  ? 52.453 -22.772 7.027   0.40 17.30 ?  46  GLY   B H    1 
ATOM   4484 H  HA2  A GLY   B 1 46  ? 55.026 -23.418 7.024   0.60 19.38 ?  46  GLY   B HA2  1 
ATOM   4485 H  HA2  B GLY   B 1 46  ? 55.033 -23.424 7.018   0.40 18.81 ?  46  GLY   B HA2  1 
ATOM   4486 H  HA3  A GLY   B 1 46  ? 53.903 -24.104 7.874   0.60 19.38 ?  46  GLY   B HA3  1 
ATOM   4487 H  HA3  B GLY   B 1 46  ? 53.903 -24.146 7.834   0.40 18.81 ?  46  GLY   B HA3  1 
ATOM   4488 N  N    . GLY   B 1 47  ? 53.023 -25.603 5.794   1.00 17.20 ?  47  GLY   B N    1 
ATOM   4489 C  CA   . GLY   B 1 47  ? 52.962 -26.869 5.094   1.00 15.09 ?  47  GLY   B CA   1 
ATOM   4490 C  C    . GLY   B 1 47  ? 52.041 -26.848 3.890   1.00 13.13 ?  47  GLY   B C    1 
ATOM   4491 O  O    . GLY   B 1 47  ? 51.394 -25.845 3.590   1.00 13.15 ?  47  GLY   B O    1 
ATOM   4492 H  H    A GLY   B 1 47  ? 52.252 -25.291 6.016   0.60 20.62 ?  47  GLY   B H    1 
ATOM   4493 H  H    B GLY   B 1 47  ? 52.258 -25.329 6.080   0.40 20.62 ?  47  GLY   B H    1 
ATOM   4494 H  HA2  . GLY   B 1 47  ? 53.850 -27.116 4.789   1.00 18.08 ?  47  GLY   B HA2  1 
ATOM   4495 H  HA3  . GLY   B 1 47  ? 52.653 -27.556 5.706   1.00 18.08 ?  47  GLY   B HA3  1 
ATOM   4496 N  N    . GLY   B 1 48  ? 51.999 -27.987 3.201   1.00 12.29 ?  48  GLY   B N    1 
ATOM   4497 C  CA   . GLY   B 1 48  ? 51.075 -28.132 2.093   1.00 12.04 ?  48  GLY   B CA   1 
ATOM   4498 C  C    . GLY   B 1 48  ? 51.211 -27.024 1.074   1.00 11.76 ?  48  GLY   B C    1 
ATOM   4499 O  O    . GLY   B 1 48  ? 52.311 -26.558 0.756   1.00 12.12 ?  48  GLY   B O    1 
ATOM   4500 H  H    . GLY   B 1 48  ? 52.495 -28.666 3.351   1.00 14.73 ?  48  GLY   B H    1 
ATOM   4501 H  HA2  . GLY   B 1 48  ? 51.238 -28.979 1.652   1.00 14.43 ?  48  GLY   B HA2  1 
ATOM   4502 H  HA3  . GLY   B 1 48  ? 50.166 -28.127 2.428   1.00 14.43 ?  48  GLY   B HA3  1 
ATOM   4503 N  N    . VAL   B 1 49  ? 50.063 -26.592 0.549   1.00 11.49 ?  49  VAL   B N    1 
ATOM   4504 C  CA   . VAL   B 1 49  ? 50.039 -25.566 -0.492  1.00 11.56 ?  49  VAL   B CA   1 
ATOM   4505 C  C    . VAL   B 1 49  ? 50.698 -24.276 -0.007  1.00 10.43 ?  49  VAL   B C    1 
ATOM   4506 O  O    . VAL   B 1 49  ? 51.489 -23.657 -0.728  1.00 11.19 ?  49  VAL   B O    1 
ATOM   4507 C  CB   . VAL   B 1 49  ? 48.595 -25.319 -0.970  1.00 12.74 ?  49  VAL   B CB   1 
ATOM   4508 C  CG1  . VAL   B 1 49  ? 48.522 -24.078 -1.854  1.00 12.82 ?  49  VAL   B CG1  1 
ATOM   4509 C  CG2  . VAL   B 1 49  ? 48.056 -26.539 -1.705  1.00 14.27 ?  49  VAL   B CG2  1 
ATOM   4510 H  H    . VAL   B 1 49  ? 49.282 -26.877 0.777   1.00 13.76 ?  49  VAL   B H    1 
ATOM   4511 H  HA   . VAL   B 1 49  ? 50.543 -25.885 -1.256  1.00 13.84 ?  49  VAL   B HA   1 
ATOM   4512 H  HB   . VAL   B 1 49  ? 48.029 -25.164 -0.199  1.00 15.27 ?  49  VAL   B HB   1 
ATOM   4513 H  HG11 . VAL   B 1 49  ? 47.691 -24.095 -2.356  1.00 15.36 ?  49  VAL   B HG11 1 
ATOM   4514 H  HG12 . VAL   B 1 49  ? 48.549 -23.285 -1.295  1.00 15.36 ?  49  VAL   B HG12 1 
ATOM   4515 H  HG13 . VAL   B 1 49  ? 49.274 -24.079 -2.466  1.00 15.36 ?  49  VAL   B HG13 1 
ATOM   4516 H  HG21 . VAL   B 1 49  ? 47.147 -26.360 -1.997  1.00 17.10 ?  49  VAL   B HG21 1 
ATOM   4517 H  HG22 . VAL   B 1 49  ? 48.619 -26.719 -2.476  1.00 17.10 ?  49  VAL   B HG22 1 
ATOM   4518 H  HG23 . VAL   B 1 49  ? 48.066 -27.300 -1.104  1.00 17.10 ?  49  VAL   B HG23 1 
ATOM   4519 N  N    . ALA   B 1 50  ? 50.357 -23.834 1.208   1.00 10.32 ?  50  ALA   B N    1 
ATOM   4520 C  CA   . ALA   B 1 50  ? 50.878 -22.560 1.690   1.00 10.20 ?  50  ALA   B CA   1 
ATOM   4521 C  C    . ALA   B 1 50  ? 52.398 -22.592 1.792   1.00 10.47 ?  50  ALA   B C    1 
ATOM   4522 O  O    . ALA   B 1 50  ? 53.077 -21.626 1.423   1.00 10.70 ?  50  ALA   B O    1 
ATOM   4523 C  CB   . ALA   B 1 50  ? 50.247 -22.205 3.035   1.00 10.79 ?  50  ALA   B CB   1 
ATOM   4524 H  H    . ALA   B 1 50  ? 49.838 -24.244 1.755   1.00 12.36 ?  50  ALA   B H    1 
ATOM   4525 H  HA   . ALA   B 1 50  ? 50.647 -21.865 1.062   1.00 12.22 ?  50  ALA   B HA   1 
ATOM   4526 H  HB1  . ALA   B 1 50  ? 50.606 -21.354 3.341   1.00 12.92 ?  50  ALA   B HB1  1 
ATOM   4527 H  HB2  . ALA   B 1 50  ? 49.284 -22.132 2.925   1.00 12.92 ?  50  ALA   B HB2  1 
ATOM   4528 H  HB3  . ALA   B 1 50  ? 50.453 -22.898 3.682   1.00 12.92 ?  50  ALA   B HB3  1 
ATOM   4529 N  N    . GLY   B 1 51  ? 52.952 -23.687 2.309   1.00 11.13 ?  51  GLY   B N    1 
ATOM   4530 C  CA   . GLY   B 1 51  ? 54.396 -23.788 2.382   1.00 11.91 ?  51  GLY   B CA   1 
ATOM   4531 C  C    . GLY   B 1 51  ? 55.042 -23.734 1.013   1.00 11.45 ?  51  GLY   B C    1 
ATOM   4532 O  O    . GLY   B 1 51  ? 56.083 -23.098 0.832   1.00 12.42 ?  51  GLY   B O    1 
ATOM   4533 H  H    . GLY   B 1 51  ? 52.522 -24.371 2.614   1.00 13.33 ?  51  GLY   B H    1 
ATOM   4534 H  HA2  . GLY   B 1 51  ? 54.746 -23.057 2.917   1.00 14.27 ?  51  GLY   B HA2  1 
ATOM   4535 H  HA3  . GLY   B 1 51  ? 54.644 -24.624 2.809   1.00 14.27 ?  51  GLY   B HA3  1 
ATOM   4536 N  N    . ALA   B 1 52  ? 54.435 -24.397 0.030   1.00 11.32 ?  52  ALA   B N    1 
ATOM   4537 C  CA   . ALA   B 1 52  ? 54.996 -24.404 -1.313  1.00 11.78 ?  52  ALA   B CA   1 
ATOM   4538 C  C    . ALA   B 1 52  ? 54.916 -23.029 -1.964  1.00 11.41 ?  52  ALA   B C    1 
ATOM   4539 O  O    . ALA   B 1 52  ? 55.886 -22.576 -2.590  1.00 11.86 ?  52  ALA   B O    1 
ATOM   4540 C  CB   . ALA   B 1 52  ? 54.297 -25.453 -2.170  1.00 12.36 ?  52  ALA   B CB   1 
ATOM   4541 H  H    . ALA   B 1 52  ? 53.698 -24.835 0.113   1.00 13.56 ?  52  ALA   B H    1 
ATOM   4542 H  HA   . ALA   B 1 52  ? 55.934 -24.642 -1.251  1.00 14.11 ?  52  ALA   B HA   1 
ATOM   4543 H  HB1  . ALA   B 1 52  ? 54.691 -25.443 -3.057  1.00 14.81 ?  52  ALA   B HB1  1 
ATOM   4544 H  HB2  . ALA   B 1 52  ? 54.427 -26.323 -1.762  1.00 14.81 ?  52  ALA   B HB2  1 
ATOM   4545 H  HB3  . ALA   B 1 52  ? 53.356 -25.243 -2.220  1.00 14.81 ?  52  ALA   B HB3  1 
ATOM   4546 N  N    . LEU   B 1 53  ? 53.771 -22.352 -1.845  1.00 10.84 ?  53  LEU   B N    1 
ATOM   4547 C  CA   . LEU   B 1 53  ? 53.658 -21.014 -2.416  1.00 10.79 ?  53  LEU   B CA   1 
ATOM   4548 C  C    . LEU   B 1 53  ? 54.663 -20.071 -1.769  1.00 10.89 ?  53  LEU   B C    1 
ATOM   4549 O  O    . LEU   B 1 53  ? 55.366 -19.322 -2.457  1.00 11.64 ?  53  LEU   B O    1 
ATOM   4550 C  CB   . LEU   B 1 53  ? 52.236 -20.475 -2.243  1.00 11.26 ?  53  LEU   B CB   1 
ATOM   4551 C  CG   . LEU   B 1 53  ? 51.106 -21.196 -2.979  1.00 11.66 ?  53  LEU   B CG   1 
ATOM   4552 C  CD1  . LEU   B 1 53  ? 49.762 -20.597 -2.606  1.00 13.03 ?  53  LEU   B CD1  1 
ATOM   4553 C  CD2  . LEU   B 1 53  ? 51.308 -21.165 -4.487  1.00 13.54 ?  53  LEU   B CD2  1 
ATOM   4554 H  H    . LEU   B 1 53  ? 53.064 -22.637 -1.451  1.00 12.98 ?  53  LEU   B H    1 
ATOM   4555 H  HA   . LEU   B 1 53  ? 53.853 -21.054 -3.369  1.00 12.93 ?  53  LEU   B HA   1 
ATOM   4556 H  HB2  . LEU   B 1 53  ? 52.021 -20.504 -1.300  1.00 13.49 ?  53  LEU   B HB2  1 
ATOM   4557 H  HB3  . LEU   B 1 53  ? 52.224 -19.556 -2.547  1.00 13.49 ?  53  LEU   B HB3  1 
ATOM   4558 H  HG   . LEU   B 1 53  ? 51.095 -22.125 -2.700  1.00 13.97 ?  53  LEU   B HG   1 
ATOM   4559 H  HD11 . LEU   B 1 53  ? 49.059 -21.073 -3.080  1.00 15.61 ?  53  LEU   B HD11 1 
ATOM   4560 H  HD12 . LEU   B 1 53  ? 49.627 -20.687 -1.647  1.00 15.61 ?  53  LEU   B HD12 1 
ATOM   4561 H  HD13 . LEU   B 1 53  ? 49.750 -19.661 -2.853  1.00 15.61 ?  53  LEU   B HD13 1 
ATOM   4562 H  HD21 . LEU   B 1 53  ? 50.583 -21.644 -4.915  1.00 16.23 ?  53  LEU   B HD21 1 
ATOM   4563 H  HD22 . LEU   B 1 53  ? 51.315 -20.242 -4.786  1.00 16.23 ?  53  LEU   B HD22 1 
ATOM   4564 H  HD23 . LEU   B 1 53  ? 52.155 -21.588 -4.702  1.00 16.23 ?  53  LEU   B HD23 1 
ATOM   4565 N  N    . ASN   B 1 54  ? 54.752 -20.096 -0.441  1.00 10.60 ?  54  ASN   B N    1 
ATOM   4566 C  CA   . ASN   B 1 54  ? 55.668 -19.184 0.228   1.00 11.18 ?  54  ASN   B CA   1 
ATOM   4567 C  C    . ASN   B 1 54  ? 57.110 -19.464 -0.172  1.00 11.39 ?  54  ASN   B C    1 
ATOM   4568 O  O    . ASN   B 1 54  ? 57.884 -18.528 -0.413  1.00 11.97 ?  54  ASN   B O    1 
ATOM   4569 C  CB   . ASN   B 1 54  ? 55.508 -19.265 1.739   1.00 12.09 ?  54  ASN   B CB   1 
ATOM   4570 C  CG   . ASN   B 1 54  ? 56.488 -18.354 2.450   1.00 12.25 ?  54  ASN   B CG   1 
ATOM   4571 O  OD1  . ASN   B 1 54  ? 56.497 -17.145 2.215   1.00 12.21 ?  54  ASN   B OD1  1 
ATOM   4572 N  ND2  . ASN   B 1 54  ? 57.339 -18.927 3.292   1.00 13.92 ?  54  ASN   B ND2  1 
ATOM   4573 H  H    . ASN   B 1 54  ? 54.306 -20.616 0.076   1.00 12.70 ?  54  ASN   B H    1 
ATOM   4574 H  HA   . ASN   B 1 54  ? 55.455 -18.277 -0.044  1.00 13.40 ?  54  ASN   B HA   1 
ATOM   4575 H  HB2  . ASN   B 1 54  ? 54.608 -18.986 1.982   1.00 14.49 ?  54  ASN   B HB2  1 
ATOM   4576 H  HB3  . ASN   B 1 54  ? 55.669 -20.171 2.033   1.00 14.49 ?  54  ASN   B HB3  1 
ATOM   4577 H  HD21 . ASN   B 1 54  ? 57.919 -18.448 3.711   1.00 16.68 ?  54  ASN   B HD21 1 
ATOM   4578 H  HD22 . ASN   B 1 54  ? 57.314 -19.778 3.418   1.00 16.68 ?  54  ASN   B HD22 1 
ATOM   4579 N  N    . LYS   B 1 55  ? 57.493 -20.742 -0.236  1.00 12.21 ?  55  LYS   B N    1 
ATOM   4580 C  CA   . LYS   B 1 55  ? 58.848 -21.084 -0.654  1.00 13.11 ?  55  LYS   B CA   1 
ATOM   4581 C  C    . LYS   B 1 55  ? 59.147 -20.537 -2.045  1.00 13.06 ?  55  LYS   B C    1 
ATOM   4582 O  O    . LYS   B 1 55  ? 60.247 -20.032 -2.297  1.00 13.69 ?  55  LYS   B O    1 
ATOM   4583 C  CB   . LYS   B 1 55  ? 59.038 -22.601 -0.610  1.00 14.89 ?  55  LYS   B CB   1 
ATOM   4584 C  CG   . LYS   B 1 55  ? 60.421 -23.066 -1.024  1.00 18.69 ?  55  LYS   B CG   1 
ATOM   4585 C  CD   . LYS   B 1 55  ? 60.580 -24.564 -0.848  1.00 22.28 ?  55  LYS   B CD   1 
ATOM   4586 C  CE   . LYS   B 1 55  ? 60.637 -24.954 0.626   1.00 25.37 ?  55  LYS   B CE   1 
ATOM   4587 N  NZ   . LYS   B 1 55  ? 60.984 -26.384 0.810   1.00 26.70 ?  55  LYS   B NZ   1 
ATOM   4588 H  H    . LYS   B 1 55  ? 56.989 -21.413 -0.050  1.00 14.62 ?  55  LYS   B H    1 
ATOM   4589 H  HA   . LYS   B 1 55  ? 59.476 -20.686 -0.038  1.00 15.71 ?  55  LYS   B HA   1 
ATOM   4590 H  HB2  . LYS   B 1 55  ? 58.882 -22.902 0.299   1.00 17.85 ?  55  LYS   B HB2  1 
ATOM   4591 H  HB3  . LYS   B 1 55  ? 58.397 -23.017 -1.206  1.00 17.85 ?  55  LYS   B HB3  1 
ATOM   4592 H  HG2  . LYS   B 1 55  ? 60.564 -22.855 -1.960  1.00 22.41 ?  55  LYS   B HG2  1 
ATOM   4593 H  HG3  . LYS   B 1 55  ? 61.086 -22.621 -0.475  1.00 22.41 ?  55  LYS   B HG3  1 
ATOM   4594 H  HD2  . LYS   B 1 55  ? 59.824 -25.020 -1.251  1.00 26.71 ?  55  LYS   B HD2  1 
ATOM   4595 H  HD3  . LYS   B 1 55  ? 61.407 -24.853 -1.267  1.00 26.71 ?  55  LYS   B HD3  1 
ATOM   4596 H  HE2  . LYS   B 1 55  ? 61.313 -24.413 1.068   1.00 30.42 ?  55  LYS   B HE2  1 
ATOM   4597 H  HE3  . LYS   B 1 55  ? 59.768 -24.794 1.029   1.00 30.42 ?  55  LYS   B HE3  1 
ATOM   4598 H  HZ1  . LYS   B 1 55  ? 60.971 -26.588 1.676   1.00 32.01 ?  55  LYS   B HZ1  1 
ATOM   4599 H  HZ2  . LYS   B 1 55  ? 60.391 -26.893 0.384   1.00 32.01 ?  55  LYS   B HZ2  1 
ATOM   4600 H  HZ3  . LYS   B 1 55  ? 61.793 -26.544 0.483   1.00 32.01 ?  55  LYS   B HZ3  1 
ATOM   4601 N  N    . ALA   B 1 56  ? 58.177 -20.621 -2.962  1.00 12.49 ?  56  ALA   B N    1 
ATOM   4602 C  CA   . ALA   B 1 56  ? 58.398 -20.116 -4.312  1.00 13.40 ?  56  ALA   B CA   1 
ATOM   4603 C  C    . ALA   B 1 56  ? 58.664 -18.617 -4.309  1.00 13.24 ?  56  ALA   B C    1 
ATOM   4604 O  O    . ALA   B 1 56  ? 59.389 -18.115 -5.178  1.00 14.35 ?  56  ALA   B O    1 
ATOM   4605 C  CB   . ALA   B 1 56  ? 57.206 -20.455 -5.209  1.00 14.32 ?  56  ALA   B CB   1 
ATOM   4606 H  H    . ALA   B 1 56  ? 57.395 -20.955 -2.829  1.00 14.96 ?  56  ALA   B H    1 
ATOM   4607 H  HA   . ALA   B 1 56  ? 59.178 -20.548 -4.683  1.00 16.06 ?  56  ALA   B HA   1 
ATOM   4608 H  HB1  . ALA   B 1 56  ? 57.377 -20.117 -6.105  1.00 17.16 ?  56  ALA   B HB1  1 
ATOM   4609 H  HB2  . ALA   B 1 56  ? 57.099 -21.419 -5.237  1.00 17.16 ?  56  ALA   B HB2  1 
ATOM   4610 H  HB3  . ALA   B 1 56  ? 56.407 -20.042 -4.849  1.00 17.16 ?  56  ALA   B HB3  1 
ATOM   4611 N  N    . THR   B 1 57  ? 58.100 -17.889 -3.342  1.00 12.86 ?  57  THR   B N    1 
ATOM   4612 C  CA   . THR   B 1 57  ? 58.339 -16.455 -3.216  1.00 12.94 ?  57  THR   B CA   1 
ATOM   4613 C  C    . THR   B 1 57  ? 59.589 -16.132 -2.410  1.00 13.77 ?  57  THR   B C    1 
ATOM   4614 O  O    . THR   B 1 57  ? 59.826 -14.958 -2.101  1.00 14.18 ?  57  THR   B O    1 
ATOM   4615 C  CB   . THR   B 1 57  ? 57.142 -15.728 -2.572  1.00 12.31 ?  57  THR   B CB   1 
ATOM   4616 O  OG1  . THR   B 1 57  ? 57.123 -15.946 -1.154  1.00 12.52 ?  57  THR   B OG1  1 
ATOM   4617 C  CG2  . THR   B 1 57  ? 55.821 -16.146 -3.200  1.00 12.28 ?  57  THR   B CG2  1 
ATOM   4618 H  H    . THR   B 1 57  ? 57.561 -18.205 -2.748  1.00 15.40 ?  57  THR   B H    1 
ATOM   4619 H  HA   . THR   B 1 57  ? 58.453 -16.084 -4.104  1.00 15.50 ?  57  THR   B HA   1 
ATOM   4620 H  HB   . THR   B 1 57  ? 57.241 -14.776 -2.734  1.00 14.75 ?  57  THR   B HB   1 
ATOM   4621 H  HG1  . THR   B 1 57  ? 57.058 -16.766 -0.991  1.00 15.00 ?  57  THR   B HG1  1 
ATOM   4622 H  HG21 . THR   B 1 57  ? 55.097 -15.605 -2.850  1.00 14.71 ?  57  THR   B HG21 1 
ATOM   4623 H  HG22 . THR   B 1 57  ? 55.859 -16.039 -4.163  1.00 14.71 ?  57  THR   B HG22 1 
ATOM   4624 H  HG23 . THR   B 1 57  ? 55.638 -17.079 -2.998  1.00 14.71 ?  57  THR   B HG23 1 
ATOM   4625 N  N    . ASN   B 1 58  ? 60.384 -17.138 -2.052  1.00 14.53 ?  58  ASN   B N    1 
ATOM   4626 C  CA   . ASN   B 1 58  ? 61.584 -16.924 -1.249  1.00 17.07 ?  58  ASN   B CA   1 
ATOM   4627 C  C    . ASN   B 1 58  ? 61.247 -16.210 0.061   1.00 15.30 ?  58  ASN   B C    1 
ATOM   4628 O  O    . ASN   B 1 58  ? 61.985 -15.338 0.528   1.00 15.83 ?  58  ASN   B O    1 
ATOM   4629 C  CB   . ASN   B 1 58  ? 62.670 -16.180 -2.033  1.00 24.57 ?  58  ASN   B CB   1 
ATOM   4630 C  CG   . ASN   B 1 58  ? 64.035 -16.291 -1.381  1.00 33.79 ?  58  ASN   B CG   1 
ATOM   4631 O  OD1  . ASN   B 1 58  ? 64.336 -17.281 -0.714  1.00 35.74 ?  58  ASN   B OD1  1 
ATOM   4632 N  ND2  . ASN   B 1 58  ? 64.866 -15.273 -1.568  1.00 38.28 ?  58  ASN   B ND2  1 
ATOM   4633 H  H    . ASN   B 1 58  ? 60.246 -17.964 -2.260  1.00 17.41 ?  58  ASN   B H    1 
ATOM   4634 H  HA   . ASN   B 1 58  ? 61.947 -17.795 -1.021  1.00 20.47 ?  58  ASN   B HA   1 
ATOM   4635 H  HB2  . ASN   B 1 58  ? 62.730 -16.557 -2.929  1.00 29.46 ?  58  ASN   B HB2  1 
ATOM   4636 H  HB3  . ASN   B 1 58  ? 62.439 -15.241 -2.085  1.00 29.46 ?  58  ASN   B HB3  1 
ATOM   4637 H  HD21 . ASN   B 1 58  ? 65.653 -15.290 -1.219  1.00 45.91 ?  58  ASN   B HD21 1 
ATOM   4638 H  HD22 . ASN   B 1 58  ? 64.619 -14.598 -2.038  1.00 45.91 ?  58  ASN   B HD22 1 
ATOM   4639 N  N    . ASN   B 1 59  ? 60.121 -16.592 0.665   1.00 14.02 ?  59  ASN   B N    1 
ATOM   4640 C  CA   . ASN   B 1 59  ? 59.648 -16.126 1.968   1.00 13.95 ?  59  ASN   B CA   1 
ATOM   4641 C  C    . ASN   B 1 59  ? 59.052 -14.720 1.917   1.00 13.60 ?  59  ASN   B C    1 
ATOM   4642 O  O    . ASN   B 1 59  ? 58.616 -14.220 2.962   1.00 13.70 ?  59  ASN   B O    1 
ATOM   4643 C  CB   . ASN   B 1 59  ? 60.718 -16.191 3.074   1.00 14.92 ?  59  ASN   B CB   1 
ATOM   4644 C  CG   . ASN   B 1 59  ? 60.124 -16.365 4.454   1.00 16.27 ?  59  ASN   B CG   1 
ATOM   4645 O  OD1  . ASN   B 1 59  ? 59.298 -17.254 4.679   1.00 16.40 ?  59  ASN   B OD1  1 
ATOM   4646 N  ND2  . ASN   B 1 59  ? 60.536 -15.517 5.390   1.00 16.98 ?  59  ASN   B ND2  1 
ATOM   4647 H  H    . ASN   B 1 59  ? 59.583 -17.169 0.317   1.00 16.80 ?  59  ASN   B H    1 
ATOM   4648 H  HA   . ASN   B 1 59  ? 58.938 -16.722 2.246   1.00 16.71 ?  59  ASN   B HA   1 
ATOM   4649 H  HB2  . ASN   B 1 59  ? 61.304 -16.947 2.915   1.00 17.88 ?  59  ASN   B HB2  1 
ATOM   4650 H  HB3  . ASN   B 1 59  ? 61.228 -15.368 3.078   1.00 17.88 ?  59  ASN   B HB3  1 
ATOM   4651 H  HD21 . ASN   B 1 59  ? 60.219 -15.569 6.191   1.00 20.35 ?  59  ASN   B HD21 1 
ATOM   4652 H  HD22 . ASN   B 1 59  ? 61.107 -14.906 5.195   1.00 20.35 ?  59  ASN   B HD22 1 
ATOM   4653 N  N    . ALA   B 1 60  ? 58.992 -14.073 0.750   1.00 13.27 ?  60  ALA   B N    1 
ATOM   4654 C  CA   . ALA   B 1 60  ? 58.392 -12.743 0.676   1.00 13.06 ?  60  ALA   B CA   1 
ATOM   4655 C  C    . ALA   B 1 60  ? 56.922 -12.769 1.077   1.00 12.24 ?  60  ALA   B C    1 
ATOM   4656 O  O    . ALA   B 1 60  ? 56.417 -11.818 1.689   1.00 12.88 ?  60  ALA   B O    1 
ATOM   4657 C  CB   . ALA   B 1 60  ? 58.557 -12.168 -0.730  1.00 14.01 ?  60  ALA   B CB   1 
ATOM   4658 H  H    . ALA   B 1 60  ? 59.290 -14.381 0.005   1.00 15.89 ?  60  ALA   B H    1 
ATOM   4659 H  HA   . ALA   B 1 60  ? 58.855 -12.159 1.295   1.00 15.64 ?  60  ALA   B HA   1 
ATOM   4660 H  HB1  . ALA   B 1 60  ? 58.156 -11.289 -0.759  1.00 16.79 ?  60  ALA   B HB1  1 
ATOM   4661 H  HB2  . ALA   B 1 60  ? 59.506 -12.108 -0.936  1.00 16.79 ?  60  ALA   B HB2  1 
ATOM   4662 H  HB3  . ALA   B 1 60  ? 58.121 -12.757 -1.365  1.00 16.79 ?  60  ALA   B HB3  1 
ATOM   4663 N  N    . MET   B 1 61  ? 56.216 -13.847 0.732   1.00 11.89 ?  61  MET   B N    1 
ATOM   4664 C  CA   . MET   B 1 61  ? 54.821 -13.969 1.126   1.00 11.42 ?  61  MET   B CA   1 
ATOM   4665 C  C    . MET   B 1 61  ? 54.685 -13.981 2.647   1.00 11.44 ?  61  MET   B C    1 
ATOM   4666 O  O    . MET   B 1 61  ? 53.786 -13.336 3.200   1.00 11.66 ?  61  MET   B O    1 
ATOM   4667 C  CB   . MET   B 1 61  ? 54.238 -15.234 0.493   1.00 11.30 ?  61  MET   B CB   1 
ATOM   4668 C  CG   . MET   B 1 61  ? 52.802 -15.528 0.913   1.00 11.15 ?  61  MET   B CG   1 
ATOM   4669 S  SD   . MET   B 1 61  ? 52.166 -17.034 0.149   1.00 11.94 ?  61  MET   B SD   1 
ATOM   4670 C  CE   . MET   B 1 61  ? 51.907 -16.447 -1.522  1.00 12.80 ?  61  MET   B CE   1 
ATOM   4671 H  H    . MET   B 1 61  ? 56.518 -14.518 0.278   1.00 14.25 ?  61  MET   B H    1 
ATOM   4672 H  HA   . MET   B 1 61  ? 54.326 -13.214 0.770   1.00 13.68 ?  61  MET   B HA   1 
ATOM   4673 H  HB2  . MET   B 1 61  ? 54.244 -15.136 -0.475  1.00 13.54 ?  61  MET   B HB2  1 
ATOM   4674 H  HB3  . MET   B 1 61  ? 54.780 -15.995 0.747   1.00 13.54 ?  61  MET   B HB3  1 
ATOM   4675 H  HG2  . MET   B 1 61  ? 52.764 -15.649 1.876   1.00 13.35 ?  61  MET   B HG2  1 
ATOM   4676 H  HG3  . MET   B 1 61  ? 52.230 -14.791 0.648   1.00 13.35 ?  61  MET   B HG3  1 
ATOM   4677 H  HE1  . MET   B 1 61  ? 51.518 -17.160 -2.053  1.00 15.33 ?  61  MET   B HE1  1 
ATOM   4678 H  HE2  . MET   B 1 61  ? 51.304 -15.684 -1.503  1.00 15.33 ?  61  MET   B HE2  1 
ATOM   4679 H  HE3  . MET   B 1 61  ? 52.760 -16.181 -1.900  1.00 15.33 ?  61  MET   B HE3  1 
ATOM   4680 N  N    . GLN   B 1 62  ? 55.566 -14.702 3.345   1.00 11.53 ?  62  GLN   B N    1 
ATOM   4681 C  CA   . GLN   B 1 62  ? 55.465 -14.761 4.800   1.00 11.92 ?  62  GLN   B CA   1 
ATOM   4682 C  C    . GLN   B 1 62  ? 55.751 -13.406 5.437   1.00 12.03 ?  62  GLN   B C    1 
ATOM   4683 O  O    . GLN   B 1 62  ? 55.067 -13.003 6.386   1.00 12.56 ?  62  GLN   B O    1 
ATOM   4684 C  CB   . GLN   B 1 62  ? 56.412 -15.823 5.358   1.00 12.28 ?  62  GLN   B CB   1 
ATOM   4685 C  CG   . GLN   B 1 62  ? 56.194 -16.087 6.835   1.00 12.45 ?  62  GLN   B CG   1 
ATOM   4686 C  CD   . GLN   B 1 62  ? 54.824 -16.677 7.084   1.00 12.02 ?  62  GLN   B CD   1 
ATOM   4687 O  OE1  . GLN   B 1 62  ? 54.565 -17.825 6.728   1.00 12.41 ?  62  GLN   B OE1  1 
ATOM   4688 N  NE2  . GLN   B 1 62  ? 53.914 -15.880 7.640   1.00 12.53 ?  62  GLN   B NE2  1 
ATOM   4689 H  H    . GLN   B 1 62  ? 56.213 -15.156 3.002   1.00 13.81 ?  62  GLN   B H    1 
ATOM   4690 H  HA   . GLN   B 1 62  ? 54.559 -15.017 5.032   1.00 14.28 ?  62  GLN   B HA   1 
ATOM   4691 H  HB2  . GLN   B 1 62  ? 56.275 -16.657 4.881   1.00 14.71 ?  62  GLN   B HB2  1 
ATOM   4692 H  HB3  . GLN   B 1 62  ? 57.328 -15.523 5.240   1.00 14.71 ?  62  GLN   B HB3  1 
ATOM   4693 H  HG2  . GLN   B 1 62  ? 56.860 -16.721 7.146   1.00 14.92 ?  62  GLN   B HG2  1 
ATOM   4694 H  HG3  . GLN   B 1 62  ? 56.266 -15.255 7.326   1.00 14.92 ?  62  GLN   B HG3  1 
ATOM   4695 H  HE21 . GLN   B 1 62  ? 54.124 -15.078 7.862   1.00 15.01 ?  62  GLN   B HE21 1 
ATOM   4696 H  HE22 . GLN   B 1 62  ? 53.120 -16.176 7.788   1.00 15.01 ?  62  GLN   B HE22 1 
ATOM   4697 N  N    . VAL   B 1 63  ? 56.762 -12.690 4.943   1.00 12.73 ?  63  VAL   B N    1 
ATOM   4698 C  CA   . VAL   B 1 63  ? 57.067 -11.377 5.504   1.00 13.48 ?  63  VAL   B CA   1 
ATOM   4699 C  C    . VAL   B 1 63  ? 55.877 -10.440 5.328   1.00 12.52 ?  63  VAL   B C    1 
ATOM   4700 O  O    . VAL   B 1 63  ? 55.465 -9.741  6.264   1.00 13.47 ?  63  VAL   B O    1 
ATOM   4701 C  CB   . VAL   B 1 63  ? 58.355 -10.814 4.881   1.00 14.83 ?  63  VAL   B CB   1 
ATOM   4702 C  CG1  . VAL   B 1 63  ? 58.578 -9.381  5.334   1.00 15.75 ?  63  VAL   B CG1  1 
ATOM   4703 C  CG2  . VAL   B 1 63  ? 59.536 -11.683 5.275   1.00 15.39 ?  63  VAL   B CG2  1 
ATOM   4704 H  H    . VAL   B 1 63  ? 57.263 -12.934 4.287   1.00 15.26 ?  63  VAL   B H    1 
ATOM   4705 H  HA   . VAL   B 1 63  ? 57.221 -11.483 6.452   1.00 16.16 ?  63  VAL   B HA   1 
ATOM   4706 H  HB   . VAL   B 1 63  ? 58.282 -10.827 3.914   1.00 17.77 ?  63  VAL   B HB   1 
ATOM   4707 H  HG11 . VAL   B 1 63  ? 59.495 -9.134  5.153   1.00 18.87 ?  63  VAL   B HG11 1 
ATOM   4708 H  HG12 . VAL   B 1 63  ? 57.974 -8.800  4.848   1.00 18.87 ?  63  VAL   B HG12 1 
ATOM   4709 H  HG13 . VAL   B 1 63  ? 58.401 -9.324  6.287   1.00 18.87 ?  63  VAL   B HG13 1 
ATOM   4710 H  HG21 . VAL   B 1 63  ? 60.346 -11.309 4.893   1.00 18.45 ?  63  VAL   B HG21 1 
ATOM   4711 H  HG22 . VAL   B 1 63  ? 59.607 -11.697 6.245   1.00 18.45 ?  63  VAL   B HG22 1 
ATOM   4712 H  HG23 . VAL   B 1 63  ? 59.398 -12.583 4.943   1.00 18.45 ?  63  VAL   B HG23 1 
ATOM   4713 N  N    . GLU   B 1 64  ? 55.304 -10.425 4.124   1.00 12.37 ?  64  GLU   B N    1 
ATOM   4714 C  CA   . GLU   B 1 64  ? 54.137 -9.589  3.854   1.00 12.10 ?  64  GLU   B CA   1 
ATOM   4715 C  C    . GLU   B 1 64  ? 52.957 -9.995  4.729   1.00 11.86 ?  64  GLU   B C    1 
ATOM   4716 O  O    . GLU   B 1 64  ? 52.210 -9.139  5.229   1.00 12.51 ?  64  GLU   B O    1 
ATOM   4717 C  CB   . GLU   B 1 64  ? 53.772 -9.737  2.377   1.00 12.32 ?  64  GLU   B CB   1 
ATOM   4718 C  CG   . GLU   B 1 64  ? 52.507 -9.008  1.947   1.00 12.64 ?  64  GLU   B CG   1 
ATOM   4719 C  CD   . GLU   B 1 64  ? 51.976 -9.505  0.611   1.00 13.04 ?  64  GLU   B CD   1 
ATOM   4720 O  OE1  . GLU   B 1 64  ? 52.165 -10.708 0.285   1.00 13.56 ?  64  GLU   B OE1  1 
ATOM   4721 O  OE2  . GLU   B 1 64  ? 51.355 -8.689  -0.113  1.00 13.85 -1 64  GLU   B OE2  1 
ATOM   4722 H  H    . GLU   B 1 64  ? 55.576 -10.883 3.445   1.00 14.83 ?  64  GLU   B H    1 
ATOM   4723 H  HA   . GLU   B 1 64  ? 54.352 -8.660  4.029   1.00 14.50 ?  64  GLU   B HA   1 
ATOM   4724 H  HB2  . GLU   B 1 64  ? 54.500 -9.385  1.838   1.00 14.76 ?  64  GLU   B HB2  1 
ATOM   4725 H  HB3  . GLU   B 1 64  ? 53.647 -10.675 2.182   1.00 14.76 ?  64  GLU   B HB3  1 
ATOM   4726 H  HG2  . GLU   B 1 64  ? 51.807 -9.142  2.608   1.00 15.14 ?  64  GLU   B HG2  1 
ATOM   4727 H  HG3  . GLU   B 1 64  ? 52.699 -8.060  1.862   1.00 15.14 ?  64  GLU   B HG3  1 
ATOM   4728 N  N    . SER   B 1 65  ? 52.778 -11.303 4.916   1.00 11.49 ?  65  SER   B N    1 
ATOM   4729 C  CA   . SER   B 1 65  ? 51.668 -11.811 5.712   1.00 11.67 ?  65  SER   B CA   1 
ATOM   4730 C  C    . SER   B 1 65  ? 51.802 -11.418 7.177   1.00 11.79 ?  65  SER   B C    1 
ATOM   4731 O  O    . SER   B 1 65  ? 50.806 -11.055 7.818   1.00 12.18 ?  65  SER   B O    1 
ATOM   4732 C  CB   . SER   B 1 65  ? 51.592 -13.330 5.580   1.00 11.79 ?  65  SER   B CB   1 
ATOM   4733 O  OG   . SER   B 1 65  ? 51.235 -13.728 4.263   1.00 11.94 ?  65  SER   B OG   1 
ATOM   4734 H  H    . SER   B 1 65  ? 53.289 -11.922 4.595   1.00 13.76 ?  65  SER   B H    1 
ATOM   4735 H  HA   . SER   B 1 65  ? 50.839 -11.439 5.374   1.00 13.98 ?  65  SER   B HA   1 
ATOM   4736 H  HB2  . SER   B 1 65  ? 52.456 -13.710 5.799   1.00 14.12 ?  65  SER   B HB2  1 
ATOM   4737 H  HB3  . SER   B 1 65  ? 50.921 -13.664 6.201   1.00 14.12 ?  65  SER   B HB3  1 
ATOM   4738 H  HG   . SER   B 1 65  ? 51.805 -13.440 3.714   1.00 14.31 ?  65  SER   B HG   1 
ATOM   4739 N  N    . ASP   B 1 66  ? 53.012 -11.512 7.736   1.00 12.31 ?  66  ASP   B N    1 
ATOM   4740 C  CA   . ASP   B 1 66  ? 53.203 -11.124 9.130   1.00 12.53 ?  66  ASP   B CA   1 
ATOM   4741 C  C    . ASP   B 1 66  ? 52.888 -9.646  9.337   1.00 12.62 ?  66  ASP   B C    1 
ATOM   4742 O  O    . ASP   B 1 66  ? 52.310 -9.260  10.360  1.00 13.08 ?  66  ASP   B O    1 
ATOM   4743 C  CB   . ASP   B 1 66  ? 54.636 -11.433 9.571   1.00 13.98 ?  66  ASP   B CB   1 
ATOM   4744 C  CG   . ASP   B 1 66  ? 54.907 -12.924 9.723   1.00 15.70 ?  66  ASP   B CG   1 
ATOM   4745 O  OD1  . ASP   B 1 66  ? 53.953 -13.733 9.657   1.00 16.16 ?  66  ASP   B OD1  1 
ATOM   4746 O  OD2  . ASP   B 1 66  ? 56.089 -13.291 9.922   1.00 18.24 -1 66  ASP   B OD2  1 
ATOM   4747 H  H    . ASP   B 1 66  ? 53.716 -11.799 7.340   1.00 14.75 ?  66  ASP   B H    1 
ATOM   4748 H  HA   . ASP   B 1 66  ? 52.602 -11.633 9.692   1.00 15.01 ?  66  ASP   B HA   1 
ATOM   4749 H  HB2  . ASP   B 1 66  ? 55.254 -11.092 8.908   1.00 16.75 ?  66  ASP   B HB2  1 
ATOM   4750 H  HB3  . ASP   B 1 66  ? 54.802 -11.006 10.429  1.00 16.75 ?  66  ASP   B HB3  1 
ATOM   4751 N  N    . ASP   B 1 67  ? 53.265 -8.799  8.379   1.00 12.13 ?  67  ASP   B N    1 
ATOM   4752 C  CA   . ASP   B 1 67  ? 52.914 -7.387  8.471   1.00 12.98 ?  67  ASP   B CA   1 
ATOM   4753 C  C    . ASP   B 1 67  ? 51.401 -7.182  8.386   1.00 13.26 ?  67  ASP   B C    1 
ATOM   4754 O  O    . ASP   B 1 67  ? 50.834 -6.382  9.140   1.00 13.75 ?  67  ASP   B O    1 
ATOM   4755 C  CB   . ASP   B 1 67  ? 53.631 -6.609  7.374   1.00 14.08 ?  67  ASP   B CB   1 
ATOM   4756 C  CG   . ASP   B 1 67  ? 53.201 -5.172  7.330   1.00 15.51 ?  67  ASP   B CG   1 
ATOM   4757 O  OD1  . ASP   B 1 67  ? 53.688 -4.366  8.157   1.00 16.39 ?  67  ASP   B OD1  1 
ATOM   4758 O  OD2  . ASP   B 1 67  ? 52.345 -4.863  6.484   1.00 16.74 -1 67  ASP   B OD2  1 
ATOM   4759 H  H    . ASP   B 1 67  ? 53.724 -9.012  7.683   1.00 14.53 ?  67  ASP   B H    1 
ATOM   4760 H  HA   . ASP   B 1 67  ? 53.217 -7.039  9.325   1.00 15.55 ?  67  ASP   B HA   1 
ATOM   4761 H  HB2  . ASP   B 1 67  ? 54.588 -6.628  7.537   1.00 16.87 ?  67  ASP   B HB2  1 
ATOM   4762 H  HB3  . ASP   B 1 67  ? 53.436 -7.016  6.513   1.00 16.87 ?  67  ASP   B HB3  1 
ATOM   4763 N  N    . TYR   B 1 68  ? 50.727 -7.915  7.494   1.00 12.64 ?  68  TYR   B N    1 
ATOM   4764 C  CA   . TYR   B 1 68  ? 49.269 -7.842  7.421   1.00 13.42 ?  68  TYR   B CA   1 
ATOM   4765 C  C    . TYR   B 1 68  ? 48.636 -8.186  8.765   1.00 13.05 ?  68  TYR   B C    1 
ATOM   4766 O  O    . TYR   B 1 68  ? 47.705 -7.511  9.219   1.00 13.75 ?  68  TYR   B O    1 
ATOM   4767 C  CB   . TYR   B 1 68  ? 48.738 -8.777  6.327   1.00 14.17 ?  68  TYR   B CB   1 
ATOM   4768 C  CG   . TYR   B 1 68  ? 47.234 -8.929  6.388   1.00 15.09 ?  68  TYR   B CG   1 
ATOM   4769 C  CD1  . TYR   B 1 68  ? 46.643 -9.887  7.207   1.00 15.93 ?  68  TYR   B CD1  1 
ATOM   4770 C  CD2  . TYR   B 1 68  ? 46.406 -8.096  5.659   1.00 16.31 ?  68  TYR   B CD2  1 
ATOM   4771 C  CE1  . TYR   B 1 68  ? 45.279 -10.010 7.294   1.00 17.32 ?  68  TYR   B CE1  1 
ATOM   4772 C  CE2  . TYR   B 1 68  ? 45.027 -8.216  5.736   1.00 17.07 ?  68  TYR   B CE2  1 
ATOM   4773 C  CZ   . TYR   B 1 68  ? 44.481 -9.175  6.555   1.00 17.54 ?  68  TYR   B CZ   1 
ATOM   4774 O  OH   . TYR   B 1 68  ? 43.113 -9.292  6.644   1.00 18.60 ?  68  TYR   B OH   1 
ATOM   4775 H  H    . TYR   B 1 68  ? 51.088 -8.465  6.932   1.00 15.14 ?  68  TYR   B H    1 
ATOM   4776 H  HA   . TYR   B 1 68  ? 49.018 -6.937  7.197   1.00 16.08 ?  68  TYR   B HA   1 
ATOM   4777 H  HB2  . TYR   B 1 68  ? 48.965 -8.409  5.463   1.00 16.98 ?  68  TYR   B HB2  1 
ATOM   4778 H  HB3  . TYR   B 1 68  ? 49.134 -9.653  6.438   1.00 16.98 ?  68  TYR   B HB3  1 
ATOM   4779 H  HD1  . TYR   B 1 68  ? 47.183 -10.455 7.712   1.00 19.09 ?  68  TYR   B HD1  1 
ATOM   4780 H  HD2  . TYR   B 1 68  ? 46.781 -7.443  5.119   1.00 19.54 ?  68  TYR   B HD2  1 
ATOM   4781 H  HE1  . TYR   B 1 68  ? 44.900 -10.666 7.837   1.00 20.76 ?  68  TYR   B HE1  1 
ATOM   4782 H  HE2  . TYR   B 1 68  ? 44.476 -7.654  5.243   1.00 20.46 ?  68  TYR   B HE2  1 
ATOM   4783 H  HH   . TYR   B 1 68  ? 42.732 -8.740  6.133   1.00 22.29 ?  68  TYR   B HH   1 
ATOM   4784 N  N    . ILE   B 1 69  ? 49.115 -9.258  9.406   1.00 12.93 ?  69  ILE   B N    1 
ATOM   4785 C  CA   . ILE   B 1 69  ? 48.557 -9.688  10.687  1.00 13.48 ?  69  ILE   B CA   1 
ATOM   4786 C  C    . ILE   B 1 69  ? 48.812 -8.646  11.768  1.00 13.17 ?  69  ILE   B C    1 
ATOM   4787 O  O    . ILE   B 1 69  ? 47.944 -8.373  12.603  1.00 13.52 ?  69  ILE   B O    1 
ATOM   4788 C  CB   . ILE   B 1 69  ? 49.135 -11.063 11.074  1.00 14.13 ?  69  ILE   B CB   1 
ATOM   4789 C  CG1  . ILE   B 1 69  ? 48.601 -12.160 10.146  1.00 14.47 ?  69  ILE   B CG1  1 
ATOM   4790 C  CG2  . ILE   B 1 69  ? 48.852 -11.379 12.536  1.00 14.96 ?  69  ILE   B CG2  1 
ATOM   4791 C  CD1  . ILE   B 1 69  ? 47.131 -12.472 10.319  1.00 15.16 ?  69  ILE   B CD1  1 
ATOM   4792 H  H    . ILE   B 1 69  ? 49.760 -9.748  9.125   1.00 15.49 ?  69  ILE   B H    1 
ATOM   4793 H  HA   . ILE   B 1 69  ? 47.599 -9.784  10.595  1.00 16.15 ?  69  ILE   B HA   1 
ATOM   4794 H  HB   . ILE   B 1 69  ? 50.099 -11.024 10.962  1.00 16.93 ?  69  ILE   B HB   1 
ATOM   4795 H  HG12 . ILE   B 1 69  ? 48.737 -11.877 9.227   1.00 17.34 ?  69  ILE   B HG12 1 
ATOM   4796 H  HG13 . ILE   B 1 69  ? 49.099 -12.975 10.312  1.00 17.34 ?  69  ILE   B HG13 1 
ATOM   4797 H  HG21 . ILE   B 1 69  ? 48.989 -12.330 12.681  1.00 17.93 ?  69  ILE   B HG21 1 
ATOM   4798 H  HG22 . ILE   B 1 69  ? 49.460 -10.873 13.097  1.00 17.93 ?  69  ILE   B HG22 1 
ATOM   4799 H  HG23 . ILE   B 1 69  ? 47.934 -11.145 12.739  1.00 17.93 ?  69  ILE   B HG23 1 
ATOM   4800 H  HD11 . ILE   B 1 69  ? 46.889 -13.177 9.700   1.00 18.17 ?  69  ILE   B HD11 1 
ATOM   4801 H  HD12 . ILE   B 1 69  ? 46.974 -12.766 11.230  1.00 18.17 ?  69  ILE   B HD12 1 
ATOM   4802 H  HD13 . ILE   B 1 69  ? 46.611 -11.677 10.133  1.00 18.17 ?  69  ILE   B HD13 1 
ATOM   4803 N  N    . ALA   B 1 70  ? 50.008 -8.063  11.792  1.00 13.32 ?  70  ALA   B N    1 
ATOM   4804 C  CA   . ALA   B 1 70  ? 50.291 -7.026  12.781  1.00 13.23 ?  70  ALA   B CA   1 
ATOM   4805 C  C    . ALA   B 1 70  ? 49.295 -5.879  12.671  1.00 13.17 ?  70  ALA   B C    1 
ATOM   4806 O  O    . ALA   B 1 70  ? 48.854 -5.332  13.686  1.00 13.42 ?  70  ALA   B O    1 
ATOM   4807 C  CB   . ALA   B 1 70  ? 51.722 -6.518  12.611  1.00 13.59 ?  70  ALA   B CB   1 
ATOM   4808 H  H    . ALA   B 1 70  ? 50.654 -8.244  11.264  1.00 15.96 ?  70  ALA   B H    1 
ATOM   4809 H  HA   . ALA   B 1 70  ? 50.215 -7.405  13.672  1.00 15.85 ?  70  ALA   B HA   1 
ATOM   4810 H  HB1  . ALA   B 1 70  ? 51.907 -5.853  13.295  1.00 16.29 ?  70  ALA   B HB1  1 
ATOM   4811 H  HB2  . ALA   B 1 70  ? 52.337 -7.264  12.705  1.00 16.29 ?  70  ALA   B HB2  1 
ATOM   4812 H  HB3  . ALA   B 1 70  ? 51.817 -6.122  11.731  1.00 16.29 ?  70  ALA   B HB3  1 
ATOM   4813 N  N    . THR   B 1 71  ? 48.925 -5.507  11.447  1.00 13.77 ?  71  THR   B N    1 
ATOM   4814 C  CA   . THR   B 1 71  ? 48.032 -4.374  11.238  1.00 14.85 ?  71  THR   B CA   1 
ATOM   4815 C  C    . THR   B 1 71  ? 46.567 -4.742  11.443  1.00 15.32 ?  71  THR   B C    1 
ATOM   4816 O  O    . THR   B 1 71  ? 45.787 -3.926  11.952  1.00 16.74 ?  71  THR   B O    1 
ATOM   4817 C  CB   . THR   B 1 71  ? 48.250 -3.809  9.833   1.00 16.59 ?  71  THR   B CB   1 
ATOM   4818 O  OG1  . THR   B 1 71  ? 49.575 -3.271  9.733   1.00 18.48 ?  71  THR   B OG1  1 
ATOM   4819 C  CG2  . THR   B 1 71  ? 47.230 -2.720  9.514   1.00 17.67 ?  71  THR   B CG2  1 
ATOM   4820 H  H    . THR   B 1 71  ? 49.179 -5.895  10.725  1.00 16.49 ?  71  THR   B H    1 
ATOM   4821 H  HA   . THR   B 1 71  ? 48.254 -3.676  11.874  1.00 17.79 ?  71  THR   B HA   1 
ATOM   4822 H  HB   . THR   B 1 71  ? 48.149 -4.519  9.181   1.00 19.88 ?  71  THR   B HB   1 
ATOM   4823 H  HG1  . THR   B 1 71  ? 49.703 -2.953  8.964   1.00 22.15 ?  71  THR   B HG1  1 
ATOM   4824 H  HG21 . THR   B 1 71  ? 47.534 -2.194  8.754   1.00 21.18 ?  71  THR   B HG21 1 
ATOM   4825 H  HG22 . THR   B 1 71  ? 46.373 -3.115  9.297   1.00 21.18 ?  71  THR   B HG22 1 
ATOM   4826 H  HG23 . THR   B 1 71  ? 47.125 -2.128  10.277  1.00 21.18 ?  71  THR   B HG23 1 
ATOM   4827 N  N    . ASN   B 1 72  ? 46.173 -5.955  11.050  1.00 15.07 ?  72  ASN   B N    1 
ATOM   4828 C  CA   . ASN   B 1 72  ? 44.769 -6.310  10.923  1.00 15.73 ?  72  ASN   B CA   1 
ATOM   4829 C  C    . ASN   B 1 72  ? 44.300 -7.411  11.861  1.00 16.25 ?  72  ASN   B C    1 
ATOM   4830 O  O    . ASN   B 1 72  ? 43.086 -7.575  12.024  1.00 17.23 ?  72  ASN   B O    1 
ATOM   4831 C  CB   . ASN   B 1 72  ? 44.471 -6.739  9.480   1.00 16.39 ?  72  ASN   B CB   1 
ATOM   4832 C  CG   . ASN   B 1 72  ? 44.741 -5.638  8.490   1.00 17.37 ?  72  ASN   B CG   1 
ATOM   4833 O  OD1  . ASN   B 1 72  ? 45.756 -5.641  7.791   1.00 18.56 ?  72  ASN   B OD1  1 
ATOM   4834 N  ND2  . ASN   B 1 72  ? 43.849 -4.669  8.443   1.00 19.09 ?  72  ASN   B ND2  1 
ATOM   4835 H  H    . ASN   B 1 72  ? 46.715 -6.596  10.844  1.00 18.05 ?  72  ASN   B H    1 
ATOM   4836 H  HA   . ASN   B 1 72  ? 44.238 -5.524  11.106  1.00 18.85 ?  72  ASN   B HA   1 
ATOM   4837 H  HB2  . ASN   B 1 72  ? 45.036 -7.494  9.247   1.00 19.64 ?  72  ASN   B HB2  1 
ATOM   4838 H  HB3  . ASN   B 1 72  ? 43.538 -6.987  9.408   1.00 19.64 ?  72  ASN   B HB3  1 
ATOM   4839 H  HD21 . ASN   B 1 72  ? 43.949 -4.012  7.894   1.00 22.88 ?  72  ASN   B HD21 1 
ATOM   4840 H  HD22 . ASN   B 1 72  ? 43.150 -4.699  8.947   1.00 22.88 ?  72  ASN   B HD22 1 
ATOM   4841 N  N    . GLY   B 1 73  ? 45.204 -8.162  12.477  1.00 15.70 ?  73  GLY   B N    1 
ATOM   4842 C  CA   . GLY   B 1 73  ? 44.817 -9.304  13.267  1.00 15.19 ?  73  GLY   B CA   1 
ATOM   4843 C  C    . GLY   B 1 73  ? 44.448 -10.484 12.393  1.00 13.83 ?  73  GLY   B C    1 
ATOM   4844 O  O    . GLY   B 1 73  ? 44.430 -10.400 11.162  1.00 13.58 ?  73  GLY   B O    1 
ATOM   4845 H  H    . GLY   B 1 73  ? 46.054 -8.021  12.456  1.00 18.81 ?  73  GLY   B H    1 
ATOM   4846 H  HA2  . GLY   B 1 73  ? 45.549 -9.561  13.851  1.00 18.20 ?  73  GLY   B HA2  1 
ATOM   4847 H  HA3  . GLY   B 1 73  ? 44.050 -9.075  13.820  1.00 18.20 ?  73  GLY   B HA3  1 
ATOM   4848 N  N    . PRO   B 1 74  ? 44.139 -11.608 13.030  1.00 13.84 ?  74  PRO   B N    1 
ATOM   4849 C  CA   . PRO   B 1 74  ? 43.891 -12.841 12.281  1.00 13.50 ?  74  PRO   B CA   1 
ATOM   4850 C  C    . PRO   B 1 74  ? 42.588 -12.786 11.495  1.00 12.80 ?  74  PRO   B C    1 
ATOM   4851 O  O    . PRO   B 1 74  ? 41.646 -12.053 11.820  1.00 13.87 ?  74  PRO   B O    1 
ATOM   4852 C  CB   . PRO   B 1 74  ? 43.822 -13.906 13.381  1.00 14.48 ?  74  PRO   B CB   1 
ATOM   4853 C  CG   . PRO   B 1 74  ? 43.367 -13.161 14.589  1.00 15.66 ?  74  PRO   B CG   1 
ATOM   4854 C  CD   . PRO   B 1 74  ? 44.012 -11.807 14.484  1.00 15.27 ?  74  PRO   B CD   1 
ATOM   4855 H  HA   . PRO   B 1 74  ? 44.636 -13.030 11.681  1.00 16.18 ?  74  PRO   B HA   1 
ATOM   4856 H  HB2  . PRO   B 1 74  ? 43.181 -14.589 13.131  1.00 17.35 ?  74  PRO   B HB2  1 
ATOM   4857 H  HB3  . PRO   B 1 74  ? 44.702 -14.290 13.521  1.00 17.35 ?  74  PRO   B HB3  1 
ATOM   4858 H  HG2  . PRO   B 1 74  ? 42.399 -13.083 14.576  1.00 18.77 ?  74  PRO   B HG2  1 
ATOM   4859 H  HG3  . PRO   B 1 74  ? 43.665 -13.622 15.386  1.00 18.77 ?  74  PRO   B HG3  1 
ATOM   4860 H  HD2  . PRO   B 1 74  ? 43.435 -11.126 14.873  1.00 18.31 ?  74  PRO   B HD2  1 
ATOM   4861 H  HD3  . PRO   B 1 74  ? 44.886 -11.812 14.901  1.00 18.31 ?  74  PRO   B HD3  1 
ATOM   4862 N  N    . LEU   B 1 75  ? 42.551 -13.598 10.444  1.00 11.87 ?  75  LEU   B N    1 
ATOM   4863 C  CA   . LEU   B 1 75  ? 41.337 -13.808 9.679   1.00 12.09 ?  75  LEU   B CA   1 
ATOM   4864 C  C    . LEU   B 1 75  ? 40.369 -14.676 10.480  1.00 12.56 ?  75  LEU   B C    1 
ATOM   4865 O  O    . LEU   B 1 75  ? 40.715 -15.236 11.522  1.00 13.51 ?  75  LEU   B O    1 
ATOM   4866 C  CB   . LEU   B 1 75  ? 41.661 -14.515 8.363   1.00 12.28 ?  75  LEU   B CB   1 
ATOM   4867 C  CG   . LEU   B 1 75  ? 42.512 -13.768 7.331   1.00 14.03 ?  75  LEU   B CG   1 
ATOM   4868 C  CD1  . LEU   B 1 75  ? 42.719 -14.615 6.079   1.00 15.56 ?  75  LEU   B CD1  1 
ATOM   4869 C  CD2  . LEU   B 1 75  ? 41.919 -12.429 6.969   1.00 17.29 ?  75  LEU   B CD2  1 
ATOM   4870 H  H    . LEU   B 1 75  ? 43.226 -14.046 10.153  1.00 14.22 ?  75  LEU   B H    1 
ATOM   4871 H  HA   . LEU   B 1 75  ? 40.914 -12.959 9.487   1.00 14.48 ?  75  LEU   B HA   1 
ATOM   4872 H  HB2  . LEU   B 1 75  ? 42.130 -15.339 8.572   1.00 14.71 ?  75  LEU   B HB2  1 
ATOM   4873 H  HB3  . LEU   B 1 75  ? 40.821 -14.734 7.927   1.00 14.71 ?  75  LEU   B HB3  1 
ATOM   4874 H  HG   . LEU   B 1 75  ? 43.388 -13.608 7.716   1.00 16.82 ?  75  LEU   B HG   1 
ATOM   4875 H  HD11 . LEU   B 1 75  ? 43.266 -14.116 5.447   1.00 18.65 ?  75  LEU   B HD11 1 
ATOM   4876 H  HD12 . LEU   B 1 75  ? 43.171 -15.439 6.321   1.00 18.65 ?  75  LEU   B HD12 1 
ATOM   4877 H  HD13 . LEU   B 1 75  ? 41.858 -14.813 5.682   1.00 18.65 ?  75  LEU   B HD13 1 
ATOM   4878 H  HD21 . LEU   B 1 75  ? 42.453 -12.026 6.269   1.00 20.72 ?  75  LEU   B HD21 1 
ATOM   4879 H  HD22 . LEU   B 1 75  ? 41.009 -12.561 6.662   1.00 20.72 ?  75  LEU   B HD22 1 
ATOM   4880 H  HD23 . LEU   B 1 75  ? 41.923 -11.861 7.757   1.00 20.72 ?  75  LEU   B HD23 1 
ATOM   4881 N  N    . LYS   B 1 76  ? 39.139 -14.776 9.977   1.00 13.59 ?  76  LYS   B N    1 
ATOM   4882 C  CA   . LYS   B 1 76  ? 38.154 -15.738 10.452  1.00 14.98 ?  76  LYS   B CA   1 
ATOM   4883 C  C    . LYS   B 1 76  ? 38.245 -17.008 9.609   1.00 13.55 ?  76  LYS   B C    1 
ATOM   4884 O  O    . LYS   B 1 76  ? 38.517 -16.948 8.410   1.00 13.13 ?  76  LYS   B O    1 
ATOM   4885 C  CB   . LYS   B 1 76  ? 36.736 -15.168 10.274  1.00 17.63 ?  76  LYS   B CB   1 
ATOM   4886 C  CG   . LYS   B 1 76  ? 36.464 -13.776 10.874  1.00 19.87 ?  76  LYS   B CG   1 
ATOM   4887 C  CD   . LYS   B 1 76  ? 35.058 -13.256 10.516  1.00 21.04 ?  76  LYS   B CD   1 
ATOM   4888 C  CE   . LYS   B 1 76  ? 34.791 -11.889 11.129  1.00 23.42 ?  76  LYS   B CE   1 
ATOM   4889 N  NZ   . LYS   B 1 76  ? 33.491 -11.310 10.690  1.00 23.96 ?  76  LYS   B NZ   1 
ATOM   4890 H  H    . LYS   B 1 76  ? 38.847 -14.284 9.337   1.00 16.29 ?  76  LYS   B H    1 
ATOM   4891 H  HA   . LYS   B 1 76  ? 38.304 -15.955 11.387  1.00 17.95 ?  76  LYS   B HA   1 
ATOM   4892 H  HB2  . LYS   B 1 76  ? 36.551 -15.109 9.323   1.00 21.13 ?  76  LYS   B HB2  1 
ATOM   4893 H  HB3  . LYS   B 1 76  ? 36.107 -15.782 10.684  1.00 21.13 ?  76  LYS   B HB3  1 
ATOM   4894 H  HG2  . LYS   B 1 76  ? 36.532 -13.828 11.840  1.00 23.82 ?  76  LYS   B HG2  1 
ATOM   4895 H  HG3  . LYS   B 1 76  ? 37.118 -13.147 10.527  1.00 23.82 ?  76  LYS   B HG3  1 
ATOM   4896 H  HD2  . LYS   B 1 76  ? 34.984 -13.176 9.551   1.00 25.23 ?  76  LYS   B HD2  1 
ATOM   4897 H  HD3  . LYS   B 1 76  ? 34.393 -13.876 10.853  1.00 25.23 ?  76  LYS   B HD3  1 
ATOM   4898 H  HE2  . LYS   B 1 76  ? 34.773 -11.974 12.095  1.00 28.08 ?  76  LYS   B HE2  1 
ATOM   4899 H  HE3  . LYS   B 1 76  ? 35.498 -11.279 10.863  1.00 28.08 ?  76  LYS   B HE3  1 
ATOM   4900 H  HZ1  . LYS   B 1 76  ? 33.368 -10.512 11.068  1.00 28.72 ?  76  LYS   B HZ1  1 
ATOM   4901 H  HZ2  . LYS   B 1 76  ? 33.482 -11.213 9.805   1.00 28.72 ?  76  LYS   B HZ2  1 
ATOM   4902 H  HZ3  . LYS   B 1 76  ? 32.821 -11.847 10.928  1.00 28.72 ?  76  LYS   B HZ3  1 
ATOM   4903 N  N    . VAL   B 1 77  ? 37.994 -18.164 10.234  1.00 13.90 ?  77  VAL   B N    1 
ATOM   4904 C  CA   . VAL   B 1 77  ? 37.786 -19.374 9.447   1.00 13.83 ?  77  VAL   B CA   1 
ATOM   4905 C  C    . VAL   B 1 77  ? 36.594 -19.140 8.531   1.00 12.95 ?  77  VAL   B C    1 
ATOM   4906 O  O    . VAL   B 1 77  ? 35.530 -18.690 8.977   1.00 13.08 ?  77  VAL   B O    1 
ATOM   4907 C  CB   . VAL   B 1 77  ? 37.591 -20.601 10.350  1.00 15.01 ?  77  VAL   B CB   1 
ATOM   4908 C  CG1  . VAL   B 1 77  ? 37.307 -21.827 9.495   1.00 15.96 ?  77  VAL   B CG1  1 
ATOM   4909 C  CG2  . VAL   B 1 77  ? 38.824 -20.831 11.216  1.00 16.64 ?  77  VAL   B CG2  1 
ATOM   4910 H  H    . VAL   B 1 77  ? 37.935 -18.266 11.083  1.00 16.66 ?  77  VAL   B H    1 
ATOM   4911 H  HA   . VAL   B 1 77  ? 38.561 -19.527 8.889   1.00 16.57 ?  77  VAL   B HA   1 
ATOM   4912 H  HB   . VAL   B 1 77  ? 36.828 -20.450 10.932  1.00 17.99 ?  77  VAL   B HB   1 
ATOM   4913 H  HG11 . VAL   B 1 77  ? 37.382 -22.618 10.051  1.00 19.13 ?  77  VAL   B HG11 1 
ATOM   4914 H  HG12 . VAL   B 1 77  ? 36.404 -21.764 9.137   1.00 19.13 ?  77  VAL   B HG12 1 
ATOM   4915 H  HG13 . VAL   B 1 77  ? 37.948 -21.864 8.773   1.00 19.13 ?  77  VAL   B HG13 1 
ATOM   4916 H  HG21 . VAL   B 1 77  ? 38.685 -21.627 11.748  1.00 19.95 ?  77  VAL   B HG21 1 
ATOM   4917 H  HG22 . VAL   B 1 77  ? 39.593 -20.943 10.639  1.00 19.95 ?  77  VAL   B HG22 1 
ATOM   4918 H  HG23 . VAL   B 1 77  ? 38.948 -20.061 11.793  1.00 19.95 ?  77  VAL   B HG23 1 
ATOM   4919 N  N    . GLY   B 1 78  ? 36.778 -19.416 7.240   1.00 12.37 ?  78  GLY   B N    1 
ATOM   4920 C  CA   . GLY   B 1 78  ? 35.807 -19.093 6.221   1.00 12.00 ?  78  GLY   B CA   1 
ATOM   4921 C  C    . GLY   B 1 78  ? 36.044 -17.772 5.531   1.00 11.46 ?  78  GLY   B C    1 
ATOM   4922 O  O    . GLY   B 1 78  ? 35.360 -17.479 4.548   1.00 11.91 ?  78  GLY   B O    1 
ATOM   4923 H  H    . GLY   B 1 78  ? 37.480 -19.800 6.928   1.00 14.82 ?  78  GLY   B H    1 
ATOM   4924 H  HA2  . GLY   B 1 78  ? 35.811 -19.786 5.544   1.00 14.38 ?  78  GLY   B HA2  1 
ATOM   4925 H  HA3  . GLY   B 1 78  ? 34.923 -19.063 6.619   1.00 14.38 ?  78  GLY   B HA3  1 
ATOM   4926 N  N    . GLY   B 1 79  ? 36.997 -16.972 6.014   1.00 11.37 ?  79  GLY   B N    1 
ATOM   4927 C  CA   . GLY   B 1 79  ? 37.292 -15.673 5.448   1.00 11.15 ?  79  GLY   B CA   1 
ATOM   4928 C  C    . GLY   B 1 79  ? 38.527 -15.686 4.559   1.00 10.83 ?  79  GLY   B C    1 
ATOM   4929 O  O    . GLY   B 1 79  ? 39.143 -16.718 4.303   1.00 11.31 ?  79  GLY   B O    1 
ATOM   4930 H  H    . GLY   B 1 79  ? 37.499 -17.170 6.679   1.00 13.62 ?  79  GLY   B H    1 
ATOM   4931 H  HA2  . GLY   B 1 79  ? 36.537 -15.366 4.917   1.00 13.36 ?  79  GLY   B HA2  1 
ATOM   4932 H  HA3  . GLY   B 1 79  ? 37.439 -15.031 6.162   1.00 13.36 ?  79  GLY   B HA3  1 
ATOM   4933 N  N    . SER   B 1 80  ? 38.886 -14.490 4.085   1.00 10.92 ?  80  SER   B N    1 
ATOM   4934 C  CA   . SER   B 1 80  ? 39.993 -14.359 3.150   1.00 10.80 ?  80  SER   B CA   1 
ATOM   4935 C  C    . SER   B 1 80  ? 40.569 -12.950 3.206   1.00 10.65 ?  80  SER   B C    1 
ATOM   4936 O  O    . SER   B 1 80  ? 39.954 -12.017 3.729   1.00 11.72 ?  80  SER   B O    1 
ATOM   4937 C  CB   . SER   B 1 80  ? 39.550 -14.649 1.711   1.00 11.02 ?  80  SER   B CB   1 
ATOM   4938 O  OG   . SER   B 1 80  ? 38.714 -13.626 1.203   1.00 12.15 ?  80  SER   B OG   1 
ATOM   4939 H  H    . SER   B 1 80  ? 38.510 -13.748 4.290   1.00 13.08 ?  80  SER   B H    1 
ATOM   4940 H  HA   . SER   B 1 80  ? 40.687 -14.988 3.394   1.00 12.94 ?  80  SER   B HA   1 
ATOM   4941 H  HB2  . SER   B 1 80  ? 40.331 -14.718 1.143   1.00 13.20 ?  80  SER   B HB2  1 
ATOM   4942 H  HB3  . SER   B 1 80  ? 39.057 -15.486 1.697   1.00 13.20 ?  80  SER   B HB3  1 
ATOM   4943 H  HG   . SER   B 1 80  ? 38.024 -13.553 1.687   1.00 14.56 ?  80  SER   B HG   1 
ATOM   4944 N  N    . CYS   B 1 81  ? 41.755 -12.805 2.621   1.00 10.41 ?  81  CYS   B N    1 
ATOM   4945 C  CA   . CYS   B 1 81  ? 42.304 -11.492 2.313   1.00 10.68 ?  81  CYS   B CA   1 
ATOM   4946 C  C    . CYS   B 1 81  ? 43.082 -11.571 1.009   1.00 10.05 ?  81  CYS   B C    1 
ATOM   4947 O  O    . CYS   B 1 81  ? 43.592 -12.631 0.631   1.00 11.00 ?  81  CYS   B O    1 
ATOM   4948 C  CB   . CYS   B 1 81  ? 43.192 -10.940 3.436   1.00 11.45 ?  81  CYS   B CB   1 
ATOM   4949 S  SG   . CYS   B 1 81  ? 44.719 -11.874 3.685   1.00 11.91 ?  81  CYS   B SG   1 
ATOM   4950 H  H    . CYS   B 1 81  ? 42.266 -13.459 2.380   1.00 12.47 ?  81  CYS   B H    1 
ATOM   4951 H  HA   . CYS   B 1 81  ? 41.571 -10.869 2.185   1.00 12.80 ?  81  CYS   B HA   1 
ATOM   4952 H  HB2  . CYS   B 1 81  ? 43.437 -10.027 3.223   1.00 13.71 ?  81  CYS   B HB2  1 
ATOM   4953 H  HB3  . CYS   B 1 81  ? 42.689 -10.958 4.268   1.00 13.71 ?  81  CYS   B HB3  1 
ATOM   4954 H  HG   . CYS   B 1 81  ? 45.339 -11.374 4.587   1.00 14.27 ?  81  CYS   B HG   1 
ATOM   4955 N  N    . VAL   B 1 82  ? 43.176 -10.429 0.332   1.00 10.53 ?  82  VAL   B N    1 
ATOM   4956 C  CA   . VAL   B 1 82  ? 43.939 -10.301 -0.907  1.00 10.64 ?  82  VAL   B CA   1 
ATOM   4957 C  C    . VAL   B 1 82  ? 45.279 -9.660  -0.589  1.00 10.85 ?  82  VAL   B C    1 
ATOM   4958 O  O    . VAL   B 1 82  ? 45.330 -8.541  -0.057  1.00 11.85 ?  82  VAL   B O    1 
ATOM   4959 C  CB   . VAL   B 1 82  ? 43.193 -9.458  -1.951  1.00 11.82 ?  82  VAL   B CB   1 
ATOM   4960 C  CG1  . VAL   B 1 82  ? 44.040 -9.312  -3.210  1.00 13.04 ?  82  VAL   B CG1  1 
ATOM   4961 C  CG2  . VAL   B 1 82  ? 41.841 -10.069 -2.269  1.00 12.80 ?  82  VAL   B CG2  1 
ATOM   4962 H  H    . VAL   B 1 82  ? 42.796 -9.691  0.573   1.00 12.61 ?  82  VAL   B H    1 
ATOM   4963 H  HA   . VAL   B 1 82  ? 44.097 -11.181 -1.282  1.00 12.74 ?  82  VAL   B HA   1 
ATOM   4964 H  HB   . VAL   B 1 82  ? 43.039 -8.571  -1.592  1.00 14.16 ?  82  VAL   B HB   1 
ATOM   4965 H  HG11 . VAL   B 1 82  ? 43.479 -9.004  -3.938  1.00 15.62 ?  82  VAL   B HG11 1 
ATOM   4966 H  HG12 . VAL   B 1 82  ? 44.748 -8.665  -3.045  1.00 15.62 ?  82  VAL   B HG12 1 
ATOM   4967 H  HG13 . VAL   B 1 82  ? 44.427 -10.173 -3.434  1.00 15.62 ?  82  VAL   B HG13 1 
ATOM   4968 H  HG21 . VAL   B 1 82  ? 41.404 -9.543  -2.960  1.00 15.34 ?  82  VAL   B HG21 1 
ATOM   4969 H  HG22 . VAL   B 1 82  ? 41.967 -10.980 -2.585  1.00 15.34 ?  82  VAL   B HG22 1 
ATOM   4970 H  HG23 . VAL   B 1 82  ? 41.294 -10.074 -1.467  1.00 15.34 ?  82  VAL   B HG23 1 
ATOM   4971 N  N    . LEU   B 1 83  ? 46.359 -10.345 -0.951  1.00 10.54 ?  83  LEU   B N    1 
ATOM   4972 C  CA   . LEU   B 1 83  ? 47.713 -9.828  -0.832  1.00 10.63 ?  83  LEU   B CA   1 
ATOM   4973 C  C    . LEU   B 1 83  ? 48.414 -9.965  -2.183  1.00 10.55 ?  83  LEU   B C    1 
ATOM   4974 O  O    . LEU   B 1 83  ? 47.813 -10.382 -3.177  1.00 10.51 ?  83  LEU   B O    1 
ATOM   4975 C  CB   . LEU   B 1 83  ? 48.465 -10.498 0.326   1.00 11.14 ?  83  LEU   B CB   1 
ATOM   4976 C  CG   . LEU   B 1 83  ? 47.944 -10.141 1.724   1.00 12.41 ?  83  LEU   B CG   1 
ATOM   4977 C  CD1  . LEU   B 1 83  ? 48.584 -11.010 2.794   1.00 12.96 ?  83  LEU   B CD1  1 
ATOM   4978 C  CD2  . LEU   B 1 83  ? 48.146 -8.664  2.050   1.00 13.32 ?  83  LEU   B CD2  1 
ATOM   4979 H  H    . LEU   B 1 83  ? 46.326 -11.145 -1.275  1.00 12.62 ?  83  LEU   B H    1 
ATOM   4980 H  HA   . LEU   B 1 83  ? 47.656 -8.881  -0.636  1.00 12.73 ?  83  LEU   B HA   1 
ATOM   4981 H  HB2  . LEU   B 1 83  ? 48.400 -11.456 0.225   1.00 13.34 ?  83  LEU   B HB2  1 
ATOM   4982 H  HB3  . LEU   B 1 83  ? 49.395 -10.224 0.284   1.00 13.34 ?  83  LEU   B HB3  1 
ATOM   4983 H  HG   . LEU   B 1 83  ? 46.990 -10.310 1.744   1.00 14.86 ?  83  LEU   B HG   1 
ATOM   4984 H  HD11 . LEU   B 1 83  ? 48.223 -10.762 3.661   1.00 15.52 ?  83  LEU   B HD11 1 
ATOM   4985 H  HD12 . LEU   B 1 83  ? 48.377 -11.941 2.607   1.00 15.52 ?  83  LEU   B HD12 1 
ATOM   4986 H  HD13 . LEU   B 1 83  ? 49.542 -10.876 2.783   1.00 15.52 ?  83  LEU   B HD13 1 
ATOM   4987 H  HD21 . LEU   B 1 83  ? 47.928 -8.516  2.984   1.00 15.96 ?  83  LEU   B HD21 1 
ATOM   4988 H  HD22 . LEU   B 1 83  ? 49.070 -8.427  1.883   1.00 15.96 ?  83  LEU   B HD22 1 
ATOM   4989 H  HD23 . LEU   B 1 83  ? 47.560 -8.133  1.487   1.00 15.96 ?  83  LEU   B HD23 1 
ATOM   4990 N  N    . SER   B 1 84  ? 49.691 -9.593  -2.233  1.00 11.45 ?  84  SER   B N    1 
ATOM   4991 C  CA   . SER   B 1 84  ? 50.426 -9.705  -3.483  1.00 11.53 ?  84  SER   B CA   1 
ATOM   4992 C  C    . SER   B 1 84  ? 50.580 -11.164 -3.902  1.00 10.99 ?  84  SER   B C    1 
ATOM   4993 O  O    . SER   B 1 84  ? 50.691 -12.065 -3.073  1.00 10.81 ?  84  SER   B O    1 
ATOM   4994 C  CB   . SER   B 1 84  ? 51.821 -9.108  -3.331  1.00 13.27 ?  84  SER   B CB   1 
ATOM   4995 O  OG   . SER   B 1 84  ? 52.567 -9.309  -4.516  1.00 14.87 ?  84  SER   B OG   1 
ATOM   4996 H  H    . SER   B 1 84  ? 50.140 -9.276  -1.571  1.00 13.71 ?  84  SER   B H    1 
ATOM   4997 H  HA   . SER   B 1 84  ? 49.957 -9.228  -4.184  1.00 13.82 ?  84  SER   B HA   1 
ATOM   4998 H  HB2  . SER   B 1 84  ? 51.742 -8.152  -3.159  1.00 15.90 ?  84  SER   B HB2  1 
ATOM   4999 H  HB3  . SER   B 1 84  ? 52.278 -9.539  -2.595  1.00 15.90 ?  84  SER   B HB3  1 
ATOM   5000 H  HG   . SER   B 1 84  ? 53.337 -8.967  -4.437  1.00 17.82 ?  84  SER   B HG   1 
ATOM   5001 N  N    . GLY   B 1 85  ? 50.636 -11.382 -5.211  1.00 12.12 ?  85  GLY   B N    1 
ATOM   5002 C  CA   . GLY   B 1 85  ? 50.989 -12.671 -5.758  1.00 12.65 ?  85  GLY   B CA   1 
ATOM   5003 C  C    . GLY   B 1 85  ? 52.461 -12.862 -6.057  1.00 11.91 ?  85  GLY   B C    1 
ATOM   5004 O  O    . GLY   B 1 85  ? 52.841 -13.940 -6.517  1.00 12.17 ?  85  GLY   B O    1 
ATOM   5005 H  H    . GLY   B 1 85  ? 50.479 -10.788 -5.806  1.00 14.51 ?  85  GLY   B H    1 
ATOM   5006 H  HA2  . GLY   B 1 85  ? 50.722 -13.363 -5.130  1.00 15.15 ?  85  GLY   B HA2  1 
ATOM   5007 H  HA3  . GLY   B 1 85  ? 50.500 -12.809 -6.579  1.00 15.15 ?  85  GLY   B HA3  1 
ATOM   5008 N  N    . HIS   B 1 86  ? 53.312 -11.863 -5.827  1.00 11.89 ?  86  HIS   B N    1 
ATOM   5009 C  CA   . HIS   B 1 86  ? 54.775 -12.032 -5.910  1.00 11.90 ?  86  HIS   B CA   1 
ATOM   5010 C  C    . HIS   B 1 86  ? 55.146 -12.539 -7.301  1.00 12.12 ?  86  HIS   B C    1 
ATOM   5011 O  O    . HIS   B 1 86  ? 54.756 -11.918 -8.303  1.00 12.82 ?  86  HIS   B O    1 
ATOM   5012 C  CB   . HIS   B 1 86  ? 55.262 -12.880 -4.741  1.00 12.38 ?  86  HIS   B CB   1 
ATOM   5013 C  CG   . HIS   B 1 86  ? 54.950 -12.278 -3.413  1.00 12.48 ?  86  HIS   B CG   1 
ATOM   5014 N  ND1  . HIS   B 1 86  ? 55.777 -11.363 -2.796  1.00 13.86 ?  86  HIS   B ND1  1 
ATOM   5015 C  CD2  . HIS   B 1 86  ? 53.878 -12.432 -2.602  1.00 12.74 ?  86  HIS   B CD2  1 
ATOM   5016 C  CE1  . HIS   B 1 86  ? 55.223 -10.983 -1.659  1.00 13.74 ?  86  HIS   B CE1  1 
ATOM   5017 N  NE2  . HIS   B 1 86  ? 54.071 -11.614 -1.518  1.00 13.03 ?  86  HIS   B NE2  1 
ATOM   5018 H  H    . HIS   B 1 86  ? 53.074 -11.067 -5.621  1.00 14.25 ?  86  HIS   B H    1 
ATOM   5019 H  HA   . HIS   B 1 86  ? 55.186 -11.162 -5.813  1.00 14.25 ?  86  HIS   B HA   1 
ATOM   5020 H  HB2  . HIS   B 1 86  ? 54.846 -13.754 -4.783  1.00 14.83 ?  86  HIS   B HB2  1 
ATOM   5021 H  HB3  . HIS   B 1 86  ? 56.231 -12.977 -4.801  1.00 14.83 ?  86  HIS   B HB3  1 
ATOM   5022 H  HD2  . HIS   B 1 86  ? 53.139 -12.982 -2.757  1.00 15.26 ?  86  HIS   B HD2  1 
ATOM   5023 H  HE1  . HIS   B 1 86  ? 55.590 -10.385 -1.049  1.00 16.46 ?  86  HIS   B HE1  1 
ATOM   5024 H  HE2  . HIS   B 1 86  ? 53.533 -11.538 -0.849  1.00 15.61 ?  86  HIS   B HE2  1 
ATOM   5025 N  N    . ASN   B 1 87  ? 55.910 -13.625 -7.413  1.00 12.43 ?  87  ASN   B N    1 
ATOM   5026 C  CA   . ASN   B 1 87  ? 56.301 -14.196 -8.692  1.00 12.95 ?  87  ASN   B CA   1 
ATOM   5027 C  C    . ASN   B 1 87  ? 55.320 -15.240 -9.192  1.00 12.87 ?  87  ASN   B C    1 
ATOM   5028 O  O    . ASN   B 1 87  ? 55.636 -15.954 -10.151 1.00 14.60 ?  87  ASN   B O    1 
ATOM   5029 C  CB   . ASN   B 1 87  ? 57.695 -14.828 -8.583  1.00 14.65 ?  87  ASN   B CB   1 
ATOM   5030 C  CG   . ASN   B 1 87  ? 57.755 -15.940 -7.544  1.00 15.69 ?  87  ASN   B CG   1 
ATOM   5031 O  OD1  . ASN   B 1 87  ? 57.114 -15.861 -6.491  1.00 14.95 ?  87  ASN   B OD1  1 
ATOM   5032 N  ND2  . ASN   B 1 87  ? 58.503 -17.002 -7.852  1.00 18.16 ?  87  ASN   B ND2  1 
ATOM   5033 H  H    . ASN   B 1 87  ? 56.216 -14.066 -6.742  1.00 14.89 ?  87  ASN   B H    1 
ATOM   5034 H  HA   . ASN   B 1 87  ? 56.345 -13.488 -9.352  1.00 15.52 ?  87  ASN   B HA   1 
ATOM   5035 H  HB2  . ASN   B 1 87  ? 57.940 -15.205 -9.445  1.00 17.55 ?  87  ASN   B HB2  1 
ATOM   5036 H  HB3  . ASN   B 1 87  ? 58.331 -14.146 -8.327  1.00 17.55 ?  87  ASN   B HB3  1 
ATOM   5037 H  HD21 . ASN   B 1 87  ? 58.570 -17.656 -7.300  1.00 21.76 ?  87  ASN   B HD21 1 
ATOM   5038 H  HD22 . ASN   B 1 87  ? 58.932 -17.025 -8.600  1.00 21.76 ?  87  ASN   B HD22 1 
ATOM   5039 N  N    . LEU   B 1 88  ? 54.145 -15.335 -8.575  1.00 11.86 ?  88  LEU   B N    1 
ATOM   5040 C  CA   . LEU   B 1 88  ? 53.170 -16.368 -8.895  1.00 12.12 ?  88  LEU   B CA   1 
ATOM   5041 C  C    . LEU   B 1 88  ? 51.933 -15.856 -9.612  1.00 11.69 ?  88  LEU   B C    1 
ATOM   5042 O  O    . LEU   B 1 88  ? 51.331 -16.605 -10.391 1.00 13.41 ?  88  LEU   B O    1 
ATOM   5043 C  CB   . LEU   B 1 88  ? 52.706 -17.054 -7.606  1.00 13.11 ?  88  LEU   B CB   1 
ATOM   5044 C  CG   . LEU   B 1 88  ? 53.824 -17.715 -6.809  1.00 15.35 ?  88  LEU   B CG   1 
ATOM   5045 C  CD1  . LEU   B 1 88  ? 53.328 -18.066 -5.414  1.00 16.93 ?  88  LEU   B CD1  1 
ATOM   5046 C  CD2  . LEU   B 1 88  ? 54.305 -18.952 -7.538  1.00 18.52 ?  88  LEU   B CD2  1 
ATOM   5047 H  H    . LEU   B 1 88  ? 53.886 -14.805 -7.944  1.00 14.20 ?  88  LEU   B H    1 
ATOM   5048 H  HA   . LEU   B 1 88  ? 53.585 -17.036 -9.454  1.00 14.52 ?  88  LEU   B HA   1 
ATOM   5049 H  HB2  . LEU   B 1 88  ? 52.287 -16.395 -7.029  1.00 15.71 ?  88  LEU   B HB2  1 
ATOM   5050 H  HB3  . LEU   B 1 88  ? 52.061 -17.744 -7.832  1.00 15.71 ?  88  LEU   B HB3  1 
ATOM   5051 H  HG   . LEU   B 1 88  ? 54.569 -17.099 -6.723  1.00 18.40 ?  88  LEU   B HG   1 
ATOM   5052 H  HD11 . LEU   B 1 88  ? 53.970 -18.655 -4.989  1.00 20.29 ?  88  LEU   B HD11 1 
ATOM   5053 H  HD12 . LEU   B 1 88  ? 53.235 -17.249 -4.898  1.00 20.29 ?  88  LEU   B HD12 1 
ATOM   5054 H  HD13 . LEU   B 1 88  ? 52.470 -18.509 -5.490  1.00 20.29 ?  88  LEU   B HD13 1 
ATOM   5055 H  HD21 . LEU   B 1 88  ? 54.960 -19.407 -6.987  1.00 22.20 ?  88  LEU   B HD21 1 
ATOM   5056 H  HD22 . LEU   B 1 88  ? 53.548 -19.535 -7.703  1.00 22.20 ?  88  LEU   B HD22 1 
ATOM   5057 H  HD23 . LEU   B 1 88  ? 54.708 -18.685 -8.379  1.00 22.20 ?  88  LEU   B HD23 1 
ATOM   5058 N  N    . ALA   B 1 89  ? 51.529 -14.620 -9.350  1.00 11.10 ?  89  ALA   B N    1 
ATOM   5059 C  CA   . ALA   B 1 89  ? 50.236 -14.130 -9.800  1.00 10.72 ?  89  ALA   B CA   1 
ATOM   5060 C  C    . ALA   B 1 89  ? 50.209 -12.639 -9.521  1.00 11.15 ?  89  ALA   B C    1 
ATOM   5061 O  O    . ALA   B 1 89  ? 51.046 -12.122 -8.783  1.00 12.01 ?  89  ALA   B O    1 
ATOM   5062 C  CB   . ALA   B 1 89  ? 49.099 -14.813 -9.049  1.00 11.44 ?  89  ALA   B CB   1 
ATOM   5063 H  H    . ALA   B 1 89  ? 51.980 -14.041 -8.898  1.00 13.29 ?  89  ALA   B H    1 
ATOM   5064 H  HA   . ALA   B 1 89  ? 50.130 -14.280 -10.754 1.00 12.83 ?  89  ALA   B HA   1 
ATOM   5065 H  HB1  . ALA   B 1 89  ? 48.250 -14.488 -9.396  1.00 13.71 ?  89  ALA   B HB1  1 
ATOM   5066 H  HB2  . ALA   B 1 89  ? 49.162 -15.774 -9.191  1.00 13.71 ?  89  ALA   B HB2  1 
ATOM   5067 H  HB3  . ALA   B 1 89  ? 49.174 -14.612 -8.109  1.00 13.71 ?  89  ALA   B HB3  1 
ATOM   5068 N  N    . LYS   B 1 90  ? 49.212 -11.950 -10.075 1.00 11.94 ?  90  LYS   B N    1 
ATOM   5069 C  CA   . LYS   B 1 90  ? 49.016 -10.565 -9.670  1.00 12.15 ?  90  LYS   B CA   1 
ATOM   5070 C  C    . LYS   B 1 90  ? 48.700 -10.491 -8.181  1.00 12.10 ?  90  LYS   B C    1 
ATOM   5071 O  O    . LYS   B 1 90  ? 49.337 -9.737  -7.429  1.00 13.19 ?  90  LYS   B O    1 
ATOM   5072 C  CB   . LYS   B 1 90  ? 47.930 -9.908  -10.522 1.00 13.93 ?  90  LYS   B CB   1 
ATOM   5073 C  CG   . LYS   B 1 90  ? 47.638 -8.467  -10.145 1.00 14.42 ?  90  LYS   B CG   1 
ATOM   5074 C  CD   . LYS   B 1 90  ? 48.847 -7.570  -10.247 1.00 17.37 ?  90  LYS   B CD   1 
ATOM   5075 C  CE   . LYS   B 1 90  ? 48.416 -6.143  -10.012 1.00 19.51 ?  90  LYS   B CE   1 
ATOM   5076 N  NZ   . LYS   B 1 90  ? 49.570 -5.227  -9.892  1.00 19.86 ?  90  LYS   B NZ   1 
ATOM   5077 H  H    . LYS   B 1 90  ? 48.653 -12.255 -10.656 1.00 14.31 ?  90  LYS   B H    1 
ATOM   5078 H  HA   . LYS   B 1 90  ? 49.841 -10.085 -9.819  1.00 14.56 ?  90  LYS   B HA   1 
ATOM   5079 H  HB2  . LYS   B 1 90  ? 48.215 -9.920  -11.451 1.00 16.69 ?  90  LYS   B HB2  1 
ATOM   5080 H  HB3  . LYS   B 1 90  ? 47.108 -10.416 -10.429 1.00 16.69 ?  90  LYS   B HB3  1 
ATOM   5081 H  HG2  . LYS   B 1 90  ? 46.956 -8.120  -10.743 1.00 17.28 ?  90  LYS   B HG2  1 
ATOM   5082 H  HG3  . LYS   B 1 90  ? 47.314 -8.438  -9.229  1.00 17.28 ?  90  LYS   B HG3  1 
ATOM   5083 H  HD2  . LYS   B 1 90  ? 49.495 -7.816  -9.567  1.00 20.82 ?  90  LYS   B HD2  1 
ATOM   5084 H  HD3  . LYS   B 1 90  ? 49.234 -7.642  -11.133 1.00 20.82 ?  90  LYS   B HD3  1 
ATOM   5085 H  HE2  . LYS   B 1 90  ? 47.874 -5.844  -10.761 1.00 23.38 ?  90  LYS   B HE2  1 
ATOM   5086 H  HE3  . LYS   B 1 90  ? 47.905 -6.090  -9.190  1.00 23.38 ?  90  LYS   B HE3  1 
ATOM   5087 H  HZ1  . LYS   B 1 90  ? 49.288 -4.392  -9.757  1.00 23.81 ?  90  LYS   B HZ1  1 
ATOM   5088 H  HZ2  . LYS   B 1 90  ? 50.085 -5.470  -9.208  1.00 23.81 ?  90  LYS   B HZ2  1 
ATOM   5089 H  HZ3  . LYS   B 1 90  ? 50.056 -5.246  -10.640 1.00 23.81 ?  90  LYS   B HZ3  1 
ATOM   5090 N  N    . HIS   B 1 91  ? 47.746 -11.309 -7.734  1.00 10.60 ?  91  HIS   B N    1 
ATOM   5091 C  CA   . HIS   B 1 91  ? 47.284 -11.333 -6.360  1.00 10.70 ?  91  HIS   B CA   1 
ATOM   5092 C  C    . HIS   B 1 91  ? 47.286 -12.760 -5.847  1.00 10.00 ?  91  HIS   B C    1 
ATOM   5093 O  O    . HIS   B 1 91  ? 47.052 -13.712 -6.600  1.00 10.54 ?  91  HIS   B O    1 
ATOM   5094 C  CB   . HIS   B 1 91  ? 45.835 -10.856 -6.246  1.00 12.01 ?  91  HIS   B CB   1 
ATOM   5095 C  CG   . HIS   B 1 91  ? 45.620 -9.451  -6.683  1.00 15.63 ?  91  HIS   B CG   1 
ATOM   5096 N  ND1  . HIS   B 1 91  ? 46.212 -8.375  -6.057  1.00 18.47 ?  91  HIS   B ND1  1 
ATOM   5097 C  CD2  . HIS   B 1 91  ? 44.847 -8.938  -7.665  1.00 18.07 ?  91  HIS   B CD2  1 
ATOM   5098 C  CE1  . HIS   B 1 91  ? 45.829 -7.257  -6.648  1.00 19.33 ?  91  HIS   B CE1  1 
ATOM   5099 N  NE2  . HIS   B 1 91  ? 44.994 -7.572  -7.623  1.00 19.46 ?  91  HIS   B NE2  1 
ATOM   5100 H  H    . HIS   B 1 91  ? 47.335 -11.880 -8.233  1.00 12.69 ?  91  HIS   B H    1 
ATOM   5101 H  HA   . HIS   B 1 91  ? 47.854 -10.778 -5.799  1.00 12.81 ?  91  HIS   B HA   1 
ATOM   5102 H  HB2  . HIS   B 1 91  ? 45.275 -11.423 -6.797  1.00 14.39 ?  91  HIS   B HB2  1 
ATOM   5103 H  HB3  . HIS   B 1 91  ? 45.556 -10.921 -5.318  1.00 14.39 ?  91  HIS   B HB3  1 
ATOM   5104 H  HD1  . HIS   B 1 91  ? 46.753 -8.423  -5.388  1.00 22.14 ?  91  HIS   B HD1  1 
ATOM   5105 H  HD2  . HIS   B 1 91  ? 44.321 -9.407  -8.265  1.00 21.66 ?  91  HIS   B HD2  1 
ATOM   5106 H  HE1  . HIS   B 1 91  ? 46.098 -6.394  -6.409  1.00 23.18 ?  91  HIS   B HE1  1 
ATOM   5107 N  N    . CYS   B 1 92  ? 47.486 -12.891 -4.543  1.00 9.72  ?  92  CYS   B N    1 
ATOM   5108 C  CA   . CYS   B 1 92  ? 47.184 -14.125 -3.831  1.00 9.72  ?  92  CYS   B CA   1 
ATOM   5109 C  C    . CYS   B 1 92  ? 45.966 -13.893 -2.949  1.00 9.17  ?  92  CYS   B C    1 
ATOM   5110 O  O    . CYS   B 1 92  ? 45.971 -12.997 -2.094  1.00 10.28 ?  92  CYS   B O    1 
ATOM   5111 C  CB   . CYS   B 1 92  ? 48.363 -14.583 -2.980  1.00 10.12 ?  92  CYS   B CB   1 
ATOM   5112 S  SG   . CYS   B 1 92  ? 48.012 -16.119 -2.091  1.00 10.39 ?  92  CYS   B SG   1 
ATOM   5113 H  H    . CYS   B 1 92  ? 47.817 -12.273 -4.036  1.00 11.64 ?  92  CYS   B H    1 
ATOM   5114 H  HA   . CYS   B 1 92  ? 46.985 -14.824 -4.474  1.00 11.64 ?  92  CYS   B HA   1 
ATOM   5115 H  HB2  . CYS   B 1 92  ? 49.130 -14.730 -3.549  1.00 12.12 ?  92  CYS   B HB2  1 
ATOM   5116 H  HB3  . CYS   B 1 92  ? 48.559 -13.896 -2.322  1.00 12.12 ?  92  CYS   B HB3  1 
ATOM   5117 H  HG   . CYS   B 1 92  ? 48.985 -16.434 -1.464  1.00 12.44 ?  92  CYS   B HG   1 
ATOM   5118 N  N    . LEU   B 1 93  ? 44.929 -14.697 -3.165  1.00 9.37  ?  93  LEU   B N    1 
ATOM   5119 C  CA   . LEU   B 1 93  ? 43.758 -14.719 -2.302  1.00 9.52  ?  93  LEU   B CA   1 
ATOM   5120 C  C    . LEU   B 1 93  ? 43.980 -15.784 -1.237  1.00 8.99  ?  93  LEU   B C    1 
ATOM   5121 O  O    . LEU   B 1 93  ? 43.936 -16.984 -1.532  1.00 9.64  ?  93  LEU   B O    1 
ATOM   5122 C  CB   . LEU   B 1 93  ? 42.494 -15.001 -3.110  1.00 9.63  ?  93  LEU   B CB   1 
ATOM   5123 C  CG   . LEU   B 1 93  ? 41.199 -15.030 -2.300  1.00 10.30 ?  93  LEU   B CG   1 
ATOM   5124 C  CD1  . LEU   B 1 93  ? 40.845 -13.645 -1.792  1.00 10.85 ?  93  LEU   B CD1  1 
ATOM   5125 C  CD2  . LEU   B 1 93  ? 40.075 -15.622 -3.139  1.00 10.84 ?  93  LEU   B CD2  1 
ATOM   5126 H  H    . LEU   B 1 93  ? 44.887 -15.264 -3.823  1.00 11.23 ?  93  LEU   B H    1 
ATOM   5127 H  HA   . LEU   B 1 93  ? 43.667 -13.860 -1.869  1.00 11.41 ?  93  LEU   B HA   1 
ATOM   5128 H  HB2  . LEU   B 1 93  ? 42.399 -14.306 -3.783  1.00 11.53 ?  93  LEU   B HB2  1 
ATOM   5129 H  HB3  . LEU   B 1 93  ? 42.587 -15.861 -3.542  1.00 11.53 ?  93  LEU   B HB3  1 
ATOM   5130 H  HG   . LEU   B 1 93  ? 41.323 -15.602 -1.530  1.00 12.34 ?  93  LEU   B HG   1 
ATOM   5131 H  HD11 . LEU   B 1 93  ? 39.994 -13.685 -1.334  1.00 13.00 ?  93  LEU   B HD11 1 
ATOM   5132 H  HD12 . LEU   B 1 93  ? 41.538 -13.347 -1.181  1.00 13.00 ?  93  LEU   B HD12 1 
ATOM   5133 H  HD13 . LEU   B 1 93  ? 40.788 -13.037 -2.547  1.00 13.00 ?  93  LEU   B HD13 1 
ATOM   5134 H  HD21 . LEU   B 1 93  ? 39.259 -15.625 -2.616  1.00 12.98 ?  93  LEU   B HD21 1 
ATOM   5135 H  HD22 . LEU   B 1 93  ? 39.956 -15.081 -3.936  1.00 12.98 ?  93  LEU   B HD22 1 
ATOM   5136 H  HD23 . LEU   B 1 93  ? 40.312 -16.529 -3.389  1.00 12.98 ?  93  LEU   B HD23 1 
ATOM   5137 N  N    . HIS   B 1 94  ? 44.258 -15.348 -0.014  1.00 9.12  ?  94  HIS   B N    1 
ATOM   5138 C  CA   . HIS   B 1 94  ? 44.480 -16.252 1.105   1.00 9.13  ?  94  HIS   B CA   1 
ATOM   5139 C  C    . HIS   B 1 94  ? 43.119 -16.608 1.684   1.00 9.57  ?  94  HIS   B C    1 
ATOM   5140 O  O    . HIS   B 1 94  ? 42.447 -15.735 2.237   1.00 11.01 ?  94  HIS   B O    1 
ATOM   5141 C  CB   . HIS   B 1 94  ? 45.352 -15.570 2.156   1.00 9.78  ?  94  HIS   B CB   1 
ATOM   5142 C  CG   . HIS   B 1 94  ? 46.736 -15.272 1.684   1.00 9.87  ?  94  HIS   B CG   1 
ATOM   5143 N  ND1  . HIS   B 1 94  ? 47.763 -16.190 1.761   1.00 10.16 ?  94  HIS   B ND1  1 
ATOM   5144 C  CD2  . HIS   B 1 94  ? 47.247 -14.162 1.097   1.00 10.24 ?  94  HIS   B CD2  1 
ATOM   5145 C  CE1  . HIS   B 1 94  ? 48.853 -15.638 1.260   1.00 9.90  ?  94  HIS   B CE1  1 
ATOM   5146 N  NE2  . HIS   B 1 94  ? 48.567 -14.415 0.843   1.00 10.15 ?  94  HIS   B NE2  1 
ATOM   5147 H  H    . HIS   B 1 94  ? 44.327 -14.513 0.194   1.00 10.91 ?  94  HIS   B H    1 
ATOM   5148 H  HA   . HIS   B 1 94  ? 44.919 -17.060 0.798   1.00 10.93 ?  94  HIS   B HA   1 
ATOM   5149 H  HB2  . HIS   B 1 94  ? 44.938 -14.733 2.410   1.00 11.72 ?  94  HIS   B HB2  1 
ATOM   5150 H  HB3  . HIS   B 1 94  ? 45.426 -16.153 2.925   1.00 11.72 ?  94  HIS   B HB3  1 
ATOM   5151 H  HD2  . HIS   B 1 94  ? 46.795 -13.372 0.902   1.00 12.26 ?  94  HIS   B HD2  1 
ATOM   5152 H  HE1  . HIS   B 1 94  ? 49.683 -16.058 1.197   1.00 11.85 ?  94  HIS   B HE1  1 
ATOM   5153 H  HE2  . HIS   B 1 94  ? 49.129 -13.872 0.480   1.00 12.16 ?  94  HIS   B HE2  1 
ATOM   5154 N  N    . VAL   B 1 95  ? 42.688 -17.861 1.528   1.00 9.50  ?  95  VAL   B N    1 
ATOM   5155 C  CA   . VAL   B 1 95  ? 41.362 -18.304 1.961   1.00 9.54  ?  95  VAL   B CA   1 
ATOM   5156 C  C    . VAL   B 1 95  ? 41.529 -19.339 3.058   1.00 9.63  ?  95  VAL   B C    1 
ATOM   5157 O  O    . VAL   B 1 95  ? 42.300 -20.292 2.899   1.00 10.48 ?  95  VAL   B O    1 
ATOM   5158 C  CB   . VAL   B 1 95  ? 40.541 -18.907 0.804   1.00 10.07 ?  95  VAL   B CB   1 
ATOM   5159 C  CG1  . VAL   B 1 95  ? 39.165 -19.355 1.295   1.00 11.12 ?  95  VAL   B CG1  1 
ATOM   5160 C  CG2  . VAL   B 1 95  ? 40.413 -17.924 -0.327  1.00 10.24 ?  95  VAL   B CG2  1 
ATOM   5161 H  H    . VAL   B 1 95  ? 43.153 -18.489 1.168   1.00 11.37 ?  95  VAL   B H    1 
ATOM   5162 H  HA   . VAL   B 1 95  ? 40.867 -17.551 2.324   1.00 11.42 ?  95  VAL   B HA   1 
ATOM   5163 H  HB   . VAL   B 1 95  ? 41.001 -19.689 0.468   1.00 12.06 ?  95  VAL   B HB   1 
ATOM   5164 H  HG11 . VAL   B 1 95  ? 38.601 -19.546 0.526   1.00 13.32 ?  95  VAL   B HG11 1 
ATOM   5165 H  HG12 . VAL   B 1 95  ? 39.260 -20.157 1.834   1.00 13.32 ?  95  VAL   B HG12 1 
ATOM   5166 H  HG13 . VAL   B 1 95  ? 38.766 -18.646 1.824   1.00 13.32 ?  95  VAL   B HG13 1 
ATOM   5167 H  HG21 . VAL   B 1 95  ? 39.834 -18.302 -1.008  1.00 12.26 ?  95  VAL   B HG21 1 
ATOM   5168 H  HG22 . VAL   B 1 95  ? 40.023 -17.101 0.014   1.00 12.26 ?  95  VAL   B HG22 1 
ATOM   5169 H  HG23 . VAL   B 1 95  ? 41.290 -17.750 -0.693  1.00 12.26 ?  95  VAL   B HG23 1 
ATOM   5170 N  N    . VAL   B 1 96  ? 40.795 -19.171 4.152   1.00 10.18 ?  96  VAL   B N    1 
ATOM   5171 C  CA   . VAL   B 1 96  ? 40.877 -20.084 5.290   1.00 10.78 ?  96  VAL   B CA   1 
ATOM   5172 C  C    . VAL   B 1 96  ? 39.688 -21.043 5.240   1.00 10.85 ?  96  VAL   B C    1 
ATOM   5173 O  O    . VAL   B 1 96  ? 38.567 -20.690 5.621   1.00 11.67 ?  96  VAL   B O    1 
ATOM   5174 C  CB   . VAL   B 1 96  ? 40.932 -19.339 6.626   1.00 11.24 ?  96  VAL   B CB   1 
ATOM   5175 C  CG1  . VAL   B 1 96  ? 41.107 -20.335 7.770   1.00 12.16 ?  96  VAL   B CG1  1 
ATOM   5176 C  CG2  . VAL   B 1 96  ? 42.045 -18.302 6.635   1.00 12.13 ?  96  VAL   B CG2  1 
ATOM   5177 H  H    . VAL   B 1 96  ? 40.232 -18.532 4.264   1.00 12.19 ?  96  VAL   B H    1 
ATOM   5178 H  HA   . VAL   B 1 96  ? 41.690 -20.613 5.214   1.00 12.91 ?  96  VAL   B HA   1 
ATOM   5179 H  HB   . VAL   B 1 96  ? 40.092 -18.878 6.765   1.00 13.46 ?  96  VAL   B HB   1 
ATOM   5180 H  HG11 . VAL   B 1 96  ? 41.293 -19.845 8.590   1.00 14.57 ?  96  VAL   B HG11 1 
ATOM   5181 H  HG12 . VAL   B 1 96  ? 40.292 -20.849 7.876   1.00 14.57 ?  96  VAL   B HG12 1 
ATOM   5182 H  HG13 . VAL   B 1 96  ? 41.850 -20.925 7.568   1.00 14.57 ?  96  VAL   B HG13 1 
ATOM   5183 H  HG21 . VAL   B 1 96  ? 42.091 -17.893 7.518   1.00 14.54 ?  96  VAL   B HG21 1 
ATOM   5184 H  HG22 . VAL   B 1 96  ? 42.886 -18.731 6.427   1.00 14.54 ?  96  VAL   B HG22 1 
ATOM   5185 H  HG23 . VAL   B 1 96  ? 41.846 -17.619 5.972   1.00 14.54 ?  96  VAL   B HG23 1 
ATOM   5186 N  N    . GLY   B 1 97  ? 39.928 -22.275 4.801   1.00 11.16 ?  97  GLY   B N    1 
ATOM   5187 C  CA   . GLY   B 1 97  ? 38.956 -23.334 4.959   1.00 11.70 ?  97  GLY   B CA   1 
ATOM   5188 C  C    . GLY   B 1 97  ? 39.079 -23.946 6.338   1.00 12.49 ?  97  GLY   B C    1 
ATOM   5189 O  O    . GLY   B 1 97  ? 40.119 -23.824 6.999   1.00 12.91 ?  97  GLY   B O    1 
ATOM   5190 H  H    . GLY   B 1 97  ? 40.655 -22.516 4.405   1.00 13.37 ?  97  GLY   B H    1 
ATOM   5191 H  HA2  . GLY   B 1 97  ? 38.061 -22.969 4.842   1.00 14.02 ?  97  GLY   B HA2  1 
ATOM   5192 H  HA3  . GLY   B 1 97  ? 39.102 -24.017 4.285   1.00 14.02 ?  97  GLY   B HA3  1 
ATOM   5193 N  N    . PRO   B 1 98  ? 38.032 -24.629 6.798   1.00 13.34 ?  98  PRO   B N    1 
ATOM   5194 C  CA   . PRO   B 1 98  ? 38.121 -25.321 8.086   1.00 14.19 ?  98  PRO   B CA   1 
ATOM   5195 C  C    . PRO   B 1 98  ? 39.146 -26.443 8.045   1.00 13.71 ?  98  PRO   B C    1 
ATOM   5196 O  O    . PRO   B 1 98  ? 39.251 -27.182 7.067   1.00 13.90 ?  98  PRO   B O    1 
ATOM   5197 C  CB   . PRO   B 1 98  ? 36.702 -25.864 8.289   1.00 14.33 ?  98  PRO   B CB   1 
ATOM   5198 C  CG   . PRO   B 1 98  ? 36.149 -26.003 6.914   1.00 13.83 ?  98  PRO   B CG   1 
ATOM   5199 C  CD   . PRO   B 1 98  ? 36.721 -24.831 6.155   1.00 13.29 ?  98  PRO   B CD   1 
ATOM   5200 H  HA   . PRO   B 1 98  ? 38.339 -24.697 8.792   1.00 17.00 ?  98  PRO   B HA   1 
ATOM   5201 H  HB2  . PRO   B 1 98  ? 36.742 -26.729 8.731   1.00 17.17 ?  98  PRO   B HB2  1 
ATOM   5202 H  HB3  . PRO   B 1 98  ? 36.179 -25.236 8.806   1.00 17.17 ?  98  PRO   B HB3  1 
ATOM   5203 H  HG2  . PRO   B 1 98  ? 36.443 -26.845 6.526   1.00 16.57 ?  98  PRO   B HG2  1 
ATOM   5204 H  HG3  . PRO   B 1 98  ? 35.182 -25.958 6.943   1.00 16.57 ?  98  PRO   B HG3  1 
ATOM   5205 H  HD2  . PRO   B 1 98  ? 36.829 -25.058 5.214   1.00 15.92 ?  98  PRO   B HD2  1 
ATOM   5206 H  HD3  . PRO   B 1 98  ? 36.167 -24.047 6.269   1.00 15.92 ?  98  PRO   B HD3  1 
ATOM   5207 N  N    . ASN   B 1 99  ? 39.892 -26.570 9.132   1.00 14.66 ?  99  ASN   B N    1 
ATOM   5208 C  CA   . ASN   B 1 99  ? 40.868 -27.641 9.298   1.00 15.57 ?  99  ASN   B CA   1 
ATOM   5209 C  C    . ASN   B 1 99  ? 40.230 -28.726 10.165  1.00 17.75 ?  99  ASN   B C    1 
ATOM   5210 O  O    . ASN   B 1 99  ? 40.145 -28.585 11.386  1.00 18.60 ?  99  ASN   B O    1 
ATOM   5211 C  CB   . ASN   B 1 99  ? 42.137 -27.087 9.931   1.00 15.79 ?  99  ASN   B CB   1 
ATOM   5212 C  CG   . ASN   B 1 99  ? 43.272 -28.086 9.924   1.00 16.61 ?  99  ASN   B CG   1 
ATOM   5213 O  OD1  . ASN   B 1 99  ? 43.053 -29.282 10.074  1.00 17.60 ?  99  ASN   B OD1  1 
ATOM   5214 N  ND2  . ASN   B 1 99  ? 44.491 -27.601 9.745   1.00 17.03 ?  99  ASN   B ND2  1 
ATOM   5215 H  H    . ASN   B 1 99  ? 39.851 -26.035 9.803   1.00 17.57 ?  99  ASN   B H    1 
ATOM   5216 H  HA   . ASN   B 1 99  ? 41.087 -28.027 8.437   1.00 18.66 ?  99  ASN   B HA   1 
ATOM   5217 H  HB2  . ASN   B 1 99  ? 42.418 -26.307 9.439   1.00 18.92 ?  99  ASN   B HB2  1 
ATOM   5218 H  HB3  . ASN   B 1 99  ? 41.948 -26.853 10.856  1.00 18.92 ?  99  ASN   B HB3  1 
ATOM   5219 H  HD21 . ASN   B 1 99  ? 45.168 -28.130 9.733   1.00 20.41 ?  99  ASN   B HD21 1 
ATOM   5220 H  HD22 . ASN   B 1 99  ? 44.601 -26.755 9.646   1.00 20.41 ?  99  ASN   B HD22 1 
ATOM   5221 N  N    A VAL   B 1 100 ? 39.766 -29.803 9.525   0.60 19.82 ?  100 VAL   B N    1 
ATOM   5222 N  N    B VAL   B 1 100 ? 39.769 -29.802 9.520   0.40 19.87 ?  100 VAL   B N    1 
ATOM   5223 C  CA   A VAL   B 1 100 ? 39.145 -30.901 10.266  0.60 22.32 ?  100 VAL   B CA   1 
ATOM   5224 C  CA   B VAL   B 1 100 ? 39.148 -30.911 10.242  0.40 22.12 ?  100 VAL   B CA   1 
ATOM   5225 C  C    A VAL   B 1 100 ? 40.148 -31.561 11.203  0.60 22.63 ?  100 VAL   B C    1 
ATOM   5226 C  C    B VAL   B 1 100 ? 40.143 -31.576 11.186  0.40 22.63 ?  100 VAL   B C    1 
ATOM   5227 O  O    A VAL   B 1 100 ? 39.776 -32.056 12.275  0.60 23.21 ?  100 VAL   B O    1 
ATOM   5228 O  O    B VAL   B 1 100 ? 39.760 -32.085 12.247  0.40 22.96 ?  100 VAL   B O    1 
ATOM   5229 C  CB   A VAL   B 1 100 ? 38.508 -31.916 9.295   0.60 24.71 ?  100 VAL   B CB   1 
ATOM   5230 C  CB   B VAL   B 1 100 ? 38.531 -31.915 9.246   0.40 23.97 ?  100 VAL   B CB   1 
ATOM   5231 C  CG1  A VAL   B 1 100 ? 38.039 -33.158 10.046  0.60 25.90 ?  100 VAL   B CG1  1 
ATOM   5232 C  CG1  B VAL   B 1 100 ? 38.026 -33.156 9.972   0.40 24.85 ?  100 VAL   B CG1  1 
ATOM   5233 C  CG2  A VAL   B 1 100 ? 37.349 -31.279 8.549   0.60 25.19 ?  100 VAL   B CG2  1 
ATOM   5234 C  CG2  B VAL   B 1 100 ? 37.402 -31.261 8.466   0.40 24.40 ?  100 VAL   B CG2  1 
ATOM   5235 H  H    A VAL   B 1 100 ? 39.793 -29.918 8.672   0.60 23.76 ?  100 VAL   B H    1 
ATOM   5236 H  H    B VAL   B 1 100 ? 39.796 -29.909 8.666   0.40 23.82 ?  100 VAL   B H    1 
ATOM   5237 H  HA   A VAL   B 1 100 ? 38.427 -30.538 10.808  0.60 26.76 ?  100 VAL   B HA   1 
ATOM   5238 H  HA   B VAL   B 1 100 ? 38.423 -30.562 10.782  0.40 26.52 ?  100 VAL   B HA   1 
ATOM   5239 H  HB   A VAL   B 1 100 ? 39.171 -32.195 8.645   0.60 29.63 ?  100 VAL   B HB   1 
ATOM   5240 H  HB   B VAL   B 1 100 ? 39.210 -32.196 8.614   0.40 28.73 ?  100 VAL   B HB   1 
ATOM   5241 H  HG11 A VAL   B 1 100 ? 37.442 -33.667 9.473   0.60 31.05 ?  100 VAL   B HG11 1 
ATOM   5242 H  HG11 B VAL   B 1 100 ? 37.452 -33.661 9.372   0.40 29.79 ?  100 VAL   B HG11 1 
ATOM   5243 H  HG12 A VAL   B 1 100 ? 38.808 -33.701 10.282  0.60 31.05 ?  100 VAL   B HG12 1 
ATOM   5244 H  HG12 B VAL   B 1 100 ? 38.783 -33.702 10.237  0.40 29.79 ?  100 VAL   B HG12 1 
ATOM   5245 H  HG13 A VAL   B 1 100 ? 37.567 -32.884 10.849  0.60 31.05 ?  100 VAL   B HG13 1 
ATOM   5246 H  HG13 B VAL   B 1 100 ? 37.523 -32.883 10.755  0.40 29.79 ?  100 VAL   B HG13 1 
ATOM   5247 H  HG21 A VAL   B 1 100 ? 36.977 -31.929 7.931   0.60 30.21 ?  100 VAL   B HG21 1 
ATOM   5248 H  HG21 B VAL   B 1 100 ? 37.024 -31.911 7.853   0.40 29.26 ?  100 VAL   B HG21 1 
ATOM   5249 H  HG22 A VAL   B 1 100 ? 36.672 -31.010 9.190   0.60 30.21 ?  100 VAL   B HG22 1 
ATOM   5250 H  HG22 B VAL   B 1 100 ? 36.722 -30.960 9.089   0.40 29.26 ?  100 VAL   B HG22 1 
ATOM   5251 H  HG23 A VAL   B 1 100 ? 37.673 -30.507 8.064   0.60 30.21 ?  100 VAL   B HG23 1 
ATOM   5252 H  HG23 B VAL   B 1 100 ? 37.757 -30.507 7.972   0.40 29.26 ?  100 VAL   B HG23 1 
ATOM   5253 N  N    . ASN   B 1 101 ? 41.425 -31.599 10.816  1.00 23.32 ?  101 ASN   B N    1 
ATOM   5254 C  CA   . ASN   B 1 101 ? 42.459 -32.138 11.698  1.00 25.33 ?  101 ASN   B CA   1 
ATOM   5255 C  C    . ASN   B 1 101 ? 42.647 -31.306 12.961  1.00 27.40 ?  101 ASN   B C    1 
ATOM   5256 O  O    . ASN   B 1 101 ? 43.279 -31.784 13.911  1.00 28.94 ?  101 ASN   B O    1 
ATOM   5257 C  CB   . ASN   B 1 101 ? 43.787 -32.271 10.944  1.00 25.44 ?  101 ASN   B CB   1 
ATOM   5258 C  CG   . ASN   B 1 101 ? 43.775 -33.411 9.943   1.00 25.12 ?  101 ASN   B CG   1 
ATOM   5259 O  OD1  . ASN   B 1 101 ? 43.096 -34.412 10.143  1.00 25.74 ?  101 ASN   B OD1  1 
ATOM   5260 N  ND2  . ASN   B 1 101 ? 44.522 -33.260 8.857   1.00 24.65 ?  101 ASN   B ND2  1 
ATOM   5261 H  H    A ASN   B 1 101 ? 41.708 -31.333 10.048  0.60 27.95 ?  101 ASN   B H    1 
ATOM   5262 H  H    B ASN   B 1 101 ? 41.715 -31.316 10.057  0.40 27.95 ?  101 ASN   B H    1 
ATOM   5263 H  HA   . ASN   B 1 101 ? 42.192 -33.021 11.978  1.00 30.37 ?  101 ASN   B HA   1 
ATOM   5264 H  HB2  . ASN   B 1 101 ? 43.968 -31.452 10.457  1.00 30.51 ?  101 ASN   B HB2  1 
ATOM   5265 H  HB3  . ASN   B 1 101 ? 44.497 -32.440 11.582  1.00 30.51 ?  101 ASN   B HB3  1 
ATOM   5266 H  HD21 . ASN   B 1 101 ? 44.546 -33.882 8.262   1.00 29.56 ?  101 ASN   B HD21 1 
ATOM   5267 H  HD22 . ASN   B 1 101 ? 44.980 -32.542 8.747   1.00 29.56 ?  101 ASN   B HD22 1 
ATOM   5268 N  N    . LYS   B 1 102 ? 42.119 -30.080 12.987  1.00 29.41 ?  102 LYS   B N    1 
ATOM   5269 C  CA   . LYS   B 1 102 ? 42.091 -29.239 14.176  1.00 31.86 ?  102 LYS   B CA   1 
ATOM   5270 C  C    . LYS   B 1 102 ? 40.713 -29.195 14.823  1.00 31.12 ?  102 LYS   B C    1 
ATOM   5271 O  O    . LYS   B 1 102 ? 40.494 -28.398 15.740  1.00 32.32 ?  102 LYS   B O    1 
ATOM   5272 C  CB   . LYS   B 1 102 ? 42.515 -27.810 13.831  1.00 35.45 ?  102 LYS   B CB   1 
ATOM   5273 C  CG   . LYS   B 1 102 ? 43.975 -27.635 13.456  1.00 38.58 ?  102 LYS   B CG   1 
ATOM   5274 C  CD   . LYS   B 1 102 ? 44.217 -26.213 12.973  1.00 41.66 ?  102 LYS   B CD   1 
ATOM   5275 C  CE   . LYS   B 1 102 ? 45.692 -25.908 12.791  1.00 43.97 ?  102 LYS   B CE   1 
ATOM   5276 N  NZ   . LYS   B 1 102 ? 45.893 -24.508 12.313  1.00 45.12 ?  102 LYS   B NZ   1 
ATOM   5277 H  H    . LYS   B 1 102 ? 41.751 -29.702 12.304  1.00 35.27 ?  102 LYS   B H    1 
ATOM   5278 H  HA   . LYS   B 1 102 ? 42.723 -29.587 14.823  1.00 38.20 ?  102 LYS   B HA   1 
ATOM   5279 H  HB2  . LYS   B 1 102 ? 41.981 -27.502 13.083  1.00 42.51 ?  102 LYS   B HB2  1 
ATOM   5280 H  HB3  . LYS   B 1 102 ? 42.344 -27.244 14.603  1.00 42.51 ?  102 LYS   B HB3  1 
ATOM   5281 H  HG2  . LYS   B 1 102 ? 44.533 -27.797 14.233  1.00 46.27 ?  102 LYS   B HG2  1 
ATOM   5282 H  HG3  . LYS   B 1 102 ? 44.202 -28.248 12.739  1.00 46.27 ?  102 LYS   B HG3  1 
ATOM   5283 H  HD2  . LYS   B 1 102 ? 43.775 -26.089 12.118  1.00 49.97 ?  102 LYS   B HD2  1 
ATOM   5284 H  HD3  . LYS   B 1 102 ? 43.858 -25.591 13.626  1.00 49.97 ?  102 LYS   B HD3  1 
ATOM   5285 H  HE2  . LYS   B 1 102 ? 46.149 -26.009 13.641  1.00 52.74 ?  102 LYS   B HE2  1 
ATOM   5286 H  HE3  . LYS   B 1 102 ? 46.067 -26.513 12.132  1.00 52.74 ?  102 LYS   B HE3  1 
ATOM   5287 H  HZ1  . LYS   B 1 102 ? 46.761 -24.343 12.211  1.00 54.12 ?  102 LYS   B HZ1  1 
ATOM   5288 H  HZ2  . LYS   B 1 102 ? 45.482 -24.392 11.532  1.00 54.12 ?  102 LYS   B HZ2  1 
ATOM   5289 H  HZ3  . LYS   B 1 102 ? 45.556 -23.934 12.904  1.00 54.12 ?  102 LYS   B HZ3  1 
ATOM   5290 N  N    . GLY   B 1 103 ? 39.773 -30.012 14.353  1.00 29.95 ?  103 GLY   B N    1 
ATOM   5291 C  CA   . GLY   B 1 103 ? 38.444 -30.051 14.926  1.00 29.48 ?  103 GLY   B CA   1 
ATOM   5292 C  C    . GLY   B 1 103 ? 37.510 -28.959 14.461  1.00 28.06 ?  103 GLY   B C    1 
ATOM   5293 O  O    . GLY   B 1 103 ? 36.419 -28.819 15.026  1.00 28.82 ?  103 GLY   B O    1 
ATOM   5294 H  H    . GLY   B 1 103 ? 39.886 -30.554 13.696  1.00 35.92 ?  103 GLY   B H    1 
ATOM   5295 H  HA2  . GLY   B 1 103 ? 38.033 -30.899 14.708  1.00 35.35 ?  103 GLY   B HA2  1 
ATOM   5296 H  HA3  . GLY   B 1 103 ? 38.517 -29.992 15.893  1.00 35.35 ?  103 GLY   B HA3  1 
ATOM   5297 N  N    A GLU   B 1 104 ? 37.901 -28.178 13.459  0.60 26.73 ?  104 GLU   B N    1 
ATOM   5298 N  N    B GLU   B 1 104 ? 37.885 -28.190 13.444  0.40 27.24 ?  104 GLU   B N    1 
ATOM   5299 C  CA   A GLU   B 1 104 ? 37.079 -27.070 13.001  0.60 25.40 ?  104 GLU   B CA   1 
ATOM   5300 C  CA   B GLU   B 1 104 ? 37.039 -27.106 12.971  0.40 26.25 ?  104 GLU   B CA   1 
ATOM   5301 C  C    A GLU   B 1 104 ? 35.900 -27.581 12.177  0.60 26.15 ?  104 GLU   B C    1 
ATOM   5302 C  C    B GLU   B 1 104 ? 35.881 -27.646 12.136  0.40 26.53 ?  104 GLU   B C    1 
ATOM   5303 O  O    A GLU   B 1 104 ? 35.951 -28.657 11.574  0.60 27.08 ?  104 GLU   B O    1 
ATOM   5304 O  O    B GLU   B 1 104 ? 35.966 -28.718 11.530  0.40 27.02 ?  104 GLU   B O    1 
ATOM   5305 C  CB   A GLU   B 1 104 ? 37.927 -26.077 12.206  0.60 24.12 ?  104 GLU   B CB   1 
ATOM   5306 C  CB   B GLU   B 1 104 ? 37.871 -26.098 12.179  0.40 25.32 ?  104 GLU   B CB   1 
ATOM   5307 C  CG   A GLU   B 1 104 ? 39.039 -25.460 13.047  0.60 22.91 ?  104 GLU   B CG   1 
ATOM   5308 C  CG   B GLU   B 1 104 ? 38.962 -25.460 13.029  0.40 24.54 ?  104 GLU   B CG   1 
ATOM   5309 C  CD   A GLU   B 1 104 ? 39.971 -24.562 12.264  0.60 21.62 ?  104 GLU   B CD   1 
ATOM   5310 C  CD   B GLU   B 1 104 ? 39.914 -24.588 12.240  0.40 23.85 ?  104 GLU   B CD   1 
ATOM   5311 O  OE1  A GLU   B 1 104 ? 39.965 -24.605 11.016  0.60 19.38 ?  104 GLU   B OE1  1 
ATOM   5312 O  OE1  B GLU   B 1 104 ? 39.872 -24.614 10.992  0.40 23.01 ?  104 GLU   B OE1  1 
ATOM   5313 O  OE2  A GLU   B 1 104 ? 40.720 -23.808 12.917  0.60 22.34 -1 104 GLU   B OE2  1 
ATOM   5314 O  OE2  B GLU   B 1 104 ? 40.714 -23.875 12.880  0.40 24.04 -1 104 GLU   B OE2  1 
ATOM   5315 H  H    A GLU   B 1 104 ? 38.645 -28.267 13.035  0.60 32.06 ?  104 GLU   B H    1 
ATOM   5316 H  H    B GLU   B 1 104 ? 38.627 -28.273 13.018  0.40 32.67 ?  104 GLU   B H    1 
ATOM   5317 H  HA   A GLU   B 1 104 ? 36.727 -26.604 13.775  0.60 30.45 ?  104 GLU   B HA   1 
ATOM   5318 H  HA   B GLU   B 1 104 ? 36.664 -26.643 13.737  0.40 31.48 ?  104 GLU   B HA   1 
ATOM   5319 H  HB2  A GLU   B 1 104 ? 38.337 -26.533 11.456  0.60 28.92 ?  104 GLU   B HB2  1 
ATOM   5320 H  HB2  B GLU   B 1 104 ? 38.296 -26.550 11.434  0.40 30.36 ?  104 GLU   B HB2  1 
ATOM   5321 H  HB3  A GLU   B 1 104 ? 37.359 -25.357 11.889  0.60 28.92 ?  104 GLU   B HB3  1 
ATOM   5322 H  HB3  B GLU   B 1 104 ? 37.291 -25.391 11.854  0.40 30.36 ?  104 GLU   B HB3  1 
ATOM   5323 H  HG2  A GLU   B 1 104 ? 38.647 -24.922 13.754  0.60 27.47 ?  104 GLU   B HG2  1 
ATOM   5324 H  HG2  B GLU   B 1 104 ? 38.546 -24.908 13.711  0.40 29.43 ?  104 GLU   B HG2  1 
ATOM   5325 H  HG3  A GLU   B 1 104 ? 39.578 -26.166 13.435  0.60 27.47 ?  104 GLU   B HG3  1 
ATOM   5326 H  HG3  B GLU   B 1 104 ? 39.486 -26.160 13.449  0.40 29.43 ?  104 GLU   B HG3  1 
ATOM   5327 N  N    A ASP   B 1 105 ? 34.828 -26.792 12.165  0.60 26.04 ?  105 ASP   B N    1 
ATOM   5328 N  N    B ASP   B 1 105 ? 34.789 -26.884 12.116  0.40 26.18 ?  105 ASP   B N    1 
ATOM   5329 C  CA   A ASP   B 1 105 ? 33.551 -27.241 11.624  0.60 26.63 ?  105 ASP   B CA   1 
ATOM   5330 C  CA   B ASP   B 1 105 ? 33.528 -27.359 11.556  0.40 26.31 ?  105 ASP   B CA   1 
ATOM   5331 C  C    A ASP   B 1 105 ? 33.606 -27.296 10.102  0.60 25.07 ?  105 ASP   B C    1 
ATOM   5332 C  C    B ASP   B 1 105 ? 33.595 -27.374 10.034  0.40 25.36 ?  105 ASP   B C    1 
ATOM   5333 O  O    A ASP   B 1 105 ? 33.752 -26.263 9.440   0.60 24.29 ?  105 ASP   B O    1 
ATOM   5334 O  O    B ASP   B 1 105 ? 33.772 -26.329 9.400   0.40 24.77 ?  105 ASP   B O    1 
ATOM   5335 C  CB   A ASP   B 1 105 ? 32.443 -26.292 12.077  0.60 29.54 ?  105 ASP   B CB   1 
ATOM   5336 C  CB   B ASP   B 1 105 ? 32.384 -26.464 12.031  0.40 27.55 ?  105 ASP   B CB   1 
ATOM   5337 C  CG   A ASP   B 1 105 ? 31.065 -26.750 11.642  0.60 32.22 ?  105 ASP   B CG   1 
ATOM   5338 C  CG   B ASP   B 1 105 ? 31.018 -27.048 11.714  0.40 28.71 ?  105 ASP   B CG   1 
ATOM   5339 O  OD1  A ASP   B 1 105 ? 30.949 -27.860 11.082  0.60 32.53 ?  105 ASP   B OD1  1 
ATOM   5340 O  OD1  B ASP   B 1 105 ? 30.952 -28.027 10.940  0.40 28.96 ?  105 ASP   B OD1  1 
ATOM   5341 O  OD2  A ASP   B 1 105 ? 30.095 -25.991 11.855  0.60 33.65 -1 105 ASP   B OD2  1 
ATOM   5342 O  OD2  B ASP   B 1 105 ? 30.009 -26.538 12.247  0.40 28.84 -1 105 ASP   B OD2  1 
ATOM   5343 H  H    A ASP   B 1 105 ? 34.820 -25.987 12.463  0.60 31.22 ?  105 ASP   B H    1 
ATOM   5344 H  H    B ASP   B 1 105 ? 34.755 -26.085 12.418  0.40 31.40 ?  105 ASP   B H    1 
ATOM   5345 H  HA   A ASP   B 1 105 ? 33.351 -28.131 11.956  0.60 31.93 ?  105 ASP   B HA   1 
ATOM   5346 H  HA   B ASP   B 1 105 ? 33.352 -28.261 11.864  0.40 31.55 ?  105 ASP   B HA   1 
ATOM   5347 H  HB2  A ASP   B 1 105 ? 32.467 -26.220 13.047  0.60 35.42 ?  105 ASP   B HB2  1 
ATOM   5348 H  HB2  B ASP   B 1 105 ? 32.445 -26.350 12.994  0.40 33.03 ?  105 ASP   B HB2  1 
ATOM   5349 H  HB3  A ASP   B 1 105 ? 32.586 -25.423 11.677  0.60 35.42 ?  105 ASP   B HB3  1 
ATOM   5350 H  HB3  B ASP   B 1 105 ? 32.454 -25.598 11.594  0.40 33.03 ?  105 ASP   B HB3  1 
ATOM   5351 N  N    A ILE   B 1 106 ? 33.464 -28.503 9.549   0.60 24.67 ?  106 ILE   B N    1 
ATOM   5352 N  N    B ILE   B 1 106 ? 33.436 -28.565 9.449   0.40 24.94 ?  106 ILE   B N    1 
ATOM   5353 C  CA   A ILE   B 1 106 ? 33.461 -28.688 8.102   0.60 23.69 ?  106 ILE   B CA   1 
ATOM   5354 C  CA   B ILE   B 1 106 ? 33.444 -28.714 7.998   0.40 24.38 ?  106 ILE   B CA   1 
ATOM   5355 C  C    A ILE   B 1 106 ? 32.358 -27.877 7.431   0.60 22.46 ?  106 ILE   B C    1 
ATOM   5356 C  C    B ILE   B 1 106 ? 32.342 -27.892 7.341   0.40 23.61 ?  106 ILE   B C    1 
ATOM   5357 O  O    A ILE   B 1 106 ? 32.451 -27.573 6.238   0.60 21.58 ?  106 ILE   B O    1 
ATOM   5358 O  O    B ILE   B 1 106 ? 32.431 -27.576 6.150   0.40 23.17 ?  106 ILE   B O    1 
ATOM   5359 C  CB   A ILE   B 1 106 ? 33.366 -30.197 7.776   0.60 24.60 ?  106 ILE   B CB   1 
ATOM   5360 C  CB   B ILE   B 1 106 ? 33.355 -30.214 7.634   0.40 24.86 ?  106 ILE   B CB   1 
ATOM   5361 C  CG1  A ILE   B 1 106 ? 33.611 -30.454 6.288   0.60 24.88 ?  106 ILE   B CG1  1 
ATOM   5362 C  CG1  B ILE   B 1 106 ? 33.611 -30.436 6.142   0.40 24.99 ?  106 ILE   B CG1  1 
ATOM   5363 C  CG2  A ILE   B 1 106 ? 32.011 -30.755 8.202   0.60 25.29 ?  106 ILE   B CG2  1 
ATOM   5364 C  CG2  B ILE   B 1 106 ? 31.997 -30.782 8.028   0.40 25.39 ?  106 ILE   B CG2  1 
ATOM   5365 C  CD1  A ILE   B 1 106 ? 34.970 -29.995 5.810   0.60 25.05 ?  106 ILE   B CD1  1 
ATOM   5366 C  CD1  B ILE   B 1 106 ? 34.972 -29.965 5.682   0.40 25.07 ?  106 ILE   B CD1  1 
ATOM   5367 H  H    A ILE   B 1 106 ? 33.374 -29.229 9.996   0.60 29.58 ?  106 ILE   B H    1 
ATOM   5368 H  H    B ILE   B 1 106 ? 33.327 -29.301 9.875   0.40 29.90 ?  106 ILE   B H    1 
ATOM   5369 H  HA   A ILE   B 1 106 ? 34.306 -28.364 7.758   0.60 28.41 ?  106 ILE   B HA   1 
ATOM   5370 H  HA   B ILE   B 1 106 ? 34.288 -28.379 7.664   0.40 29.23 ?  106 ILE   B HA   1 
ATOM   5371 H  HB   A ILE   B 1 106 ? 34.054 -30.659 8.279   0.60 29.49 ?  106 ILE   B HB   1 
ATOM   5372 H  HB   B ILE   B 1 106 ? 34.037 -30.690 8.134   0.40 29.81 ?  106 ILE   B HB   1 
ATOM   5373 H  HG12 A ILE   B 1 106 ? 33.549 -31.410 6.122   0.60 29.84 ?  106 ILE   B HG12 1 
ATOM   5374 H  HG12 B ILE   B 1 106 ? 33.550 -31.387 5.953   0.40 29.96 ?  106 ILE   B HG12 1 
ATOM   5375 H  HG13 A ILE   B 1 106 ? 32.939 -29.987 5.770   0.60 29.84 ?  106 ILE   B HG13 1 
ATOM   5376 H  HG13 B ILE   B 1 106 ? 32.942 -29.958 5.631   0.40 29.96 ?  106 ILE   B HG13 1 
ATOM   5377 H  HG21 A ILE   B 1 106 ? 32.023 -31.720 8.108   0.60 30.32 ?  106 ILE   B HG21 1 
ATOM   5378 H  HG21 B ILE   B 1 106 ? 32.019 -31.747 7.931   0.40 30.44 ?  106 ILE   B HG21 1 
ATOM   5379 H  HG22 A ILE   B 1 106 ? 31.847 -30.515 9.128   0.60 30.32 ?  106 ILE   B HG22 1 
ATOM   5380 H  HG22 B ILE   B 1 106 ? 31.814 -30.548 8.952   0.40 30.44 ?  106 ILE   B HG22 1 
ATOM   5381 H  HG23 A ILE   B 1 106 ? 31.319 -30.378 7.636   0.60 30.32 ?  106 ILE   B HG23 1 
ATOM   5382 H  HG23 B ILE   B 1 106 ? 31.316 -30.406 7.450   0.40 30.44 ?  106 ILE   B HG23 1 
ATOM   5383 H  HD11 A ILE   B 1 106 ? 35.156 -30.400 4.950   0.60 30.04 ?  106 ILE   B HD11 1 
ATOM   5384 H  HD11 B ILE   B 1 106 ? 35.160 -30.349 4.813   0.40 30.06 ?  106 ILE   B HD11 1 
ATOM   5385 H  HD12 A ILE   B 1 106 ? 34.967 -29.028 5.726   0.60 30.04 ?  106 ILE   B HD12 1 
ATOM   5386 H  HD12 B ILE   B 1 106 ? 34.967 -28.997 5.623   0.40 30.06 ?  106 ILE   B HD12 1 
ATOM   5387 H  HD13 A ILE   B 1 106 ? 35.642 -30.269 6.455   0.60 30.04 ?  106 ILE   B HD13 1 
ATOM   5388 H  HD13 B ILE   B 1 106 ? 35.639 -30.256 6.324   0.40 30.06 ?  106 ILE   B HD13 1 
ATOM   5389 N  N    A GLN   B 1 107 ? 31.317 -27.498 8.177   0.60 22.87 ?  107 GLN   B N    1 
ATOM   5390 N  N    B GLN   B 1 107 ? 31.299 -27.532 8.093   0.40 23.75 ?  107 GLN   B N    1 
ATOM   5391 C  CA   A GLN   B 1 107 ? 30.233 -26.713 7.596   0.60 23.32 ?  107 GLN   B CA   1 
ATOM   5392 C  CA   B GLN   B 1 107 ? 30.220 -26.719 7.542   0.40 23.92 ?  107 GLN   B CA   1 
ATOM   5393 C  C    A GLN   B 1 107 ? 30.715 -25.371 7.065   0.60 21.23 ?  107 GLN   B C    1 
ATOM   5394 C  C    B GLN   B 1 107 ? 30.705 -25.354 7.059   0.40 21.69 ?  107 GLN   B C    1 
ATOM   5395 O  O    A GLN   B 1 107 ? 30.076 -24.805 6.174   0.60 21.92 ?  107 GLN   B O    1 
ATOM   5396 O  O    B GLN   B 1 107 ? 30.052 -24.748 6.205   0.40 22.18 ?  107 GLN   B O    1 
ATOM   5397 C  CB   A GLN   B 1 107 ? 29.129 -26.506 8.636   0.60 26.76 ?  107 GLN   B CB   1 
ATOM   5398 C  CB   B GLN   B 1 107 ? 29.112 -26.553 8.589   0.40 26.70 ?  107 GLN   B CB   1 
ATOM   5399 C  CG   A GLN   B 1 107 ? 27.804 -25.998 8.074   0.60 30.43 ?  107 GLN   B CG   1 
ATOM   5400 C  CG   B GLN   B 1 107 ? 27.782 -26.051 8.034   0.40 29.52 ?  107 GLN   B CG   1 
ATOM   5401 C  CD   A GLN   B 1 107 ? 27.747 -24.485 7.960   0.60 33.32 ?  107 GLN   B CD   1 
ATOM   5402 C  CD   B GLN   B 1 107 ? 27.679 -24.536 8.019   0.40 31.78 ?  107 GLN   B CD   1 
ATOM   5403 O  OE1  A GLN   B 1 107 ? 28.594 -23.775 8.505   0.60 34.32 ?  107 GLN   B OE1  1 
ATOM   5404 O  OE1  B GLN   B 1 107 ? 28.523 -23.836 8.581   0.40 32.61 ?  107 GLN   B OE1  1 
ATOM   5405 N  NE2  A GLN   B 1 107 ? 26.740 -23.983 7.249   0.60 34.23 ?  107 GLN   B NE2  1 
ATOM   5406 N  NE2  B GLN   B 1 107 ? 26.635 -24.022 7.375   0.40 32.53 ?  107 GLN   B NE2  1 
ATOM   5407 H  H    A GLN   B 1 107 ? 31.226 -27.663 9.011   0.60 27.42 ?  107 GLN   B H    1 
ATOM   5408 H  H    B GLN   B 1 107 ? 31.192 -27.750 8.917   0.40 28.48 ?  107 GLN   B H    1 
ATOM   5409 H  HA   A GLN   B 1 107 ? 29.852 -27.207 6.855   0.60 27.96 ?  107 GLN   B HA   1 
ATOM   5410 H  HA   B GLN   B 1 107 ? 29.833 -27.187 6.781   0.40 28.68 ?  107 GLN   B HA   1 
ATOM   5411 H  HB2  A GLN   B 1 107 ? 28.955 -27.354 9.067   0.60 32.09 ?  107 GLN   B HB2  1 
ATOM   5412 H  HB2  B GLN   B 1 107 ? 28.945 -27.412 9.006   0.40 32.02 ?  107 GLN   B HB2  1 
ATOM   5413 H  HB3  A GLN   B 1 107 ? 29.437 -25.862 9.293   0.60 32.09 ?  107 GLN   B HB3  1 
ATOM   5414 H  HB3  B GLN   B 1 107 ? 29.411 -25.920 9.261   0.40 32.02 ?  107 GLN   B HB3  1 
ATOM   5415 H  HG2  A GLN   B 1 107 ? 27.671 -26.367 7.187   0.60 36.50 ?  107 GLN   B HG2  1 
ATOM   5416 H  HG2  B GLN   B 1 107 ? 27.681 -26.365 7.123   0.40 35.40 ?  107 GLN   B HG2  1 
ATOM   5417 H  HG3  A GLN   B 1 107 ? 27.082 -26.284 8.660   0.60 36.50 ?  107 GLN   B HG3  1 
ATOM   5418 H  HG3  B GLN   B 1 107 ? 27.059 -26.397 8.584   0.40 35.40 ?  107 GLN   B HG3  1 
ATOM   5419 H  HE21 A GLN   B 1 107 ? 26.166 -24.509 6.881   0.60 41.05 ?  107 GLN   B HE21 1 
ATOM   5420 H  HE21 B GLN   B 1 107 ? 26.065 -24.542 6.993   0.40 39.01 ?  107 GLN   B HE21 1 
ATOM   5421 H  HE22 A GLN   B 1 107 ? 26.659 -23.131 7.158   0.60 41.05 ?  107 GLN   B HE22 1 
ATOM   5422 H  HE22 B GLN   B 1 107 ? 26.527 -23.169 7.340   0.40 39.01 ?  107 GLN   B HE22 1 
ATOM   5423 N  N    . LEU   B 1 108 ? 31.837 -24.861 7.574   1.00 19.45 ?  108 LEU   B N    1 
ATOM   5424 C  CA   . LEU   B 1 108 ? 32.378 -23.563 7.163   1.00 16.94 ?  108 LEU   B CA   1 
ATOM   5425 C  C    . LEU   B 1 108 ? 33.028 -23.584 5.788   1.00 14.89 ?  108 LEU   B C    1 
ATOM   5426 O  O    . LEU   B 1 108 ? 33.462 -22.528 5.300   1.00 14.76 ?  108 LEU   B O    1 
ATOM   5427 C  CB   . LEU   B 1 108 ? 33.382 -23.077 8.205   1.00 17.47 ?  108 LEU   B CB   1 
ATOM   5428 C  CG   . LEU   B 1 108 ? 32.750 -22.645 9.526   1.00 18.78 ?  108 LEU   B CG   1 
ATOM   5429 C  CD1  . LEU   B 1 108 ? 33.773 -22.611 10.645  1.00 18.81 ?  108 LEU   B CD1  1 
ATOM   5430 C  CD2  . LEU   B 1 108 ? 32.110 -21.279 9.357   1.00 20.15 ?  108 LEU   B CD2  1 
ATOM   5431 H  H    A LEU   B 1 108 ? 32.296 -25.252 8.182   0.60 23.31 ?  108 LEU   B H    1 
ATOM   5432 H  H    B LEU   B 1 108 ? 32.304 -25.262 8.169   0.40 23.31 ?  108 LEU   B H    1 
ATOM   5433 H  HA   . LEU   B 1 108 ? 31.648 -22.925 7.134   1.00 20.30 ?  108 LEU   B HA   1 
ATOM   5434 H  HB2  . LEU   B 1 108 ? 34.002 -23.794 8.401   1.00 20.93 ?  108 LEU   B HB2  1 
ATOM   5435 H  HB3  . LEU   B 1 108 ? 33.857 -22.314 7.847   1.00 20.93 ?  108 LEU   B HB3  1 
ATOM   5436 H  HG   . LEU   B 1 108 ? 32.052 -23.275 9.774   1.00 22.51 ?  108 LEU   B HG   1 
ATOM   5437 H  HD11 . LEU   B 1 108 ? 33.332 -22.347 11.471  1.00 22.55 ?  108 LEU   B HD11 1 
ATOM   5438 H  HD12 . LEU   B 1 108 ? 34.160 -23.494 10.746  1.00 22.55 ?  108 LEU   B HD12 1 
ATOM   5439 H  HD13 . LEU   B 1 108 ? 34.463 -21.968 10.421  1.00 22.55 ?  108 LEU   B HD13 1 
ATOM   5440 H  HD21 . LEU   B 1 108 ? 31.763 -20.983 10.213  1.00 24.16 ?  108 LEU   B HD21 1 
ATOM   5441 H  HD22 . LEU   B 1 108 ? 32.780 -20.655 9.038   1.00 24.16 ?  108 LEU   B HD22 1 
ATOM   5442 H  HD23 . LEU   B 1 108 ? 31.386 -21.346 8.714   1.00 24.16 ?  108 LEU   B HD23 1 
ATOM   5443 N  N    . LEU   B 1 109 ? 33.097 -24.753 5.157   1.00 13.89 ?  109 LEU   B N    1 
ATOM   5444 C  CA   . LEU   B 1 109 ? 33.728 -24.861 3.851   1.00 13.26 ?  109 LEU   B CA   1 
ATOM   5445 C  C    . LEU   B 1 109 ? 32.964 -24.077 2.791   1.00 12.52 ?  109 LEU   B C    1 
ATOM   5446 O  O    . LEU   B 1 109 ? 33.577 -23.483 1.897   1.00 12.26 ?  109 LEU   B O    1 
ATOM   5447 C  CB   . LEU   B 1 109 ? 33.836 -26.334 3.466   1.00 13.47 ?  109 LEU   B CB   1 
ATOM   5448 C  CG   . LEU   B 1 109 ? 34.629 -26.670 2.210   1.00 13.52 ?  109 LEU   B CG   1 
ATOM   5449 C  CD1  . LEU   B 1 109 ? 36.010 -26.023 2.238   1.00 13.16 ?  109 LEU   B CD1  1 
ATOM   5450 C  CD2  . LEU   B 1 109 ? 34.743 -28.181 2.066   1.00 13.94 ?  109 LEU   B CD2  1 
ATOM   5451 H  H    . LEU   B 1 109 ? 32.790 -25.492 5.460   1.00 16.64 ?  109 LEU   B H    1 
ATOM   5452 H  HA   . LEU   B 1 109 ? 34.622 -24.496 3.900   1.00 15.89 ?  109 LEU   B HA   1 
ATOM   5453 H  HB2  . LEU   B 1 109 ? 34.256 -26.807 4.200   1.00 16.14 ?  109 LEU   B HB2  1 
ATOM   5454 H  HB3  . LEU   B 1 109 ? 32.938 -26.681 3.336   1.00 16.14 ?  109 LEU   B HB3  1 
ATOM   5455 H  HG   . LEU   B 1 109 ? 34.153 -26.340 1.431   1.00 16.20 ?  109 LEU   B HG   1 
ATOM   5456 H  HD11 . LEU   B 1 109 ? 36.550 -26.392 1.522   1.00 15.77 ?  109 LEU   B HD11 1 
ATOM   5457 H  HD12 . LEU   B 1 109 ? 35.910 -25.066 2.116   1.00 15.77 ?  109 LEU   B HD12 1 
ATOM   5458 H  HD13 . LEU   B 1 109 ? 36.427 -26.207 3.094   1.00 15.77 ?  109 LEU   B HD13 1 
ATOM   5459 H  HD21 . LEU   B 1 109 ? 35.319 -28.387 1.310   1.00 16.70 ?  109 LEU   B HD21 1 
ATOM   5460 H  HD22 . LEU   B 1 109 ? 35.121 -28.551 2.877   1.00 16.70 ?  109 LEU   B HD22 1 
ATOM   5461 H  HD23 . LEU   B 1 109 ? 33.858 -28.556 1.914   1.00 16.70 ?  109 LEU   B HD23 1 
ATOM   5462 N  N    . LYS   B 1 110 ? 31.631 -24.047 2.870   1.00 12.30 ?  110 LYS   B N    1 
ATOM   5463 C  CA   . LYS   B 1 110 ? 30.875 -23.283 1.883   1.00 12.08 ?  110 LYS   B CA   1 
ATOM   5464 C  C    . LYS   B 1 110 ? 31.212 -21.796 1.974   1.00 11.60 ?  110 LYS   B C    1 
ATOM   5465 O  O    . LYS   B 1 110 ? 31.468 -21.147 0.955   1.00 11.61 ?  110 LYS   B O    1 
ATOM   5466 C  CB   . LYS   B 1 110 ? 29.372 -23.531 2.031   1.00 12.59 ?  110 LYS   B CB   1 
ATOM   5467 C  CG   . LYS   B 1 110 ? 28.565 -22.904 0.898   1.00 13.19 ?  110 LYS   B CG   1 
ATOM   5468 C  CD   . LYS   B 1 110 ? 27.102 -23.331 0.919   1.00 13.46 ?  110 LYS   B CD   1 
ATOM   5469 C  CE   . LYS   B 1 110 ? 26.327 -22.796 -0.290  1.00 13.99 ?  110 LYS   B CE   1 
ATOM   5470 N  NZ   . LYS   B 1 110 ? 26.669 -23.510 -1.554  1.00 14.11 ?  110 LYS   B NZ   1 
ATOM   5471 H  H    . LYS   B 1 110 ? 31.157 -24.455 3.460   1.00 14.74 ?  110 LYS   B H    1 
ATOM   5472 H  HA   . LYS   B 1 110 ? 31.130 -23.587 0.995   1.00 14.47 ?  110 LYS   B HA   1 
ATOM   5473 H  HB2  . LYS   B 1 110 ? 29.205 -24.492 2.021   1.00 15.08 ?  110 LYS   B HB2  1 
ATOM   5474 H  HB3  . LYS   B 1 110 ? 29.066 -23.152 2.867   1.00 15.08 ?  110 LYS   B HB3  1 
ATOM   5475 H  HG2  . LYS   B 1 110 ? 28.589 -21.939 0.983   1.00 15.81 ?  110 LYS   B HG2  1 
ATOM   5476 H  HG3  . LYS   B 1 110 ? 28.939 -23.175 0.046   1.00 15.81 ?  110 LYS   B HG3  1 
ATOM   5477 H  HD2  . LYS   B 1 110 ? 27.050 -24.306 0.904   1.00 16.12 ?  110 LYS   B HD2  1 
ATOM   5478 H  HD3  . LYS   B 1 110 ? 26.676 -22.995 1.725   1.00 16.12 ?  110 LYS   B HD3  1 
ATOM   5479 H  HE2  . LYS   B 1 110 ? 25.376 -22.904 -0.134  1.00 16.76 ?  110 LYS   B HE2  1 
ATOM   5480 H  HE3  . LYS   B 1 110 ? 26.541 -21.858 -0.409  1.00 16.76 ?  110 LYS   B HE3  1 
ATOM   5481 H  HZ1  . LYS   B 1 110 ? 26.203 -23.169 -2.231  1.00 16.91 ?  110 LYS   B HZ1  1 
ATOM   5482 H  HZ2  . LYS   B 1 110 ? 27.538 -23.422 -1.726  1.00 16.91 ?  110 LYS   B HZ2  1 
ATOM   5483 H  HZ3  . LYS   B 1 110 ? 26.475 -24.375 -1.475  1.00 16.91 ?  110 LYS   B HZ3  1 
ATOM   5484 N  N    . SER   B 1 111 ? 31.235 -21.246 3.193   1.00 12.17 ?  111 SER   B N    1 
ATOM   5485 C  CA   . SER   B 1 111 ? 31.626 -19.847 3.373   1.00 12.11 ?  111 SER   B CA   1 
ATOM   5486 C  C    . SER   B 1 111 ? 33.007 -19.585 2.788   1.00 11.55 ?  111 SER   B C    1 
ATOM   5487 O  O    . SER   B 1 111 ? 33.235 -18.548 2.147   1.00 11.77 ?  111 SER   B O    1 
ATOM   5488 C  CB   . SER   B 1 111 ? 31.615 -19.487 4.857   1.00 13.30 ?  111 SER   B CB   1 
ATOM   5489 O  OG   . SER   B 1 111 ? 30.307 -19.485 5.380   1.00 14.74 ?  111 SER   B OG   1 
ATOM   5490 H  H    . SER   B 1 111 ? 31.033 -21.661 3.919   1.00 14.58 ?  111 SER   B H    1 
ATOM   5491 H  HA   . SER   B 1 111 ? 30.993 -19.279 2.917   1.00 14.51 ?  111 SER   B HA   1 
ATOM   5492 H  HB2  . SER   B 1 111 ? 32.140 -20.143 5.345   1.00 15.93 ?  111 SER   B HB2  1 
ATOM   5493 H  HB3  . SER   B 1 111 ? 31.998 -18.607 4.970   1.00 15.93 ?  111 SER   B HB3  1 
ATOM   5494 H  HG   . SER   B 1 111 ? 30.320 -19.282 6.200   1.00 17.66 ?  111 SER   B HG   1 
ATOM   5495 N  N    . ALA   B 1 112 ? 33.944 -20.507 3.006   1.00 11.64 ?  112 ALA   B N    1 
ATOM   5496 C  CA   . ALA   B 1 112 ? 35.286 -20.335 2.464   1.00 11.21 ?  112 ALA   B CA   1 
ATOM   5497 C  C    . ALA   B 1 112 ? 35.252 -20.235 0.943   1.00 10.71 ?  112 ALA   B C    1 
ATOM   5498 O  O    . ALA   B 1 112 ? 35.879 -19.347 0.353   1.00 11.14 ?  112 ALA   B O    1 
ATOM   5499 C  CB   . ALA   B 1 112 ? 36.182 -21.485 2.926   1.00 11.78 ?  112 ALA   B CB   1 
ATOM   5500 H  H    . ALA   B 1 112 ? 33.830 -21.232 3.466   1.00 13.94 ?  112 ALA   B H    1 
ATOM   5501 H  HA   . ALA   B 1 112 ? 35.658 -19.510 2.811   1.00 13.42 ?  112 ALA   B HA   1 
ATOM   5502 H  HB1  . ALA   B 1 112 ? 37.074 -21.350 2.564   1.00 14.11 ?  112 ALA   B HB1  1 
ATOM   5503 H  HB2  . ALA   B 1 112 ? 36.221 -21.484 3.897   1.00 14.11 ?  112 ALA   B HB2  1 
ATOM   5504 H  HB3  . ALA   B 1 112 ? 35.817 -22.321 2.608   1.00 14.11 ?  112 ALA   B HB3  1 
ATOM   5505 N  N    . TYR   B 1 113 ? 34.520 -21.140 0.284   1.00 10.66 ?  113 TYR   B N    1 
ATOM   5506 C  CA   . TYR   B 1 113 ? 34.443 -21.089 -1.170  1.00 10.54 ?  113 TYR   B CA   1 
ATOM   5507 C  C    . TYR   B 1 113 ? 33.739 -19.838 -1.681  1.00 10.20 ?  113 TYR   B C    1 
ATOM   5508 O  O    . TYR   B 1 113 ? 34.009 -19.404 -2.805  1.00 10.45 ?  113 TYR   B O    1 
ATOM   5509 C  CB   . TYR   B 1 113 ? 33.777 -22.348 -1.725  1.00 10.87 ?  113 TYR   B CB   1 
ATOM   5510 C  CG   . TYR   B 1 113 ? 34.739 -23.494 -1.984  1.00 11.30 ?  113 TYR   B CG   1 
ATOM   5511 C  CD1  . TYR   B 1 113 ? 35.730 -23.391 -2.954  1.00 11.52 ?  113 TYR   B CD1  1 
ATOM   5512 C  CD2  . TYR   B 1 113 ? 34.637 -24.685 -1.281  1.00 11.45 ?  113 TYR   B CD2  1 
ATOM   5513 C  CE1  . TYR   B 1 113 ? 36.612 -24.425 -3.195  1.00 11.30 ?  113 TYR   B CE1  1 
ATOM   5514 C  CE2  . TYR   B 1 113 ? 35.506 -25.733 -1.522  1.00 11.55 ?  113 TYR   B CE2  1 
ATOM   5515 C  CZ   . TYR   B 1 113 ? 36.484 -25.605 -2.488  1.00 11.73 ?  113 TYR   B CZ   1 
ATOM   5516 O  OH   . TYR   B 1 113 ? 37.365 -26.622 -2.762  1.00 12.53 ?  113 TYR   B OH   1 
ATOM   5517 H  H    . TYR   B 1 113 ? 34.063 -21.772 0.655   1.00 12.77 ?  113 TYR   B H    1 
ATOM   5518 H  HA   . TYR   B 1 113 ? 35.343 -21.067 -1.509  1.00 12.62 ?  113 TYR   B HA   1 
ATOM   5519 H  HB2  . TYR   B 1 113 ? 33.111 -22.664 -1.091  1.00 13.02 ?  113 TYR   B HB2  1 
ATOM   5520 H  HB3  . TYR   B 1 113 ? 33.345 -22.128 -2.566  1.00 13.02 ?  113 TYR   B HB3  1 
ATOM   5521 H  HD1  . TYR   B 1 113 ? 35.817 -22.597 -3.438  1.00 13.80 ?  113 TYR   B HD1  1 
ATOM   5522 H  HD2  . TYR   B 1 113 ? 33.967 -24.775 -0.643  1.00 13.72 ?  113 TYR   B HD2  1 
ATOM   5523 H  HE1  . TYR   B 1 113 ? 37.267 -24.340 -3.855  1.00 13.53 ?  113 TYR   B HE1  1 
ATOM   5524 H  HE2  . TYR   B 1 113 ? 35.410 -26.527 -1.051  1.00 13.83 ?  113 TYR   B HE2  1 
ATOM   5525 H  HH   . TYR   B 1 113 ? 37.181 -27.291 -2.285  1.00 15.02 ?  113 TYR   B HH   1 
ATOM   5526 N  N    . GLU   B 1 114 ? 32.819 -19.260 -0.901  1.00 10.48 ?  114 GLU   B N    1 
ATOM   5527 C  CA   . GLU   B 1 114 ? 32.131 -18.058 -1.360  1.00 10.44 ?  114 GLU   B CA   1 
ATOM   5528 C  C    . GLU   B 1 114 ? 33.114 -16.933 -1.655  1.00 10.30 ?  114 GLU   B C    1 
ATOM   5529 O  O    . GLU   B 1 114 ? 32.837 -16.070 -2.493  1.00 10.76 ?  114 GLU   B O    1 
ATOM   5530 C  CB   . GLU   B 1 114 ? 31.073 -17.636 -0.338  1.00 10.80 ?  114 GLU   B CB   1 
ATOM   5531 C  CG   . GLU   B 1 114 ? 29.853 -18.549 -0.408  1.00 11.12 ?  114 GLU   B CG   1 
ATOM   5532 C  CD   . GLU   B 1 114 ? 28.836 -18.360 0.707   1.00 11.35 ?  114 GLU   B CD   1 
ATOM   5533 O  OE1  . GLU   B 1 114 ? 29.126 -17.737 1.752   1.00 11.63 ?  114 GLU   B OE1  1 
ATOM   5534 O  OE2  . GLU   B 1 114 ? 27.712 -18.895 0.545   1.00 12.28 -1 114 GLU   B OE2  1 
ATOM   5535 H  H    . GLU   B 1 114 ? 32.572 -19.546 -0.123  1.00 12.55 ?  114 GLU   B H    1 
ATOM   5536 H  HA   . GLU   B 1 114 ? 31.673 -18.261 -2.186  1.00 12.51 ?  114 GLU   B HA   1 
ATOM   5537 H  HB2  . GLU   B 1 114 ? 31.448 -17.696 0.556   1.00 12.94 ?  114 GLU   B HB2  1 
ATOM   5538 H  HB3  . GLU   B 1 114 ? 30.788 -16.732 -0.527  1.00 12.94 ?  114 GLU   B HB3  1 
ATOM   5539 H  HG2  . GLU   B 1 114 ? 29.404 -18.395 -1.252  1.00 13.32 ?  114 GLU   B HG2  1 
ATOM   5540 H  HG3  . GLU   B 1 114 ? 30.161 -19.473 -0.370  1.00 13.32 ?  114 GLU   B HG3  1 
ATOM   5541 N  N    . ASN   B 1 115 ? 34.280 -16.933 -1.007  1.00 10.18 ?  115 ASN   B N    1 
ATOM   5542 C  CA   . ASN   B 1 115 ? 35.268 -15.898 -1.301  1.00 10.18 ?  115 ASN   B CA   1 
ATOM   5543 C  C    . ASN   B 1 115 ? 35.679 -15.915 -2.767  1.00 9.89  ?  115 ASN   B C    1 
ATOM   5544 O  O    . ASN   B 1 115 ? 36.064 -14.876 -3.321  1.00 10.53 ?  115 ASN   B O    1 
ATOM   5545 C  CB   . ASN   B 1 115 ? 36.505 -16.078 -0.419  1.00 10.93 ?  115 ASN   B CB   1 
ATOM   5546 C  CG   . ASN   B 1 115 ? 36.238 -15.814 1.041   1.00 11.43 ?  115 ASN   B CG   1 
ATOM   5547 O  OD1  . ASN   B 1 115 ? 36.247 -14.670 1.482   1.00 13.34 ?  115 ASN   B OD1  1 
ATOM   5548 N  ND2  . ASN   B 1 115 ? 36.080 -16.878 1.820   1.00 11.35 ?  115 ASN   B ND2  1 
ATOM   5549 H  H    . ASN   B 1 115 ? 34.516 -17.504 -0.400  1.00 12.19 ?  115 ASN   B H    1 
ATOM   5550 H  HA   . ASN   B 1 115 ? 34.885 -15.030 -1.102  1.00 12.19 ?  115 ASN   B HA   1 
ATOM   5551 H  HB2  . ASN   B 1 115 ? 36.826 -16.989 -0.506  1.00 13.10 ?  115 ASN   B HB2  1 
ATOM   5552 H  HB3  . ASN   B 1 115 ? 37.191 -15.457 -0.710  1.00 13.10 ?  115 ASN   B HB3  1 
ATOM   5553 H  HD21 . ASN   B 1 115 ? 35.938 -16.775 2.665   1.00 13.59 ?  115 ASN   B HD21 1 
ATOM   5554 H  HD22 . ASN   B 1 115 ? 36.100 -17.668 1.484   1.00 13.59 ?  115 ASN   B HD22 1 
ATOM   5555 N  N    . PHE   B 1 116 ? 35.656 -17.092 -3.402  1.00 9.69  ?  116 PHE   B N    1 
ATOM   5556 C  CA   . PHE   B 1 116 ? 36.085 -17.189 -4.793  1.00 10.04 ?  116 PHE   B CA   1 
ATOM   5557 C  C    . PHE   B 1 116 ? 35.181 -16.364 -5.705  1.00 9.90  ?  116 PHE   B C    1 
ATOM   5558 O  O    . PHE   B 1 116 ? 35.616 -15.936 -6.779  1.00 10.50 ?  116 PHE   B O    1 
ATOM   5559 C  CB   . PHE   B 1 116 ? 36.050 -18.635 -5.312  1.00 9.72  ?  116 PHE   B CB   1 
ATOM   5560 C  CG   . PHE   B 1 116 ? 37.117 -19.588 -4.764  1.00 9.86  ?  116 PHE   B CG   1 
ATOM   5561 C  CD1  . PHE   B 1 116 ? 37.773 -19.394 -3.559  1.00 10.71 ?  116 PHE   B CD1  1 
ATOM   5562 C  CD2  . PHE   B 1 116 ? 37.420 -20.722 -5.498  1.00 10.20 ?  116 PHE   B CD2  1 
ATOM   5563 C  CE1  . PHE   B 1 116 ? 38.707 -20.333 -3.105  1.00 10.75 ?  116 PHE   B CE1  1 
ATOM   5564 C  CE2  . PHE   B 1 116 ? 38.348 -21.654 -5.053  1.00 10.32 ?  116 PHE   B CE2  1 
ATOM   5565 C  CZ   . PHE   B 1 116 ? 38.984 -21.463 -3.860  1.00 10.40 ?  116 PHE   B CZ   1 
ATOM   5566 H  H    . PHE   B 1 116 ? 35.395 -17.838 -3.054  1.00 11.60 ?  116 PHE   B H    1 
ATOM   5567 H  HA   . PHE   B 1 116 ? 36.991 -16.856 -4.875  1.00 12.02 ?  116 PHE   B HA   1 
ATOM   5568 H  HB2  . PHE   B 1 116 ? 35.179 -19.014 -5.089  1.00 11.64 ?  116 PHE   B HB2  1 
ATOM   5569 H  HB3  . PHE   B 1 116 ? 36.145 -18.613 -6.276  1.00 11.64 ?  116 PHE   B HB3  1 
ATOM   5570 H  HD1  . PHE   B 1 116 ? 37.577 -18.649 -3.040  1.00 12.82 ?  116 PHE   B HD1  1 
ATOM   5571 H  HD2  . PHE   B 1 116 ? 36.980 -20.872 -6.304  1.00 12.21 ?  116 PHE   B HD2  1 
ATOM   5572 H  HE1  . PHE   B 1 116 ? 39.147 -20.196 -2.295  1.00 12.87 ?  116 PHE   B HE1  1 
ATOM   5573 H  HE2  . PHE   B 1 116 ? 38.539 -22.406 -5.563  1.00 12.35 ?  116 PHE   B HE2  1 
ATOM   5574 H  HZ   . PHE   B 1 116 ? 39.621 -22.072 -3.563  1.00 12.45 ?  116 PHE   B HZ   1 
ATOM   5575 N  N    . ASN   B 1 117 ? 33.913 -16.162 -5.319  1.00 10.24 ?  117 ASN   B N    1 
ATOM   5576 C  CA   . ASN   B 1 117 ? 32.969 -15.460 -6.185  1.00 10.46 ?  117 ASN   B CA   1 
ATOM   5577 C  C    . ASN   B 1 117 ? 33.279 -13.980 -6.329  1.00 10.75 ?  117 ASN   B C    1 
ATOM   5578 O  O    . ASN   B 1 117 ? 32.681 -13.324 -7.183  1.00 11.87 ?  117 ASN   B O    1 
ATOM   5579 C  CB   . ASN   B 1 117 ? 31.547 -15.680 -5.691  1.00 10.67 ?  117 ASN   B CB   1 
ATOM   5580 C  CG   . ASN   B 1 117 ? 31.092 -17.084 -5.942  1.00 10.81 ?  117 ASN   B CG   1 
ATOM   5581 O  OD1  . ASN   B 1 117 ? 31.440 -17.677 -6.963  1.00 11.83 ?  117 ASN   B OD1  1 
ATOM   5582 N  ND2  . ASN   B 1 117 ? 30.357 -17.650 -4.998  1.00 11.18 ?  117 ASN   B ND2  1 
ATOM   5583 H  H    . ASN   B 1 117 ? 33.586 -16.425 -4.563  1.00 12.26 ?  117 ASN   B H    1 
ATOM   5584 H  HA   . ASN   B 1 117 ? 33.034 -15.854 -7.064  1.00 12.53 ?  117 ASN   B HA   1 
ATOM   5585 H  HB2  . ASN   B 1 117 ? 31.510 -15.511 -4.735  1.00 12.78 ?  117 ASN   B HB2  1 
ATOM   5586 H  HB3  . ASN   B 1 117 ? 30.956 -15.068 -6.159  1.00 12.78 ?  117 ASN   B HB3  1 
ATOM   5587 H  HD21 . ASN   B 1 117 ? 30.072 -18.453 -5.097  1.00 13.39 ?  117 ASN   B HD21 1 
ATOM   5588 H  HD22 . ASN   B 1 117 ? 30.141 -17.200 -4.294  1.00 13.39 ?  117 ASN   B HD22 1 
ATOM   5589 N  N    . GLN   B 1 118 ? 34.219 -13.452 -5.554  1.00 10.45 ?  118 GLN   B N    1 
ATOM   5590 C  CA   . GLN   B 1 118 ? 34.646 -12.066 -5.692  1.00 11.21 ?  118 GLN   B CA   1 
ATOM   5591 C  C    . GLN   B 1 118 ? 35.714 -11.878 -6.763  1.00 11.40 ?  118 GLN   B C    1 
ATOM   5592 O  O    . GLN   B 1 118 ? 36.186 -10.753 -6.946  1.00 12.51 ?  118 GLN   B O    1 
ATOM   5593 C  CB   . GLN   B 1 118 ? 35.125 -11.536 -4.339  1.00 11.69 ?  118 GLN   B CB   1 
ATOM   5594 C  CG   . GLN   B 1 118 ? 34.036 -11.577 -3.275  1.00 11.63 ?  118 GLN   B CG   1 
ATOM   5595 C  CD   . GLN   B 1 118 ? 32.866 -10.672 -3.608  1.00 11.66 ?  118 GLN   B CD   1 
ATOM   5596 O  OE1  . GLN   B 1 118 ? 33.054 -9.534  -4.055  1.00 12.50 ?  118 GLN   B OE1  1 
ATOM   5597 N  NE2  . GLN   B 1 118 ? 31.654 -11.164 -3.396  1.00 12.08 ?  118 GLN   B NE2  1 
ATOM   5598 H  H    . GLN   B 1 118 ? 34.646 -13.882 -4.937  1.00 12.51 ?  118 GLN   B H    1 
ATOM   5599 H  HA   . GLN   B 1 118 ? 33.880 -11.538 -5.962  1.00 13.43 ?  118 GLN   B HA   1 
ATOM   5600 H  HB2  . GLN   B 1 118 ? 35.869 -12.070 -4.031  1.00 14.00 ?  118 GLN   B HB2  1 
ATOM   5601 H  HB3  . GLN   B 1 118 ? 35.403 -10.608 -4.442  1.00 14.00 ?  118 GLN   B HB3  1 
ATOM   5602 H  HG2  . GLN   B 1 118 ? 33.704 -12.486 -3.198  1.00 13.93 ?  118 GLN   B HG2  1 
ATOM   5603 H  HG3  . GLN   B 1 118 ? 34.411 -11.289 -2.427  1.00 13.93 ?  118 GLN   B HG3  1 
ATOM   5604 H  HE21 . GLN   B 1 118 ? 31.566 -11.961 -3.082  1.00 14.47 ?  118 GLN   B HE21 1 
ATOM   5605 H  HE22 . GLN   B 1 118 ? 30.965 -10.688 -3.569  1.00 14.47 ?  118 GLN   B HE22 1 
ATOM   5606 N  N    . HIS   B 1 119 ? 36.066 -12.935 -7.496  1.00 10.76 ?  119 HIS   B N    1 
ATOM   5607 C  CA   . HIS   B 1 119 ? 37.108 -12.888 -8.512  1.00 11.18 ?  119 HIS   B CA   1 
ATOM   5608 C  C    . HIS   B 1 119 ? 36.634 -13.621 -9.751  1.00 11.04 ?  119 HIS   B C    1 
ATOM   5609 O  O    . HIS   B 1 119 ? 36.126 -14.737 -9.649  1.00 11.71 ?  119 HIS   B O    1 
ATOM   5610 C  CB   . HIS   B 1 119 ? 38.391 -13.510 -7.963  1.00 11.67 ?  119 HIS   B CB   1 
ATOM   5611 C  CG   . HIS   B 1 119 ? 38.869 -12.812 -6.737  1.00 12.70 ?  119 HIS   B CG   1 
ATOM   5612 N  ND1  . HIS   B 1 119 ? 39.668 -11.691 -6.789  1.00 14.42 ?  119 HIS   B ND1  1 
ATOM   5613 C  CD2  . HIS   B 1 119 ? 38.580 -13.014 -5.431  1.00 13.53 ?  119 HIS   B CD2  1 
ATOM   5614 C  CE1  . HIS   B 1 119 ? 39.879 -11.255 -5.560  1.00 15.52 ?  119 HIS   B CE1  1 
ATOM   5615 N  NE2  . HIS   B 1 119 ? 39.222 -12.032 -4.720  1.00 15.47 ?  119 HIS   B NE2  1 
ATOM   5616 H  H    . HIS   B 1 119 ? 35.702 -13.714 -7.422  1.00 12.88 ?  119 HIS   B H    1 
ATOM   5617 H  HA   . HIS   B 1 119 ? 37.287 -11.964 -8.751  1.00 13.39 ?  119 HIS   B HA   1 
ATOM   5618 H  HB2  . HIS   B 1 119 ? 38.224 -14.437 -7.744  1.00 13.98 ?  119 HIS   B HB2  1 
ATOM   5619 H  HB3  . HIS   B 1 119 ? 39.085 -13.446 -8.641  1.00 13.98 ?  119 HIS   B HB3  1 
ATOM   5620 H  HD2  . HIS   B 1 119 ? 38.047 -13.695 -5.084  1.00 16.21 ?  119 HIS   B HD2  1 
ATOM   5621 H  HE1  . HIS   B 1 119 ? 40.409 -10.527 -5.322  1.00 18.59 ?  119 HIS   B HE1  1 
ATOM   5622 H  HE2  . HIS   B 1 119 ? 39.226 -11.962 -3.862  1.00 18.54 ?  119 HIS   B HE2  1 
ATOM   5623 N  N    . GLU   B 1 120 ? 36.784 -13.001 -10.921 1.00 11.53 ?  120 GLU   B N    1 
ATOM   5624 C  CA   . GLU   B 1 120 ? 36.189 -13.579 -12.121 1.00 13.03 ?  120 GLU   B CA   1 
ATOM   5625 C  C    . GLU   B 1 120 ? 36.861 -14.881 -12.536 1.00 12.07 ?  120 GLU   B C    1 
ATOM   5626 O  O    . GLU   B 1 120 ? 36.196 -15.754 -13.105 1.00 12.16 ?  120 GLU   B O    1 
ATOM   5627 C  CB   . GLU   B 1 120 ? 36.205 -12.572 -13.269 1.00 17.68 ?  120 GLU   B CB   1 
ATOM   5628 C  CG   . GLU   B 1 120 ? 35.240 -11.420 -13.064 1.00 24.20 ?  120 GLU   B CG   1 
ATOM   5629 C  CD   . GLU   B 1 120 ? 35.086 -10.550 -14.295 1.00 30.81 ?  120 GLU   B CD   1 
ATOM   5630 O  OE1  . GLU   B 1 120 ? 36.083 -10.364 -15.024 1.00 32.96 ?  120 GLU   B OE1  1 
ATOM   5631 O  OE2  . GLU   B 1 120 ? 33.965 -10.054 -14.530 1.00 33.98 -1 120 GLU   B OE2  1 
ATOM   5632 H  H    . GLU   B 1 120 ? 37.207 -12.261 -11.047 1.00 13.81 ?  120 GLU   B H    1 
ATOM   5633 H  HA   . GLU   B 1 120 ? 35.264 -13.785 -11.935 1.00 15.61 ?  120 GLU   B HA   1 
ATOM   5634 H  HB2  . GLU   B 1 120 ? 37.094 -12.201 -13.357 1.00 21.19 ?  120 GLU   B HB2  1 
ATOM   5635 H  HB3  . GLU   B 1 120 ? 35.952 -13.025 -14.091 1.00 21.19 ?  120 GLU   B HB3  1 
ATOM   5636 H  HG2  . GLU   B 1 120 ? 34.364 -11.774 -12.841 1.00 29.02 ?  120 GLU   B HG2  1 
ATOM   5637 H  HG3  . GLU   B 1 120 ? 35.565 -10.859 -12.345 1.00 29.02 ?  120 GLU   B HG3  1 
ATOM   5638 N  N    . VAL   B 1 121 ? 38.161 -15.025 -12.276 1.00 11.59 ?  121 VAL   B N    1 
ATOM   5639 C  CA   . VAL   B 1 121 ? 38.909 -16.231 -12.625 1.00 11.40 ?  121 VAL   B CA   1 
ATOM   5640 C  C    . VAL   B 1 121 ? 40.021 -16.436 -11.604 1.00 10.90 ?  121 VAL   B C    1 
ATOM   5641 O  O    . VAL   B 1 121 ? 40.692 -15.481 -11.199 1.00 11.64 ?  121 VAL   B O    1 
ATOM   5642 C  CB   . VAL   B 1 121 ? 39.422 -16.181 -14.084 1.00 13.25 ?  121 VAL   B CB   1 
ATOM   5643 C  CG1  . VAL   B 1 121 ? 40.285 -14.953 -14.334 1.00 14.36 ?  121 VAL   B CG1  1 
ATOM   5644 C  CG2  . VAL   B 1 121 ? 40.164 -17.461 -14.440 1.00 14.57 ?  121 VAL   B CG2  1 
ATOM   5645 H  H    . VAL   B 1 121 ? 38.643 -14.420 -11.898 1.00 13.88 ?  121 VAL   B H    1 
ATOM   5646 H  HA   . VAL   B 1 121 ? 38.303 -16.984 -12.561 1.00 13.65 ?  121 VAL   B HA   1 
ATOM   5647 H  HB   . VAL   B 1 121 ? 38.654 -16.121 -14.678 1.00 15.88 ?  121 VAL   B HB   1 
ATOM   5648 H  HG11 . VAL   B 1 121 ? 40.595 -14.963 -15.255 1.00 17.21 ?  121 VAL   B HG11 1 
ATOM   5649 H  HG12 . VAL   B 1 121 ? 39.755 -14.154 -14.177 1.00 17.21 ?  121 VAL   B HG12 1 
ATOM   5650 H  HG13 . VAL   B 1 121 ? 41.045 -14.969 -13.732 1.00 17.21 ?  121 VAL   B HG13 1 
ATOM   5651 H  HG21 . VAL   B 1 121 ? 40.364 -17.453 -15.391 1.00 17.47 ?  121 VAL   B HG21 1 
ATOM   5652 H  HG22 . VAL   B 1 121 ? 40.989 -17.499 -13.932 1.00 17.47 ?  121 VAL   B HG22 1 
ATOM   5653 H  HG23 . VAL   B 1 121 ? 39.604 -18.221 -14.227 1.00 17.47 ?  121 VAL   B HG23 1 
ATOM   5654 N  N    . LEU   B 1 122 ? 40.207 -17.691 -11.179 1.00 10.45 ?  122 LEU   B N    1 
ATOM   5655 C  CA   . LEU   B 1 122 ? 41.185 -18.038 -10.153 1.00 9.95  ?  122 LEU   B CA   1 
ATOM   5656 C  C    . LEU   B 1 122 ? 41.841 -19.369 -10.475 1.00 10.04 ?  122 LEU   B C    1 
ATOM   5657 O  O    . LEU   B 1 122 ? 41.185 -20.289 -10.980 1.00 11.37 ?  122 LEU   B O    1 
ATOM   5658 C  CB   . LEU   B 1 122 ? 40.526 -18.274 -8.782  1.00 11.78 ?  122 LEU   B CB   1 
ATOM   5659 C  CG   . LEU   B 1 122 ? 39.502 -17.250 -8.288  1.00 12.09 ?  122 LEU   B CG   1 
ATOM   5660 C  CD1  . LEU   B 1 122 ? 38.104 -17.604 -8.761  1.00 12.93 ?  122 LEU   B CD1  1 
ATOM   5661 C  CD2  . LEU   B 1 122 ? 39.552 -17.141 -6.777  1.00 11.81 ?  122 LEU   B CD2  1 
ATOM   5662 H  H    . LEU   B 1 122 ? 39.768 -18.368 -11.476 1.00 12.52 ?  122 LEU   B H    1 
ATOM   5663 H  HA   . LEU   B 1 122 ? 41.864 -17.344 -10.075 1.00 11.91 ?  122 LEU   B HA   1 
ATOM   5664 H  HB2  . LEU   B 1 122 ? 40.074 -19.127 -8.817  1.00 14.11 ?  122 LEU   B HB2  1 
ATOM   5665 H  HB3  . LEU   B 1 122 ? 41.229 -18.309 -8.118  1.00 14.11 ?  122 LEU   B HB3  1 
ATOM   5666 H  HG   . LEU   B 1 122 ? 39.725 -16.379 -8.651  1.00 14.49 ?  122 LEU   B HG   1 
ATOM   5667 H  HD11 . LEU   B 1 122 ? 37.477 -16.955 -8.404  1.00 15.49 ?  122 LEU   B HD11 1 
ATOM   5668 H  HD12 . LEU   B 1 122 ? 38.085 -17.582 -9.730  1.00 15.49 ?  122 LEU   B HD12 1 
ATOM   5669 H  HD13 . LEU   B 1 122 ? 37.879 -18.491 -8.444  1.00 15.49 ?  122 LEU   B HD13 1 
ATOM   5670 H  HD21 . LEU   B 1 122 ? 38.876 -16.513 -6.479  1.00 14.15 ?  122 LEU   B HD21 1 
ATOM   5671 H  HD22 . LEU   B 1 122 ? 39.385 -18.015 -6.389  1.00 14.15 ?  122 LEU   B HD22 1 
ATOM   5672 H  HD23 . LEU   B 1 122 ? 40.433 -16.828 -6.510  1.00 14.15 ?  122 LEU   B HD23 1 
ATOM   5673 N  N    . LEU   B 1 123 ? 43.128 -19.473 -10.120 1.00 9.74  ?  123 LEU   B N    1 
ATOM   5674 C  CA   . LEU   B 1 123 ? 43.843 -20.741 -9.998  1.00 9.93  ?  123 LEU   B CA   1 
ATOM   5675 C  C    . LEU   B 1 123 ? 43.812 -21.137 -8.527  1.00 9.71  ?  123 LEU   B C    1 
ATOM   5676 O  O    . LEU   B 1 123 ? 44.160 -20.315 -7.670  1.00 10.30 ?  123 LEU   B O    1 
ATOM   5677 C  CB   . LEU   B 1 123 ? 45.292 -20.560 -10.458 1.00 10.54 ?  123 LEU   B CB   1 
ATOM   5678 C  CG   . LEU   B 1 123 ? 46.236 -21.741 -10.206 1.00 10.77 ?  123 LEU   B CG   1 
ATOM   5679 C  CD1  . LEU   B 1 123 ? 45.820 -22.990 -10.983 1.00 11.24 ?  123 LEU   B CD1  1 
ATOM   5680 C  CD2  . LEU   B 1 123 ? 47.652 -21.350 -10.569 1.00 11.74 ?  123 LEU   B CD2  1 
ATOM   5681 H  H    . LEU   B 1 123 ? 43.622 -18.795 -9.927  1.00 11.66 ?  123 LEU   B H    1 
ATOM   5682 H  HA   . LEU   B 1 123 ? 43.406 -21.431 -10.528 1.00 11.90 ?  123 LEU   B HA   1 
ATOM   5683 H  HB2  . LEU   B 1 123 ? 45.284 -20.401 -11.415 1.00 12.62 ?  123 LEU   B HB2  1 
ATOM   5684 H  HB3  . LEU   B 1 123 ? 45.661 -19.795 -10.002 1.00 12.62 ?  123 LEU   B HB3  1 
ATOM   5685 H  HG   . LEU   B 1 123 ? 46.224 -21.965 -9.262  1.00 12.90 ?  123 LEU   B HG   1 
ATOM   5686 H  HD11 . LEU   B 1 123 ? 46.455 -23.700 -10.802 1.00 13.47 ?  123 LEU   B HD11 1 
ATOM   5687 H  HD12 . LEU   B 1 123 ? 44.932 -23.259 -10.698 1.00 13.47 ?  123 LEU   B HD12 1 
ATOM   5688 H  HD13 . LEU   B 1 123 ? 45.816 -22.784 -11.931 1.00 13.47 ?  123 LEU   B HD13 1 
ATOM   5689 H  HD21 . LEU   B 1 123 ? 48.240 -22.105 -10.405 1.00 14.07 ?  123 LEU   B HD21 1 
ATOM   5690 H  HD22 . LEU   B 1 123 ? 47.681 -21.105 -11.506 1.00 14.07 ?  123 LEU   B HD22 1 
ATOM   5691 H  HD23 . LEU   B 1 123 ? 47.920 -20.597 -10.020 1.00 14.07 ?  123 LEU   B HD23 1 
ATOM   5692 N  N    . ALA   B 1 124 ? 43.379 -22.366 -8.221  1.00 9.78  ?  124 ALA   B N    1 
ATOM   5693 C  CA   . ALA   B 1 124 ? 43.127 -22.687 -6.824  1.00 10.01 ?  124 ALA   B CA   1 
ATOM   5694 C  C    . ALA   B 1 124 ? 43.398 -24.145 -6.492  1.00 9.84  ?  124 ALA   B C    1 
ATOM   5695 O  O    . ALA   B 1 124 ? 43.269 -25.021 -7.358  1.00 10.37 ?  124 ALA   B O    1 
ATOM   5696 C  CB   . ALA   B 1 124 ? 41.670 -22.368 -6.457  1.00 10.35 ?  124 ALA   B CB   1 
ATOM   5697 H  H    . ALA   B 1 124 ? 43.214 -23.003 -8.781  1.00 11.72 ?  124 ALA   B H    1 
ATOM   5698 H  HA   . ALA   B 1 124 ? 43.697 -22.134 -6.276  1.00 11.99 ?  124 ALA   B HA   1 
ATOM   5699 H  HB1  . ALA   B 1 124 ? 41.517 -22.586 -5.523  1.00 12.40 ?  124 ALA   B HB1  1 
ATOM   5700 H  HB2  . ALA   B 1 124 ? 41.506 -21.420 -6.603  1.00 12.40 ?  124 ALA   B HB2  1 
ATOM   5701 H  HB3  . ALA   B 1 124 ? 41.075 -22.892 -7.018  1.00 12.40 ?  124 ALA   B HB3  1 
ATOM   5702 N  N    . PRO   B 1 125 ? 43.695 -24.436 -5.229  1.00 10.04 ?  125 PRO   B N    1 
ATOM   5703 C  CA   . PRO   B 1 125 ? 43.635 -25.800 -4.708  1.00 10.66 ?  125 PRO   B CA   1 
ATOM   5704 C  C    . PRO   B 1 125 ? 42.235 -26.078 -4.165  1.00 10.56 ?  125 PRO   B C    1 
ATOM   5705 O  O    . PRO   B 1 125 ? 41.435 -25.165 -3.961  1.00 11.16 ?  125 PRO   B O    1 
ATOM   5706 C  CB   . PRO   B 1 125 ? 44.621 -25.722 -3.539  1.00 11.55 ?  125 PRO   B CB   1 
ATOM   5707 C  CG   . PRO   B 1 125 ? 44.360 -24.336 -2.965  1.00 11.46 ?  125 PRO   B CG   1 
ATOM   5708 C  CD   . PRO   B 1 125 ? 44.020 -23.465 -4.166  1.00 10.49 ?  125 PRO   B CD   1 
ATOM   5709 H  HA   . PRO   B 1 125 ? 43.911 -26.466 -5.357  1.00 12.77 ?  125 PRO   B HA   1 
ATOM   5710 H  HB2  . PRO   B 1 125 ? 44.422 -26.410 -2.880  1.00 13.83 ?  125 PRO   B HB2  1 
ATOM   5711 H  HB3  . PRO   B 1 125 ? 45.533 -25.800 -3.858  1.00 13.83 ?  125 PRO   B HB3  1 
ATOM   5712 H  HG2  . PRO   B 1 125 ? 43.612 -24.365 -2.346  1.00 13.73 ?  125 PRO   B HG2  1 
ATOM   5713 H  HG3  . PRO   B 1 125 ? 45.158 -24.005 -2.517  1.00 13.73 ?  125 PRO   B HG3  1 
ATOM   5714 H  HD2  . PRO   B 1 125 ? 43.256 -22.900 -3.972  1.00 12.57 ?  125 PRO   B HD2  1 
ATOM   5715 H  HD3  . PRO   B 1 125 ? 44.795 -22.930 -4.423  1.00 12.57 ?  125 PRO   B HD3  1 
ATOM   5716 N  N    . LEU   B 1 126 ? 41.966 -27.355 -3.891  1.00 11.23 ?  126 LEU   B N    1 
ATOM   5717 C  CA   . LEU   B 1 126 ? 40.746 -27.726 -3.182  1.00 11.66 ?  126 LEU   B CA   1 
ATOM   5718 C  C    . LEU   B 1 126 ? 40.860 -27.325 -1.720  1.00 12.13 ?  126 LEU   B C    1 
ATOM   5719 O  O    . LEU   B 1 126 ? 41.746 -27.787 -0.996  1.00 13.59 ?  126 LEU   B O    1 
ATOM   5720 C  CB   . LEU   B 1 126 ? 40.494 -29.222 -3.303  1.00 13.19 ?  126 LEU   B CB   1 
ATOM   5721 C  CG   . LEU   B 1 126 ? 39.958 -29.700 -4.653  1.00 13.90 ?  126 LEU   B CG   1 
ATOM   5722 C  CD1  . LEU   B 1 126 ? 40.004 -31.214 -4.737  1.00 15.56 ?  126 LEU   B CD1  1 
ATOM   5723 C  CD2  . LEU   B 1 126 ? 38.537 -29.200 -4.886  1.00 14.07 ?  126 LEU   B CD2  1 
ATOM   5724 H  H    . LEU   B 1 126 ? 42.475 -28.020 -4.095  1.00 13.46 ?  126 LEU   B H    1 
ATOM   5725 H  HA   . LEU   B 1 126 ? 39.995 -27.253 -3.574  1.00 13.97 ?  126 LEU   B HA   1 
ATOM   5726 H  HB2  . LEU   B 1 126 ? 41.328 -29.686 -3.141  1.00 15.80 ?  126 LEU   B HB2  1 
ATOM   5727 H  HB3  . LEU   B 1 126 ? 39.844 -29.477 -2.630  1.00 15.80 ?  126 LEU   B HB3  1 
ATOM   5728 H  HG   . LEU   B 1 126 ? 40.522 -29.345 -5.361  1.00 16.66 ?  126 LEU   B HG   1 
ATOM   5729 H  HD11 . LEU   B 1 126 ? 39.661 -31.493 -5.601  1.00 18.65 ?  126 LEU   B HD11 1 
ATOM   5730 H  HD12 . LEU   B 1 126 ? 40.921 -31.509 -4.633  1.00 18.65 ?  126 LEU   B HD12 1 
ATOM   5731 H  HD13 . LEU   B 1 126 ? 39.454 -31.584 -4.028  1.00 18.65 ?  126 LEU   B HD13 1 
ATOM   5732 H  HD21 . LEU   B 1 126 ? 38.183 -29.618 -5.687  1.00 16.86 ?  126 LEU   B HD21 1 
ATOM   5733 H  HD22 . LEU   B 1 126 ? 37.992 -29.434 -4.120  1.00 16.86 ?  126 LEU   B HD22 1 
ATOM   5734 H  HD23 . LEU   B 1 126 ? 38.555 -28.236 -4.998  1.00 16.86 ?  126 LEU   B HD23 1 
ATOM   5735 N  N    . LEU   B 1 127 ? 39.937 -26.488 -1.272  1.00 11.83 ?  127 LEU   B N    1 
ATOM   5736 C  CA   . LEU   B 1 127 ? 39.985 -25.998 0.093   1.00 12.11 ?  127 LEU   B CA   1 
ATOM   5737 C  C    . LEU   B 1 127 ? 39.715 -27.119 1.087   1.00 11.91 ?  127 LEU   B C    1 
ATOM   5738 O  O    . LEU   B 1 127 ? 38.896 -28.016 0.854   1.00 12.08 ?  127 LEU   B O    1 
ATOM   5739 C  CB   . LEU   B 1 127 ? 38.958 -24.885 0.295   1.00 12.46 ?  127 LEU   B CB   1 
ATOM   5740 C  CG   . LEU   B 1 127 ? 39.147 -23.616 -0.533  1.00 12.95 ?  127 LEU   B CG   1 
ATOM   5741 C  CD1  . LEU   B 1 127 ? 38.028 -22.641 -0.202  1.00 13.38 ?  127 LEU   B CD1  1 
ATOM   5742 C  CD2  . LEU   B 1 127 ? 40.510 -22.983 -0.284  1.00 13.82 ?  127 LEU   B CD2  1 
ATOM   5743 H  H    . LEU   B 1 127 ? 39.272 -26.186 -1.737  1.00 14.17 ?  127 LEU   B H    1 
ATOM   5744 H  HA   . LEU   B 1 127 ? 40.867 -25.635 0.268   1.00 14.50 ?  127 LEU   B HA   1 
ATOM   5745 H  HB2  . LEU   B 1 127 ? 38.080 -25.240 0.081   1.00 14.93 ?  127 LEU   B HB2  1 
ATOM   5746 H  HB3  . LEU   B 1 127 ? 38.977 -24.622 1.228   1.00 14.93 ?  127 LEU   B HB3  1 
ATOM   5747 H  HG   . LEU   B 1 127 ? 39.073 -23.831 -1.474  1.00 15.51 ?  127 LEU   B HG   1 
ATOM   5748 H  HD11 . LEU   B 1 127 ? 38.150 -21.827 -0.721  1.00 16.04 ?  127 LEU   B HD11 1 
ATOM   5749 H  HD12 . LEU   B 1 127 ? 37.174 -23.044 -0.418  1.00 16.04 ?  127 LEU   B HD12 1 
ATOM   5750 H  HD13 . LEU   B 1 127 ? 38.063 -22.428 0.747   1.00 16.04 ?  127 LEU   B HD13 1 
ATOM   5751 H  HD21 . LEU   B 1 127 ? 40.548 -22.120 -0.724  1.00 16.56 ?  127 LEU   B HD21 1 
ATOM   5752 H  HD22 . LEU   B 1 127 ? 40.639 -22.873 0.672   1.00 16.56 ?  127 LEU   B HD22 1 
ATOM   5753 H  HD23 . LEU   B 1 127 ? 41.196 -23.568 -0.643  1.00 16.56 ?  127 LEU   B HD23 1 
ATOM   5754 N  N    . SER   B 1 128 ? 40.403 -27.038 2.219   1.00 11.83 ?  128 SER   B N    1 
ATOM   5755 C  CA   . SER   B 1 128 ? 40.291 -27.954 3.343   1.00 12.31 ?  128 SER   B CA   1 
ATOM   5756 C  C    . SER   B 1 128 ? 40.783 -29.362 3.022   1.00 13.19 ?  128 SER   B C    1 
ATOM   5757 O  O    . SER   B 1 128 ? 40.696 -30.240 3.879   1.00 14.39 ?  128 SER   B O    1 
ATOM   5758 C  CB   . SER   B 1 128 ? 38.888 -27.963 3.967   1.00 12.70 ?  128 SER   B CB   1 
ATOM   5759 O  OG   . SER   B 1 128 ? 38.566 -26.692 4.518   1.00 13.45 ?  128 SER   B OG   1 
ATOM   5760 H  H    . SER   B 1 128 ? 40.976 -26.409 2.366   1.00 14.17 ?  128 SER   B H    1 
ATOM   5761 H  HA   . SER   B 1 128 ? 40.877 -27.619 4.031   1.00 14.75 ?  128 SER   B HA   1 
ATOM   5762 H  HB2  . SER   B 1 128 ? 38.233 -28.195 3.288   1.00 15.22 ?  128 SER   B HB2  1 
ATOM   5763 H  HB3  . SER   B 1 128 ? 38.864 -28.632 4.680   1.00 15.22 ?  128 SER   B HB3  1 
ATOM   5764 H  HG   . SER   B 1 128 ? 39.128 -26.488 5.106   1.00 16.11 ?  128 SER   B HG   1 
ATOM   5765 N  N    . ALA   B 1 129 ? 41.351 -29.585 1.836   1.00 14.18 ?  129 ALA   B N    1 
ATOM   5766 C  CA   . ALA   B 1 129 ? 41.894 -30.884 1.478   1.00 15.02 ?  129 ALA   B CA   1 
ATOM   5767 C  C    . ALA   B 1 129 ? 43.287 -31.057 2.070   1.00 14.14 ?  129 ALA   B C    1 
ATOM   5768 O  O    . ALA   B 1 129 ? 43.847 -30.155 2.708   1.00 14.28 ?  129 ALA   B O    1 
ATOM   5769 C  CB   . ALA   B 1 129 ? 41.934 -31.042 -0.040  1.00 17.02 ?  129 ALA   B CB   1 
ATOM   5770 H  H    . ALA   B 1 129 ? 41.432 -28.990 1.216   1.00 17.00 ?  129 ALA   B H    1 
ATOM   5771 H  HA   . ALA   B 1 129 ? 41.322 -31.576 1.837   1.00 18.00 ?  129 ALA   B HA   1 
ATOM   5772 H  HB1  . ALA   B 1 129 ? 42.289 -31.918 -0.258  1.00 20.40 ?  129 ALA   B HB1  1 
ATOM   5773 H  HB2  . ALA   B 1 129 ? 41.033 -30.955 -0.390  1.00 20.40 ?  129 ALA   B HB2  1 
ATOM   5774 H  HB3  . ALA   B 1 129 ? 42.503 -30.352 -0.416  1.00 20.40 ?  129 ALA   B HB3  1 
ATOM   5775 N  N    . GLY   B 1 130 ? 43.845 -32.241 1.843   1.00 14.44 ?  130 GLY   B N    1 
ATOM   5776 C  CA   . GLY   B 1 130 ? 45.231 -32.482 2.192   1.00 14.83 ?  130 GLY   B CA   1 
ATOM   5777 C  C    . GLY   B 1 130 ? 45.446 -32.384 3.684   1.00 14.95 ?  130 GLY   B C    1 
ATOM   5778 O  O    . GLY   B 1 130 ? 44.753 -33.030 4.484   1.00 15.68 ?  130 GLY   B O    1 
ATOM   5779 H  H    . GLY   B 1 130 ? 43.446 -32.915 1.483   1.00 17.30 ?  130 GLY   B H    1 
ATOM   5780 H  HA2  . GLY   B 1 130 ? 45.492 -33.371 1.899   1.00 17.77 ?  130 GLY   B HA2  1 
ATOM   5781 H  HA3  . GLY   B 1 130 ? 45.798 -31.832 1.751   1.00 17.77 ?  130 GLY   B HA3  1 
ATOM   5782 N  N    . ILE   B 1 131 ? 46.420 -31.554 4.069   1.00 15.13 ?  131 ILE   B N    1 
ATOM   5783 C  CA   . ILE   B 1 131 ? 46.778 -31.419 5.474   1.00 15.96 ?  131 ILE   B CA   1 
ATOM   5784 C  C    . ILE   B 1 131 ? 45.662 -30.817 6.309   1.00 15.43 ?  131 ILE   B C    1 
ATOM   5785 O  O    . ILE   B 1 131 ? 45.738 -30.883 7.540   1.00 16.73 ?  131 ILE   B O    1 
ATOM   5786 C  CB   . ILE   B 1 131 ? 48.103 -30.647 5.665   1.00 17.99 ?  131 ILE   B CB   1 
ATOM   5787 C  CG1  . ILE   B 1 131 ? 47.940 -29.168 5.287   1.00 18.98 ?  131 ILE   B CG1  1 
ATOM   5788 C  CG2  . ILE   B 1 131 ? 49.216 -31.296 4.850   1.00 19.08 ?  131 ILE   B CG2  1 
ATOM   5789 C  CD1  . ILE   B 1 131 ? 49.153 -28.313 5.616   1.00 20.03 ?  131 ILE   B CD1  1 
ATOM   5790 H  H    . ILE   B 1 131 ? 46.887 -31.065 3.535   1.00 18.14 ?  131 ILE   B H    1 
ATOM   5791 H  HA   . ILE   B 1 131 ? 46.921 -32.310 5.821   1.00 19.12 ?  131 ILE   B HA   1 
ATOM   5792 H  HB   . ILE   B 1 131 ? 48.342 -30.696 6.604   1.00 21.56 ?  131 ILE   B HB   1 
ATOM   5793 H  HG12 . ILE   B 1 131 ? 47.780 -29.107 4.333   1.00 22.75 ?  131 ILE   B HG12 1 
ATOM   5794 H  HG13 . ILE   B 1 131 ? 47.184 -28.794 5.769   1.00 22.75 ?  131 ILE   B HG13 1 
ATOM   5795 H  HG21 . ILE   B 1 131 ? 50.059 -30.897 5.105   1.00 22.87 ?  131 ILE   B HG21 1 
ATOM   5796 H  HG22 . ILE   B 1 131 ? 49.223 -32.245 5.036   1.00 22.87 ?  131 ILE   B HG22 1 
ATOM   5797 H  HG23 . ILE   B 1 131 ? 49.042 -31.141 3.909   1.00 22.87 ?  131 ILE   B HG23 1 
ATOM   5798 H  HD11 . ILE   B 1 131 ? 48.942 -27.385 5.434   1.00 24.02 ?  131 ILE   B HD11 1 
ATOM   5799 H  HD12 . ILE   B 1 131 ? 49.372 -28.426 6.554   1.00 24.02 ?  131 ILE   B HD12 1 
ATOM   5800 H  HD13 . ILE   B 1 131 ? 49.898 -28.598 5.065   1.00 24.02 ?  131 ILE   B HD13 1 
ATOM   5801 N  N    . PHE   B 1 132 ? 44.631 -30.236 5.678   1.00 14.35 ?  132 PHE   B N    1 
ATOM   5802 C  CA   . PHE   B 1 132 ? 43.468 -29.738 6.405   1.00 14.28 ?  132 PHE   B CA   1 
ATOM   5803 C  C    . PHE   B 1 132 ? 42.448 -30.831 6.728   1.00 15.69 ?  132 PHE   B C    1 
ATOM   5804 O  O    . PHE   B 1 132 ? 41.537 -30.587 7.528   1.00 17.45 ?  132 PHE   B O    1 
ATOM   5805 C  CB   . PHE   B 1 132 ? 42.795 -28.598 5.629   1.00 13.50 ?  132 PHE   B CB   1 
ATOM   5806 C  CG   . PHE   B 1 132 ? 43.498 -27.258 5.742   1.00 13.24 ?  132 PHE   B CG   1 
ATOM   5807 C  CD1  . PHE   B 1 132 ? 44.796 -27.081 5.280   1.00 14.48 ?  132 PHE   B CD1  1 
ATOM   5808 C  CD2  . PHE   B 1 132 ? 42.828 -26.159 6.258   1.00 12.87 ?  132 PHE   B CD2  1 
ATOM   5809 C  CE1  . PHE   B 1 132 ? 45.419 -25.843 5.374   1.00 14.98 ?  132 PHE   B CE1  1 
ATOM   5810 C  CE2  . PHE   B 1 132 ? 43.440 -24.922 6.349   1.00 13.28 ?  132 PHE   B CE2  1 
ATOM   5811 C  CZ   . PHE   B 1 132 ? 44.735 -24.764 5.905   1.00 14.20 ?  132 PHE   B CZ   1 
ATOM   5812 H  H    . PHE   B 1 132 ? 44.587 -30.119 4.822   1.00 17.19 ?  132 PHE   B H    1 
ATOM   5813 H  HA   . PHE   B 1 132 ? 43.776 -29.369 7.244   1.00 17.12 ?  132 PHE   B HA   1 
ATOM   5814 H  HB2  . PHE   B 1 132 ? 42.775 -28.834 4.691   1.00 16.17 ?  132 PHE   B HB2  1 
ATOM   5815 H  HB3  . PHE   B 1 132 ? 41.891 -28.486 5.962   1.00 16.17 ?  132 PHE   B HB3  1 
ATOM   5816 H  HD1  . PHE   B 1 132 ? 45.262 -27.806 4.928   1.00 17.35 ?  132 PHE   B HD1  1 
ATOM   5817 H  HD2  . PHE   B 1 132 ? 41.954 -26.259 6.560   1.00 15.42 ?  132 PHE   B HD2  1 
ATOM   5818 H  HE1  . PHE   B 1 132 ? 46.295 -25.740 5.076   1.00 17.95 ?  132 PHE   B HE1  1 
ATOM   5819 H  HE2  . PHE   B 1 132 ? 42.980 -24.195 6.710   1.00 15.92 ?  132 PHE   B HE2  1 
ATOM   5820 H  HZ   . PHE   B 1 132 ? 45.152 -23.931 5.970   1.00 17.01 ?  132 PHE   B HZ   1 
ATOM   5821 N  N    . GLY   B 1 133 ? 42.566 -32.022 6.131   1.00 15.61 ?  133 GLY   B N    1 
ATOM   5822 C  CA   . GLY   B 1 133 ? 41.860 -33.194 6.616   1.00 16.53 ?  133 GLY   B CA   1 
ATOM   5823 C  C    . GLY   B 1 133 ? 40.463 -33.454 6.085   1.00 16.77 ?  133 GLY   B C    1 
ATOM   5824 O  O    . GLY   B 1 133 ? 39.877 -34.480 6.449   1.00 18.95 ?  133 GLY   B O    1 
ATOM   5825 H  H    . GLY   B 1 133 ? 43.061 -32.171 5.440   1.00 18.71 ?  133 GLY   B H    1 
ATOM   5826 H  HA2  . GLY   B 1 133 ? 42.395 -33.976 6.413   1.00 19.81 ?  133 GLY   B HA2  1 
ATOM   5827 H  HA3  . GLY   B 1 133 ? 41.791 -33.127 7.579   1.00 19.81 ?  133 GLY   B HA3  1 
ATOM   5828 N  N    . ALA   B 1 134 ? 39.900 -32.583 5.256   1.00 15.91 ?  134 ALA   B N    1 
ATOM   5829 C  CA   . ALA   B 1 134 ? 38.574 -32.861 4.723   1.00 15.98 ?  134 ALA   B CA   1 
ATOM   5830 C  C    . ALA   B 1 134 ? 38.656 -33.858 3.572   1.00 16.14 ?  134 ALA   B C    1 
ATOM   5831 O  O    . ALA   B 1 134 ? 39.709 -34.054 2.960   1.00 16.90 ?  134 ALA   B O    1 
ATOM   5832 C  CB   . ALA   B 1 134 ? 37.901 -31.577 4.246   1.00 16.32 ?  134 ALA   B CB   1 
ATOM   5833 H  H    . ALA   B 1 134 ? 40.253 -31.838 4.994   1.00 19.07 ?  134 ALA   B H    1 
ATOM   5834 H  HA   . ALA   B 1 134 ? 38.026 -33.245 5.423   1.00 19.15 ?  134 ALA   B HA   1 
ATOM   5835 H  HB1  . ALA   B 1 134 ? 37.015 -31.791 3.916   1.00 19.56 ?  134 ALA   B HB1  1 
ATOM   5836 H  HB2  . ALA   B 1 134 ? 37.836 -30.957 4.990   1.00 19.56 ?  134 ALA   B HB2  1 
ATOM   5837 H  HB3  . ALA   B 1 134 ? 38.433 -31.185 3.536   1.00 19.56 ?  134 ALA   B HB3  1 
ATOM   5838 N  N    . ASP   B 1 135 ? 37.522 -34.480 3.281   1.00 16.10 ?  135 ASP   B N    1 
ATOM   5839 C  CA   . ASP   B 1 135 ? 37.426 -35.376 2.139   1.00 17.06 ?  135 ASP   B CA   1 
ATOM   5840 C  C    . ASP   B 1 135 ? 37.523 -34.541 0.869   1.00 15.76 ?  135 ASP   B C    1 
ATOM   5841 O  O    . ASP   B 1 135 ? 36.668 -33.673 0.646   1.00 15.73 ?  135 ASP   B O    1 
ATOM   5842 C  CB   . ASP   B 1 135 ? 36.085 -36.110 2.194   1.00 18.81 ?  135 ASP   B CB   1 
ATOM   5843 C  CG   . ASP   B 1 135 ? 35.899 -37.096 1.055   1.00 21.05 ?  135 ASP   B CG   1 
ATOM   5844 O  OD1  . ASP   B 1 135 ? 36.765 -37.159 0.158   1.00 20.61 ?  135 ASP   B OD1  1 
ATOM   5845 O  OD2  . ASP   B 1 135 ? 34.884 -37.834 1.068   1.00 23.80 -1 135 ASP   B OD2  1 
ATOM   5846 H  H    . ASP   B 1 135 ? 36.793 -34.395 3.727   1.00 19.29 ?  135 ASP   B H    1 
ATOM   5847 H  HA   . ASP   B 1 135 ? 38.146 -36.027 2.171   1.00 20.45 ?  135 ASP   B HA   1 
ATOM   5848 H  HB2  . ASP   B 1 135 ? 36.035 -36.604 3.024   1.00 22.55 ?  135 ASP   B HB2  1 
ATOM   5849 H  HB3  . ASP   B 1 135 ? 35.373 -35.456 2.147   1.00 22.55 ?  135 ASP   B HB3  1 
ATOM   5850 N  N    . PRO   B 1 136 ? 38.534 -34.745 0.022   1.00 15.85 ?  136 PRO   B N    1 
ATOM   5851 C  CA   . PRO   B 1 136 ? 38.631 -33.922 -1.194  1.00 15.11 ?  136 PRO   B CA   1 
ATOM   5852 C  C    . PRO   B 1 136 ? 37.443 -34.078 -2.121  1.00 14.37 ?  136 PRO   B C    1 
ATOM   5853 O  O    . PRO   B 1 136 ? 37.118 -33.130 -2.845  1.00 13.54 ?  136 PRO   B O    1 
ATOM   5854 C  CB   . PRO   B 1 136 ? 39.943 -34.391 -1.840  1.00 16.23 ?  136 PRO   B CB   1 
ATOM   5855 C  CG   . PRO   B 1 136 ? 40.148 -35.784 -1.306  1.00 17.49 ?  136 PRO   B CG   1 
ATOM   5856 C  CD   . PRO   B 1 136 ? 39.605 -35.753 0.094   1.00 16.87 ?  136 PRO   B CD   1 
ATOM   5857 H  HA   . PRO   B 1 136 ? 38.717 -32.986 -0.955  1.00 18.11 ?  136 PRO   B HA   1 
ATOM   5858 H  HB2  . PRO   B 1 136 ? 39.849 -34.403 -2.807  1.00 19.45 ?  136 PRO   B HB2  1 
ATOM   5859 H  HB3  . PRO   B 1 136 ? 40.668 -33.807 -1.573  1.00 19.45 ?  136 PRO   B HB3  1 
ATOM   5860 H  HG2  . PRO   B 1 136 ? 39.658 -36.421 -1.849  1.00 20.96 ?  136 PRO   B HG2  1 
ATOM   5861 H  HG3  . PRO   B 1 136 ? 41.096 -35.996 -1.300  1.00 20.96 ?  136 PRO   B HG3  1 
ATOM   5862 H  HD2  . PRO   B 1 136 ? 39.239 -36.619 0.336   1.00 20.22 ?  136 PRO   B HD2  1 
ATOM   5863 H  HD3  . PRO   B 1 136 ? 40.290 -35.470 0.723   1.00 20.22 ?  136 PRO   B HD3  1 
ATOM   5864 N  N    . ILE   B 1 137 ? 36.788 -35.245 -2.130  1.00 14.94 ?  137 ILE   B N    1 
ATOM   5865 C  CA   . ILE   B 1 137 ? 35.573 -35.406 -2.923  1.00 15.40 ?  137 ILE   B CA   1 
ATOM   5866 C  C    . ILE   B 1 137 ? 34.500 -34.437 -2.444  1.00 15.01 ?  137 ILE   B C    1 
ATOM   5867 O  O    . ILE   B 1 137 ? 33.784 -33.825 -3.246  1.00 14.64 ?  137 ILE   B O    1 
ATOM   5868 C  CB   . ILE   B 1 137 ? 35.097 -36.872 -2.871  1.00 17.55 ?  137 ILE   B CB   1 
ATOM   5869 C  CG1  . ILE   B 1 137 ? 36.094 -37.771 -3.607  1.00 20.22 ?  137 ILE   B CG1  1 
ATOM   5870 C  CG2  . ILE   B 1 137 ? 33.691 -37.010 -3.455  1.00 17.99 ?  137 ILE   B CG2  1 
ATOM   5871 C  CD1  . ILE   B 1 137 ? 35.783 -39.252 -3.501  1.00 22.74 ?  137 ILE   B CD1  1 
ATOM   5872 H  H    . ILE   B 1 137 ? 37.023 -35.945 -1.695  1.00 17.90 ?  137 ILE   B H    1 
ATOM   5873 H  HA   . ILE   B 1 137 ? 35.768 -35.194 -3.850  1.00 18.46 ?  137 ILE   B HA   1 
ATOM   5874 H  HB   . ILE   B 1 137 ? 35.064 -37.149 -1.948  1.00 21.04 ?  137 ILE   B HB   1 
ATOM   5875 H  HG12 . ILE   B 1 137 ? 36.095 -37.538 -4.549  1.00 24.25 ?  137 ILE   B HG12 1 
ATOM   5876 H  HG13 . ILE   B 1 137 ? 36.977 -37.629 -3.233  1.00 24.25 ?  137 ILE   B HG13 1 
ATOM   5877 H  HG21 . ILE   B 1 137 ? 33.467 -37.951 -3.543  1.00 21.57 ?  137 ILE   B HG21 1 
ATOM   5878 H  HG22 . ILE   B 1 137 ? 33.055 -36.585 -2.860  1.00 21.57 ?  137 ILE   B HG22 1 
ATOM   5879 H  HG23 . ILE   B 1 137 ? 33.666 -36.586 -4.327  1.00 21.57 ?  137 ILE   B HG23 1 
ATOM   5880 H  HD11 . ILE   B 1 137 ? 36.519 -39.750 -3.886  1.00 27.26 ?  137 ILE   B HD11 1 
ATOM   5881 H  HD12 . ILE   B 1 137 ? 35.674 -39.488 -2.566  1.00 27.26 ?  137 ILE   B HD12 1 
ATOM   5882 H  HD13 . ILE   B 1 137 ? 34.967 -39.446 -3.989  1.00 27.26 ?  137 ILE   B HD13 1 
ATOM   5883 N  N    . HIS   B 1 138 ? 34.367 -34.289 -1.128  1.00 15.13 ?  138 HIS   B N    1 
ATOM   5884 C  CA   . HIS   B 1 138 ? 33.417 -33.324 -0.591  1.00 15.44 ?  138 HIS   B CA   1 
ATOM   5885 C  C    . HIS   B 1 138 ? 33.836 -31.894 -0.906  1.00 14.23 ?  138 HIS   B C    1 
ATOM   5886 O  O    . HIS   B 1 138 ? 32.989 -31.047 -1.211  1.00 14.68 ?  138 HIS   B O    1 
ATOM   5887 C  CB   . HIS   B 1 138 ? 33.290 -33.507 0.914   1.00 16.89 ?  138 HIS   B CB   1 
ATOM   5888 C  CG   . HIS   B 1 138 ? 32.357 -32.528 1.548   1.00 17.97 ?  138 HIS   B CG   1 
ATOM   5889 N  ND1  . HIS   B 1 138 ? 31.016 -32.472 1.236   1.00 19.43 ?  138 HIS   B ND1  1 
ATOM   5890 C  CD2  . HIS   B 1 138 ? 32.574 -31.546 2.455   1.00 18.47 ?  138 HIS   B CD2  1 
ATOM   5891 C  CE1  . HIS   B 1 138 ? 30.443 -31.508 1.934   1.00 19.47 ?  138 HIS   B CE1  1 
ATOM   5892 N  NE2  . HIS   B 1 138 ? 31.367 -30.931 2.682   1.00 18.80 ?  138 HIS   B NE2  1 
ATOM   5893 H  H    . HIS   B 1 138 ? 34.808 -34.733 -0.541  1.00 18.13 ?  138 HIS   B H    1 
ATOM   5894 H  HA   . HIS   B 1 138 ? 32.545 -33.484 -0.991  1.00 18.51 ?  138 HIS   B HA   1 
ATOM   5895 H  HB2  . HIS   B 1 138 ? 32.950 -34.397 1.097   1.00 20.24 ?  138 HIS   B HB2  1 
ATOM   5896 H  HB3  . HIS   B 1 138 ? 34.161 -33.392 1.319   1.00 20.24 ?  138 HIS   B HB3  1 
ATOM   5897 H  HD1  . HIS   B 1 138 ? 30.612 -32.991 0.677   1.00 23.29 ?  138 HIS   B HD1  1 
ATOM   5898 H  HD2  . HIS   B 1 138 ? 33.380 -31.330 2.857   1.00 22.14 ?  138 HIS   B HD2  1 
ATOM   5899 H  HE1  . HIS   B 1 138 ? 29.536 -31.282 1.905   1.00 23.34 ?  138 HIS   B HE1  1 
ATOM   5900 N  N    . SER   B 1 139 ? 35.128 -31.595 -0.827  1.00 13.82 ?  139 SER   B N    1 
ATOM   5901 C  CA   . SER   B 1 139 ? 35.563 -30.243 -1.143  1.00 13.29 ?  139 SER   B CA   1 
ATOM   5902 C  C    . SER   B 1 139 ? 35.229 -29.895 -2.583  1.00 12.60 ?  139 SER   B C    1 
ATOM   5903 O  O    . SER   B 1 139 ? 34.781 -28.780 -2.866  1.00 12.47 ?  139 SER   B O    1 
ATOM   5904 C  CB   . SER   B 1 139 ? 37.055 -30.105 -0.875  1.00 13.51 ?  139 SER   B CB   1 
ATOM   5905 O  OG   . SER   B 1 139 ? 37.465 -28.781 -1.147  1.00 13.64 ?  139 SER   B OG   1 
ATOM   5906 H  H    . SER   B 1 139 ? 35.751 -32.141 -0.609  1.00 16.56 ?  139 SER   B H    1 
ATOM   5907 H  HA   . SER   B 1 139 ? 35.090 -29.621 -0.572  1.00 15.92 ?  139 SER   B HA   1 
ATOM   5908 H  HB2  . SER   B 1 139 ? 37.229 -30.304 0.057   1.00 16.19 ?  139 SER   B HB2  1 
ATOM   5909 H  HB3  . SER   B 1 139 ? 37.542 -30.716 -1.448  1.00 16.19 ?  139 SER   B HB3  1 
ATOM   5910 H  HG   . SER   B 1 139 ? 38.292 -28.698 -1.003  1.00 16.34 ?  139 SER   B HG   1 
ATOM   5911 N  N    . LEU   B 1 140 ? 35.418 -30.838 -3.507  1.00 12.54 ?  140 LEU   B N    1 
ATOM   5912 C  CA   . LEU   B 1 140 ? 35.051 -30.593 -4.895  1.00 12.64 ?  140 LEU   B CA   1 
ATOM   5913 C  C    . LEU   B 1 140 ? 33.548 -30.363 -5.025  1.00 12.72 ?  140 LEU   B C    1 
ATOM   5914 O  O    . LEU   B 1 140 ? 33.111 -29.470 -5.757  1.00 12.62 ?  140 LEU   B O    1 
ATOM   5915 C  CB   . LEU   B 1 140 ? 35.523 -31.751 -5.775  1.00 12.40 ?  140 LEU   B CB   1 
ATOM   5916 C  CG   . LEU   B 1 140 ? 35.148 -31.641 -7.245  1.00 12.61 ?  140 LEU   B CG   1 
ATOM   5917 C  CD1  . LEU   B 1 140 ? 35.721 -30.372 -7.846  1.00 13.37 ?  140 LEU   B CD1  1 
ATOM   5918 C  CD2  . LEU   B 1 140 ? 35.616 -32.863 -8.004  1.00 13.85 ?  140 LEU   B CD2  1 
ATOM   5919 H  H    . LEU   B 1 140 ? 35.744 -31.617 -3.358  1.00 15.02 ?  140 LEU   B H    1 
ATOM   5920 H  HA   . LEU   B 1 140 ? 35.504 -29.787 -5.198  1.00 15.14 ?  140 LEU   B HA   1 
ATOM   5921 H  HB2  . LEU   B 1 140 ? 36.492 -31.802 -5.726  1.00 14.85 ?  140 LEU   B HB2  1 
ATOM   5922 H  HB3  . LEU   B 1 140 ? 35.136 -32.572 -5.440  1.00 14.85 ?  140 LEU   B HB3  1 
ATOM   5923 H  HG   . LEU   B 1 140 ? 34.183 -31.588 -7.321  1.00 15.10 ?  140 LEU   B HG   1 
ATOM   5924 H  HD11 . LEU   B 1 140 ? 35.597 -30.397 -8.807  1.00 16.02 ?  140 LEU   B HD11 1 
ATOM   5925 H  HD12 . LEU   B 1 140 ? 35.256 -29.604 -7.474  1.00 16.02 ?  140 LEU   B HD12 1 
ATOM   5926 H  HD13 . LEU   B 1 140 ? 36.666 -30.321 -7.635  1.00 16.02 ?  140 LEU   B HD13 1 
ATOM   5927 H  HD21 . LEU   B 1 140 ? 35.358 -32.764 -8.936  1.00 16.60 ?  140 LEU   B HD21 1 
ATOM   5928 H  HD22 . LEU   B 1 140 ? 36.574 -32.932 -7.928  1.00 16.60 ?  140 LEU   B HD22 1 
ATOM   5929 H  HD23 . LEU   B 1 140 ? 35.186 -33.643 -7.623  1.00 16.60 ?  140 LEU   B HD23 1 
ATOM   5930 N  N    . ARG   B 1 141 ? 32.748 -31.155 -4.311  1.00 12.69 ?  141 ARG   B N    1 
ATOM   5931 C  CA   . ARG   B 1 141 ? 31.298 -30.979 -4.294  1.00 13.83 ?  141 ARG   B CA   1 
ATOM   5932 C  C    . ARG   B 1 141 ? 30.920 -29.567 -3.868  1.00 13.26 ?  141 ARG   B C    1 
ATOM   5933 O  O    . ARG   B 1 141 ? 30.109 -28.895 -4.525  1.00 13.38 ?  141 ARG   B O    1 
ATOM   5934 C  CB   . ARG   B 1 141 ? 30.718 -32.005 -3.312  1.00 15.47 ?  141 ARG   B CB   1 
ATOM   5935 C  CG   . ARG   B 1 141 ? 29.251 -31.891 -2.984  1.00 17.65 ?  141 ARG   B CG   1 
ATOM   5936 C  CD   . ARG   B 1 141 ? 28.444 -32.526 -4.049  1.00 19.44 ?  141 ARG   B CD   1 
ATOM   5937 N  NE   . ARG   B 1 141 ? 28.181 -31.615 -5.152  1.00 20.04 ?  141 ARG   B NE   1 
ATOM   5938 C  CZ   . ARG   B 1 141 ? 28.176 -31.965 -6.430  1.00 19.46 ?  141 ARG   B CZ   1 
ATOM   5939 N  NH1  . ARG   B 1 141 ? 28.614 -33.151 -6.826  1.00 19.09 ?  141 ARG   B NH1  1 
ATOM   5940 N  NH2  . ARG   B 1 141 ? 27.721 -31.102 -7.335  1.00 20.41 ?  141 ARG   B NH2  1 
ATOM   5941 H  H    . ARG   B 1 141 ? 33.029 -31.803 -3.825  1.00 15.20 ?  141 ARG   B H    1 
ATOM   5942 H  HA   . ARG   B 1 141 ? 30.936 -31.148 -5.176  1.00 16.57 ?  141 ARG   B HA   1 
ATOM   5943 H  HB2  . ARG   B 1 141 ? 30.871 -32.892 -3.678  1.00 18.55 ?  141 ARG   B HB2  1 
ATOM   5944 H  HB3  . ARG   B 1 141 ? 31.203 -31.928 -2.476  1.00 18.55 ?  141 ARG   B HB3  1 
ATOM   5945 H  HG2  . ARG   B 1 141 ? 29.080 -32.343 -2.147  1.00 21.16 ?  141 ARG   B HG2  1 
ATOM   5946 H  HG3  . ARG   B 1 141 ? 28.998 -30.954 -2.916  1.00 21.16 ?  141 ARG   B HG3  1 
ATOM   5947 H  HD2  . ARG   B 1 141 ? 28.921 -33.304 -4.388  1.00 23.30 ?  141 ARG   B HD2  1 
ATOM   5948 H  HD3  . ARG   B 1 141 ? 27.600 -32.806 -3.673  1.00 23.30 ?  141 ARG   B HD3  1 
ATOM   5949 H  HE   . ARG   B 1 141 ? 27.995 -30.798 -4.959  1.00 24.02 ?  141 ARG   B HE   1 
ATOM   5950 H  HH11 . ARG   B 1 141 ? 28.902 -33.723 -6.254  1.00 22.89 ?  141 ARG   B HH11 1 
ATOM   5951 H  HH12 . ARG   B 1 141 ? 28.613 -33.347 -7.661  1.00 22.89 ?  141 ARG   B HH12 1 
ATOM   5952 H  HH21 . ARG   B 1 141 ? 27.439 -30.326 -7.090  1.00 24.47 ?  141 ARG   B HH21 1 
ATOM   5953 H  HH22 . ARG   B 1 141 ? 27.733 -31.307 -8.171  1.00 24.47 ?  141 ARG   B HH22 1 
ATOM   5954 N  N    . VAL   B 1 142 ? 31.460 -29.121 -2.736  1.00 12.82 ?  142 VAL   B N    1 
ATOM   5955 C  CA   . VAL   B 1 142 ? 31.130 -27.789 -2.251  1.00 12.78 ?  142 VAL   B CA   1 
ATOM   5956 C  C    . VAL   B 1 142 ? 31.606 -26.731 -3.236  1.00 12.54 ?  142 VAL   B C    1 
ATOM   5957 O  O    . VAL   B 1 142 ? 30.908 -25.744 -3.489  1.00 13.04 ?  142 VAL   B O    1 
ATOM   5958 C  CB   . VAL   B 1 142 ? 31.675 -27.563 -0.828  1.00 13.55 ?  142 VAL   B CB   1 
ATOM   5959 C  CG1  . VAL   B 1 142 ? 31.353 -26.146 -0.354  1.00 13.38 ?  142 VAL   B CG1  1 
ATOM   5960 C  CG2  . VAL   B 1 142 ? 31.103 -28.593 0.128   1.00 14.39 ?  142 VAL   B CG2  1 
ATOM   5961 H  H    . VAL   B 1 142 ? 32.017 -29.558 -2.243  1.00 15.36 ?  142 VAL   B H    1 
ATOM   5962 H  HA   . VAL   B 1 142 ? 30.168 -27.718 -2.198  1.00 15.31 ?  142 VAL   B HA   1 
ATOM   5963 H  HB   . VAL   B 1 142 ? 32.641 -27.662 -0.837  1.00 16.24 ?  142 VAL   B HB   1 
ATOM   5964 H  HG11 . VAL   B 1 142 ? 31.537 -26.084 0.595   1.00 16.03 ?  142 VAL   B HG11 1 
ATOM   5965 H  HG12 . VAL   B 1 142 ? 31.912 -25.515 -0.839  1.00 16.03 ?  142 VAL   B HG12 1 
ATOM   5966 H  HG13 . VAL   B 1 142 ? 30.419 -25.961 -0.526  1.00 16.03 ?  142 VAL   B HG13 1 
ATOM   5967 H  HG21 . VAL   B 1 142 ? 31.420 -28.400 1.023   1.00 17.24 ?  142 VAL   B HG21 1 
ATOM   5968 H  HG22 . VAL   B 1 142 ? 30.136 -28.542 0.099   1.00 17.24 ?  142 VAL   B HG22 1 
ATOM   5969 H  HG23 . VAL   B 1 142 ? 31.399 -29.474 -0.147  1.00 17.24 ?  142 VAL   B HG23 1 
ATOM   5970 N  N    . CYS   B 1 143 ? 32.788 -26.925 -3.822  1.00 12.13 ?  143 CYS   B N    1 
ATOM   5971 C  CA   . CYS   B 1 143 ? 33.281 -25.985 -4.825  1.00 11.98 ?  143 CYS   B CA   1 
ATOM   5972 C  C    . CYS   B 1 143 ? 32.280 -25.838 -5.966  1.00 12.05 ?  143 CYS   B C    1 
ATOM   5973 O  O    . CYS   B 1 143 ? 31.881 -24.728 -6.328  1.00 12.33 ?  143 CYS   B O    1 
ATOM   5974 C  CB   . CYS   B 1 143 ? 34.633 -26.471 -5.353  1.00 12.29 ?  143 CYS   B CB   1 
ATOM   5975 S  SG   . CYS   B 1 143 ? 35.386 -25.373 -6.568  1.00 12.90 ?  143 CYS   B SG   1 
ATOM   5976 H  H    . CYS   B 1 143 ? 33.320 -27.580 -3.654  1.00 14.53 ?  143 CYS   B H    1 
ATOM   5977 H  HA   . CYS   B 1 143 ? 33.412 -25.116 -4.417  1.00 14.36 ?  143 CYS   B HA   1 
ATOM   5978 H  HB2  . CYS   B 1 143 ? 35.253 -26.559 -4.611  1.00 14.73 ?  143 CYS   B HB2  1 
ATOM   5979 H  HB3  . CYS   B 1 143 ? 34.511 -27.335 -5.773  1.00 14.73 ?  143 CYS   B HB3  1 
ATOM   5980 H  HG   . CYS   B 1 143 ? 36.454 -25.811 -6.892  1.00 15.45 ?  143 CYS   B HG   1 
ATOM   5981 N  N    . VAL   B 1 144 ? 31.876 -26.959 -6.558  1.00 12.55 ?  144 VAL   B N    1 
ATOM   5982 C  CA   . VAL   B 1 144 ? 30.965 -26.906 -7.697  1.00 13.43 ?  144 VAL   B CA   1 
ATOM   5983 C  C    . VAL   B 1 144 ? 29.625 -26.293 -7.321  1.00 13.65 ?  144 VAL   B C    1 
ATOM   5984 O  O    . VAL   B 1 144 ? 29.013 -25.583 -8.127  1.00 14.99 ?  144 VAL   B O    1 
ATOM   5985 C  CB   . VAL   B 1 144 ? 30.806 -28.318 -8.272  1.00 16.13 ?  144 VAL   B CB   1 
ATOM   5986 C  CG1  . VAL   B 1 144 ? 29.539 -28.438 -9.117  1.00 18.64 ?  144 VAL   B CG1  1 
ATOM   5987 C  CG2  . VAL   B 1 144 ? 32.053 -28.713 -9.052  1.00 16.48 ?  144 VAL   B CG2  1 
ATOM   5988 H  H    . VAL   B 1 144 ? 32.115 -27.751 -6.328  1.00 15.04 ?  144 VAL   B H    1 
ATOM   5989 H  HA   . VAL   B 1 144 ? 31.353 -26.352 -8.388  1.00 16.09 ?  144 VAL   B HA   1 
ATOM   5990 H  HB   . VAL   B 1 144 ? 30.716 -28.942 -7.534  1.00 19.34 ?  144 VAL   B HB   1 
ATOM   5991 H  HG11 . VAL   B 1 144 ? 29.620 -29.220 -9.688  1.00 22.35 ?  144 VAL   B HG11 1 
ATOM   5992 H  HG12 . VAL   B 1 144 ? 28.776 -28.539 -8.530  1.00 22.35 ?  144 VAL   B HG12 1 
ATOM   5993 H  HG13 . VAL   B 1 144 ? 29.445 -27.643 -9.662  1.00 22.35 ?  144 VAL   B HG13 1 
ATOM   5994 H  HG21 . VAL   B 1 144 ? 31.934 -29.613 -9.401  1.00 19.75 ?  144 VAL   B HG21 1 
ATOM   5995 H  HG22 . VAL   B 1 144 ? 32.177 -28.090 -9.784  1.00 19.75 ?  144 VAL   B HG22 1 
ATOM   5996 H  HG23 . VAL   B 1 144 ? 32.817 -28.687 -8.458  1.00 19.75 ?  144 VAL   B HG23 1 
ATOM   5997 N  N    . ASP   B 1 145 ? 29.158 -26.536 -6.102  1.00 13.75 ?  145 ASP   B N    1 
ATOM   5998 C  CA   . ASP   B 1 145 ? 27.852 -26.069 -5.663  1.00 14.53 ?  145 ASP   B CA   1 
ATOM   5999 C  C    . ASP   B 1 145 ? 27.884 -24.649 -5.116  1.00 13.79 ?  145 ASP   B C    1 
ATOM   6000 O  O    . ASP   B 1 145 ? 26.824 -24.110 -4.782  1.00 15.53 ?  145 ASP   B O    1 
ATOM   6001 C  CB   . ASP   B 1 145 ? 27.279 -26.995 -4.582  1.00 16.33 ?  145 ASP   B CB   1 
ATOM   6002 C  CG   . ASP   B 1 145 ? 26.913 -28.366 -5.099  1.00 18.31 ?  145 ASP   B CG   1 
ATOM   6003 O  OD1  . ASP   B 1 145 ? 26.798 -28.546 -6.326  1.00 18.44 ?  145 ASP   B OD1  1 
ATOM   6004 O  OD2  . ASP   B 1 145 ? 26.731 -29.262 -4.252  1.00 20.39 -1 145 ASP   B OD2  1 
ATOM   6005 H  H    . ASP   B 1 145 ? 29.595 -26.962 -5.501  1.00 16.48 ?  145 ASP   B H    1 
ATOM   6006 H  HA   . ASP   B 1 145 ? 27.250 -26.064 -6.416  1.00 17.41 ?  145 ASP   B HA   1 
ATOM   6007 H  HB2  . ASP   B 1 145 ? 27.935 -27.119 -3.891  1.00 19.57 ?  145 ASP   B HB2  1 
ATOM   6008 H  HB3  . ASP   B 1 145 ? 26.474 -26.591 -4.222  1.00 19.57 ?  145 ASP   B HB3  1 
ATOM   6009 N  N    . THR   B 1 146 ? 29.057 -24.033 -5.008  1.00 12.28 ?  146 THR   B N    1 
ATOM   6010 C  CA   . THR   B 1 146 ? 29.191 -22.712 -4.400  1.00 11.92 ?  146 THR   B CA   1 
ATOM   6011 C  C    . THR   B 1 146 ? 29.821 -21.683 -5.320  1.00 11.75 ?  146 THR   B C    1 
ATOM   6012 O  O    . THR   B 1 146 ? 29.366 -20.525 -5.364  1.00 12.17 ?  146 THR   B O    1 
ATOM   6013 C  CB   . THR   B 1 146 ? 30.021 -22.817 -3.113  1.00 12.20 ?  146 THR   B CB   1 
ATOM   6014 O  OG1  . THR   B 1 146 ? 29.454 -23.811 -2.256  1.00 12.62 ?  146 THR   B OG1  1 
ATOM   6015 C  CG2  . THR   B 1 146 ? 30.086 -21.482 -2.389  1.00 12.21 ?  146 THR   B CG2  1 
ATOM   6016 H  H    . THR   B 1 146 ? 29.808 -24.360 -5.282  1.00 14.72 ?  146 THR   B H    1 
ATOM   6017 H  HA   . THR   B 1 146 ? 28.318 -22.385 -4.157  1.00 14.28 ?  146 THR   B HA   1 
ATOM   6018 H  HB   . THR   B 1 146 ? 30.929 -23.073 -3.336  1.00 14.62 ?  146 THR   B HB   1 
ATOM   6019 H  HG1  . THR   B 1 146 ? 29.491 -24.568 -2.639  1.00 15.12 ?  146 THR   B HG1  1 
ATOM   6020 H  HG21 . THR   B 1 146 ? 30.439 -21.608 -1.496  1.00 14.63 ?  146 THR   B HG21 1 
ATOM   6021 H  HG22 . THR   B 1 146 ? 30.665 -20.871 -2.873  1.00 14.63 ?  146 THR   B HG22 1 
ATOM   6022 H  HG23 . THR   B 1 146 ? 29.199 -21.097 -2.328  1.00 14.63 ?  146 THR   B HG23 1 
ATOM   6023 N  N    . VAL   B 1 147 ? 30.884 -22.054 -6.022  1.00 11.79 ?  147 VAL   B N    1 
ATOM   6024 C  CA   . VAL   B 1 147 ? 31.607 -21.108 -6.856  1.00 11.28 ?  147 VAL   B CA   1 
ATOM   6025 C  C    . VAL   B 1 147 ? 30.872 -20.976 -8.176  1.00 11.60 ?  147 VAL   B C    1 
ATOM   6026 O  O    . VAL   B 1 147 ? 30.509 -21.979 -8.805  1.00 12.39 ?  147 VAL   B O    1 
ATOM   6027 C  CB   . VAL   B 1 147 ? 33.060 -21.564 -7.067  1.00 11.52 ?  147 VAL   B CB   1 
ATOM   6028 C  CG1  . VAL   B 1 147 ? 33.819 -20.538 -7.878  1.00 12.01 ?  147 VAL   B CG1  1 
ATOM   6029 C  CG2  . VAL   B 1 147 ? 33.746 -21.783 -5.732  1.00 11.75 ?  147 VAL   B CG2  1 
ATOM   6030 H  H    . VAL   B 1 147 ? 31.210 -22.854 -6.036  1.00 14.13 ?  147 VAL   B H    1 
ATOM   6031 H  HA   . VAL   B 1 147 ? 31.625 -20.241 -6.426  1.00 13.51 ?  147 VAL   B HA   1 
ATOM   6032 H  HB   . VAL   B 1 147 ? 33.070 -22.406 -7.558  1.00 13.80 ?  147 VAL   B HB   1 
ATOM   6033 H  HG11 . VAL   B 1 147 ? 34.763 -20.761 -7.870  1.00 14.39 ?  147 VAL   B HG11 1 
ATOM   6034 H  HG12 . VAL   B 1 147 ? 33.487 -20.539 -8.789  1.00 14.39 ?  147 VAL   B HG12 1 
ATOM   6035 H  HG13 . VAL   B 1 147 ? 33.685 -19.662 -7.478  1.00 14.39 ?  147 VAL   B HG13 1 
ATOM   6036 H  HG21 . VAL   B 1 147 ? 34.685 -21.983 -5.886  1.00 14.08 ?  147 VAL   B HG21 1 
ATOM   6037 H  HG22 . VAL   B 1 147 ? 33.665 -20.975 -5.202  1.00 14.08 ?  147 VAL   B HG22 1 
ATOM   6038 H  HG23 . VAL   B 1 147 ? 33.323 -22.524 -5.274  1.00 14.08 ?  147 VAL   B HG23 1 
ATOM   6039 N  N    . ARG   B 1 148 ? 30.664 -19.729 -8.597  1.00 11.79 ?  148 ARG   B N    1 
ATOM   6040 C  CA   . ARG   B 1 148 ? 30.038 -19.412 -9.868  1.00 11.67 ?  148 ARG   B CA   1 
ATOM   6041 C  C    . ARG   B 1 148 ? 30.992 -18.738 -10.841 1.00 11.97 ?  148 ARG   B C    1 
ATOM   6042 O  O    . ARG   B 1 148 ? 30.708 -18.719 -12.041 1.00 13.29 ?  148 ARG   B O    1 
ATOM   6043 C  CB   . ARG   B 1 148 ? 28.804 -18.522 -9.644  1.00 12.20 ?  148 ARG   B CB   1 
ATOM   6044 C  CG   . ARG   B 1 148 ? 27.727 -19.229 -8.839  1.00 13.22 ?  148 ARG   B CG   1 
ATOM   6045 C  CD   . ARG   B 1 148 ? 26.524 -18.343 -8.535  1.00 14.01 ?  148 ARG   B CD   1 
ATOM   6046 N  NE   . ARG   B 1 148 ? 26.912 -17.144 -7.802  1.00 13.61 ?  148 ARG   B NE   1 
ATOM   6047 C  CZ   . ARG   B 1 148 ? 27.215 -17.115 -6.511  1.00 12.81 ?  148 ARG   B CZ   1 
ATOM   6048 N  NH1  . ARG   B 1 148 ? 27.142 -18.200 -5.756  1.00 12.79 ?  148 ARG   B NH1  1 
ATOM   6049 N  NH2  . ARG   B 1 148 ? 27.611 -15.968 -5.964  1.00 13.18 ?  148 ARG   B NH2  1 
ATOM   6050 H  H    . ARG   B 1 148 ? 30.889 -19.032 -8.142  1.00 14.12 ?  148 ARG   B H    1 
ATOM   6051 H  HA   . ARG   B 1 148 ? 29.735 -20.235 -10.275 1.00 13.98 ?  148 ARG   B HA   1 
ATOM   6052 H  HB2  . ARG   B 1 148 ? 29.067 -17.725 -9.156  1.00 14.62 ?  148 ARG   B HB2  1 
ATOM   6053 H  HB3  . ARG   B 1 148 ? 28.427 -18.279 -10.503 1.00 14.62 ?  148 ARG   B HB3  1 
ATOM   6054 H  HG2  . ARG   B 1 148 ? 27.411 -19.997 -9.344  1.00 15.84 ?  148 ARG   B HG2  1 
ATOM   6055 H  HG3  . ARG   B 1 148 ? 28.102 -19.522 -7.995  1.00 15.84 ?  148 ARG   B HG3  1 
ATOM   6056 H  HD2  . ARG   B 1 148 ? 26.110 -18.070 -9.368  1.00 16.79 ?  148 ARG   B HD2  1 
ATOM   6057 H  HD3  . ARG   B 1 148 ? 25.889 -18.843 -7.995  1.00 16.79 ?  148 ARG   B HD3  1 
ATOM   6058 H  HE   . ARG   B 1 148 ? 26.948 -16.408 -8.237  1.00 16.31 ?  148 ARG   B HE   1 
ATOM   6059 H  HH11 . ARG   B 1 148 ? 26.880 -18.949 -6.092  1.00 15.32 ?  148 ARG   B HH11 1 
ATOM   6060 H  HH12 . ARG   B 1 148 ? 27.336 -18.157 -4.917  1.00 15.32 ?  148 ARG   B HH12 1 
ATOM   6061 H  HH21 . ARG   B 1 148 ? 27.667 -15.261 -6.448  1.00 15.80 ?  148 ARG   B HH21 1 
ATOM   6062 H  HH22 . ARG   B 1 148 ? 27.810 -15.936 -5.129  1.00 15.80 ?  148 ARG   B HH22 1 
ATOM   6063 N  N    . THR   B 1 149 ? 32.099 -18.184 -10.355 1.00 11.99 ?  149 THR   B N    1 
ATOM   6064 C  CA   . THR   B 1 149 ? 33.139 -17.625 -11.205 1.00 12.03 ?  149 THR   B CA   1 
ATOM   6065 C  C    . THR   B 1 149 ? 34.027 -18.763 -11.709 1.00 11.47 ?  149 THR   B C    1 
ATOM   6066 O  O    . THR   B 1 149 ? 33.839 -19.927 -11.358 1.00 12.10 ?  149 THR   B O    1 
ATOM   6067 C  CB   . THR   B 1 149 ? 33.917 -16.574 -10.426 1.00 11.84 ?  149 THR   B CB   1 
ATOM   6068 O  OG1  . THR   B 1 149 ? 34.378 -17.171 -9.211  1.00 11.80 ?  149 THR   B OG1  1 
ATOM   6069 C  CG2  . THR   B 1 149 ? 33.031 -15.370 -10.123 1.00 12.50 ?  149 THR   B CG2  1 
ATOM   6070 H  H    . THR   B 1 149 ? 32.263 -18.107 -9.515  1.00 14.36 ?  149 THR   B H    1 
ATOM   6071 H  HA   . THR   B 1 149 ? 32.732 -17.191 -11.971 1.00 14.42 ?  149 THR   B HA   1 
ATOM   6072 H  HB   . THR   B 1 149 ? 34.678 -16.281 -10.947 1.00 14.18 ?  149 THR   B HB   1 
ATOM   6073 H  HG1  . THR   B 1 149 ? 34.802 -16.597 -8.755  1.00 14.14 ?  149 THR   B HG1  1 
ATOM   6074 H  HG21 . THR   B 1 149 ? 33.542 -14.698 -9.641  1.00 14.97 ?  149 THR   B HG21 1 
ATOM   6075 H  HG22 . THR   B 1 149 ? 32.707 -14.981 -10.951 1.00 14.97 ?  149 THR   B HG22 1 
ATOM   6076 H  HG23 . THR   B 1 149 ? 32.275 -15.638 -9.581  1.00 14.97 ?  149 THR   B HG23 1 
ATOM   6077 N  N    . ASN   B 1 150 ? 34.992 -18.443 -12.561 1.00 11.61 ?  150 ASN   B N    1 
ATOM   6078 C  CA   . ASN   B 1 150 ? 35.754 -19.469 -13.263 1.00 12.27 ?  150 ASN   B CA   1 
ATOM   6079 C  C    . ASN   B 1 150 ? 36.922 -19.921 -12.393 1.00 11.81 ?  150 ASN   B C    1 
ATOM   6080 O  O    . ASN   B 1 150 ? 37.850 -19.148 -12.134 1.00 12.60 ?  150 ASN   B O    1 
ATOM   6081 C  CB   . ASN   B 1 150 ? 36.223 -18.932 -14.607 1.00 13.86 ?  150 ASN   B CB   1 
ATOM   6082 C  CG   . ASN   B 1 150 ? 35.080 -18.708 -15.552 1.00 16.33 ?  150 ASN   B CG   1 
ATOM   6083 O  OD1  . ASN   B 1 150 ? 34.192 -19.541 -15.651 1.00 17.44 ?  150 ASN   B OD1  1 
ATOM   6084 N  ND2  . ASN   B 1 150 ? 35.073 -17.572 -16.227 1.00 17.87 ?  150 ASN   B ND2  1 
ATOM   6085 H  H    . ASN   B 1 150 ? 35.233 -17.635 -12.744 1.00 13.91 ?  150 ASN   B H    1 
ATOM   6086 H  HA   . ASN   B 1 150 ? 35.174 -20.233 -13.427 1.00 14.69 ?  150 ASN   B HA   1 
ATOM   6087 H  HB2  . ASN   B 1 150 ? 36.670 -18.081 -14.470 1.00 16.60 ?  150 ASN   B HB2  1 
ATOM   6088 H  HB3  . ASN   B 1 150 ? 36.828 -19.568 -15.011 1.00 16.60 ?  150 ASN   B HB3  1 
ATOM   6089 H  HD21 . ASN   B 1 150 ? 34.434 -17.399 -16.781 1.00 21.41 ?  150 ASN   B HD21 1 
ATOM   6090 H  HD22 . ASN   B 1 150 ? 35.710 -17.002 -16.123 1.00 21.41 ?  150 ASN   B HD22 1 
ATOM   6091 N  N    . VAL   B 1 151 ? 36.881 -21.169 -11.938 1.00 11.35 ?  151 VAL   B N    1 
ATOM   6092 C  CA   . VAL   B 1 151 ? 37.902 -21.694 -11.046 1.00 11.35 ?  151 VAL   B CA   1 
ATOM   6093 C  C    . VAL   B 1 151 ? 38.607 -22.862 -11.722 1.00 11.40 ?  151 VAL   B C    1 
ATOM   6094 O  O    . VAL   B 1 151 ? 37.965 -23.797 -12.223 1.00 12.44 ?  151 VAL   B O    1 
ATOM   6095 C  CB   . VAL   B 1 151 ? 37.339 -22.026 -9.650  1.00 12.98 ?  151 VAL   B CB   1 
ATOM   6096 C  CG1  . VAL   B 1 151 ? 36.181 -23.023 -9.729  1.00 13.93 ?  151 VAL   B CG1  1 
ATOM   6097 C  CG2  . VAL   B 1 151 ? 38.446 -22.511 -8.726  1.00 13.32 ?  151 VAL   B CG2  1 
ATOM   6098 H  H    . VAL   B 1 151 ? 36.260 -21.735 -12.136 1.00 13.60 ?  151 VAL   B H    1 
ATOM   6099 H  HA   . VAL   B 1 151 ? 38.569 -20.999 -10.919 1.00 13.60 ?  151 VAL   B HA   1 
ATOM   6100 H  HB   . VAL   B 1 151 ? 36.985 -21.207 -9.266  1.00 15.55 ?  151 VAL   B HB   1 
ATOM   6101 H  HG11 . VAL   B 1 151 ? 35.862 -23.210 -8.831  1.00 16.70 ?  151 VAL   B HG11 1 
ATOM   6102 H  HG12 . VAL   B 1 151 ? 35.464 -22.640 -10.260 1.00 16.70 ?  151 VAL   B HG12 1 
ATOM   6103 H  HG13 . VAL   B 1 151 ? 36.495 -23.843 -10.143 1.00 16.70 ?  151 VAL   B HG13 1 
ATOM   6104 H  HG21 . VAL   B 1 151 ? 38.089 -22.593 -7.827  1.00 15.96 ?  151 VAL   B HG21 1 
ATOM   6105 H  HG22 . VAL   B 1 151 ? 38.765 -23.371 -9.036  1.00 15.96 ?  151 VAL   B HG22 1 
ATOM   6106 H  HG23 . VAL   B 1 151 ? 39.170 -21.864 -8.733  1.00 15.96 ?  151 VAL   B HG23 1 
ATOM   6107 N  N    . TYR   B 1 152 ? 39.935 -22.775 -11.747 1.00 10.68 ?  152 TYR   B N    1 
ATOM   6108 C  CA   . TYR   B 1 152 ? 40.840 -23.756 -12.326 1.00 11.12 ?  152 TYR   B CA   1 
ATOM   6109 C  C    . TYR   B 1 152 ? 41.563 -24.430 -11.166 1.00 10.65 ?  152 TYR   B C    1 
ATOM   6110 O  O    . TYR   B 1 152 ? 42.406 -23.810 -10.507 1.00 11.22 ?  152 TYR   B O    1 
ATOM   6111 C  CB   . TYR   B 1 152 ? 41.812 -23.046 -13.269 1.00 12.22 ?  152 TYR   B CB   1 
ATOM   6112 C  CG   . TYR   B 1 152 ? 41.131 -22.583 -14.537 1.00 12.35 ?  152 TYR   B CG   1 
ATOM   6113 C  CD1  . TYR   B 1 152 ? 40.464 -21.362 -14.606 1.00 12.82 ?  152 TYR   B CD1  1 
ATOM   6114 C  CD2  . TYR   B 1 152 ? 41.136 -23.388 -15.661 1.00 13.65 ?  152 TYR   B CD2  1 
ATOM   6115 C  CE1  . TYR   B 1 152 ? 39.822 -20.967 -15.768 1.00 14.22 ?  152 TYR   B CE1  1 
ATOM   6116 C  CE2  . TYR   B 1 152 ? 40.498 -23.005 -16.824 1.00 14.53 ?  152 TYR   B CE2  1 
ATOM   6117 C  CZ   . TYR   B 1 152 ? 39.845 -21.790 -16.877 1.00 14.85 ?  152 TYR   B CZ   1 
ATOM   6118 O  OH   . TYR   B 1 152 ? 39.217 -21.417 -18.043 1.00 17.41 ?  152 TYR   B OH   1 
ATOM   6119 H  H    . TYR   B 1 152 ? 40.364 -22.109 -11.404 1.00 12.79 ?  152 TYR   B H    1 
ATOM   6120 H  HA   . TYR   B 1 152 ? 40.335 -24.425 -12.822 1.00 13.32 ?  152 TYR   B HA   1 
ATOM   6121 H  HB2  . TYR   B 1 152 ? 42.175 -22.269 -12.818 1.00 14.65 ?  152 TYR   B HB2  1 
ATOM   6122 H  HB3  . TYR   B 1 152 ? 42.525 -23.656 -13.511 1.00 14.65 ?  152 TYR   B HB3  1 
ATOM   6123 H  HD1  . TYR   B 1 152 ? 40.440 -20.809 -13.857 1.00 15.36 ?  152 TYR   B HD1  1 
ATOM   6124 H  HD2  . TYR   B 1 152 ? 41.568 -24.213 -15.631 1.00 16.36 ?  152 TYR   B HD2  1 
ATOM   6125 H  HE1  . TYR   B 1 152 ? 39.381 -20.151 -15.805 1.00 17.04 ?  152 TYR   B HE1  1 
ATOM   6126 H  HE2  . TYR   B 1 152 ? 40.516 -23.562 -17.569 1.00 17.41 ?  152 TYR   B HE2  1 
ATOM   6127 H  HH   . TYR   B 1 152 ? 39.320 -22.021 -18.620 1.00 20.87 ?  152 TYR   B HH   1 
ATOM   6128 N  N    . LEU   B 1 153 ? 41.201 -25.687 -10.900 1.00 11.01 ?  153 LEU   B N    1 
ATOM   6129 C  CA   . LEU   B 1 153 ? 41.705 -26.436 -9.759  1.00 10.55 ?  153 LEU   B CA   1 
ATOM   6130 C  C    . LEU   B 1 153 ? 42.937 -27.236 -10.154 1.00 10.77 ?  153 LEU   B C    1 
ATOM   6131 O  O    . LEU   B 1 153 ? 42.916 -27.970 -11.146 1.00 12.03 ?  153 LEU   B O    1 
ATOM   6132 C  CB   . LEU   B 1 153 ? 40.628 -27.393 -9.243  1.00 11.03 ?  153 LEU   B CB   1 
ATOM   6133 C  CG   . LEU   B 1 153 ? 39.369 -26.739 -8.675  1.00 11.95 ?  153 LEU   B CG   1 
ATOM   6134 C  CD1  . LEU   B 1 153 ? 38.275 -27.787 -8.515  1.00 12.82 ?  153 LEU   B CD1  1 
ATOM   6135 C  CD2  . LEU   B 1 153 ? 39.665 -26.068 -7.343  1.00 12.43 ?  153 LEU   B CD2  1 
ATOM   6136 H  H    . LEU   B 1 153 ? 40.634 -26.137 -11.380 1.00 13.18 ?  153 LEU   B H    1 
ATOM   6137 H  HA   . LEU   B 1 153 ? 41.935 -25.822 -9.049  1.00 12.63 ?  153 LEU   B HA   1 
ATOM   6138 H  HB2  . LEU   B 1 153 ? 40.348 -27.968 -9.972  1.00 13.21 ?  153 LEU   B HB2  1 
ATOM   6139 H  HB3  . LEU   B 1 153 ? 41.012 -27.936 -8.534  1.00 13.21 ?  153 LEU   B HB3  1 
ATOM   6140 H  HG   . LEU   B 1 153 ? 39.051 -26.057 -9.291  1.00 14.31 ?  153 LEU   B HG   1 
ATOM   6141 H  HD11 . LEU   B 1 153 ? 37.472 -27.352 -8.187  1.00 15.36 ?  153 LEU   B HD11 1 
ATOM   6142 H  HD12 . LEU   B 1 153 ? 38.108 -28.191 -9.376  1.00 15.36 ?  153 LEU   B HD12 1 
ATOM   6143 H  HD13 . LEU   B 1 153 ? 38.576 -28.453 -7.881  1.00 15.36 ?  153 LEU   B HD13 1 
ATOM   6144 H  HD21 . LEU   B 1 153 ? 38.846 -25.694 -6.982  1.00 14.89 ?  153 LEU   B HD21 1 
ATOM   6145 H  HD22 . LEU   B 1 153 ? 40.027 -26.727 -6.730  1.00 14.89 ?  153 LEU   B HD22 1 
ATOM   6146 H  HD23 . LEU   B 1 153 ? 40.316 -25.358 -7.482  1.00 14.89 ?  153 LEU   B HD23 1 
ATOM   6147 N  N    . ALA   B 1 154 ? 43.992 -27.121 -9.354  1.00 10.93 ?  154 ALA   B N    1 
ATOM   6148 C  CA   . ALA   B 1 154 ? 45.218 -27.882 -9.545  1.00 12.41 ?  154 ALA   B CA   1 
ATOM   6149 C  C    . ALA   B 1 154 ? 45.282 -28.960 -8.472  1.00 12.90 ?  154 ALA   B C    1 
ATOM   6150 O  O    . ALA   B 1 154 ? 45.194 -28.663 -7.274  1.00 14.01 ?  154 ALA   B O    1 
ATOM   6151 C  CB   . ALA   B 1 154 ? 46.440 -26.969 -9.481  1.00 13.17 ?  154 ALA   B CB   1 
ATOM   6152 H  H    . ALA   B 1 154 ? 44.016 -26.592 -8.673  1.00 13.09 ?  154 ALA   B H    1 
ATOM   6153 H  HA   . ALA   B 1 154 ? 45.203 -28.310 -10.412 1.00 14.87 ?  154 ALA   B HA   1 
ATOM   6154 H  HB1  . ALA   B 1 154 ? 47.242 -27.498 -9.609  1.00 15.78 ?  154 ALA   B HB1  1 
ATOM   6155 H  HB2  . ALA   B 1 154 ? 46.374 -26.296 -10.180 1.00 15.78 ?  154 ALA   B HB2  1 
ATOM   6156 H  HB3  . ALA   B 1 154 ? 46.470 -26.532 -8.612  1.00 15.78 ?  154 ALA   B HB3  1 
ATOM   6157 N  N    . VAL   B 1 155 ? 45.402 -30.209 -8.904  1.00 12.29 ?  155 VAL   B N    1 
ATOM   6158 C  CA   . VAL   B 1 155 ? 45.510 -31.353 -8.007  1.00 12.34 ?  155 VAL   B CA   1 
ATOM   6159 C  C    . VAL   B 1 155 ? 46.851 -32.025 -8.284  1.00 12.24 ?  155 VAL   B C    1 
ATOM   6160 O  O    . VAL   B 1 155 ? 47.087 -32.514 -9.395  1.00 14.13 ?  155 VAL   B O    1 
ATOM   6161 C  CB   . VAL   B 1 155 ? 44.355 -32.348 -8.206  1.00 13.54 ?  155 VAL   B CB   1 
ATOM   6162 C  CG1  . VAL   B 1 155 ? 44.538 -33.548 -7.300  1.00 13.44 ?  155 VAL   B CG1  1 
ATOM   6163 C  CG2  . VAL   B 1 155 ? 43.017 -31.667 -7.945  1.00 14.48 ?  155 VAL   B CG2  1 
ATOM   6164 H  H    . VAL   B 1 155 ? 45.434 -30.423 -9.735  1.00 14.72 ?  155 VAL   B H    1 
ATOM   6165 H  HA   . VAL   B 1 155 ? 45.500 -31.053 -7.087  1.00 14.78 ?  155 VAL   B HA   1 
ATOM   6166 H  HB   . VAL   B 1 155 ? 44.356 -32.657 -9.126  1.00 16.22 ?  155 VAL   B HB   1 
ATOM   6167 H  HG11 . VAL   B 1 155 ? 43.709 -34.050 -7.262  1.00 16.10 ?  155 VAL   B HG11 1 
ATOM   6168 H  HG12 . VAL   B 1 155 ? 45.246 -34.114 -7.657  1.00 16.10 ?  155 VAL   B HG12 1 
ATOM   6169 H  HG13 . VAL   B 1 155 ? 44.780 -33.244 -6.411  1.00 16.10 ?  155 VAL   B HG13 1 
ATOM   6170 H  HG21 . VAL   B 1 155 ? 42.308 -32.322 -8.040  1.00 17.35 ?  155 VAL   B HG21 1 
ATOM   6171 H  HG22 . VAL   B 1 155 ? 43.019 -31.308 -7.044  1.00 17.35 ?  155 VAL   B HG22 1 
ATOM   6172 H  HG23 . VAL   B 1 155 ? 42.896 -30.951 -8.587  1.00 17.35 ?  155 VAL   B HG23 1 
ATOM   6173 N  N    . PHE   B 1 156 ? 47.716 -32.069 -7.268  1.00 12.65 ?  156 PHE   B N    1 
ATOM   6174 C  CA   . PHE   B 1 156 ? 49.093 -32.520 -7.469  1.00 13.74 ?  156 PHE   B CA   1 
ATOM   6175 C  C    . PHE   B 1 156 ? 49.194 -34.019 -7.749  1.00 14.74 ?  156 PHE   B C    1 
ATOM   6176 O  O    . PHE   B 1 156 ? 49.920 -34.442 -8.658  1.00 16.33 ?  156 PHE   B O    1 
ATOM   6177 C  CB   . PHE   B 1 156 ? 49.921 -32.145 -6.244  1.00 13.74 ?  156 PHE   B CB   1 
ATOM   6178 C  CG   . PHE   B 1 156 ? 51.345 -32.610 -6.302  1.00 14.45 ?  156 PHE   B CG   1 
ATOM   6179 C  CD1  . PHE   B 1 156 ? 52.228 -32.071 -7.219  1.00 16.37 ?  156 PHE   B CD1  1 
ATOM   6180 C  CD2  . PHE   B 1 156 ? 51.806 -33.573 -5.426  1.00 15.05 ?  156 PHE   B CD2  1 
ATOM   6181 C  CE1  . PHE   B 1 156 ? 53.545 -32.482 -7.267  1.00 17.17 ?  156 PHE   B CE1  1 
ATOM   6182 C  CE2  . PHE   B 1 156 ? 53.123 -33.990 -5.470  1.00 16.44 ?  156 PHE   B CE2  1 
ATOM   6183 C  CZ   . PHE   B 1 156 ? 53.987 -33.446 -6.396  1.00 16.99 ?  156 PHE   B CZ   1 
ATOM   6184 H  H    . PHE   B 1 156 ? 47.528 -31.850 -6.457  1.00 15.16 ?  156 PHE   B H    1 
ATOM   6185 H  HA   . PHE   B 1 156 ? 49.462 -32.053 -8.230  1.00 16.46 ?  156 PHE   B HA   1 
ATOM   6186 H  HB2  . PHE   B 1 156 ? 49.932 -31.179 -6.161  1.00 16.47 ?  156 PHE   B HB2  1 
ATOM   6187 H  HB3  . PHE   B 1 156 ? 49.515 -32.538 -5.456  1.00 16.47 ?  156 PHE   B HB3  1 
ATOM   6188 H  HD1  . PHE   B 1 156 ? 51.934 -31.414 -7.811  1.00 19.62 ?  156 PHE   B HD1  1 
ATOM   6189 H  HD2  . PHE   B 1 156 ? 51.221 -33.944 -4.804  1.00 18.04 ?  156 PHE   B HD2  1 
ATOM   6190 H  HE1  . PHE   B 1 156 ? 54.128 -32.112 -7.893  1.00 20.58 ?  156 PHE   B HE1  1 
ATOM   6191 H  HE2  . PHE   B 1 156 ? 53.420 -34.648 -4.882  1.00 19.70 ?  156 PHE   B HE2  1 
ATOM   6192 H  HZ   . PHE   B 1 156 ? 54.871 -33.732 -6.427  1.00 20.36 ?  156 PHE   B HZ   1 
ATOM   6193 N  N    . ASP   B 1 157 ? 48.523 -34.839 -6.952  1.00 15.09 ?  157 ASP   B N    1 
ATOM   6194 C  CA   . ASP   B 1 157 ? 48.671 -36.286 -7.051  1.00 16.38 ?  157 ASP   B CA   1 
ATOM   6195 C  C    . ASP   B 1 157 ? 47.755 -36.827 -8.144  1.00 16.35 ?  157 ASP   B C    1 
ATOM   6196 O  O    . ASP   B 1 157 ? 46.529 -36.703 -8.044  1.00 15.87 ?  157 ASP   B O    1 
ATOM   6197 C  CB   . ASP   B 1 157 ? 48.310 -36.905 -5.706  1.00 17.98 ?  157 ASP   B CB   1 
ATOM   6198 C  CG   . ASP   B 1 157 ? 48.447 -38.411 -5.694  1.00 19.74 ?  157 ASP   B CG   1 
ATOM   6199 O  OD1  . ASP   B 1 157 ? 48.779 -39.012 -6.744  1.00 20.37 ?  157 ASP   B OD1  1 
ATOM   6200 O  OD2  . ASP   B 1 157 ? 48.237 -38.998 -4.614  1.00 21.66 -1 157 ASP   B OD2  1 
ATOM   6201 H  H    . ASP   B 1 157 ? 47.976 -34.586 -6.344  1.00 18.08 ?  157 ASP   B H    1 
ATOM   6202 H  HA   . ASP   B 1 157 ? 49.593 -36.516 -7.267  1.00 19.64 ?  157 ASP   B HA   1 
ATOM   6203 H  HB2  . ASP   B 1 157 ? 48.889 -36.530 -5.026  1.00 21.55 ?  157 ASP   B HB2  1 
ATOM   6204 H  HB3  . ASP   B 1 157 ? 47.385 -36.691 -5.505  1.00 21.55 ?  157 ASP   B HB3  1 
ATOM   6205 N  N    . LYS   B 1 158 ? 48.350 -37.444 -9.174  1.00 17.75 ?  158 LYS   B N    1 
ATOM   6206 C  CA   . LYS   B 1 158 ? 47.573 -38.051 -10.256 1.00 18.93 ?  158 LYS   B CA   1 
ATOM   6207 C  C    . LYS   B 1 158 ? 46.513 -39.017 -9.729  1.00 18.64 ?  158 LYS   B C    1 
ATOM   6208 O  O    . LYS   B 1 158 ? 45.410 -39.104 -10.282 1.00 18.55 ?  158 LYS   B O    1 
ATOM   6209 C  CB   . LYS   B 1 158 ? 48.518 -38.763 -11.233 1.00 20.55 ?  158 LYS   B CB   1 
ATOM   6210 C  CG   . LYS   B 1 158 ? 47.836 -39.672 -12.248 1.00 22.85 ?  158 LYS   B CG   1 
ATOM   6211 C  CD   . LYS   B 1 158 ? 46.980 -38.898 -13.227 1.00 25.23 ?  158 LYS   B CD   1 
ATOM   6212 C  CE   . LYS   B 1 158 ? 46.400 -39.822 -14.287 1.00 26.90 ?  158 LYS   B CE   1 
ATOM   6213 N  NZ   . LYS   B 1 158 ? 45.343 -39.150 -15.097 1.00 27.40 ?  158 LYS   B NZ   1 
ATOM   6214 H  H    . LYS   B 1 158 ? 49.208 -37.526 -9.270  1.00 21.28 ?  158 LYS   B H    1 
ATOM   6215 H  HA   . LYS   B 1 158 ? 47.123 -37.347 -10.750 1.00 22.69 ?  158 LYS   B HA   1 
ATOM   6216 H  HB2  . LYS   B 1 158 ? 49.012 -38.092 -11.738 1.00 24.63 ?  158 LYS   B HB2  1 
ATOM   6217 H  HB3  . LYS   B 1 158 ? 49.140 -39.307 -10.728 1.00 24.63 ?  158 LYS   B HB3  1 
ATOM   6218 H  HG2  . LYS   B 1 158 ? 48.519 -40.137 -12.757 1.00 27.40 ?  158 LYS   B HG2  1 
ATOM   6219 H  HG3  . LYS   B 1 158 ? 47.276 -40.322 -11.793 1.00 27.40 ?  158 LYS   B HG3  1 
ATOM   6220 H  HD2  . LYS   B 1 158 ? 46.245 -38.479 -12.753 1.00 30.25 ?  158 LYS   B HD2  1 
ATOM   6221 H  HD3  . LYS   B 1 158 ? 47.523 -38.229 -13.672 1.00 30.25 ?  158 LYS   B HD3  1 
ATOM   6222 H  HE2  . LYS   B 1 158 ? 47.106 -40.104 -14.888 1.00 32.25 ?  158 LYS   B HE2  1 
ATOM   6223 H  HE3  . LYS   B 1 158 ? 46.003 -40.596 -13.855 1.00 32.25 ?  158 LYS   B HE3  1 
ATOM   6224 H  HZ1  . LYS   B 1 158 ? 45.021 -39.712 -15.707 1.00 32.86 ?  158 LYS   B HZ1  1 
ATOM   6225 H  HZ2  . LYS   B 1 158 ? 44.677 -38.884 -14.569 1.00 32.86 ?  158 LYS   B HZ2  1 
ATOM   6226 H  HZ3  . LYS   B 1 158 ? 45.684 -38.439 -15.510 1.00 32.86 ?  158 LYS   B HZ3  1 
ATOM   6227 N  N    . ASN   B 1 159 ? 46.836 -39.775 -8.679  1.00 18.79 ?  159 ASN   B N    1 
ATOM   6228 C  CA   . ASN   B 1 159 ? 45.882 -40.758 -8.173  1.00 19.62 ?  159 ASN   B CA   1 
ATOM   6229 C  C    . ASN   B 1 159 ? 44.684 -40.086 -7.499  1.00 18.56 ?  159 ASN   B C    1 
ATOM   6230 O  O    . ASN   B 1 159 ? 43.550 -40.576 -7.605  1.00 18.83 ?  159 ASN   B O    1 
ATOM   6231 C  CB   . ASN   B 1 159 ? 46.591 -41.738 -7.243  1.00 21.34 ?  159 ASN   B CB   1 
ATOM   6232 C  CG   . ASN   B 1 159 ? 47.613 -42.585 -7.971  1.00 23.42 ?  159 ASN   B CG   1 
ATOM   6233 O  OD1  . ASN   B 1 159 ? 47.344 -43.097 -9.062  1.00 23.85 ?  159 ASN   B OD1  1 
ATOM   6234 N  ND2  . ASN   B 1 159 ? 48.792 -42.736 -7.376  1.00 24.23 ?  159 ASN   B ND2  1 
ATOM   6235 H  H    . ASN   B 1 159 ? 47.581 -39.730 -8.257  1.00 22.53 ?  159 ASN   B H    1 
ATOM   6236 H  HA   . ASN   B 1 159 ? 45.545 -41.263 -8.930  1.00 23.52 ?  159 ASN   B HA   1 
ATOM   6237 H  HB2  . ASN   B 1 159 ? 47.051 -41.244 -6.550  1.00 25.58 ?  159 ASN   B HB2  1 
ATOM   6238 H  HB3  . ASN   B 1 159 ? 45.935 -42.334 -6.858  1.00 25.58 ?  159 ASN   B HB3  1 
ATOM   6239 H  HD21 . ASN   B 1 159 ? 49.410 -43.207 -7.752  1.00 29.05 ?  159 ASN   B HD21 1 
ATOM   6240 H  HD22 . ASN   B 1 159 ? 48.940 -42.371 -6.612  1.00 29.05 ?  159 ASN   B HD22 1 
ATOM   6241 N  N    . LEU   B 1 160 ? 44.900 -38.957 -6.816  1.00 17.47 ?  160 LEU   B N    1 
ATOM   6242 C  CA   . LEU   B 1 160 ? 43.768 -38.220 -6.271  1.00 16.61 ?  160 LEU   B CA   1 
ATOM   6243 C  C    . LEU   B 1 160 ? 42.977 -37.551 -7.384  1.00 15.64 ?  160 LEU   B C    1 
ATOM   6244 O  O    . LEU   B 1 160 ? 41.741 -37.561 -7.367  1.00 15.24 ?  160 LEU   B O    1 
ATOM   6245 C  CB   . LEU   B 1 160 ? 44.232 -37.194 -5.239  1.00 15.90 ?  160 LEU   B CB   1 
ATOM   6246 C  CG   . LEU   B 1 160 ? 43.107 -36.296 -4.706  1.00 15.84 ?  160 LEU   B CG   1 
ATOM   6247 C  CD1  . LEU   B 1 160 ? 41.983 -37.120 -4.093  1.00 16.53 ?  160 LEU   B CD1  1 
ATOM   6248 C  CD2  . LEU   B 1 160 ? 43.647 -35.299 -3.696  1.00 15.98 ?  160 LEU   B CD2  1 
ATOM   6249 H  H    . LEU   B 1 160 ? 45.674 -38.605 -6.668  1.00 20.94 ?  160 LEU   B H    1 
ATOM   6250 H  HA   . LEU   B 1 160 ? 43.180 -38.847 -5.830  1.00 19.90 ?  160 LEU   B HA   1 
ATOM   6251 H  HB2  . LEU   B 1 160 ? 44.624 -37.670 -4.487  1.00 19.06 ?  160 LEU   B HB2  1 
ATOM   6252 H  HB3  . LEU   B 1 160 ? 44.906 -36.623 -5.647  1.00 19.06 ?  160 LEU   B HB3  1 
ATOM   6253 H  HG   . LEU   B 1 160 ? 42.737 -35.793 -5.443  1.00 18.99 ?  160 LEU   B HG   1 
ATOM   6254 H  HD11 . LEU   B 1 160 ? 41.351 -36.519 -3.671  1.00 19.81 ?  160 LEU   B HD11 1 
ATOM   6255 H  HD12 . LEU   B 1 160 ? 41.539 -37.627 -4.793  1.00 19.81 ?  160 LEU   B HD12 1 
ATOM   6256 H  HD13 . LEU   B 1 160 ? 42.356 -37.726 -3.432  1.00 19.81 ?  160 LEU   B HD13 1 
ATOM   6257 H  HD21 . LEU   B 1 160 ? 42.919 -34.732 -3.399  1.00 19.15 ?  160 LEU   B HD21 1 
ATOM   6258 H  HD22 . LEU   B 1 160 ? 44.022 -35.780 -2.943  1.00 19.15 ?  160 LEU   B HD22 1 
ATOM   6259 H  HD23 . LEU   B 1 160 ? 44.333 -34.760 -4.121  1.00 19.15 ?  160 LEU   B HD23 1 
ATOM   6260 N  N    . TYR   B 1 161 ? 43.675 -36.981 -8.368  1.00 15.63 ?  161 TYR   B N    1 
ATOM   6261 C  CA   . TYR   B 1 161 ? 43.004 -36.418 -9.535  1.00 15.64 ?  161 TYR   B CA   1 
ATOM   6262 C  C    . TYR   B 1 161 ? 42.058 -37.439 -10.155 1.00 15.35 ?  161 TYR   B C    1 
ATOM   6263 O  O    . TYR   B 1 161 ? 40.887 -37.143 -10.416 1.00 15.08 ?  161 TYR   B O    1 
ATOM   6264 C  CB   . TYR   B 1 161 ? 44.049 -35.943 -10.553 1.00 16.22 ?  161 TYR   B CB   1 
ATOM   6265 C  CG   . TYR   B 1 161 ? 43.471 -35.473 -11.868 1.00 16.75 ?  161 TYR   B CG   1 
ATOM   6266 C  CD1  . TYR   B 1 161 ? 43.075 -34.152 -12.039 1.00 16.75 ?  161 TYR   B CD1  1 
ATOM   6267 C  CD2  . TYR   B 1 161 ? 43.310 -36.348 -12.937 1.00 17.06 ?  161 TYR   B CD2  1 
ATOM   6268 C  CE1  . TYR   B 1 161 ? 42.545 -33.717 -13.229 1.00 17.76 ?  161 TYR   B CE1  1 
ATOM   6269 C  CE2  . TYR   B 1 161 ? 42.773 -35.922 -14.132 1.00 18.33 ?  161 TYR   B CE2  1 
ATOM   6270 C  CZ   . TYR   B 1 161 ? 42.393 -34.605 -14.273 1.00 18.38 ?  161 TYR   B CZ   1 
ATOM   6271 O  OH   . TYR   B 1 161 ? 41.859 -34.168 -15.458 1.00 20.28 ?  161 TYR   B OH   1 
ATOM   6272 H  H    . TYR   B 1 161 ? 44.531 -36.911 -8.387  1.00 18.73 ?  161 TYR   B H    1 
ATOM   6273 H  HA   . TYR   B 1 161 ? 42.480 -35.648 -9.265  1.00 18.75 ?  161 TYR   B HA   1 
ATOM   6274 H  HB2  . TYR   B 1 161 ? 44.545 -35.198 -10.172 1.00 19.45 ?  161 TYR   B HB2  1 
ATOM   6275 H  HB3  . TYR   B 1 161 ? 44.657 -36.672 -10.748 1.00 19.45 ?  161 TYR   B HB3  1 
ATOM   6276 H  HD1  . TYR   B 1 161 ? 43.177 -33.545 -11.340 1.00 20.07 ?  161 TYR   B HD1  1 
ATOM   6277 H  HD2  . TYR   B 1 161 ? 43.562 -37.238 -12.848 1.00 20.44 ?  161 TYR   B HD2  1 
ATOM   6278 H  HE1  . TYR   B 1 161 ? 42.285 -32.824 -13.327 1.00 21.28 ?  161 TYR   B HE1  1 
ATOM   6279 H  HE2  . TYR   B 1 161 ? 42.667 -36.515 -14.841 1.00 21.97 ?  161 TYR   B HE2  1 
ATOM   6280 H  HH   . TYR   B 1 161 ? 41.814 -34.805 -16.005 1.00 24.32 ?  161 TYR   B HH   1 
ATOM   6281 N  N    . ASP   B 1 162 ? 42.554 -38.657 -10.381 1.00 15.89 ?  162 ASP   B N    1 
ATOM   6282 C  CA   . ASP   B 1 162 ? 41.727 -39.690 -10.998 1.00 16.71 ?  162 ASP   B CA   1 
ATOM   6283 C  C    . ASP   B 1 162 ? 40.522 -40.030 -10.128 1.00 16.07 ?  162 ASP   B C    1 
ATOM   6284 O  O    . ASP   B 1 162 ? 39.417 -40.243 -10.641 1.00 16.35 ?  162 ASP   B O    1 
ATOM   6285 C  CB   . ASP   B 1 162 ? 42.559 -40.949 -11.252 1.00 18.33 ?  162 ASP   B CB   1 
ATOM   6286 C  CG   . ASP   B 1 162 ? 43.566 -40.783 -12.376 1.00 19.78 ?  162 ASP   B CG   1 
ATOM   6287 O  OD1  . ASP   B 1 162 ? 43.444 -39.840 -13.178 1.00 19.88 ?  162 ASP   B OD1  1 
ATOM   6288 O  OD2  . ASP   B 1 162 ? 44.471 -41.636 -12.475 1.00 21.40 -1 162 ASP   B OD2  1 
ATOM   6289 H  H    . ASP   B 1 162 ? 43.353 -38.903 -10.190 1.00 19.04 ?  162 ASP   B H    1 
ATOM   6290 H  HA   . ASP   B 1 162 ? 41.397 -39.366 -11.849 1.00 20.03 ?  162 ASP   B HA   1 
ATOM   6291 H  HB2  . ASP   B 1 162 ? 43.052 -41.171 -10.450 1.00 21.97 ?  162 ASP   B HB2  1 
ATOM   6292 H  HB3  . ASP   B 1 162 ? 41.964 -41.675 -11.492 1.00 21.97 ?  162 ASP   B HB3  1 
ATOM   6293 N  N    . LYS   B 1 163 ? 40.716 -40.102 -8.810  1.00 15.54 ?  163 LYS   B N    1 
ATOM   6294 C  CA   . LYS   B 1 163 ? 39.596 -40.380 -7.917  1.00 16.04 ?  163 LYS   B CA   1 
ATOM   6295 C  C    . LYS   B 1 163 ? 38.549 -39.274 -7.980  1.00 14.93 ?  163 LYS   B C    1 
ATOM   6296 O  O    . LYS   B 1 163 ? 37.342 -39.549 -7.981  1.00 15.82 ?  163 LYS   B O    1 
ATOM   6297 C  CB   . LYS   B 1 163 ? 40.094 -40.553 -6.484  1.00 18.93 ?  163 LYS   B CB   1 
ATOM   6298 C  CG   . LYS   B 1 163 ? 39.009 -41.046 -5.551  1.00 24.79 ?  163 LYS   B CG   1 
ATOM   6299 C  CD   . LYS   B 1 163 ? 39.490 -41.214 -4.124  1.00 30.79 ?  163 LYS   B CD   1 
ATOM   6300 C  CE   . LYS   B 1 163 ? 38.417 -41.893 -3.283  1.00 35.42 ?  163 LYS   B CE   1 
ATOM   6301 N  NZ   . LYS   B 1 163 ? 38.555 -41.598 -1.831  1.00 38.53 ?  163 LYS   B NZ   1 
ATOM   6302 H  H    . LYS   B 1 163 ? 41.476 -39.991 -8.418  1.00 18.62 ?  163 LYS   B H    1 
ATOM   6303 H  HA   . LYS   B 1 163 ? 39.178 -41.209 -8.191  1.00 19.22 ?  163 LYS   B HA   1 
ATOM   6304 H  HB2  . LYS   B 1 163 ? 40.817 -41.202 -6.476  1.00 22.69 ?  163 LYS   B HB2  1 
ATOM   6305 H  HB3  . LYS   B 1 163 ? 40.412 -39.699 -6.153  1.00 22.69 ?  163 LYS   B HB3  1 
ATOM   6306 H  HG2  . LYS   B 1 163 ? 38.280 -40.407 -5.546  1.00 29.73 ?  163 LYS   B HG2  1 
ATOM   6307 H  HG3  . LYS   B 1 163 ? 38.692 -41.909 -5.865  1.00 29.73 ?  163 LYS   B HG3  1 
ATOM   6308 H  HD2  . LYS   B 1 163 ? 40.286 -41.770 -4.114  1.00 36.92 ?  163 LYS   B HD2  1 
ATOM   6309 H  HD3  . LYS   B 1 163 ? 39.678 -40.344 -3.741  1.00 36.92 ?  163 LYS   B HD3  1 
ATOM   6310 H  HE2  . LYS   B 1 163 ? 37.542 -41.593 -3.574  1.00 42.48 ?  163 LYS   B HE2  1 
ATOM   6311 H  HE3  . LYS   B 1 163 ? 38.489 -42.853 -3.400  1.00 42.48 ?  163 LYS   B HE3  1 
ATOM   6312 H  HZ1  . LYS   B 1 163 ? 37.911 -42.010 -1.375  1.00 46.21 ?  163 LYS   B HZ1  1 
ATOM   6313 H  HZ2  . LYS   B 1 163 ? 39.345 -41.882 -1.537  1.00 46.21 ?  163 LYS   B HZ2  1 
ATOM   6314 H  HZ3  . LYS   B 1 163 ? 38.491 -40.721 -1.692  1.00 46.21 ?  163 LYS   B HZ3  1 
ATOM   6315 N  N    . LEU   B 1 164 ? 39.000 -38.019 -8.034  1.00 13.84 ?  164 LEU   B N    1 
ATOM   6316 C  CA   . LEU   B 1 164 ? 38.089 -36.881 -8.091  1.00 13.46 ?  164 LEU   B CA   1 
ATOM   6317 C  C    . LEU   B 1 164 ? 37.308 -36.863 -9.399  1.00 13.56 ?  164 LEU   B C    1 
ATOM   6318 O  O    . LEU   B 1 164 ? 36.085 -36.671 -9.402  1.00 14.40 ?  164 LEU   B O    1 
ATOM   6319 C  CB   . LEU   B 1 164 ? 38.890 -35.589 -7.930  1.00 12.83 ?  164 LEU   B CB   1 
ATOM   6320 C  CG   . LEU   B 1 164 ? 39.415 -35.312 -6.524  1.00 13.73 ?  164 LEU   B CG   1 
ATOM   6321 C  CD1  . LEU   B 1 164 ? 40.505 -34.257 -6.570  1.00 13.80 ?  164 LEU   B CD1  1 
ATOM   6322 C  CD2  . LEU   B 1 164 ? 38.294 -34.885 -5.598  1.00 15.24 ?  164 LEU   B CD2  1 
ATOM   6323 H  H    . LEU   B 1 164 ? 39.836 -37.802 -8.038  1.00 16.58 ?  164 LEU   B H    1 
ATOM   6324 H  HA   . LEU   B 1 164 ? 37.459 -36.940 -7.362  1.00 16.12 ?  164 LEU   B HA   1 
ATOM   6325 H  HB2  . LEU   B 1 164 ? 39.660 -35.626 -8.525  1.00 15.37 ?  164 LEU   B HB2  1 
ATOM   6326 H  HB3  . LEU   B 1 164 ? 38.328 -34.842 -8.182  1.00 15.37 ?  164 LEU   B HB3  1 
ATOM   6327 H  HG   . LEU   B 1 164 ? 39.811 -36.120 -6.170  1.00 16.45 ?  164 LEU   B HG   1 
ATOM   6328 H  HD11 . LEU   B 1 164 ? 40.823 -34.084 -5.668  1.00 16.53 ?  164 LEU   B HD11 1 
ATOM   6329 H  HD12 . LEU   B 1 164 ? 41.242 -34.577 -7.119  1.00 16.53 ?  164 LEU   B HD12 1 
ATOM   6330 H  HD13 . LEU   B 1 164 ? 40.147 -33.438 -6.953  1.00 16.53 ?  164 LEU   B HD13 1 
ATOM   6331 H  HD21 . LEU   B 1 164 ? 38.668 -34.654 -4.734  1.00 18.26 ?  164 LEU   B HD21 1 
ATOM   6332 H  HD22 . LEU   B 1 164 ? 37.843 -34.116 -5.981  1.00 18.26 ?  164 LEU   B HD22 1 
ATOM   6333 H  HD23 . LEU   B 1 164 ? 37.671 -35.622 -5.504  1.00 18.26 ?  164 LEU   B HD23 1 
ATOM   6334 N  N    . VAL   B 1 165 ? 38.000 -37.036 -10.526 1.00 14.96 ?  165 VAL   B N    1 
ATOM   6335 C  CA   . VAL   B 1 165 ? 37.344 -36.972 -11.828 1.00 16.24 ?  165 VAL   B CA   1 
ATOM   6336 C  C    . VAL   B 1 165 ? 36.424 -38.169 -12.015 1.00 17.72 ?  165 VAL   B C    1 
ATOM   6337 O  O    . VAL   B 1 165 ? 35.269 -38.030 -12.435 1.00 18.80 ?  165 VAL   B O    1 
ATOM   6338 C  CB   . VAL   B 1 165 ? 38.393 -36.885 -12.952 1.00 17.47 ?  165 VAL   B CB   1 
ATOM   6339 C  CG1  . VAL   B 1 165 ? 37.734 -36.995 -14.308 1.00 18.78 ?  165 VAL   B CG1  1 
ATOM   6340 C  CG2  . VAL   B 1 165 ? 39.184 -35.600 -12.842 1.00 17.36 ?  165 VAL   B CG2  1 
ATOM   6341 H  H    . VAL   B 1 165 ? 38.849 -37.181 -10.563 1.00 17.92 ?  165 VAL   B H    1 
ATOM   6342 H  HA   . VAL   B 1 165 ? 36.802 -36.171 -11.869 1.00 19.46 ?  165 VAL   B HA   1 
ATOM   6343 H  HB   . VAL   B 1 165 ? 39.017 -37.620 -12.860 1.00 20.93 ?  165 VAL   B HB   1 
ATOM   6344 H  HG11 . VAL   B 1 165 ? 38.355 -36.695 -14.986 1.00 22.52 ?  165 VAL   B HG11 1 
ATOM   6345 H  HG12 . VAL   B 1 165 ? 37.501 -37.926 -14.466 1.00 22.52 ?  165 VAL   B HG12 1 
ATOM   6346 H  HG13 . VAL   B 1 165 ? 36.936 -36.449 -14.317 1.00 22.52 ?  165 VAL   B HG13 1 
ATOM   6347 H  HG21 . VAL   B 1 165 ? 39.820 -35.553 -13.575 1.00 20.80 ?  165 VAL   B HG21 1 
ATOM   6348 H  HG22 . VAL   B 1 165 ? 38.574 -34.846 -12.888 1.00 20.80 ?  165 VAL   B HG22 1 
ATOM   6349 H  HG23 . VAL   B 1 165 ? 39.658 -35.588 -11.995 1.00 20.80 ?  165 VAL   B HG23 1 
ATOM   6350 N  N    . SER   B 1 166 ? 36.928 -39.367 -11.704 1.00 18.45 ?  166 SER   B N    1 
ATOM   6351 C  CA   . SER   B 1 166 ? 36.173 -40.579 -11.987 1.00 20.23 ?  166 SER   B CA   1 
ATOM   6352 C  C    . SER   B 1 166 ? 34.915 -40.669 -11.138 1.00 20.37 ?  166 SER   B C    1 
ATOM   6353 O  O    . SER   B 1 166 ? 33.940 -41.290 -11.564 1.00 21.97 ?  166 SER   B O    1 
ATOM   6354 C  CB   . SER   B 1 166 ? 37.044 -41.830 -11.816 1.00 21.37 ?  166 SER   B CB   1 
ATOM   6355 O  OG   . SER   B 1 166 ? 37.413 -42.045 -10.465 1.00 21.44 ?  166 SER   B OG   1 
ATOM   6356 H  H    . SER   B 1 166 ? 37.698 -39.499 -11.337 1.00 22.12 ?  166 SER   B H    1 
ATOM   6357 H  HA   . SER   B 1 166 ? 35.896 -40.552 -12.915 1.00 24.25 ?  166 SER   B HA   1 
ATOM   6358 H  HB2  . SER   B 1 166 ? 36.545 -42.602 -12.127 1.00 25.62 ?  166 SER   B HB2  1 
ATOM   6359 H  HB3  . SER   B 1 166 ? 37.849 -41.726 -12.351 1.00 25.62 ?  166 SER   B HB3  1 
ATOM   6360 H  HG   . SER   B 1 166 ? 37.861 -41.389 -10.187 1.00 25.71 ?  166 SER   B HG   1 
ATOM   6361 N  N    . SER   B 1 167 ? 34.901 -40.057 -9.955  1.00 18.99 ?  167 SER   B N    1 
ATOM   6362 C  CA   . SER   B 1 167 ? 33.744 -40.118 -9.071  1.00 18.65 ?  167 SER   B CA   1 
ATOM   6363 C  C    . SER   B 1 167 ? 32.827 -38.902 -9.172  1.00 17.98 ?  167 SER   B C    1 
ATOM   6364 O  O    . SER   B 1 167 ? 31.753 -38.904 -8.561  1.00 18.00 ?  167 SER   B O    1 
ATOM   6365 C  CB   . SER   B 1 167 ? 34.187 -40.300 -7.614  1.00 18.72 ?  167 SER   B CB   1 
ATOM   6366 O  OG   . SER   B 1 167 ? 34.860 -39.141 -7.143  1.00 18.43 ?  167 SER   B OG   1 
ATOM   6367 H  H    . SER   B 1 167 ? 35.555 -39.601 -9.643  1.00 22.76 ?  167 SER   B H    1 
ATOM   6368 H  HA   . SER   B 1 167 ? 33.218 -40.898 -9.312  1.00 22.36 ?  167 SER   B HA   1 
ATOM   6369 H  HB2  . SER   B 1 167 ? 33.404 -40.461 -7.065  1.00 22.43 ?  167 SER   B HB2  1 
ATOM   6370 H  HB3  . SER   B 1 167 ? 34.786 -41.067 -7.563  1.00 22.43 ?  167 SER   B HB3  1 
ATOM   6371 H  HG   . SER   B 1 167 ? 35.544 -39.006 -7.612  1.00 22.09 ?  167 SER   B HG   1 
ATOM   6372 N  N    . PHE   B 1 168 ? 33.204 -37.871 -9.928  1.00 17.57 ?  168 PHE   B N    1 
ATOM   6373 C  CA   . PHE   B 1 168 ? 32.372 -36.670 -9.986  1.00 16.96 ?  168 PHE   B CA   1 
ATOM   6374 C  C    . PHE   B 1 168 ? 31.056 -36.928 -10.713 1.00 14.98 ?  168 PHE   B C    1 
ATOM   6375 O  O    . PHE   B 1 168 ? 30.017 -36.331 -10.372 1.00 15.58 ?  168 PHE   B O    1 
ATOM   6376 C  CB   . PHE   B 1 168 ? 33.129 -35.532 -10.661 1.00 17.84 ?  168 PHE   B CB   1 
ATOM   6377 C  CG   . PHE   B 1 168 ? 32.325 -34.283 -10.776 1.00 18.03 ?  168 PHE   B CG   1 
ATOM   6378 C  CD1  . PHE   B 1 168 ? 32.005 -33.551 -9.642  1.00 19.00 ?  168 PHE   B CD1  1 
ATOM   6379 C  CD2  . PHE   B 1 168 ? 31.868 -33.846 -12.001 1.00 17.40 ?  168 PHE   B CD2  1 
ATOM   6380 C  CE1  . PHE   B 1 168 ? 31.243 -32.402 -9.728  1.00 19.28 ?  168 PHE   B CE1  1 
ATOM   6381 C  CE2  . PHE   B 1 168 ? 31.118 -32.683 -12.099 1.00 18.32 ?  168 PHE   B CE2  1 
ATOM   6382 C  CZ   . PHE   B 1 168 ? 30.800 -31.963 -10.958 1.00 18.57 ?  168 PHE   B CZ   1 
ATOM   6383 H  H    . PHE   B 1 168 ? 33.923 -37.840 -10.400 1.00 21.06 ?  168 PHE   B H    1 
ATOM   6384 H  HA   . PHE   B 1 168 ? 32.160 -36.393 -9.085  1.00 20.33 ?  168 PHE   B HA   1 
ATOM   6385 H  HB2  . PHE   B 1 168 ? 33.921 -35.328 -10.140 1.00 21.38 ?  168 PHE   B HB2  1 
ATOM   6386 H  HB3  . PHE   B 1 168 ? 33.382 -35.803 -11.556 1.00 21.38 ?  168 PHE   B HB3  1 
ATOM   6387 H  HD1  . PHE   B 1 168 ? 32.298 -33.847 -8.811  1.00 22.78 ?  168 PHE   B HD1  1 
ATOM   6388 H  HD2  . PHE   B 1 168 ? 32.078 -34.320 -12.769 1.00 20.85 ?  168 PHE   B HD2  1 
ATOM   6389 H  HE1  . PHE   B 1 168 ? 31.037 -31.922 -8.958  1.00 23.12 ?  168 PHE   B HE1  1 
ATOM   6390 H  HE2  . PHE   B 1 168 ? 30.815 -32.392 -12.931 1.00 21.95 ?  168 PHE   B HE2  1 
ATOM   6391 H  HZ   . PHE   B 1 168 ? 30.290 -31.186 -11.024 1.00 22.26 ?  168 PHE   B HZ   1 
ATOM   6392 N  N    . LEU   B 1 169 ? 31.083 -37.813 -11.705 1.00 15.15 ?  169 LEU   B N    1 
ATOM   6393 C  CA   . LEU   B 1 169 ? 29.906 -38.119 -12.504 1.00 17.80 ?  169 LEU   B CA   1 
ATOM   6394 C  C    . LEU   B 1 169 ? 29.905 -39.559 -12.996 1.00 20.73 ?  169 LEU   B C    1 
ATOM   6395 O  O    . LEU   B 1 169 ? 29.019 -39.972 -13.744 1.00 23.05 ?  169 LEU   B O    1 
ATOM   6396 C  CB   . LEU   B 1 169 ? 29.839 -37.180 -13.707 1.00 19.72 ?  169 LEU   B CB   1 
ATOM   6397 C  CG   . LEU   B 1 169 ? 28.586 -36.313 -13.800 1.00 22.76 ?  169 LEU   B CG   1 
ATOM   6398 C  CD1  . LEU   B 1 169 ? 28.534 -35.628 -15.150 1.00 23.67 ?  169 LEU   B CD1  1 
ATOM   6399 C  CD2  . LEU   B 1 169 ? 27.327 -37.127 -13.562 1.00 23.07 ?  169 LEU   B CD2  1 
ATOM   6400 O  OXT  . LEU   B 1 169 ? 30.797 -40.335 -12.667 1.00 21.42 -1 169 LEU   B OXT  1 
ATOM   6401 H  H    . LEU   B 1 169 ? 31.783 -38.254 -11.944 1.00 18.15 ?  169 LEU   B H    1 
ATOM   6402 H  HA   . LEU   B 1 169 ? 29.119 -37.982 -11.957 1.00 21.33 ?  169 LEU   B HA   1 
ATOM   6403 H  HB2  . LEU   B 1 169 ? 30.602 -36.581 -13.676 1.00 23.64 ?  169 LEU   B HB2  1 
ATOM   6404 H  HB3  . LEU   B 1 169 ? 29.879 -37.711 -14.518 1.00 23.64 ?  169 LEU   B HB3  1 
ATOM   6405 H  HG   . LEU   B 1 169 ? 28.628 -35.620 -13.120 1.00 27.28 ?  169 LEU   B HG   1 
ATOM   6406 H  HD11 . LEU   B 1 169 ? 27.749 -35.060 -15.186 1.00 28.38 ?  169 LEU   B HD11 1 
ATOM   6407 H  HD12 . LEU   B 1 169 ? 29.336 -35.095 -15.263 1.00 28.38 ?  169 LEU   B HD12 1 
ATOM   6408 H  HD13 . LEU   B 1 169 ? 28.486 -36.306 -15.842 1.00 28.38 ?  169 LEU   B HD13 1 
ATOM   6409 H  HD21 . LEU   B 1 169 ? 26.580 -36.696 -14.000 1.00 27.66 ?  169 LEU   B HD21 1 
ATOM   6410 H  HD22 . LEU   B 1 169 ? 27.456 -38.019 -13.926 1.00 27.66 ?  169 LEU   B HD22 1 
ATOM   6411 H  HD23 . LEU   B 1 169 ? 27.166 -37.182 -12.607 1.00 27.66 ?  169 LEU   B HD23 1 
HETATM 6412 N  N2   B A1BAD C 2 .   ? 15.102 1.056   1.629   0.20 15.09 ?  201 A1BAD A N2   1 
HETATM 6413 C  C3   B A1BAD C 2 .   ? 13.488 -0.577  0.445   0.20 17.51 ?  201 A1BAD A C3   1 
HETATM 6414 C  C6   B A1BAD C 2 .   ? 11.273 2.615   0.184   0.20 18.83 ?  201 A1BAD A C6   1 
HETATM 6415 C  C9   B A1BAD C 2 .   ? 15.111 1.040   3.054   0.20 14.09 ?  201 A1BAD A C9   1 
HETATM 6416 C  C12  B A1BAD C 2 .   ? 15.352 2.236   3.811   0.20 13.39 ?  201 A1BAD A C12  1 
HETATM 6417 C  C14  B A1BAD C 2 .   ? 15.758 4.242   4.842   0.20 13.06 ?  201 A1BAD A C14  1 
HETATM 6418 C  C1   B A1BAD C 2 .   ? 15.955 -1.265  0.903   0.20 17.00 ?  201 A1BAD A C1   1 
HETATM 6419 C  C10  B A1BAD C 2 .   ? 14.905 -0.092  5.139   0.20 13.59 ?  201 A1BAD A C10  1 
HETATM 6420 C  C11  B A1BAD C 2 .   ? 15.334 2.082   5.221   0.20 13.08 ?  201 A1BAD A C11  1 
HETATM 6421 C  C13  B A1BAD C 2 .   ? 15.629 3.628   3.611   0.20 13.27 ?  201 A1BAD A C13  1 
HETATM 6422 C  C2   B A1BAD C 2 .   ? 14.972 -0.051  0.610   0.20 16.47 ?  201 A1BAD A C2   1 
HETATM 6423 C  C4   B A1BAD C 2 .   ? 12.401 0.455   0.000   0.20 18.16 ?  201 A1BAD A C4   1 
HETATM 6424 C  C5   B A1BAD C 2 .   ? 12.264 1.724   0.608   0.20 18.50 ?  201 A1BAD A C5   1 
HETATM 6425 C  C7   B A1BAD C 2 .   ? 10.403 2.257   -0.838  0.20 18.76 ?  201 A1BAD A C7   1 
HETATM 6426 C  C8   B A1BAD C 2 .   ? 10.577 0.986   -1.399  0.20 18.56 ?  201 A1BAD A C8   1 
HETATM 6427 N  N1   B A1BAD C 2 .   ? 11.536 0.102   -1.003  0.20 18.29 ?  201 A1BAD A N1   1 
HETATM 6428 N  N3   B A1BAD C 2 .   ? 14.887 -0.126  3.749   0.20 13.99 ?  201 A1BAD A N3   1 
HETATM 6429 N  N4   B A1BAD C 2 .   ? 15.117 0.953   5.961   0.20 13.15 ?  201 A1BAD A N4   1 
HETATM 6430 N  N5   B A1BAD C 2 .   ? 15.581 3.295   5.878   0.20 12.94 ?  201 A1BAD A N5   1 
HETATM 6431 O  O1   B A1BAD C 2 .   ? 15.578 -2.347  0.093   0.20 17.22 ?  201 A1BAD A O1   1 
HETATM 6432 H  H11  B A1BAD C 2 .   ? 15.197 1.966   1.238   0.20 18.08 ?  201 A1BAD A H11  1 
HETATM 6433 H  H5   B A1BAD C 2 .   ? 13.485 -1.380  -0.297  0.20 20.99 ?  201 A1BAD A H5   1 
HETATM 6434 H  H6   B A1BAD C 2 .   ? 13.196 -1.130  1.344   0.20 20.99 ?  201 A1BAD A H6   1 
HETATM 6435 H  H8   B A1BAD C 2 .   ? 11.171 3.605   0.646   0.20 22.57 ?  201 A1BAD A H8   1 
HETATM 6436 H  H14  B A1BAD C 2 .   ? 15.955 5.219   5.232   0.20 15.65 ?  201 A1BAD A H14  1 
HETATM 6437 H  H3   B A1BAD C 2 .   ? 17.011 -1.005  0.675   0.20 20.37 ?  201 A1BAD A H3   1 
HETATM 6438 H  H4   B A1BAD C 2 .   ? 15.948 -1.537  1.968   0.20 20.37 ?  201 A1BAD A H4   1 
HETATM 6439 H  H12  B A1BAD C 2 .   ? 14.718 -1.029  5.724   0.20 16.29 ?  201 A1BAD A H12  1 
HETATM 6440 H  H13  B A1BAD C 2 .   ? 15.730 4.195   2.711   0.20 15.90 ?  201 A1BAD A H13  1 
HETATM 6441 H  H1   B A1BAD C 2 .   ? 15.232 0.394   -0.369  0.20 19.75 ?  201 A1BAD A H1   1 
HETATM 6442 H  H7   B A1BAD C 2 .   ? 12.924 2.054   1.407   0.20 22.17 ?  201 A1BAD A H7   1 
HETATM 6443 H  H9   B A1BAD C 2 .   ? 9.621  2.948   -1.178  0.20 22.48 ?  201 A1BAD A H9   1 
HETATM 6444 H  H10  B A1BAD C 2 .   ? 9.895  0.670   -2.217  0.20 22.25 ?  201 A1BAD A H10  1 
HETATM 6445 H  H15  B A1BAD C 2 .   ? 15.622 3.465   6.848   0.20 15.50 ?  201 A1BAD A H15  1 
HETATM 6446 H  H2   B A1BAD C 2 .   ? 16.114 -3.114  0.322   0.20 20.64 ?  201 A1BAD A H2   1 
HETATM 6447 O  O1   C A1BAE D 3 .   ? 15.495 -2.229  -0.095  0.20 12.72 ?  202 A1BAE A O1   1 
HETATM 6448 C  C1   C A1BAE D 3 .   ? 15.884 -1.234  0.799   0.20 12.11 ?  202 A1BAE A C1   1 
HETATM 6449 C  C2   C A1BAE D 3 .   ? 14.609 -0.362  1.027   0.20 10.84 ?  202 A1BAE A C2   1 
HETATM 6450 C  C3   C A1BAE D 3 .   ? 14.081 0.113   -0.366  0.20 11.57 ?  202 A1BAE A C3   1 
HETATM 6451 C  C4   C A1BAE D 3 .   ? 12.729 0.811   -0.397  0.20 12.97 ?  202 A1BAE A C4   1 
HETATM 6452 C  C5   C A1BAE D 3 .   ? 12.525 2.064   0.209   0.20 13.63 ?  202 A1BAE A C5   1 
HETATM 6453 C  C6   C A1BAE D 3 .   ? 11.263 2.654   0.153   0.20 14.44 ?  202 A1BAE A C6   1 
HETATM 6454 C  C7   C A1BAE D 3 .   ? 10.231 2.000   -0.502  0.20 14.43 ?  202 A1BAE A C7   1 
HETATM 6455 C  C8   C A1BAE D 3 .   ? 10.514 0.758   -1.079  0.20 14.22 ?  202 A1BAE A C8   1 
HETATM 6456 C  C10  C A1BAE D 3 .   ? 14.895 -0.112  5.336   0.20 9.70  ?  202 A1BAE A C10  1 
HETATM 6457 C  C11  C A1BAE D 3 .   ? 15.357 2.094   5.293   0.20 9.20  ?  202 A1BAE A C11  1 
HETATM 6458 C  C12  C A1BAE D 3 .   ? 15.300 2.132   3.872   0.20 9.22  ?  202 A1BAE A C12  1 
HETATM 6459 C  C13  C A1BAE D 3 .   ? 15.573 3.486   3.506   0.20 9.42  ?  202 A1BAE A C13  1 
HETATM 6460 C  C14  C A1BAE D 3 .   ? 15.775 4.216   4.660   0.20 9.39  ?  202 A1BAE A C14  1 
HETATM 6461 C  C9   C A1BAE D 3 .   ? 15.011 0.903   3.221   0.20 9.44  ?  202 A1BAE A C9   1 
HETATM 6462 N  N1   C A1BAE D 3 .   ? 11.723 0.157   -1.038  0.20 13.68 ?  202 A1BAE A N1   1 
HETATM 6463 N  N2   C A1BAE D 3 .   ? 14.936 0.827   1.836   0.20 9.75  ?  202 A1BAE A N2   1 
HETATM 6464 N  N3   C A1BAE D 3 .   ? 14.812 -0.231  3.969   0.20 9.87  ?  202 A1BAE A N3   1 
HETATM 6465 N  N4   C A1BAE D 3 .   ? 15.161 0.981   6.082   0.20 9.44  ?  202 A1BAE A N4   1 
HETATM 6466 N  N5   C A1BAE D 3 .   ? 15.648 3.363   5.773   0.20 9.13  ?  202 A1BAE A N5   1 
HETATM 6467 H  H2   C A1BAE D 3 .   ? 16.280 -2.708  -0.358  0.20 15.24 ?  202 A1BAE A H2   1 
HETATM 6468 H  H4   C A1BAE D 3 .   ? 16.746 -0.642  0.434   0.20 14.51 ?  202 A1BAE A H4   1 
HETATM 6469 H  H3   C A1BAE D 3 .   ? 16.246 -1.705  1.749   0.20 14.51 ?  202 A1BAE A H3   1 
HETATM 6470 H  H1   C A1BAE D 3 .   ? 13.818 -0.977  1.557   0.20 12.98 ?  202 A1BAE A H1   1 
HETATM 6471 H  H6   C A1BAE D 3 .   ? 14.833 0.781   -0.841  0.20 13.86 ?  202 A1BAE A H6   1 
HETATM 6472 H  H5   C A1BAE D 3 .   ? 13.998 -0.738  -1.074  0.20 13.86 ?  202 A1BAE A H5   1 
HETATM 6473 H  H7   C A1BAE D 3 .   ? 13.331 2.587   0.727   0.20 16.34 ?  202 A1BAE A H7   1 
HETATM 6474 H  H8   C A1BAE D 3 .   ? 11.084 3.626   0.613   0.20 17.30 ?  202 A1BAE A H8   1 
HETATM 6475 H  H9   C A1BAE D 3 .   ? 9.238  2.435   -0.566  0.20 17.29 ?  202 A1BAE A H9   1 
HETATM 6476 H  H10  C A1BAE D 3 .   ? 9.739  0.194   -1.608  0.20 17.04 ?  202 A1BAE A H10  1 
HETATM 6477 H  H12  C A1BAE D 3 .   ? 14.720 -1.046  5.908   0.20 11.62 ?  202 A1BAE A H12  1 
HETATM 6478 H  H13  C A1BAE D 3 .   ? 15.614 3.896   2.510   0.20 11.28 ?  202 A1BAE A H13  1 
HETATM 6479 H  H14  C A1BAE D 3 .   ? 16.003 5.262   4.806   0.20 11.24 ?  202 A1BAE A H14  1 
HETATM 6480 H  H11  C A1BAE D 3 .   ? 15.128 1.669   1.340   0.20 11.67 ?  202 A1BAE A H11  1 
HETATM 6481 H  H15  C A1BAE D 3 .   ? 15.739 3.605   6.741   0.20 10.93 ?  202 A1BAE A H15  1 
HETATM 6482 CL CL   B CL    E 4 .   ? 16.154 2.791   -0.879  0.40 18.11 ?  203 CL    A CL   1 
HETATM 6483 O  O    . HOH   F 5 .   ? 4.797  3.829   0.770   1.00 23.25 ?  301 HOH   A O    1 
HETATM 6484 O  O    . HOH   F 5 .   ? 14.816 -4.626  20.529  1.00 43.64 ?  302 HOH   A O    1 
HETATM 6485 O  O    . HOH   F 5 .   ? 24.518 1.983   -6.972  1.00 20.64 ?  303 HOH   A O    1 
HETATM 6486 O  O    . HOH   F 5 .   ? 17.119 -18.010 15.087  1.00 26.13 ?  304 HOH   A O    1 
HETATM 6487 O  O    . HOH   F 5 .   ? 34.330 -1.878  12.500  1.00 35.40 ?  305 HOH   A O    1 
HETATM 6488 O  O    . HOH   F 5 .   ? 18.615 -2.385  -16.410 1.00 44.27 ?  306 HOH   A O    1 
HETATM 6489 O  O    . HOH   F 5 .   ? 28.900 0.459   -9.681  1.00 20.21 ?  307 HOH   A O    1 
HETATM 6490 O  O    . HOH   F 5 .   ? 12.046 0.394   14.842  1.00 34.64 ?  308 HOH   A O    1 
HETATM 6491 O  O    . HOH   F 5 .   ? 6.973  -8.081  11.966  1.00 20.09 ?  309 HOH   A O    1 
HETATM 6492 O  O    . HOH   F 5 .   ? 7.652  -6.301  -6.577  1.00 41.64 ?  310 HOH   A O    1 
HETATM 6493 O  O    . HOH   F 5 .   ? 13.980 -4.902  17.459  1.00 24.44 ?  311 HOH   A O    1 
HETATM 6494 O  O    . HOH   F 5 .   ? 11.651 -10.806 -10.020 1.00 44.18 ?  312 HOH   A O    1 
HETATM 6495 O  O    . HOH   F 5 .   ? 18.928 -21.946 6.933   1.00 31.52 ?  313 HOH   A O    1 
HETATM 6496 O  O    . HOH   F 5 .   ? 26.819 11.419  1.678   1.00 15.75 ?  314 HOH   A O    1 
HETATM 6497 O  O    . HOH   F 5 .   ? 15.112 -12.197 18.692  1.00 36.08 ?  315 HOH   A O    1 
HETATM 6498 O  O    B HOH   F 5 .   ? 15.260 6.935   7.117   0.40 20.05 ?  316 HOH   A O    1 
HETATM 6499 O  O    . HOH   F 5 .   ? 42.426 10.553  5.203   1.00 19.42 ?  317 HOH   A O    1 
HETATM 6500 O  O    . HOH   F 5 .   ? 14.734 -13.981 16.699  1.00 23.87 ?  318 HOH   A O    1 
HETATM 6501 O  O    . HOH   F 5 .   ? 30.204 -13.325 -8.530  1.00 18.85 ?  319 HOH   A O    1 
HETATM 6502 O  O    . HOH   F 5 .   ? 28.176 -6.295  19.643  1.00 41.90 ?  320 HOH   A O    1 
HETATM 6503 O  O    . HOH   F 5 .   ? 19.852 -12.489 -8.892  1.00 24.25 ?  321 HOH   A O    1 
HETATM 6504 O  O    . HOH   F 5 .   ? 36.159 -5.087  -0.538  1.00 28.13 ?  322 HOH   A O    1 
HETATM 6505 O  O    . HOH   F 5 .   ? 9.850  -21.327 5.738   1.00 18.54 ?  323 HOH   A O    1 
HETATM 6506 O  O    . HOH   F 5 .   ? 33.944 -1.046  -8.908  1.00 26.96 ?  324 HOH   A O    1 
HETATM 6507 O  O    A HOH   F 5 .   ? 17.471 -1.694  0.470   0.60 17.17 ?  325 HOH   A O    1 
HETATM 6508 O  O    . HOH   F 5 .   ? 30.992 -18.133 7.796   1.00 19.11 ?  326 HOH   A O    1 
HETATM 6509 O  O    . HOH   F 5 .   ? 28.258 -0.121  -13.360 1.00 32.57 ?  327 HOH   A O    1 
HETATM 6510 O  O    . HOH   F 5 .   ? 14.127 -4.521  -11.839 1.00 33.15 ?  328 HOH   A O    1 
HETATM 6511 O  O    . HOH   F 5 .   ? 15.003 3.915   17.690  1.00 40.33 ?  329 HOH   A O    1 
HETATM 6512 O  O    . HOH   F 5 .   ? 8.023  -21.476 4.018   1.00 48.19 ?  330 HOH   A O    1 
HETATM 6513 O  O    A HOH   F 5 .   ? 3.582  -9.446  9.768   0.60 29.97 ?  331 HOH   A O    1 
HETATM 6514 O  O    . HOH   F 5 .   ? -0.722 -8.468  2.201   1.00 45.15 ?  332 HOH   A O    1 
HETATM 6515 O  O    . HOH   F 5 .   ? 23.893 -15.722 -9.158  1.00 34.06 ?  333 HOH   A O    1 
HETATM 6516 O  O    . HOH   F 5 .   ? 27.271 13.755  2.879   1.00 27.36 ?  334 HOH   A O    1 
HETATM 6517 O  O    A HOH   F 5 .   ? 14.612 -3.636  3.127   0.60 16.23 ?  335 HOH   A O    1 
HETATM 6518 O  O    . HOH   F 5 .   ? 0.755  -4.401  0.199   1.00 30.43 ?  336 HOH   A O    1 
HETATM 6519 O  O    . HOH   F 5 .   ? 20.576 -19.702 -5.020  1.00 25.76 ?  337 HOH   A O    1 
HETATM 6520 O  O    . HOH   F 5 .   ? 11.758 -10.699 17.081  1.00 27.04 ?  338 HOH   A O    1 
HETATM 6521 O  O    . HOH   F 5 .   ? 7.941  -12.530 -0.832  1.00 20.98 ?  339 HOH   A O    1 
HETATM 6522 O  O    . HOH   F 5 .   ? 13.525 -15.224 -7.427  1.00 24.94 ?  340 HOH   A O    1 
HETATM 6523 O  O    B HOH   F 5 .   ? 21.364 -2.282  -2.645  0.40 14.41 ?  341 HOH   A O    1 
HETATM 6524 O  O    . HOH   F 5 .   ? 38.545 4.979   6.962   1.00 14.99 ?  342 HOH   A O    1 
HETATM 6525 O  O    . HOH   F 5 .   ? 37.556 2.774   10.202  1.00 26.97 ?  343 HOH   A O    1 
HETATM 6526 O  O    . HOH   F 5 .   ? 18.652 -19.345 13.570  1.00 33.48 ?  344 HOH   A O    1 
HETATM 6527 O  O    . HOH   F 5 .   ? 39.710 -1.019  -5.219  1.00 19.63 ?  345 HOH   A O    1 
HETATM 6528 O  O    . HOH   F 5 .   ? 38.267 10.104  7.176   1.00 39.87 ?  346 HOH   A O    1 
HETATM 6529 O  O    . HOH   F 5 .   ? 44.292 7.093   6.435   1.00 26.26 ?  347 HOH   A O    1 
HETATM 6530 O  O    . HOH   F 5 .   ? 17.108 -17.783 -5.002  1.00 26.59 ?  348 HOH   A O    1 
HETATM 6531 O  O    . HOH   F 5 .   ? 14.446 -0.513  -12.043 1.00 23.99 ?  349 HOH   A O    1 
HETATM 6532 O  O    . HOH   F 5 .   ? 22.722 12.516  1.660   1.00 13.82 ?  350 HOH   A O    1 
HETATM 6533 O  O    . HOH   F 5 .   ? 42.516 4.266   5.336   1.00 29.86 ?  351 HOH   A O    1 
HETATM 6534 O  O    . HOH   F 5 .   ? 14.311 -21.135 -4.235  1.00 30.33 ?  352 HOH   A O    1 
HETATM 6535 O  O    . HOH   F 5 .   ? 31.687 8.218   14.815  1.00 22.38 ?  353 HOH   A O    1 
HETATM 6536 O  O    . HOH   F 5 .   ? 13.230 -1.430  -6.595  1.00 16.63 ?  354 HOH   A O    1 
HETATM 6537 O  O    A HOH   F 5 .   ? -0.500 -3.070  3.145   0.60 30.76 ?  355 HOH   A O    1 
HETATM 6538 O  O    . HOH   F 5 .   ? 37.207 -2.803  9.675   1.00 40.26 ?  356 HOH   A O    1 
HETATM 6539 O  O    B HOH   F 5 .   ? 8.135  3.937   1.386   0.40 19.53 ?  357 HOH   A O    1 
HETATM 6540 O  O    . HOH   F 5 .   ? 24.377 3.561   -1.788  1.00 14.01 ?  358 HOH   A O    1 
HETATM 6541 O  O    . HOH   F 5 .   ? 35.763 -12.683 6.829   1.00 15.05 ?  359 HOH   A O    1 
HETATM 6542 O  O    . HOH   F 5 .   ? 24.012 -2.107  -2.082  1.00 10.09 ?  360 HOH   A O    1 
HETATM 6543 O  O    . HOH   F 5 .   ? 37.311 11.945  4.927   1.00 32.70 ?  361 HOH   A O    1 
HETATM 6544 O  O    . HOH   F 5 .   ? 18.564 9.446   9.007   1.00 21.15 ?  362 HOH   A O    1 
HETATM 6545 O  O    . HOH   F 5 .   ? 22.179 -19.245 11.402  1.00 32.97 ?  363 HOH   A O    1 
HETATM 6546 O  O    . HOH   F 5 .   ? 33.635 -7.152  4.279   1.00 15.75 ?  364 HOH   A O    1 
HETATM 6547 O  O    A HOH   F 5 .   ? 14.257 0.590   6.833   0.60 24.05 ?  365 HOH   A O    1 
HETATM 6548 O  O    . HOH   F 5 .   ? 22.322 5.382   19.017  1.00 43.38 ?  366 HOH   A O    1 
HETATM 6549 O  O    B HOH   F 5 .   ? 21.196 2.696   0.023   0.40 15.52 ?  367 HOH   A O    1 
HETATM 6550 O  O    . HOH   F 5 .   ? 31.049 -13.926 -2.472  1.00 12.63 ?  368 HOH   A O    1 
HETATM 6551 O  O    . HOH   F 5 .   ? 31.805 -9.334  -6.647  1.00 21.19 ?  369 HOH   A O    1 
HETATM 6552 O  O    . HOH   F 5 .   ? 30.794 3.092   8.269   1.00 11.38 ?  370 HOH   A O    1 
HETATM 6553 O  O    B HOH   F 5 .   ? 14.981 -2.867  3.450   0.40 13.65 ?  371 HOH   A O    1 
HETATM 6554 O  O    A HOH   F 5 .   ? 21.218 -2.376  -2.027  0.60 11.58 ?  372 HOH   A O    1 
HETATM 6555 O  O    . HOH   F 5 .   ? 43.879 8.445   -3.089  1.00 25.73 ?  373 HOH   A O    1 
HETATM 6556 O  O    . HOH   F 5 .   ? 15.485 11.893  7.935   1.00 35.82 ?  374 HOH   A O    1 
HETATM 6557 O  O    . HOH   F 5 .   ? 16.488 -22.007 0.993   1.00 27.55 ?  375 HOH   A O    1 
HETATM 6558 O  O    B HOH   F 5 .   ? 11.193 -0.958  2.336   0.40 24.51 ?  376 HOH   A O    1 
HETATM 6559 O  O    . HOH   F 5 .   ? 16.981 -19.245 4.925   1.00 14.36 ?  377 HOH   A O    1 
HETATM 6560 O  O    . HOH   F 5 .   ? 21.888 -21.906 8.429   1.00 27.01 ?  378 HOH   A O    1 
HETATM 6561 O  O    B HOH   F 5 .   ? 13.137 -3.435  -0.673  0.40 28.00 ?  379 HOH   A O    1 
HETATM 6562 O  O    . HOH   F 5 .   ? 43.344 7.821   2.676   1.00 24.66 ?  380 HOH   A O    1 
HETATM 6563 O  O    . HOH   F 5 .   ? 23.450 11.380  4.102   1.00 11.55 ?  381 HOH   A O    1 
HETATM 6564 O  O    . HOH   F 5 .   ? 22.634 -11.927 21.861  1.00 44.96 ?  382 HOH   A O    1 
HETATM 6565 O  O    . HOH   F 5 .   ? 25.665 -0.787  -7.327  1.00 14.87 ?  383 HOH   A O    1 
HETATM 6566 O  O    . HOH   F 5 .   ? 6.441  -5.533  11.220  1.00 19.12 ?  384 HOH   A O    1 
HETATM 6567 O  O    A HOH   F 5 .   ? 9.240  -10.218 19.413  0.60 31.77 ?  385 HOH   A O    1 
HETATM 6568 O  O    . HOH   F 5 .   ? 31.723 -7.287  -9.864  1.00 20.65 ?  386 HOH   A O    1 
HETATM 6569 O  O    . HOH   F 5 .   ? 27.499 -10.624 14.068  1.00 16.33 ?  387 HOH   A O    1 
HETATM 6570 O  O    B HOH   F 5 .   ? 11.469 6.487   9.194   0.40 26.97 ?  388 HOH   A O    1 
HETATM 6571 O  O    . HOH   F 5 .   ? 24.250 -7.759  14.451  1.00 16.06 ?  389 HOH   A O    1 
HETATM 6572 O  O    . HOH   F 5 .   ? 14.063 -23.038 7.422   1.00 17.25 ?  390 HOH   A O    1 
HETATM 6573 O  O    . HOH   F 5 .   ? 24.716 -17.534 12.696  1.00 23.53 ?  391 HOH   A O    1 
HETATM 6574 O  O    . HOH   F 5 .   ? 32.780 -9.226  5.995   1.00 19.43 ?  392 HOH   A O    1 
HETATM 6575 O  O    . HOH   F 5 .   ? 21.189 10.256  15.030  1.00 37.03 ?  393 HOH   A O    1 
HETATM 6576 O  O    . HOH   F 5 .   ? 21.719 -13.805 -8.158  1.00 46.13 ?  394 HOH   A O    1 
HETATM 6577 O  O    . HOH   F 5 .   ? 28.532 -10.598 -14.012 1.00 43.80 ?  395 HOH   A O    1 
HETATM 6578 O  O    . HOH   F 5 .   ? 27.364 -5.996  -13.982 1.00 35.74 ?  396 HOH   A O    1 
HETATM 6579 O  O    . HOH   F 5 .   ? 20.064 4.554   -7.486  1.00 18.65 ?  397 HOH   A O    1 
HETATM 6580 O  O    B HOH   F 5 .   ? 12.043 -2.044  -2.933  0.40 13.77 ?  398 HOH   A O    1 
HETATM 6581 O  O    . HOH   F 5 .   ? 23.977 3.901   -4.771  1.00 22.12 ?  399 HOH   A O    1 
HETATM 6582 O  O    . HOH   F 5 .   ? 15.202 -21.560 14.237  1.00 17.06 ?  400 HOH   A O    1 
HETATM 6583 O  O    . HOH   F 5 .   ? 37.556 -1.980  5.779   1.00 25.61 ?  401 HOH   A O    1 
HETATM 6584 O  O    . HOH   F 5 .   ? 6.741  -3.275  12.953  1.00 29.11 ?  402 HOH   A O    1 
HETATM 6585 O  O    . HOH   F 5 .   ? 14.420 -24.709 11.552  1.00 34.27 ?  403 HOH   A O    1 
HETATM 6586 O  O    . HOH   F 5 .   ? 26.915 4.148   -0.655  1.00 11.97 ?  404 HOH   A O    1 
HETATM 6587 O  O    . HOH   F 5 .   ? 30.071 -10.097 12.999  1.00 20.65 ?  405 HOH   A O    1 
HETATM 6588 O  O    . HOH   F 5 .   ? 27.364 2.293   18.704  1.00 28.27 ?  406 HOH   A O    1 
HETATM 6589 O  O    A HOH   F 5 .   ? 18.931 -0.649  -1.598  0.60 10.84 ?  407 HOH   A O    1 
HETATM 6590 O  O    A HOH   F 5 .   ? 11.023 1.565   12.788  0.60 19.48 ?  408 HOH   A O    1 
HETATM 6591 O  O    . HOH   F 5 .   ? 30.713 1.864   16.684  1.00 19.42 ?  409 HOH   A O    1 
HETATM 6592 O  O    . HOH   F 5 .   ? 20.562 -20.002 2.783   1.00 16.74 ?  410 HOH   A O    1 
HETATM 6593 O  O    . HOH   F 5 .   ? 38.072 -1.342  -1.949  1.00 18.26 ?  411 HOH   A O    1 
HETATM 6594 O  O    A HOH   F 5 .   ? 15.780 -0.928  5.301   0.60 27.07 ?  412 HOH   A O    1 
HETATM 6595 O  O    . HOH   F 5 .   ? 15.812 2.105   24.766  1.00 47.68 ?  413 HOH   A O    1 
HETATM 6596 O  O    . HOH   F 5 .   ? 30.936 6.205   -12.255 1.00 28.70 ?  414 HOH   A O    1 
HETATM 6597 O  O    . HOH   F 5 .   ? 10.345 -22.101 -1.192  1.00 45.45 ?  415 HOH   A O    1 
HETATM 6598 O  O    . HOH   F 5 .   ? 23.897 -20.258 -1.358  1.00 15.24 ?  416 HOH   A O    1 
HETATM 6599 O  O    A HOH   F 5 .   ? 21.323 3.175   -0.322  0.60 9.66  ?  417 HOH   A O    1 
HETATM 6600 O  O    . HOH   F 5 .   ? 16.025 6.959   2.996   1.00 17.38 ?  418 HOH   A O    1 
HETATM 6601 O  O    . HOH   F 5 .   ? 5.296  2.793   5.077   1.00 28.76 ?  419 HOH   A O    1 
HETATM 6602 O  O    . HOH   F 5 .   ? 30.328 -12.938 13.515  1.00 18.75 ?  420 HOH   A O    1 
HETATM 6603 O  O    . HOH   F 5 .   ? 41.575 1.501   4.953   1.00 36.14 ?  421 HOH   A O    1 
HETATM 6604 O  O    B HOH   F 5 .   ? 10.969 2.238   12.140  0.40 23.09 ?  422 HOH   A O    1 
HETATM 6605 O  O    . HOH   F 5 .   ? 16.223 16.657  8.669   1.00 31.35 ?  423 HOH   A O    1 
HETATM 6606 O  O    . HOH   F 5 .   ? 36.694 -4.983  5.381   1.00 23.90 ?  424 HOH   A O    1 
HETATM 6607 O  O    . HOH   F 5 .   ? 32.603 -4.242  -9.907  1.00 26.90 ?  425 HOH   A O    1 
HETATM 6608 O  O    . HOH   F 5 .   ? 16.260 -14.119 20.249  1.00 48.71 ?  426 HOH   A O    1 
HETATM 6609 O  O    . HOH   F 5 .   ? 35.046 -5.210  -3.096  1.00 17.19 ?  427 HOH   A O    1 
HETATM 6610 O  O    A HOH   F 5 .   ? 8.997  -12.111 17.219  0.60 33.65 ?  428 HOH   A O    1 
HETATM 6611 O  O    . HOH   F 5 .   ? 32.568 -10.664 3.165   1.00 31.22 ?  429 HOH   A O    1 
HETATM 6612 O  O    . HOH   F 5 .   ? 10.364 -13.691 -1.637  1.00 16.28 ?  430 HOH   A O    1 
HETATM 6613 O  O    . HOH   F 5 .   ? 44.920 -0.633  2.982   1.00 42.35 ?  431 HOH   A O    1 
HETATM 6614 O  O    . HOH   F 5 .   ? 27.874 0.823   -7.151  1.00 13.50 ?  432 HOH   A O    1 
HETATM 6615 O  O    . HOH   F 5 .   ? 40.917 -8.224  -6.785  1.00 37.76 ?  433 HOH   A O    1 
HETATM 6616 O  O    . HOH   F 5 .   ? 15.106 -8.094  -9.644  1.00 21.40 ?  434 HOH   A O    1 
HETATM 6617 O  O    A HOH   F 5 .   ? 11.044 -0.360  1.969   0.60 21.60 ?  435 HOH   A O    1 
HETATM 6618 O  O    . HOH   F 5 .   ? 22.667 8.142   18.396  1.00 44.78 ?  436 HOH   A O    1 
HETATM 6619 O  O    . HOH   F 5 .   ? 18.471 4.898   -15.087 1.00 46.32 ?  437 HOH   A O    1 
HETATM 6620 O  O    . HOH   F 5 .   ? 23.197 7.653   -3.157  1.00 32.71 ?  438 HOH   A O    1 
HETATM 6621 O  O    . HOH   F 5 .   ? 21.303 -9.170  21.320  1.00 48.94 ?  439 HOH   A O    1 
HETATM 6622 O  O    A HOH   F 5 .   ? 18.837 2.053   -0.722  0.60 10.69 ?  440 HOH   A O    1 
HETATM 6623 O  O    B HOH   F 5 .   ? 18.691 -1.573  -1.531  0.40 35.08 ?  441 HOH   A O    1 
HETATM 6624 O  O    . HOH   F 5 .   ? 19.447 -11.044 24.086  1.00 67.36 ?  442 HOH   A O    1 
HETATM 6625 O  O    . HOH   F 5 .   ? 27.137 -3.191  19.298  1.00 32.93 ?  443 HOH   A O    1 
HETATM 6626 O  O    . HOH   F 5 .   ? 37.699 -8.804  -3.496  1.00 24.01 ?  444 HOH   A O    1 
HETATM 6627 O  O    . HOH   F 5 .   ? 23.541 -8.017  17.100  1.00 20.51 ?  445 HOH   A O    1 
HETATM 6628 O  O    . HOH   F 5 .   ? 23.304 -20.917 1.320   1.00 17.60 ?  446 HOH   A O    1 
HETATM 6629 O  O    A HOH   F 5 .   ? 16.232 2.968   -1.409  0.60 17.05 ?  447 HOH   A O    1 
HETATM 6630 O  O    . HOH   F 5 .   ? 18.387 -16.023 16.392  1.00 35.31 ?  448 HOH   A O    1 
HETATM 6631 O  O    . HOH   F 5 .   ? 34.398 -8.071  -0.525  1.00 27.23 ?  449 HOH   A O    1 
HETATM 6632 O  O    B HOH   F 5 .   ? 20.693 4.222   -2.294  0.40 30.29 ?  450 HOH   A O    1 
HETATM 6633 O  O    . HOH   F 5 .   ? 9.405  -16.258 -1.981  1.00 40.76 ?  451 HOH   A O    1 
HETATM 6634 O  O    . HOH   F 5 .   ? 20.568 -17.777 24.840  1.00 55.72 ?  452 HOH   A O    1 
HETATM 6635 O  O    . HOH   F 5 .   ? 30.578 14.765  2.796   1.00 17.49 ?  453 HOH   A O    1 
HETATM 6636 O  O    . HOH   F 5 .   ? 31.319 -12.776 0.011   1.00 18.65 ?  454 HOH   A O    1 
HETATM 6637 O  O    . HOH   F 5 .   ? 21.541 -14.704 17.948  1.00 52.99 ?  455 HOH   A O    1 
HETATM 6638 O  O    . HOH   F 5 .   ? -1.482 -4.856  7.728   1.00 45.66 ?  456 HOH   A O    1 
HETATM 6639 O  O    A HOH   F 5 .   ? 14.005 -0.320  3.494   0.60 20.28 ?  457 HOH   A O    1 
HETATM 6640 O  O    . HOH   F 5 .   ? 29.800 -16.022 10.671  1.00 30.52 ?  458 HOH   A O    1 
HETATM 6641 O  O    . HOH   F 5 .   ? 27.749 7.009   -6.421  1.00 34.08 ?  459 HOH   A O    1 
HETATM 6642 O  O    B HOH   F 5 .   ? 7.900  1.521   -2.987  0.40 29.74 ?  460 HOH   A O    1 
HETATM 6643 O  O    . HOH   F 5 .   ? 29.727 -1.972  -12.705 1.00 43.77 ?  461 HOH   A O    1 
HETATM 6644 O  O    . HOH   F 5 .   ? 25.370 8.236   -4.810  1.00 28.40 ?  462 HOH   A O    1 
HETATM 6645 O  O    . HOH   F 5 .   ? 32.444 -15.938 10.815  1.00 34.93 ?  463 HOH   A O    1 
HETATM 6646 O  O    . HOH   F 5 .   ? 12.009 -13.355 16.416  1.00 48.90 ?  464 HOH   A O    1 
HETATM 6647 O  O    . HOH   F 5 .   ? 19.830 -17.292 -5.054  1.00 22.98 ?  465 HOH   A O    1 
HETATM 6648 O  O    . HOH   F 5 .   ? 24.911 5.661   20.760  1.00 52.07 ?  466 HOH   A O    1 
HETATM 6649 O  O    . HOH   F 5 .   ? 23.209 -22.331 -3.279  1.00 32.84 ?  467 HOH   A O    1 
HETATM 6650 O  O    . HOH   F 5 .   ? 24.574 14.539  7.868   1.00 34.03 ?  468 HOH   A O    1 
HETATM 6651 O  O    . HOH   F 5 .   ? 18.757 10.830  11.335  1.00 33.45 ?  469 HOH   A O    1 
HETATM 6652 O  O    . HOH   F 5 .   ? 21.917 5.202   -5.862  1.00 31.94 ?  470 HOH   A O    1 
HETATM 6653 O  O    . HOH   F 5 .   ? 26.902 11.655  -1.325  1.00 29.66 ?  471 HOH   A O    1 
HETATM 6654 O  O    . HOH   F 5 .   ? 39.599 -7.049  -3.574  1.00 47.23 ?  472 HOH   A O    1 
HETATM 6655 O  O    . HOH   F 5 .   ? 15.695 -21.455 3.688   1.00 21.85 ?  473 HOH   A O    1 
HETATM 6656 O  O    . HOH   F 5 .   ? 23.481 13.708  5.509   1.00 18.26 ?  474 HOH   A O    1 
HETATM 6657 O  O    B HOH   F 5 .   ? 18.929 0.966   -0.693  0.40 24.39 ?  475 HOH   A O    1 
HETATM 6658 O  O    B HOH   F 5 .   ? 12.379 -3.110  2.061   0.40 26.55 ?  476 HOH   A O    1 
HETATM 6659 O  O    . HOH   F 5 .   ? 27.502 -11.378 16.551  1.00 37.32 ?  477 HOH   A O    1 
HETATM 6660 O  O    . HOH   F 5 .   ? 12.365 1.584   17.353  1.00 40.31 ?  478 HOH   A O    1 
HETATM 6661 O  O    . HOH   F 5 .   ? 25.821 10.795  -3.716  1.00 24.50 ?  479 HOH   A O    1 
HETATM 6662 O  O    . HOH   F 5 .   ? 10.999 -14.974 -6.064  1.00 32.75 ?  480 HOH   A O    1 
HETATM 6663 O  O    . HOH   F 5 .   ? 23.114 11.811  -4.046  1.00 18.66 ?  481 HOH   A O    1 
HETATM 6664 O  O    . HOH   F 5 .   ? 18.044 -16.211 -8.769  1.00 38.88 ?  482 HOH   A O    1 
HETATM 6665 O  O    . HOH   F 5 .   ? 35.163 7.448   12.231  1.00 44.59 ?  483 HOH   A O    1 
HETATM 6666 O  O    . HOH   F 5 .   ? 16.815 -20.554 16.188  1.00 27.81 ?  484 HOH   A O    1 
HETATM 6667 O  O    . HOH   F 5 .   ? 28.825 9.023   17.503  1.00 35.37 ?  485 HOH   A O    1 
HETATM 6668 O  O    . HOH   F 5 .   ? 15.708 -17.119 -6.981  1.00 29.61 ?  486 HOH   A O    1 
HETATM 6669 O  O    . HOH   F 5 .   ? 13.933 -10.325 -10.871 1.00 31.50 ?  487 HOH   A O    1 
HETATM 6670 O  O    . HOH   F 5 .   ? 8.211  -3.006  -5.738  1.00 43.58 ?  488 HOH   A O    1 
HETATM 6671 O  O    . HOH   F 5 .   ? 40.919 -3.970  -0.343  1.00 36.63 ?  489 HOH   A O    1 
HETATM 6672 O  O    . HOH   F 5 .   ? 30.813 0.784   19.176  1.00 37.84 ?  490 HOH   A O    1 
HETATM 6673 O  O    . HOH   F 5 .   ? 17.322 -18.693 19.794  1.00 49.37 ?  491 HOH   A O    1 
HETATM 6674 O  O    B HOH   F 5 .   ? 10.613 -1.519  -5.154  0.40 16.51 ?  492 HOH   A O    1 
HETATM 6675 O  O    . HOH   F 5 .   ? 44.481 10.441  -1.624  1.00 30.83 ?  493 HOH   A O    1 
HETATM 6676 O  O    . HOH   F 5 .   ? 41.669 9.343   -4.032  1.00 31.33 ?  494 HOH   A O    1 
HETATM 6677 O  O    . HOH   F 5 .   ? 31.443 -0.598  -10.580 1.00 27.59 ?  495 HOH   A O    1 
HETATM 6678 O  O    . HOH   F 5 .   ? 23.258 -12.859 19.326  1.00 48.73 ?  496 HOH   A O    1 
HETATM 6679 O  O    . HOH   F 5 .   ? 28.667 -7.897  -15.252 1.00 45.46 ?  497 HOH   A O    1 
HETATM 6680 O  O    . HOH   F 5 .   ? 28.542 -4.679  -12.315 1.00 37.38 ?  498 HOH   A O    1 
HETATM 6681 O  O    B HOH   F 5 .   ? 11.337 8.740   7.858   0.40 33.58 ?  499 HOH   A O    1 
HETATM 6682 O  O    . HOH   F 5 .   ? 39.140 2.393   7.493   1.00 32.42 ?  500 HOH   A O    1 
HETATM 6683 O  O    . HOH   F 5 .   ? 40.501 -0.229  -7.821  1.00 32.37 ?  501 HOH   A O    1 
HETATM 6684 O  O    . HOH   F 5 .   ? 13.988 -25.239 8.938   1.00 29.24 ?  502 HOH   A O    1 
HETATM 6685 O  O    . HOH   F 5 .   ? 20.002 -22.319 4.173   1.00 29.31 ?  503 HOH   A O    1 
HETATM 6686 O  O    . HOH   F 5 .   ? 18.460 -23.256 1.947   1.00 37.90 ?  504 HOH   A O    1 
HETATM 6687 O  O    . HOH   F 5 .   ? 16.013 -6.818  -11.771 1.00 41.72 ?  505 HOH   A O    1 
HETATM 6688 O  O    . HOH   F 5 .   ? 20.474 -16.036 -7.375  1.00 29.20 ?  506 HOH   A O    1 
HETATM 6689 O  O    . HOH   F 5 .   ? 16.158 -23.361 5.734   1.00 27.11 ?  507 HOH   A O    1 
HETATM 6690 O  O    B HOH   F 5 .   ? 9.474  0.802   -4.973  0.40 19.43 ?  508 HOH   A O    1 
HETATM 6691 O  O    . HOH   F 5 .   ? 25.791 -18.870 -11.915 1.00 38.53 ?  509 HOH   A O    1 
HETATM 6692 O  O    . HOH   F 5 .   ? 30.714 -5.796  -11.845 1.00 47.30 ?  510 HOH   A O    1 
HETATM 6693 O  O    . HOH   F 5 .   ? 37.378 -6.665  7.513   1.00 24.82 ?  511 HOH   A O    1 
HETATM 6694 O  O    . HOH   F 5 .   ? 23.082 -23.727 1.666   1.00 29.51 ?  512 HOH   A O    1 
HETATM 6695 O  O    . HOH   F 5 .   ? 30.712 5.835   -14.692 1.00 33.68 ?  513 HOH   A O    1 
HETATM 6696 O  O    B HOH   F 5 .   ? 14.612 7.962   4.908   0.40 23.59 ?  514 HOH   A O    1 
HETATM 6697 O  O    . HOH   F 5 .   ? 39.520 0.016   6.547   1.00 29.31 ?  515 HOH   A O    1 
HETATM 6698 O  O    . HOH   F 5 .   ? 38.023 13.863  6.737   1.00 51.05 ?  516 HOH   A O    1 
HETATM 6699 O  O    . HOH   F 5 .   ? 28.982 14.407  0.893   1.00 46.74 ?  517 HOH   A O    1 
HETATM 6700 O  O    . HOH   F 5 .   ? 21.999 -24.021 4.455   1.00 24.99 ?  518 HOH   A O    1 
HETATM 6701 O  O    . HOH   F 5 .   ? 36.404 -6.532  10.155  1.00 43.79 ?  519 HOH   A O    1 
HETATM 6702 O  O    . HOH   F 5 .   ? 17.265 -6.920  -14.307 1.00 40.73 ?  520 HOH   A O    1 
HETATM 6703 O  O    A HOH   F 5 .   ? 14.832 8.668   4.926   0.60 30.60 ?  521 HOH   A O    1 
HETATM 6704 O  O    . HOH   F 5 .   ? 24.025 9.088   -7.195  1.00 33.97 ?  522 HOH   A O    1 
HETATM 6705 O  O    . HOH   F 5 .   ? 16.311 -21.131 18.776  1.00 35.68 ?  523 HOH   A O    1 
HETATM 6706 O  O    . HOH   F 5 .   ? 15.834 -12.311 27.486  1.00 46.11 ?  524 HOH   A O    1 
HETATM 6707 O  O    . HOH   F 5 .   ? 14.682 -22.796 19.816  1.00 33.35 ?  525 HOH   A O    1 
HETATM 6708 O  O    . HOH   G 5 .   ? 29.791 -22.404 5.472   1.00 19.29 ?  201 HOH   B O    1 
HETATM 6709 O  O    . HOH   G 5 .   ? 41.737 -35.954 -17.229 1.00 30.50 ?  202 HOH   B O    1 
HETATM 6710 O  O    . HOH   G 5 .   ? 48.076 -6.879  15.527  1.00 31.83 ?  203 HOH   B O    1 
HETATM 6711 O  O    . HOH   G 5 .   ? 52.874 -13.423 -20.331 1.00 35.63 ?  204 HOH   B O    1 
HETATM 6712 O  O    . HOH   G 5 .   ? 27.828 -41.765 -15.117 1.00 36.37 ?  205 HOH   B O    1 
HETATM 6713 O  O    . HOH   G 5 .   ? 59.103 -18.673 6.793   1.00 37.68 ?  206 HOH   B O    1 
HETATM 6714 O  O    . HOH   G 5 .   ? 37.951 -39.422 -0.202  1.00 39.71 ?  207 HOH   B O    1 
HETATM 6715 O  O    . HOH   G 5 .   ? 41.399 -7.745  5.489   1.00 37.87 ?  208 HOH   B O    1 
HETATM 6716 O  O    . HOH   G 5 .   ? 27.708 -29.165 -1.852  1.00 38.12 ?  209 HOH   B O    1 
HETATM 6717 O  O    . HOH   G 5 .   ? 49.368 -22.698 -19.795 1.00 49.99 ?  210 HOH   B O    1 
HETATM 6718 O  O    . HOH   G 5 .   ? 58.168 -12.924 8.390   1.00 31.97 ?  211 HOH   B O    1 
HETATM 6719 O  O    . HOH   G 5 .   ? 56.321 -19.689 7.266   1.00 33.35 ?  212 HOH   B O    1 
HETATM 6720 O  O    . HOH   G 5 .   ? 55.419 -16.554 -14.345 1.00 34.89 ?  213 HOH   B O    1 
HETATM 6721 O  O    . HOH   G 5 .   ? 54.457 -9.350  -8.772  1.00 18.56 ?  214 HOH   B O    1 
HETATM 6722 O  O    . HOH   G 5 .   ? 29.871 -26.294 4.001   1.00 27.31 ?  215 HOH   B O    1 
HETATM 6723 O  O    . HOH   G 5 .   ? 50.224 -3.314  7.171   1.00 35.37 ?  216 HOH   B O    1 
HETATM 6724 O  O    . HOH   G 5 .   ? 47.359 -7.356  -3.899  1.00 40.26 ?  217 HOH   B O    1 
HETATM 6725 O  O    . HOH   G 5 .   ? 57.715 -24.457 5.026   1.00 35.41 ?  218 HOH   B O    1 
HETATM 6726 O  O    . HOH   G 5 .   ? 30.184 -41.005 -8.154  1.00 15.61 ?  219 HOH   B O    1 
HETATM 6727 O  O    . HOH   G 5 .   ? 26.462 -19.328 -1.769  1.00 12.96 ?  220 HOH   B O    1 
HETATM 6728 O  O    . HOH   G 5 .   ? 50.694 -6.106  0.194   1.00 25.86 ?  221 HOH   B O    1 
HETATM 6729 O  O    . HOH   G 5 .   ? 48.485 -36.489 -15.475 1.00 45.87 ?  222 HOH   B O    1 
HETATM 6730 O  O    . HOH   G 5 .   ? 44.389 -7.266  2.113   1.00 32.54 ?  223 HOH   B O    1 
HETATM 6731 O  O    . HOH   G 5 .   ? 29.747 -34.150 -0.444  1.00 32.29 ?  224 HOH   B O    1 
HETATM 6732 O  O    . HOH   G 5 .   ? 45.113 -34.922 6.819   1.00 38.23 ?  225 HOH   B O    1 
HETATM 6733 O  O    . HOH   G 5 .   ? 41.496 -39.139 -14.907 1.00 20.81 ?  226 HOH   B O    1 
HETATM 6734 O  O    . HOH   G 5 .   ? 57.151 -26.826 -7.622  1.00 39.24 ?  227 HOH   B O    1 
HETATM 6735 O  O    . HOH   G 5 .   ? 57.383 -16.241 -12.197 1.00 18.20 ?  228 HOH   B O    1 
HETATM 6736 O  O    . HOH   G 5 .   ? 35.920 -43.231 -8.545  1.00 31.18 ?  229 HOH   B O    1 
HETATM 6737 O  O    . HOH   G 5 .   ? 44.980 -43.494 -10.565 1.00 26.96 ?  230 HOH   B O    1 
HETATM 6738 O  O    . HOH   G 5 .   ? 56.669 -30.775 -7.753  1.00 30.47 ?  231 HOH   B O    1 
HETATM 6739 O  O    . HOH   G 5 .   ? 34.511 -36.353 -7.212  1.00 17.05 ?  232 HOH   B O    1 
HETATM 6740 O  O    . HOH   G 5 .   ? 40.573 -16.034 14.114  1.00 23.91 ?  233 HOH   B O    1 
HETATM 6741 O  O    . HOH   G 5 .   ? 51.629 -6.479  4.419   1.00 19.29 ?  234 HOH   B O    1 
HETATM 6742 O  O    . HOH   G 5 .   ? 30.857 -28.756 4.270   1.00 25.72 ?  235 HOH   B O    1 
HETATM 6743 O  O    . HOH   G 5 .   ? 41.355 -9.657  13.085  1.00 21.72 ?  236 HOH   B O    1 
HETATM 6744 O  O    . HOH   G 5 .   ? 44.459 -27.765 -0.725  1.00 20.97 ?  237 HOH   B O    1 
HETATM 6745 O  O    . HOH   G 5 .   ? 37.066 -19.741 -18.066 1.00 34.77 ?  238 HOH   B O    1 
HETATM 6746 O  O    . HOH   G 5 .   ? 46.373 -1.594  13.249  1.00 28.76 ?  239 HOH   B O    1 
HETATM 6747 O  O    . HOH   G 5 .   ? 28.377 -19.664 -13.109 1.00 23.26 ?  240 HOH   B O    1 
HETATM 6748 O  O    . HOH   G 5 .   ? 39.276 -10.880 6.124   1.00 24.55 ?  241 HOH   B O    1 
HETATM 6749 O  O    . HOH   G 5 .   ? 25.423 -25.942 -1.369  1.00 31.99 ?  242 HOH   B O    1 
HETATM 6750 O  O    . HOH   G 5 .   ? 50.705 -12.970 -0.487  1.00 11.42 ?  243 HOH   B O    1 
HETATM 6751 O  O    . HOH   G 5 .   ? 32.803 -43.778 -11.356 1.00 19.40 ?  244 HOH   B O    1 
HETATM 6752 O  O    . HOH   G 5 .   ? 35.091 -7.992  -3.048  1.00 17.32 ?  245 HOH   B O    1 
HETATM 6753 O  O    . HOH   G 5 .   ? 42.544 -25.355 2.620   1.00 14.11 ?  246 HOH   B O    1 
HETATM 6754 O  O    . HOH   G 5 .   ? 42.608 -22.862 3.845   1.00 11.17 ?  247 HOH   B O    1 
HETATM 6755 O  O    . HOH   G 5 .   ? 43.146 -32.359 -17.091 1.00 22.67 ?  248 HOH   B O    1 
HETATM 6756 O  O    . HOH   G 5 .   ? 39.479 -11.114 0.337   1.00 16.13 ?  249 HOH   B O    1 
HETATM 6757 O  O    . HOH   G 5 .   ? 48.015 -24.457 -17.772 1.00 30.20 ?  250 HOH   B O    1 
HETATM 6758 O  O    . HOH   G 5 .   ? 43.077 -43.228 -8.264  1.00 28.34 ?  251 HOH   B O    1 
HETATM 6759 O  O    . HOH   G 5 .   ? 40.303 -12.752 -11.507 1.00 14.44 ?  252 HOH   B O    1 
HETATM 6760 O  O    . HOH   G 5 .   ? 34.214 -18.502 11.412  1.00 22.97 ?  253 HOH   B O    1 
HETATM 6761 O  O    . HOH   G 5 .   ? 57.589 -24.378 -3.837  1.00 21.23 ?  254 HOH   B O    1 
HETATM 6762 O  O    . HOH   G 5 .   ? 38.447 -11.028 -2.251  1.00 17.88 ?  255 HOH   B O    1 
HETATM 6763 O  O    . HOH   G 5 .   ? 34.904 -24.599 13.872  1.00 29.01 ?  256 HOH   B O    1 
HETATM 6764 O  O    . HOH   G 5 .   ? 51.520 -13.873 10.999  1.00 27.67 ?  257 HOH   B O    1 
HETATM 6765 O  O    . HOH   G 5 .   ? 41.844 -23.505 9.283   1.00 16.03 ?  258 HOH   B O    1 
HETATM 6766 O  O    . HOH   G 5 .   ? 30.835 -15.723 2.640   1.00 12.91 ?  259 HOH   B O    1 
HETATM 6767 O  O    . HOH   G 5 .   ? 29.708 -25.215 -10.820 1.00 15.61 ?  260 HOH   B O    1 
HETATM 6768 O  O    . HOH   G 5 .   ? 30.566 -42.224 -10.617 1.00 27.73 ?  261 HOH   B O    1 
HETATM 6769 O  O    . HOH   G 5 .   ? 33.493 -17.003 8.056   1.00 18.24 ?  262 HOH   B O    1 
HETATM 6770 O  O    . HOH   G 5 .   ? 58.153 -10.624 -4.083  1.00 18.93 ?  263 HOH   B O    1 
HETATM 6771 O  O    . HOH   G 5 .   ? 50.953 -39.931 -8.259  1.00 32.22 ?  264 HOH   B O    1 
HETATM 6772 O  O    . HOH   G 5 .   ? 27.128 -31.801 -9.986  1.00 19.91 ?  265 HOH   B O    1 
HETATM 6773 O  O    . HOH   G 5 .   ? 57.455 -9.225  1.417   1.00 18.86 ?  266 HOH   B O    1 
HETATM 6774 O  O    . HOH   G 5 .   ? 31.778 -17.956 -14.521 1.00 31.03 ?  267 HOH   B O    1 
HETATM 6775 O  O    . HOH   G 5 .   ? 49.294 -28.690 -6.916  1.00 14.79 ?  268 HOH   B O    1 
HETATM 6776 O  O    . HOH   G 5 .   ? 42.305 -9.904  9.389   1.00 20.25 ?  269 HOH   B O    1 
HETATM 6777 O  O    . HOH   G 5 .   ? 38.881 -12.011 12.345  1.00 34.65 ?  270 HOH   B O    1 
HETATM 6778 O  O    . HOH   G 5 .   ? 49.725 -0.505  10.253  1.00 31.45 ?  271 HOH   B O    1 
HETATM 6779 O  O    . HOH   G 5 .   ? 28.459 -30.826 -14.740 1.00 28.67 ?  272 HOH   B O    1 
HETATM 6780 O  O    . HOH   G 5 .   ? 34.911 -33.294 -19.236 1.00 31.35 ?  273 HOH   B O    1 
HETATM 6781 O  O    . HOH   G 5 .   ? 56.908 -8.643  8.428   1.00 19.02 ?  274 HOH   B O    1 
HETATM 6782 O  O    . HOH   G 5 .   ? 28.254 -34.335 -9.426  1.00 19.18 ?  275 HOH   B O    1 
HETATM 6783 O  O    . HOH   G 5 .   ? 43.338 -15.788 -12.156 1.00 13.67 ?  276 HOH   B O    1 
HETATM 6784 O  O    . HOH   G 5 .   ? 48.009 -22.770 5.835   1.00 16.62 ?  277 HOH   B O    1 
HETATM 6785 O  O    . HOH   G 5 .   ? 46.581 -31.236 -4.799  1.00 19.02 ?  278 HOH   B O    1 
HETATM 6786 O  O    . HOH   G 5 .   ? 27.926 -22.876 -8.007  1.00 16.56 ?  279 HOH   B O    1 
HETATM 6787 O  O    . HOH   G 5 .   ? 34.434 -12.789 2.617   1.00 23.21 ?  280 HOH   B O    1 
HETATM 6788 O  O    . HOH   G 5 .   ? 48.384 -25.036 3.082   1.00 12.69 ?  281 HOH   B O    1 
HETATM 6789 O  O    . HOH   G 5 .   ? 56.161 -23.481 -14.746 1.00 26.43 ?  282 HOH   B O    1 
HETATM 6790 O  O    . HOH   G 5 .   ? 42.255 -9.994  -14.891 1.00 39.43 ?  283 HOH   B O    1 
HETATM 6791 O  O    . HOH   G 5 .   ? 42.383 -34.672 3.758   1.00 24.88 ?  284 HOH   B O    1 
HETATM 6792 O  O    . HOH   G 5 .   ? 46.853 -29.521 9.793   1.00 30.72 ?  285 HOH   B O    1 
HETATM 6793 O  O    . HOH   G 5 .   ? 27.566 -26.694 -15.648 1.00 31.05 ?  286 HOH   B O    1 
HETATM 6794 O  O    . HOH   G 5 .   ? 59.766 -15.324 8.141   1.00 32.38 ?  287 HOH   B O    1 
HETATM 6795 O  O    . HOH   G 5 .   ? 33.503 -15.318 -13.975 1.00 20.06 ?  288 HOH   B O    1 
HETATM 6796 O  O    . HOH   G 5 .   ? 42.849 -20.271 -20.772 1.00 36.77 ?  289 HOH   B O    1 
HETATM 6797 O  O    . HOH   G 5 .   ? 57.114 -12.044 12.295  1.00 37.91 ?  290 HOH   B O    1 
HETATM 6798 O  O    . HOH   G 5 .   ? 48.687 -20.029 5.910   1.00 13.28 ?  291 HOH   B O    1 
HETATM 6799 O  O    . HOH   G 5 .   ? 47.057 -33.952 -4.642  1.00 16.44 ?  292 HOH   B O    1 
HETATM 6800 O  O    . HOH   G 5 .   ? 52.521 -10.415 12.995  1.00 21.38 ?  293 HOH   B O    1 
HETATM 6801 O  O    . HOH   G 5 .   ? 45.337 -33.353 -15.956 1.00 22.83 ?  294 HOH   B O    1 
HETATM 6802 O  O    . HOH   G 5 .   ? 42.655 -12.306 -18.504 1.00 29.50 ?  295 HOH   B O    1 
HETATM 6803 O  O    . HOH   G 5 .   ? 51.206 -37.577 -9.578  1.00 24.11 ?  296 HOH   B O    1 
HETATM 6804 O  O    . HOH   G 5 .   ? 36.808 -12.767 -1.485  1.00 25.97 ?  297 HOH   B O    1 
HETATM 6805 O  O    . HOH   G 5 .   ? 35.055 -33.592 4.507   1.00 26.37 ?  298 HOH   B O    1 
HETATM 6806 O  O    . HOH   G 5 .   ? 52.571 -35.621 -8.596  1.00 27.41 ?  299 HOH   B O    1 
HETATM 6807 O  O    . HOH   G 5 .   ? 44.598 -27.444 1.985   1.00 14.56 ?  300 HOH   B O    1 
HETATM 6808 O  O    . HOH   G 5 .   ? 37.473 -18.213 13.101  1.00 28.30 ?  301 HOH   B O    1 
HETATM 6809 O  O    . HOH   G 5 .   ? 44.002 -29.327 -4.695  1.00 22.82 ?  302 HOH   B O    1 
HETATM 6810 O  O    . HOH   G 5 .   ? 45.860 -40.378 -3.633  1.00 28.43 ?  303 HOH   B O    1 
HETATM 6811 O  O    . HOH   G 5 .   ? 40.212 -10.822 -9.524  1.00 16.45 ?  304 HOH   B O    1 
HETATM 6812 O  O    . HOH   G 5 .   ? 41.136 -5.460  11.505  1.00 44.25 ?  305 HOH   B O    1 
HETATM 6813 O  O    . HOH   G 5 .   ? 25.918 -21.463 -3.507  1.00 15.24 ?  306 HOH   B O    1 
HETATM 6814 O  O    . HOH   G 5 .   ? 57.615 -22.067 3.104   1.00 26.81 ?  307 HOH   B O    1 
HETATM 6815 O  O    . HOH   G 5 .   ? 49.935 -24.633 5.826   1.00 34.29 ?  308 HOH   B O    1 
HETATM 6816 O  O    . HOH   G 5 .   ? 37.299 -35.650 7.215   1.00 33.99 ?  309 HOH   B O    1 
HETATM 6817 O  O    . HOH   G 5 .   ? 43.484 -15.411 18.174  1.00 31.81 ?  310 HOH   B O    1 
HETATM 6818 O  O    . HOH   G 5 .   ? 53.434 -30.191 4.507   1.00 18.15 ?  311 HOH   B O    1 
HETATM 6819 O  O    . HOH   G 5 .   ? 53.105 -16.057 -12.716 1.00 26.97 ?  312 HOH   B O    1 
HETATM 6820 O  O    . HOH   G 5 .   ? 41.709 -8.089  1.366   1.00 24.02 ?  313 HOH   B O    1 
HETATM 6821 O  O    . HOH   G 5 .   ? 32.795 -34.565 -5.930  1.00 16.09 ?  314 HOH   B O    1 
HETATM 6822 O  O    . HOH   G 5 .   ? 37.817 -10.238 -10.740 1.00 16.07 ?  315 HOH   B O    1 
HETATM 6823 O  O    . HOH   G 5 .   ? 62.812 -20.093 -0.821  1.00 39.24 ?  316 HOH   B O    1 
HETATM 6824 O  O    . HOH   G 5 .   ? 48.055 -32.588 -16.616 1.00 40.58 ?  317 HOH   B O    1 
HETATM 6825 O  O    . HOH   G 5 .   ? 62.663 -13.573 4.698   1.00 27.66 ?  318 HOH   B O    1 
HETATM 6826 O  O    . HOH   G 5 .   ? 52.517 -29.215 -13.054 1.00 23.79 ?  319 HOH   B O    1 
HETATM 6827 O  O    . HOH   G 5 .   ? 37.137 -30.552 -21.029 1.00 29.57 ?  320 HOH   B O    1 
HETATM 6828 O  O    . HOH   G 5 .   ? 26.310 -21.017 -6.237  1.00 15.61 ?  321 HOH   B O    1 
HETATM 6829 O  O    . HOH   G 5 .   ? 43.183 -21.432 10.681  1.00 15.11 ?  322 HOH   B O    1 
HETATM 6830 O  O    . HOH   G 5 .   ? 44.567 -24.623 9.561   1.00 19.13 ?  323 HOH   B O    1 
HETATM 6831 O  O    . HOH   G 5 .   ? 51.683 -5.955  -7.912  1.00 44.98 ?  324 HOH   B O    1 
HETATM 6832 O  O    . HOH   G 5 .   ? 41.109 -24.428 15.814  1.00 42.40 ?  325 HOH   B O    1 
HETATM 6833 O  O    . HOH   G 5 .   ? 38.311 -12.758 7.934   1.00 17.88 ?  326 HOH   B O    1 
HETATM 6834 O  O    . HOH   G 5 .   ? 51.358 -32.915 -10.801 1.00 40.06 ?  327 HOH   B O    1 
HETATM 6835 O  O    . HOH   G 5 .   ? 59.899 -17.223 -10.500 1.00 34.07 ?  328 HOH   B O    1 
HETATM 6836 O  O    . HOH   G 5 .   ? 53.614 -12.530 -22.257 1.00 37.78 ?  329 HOH   B O    1 
HETATM 6837 O  O    . HOH   G 5 .   ? 27.813 -14.762 -9.413  1.00 34.03 ?  330 HOH   B O    1 
HETATM 6838 O  O    . HOH   G 5 .   ? 36.708 -12.412 4.301   1.00 17.46 ?  331 HOH   B O    1 
HETATM 6839 O  O    . HOH   G 5 .   ? 38.317 -9.363  -13.254 1.00 26.80 ?  332 HOH   B O    1 
HETATM 6840 O  O    . HOH   G 5 .   ? 43.091 -34.588 0.080   1.00 19.86 ?  333 HOH   B O    1 
HETATM 6841 O  O    . HOH   G 5 .   ? 33.554 -31.156 11.064  1.00 33.07 ?  334 HOH   B O    1 
HETATM 6842 O  O    . HOH   G 5 .   ? 47.146 -24.487 8.135   1.00 23.45 ?  335 HOH   B O    1 
HETATM 6843 O  O    . HOH   G 5 .   ? 44.220 -1.739  7.594   1.00 43.99 ?  336 HOH   B O    1 
HETATM 6844 O  O    . HOH   G 5 .   ? 45.668 -36.264 -16.112 1.00 33.29 ?  337 HOH   B O    1 
HETATM 6845 O  O    . HOH   G 5 .   ? 48.572 -11.936 -13.907 1.00 26.02 ?  338 HOH   B O    1 
HETATM 6846 O  O    . HOH   G 5 .   ? 47.450 -27.427 2.008   1.00 14.08 ?  339 HOH   B O    1 
HETATM 6847 O  O    . HOH   G 5 .   ? 46.833 -19.854 12.243  1.00 30.44 ?  340 HOH   B O    1 
HETATM 6848 O  O    . HOH   G 5 .   ? 42.825 -43.471 -14.381 1.00 41.67 ?  341 HOH   B O    1 
HETATM 6849 O  O    . HOH   G 5 .   ? 36.998 -15.119 -16.511 1.00 40.05 ?  342 HOH   B O    1 
HETATM 6850 O  O    . HOH   G 5 .   ? 39.486 -23.605 -20.338 1.00 37.09 ?  343 HOH   B O    1 
HETATM 6851 O  O    . HOH   G 5 .   ? 38.360 -12.247 -16.235 1.00 40.96 ?  344 HOH   B O    1 
HETATM 6852 O  O    . HOH   G 5 .   ? 28.871 -42.924 -12.364 1.00 40.40 ?  345 HOH   B O    1 
HETATM 6853 O  O    . HOH   G 5 .   ? 32.975 -14.669 1.045   1.00 17.57 ?  346 HOH   B O    1 
HETATM 6854 O  O    . HOH   G 5 .   ? 39.740 -44.286 -11.220 1.00 38.22 ?  347 HOH   B O    1 
HETATM 6855 O  O    . HOH   G 5 .   ? 37.064 -45.273 -9.744  1.00 36.61 ?  348 HOH   B O    1 
HETATM 6856 O  O    . HOH   G 5 .   ? 38.573 -22.336 15.033  1.00 38.99 ?  349 HOH   B O    1 
HETATM 6857 O  O    . HOH   G 5 .   ? 40.387 -43.449 -9.113  1.00 25.51 ?  350 HOH   B O    1 
HETATM 6858 O  O    . HOH   G 5 .   ? 33.764 -9.297  -8.809  1.00 32.35 ?  351 HOH   B O    1 
HETATM 6859 O  O    . HOH   G 5 .   ? 27.756 -26.597 -0.588  1.00 30.57 ?  352 HOH   B O    1 
HETATM 6860 O  O    . HOH   G 5 .   ? 55.612 -8.260  10.813  1.00 23.90 ?  353 HOH   B O    1 
HETATM 6861 O  O    . HOH   G 5 .   ? 62.541 -20.138 -4.857  1.00 45.93 ?  354 HOH   B O    1 
HETATM 6862 O  O    . HOH   G 5 .   ? 44.113 -37.315 -17.793 1.00 32.61 ?  355 HOH   B O    1 
HETATM 6863 O  O    . HOH   G 5 .   ? 23.197 -23.683 6.761   1.00 34.09 ?  356 HOH   B O    1 
HETATM 6864 O  O    . HOH   G 5 .   ? 36.043 -8.552  -9.686  1.00 33.87 ?  357 HOH   B O    1 
HETATM 6865 O  O    . HOH   G 5 .   ? 56.548 -7.270  3.061   1.00 26.77 ?  358 HOH   B O    1 
HETATM 6866 O  O    . HOH   G 5 .   ? 34.642 -10.300 7.476   1.00 23.31 ?  359 HOH   B O    1 
HETATM 6867 O  O    . HOH   G 5 .   ? 43.107 -12.650 -21.188 1.00 38.64 ?  360 HOH   B O    1 
HETATM 6868 O  O    . HOH   G 5 .   ? 61.462 -19.869 1.607   1.00 31.71 ?  361 HOH   B O    1 
HETATM 6869 O  O    . HOH   G 5 .   ? 34.145 -7.737  11.461  1.00 38.95 ?  362 HOH   B O    1 
HETATM 6870 O  O    . HOH   G 5 .   ? 56.883 -21.540 -16.450 1.00 39.57 ?  363 HOH   B O    1 
HETATM 6871 O  O    . HOH   G 5 .   ? 40.223 -8.803  9.896   1.00 38.33 ?  364 HOH   B O    1 
HETATM 6872 O  O    . HOH   G 5 .   ? 27.129 -25.945 -11.418 1.00 31.76 ?  365 HOH   B O    1 
HETATM 6873 O  O    . HOH   G 5 .   ? 58.867 -10.446 9.216   1.00 38.86 ?  366 HOH   B O    1 
HETATM 6874 O  O    . HOH   G 5 .   ? 32.484 -23.619 14.093  1.00 40.75 ?  367 HOH   B O    1 
HETATM 6875 O  O    . HOH   G 5 .   ? 54.171 -5.724  2.977   1.00 36.07 ?  368 HOH   B O    1 
HETATM 6876 O  O    . HOH   G 5 .   ? 40.051 -11.343 -13.948 1.00 30.70 ?  369 HOH   B O    1 
HETATM 6877 O  O    . HOH   G 5 .   ? 36.184 -8.696  8.974   1.00 38.65 ?  370 HOH   B O    1 
HETATM 6878 O  O    . HOH   G 5 .   ? 41.843 -10.051 -17.463 1.00 55.98 ?  371 HOH   B O    1 
HETATM 6879 O  O    . HOH   G 5 .   ? 48.379 -26.490 8.743   1.00 39.34 ?  372 HOH   B O    1 
HETATM 6880 O  O    . HOH   G 5 .   ? 39.818 -7.038  7.846   1.00 41.90 ?  373 HOH   B O    1 
HETATM 6881 O  O    . HOH   G 5 .   ? 56.024 -7.802  -0.599  1.00 36.13 ?  374 HOH   B O    1 
HETATM 6882 O  O    . HOH   G 5 .   ? 52.057 -12.914 13.321  1.00 31.05 ?  375 HOH   B O    1 
HETATM 6883 O  O    . HOH   G 5 .   ? 63.001 -12.405 6.948   1.00 36.30 ?  376 HOH   B O    1 
HETATM 6884 O  O    . HOH   G 5 .   ? 38.028 -10.573 10.039  1.00 28.50 ?  377 HOH   B O    1 
HETATM 6885 O  O    . HOH   G 5 .   ? 44.092 -5.628  -3.523  1.00 45.08 ?  378 HOH   B O    1 
HETATM 6886 O  O    . HOH   G 5 .   ? 41.805 -6.731  -4.829  1.00 45.49 ?  379 HOH   B O    1 
HETATM 6887 O  O    . HOH   G 5 .   ? 36.488 -22.797 13.309  1.00 25.38 ?  380 HOH   B O    1 
HETATM 6888 O  O    . HOH   G 5 .   ? 40.115 -7.662  3.210   1.00 37.53 ?  381 HOH   B O    1 
HETATM 6889 O  O    . HOH   G 5 .   ? 42.657 -17.103 -23.196 1.00 42.41 ?  382 HOH   B O    1 
HETATM 6890 O  O    . HOH   G 5 .   ? 52.788 -29.861 7.140   1.00 22.90 ?  383 HOH   B O    1 
HETATM 6891 O  O    . HOH   G 5 .   ? 39.711 -14.076 15.718  1.00 53.53 ?  384 HOH   B O    1 
HETATM 6892 O  O    . HOH   G 5 .   ? 41.036 -9.782  15.778  1.00 45.64 ?  385 HOH   B O    1 
HETATM 6893 O  O    . HOH   G 5 .   ? 60.459 -22.268 2.833   1.00 47.48 ?  386 HOH   B O    1 
HETATM 6894 O  O    . HOH   G 5 .   ? 46.730 -5.431  2.934   1.00 40.12 ?  387 HOH   B O    1 
HETATM 6895 O  O    . HOH   G 5 .   ? 23.903 -20.858 -7.649  1.00 26.71 ?  388 HOH   B O    1 
HETATM 6896 O  O    . HOH   G 5 .   ? 35.335 -20.326 13.335  1.00 28.96 ?  389 HOH   B O    1 
HETATM 6897 O  O    . HOH   G 5 .   ? 35.359 -33.685 7.293   1.00 40.19 ?  390 HOH   B O    1 
HETATM 6898 O  O    . HOH   G 5 .   ? 40.697 -6.619  -0.838  1.00 23.99 ?  391 HOH   B O    1 
HETATM 6899 O  O    . HOH   G 5 .   ? 44.038 -31.725 -3.857  1.00 35.87 ?  392 HOH   B O    1 
HETATM 6900 O  O    . HOH   G 5 .   ? 27.871 -27.067 2.219   1.00 30.01 ?  393 HOH   B O    1 
HETATM 6901 O  O    . HOH   G 5 .   ? 26.583 -27.923 -13.465 1.00 34.52 ?  394 HOH   B O    1 
HETATM 6902 O  O    . HOH   G 5 .   ? 34.362 -33.457 9.575   1.00 32.42 ?  395 HOH   B O    1 
HETATM 6903 O  O    . HOH   G 5 .   ? 50.593 -30.777 8.679   1.00 26.11 ?  396 HOH   B O    1 
HETATM 6904 O  O    . HOH   G 5 .   ? 24.564 -20.663 -10.475 1.00 34.14 ?  397 HOH   B O    1 
HETATM 6905 O  O    . HOH   G 5 .   ? 26.835 -30.666 -12.615 1.00 28.14 ?  398 HOH   B O    1 
HETATM 6906 O  O    . HOH   G 5 .   ? 45.687 -20.249 15.257  1.00 50.91 ?  399 HOH   B O    1 
HETATM 6907 O  O    . HOH   G 5 .   ? 57.573 -6.492  -2.358  1.00 33.53 ?  400 HOH   B O    1 
HETATM 6908 O  O    . HOH   G 5 .   ? 40.955 -11.792 -22.322 1.00 42.16 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   A VAL   A 3   ? 0.6513 0.6483 0.6962 0.0155  -0.0325 0.0855  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.6500 0.6471 0.6830 0.0118  -0.0281 0.0735  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.6500 0.6470 0.6888 0.0133  -0.0307 0.0860  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.6488 0.6458 0.6766 0.0102  -0.0272 0.0748  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.6380 0.6381 0.6630 0.0073  -0.0327 0.0907  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.6377 0.6373 0.6562 0.0055  -0.0307 0.0843  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.6399 0.6406 0.6714 0.0081  -0.0356 0.0921  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.6401 0.6398 0.6645 0.0059  -0.0330 0.0850  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.6585 0.6529 0.7026 0.0157  -0.0282 0.0820  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.6563 0.6513 0.6868 0.0122  -0.0239 0.0677  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.6617 0.6547 0.7050 0.0169  -0.0281 0.0804  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.6591 0.6528 0.6883 0.0130  -0.0233 0.0650  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.6608 0.6552 0.7045 0.0162  -0.0274 0.0809  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.6586 0.6534 0.6881 0.0127  -0.0228 0.0657  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.6214 0.6243 0.6236 0.0000  -0.0322 0.0928  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.5855 0.5947 0.5463 -0.0137 -0.0322 0.1015  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.5337 0.5566 0.4993 -0.0285 -0.0186 0.0789  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.5340 0.5566 0.4952 -0.0305 -0.0197 0.0818  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.5968 0.6003 0.5069 -0.0131 -0.0435 0.1320  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.6039 0.6033 0.4719 -0.0134 -0.0556 0.1604  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.6072 0.6047 0.4616 -0.0146 -0.0631 0.1701  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.6050 0.6030 0.4649 -0.0118 -0.0582 0.1724  4   ASN   A ND2 
46   N  N   . SER   A 5   ? 0.4783 0.5131 0.4513 -0.0419 -0.0021 0.0535  5   SER   A N   
47   C  CA  . SER   A 5   ? 0.4204 0.4654 0.3981 -0.0542 0.0180  0.0233  5   SER   A CA  
48   C  C   . SER   A 5   ? 0.3574 0.4059 0.3295 -0.0573 0.0372  0.0033  5   SER   A C   
49   O  O   . SER   A 5   ? 0.3671 0.4148 0.3275 -0.0416 0.0392  -0.0114 5   SER   A O   
50   C  CB  . SER   A 5   ? 0.4250 0.4770 0.4319 -0.0622 0.0173  0.0122  5   SER   A CB  
51   O  OG  . SER   A 5   ? 0.4269 0.4812 0.4433 -0.0672 0.0171  0.0062  5   SER   A OG  
57   N  N   A PHE   A 6   ? 0.3091 0.3679 0.2769 -0.0699 0.0541  0.0121  6   PHE   A N   
58   N  N   B PHE   A 6   ? 0.3277 0.3729 0.2958 -0.0651 0.0442  -0.0010 6   PHE   A N   
59   C  CA  A PHE   A 6   ? 0.2641 0.3246 0.2253 -0.0796 0.0632  0.0290  6   PHE   A CA  
60   C  CA  B PHE   A 6   ? 0.2988 0.3361 0.2626 -0.0720 0.0481  -0.0010 6   PHE   A CA  
61   C  C   A PHE   A 6   ? 0.2507 0.3153 0.2323 -0.0871 0.0757  0.0256  6   PHE   A C   
62   C  C   B PHE   A 6   ? 0.2946 0.3247 0.2734 -0.0746 0.0556  -0.0013 6   PHE   A C   
63   O  O   A PHE   A 6   ? 0.2552 0.3151 0.2611 -0.0913 0.0721  0.0381  6   PHE   A O   
64   O  O   B PHE   A 6   ? 0.2987 0.3249 0.2858 -0.0769 0.0545  0.0085  6   PHE   A O   
65   C  CB  A PHE   A 6   ? 0.2401 0.2913 0.1968 -0.0722 0.0515  0.0454  6   PHE   A CB  
66   C  CB  B PHE   A 6   ? 0.2780 0.3114 0.2393 -0.0711 0.0412  -0.0031 6   PHE   A CB  
67   C  CG  A PHE   A 6   ? 0.2239 0.2638 0.1680 -0.0590 0.0353  0.0551  6   PHE   A CG  
68   C  CG  B PHE   A 6   ? 0.2619 0.2897 0.2207 -0.0677 0.0324  -0.0071 6   PHE   A CG  
69   C  CD1 A PHE   A 6   ? 0.2163 0.2537 0.1573 -0.0511 0.0222  0.0561  6   PHE   A CD1 
70   C  CD1 B PHE   A 6   ? 0.2541 0.2816 0.2106 -0.0669 0.0289  -0.0077 6   PHE   A CD1 
71   C  CD2 A PHE   A 6   ? 0.2244 0.2536 0.1750 -0.0494 0.0384  0.0577  6   PHE   A CD2 
72   C  CD2 B PHE   A 6   ? 0.2588 0.2781 0.2219 -0.0635 0.0313  -0.0101 6   PHE   A CD2 
73   C  CE1 A PHE   A 6   ? 0.2161 0.2485 0.1663 -0.0472 0.0243  0.0532  6   PHE   A CE1 
74   C  CE1 B PHE   A 6   ? 0.2514 0.2746 0.2080 -0.0661 0.0339  -0.0059 6   PHE   A CE1 
75   C  CE2 A PHE   A 6   ? 0.2237 0.2499 0.1755 -0.0426 0.0346  0.0537  6   PHE   A CE2 
76   C  CE2 B PHE   A 6   ? 0.2555 0.2694 0.2157 -0.0627 0.0345  -0.0067 6   PHE   A CE2 
77   C  CZ  A PHE   A 6   ? 0.2193 0.2472 0.1733 -0.0449 0.0268  0.0500  6   PHE   A CZ  
78   C  CZ  B PHE   A 6   ? 0.2524 0.2688 0.2102 -0.0649 0.0354  -0.0035 6   PHE   A CZ  
97   N  N   A SER   A 7   ? 0.2331 0.3060 0.2178 -0.0871 0.0886  0.0137  7   SER   A N   
98   N  N   B SER   A 7   ? 0.2853 0.3125 0.2762 -0.0719 0.0608  -0.0111 7   SER   A N   
99   C  CA  A SER   A 7   ? 0.2303 0.3019 0.2209 -0.0751 0.0831  -0.0023 7   SER   A CA  
100  C  CA  B SER   A 7   ? 0.2808 0.3032 0.2781 -0.0625 0.0626  -0.0157 7   SER   A CA  
101  C  C   A SER   A 7   ? 0.2118 0.2713 0.2115 -0.0733 0.0800  -0.0000 7   SER   A C   
102  C  C   B SER   A 7   ? 0.2683 0.2875 0.2554 -0.0563 0.0697  -0.0150 7   SER   A C   
103  O  O   A SER   A 7   ? 0.2229 0.2663 0.2227 -0.0753 0.0766  0.0064  7   SER   A O   
104  O  O   B SER   A 7   ? 0.2718 0.2850 0.2577 -0.0576 0.0690  -0.0117 7   SER   A O   
105  C  CB  A SER   A 7   ? 0.2486 0.3249 0.2399 -0.0608 0.0806  -0.0082 7   SER   A CB  
106  C  CB  B SER   A 7   ? 0.2878 0.3098 0.3010 -0.0593 0.0562  -0.0188 7   SER   A CB  
107  O  OG  A SER   A 7   ? 0.2627 0.3396 0.2665 -0.0514 0.0706  -0.0123 7   SER   A OG  
108  O  OG  B SER   A 7   ? 0.2936 0.3149 0.3264 -0.0547 0.0490  -0.0176 7   SER   A OG  
119  N  N   A GLY   A 8   ? 0.1924 0.2468 0.2019 -0.0656 0.0683  -0.0125 8   GLY   A N   
120  N  N   B GLY   A 8   ? 0.2549 0.2761 0.2332 -0.0480 0.0712  -0.0167 8   GLY   A N   
121  C  CA  A GLY   A 8   ? 0.1808 0.2236 0.1997 -0.0437 0.0728  -0.0031 8   GLY   A CA  
122  C  CA  B GLY   A 8   ? 0.2374 0.2595 0.2129 -0.0420 0.0689  -0.0109 8   GLY   A CA  
123  C  C   A GLY   A 8   ? 0.1695 0.2040 0.1960 -0.0249 0.0499  0.0059  8   GLY   A C   
124  C  C   B GLY   A 8   ? 0.2161 0.2420 0.1888 -0.0389 0.0597  -0.0002 8   GLY   A C   
125  O  O   A GLY   A 8   ? 0.1730 0.2016 0.2063 -0.0057 0.0351  -0.0104 8   GLY   A O   
126  O  O   B GLY   A 8   ? 0.2163 0.2401 0.2022 -0.0369 0.0622  -0.0008 8   GLY   A O   
133  N  N   A TYR   A 9   ? 0.1522 0.1900 0.1768 -0.0179 0.0373  0.0194  9   TYR   A N   
134  N  N   B TYR   A 9   ? 0.1916 0.2268 0.1799 -0.0338 0.0442  0.0124  9   TYR   A N   
135  C  CA  A TYR   A 9   ? 0.1355 0.1745 0.1589 -0.0184 0.0284  0.0181  9   TYR   A CA  
136  C  CA  B TYR   A 9   ? 0.1696 0.2068 0.1743 -0.0296 0.0283  0.0225  9   TYR   A CA  
137  C  C   A TYR   A 9   ? 0.1347 0.1625 0.1707 -0.0147 0.0217  0.0347  9   TYR   A C   
138  C  C   B TYR   A 9   ? 0.1582 0.1907 0.1675 -0.0267 0.0227  0.0399  9   TYR   A C   
139  O  O   A TYR   A 9   ? 0.1433 0.1802 0.1920 -0.0157 0.0149  0.0381  9   TYR   A O   
140  O  O   B TYR   A 9   ? 0.1559 0.1998 0.1745 -0.0251 0.0065  0.0590  9   TYR   A O   
141  C  CB  A TYR   A 9   ? 0.1342 0.1791 0.1607 -0.0153 0.0261  0.0087  9   TYR   A CB  
142  C  CB  B TYR   A 9   ? 0.1614 0.2037 0.1709 -0.0237 0.0157  0.0168  9   TYR   A CB  
143  C  CG  A TYR   A 9   ? 0.1410 0.1791 0.1716 -0.0114 0.0426  -0.0062 9   TYR   A CG  
144  C  CG  B TYR   A 9   ? 0.1506 0.1969 0.1621 -0.0187 0.0153  0.0092  9   TYR   A CG  
145  C  CD1 A TYR   A 9   ? 0.1474 0.1790 0.1798 -0.0173 0.0519  -0.0154 9   TYR   A CD1 
146  C  CD1 B TYR   A 9   ? 0.1524 0.1947 0.1735 -0.0210 0.0199  0.0031  9   TYR   A CD1 
147  C  CD2 A TYR   A 9   ? 0.1447 0.1769 0.1840 -0.0062 0.0402  0.0009  9   TYR   A CD2 
148  C  CD2 B TYR   A 9   ? 0.1479 0.1899 0.1524 -0.0096 0.0142  0.0068  9   TYR   A CD2 
149  C  CE1 A TYR   A 9   ? 0.1531 0.1808 0.1880 -0.0177 0.0501  -0.0232 9   TYR   A CE1 
150  C  CE1 B TYR   A 9   ? 0.1505 0.1880 0.1768 -0.0162 0.0254  -0.0060 9   TYR   A CE1 
151  C  CE2 A TYR   A 9   ? 0.1489 0.1814 0.1895 -0.0095 0.0466  -0.0093 9   TYR   A CE2 
152  C  CE2 B TYR   A 9   ? 0.1457 0.1878 0.1562 -0.0049 0.0237  0.0009  9   TYR   A CE2 
153  C  CZ  A TYR   A 9   ? 0.1524 0.1836 0.2061 -0.0203 0.0564  -0.0139 9   TYR   A CZ  
154  C  CZ  B TYR   A 9   ? 0.1430 0.1830 0.1767 -0.0063 0.0394  -0.0037 9   TYR   A CZ  
155  O  OH  A TYR   A 9   ? 0.1603 0.1897 0.2367 -0.0233 0.0557  -0.0175 9   TYR   A OH  
156  O  OH  B TYR   A 9   ? 0.1383 0.1810 0.1949 -0.0016 0.0478  -0.0007 9   TYR   A OH  
175  N  N   A LEU   A 10  ? 0.1394 0.1463 0.1706 -0.0149 0.0164  0.0252  10  LEU   A N   
176  N  N   B LEU   A 10  ? 0.1562 0.1733 0.1670 -0.0205 0.0223  0.0325  10  LEU   A N   
177  C  CA  A LEU   A 10  ? 0.1287 0.1411 0.1731 -0.0138 0.0155  0.0306  10  LEU   A CA  
178  C  CA  B LEU   A 10  ? 0.1481 0.1620 0.1772 -0.0170 0.0221  0.0215  10  LEU   A CA  
179  C  C   A LEU   A 10  ? 0.1259 0.1411 0.1676 -0.0154 0.0217  0.0326  10  LEU   A C   
180  C  C   B LEU   A 10  ? 0.1423 0.1521 0.1638 -0.0175 0.0154  0.0316  10  LEU   A C   
181  O  O   A LEU   A 10  ? 0.1246 0.1348 0.1828 -0.0117 0.0338  0.0352  10  LEU   A O   
182  O  O   B LEU   A 10  ? 0.1419 0.1502 0.1783 -0.0140 0.0278  0.0389  10  LEU   A O   
183  C  CB  A LEU   A 10  ? 0.1339 0.1404 0.1993 -0.0058 0.0154  0.0390  10  LEU   A CB  
184  C  CB  B LEU   A 10  ? 0.1505 0.1582 0.1950 -0.0180 0.0195  0.0185  10  LEU   A CB  
185  C  CG  A LEU   A 10  ? 0.1615 0.1528 0.2505 -0.0019 -0.0039 0.0381  10  LEU   A CG  
186  C  CG  B LEU   A 10  ? 0.1612 0.1677 0.2198 -0.0125 0.0110  0.0081  10  LEU   A CG  
187  C  CD1 A LEU   A 10  ? 0.1753 0.1612 0.2747 -0.0157 0.0046  0.0357  10  LEU   A CD1 
188  C  CD1 B LEU   A 10  ? 0.1691 0.1762 0.2415 -0.0195 0.0131  0.0108  10  LEU   A CD1 
189  C  CD2 A LEU   A 10  ? 0.1801 0.1627 0.2710 0.0083  -0.0055 0.0156  10  LEU   A CD2 
190  C  CD2 B LEU   A 10  ? 0.1729 0.1812 0.2467 -0.0033 0.0015  0.0012  10  LEU   A CD2 
213  N  N   A LYS   A 11  ? 0.1305 0.1404 0.1594 -0.0183 0.0203  0.0348  11  LYS   A N   
214  N  N   B LYS   A 11  ? 0.1434 0.1405 0.1461 -0.0233 0.0043  0.0286  11  LYS   A N   
215  C  CA  A LYS   A 11  ? 0.1302 0.1396 0.1727 -0.0294 0.0193  0.0274  11  LYS   A CA  
216  C  CA  B LYS   A 11  ? 0.1476 0.1340 0.1567 -0.0240 0.0058  0.0285  11  LYS   A CA  
217  C  C   A LYS   A 11  ? 0.1290 0.1441 0.1680 -0.0283 0.0279  0.0139  11  LYS   A C   
218  C  C   B LYS   A 11  ? 0.1419 0.1264 0.1561 -0.0219 0.0080  0.0186  11  LYS   A C   
219  O  O   A LYS   A 11  ? 0.1387 0.1581 0.2036 -0.0495 0.0300  0.0005  11  LYS   A O   
220  O  O   B LYS   A 11  ? 0.1339 0.1216 0.1771 -0.0208 0.0146  -0.0020 11  LYS   A O   
221  C  CB  A LYS   A 11  ? 0.1405 0.1384 0.1726 -0.0324 0.0119  0.0248  11  LYS   A CB  
222  C  CB  B LYS   A 11  ? 0.1584 0.1328 0.1624 -0.0205 0.0026  0.0337  11  LYS   A CB  
223  C  CG  A LYS   A 11  ? 0.1563 0.1426 0.1760 -0.0299 0.0185  0.0303  11  LYS   A CG  
224  C  CG  B LYS   A 11  ? 0.1704 0.1366 0.1785 -0.0160 0.0034  0.0392  11  LYS   A CG  
225  C  CD  A LYS   A 11  ? 0.1721 0.1455 0.1673 -0.0241 0.0169  0.0289  11  LYS   A CD  
226  C  CD  B LYS   A 11  ? 0.1798 0.1385 0.1929 -0.0096 0.0014  0.0433  11  LYS   A CD  
227  C  CE  A LYS   A 11  ? 0.1789 0.1461 0.1590 -0.0201 0.0202  0.0295  11  LYS   A CE  
228  C  CE  B LYS   A 11  ? 0.1845 0.1382 0.2053 -0.0048 0.0001  0.0475  11  LYS   A CE  
229  N  NZ  A LYS   A 11  ? 0.1790 0.1491 0.1657 -0.0126 0.0136  0.0335  11  LYS   A NZ  
230  N  NZ  B LYS   A 11  ? 0.1835 0.1354 0.2178 0.0026  -0.0067 0.0474  11  LYS   A NZ  
257  N  N   A LEU   A 12  ? 0.1205 0.1418 0.1495 -0.0277 0.0245  0.0114  12  LEU   A N   
258  N  N   B LEU   A 12  ? 0.1384 0.1341 0.1508 -0.0136 0.0063  0.0193  12  LEU   A N   
259  C  CA  A LEU   A 12  ? 0.1239 0.1477 0.1501 -0.0254 0.0116  0.0205  12  LEU   A CA  
260  C  CA  B LEU   A 12  ? 0.1388 0.1474 0.1501 -0.0041 0.0062  0.0143  12  LEU   A CA  
261  C  C   A LEU   A 12  ? 0.1252 0.1411 0.1697 -0.0325 0.0129  0.0249  12  LEU   A C   
262  C  C   B LEU   A 12  ? 0.1438 0.1465 0.1524 -0.0011 0.0134  0.0228  12  LEU   A C   
263  O  O   A LEU   A 12  ? 0.1283 0.1397 0.1757 -0.0281 0.0179  0.0112  12  LEU   A O   
264  O  O   B LEU   A 12  ? 0.1496 0.1421 0.1513 0.0059  0.0082  0.0218  12  LEU   A O   
265  C  CB  A LEU   A 12  ? 0.1302 0.1415 0.1492 -0.0231 0.0046  0.0243  12  LEU   A CB  
266  C  CB  B LEU   A 12  ? 0.1403 0.1561 0.1580 0.0012  0.0023  0.0101  12  LEU   A CB  
267  C  CG  A LEU   A 12  ? 0.1436 0.1430 0.1691 -0.0124 0.0158  0.0226  12  LEU   A CG  
268  C  CG  B LEU   A 12  ? 0.1454 0.1635 0.1681 0.0032  0.0123  0.0025  12  LEU   A CG  
269  C  CD1 A LEU   A 12  ? 0.1540 0.1453 0.1868 0.0033  0.0290  0.0344  12  LEU   A CD1 
270  C  CD1 B LEU   A 12  ? 0.1487 0.1684 0.1828 0.0085  0.0239  -0.0042 12  LEU   A CD1 
271  C  CD2 A LEU   A 12  ? 0.1464 0.1463 0.1775 -0.0096 0.0134  0.0145  12  LEU   A CD2 
272  C  CD2 B LEU   A 12  ? 0.1490 0.1704 0.1904 0.0042  0.0041  -0.0048 12  LEU   A CD2 
295  N  N   A THR   A 13  ? 0.1209 0.1418 0.1952 -0.0354 0.0102  0.0248  13  THR   A N   
296  N  N   B THR   A 13  ? 0.1403 0.1441 0.1609 -0.0005 0.0163  0.0221  13  THR   A N   
297  C  CA  A THR   A 13  ? 0.1261 0.1454 0.1948 -0.0299 0.0134  0.0345  13  THR   A CA  
298  C  CA  B THR   A 13  ? 0.1404 0.1409 0.1693 -0.0012 0.0208  0.0242  13  THR   A CA  
299  C  C   A THR   A 13  ? 0.1279 0.1495 0.1942 -0.0364 0.0115  0.0501  13  THR   A C   
300  C  C   B THR   A 13  ? 0.1500 0.1444 0.1695 -0.0072 0.0151  0.0200  13  THR   A C   
301  O  O   A THR   A 13  ? 0.1320 0.1514 0.2133 -0.0318 0.0094  0.0509  13  THR   A O   
302  O  O   B THR   A 13  ? 0.1531 0.1413 0.1692 -0.0023 0.0125  0.0237  13  THR   A O   
303  C  CB  A THR   A 13  ? 0.1329 0.1530 0.2034 -0.0221 0.0116  0.0326  13  THR   A CB  
304  C  CB  B THR   A 13  ? 0.1312 0.1416 0.1820 0.0012  0.0251  0.0321  13  THR   A CB  
305  O  OG1 A THR   A 13  ? 0.1316 0.1416 0.2096 -0.0184 -0.0029 0.0422  13  THR   A OG1 
306  O  OG1 B THR   A 13  ? 0.1150 0.1458 0.2062 -0.0071 0.0260  0.0402  13  THR   A OG1 
307  C  CG2 A THR   A 13  ? 0.1392 0.1603 0.2174 -0.0118 0.0141  0.0130  13  THR   A CG2 
308  C  CG2 B THR   A 13  ? 0.1401 0.1459 0.1902 0.0081  0.0248  0.0254  13  THR   A CG2 
323  N  N   A ASP   A 14  ? 0.1363 0.1482 0.1892 -0.0363 0.0032  0.0563  14  ASP   A N   
324  N  N   B ASP   A 14  ? 0.1578 0.1474 0.1792 -0.0106 0.0067  0.0076  14  ASP   A N   
325  C  CA  A ASP   A 14  ? 0.1396 0.1530 0.2041 -0.0295 -0.0061 0.0658  14  ASP   A CA  
326  C  CA  B ASP   A 14  ? 0.1599 0.1512 0.1851 -0.0067 0.0038  0.0063  14  ASP   A CA  
327  C  C   A ASP   A 14  ? 0.1329 0.1514 0.1813 -0.0219 -0.0086 0.0640  14  ASP   A C   
328  C  C   B ASP   A 14  ? 0.1445 0.1393 0.1611 -0.0046 0.0012  0.0113  14  ASP   A C   
329  O  O   A ASP   A 14  ? 0.1454 0.1543 0.1935 -0.0249 -0.0044 0.0595  14  ASP   A O   
330  O  O   B ASP   A 14  ? 0.1483 0.1389 0.1640 -0.0050 0.0064  0.0050  14  ASP   A O   
331  C  CB  A ASP   A 14  ? 0.1615 0.1627 0.2628 -0.0369 -0.0070 0.0739  14  ASP   A CB  
332  C  CB  B ASP   A 14  ? 0.1831 0.1758 0.2284 -0.0051 0.0058  0.0110  14  ASP   A CB  
333  C  CG  A ASP   A 14  ? 0.1834 0.2026 0.3329 -0.0331 0.0011  0.0707  14  ASP   A CG  
334  C  CG  B ASP   A 14  ? 0.2018 0.2107 0.2712 -0.0014 0.0077  0.0122  14  ASP   A CG  
335  O  OD1 A ASP   A 14  ? 0.1836 0.2105 0.3506 -0.0361 0.0095  0.0892  14  ASP   A OD1 
336  O  OD1 B ASP   A 14  ? 0.2101 0.2180 0.2865 0.0005  0.0095  0.0257  14  ASP   A OD1 
337  O  OD2 A ASP   A 14  ? 0.1973 0.2285 0.3683 -0.0261 -0.0129 0.0420  14  ASP   A OD2 
338  O  OD2 B ASP   A 14  ? 0.2078 0.2333 0.2914 0.0056  0.0002  -0.0001 14  ASP   A OD2 
347  N  N   A ASN   A 15  ? 0.1270 0.1491 0.1820 -0.0229 0.0104  0.0616  15  ASN   A N   
348  N  N   B ASN   A 15  ? 0.1306 0.1326 0.1520 -0.0115 0.0034  0.0194  15  ASN   A N   
349  C  CA  A ASN   A 15  ? 0.1285 0.1463 0.1977 -0.0189 0.0016  0.0458  15  ASN   A CA  
350  C  CA  B ASN   A 15  ? 0.1277 0.1356 0.1714 -0.0122 0.0003  0.0164  15  ASN   A CA  
351  C  C   A ASN   A 15  ? 0.1258 0.1388 0.1983 -0.0198 0.0067  0.0373  15  ASN   A C   
352  C  C   B ASN   A 15  ? 0.1242 0.1364 0.1893 -0.0101 0.0100  0.0237  15  ASN   A C   
353  O  O   A ASN   A 15  ? 0.1230 0.1314 0.1902 -0.0133 0.0060  0.0290  15  ASN   A O   
354  O  O   B ASN   A 15  ? 0.1199 0.1336 0.1955 -0.0020 0.0173  0.0169  15  ASN   A O   
355  C  CB  A ASN   A 15  ? 0.1250 0.1435 0.2011 -0.0136 -0.0005 0.0469  15  ASN   A CB  
356  C  CB  B ASN   A 15  ? 0.1257 0.1331 0.1739 -0.0150 0.0038  0.0121  15  ASN   A CB  
357  C  CG  A ASN   A 15  ? 0.1227 0.1494 0.2067 -0.0093 0.0155  0.0331  15  ASN   A CG  
358  C  CG  B ASN   A 15  ? 0.1243 0.1390 0.1804 -0.0104 0.0088  0.0046  15  ASN   A CG  
359  O  OD1 A ASN   A 15  ? 0.1212 0.1480 0.2214 -0.0122 0.0230  0.0311  15  ASN   A OD1 
360  O  OD1 B ASN   A 15  ? 0.1208 0.1441 0.1892 -0.0140 0.0190  0.0016  15  ASN   A OD1 
361  N  ND2 A ASN   A 15  ? 0.1262 0.1597 0.2046 -0.0120 0.0216  0.0336  15  ASN   A ND2 
362  N  ND2 B ASN   A 15  ? 0.1307 0.1418 0.1796 -0.0077 0.0023  0.0060  15  ASN   A ND2 
375  N  N   A VAL   A 16  ? 0.1235 0.1310 0.1852 -0.0134 0.0068  0.0353  16  VAL   A N   
376  N  N   B VAL   A 16  ? 0.1257 0.1351 0.1910 -0.0076 0.0112  0.0366  16  VAL   A N   
377  C  CA  A VAL   A 16  ? 0.1245 0.1336 0.1850 -0.0100 0.0104  0.0322  16  VAL   A CA  
378  C  CA  B VAL   A 16  ? 0.1293 0.1382 0.1887 -0.0054 0.0208  0.0419  16  VAL   A CA  
379  C  C   A VAL   A 16  ? 0.1180 0.1270 0.1731 -0.0155 0.0054  0.0263  16  VAL   A C   
380  C  C   B VAL   A 16  ? 0.1272 0.1452 0.1775 -0.0065 0.0147  0.0421  16  VAL   A C   
381  O  O   A VAL   A 16  ? 0.1123 0.1221 0.1688 -0.0222 0.0112  0.0122  16  VAL   A O   
382  O  O   B VAL   A 16  ? 0.1289 0.1490 0.1739 -0.0039 0.0221  0.0366  16  VAL   A O   
383  C  CB  A VAL   A 16  ? 0.1338 0.1497 0.1856 0.0039  0.0225  0.0380  16  VAL   A CB  
384  C  CB  B VAL   A 16  ? 0.1367 0.1380 0.1805 0.0033  0.0304  0.0440  16  VAL   A CB  
385  C  CG1 A VAL   A 16  ? 0.1464 0.1630 0.1972 0.0100  0.0211  0.0307  16  VAL   A CG1 
386  C  CG1 B VAL   A 16  ? 0.1426 0.1376 0.1803 0.0078  0.0263  0.0384  16  VAL   A CG1 
387  C  CG2 A VAL   A 16  ? 0.1402 0.1605 0.1938 0.0085  0.0377  0.0376  16  VAL   A CG2 
388  C  CG2 B VAL   A 16  ? 0.1412 0.1469 0.1884 0.0056  0.0461  0.0472  16  VAL   A CG2 
407  N  N   A TYR   A 17  ? 0.1210 0.1235 0.1781 -0.0137 0.0173  0.0274  17  TYR   A N   
408  N  N   B TYR   A 17  ? 0.1239 0.1410 0.1677 -0.0108 0.0059  0.0378  17  TYR   A N   
409  C  CA  A TYR   A 17  ? 0.1313 0.1299 0.1639 -0.0155 0.0131  0.0281  17  TYR   A CA  
410  C  CA  B TYR   A 17  ? 0.1229 0.1400 0.1433 -0.0164 0.0056  0.0382  17  TYR   A CA  
411  C  C   A TYR   A 17  ? 0.1302 0.1229 0.1576 -0.0142 0.0135  0.0171  17  TYR   A C   
412  C  C   B TYR   A 17  ? 0.1229 0.1377 0.1365 -0.0154 0.0107  0.0302  17  TYR   A C   
413  O  O   A TYR   A 17  ? 0.1251 0.1156 0.1612 -0.0101 0.0140  0.0185  17  TYR   A O   
414  O  O   B TYR   A 17  ? 0.1161 0.1414 0.1338 -0.0208 0.0132  0.0265  17  TYR   A O   
415  C  CB  A TYR   A 17  ? 0.1441 0.1388 0.1790 -0.0220 -0.0036 0.0398  17  TYR   A CB  
416  C  CB  B TYR   A 17  ? 0.1246 0.1439 0.1533 -0.0139 -0.0057 0.0388  17  TYR   A CB  
417  C  CG  A TYR   A 17  ? 0.1561 0.1479 0.1926 -0.0232 -0.0135 0.0402  17  TYR   A CG  
418  C  CG  B TYR   A 17  ? 0.1278 0.1502 0.1519 -0.0093 -0.0062 0.0346  17  TYR   A CG  
419  C  CD1 A TYR   A 17  ? 0.1636 0.1578 0.2106 -0.0164 -0.0054 0.0437  17  TYR   A CD1 
420  C  CD1 B TYR   A 17  ? 0.1304 0.1562 0.1568 -0.0011 -0.0020 0.0413  17  TYR   A CD1 
421  C  CD2 A TYR   A 17  ? 0.1613 0.1489 0.1891 -0.0253 -0.0149 0.0470  17  TYR   A CD2 
422  C  CD2 B TYR   A 17  ? 0.1308 0.1521 0.1530 -0.0078 -0.0028 0.0368  17  TYR   A CD2 
423  C  CE1 A TYR   A 17  ? 0.1611 0.1546 0.2154 -0.0133 -0.0061 0.0436  17  TYR   A CE1 
424  C  CE1 B TYR   A 17  ? 0.1418 0.1577 0.1644 -0.0002 0.0057  0.0410  17  TYR   A CE1 
425  C  CE2 A TYR   A 17  ? 0.1666 0.1508 0.1990 -0.0188 -0.0167 0.0388  17  TYR   A CE2 
426  C  CE2 B TYR   A 17  ? 0.1358 0.1504 0.1586 0.0002  0.0019  0.0280  17  TYR   A CE2 
427  C  CZ  A TYR   A 17  ? 0.1654 0.1479 0.2006 -0.0172 -0.0102 0.0395  17  TYR   A CZ  
428  C  CZ  B TYR   A 17  ? 0.1397 0.1500 0.1631 0.0041  0.0051  0.0365  17  TYR   A CZ  
429  O  OH  A TYR   A 17  ? 0.1787 0.1480 0.2073 -0.0070 -0.0044 0.0313  17  TYR   A OH  
430  O  OH  B TYR   A 17  ? 0.1374 0.1465 0.1788 0.0134  0.0162  0.0345  17  TYR   A OH  
449  N  N   A ILE   A 18  ? 0.1364 0.1287 0.1629 -0.0133 0.0138  0.0246  18  ILE   A N   
450  N  N   B ILE   A 18  ? 0.1215 0.1350 0.1424 -0.0135 0.0136  0.0273  18  ILE   A N   
451  C  CA  A ILE   A 18  ? 0.1395 0.1320 0.1704 -0.0144 0.0155  0.0235  18  ILE   A CA  
452  C  CA  B ILE   A 18  ? 0.1194 0.1280 0.1326 -0.0082 0.0181  0.0232  18  ILE   A CA  
453  C  C   A ILE   A 18  ? 0.1426 0.1357 0.1906 -0.0216 0.0216  0.0190  18  ILE   A C   
454  C  C   B ILE   A 18  ? 0.1183 0.1341 0.1319 -0.0105 0.0147  0.0173  18  ILE   A C   
455  O  O   A ILE   A 18  ? 0.1379 0.1425 0.1890 -0.0297 0.0319  0.0247  18  ILE   A O   
456  O  O   B ILE   A 18  ? 0.1195 0.1406 0.1331 -0.0107 0.0261  0.0189  18  ILE   A O   
457  C  CB  A ILE   A 18  ? 0.1513 0.1420 0.1532 -0.0033 0.0115  0.0217  18  ILE   A CB  
458  C  CB  B ILE   A 18  ? 0.1285 0.1260 0.1169 -0.0014 0.0179  0.0306  18  ILE   A CB  
459  C  CG1 A ILE   A 18  ? 0.1664 0.1530 0.1499 -0.0000 -0.0062 0.0184  18  ILE   A CG1 
460  C  CG1 B ILE   A 18  ? 0.1383 0.1356 0.1249 -0.0098 0.0178  0.0428  18  ILE   A CG1 
461  C  CG2 A ILE   A 18  ? 0.1449 0.1371 0.1608 0.0013  0.0221  0.0025  18  ILE   A CG2 
462  C  CG2 B ILE   A 18  ? 0.1326 0.1327 0.1172 -0.0075 0.0096  0.0333  18  ILE   A CG2 
463  C  CD1 A ILE   A 18  ? 0.1906 0.1681 0.1759 0.0060  -0.0126 0.0089  18  ILE   A CD1 
464  C  CD1 B ILE   A 18  ? 0.1594 0.1508 0.1480 -0.0123 0.0023  0.0346  18  ILE   A CD1 
487  N  N   A LYS   A 19  ? 0.1516 0.1368 0.1982 -0.0104 0.0378  0.0257  19  LYS   A N   
488  N  N   B LYS   A 19  ? 0.1222 0.1324 0.1362 -0.0095 0.0259  0.0112  19  LYS   A N   
489  C  CA  A LYS   A 19  ? 0.1628 0.1448 0.2222 -0.0076 0.0445  0.0328  19  LYS   A CA  
490  C  CA  B LYS   A 19  ? 0.1352 0.1476 0.1626 -0.0048 0.0352  0.0071  19  LYS   A CA  
491  C  C   A LYS   A 19  ? 0.1559 0.1402 0.2443 -0.0026 0.0429  0.0407  19  LYS   A C   
492  C  C   B LYS   A 19  ? 0.1300 0.1515 0.1807 0.0007  0.0365  0.0122  19  LYS   A C   
493  O  O   A LYS   A 19  ? 0.1478 0.1359 0.2355 0.0012  0.0276  0.0405  19  LYS   A O   
494  O  O   B LYS   A 19  ? 0.1272 0.1464 0.1759 -0.0024 0.0311  0.0203  19  LYS   A O   
495  C  CB  A LYS   A 19  ? 0.1828 0.1665 0.2304 -0.0053 0.0492  0.0261  19  LYS   A CB  
496  C  CB  B LYS   A 19  ? 0.1490 0.1606 0.1664 -0.0025 0.0417  -0.0085 19  LYS   A CB  
497  C  CG  A LYS   A 19  ? 0.2055 0.1847 0.2420 -0.0013 0.0573  0.0143  19  LYS   A CG  
498  C  CG  B LYS   A 19  ? 0.1738 0.1780 0.1825 0.0034  0.0462  -0.0170 19  LYS   A CG  
499  C  CD  A LYS   A 19  ? 0.2258 0.1973 0.2398 0.0038  0.0722  0.0050  19  LYS   A CD  
500  C  CD  B LYS   A 19  ? 0.1982 0.1949 0.1990 0.0047  0.0567  -0.0146 19  LYS   A CD  
501  C  CE  A LYS   A 19  ? 0.2391 0.2025 0.2552 0.0035  0.0768  -0.0028 19  LYS   A CE  
502  C  CE  B LYS   A 19  ? 0.2130 0.2074 0.2092 0.0010  0.0711  -0.0187 19  LYS   A CE  
503  N  NZ  A LYS   A 19  ? 0.2458 0.2038 0.2477 -0.0010 0.0909  -0.0112 19  LYS   A NZ  
504  N  NZ  B LYS   A 19  ? 0.2217 0.2129 0.2181 -0.0031 0.0742  -0.0194 19  LYS   A NZ  
531  N  N   A ASN   A 20  ? 0.1618 0.1434 0.2713 -0.0047 0.0480  0.0472  20  ASN   A N   
532  N  N   B ASN   A 20  ? 0.1345 0.1613 0.2116 0.0059  0.0420  0.0129  20  ASN   A N   
533  C  CA  A ASN   A 20  ? 0.1766 0.1553 0.2883 0.0104  0.0560  0.0393  20  ASN   A CA  
534  C  CA  B ASN   A 20  ? 0.1427 0.1755 0.2352 0.0161  0.0386  0.0096  20  ASN   A CA  
535  C  C   A ASN   A 20  ? 0.1900 0.1581 0.2887 0.0111  0.0598  0.0370  20  ASN   A C   
536  C  C   B ASN   A 20  ? 0.1587 0.1708 0.2452 0.0104  0.0471  0.0100  20  ASN   A C   
537  O  O   A ASN   A 20  ? 0.2055 0.1568 0.2837 0.0055  0.0618  0.0318  20  ASN   A O   
538  O  O   B ASN   A 20  ? 0.1704 0.1698 0.2539 0.0062  0.0493  0.0103  20  ASN   A O   
539  C  CB  A ASN   A 20  ? 0.1819 0.1647 0.2950 0.0124  0.0618  0.0494  20  ASN   A CB  
540  C  CB  B ASN   A 20  ? 0.1395 0.1923 0.2457 0.0227  0.0285  0.0124  20  ASN   A CB  
541  C  CG  A ASN   A 20  ? 0.1924 0.1673 0.3160 0.0224  0.0621  0.0484  20  ASN   A CG  
542  C  CG  B ASN   A 20  ? 0.1409 0.2013 0.2579 0.0307  0.0215  0.0143  20  ASN   A CG  
543  O  OD1 A ASN   A 20  ? 0.2134 0.1786 0.3439 0.0282  0.0565  0.0343  20  ASN   A OD1 
544  O  OD1 B ASN   A 20  ? 0.1407 0.1968 0.2613 0.0337  0.0285  0.0079  20  ASN   A OD1 
545  N  ND2 A ASN   A 20  ? 0.1901 0.1594 0.3156 0.0258  0.0526  0.0665  20  ASN   A ND2 
546  N  ND2 B ASN   A 20  ? 0.1507 0.2098 0.2801 0.0305  0.0077  0.0283  20  ASN   A ND2 
559  N  N   A ALA   A 21  ? 0.1897 0.1622 0.2901 0.0137  0.0497  0.0291  21  ALA   A N   
560  N  N   B ALA   A 21  ? 0.1676 0.1688 0.2475 0.0042  0.0425  0.0078  21  ALA   A N   
561  C  CA  A ALA   A 21  ? 0.1922 0.1641 0.2843 0.0176  0.0421  0.0277  21  ALA   A CA  
562  C  CA  B ALA   A 21  ? 0.1796 0.1641 0.2479 -0.0003 0.0458  0.0104  21  ALA   A CA  
563  C  C   A ALA   A 21  ? 0.1844 0.1679 0.2804 0.0143  0.0394  0.0253  21  ALA   A C   
564  C  C   B ALA   A 21  ? 0.1744 0.1520 0.2361 -0.0005 0.0548  0.0133  21  ALA   A C   
565  O  O   A ALA   A 21  ? 0.1796 0.1678 0.2796 0.0106  0.0411  0.0270  21  ALA   A O   
566  O  O   B ALA   A 21  ? 0.1712 0.1431 0.2454 0.0002  0.0531  0.0016  21  ALA   A O   
567  C  CB  A ALA   A 21  ? 0.2033 0.1664 0.2957 0.0194  0.0400  0.0270  21  ALA   A CB  
568  C  CB  B ALA   A 21  ? 0.1927 0.1694 0.2693 -0.0003 0.0415  0.0055  21  ALA   A CB  
579  N  N   A ASP   A 22  ? 0.1876 0.1697 0.2763 0.0087  0.0305  0.0210  22  ASP   A N   
580  N  N   B ASP   A 22  ? 0.1768 0.1464 0.2188 -0.0011 0.0595  0.0218  22  ASP   A N   
581  C  CA  A ASP   A 22  ? 0.1897 0.1762 0.2688 0.0043  0.0223  0.0099  22  ASP   A CA  
582  C  CA  B ASP   A 22  ? 0.1788 0.1459 0.2103 -0.0011 0.0550  0.0228  22  ASP   A CA  
583  C  C   A ASP   A 22  ? 0.1784 0.1764 0.2302 -0.0008 0.0236  0.0102  22  ASP   A C   
584  C  C   B ASP   A 22  ? 0.1618 0.1490 0.1830 -0.0147 0.0501  0.0178  22  ASP   A C   
585  O  O   A ASP   A 22  ? 0.1800 0.1837 0.2378 -0.0006 0.0268  0.0108  22  ASP   A O   
586  O  O   B ASP   A 22  ? 0.1569 0.1552 0.1742 -0.0234 0.0455  0.0025  22  ASP   A O   
587  C  CB  A ASP   A 22  ? 0.2048 0.1777 0.3035 0.0055  0.0184  0.0010  22  ASP   A CB  
588  C  CB  B ASP   A 22  ? 0.1983 0.1456 0.2325 0.0120  0.0581  0.0179  22  ASP   A CB  
589  C  CG  A ASP   A 22  ? 0.2187 0.1790 0.3405 0.0032  0.0066  0.0043  22  ASP   A CG  
590  C  CG  B ASP   A 22  ? 0.2142 0.1461 0.2501 0.0183  0.0635  0.0182  22  ASP   A CG  
591  O  OD1 A ASP   A 22  ? 0.2094 0.1725 0.3585 -0.0137 -0.0138 0.0185  22  ASP   A OD1 
592  O  OD1 B ASP   A 22  ? 0.2136 0.1424 0.2381 0.0198  0.0594  0.0162  22  ASP   A OD1 
593  O  OD2 A ASP   A 22  ? 0.2361 0.1858 0.3666 0.0140  0.0181  -0.0068 22  ASP   A OD2 
594  O  OD2 B ASP   A 22  ? 0.2256 0.1537 0.2749 0.0145  0.0724  0.0168  22  ASP   A OD2 
603  N  N   A ILE   A 23  ? 0.1776 0.1701 0.2036 -0.0024 0.0196  0.0080  23  ILE   A N   
604  N  N   B ILE   A 23  ? 0.1555 0.1487 0.1783 -0.0163 0.0406  0.0229  23  ILE   A N   
605  C  CA  A ILE   A 23  ? 0.1780 0.1640 0.1820 -0.0063 0.0248  0.0148  23  ILE   A CA  
606  C  CA  B ILE   A 23  ? 0.1474 0.1535 0.1604 -0.0188 0.0319  0.0263  23  ILE   A CA  
607  C  C   A ILE   A 23  ? 0.1782 0.1692 0.1835 -0.0026 0.0336  0.0119  23  ILE   A C   
608  C  C   B ILE   A 23  ? 0.1532 0.1641 0.1679 -0.0210 0.0330  0.0121  23  ILE   A C   
609  O  O   A ILE   A 23  ? 0.1809 0.1784 0.1810 0.0010  0.0360  0.0095  23  ILE   A O   
610  O  O   B ILE   A 23  ? 0.1512 0.1629 0.1607 -0.0209 0.0372  0.0039  23  ILE   A O   
611  C  CB  A ILE   A 23  ? 0.1898 0.1638 0.1577 -0.0023 0.0294  0.0116  23  ILE   A CB  
612  C  CB  B ILE   A 23  ? 0.1437 0.1496 0.1483 -0.0113 0.0193  0.0224  23  ILE   A CB  
613  C  CG1 A ILE   A 23  ? 0.2010 0.1666 0.1560 -0.0045 0.0309  0.0106  23  ILE   A CG1 
614  C  CG1 B ILE   A 23  ? 0.1477 0.1504 0.1408 -0.0145 0.0096  0.0132  23  ILE   A CG1 
615  C  CG2 A ILE   A 23  ? 0.1852 0.1644 0.1563 -0.0027 0.0362  0.0090  23  ILE   A CG2 
616  C  CG2 B ILE   A 23  ? 0.1420 0.1474 0.1464 -0.0057 0.0130  0.0204  23  ILE   A CG2 
617  C  CD1 A ILE   A 23  ? 0.2053 0.1675 0.1520 -0.0083 0.0242  0.0069  23  ILE   A CD1 
618  C  CD1 B ILE   A 23  ? 0.1462 0.1512 0.1412 -0.0124 -0.0030 0.0104  23  ILE   A CD1 
641  N  N   A VAL   A 24  ? 0.1815 0.1718 0.1928 -0.0087 0.0374  0.0023  24  VAL   A N   
642  N  N   B VAL   A 24  ? 0.1638 0.1734 0.1870 -0.0270 0.0283  0.0086  24  VAL   A N   
643  C  CA  A VAL   A 24  ? 0.1940 0.1839 0.2079 -0.0191 0.0414  -0.0081 24  VAL   A CA  
644  C  CA  B VAL   A 24  ? 0.1813 0.1857 0.2008 -0.0269 0.0334  0.0030  24  VAL   A CA  
645  C  C   A VAL   A 24  ? 0.1988 0.2028 0.2152 -0.0305 0.0405  -0.0148 24  VAL   A C   
646  C  C   B VAL   A 24  ? 0.1911 0.2067 0.2033 -0.0237 0.0404  -0.0104 24  VAL   A C   
647  O  O   A VAL   A 24  ? 0.2041 0.2023 0.2221 -0.0271 0.0426  -0.0213 24  VAL   A O   
648  O  O   B VAL   A 24  ? 0.1976 0.2107 0.2134 -0.0211 0.0352  -0.0092 24  VAL   A O   
649  C  CB  A VAL   A 24  ? 0.2034 0.1846 0.2227 -0.0164 0.0473  -0.0056 24  VAL   A CB  
650  C  CB  B VAL   A 24  ? 0.1890 0.1849 0.2227 -0.0270 0.0337  0.0131  24  VAL   A CB  
651  C  CG1 A VAL   A 24  ? 0.2091 0.1880 0.2358 -0.0127 0.0516  -0.0145 24  VAL   A CG1 
652  C  CG1 B VAL   A 24  ? 0.1991 0.1901 0.2464 -0.0283 0.0277  0.0134  24  VAL   A CG1 
653  C  CG2 A VAL   A 24  ? 0.2089 0.1871 0.2325 -0.0131 0.0579  0.0045  24  VAL   A CG2 
654  C  CG2 B VAL   A 24  ? 0.1927 0.1850 0.2303 -0.0245 0.0372  0.0138  24  VAL   A CG2 
673  N  N   A GLU   A 25  ? 0.2047 0.2297 0.2204 -0.0405 0.0436  -0.0287 25  GLU   A N   
674  N  N   B GLU   A 25  ? 0.1951 0.2256 0.2074 -0.0231 0.0571  -0.0261 25  GLU   A N   
675  C  CA  A GLU   A 25  ? 0.2211 0.2585 0.2305 -0.0411 0.0545  -0.0322 25  GLU   A CA  
676  C  CA  B GLU   A 25  ? 0.2058 0.2475 0.2189 -0.0313 0.0661  -0.0286 25  GLU   A CA  
677  C  C   A GLU   A 25  ? 0.2118 0.2608 0.2100 -0.0515 0.0685  -0.0312 25  GLU   A C   
678  C  C   B GLU   A 25  ? 0.2050 0.2584 0.2047 -0.0350 0.0735  -0.0330 25  GLU   A C   
679  O  O   A GLU   A 25  ? 0.2179 0.2679 0.2193 -0.0535 0.0646  -0.0341 25  GLU   A O   
680  O  O   B GLU   A 25  ? 0.2091 0.2618 0.2093 -0.0366 0.0721  -0.0401 25  GLU   A O   
681  C  CB  A GLU   A 25  ? 0.2470 0.2838 0.2668 -0.0341 0.0491  -0.0359 25  GLU   A CB  
682  C  CB  B GLU   A 25  ? 0.2207 0.2580 0.2470 -0.0337 0.0640  -0.0282 25  GLU   A CB  
683  C  CG  A GLU   A 25  ? 0.2698 0.3076 0.3133 -0.0307 0.0331  -0.0401 25  GLU   A CG  
684  C  CG  B GLU   A 25  ? 0.2401 0.2728 0.2947 -0.0358 0.0497  -0.0285 25  GLU   A CG  
685  C  CD  A GLU   A 25  ? 0.2866 0.3301 0.3564 -0.0266 0.0171  -0.0394 25  GLU   A CD  
686  C  CD  B GLU   A 25  ? 0.2549 0.2885 0.3373 -0.0376 0.0331  -0.0244 25  GLU   A CD  
687  O  OE1 A GLU   A 25  ? 0.2938 0.3412 0.3645 -0.0220 0.0028  -0.0440 25  GLU   A OE1 
688  O  OE1 B GLU   A 25  ? 0.2628 0.2971 0.3608 -0.0358 0.0269  -0.0236 25  GLU   A OE1 
689  O  OE2 A GLU   A 25  ? 0.2917 0.3373 0.3837 -0.0261 0.0141  -0.0404 25  GLU   A OE2 
690  O  OE2 B GLU   A 25  ? 0.2593 0.2929 0.3525 -0.0401 0.0265  -0.0214 25  GLU   A OE2 
703  N  N   A GLU   A 26  ? 0.2030 0.2534 0.2191 -0.0659 0.0726  -0.0295 26  GLU   A N   
704  N  N   B GLU   A 26  ? 0.2065 0.2628 0.2023 -0.0380 0.0738  -0.0323 26  GLU   A N   
705  C  CA  A GLU   A 26  ? 0.2104 0.2503 0.1916 -0.0743 0.0745  -0.0234 26  GLU   A CA  
706  C  CA  B GLU   A 26  ? 0.2133 0.2684 0.1961 -0.0388 0.0691  -0.0227 26  GLU   A CA  
707  C  C   A GLU   A 26  ? 0.2100 0.2374 0.1695 -0.0738 0.0642  -0.0172 26  GLU   A C   
708  C  C   B GLU   A 26  ? 0.2115 0.2575 0.1806 -0.0324 0.0646  -0.0115 26  GLU   A C   
709  O  O   A GLU   A 26  ? 0.2187 0.2376 0.1612 -0.0732 0.0627  -0.0118 26  GLU   A O   
710  O  O   B GLU   A 26  ? 0.2154 0.2564 0.1782 -0.0346 0.0705  -0.0064 26  GLU   A O   
711  C  CB  A GLU   A 26  ? 0.2280 0.2525 0.2151 -0.0812 0.0727  -0.0170 26  GLU   A CB  
712  C  CB  B GLU   A 26  ? 0.2267 0.2837 0.2128 -0.0445 0.0549  -0.0210 26  GLU   A CB  
713  C  CG  A GLU   A 26  ? 0.2466 0.2587 0.2689 -0.0841 0.0704  -0.0215 26  GLU   A CG  
714  C  CG  B GLU   A 26  ? 0.2381 0.2964 0.2293 -0.0511 0.0521  -0.0195 26  GLU   A CG  
715  C  CD  A GLU   A 26  ? 0.2567 0.2575 0.2942 -0.0911 0.0832  -0.0293 26  GLU   A CD  
716  C  CD  B GLU   A 26  ? 0.2444 0.3045 0.2302 -0.0616 0.0538  -0.0188 26  GLU   A CD  
717  O  OE1 A GLU   A 26  ? 0.2534 0.2683 0.2916 -0.0805 0.1047  -0.0736 26  GLU   A OE1 
718  O  OE1 B GLU   A 26  ? 0.2486 0.3169 0.2257 -0.0577 0.0587  -0.0279 26  GLU   A OE1 
719  O  OE2 A GLU   A 26  ? 0.2683 0.2581 0.3112 -0.0930 0.0801  -0.0144 26  GLU   A OE2 
720  O  OE2 B GLU   A 26  ? 0.2432 0.3019 0.2146 -0.0698 0.0568  -0.0192 26  GLU   A OE2 
733  N  N   A ALA   A 27  ? 0.1969 0.2216 0.1593 -0.0770 0.0630  -0.0181 27  ALA   A N   
734  N  N   B ALA   A 27  ? 0.2046 0.2486 0.1693 -0.0233 0.0556  -0.0008 27  ALA   A N   
735  C  CA  A ALA   A 27  ? 0.2045 0.2229 0.1437 -0.0685 0.0608  -0.0174 27  ALA   A CA  
736  C  CA  B ALA   A 27  ? 0.2095 0.2484 0.1550 -0.0133 0.0428  0.0092  27  ALA   A CA  
737  C  C   A ALA   A 27  ? 0.2265 0.2367 0.1602 -0.0721 0.0633  -0.0281 27  ALA   A C   
738  C  C   B ALA   A 27  ? 0.2236 0.2599 0.1687 -0.0071 0.0382  -0.0003 27  ALA   A C   
739  O  O   A ALA   A 27  ? 0.2341 0.2329 0.1620 -0.0802 0.0537  -0.0232 27  ALA   A O   
740  O  O   B ALA   A 27  ? 0.2223 0.2553 0.1664 -0.0041 0.0310  -0.0001 27  ALA   A O   
741  C  CB  A ALA   A 27  ? 0.1967 0.2160 0.1417 -0.0638 0.0414  -0.0160 27  ALA   A CB  
742  C  CB  B ALA   A 27  ? 0.2040 0.2408 0.1423 -0.0147 0.0341  0.0190  27  ALA   A CB  
753  N  N   A LYS   A 28  ? 0.2524 0.2599 0.1779 -0.0622 0.0641  -0.0502 28  LYS   A N   
754  N  N   B LYS   A 28  ? 0.2438 0.2764 0.1902 -0.0018 0.0412  -0.0152 28  LYS   A N   
755  C  CA  A LYS   A 28  ? 0.2845 0.2936 0.2169 -0.0492 0.0637  -0.0604 28  LYS   A CA  
756  C  CA  B LYS   A 28  ? 0.2688 0.2989 0.2210 0.0049  0.0414  -0.0312 28  LYS   A CA  
757  C  C   A LYS   A 28  ? 0.3071 0.3251 0.2137 -0.0501 0.0790  -0.0496 28  LYS   A C   
758  C  C   B LYS   A 28  ? 0.2963 0.3255 0.2277 -0.0027 0.0491  -0.0280 28  LYS   A C   
759  O  O   A LYS   A 28  ? 0.3134 0.3304 0.2432 -0.0481 0.0619  -0.0502 28  LYS   A O   
760  O  O   B LYS   A 28  ? 0.3034 0.3303 0.2413 0.0034  0.0377  -0.0311 28  LYS   A O   
761  C  CB  A LYS   A 28  ? 0.2949 0.3004 0.2533 -0.0343 0.0555  -0.0698 28  LYS   A CB  
762  C  CB  B LYS   A 28  ? 0.2693 0.2992 0.2432 0.0149  0.0336  -0.0428 28  LYS   A CB  
763  C  CG  A LYS   A 28  ? 0.3055 0.3076 0.2863 -0.0245 0.0522  -0.0694 28  LYS   A CG  
764  C  CG  B LYS   A 28  ? 0.2724 0.3025 0.2621 0.0194  0.0279  -0.0432 28  LYS   A CG  
765  C  CD  A LYS   A 28  ? 0.3156 0.3197 0.3282 -0.0183 0.0496  -0.0565 28  LYS   A CD  
766  C  CD  B LYS   A 28  ? 0.2791 0.3107 0.2904 0.0221  0.0248  -0.0378 28  LYS   A CD  
767  C  CE  A LYS   A 28  ? 0.3246 0.3297 0.3578 -0.0155 0.0531  -0.0516 28  LYS   A CE  
768  C  CE  B LYS   A 28  ? 0.2867 0.3191 0.3131 0.0233  0.0234  -0.0353 28  LYS   A CE  
769  N  NZ  A LYS   A 28  ? 0.3311 0.3349 0.3719 -0.0131 0.0609  -0.0569 28  LYS   A NZ  
770  N  NZ  B LYS   A 28  ? 0.2926 0.3246 0.3224 0.0251  0.0225  -0.0369 28  LYS   A NZ  
797  N  N   A LYS   A 29  ? 0.3204 0.3506 0.2094 -0.0560 0.1113  -0.0291 29  LYS   A N   
798  N  N   B LYS   A 29  ? 0.3146 0.3474 0.2396 -0.0199 0.0708  -0.0155 29  LYS   A N   
799  C  CA  A LYS   A 29  ? 0.3405 0.3780 0.2359 -0.0587 0.1241  -0.0135 29  LYS   A CA  
800  C  CA  B LYS   A 29  ? 0.3358 0.3701 0.2661 -0.0359 0.0851  -0.0066 29  LYS   A CA  
801  C  C   A LYS   A 29  ? 0.3428 0.3794 0.2136 -0.0666 0.1115  -0.0045 29  LYS   A C   
802  C  C   B LYS   A 29  ? 0.3387 0.3729 0.2322 -0.0562 0.0907  -0.0009 29  LYS   A C   
803  O  O   A LYS   A 29  ? 0.3529 0.3915 0.2165 -0.0617 0.1104  -0.0048 29  LYS   A O   
804  O  O   B LYS   A 29  ? 0.3459 0.3807 0.2373 -0.0538 0.0888  0.0012  29  LYS   A O   
805  C  CB  A LYS   A 29  ? 0.3580 0.4037 0.2986 -0.0519 0.1357  -0.0086 29  LYS   A CB  
806  C  CB  B LYS   A 29  ? 0.3530 0.3894 0.3217 -0.0303 0.0884  -0.0036 29  LYS   A CB  
807  C  CG  A LYS   A 29  ? 0.3766 0.4274 0.3692 -0.0457 0.1368  -0.0039 29  LYS   A CG  
808  C  CG  B LYS   A 29  ? 0.3698 0.4070 0.3816 -0.0245 0.0879  -0.0000 29  LYS   A CG  
809  C  CD  A LYS   A 29  ? 0.3926 0.4482 0.4329 -0.0414 0.1349  -0.0041 29  LYS   A CD  
810  C  CD  B LYS   A 29  ? 0.3833 0.4222 0.4333 -0.0195 0.0872  0.0006  29  LYS   A CD  
811  C  CE  A LYS   A 29  ? 0.4035 0.4633 0.4722 -0.0389 0.1358  -0.0074 29  LYS   A CE  
812  C  CE  B LYS   A 29  ? 0.3922 0.4330 0.4660 -0.0160 0.0880  -0.0016 29  LYS   A CE  
813  N  NZ  A LYS   A 29  ? 0.4083 0.4712 0.5017 -0.0373 0.1338  -0.0101 29  LYS   A NZ  
814  N  NZ  B LYS   A 29  ? 0.3962 0.4386 0.4891 -0.0139 0.0865  -0.0027 29  LYS   A NZ  
841  N  N   . VAL   A 30  ? 0.3322 0.3656 0.1997 -0.0766 0.0971  0.0003  30  VAL   A N   
842  C  CA  . VAL   A 30  ? 0.3260 0.3466 0.1767 -0.0983 0.0675  0.0153  30  VAL   A CA  
843  C  C   . VAL   A 30  ? 0.3302 0.3324 0.1401 -0.1012 0.0516  0.0186  30  VAL   A C   
844  O  O   . VAL   A 30  ? 0.3407 0.3364 0.1411 -0.1013 0.0432  0.0236  30  VAL   A O   
845  C  CB  . VAL   A 30  ? 0.3206 0.3395 0.2099 -0.1140 0.0370  0.0226  30  VAL   A CB  
846  C  CG1 . VAL   A 30  ? 0.3206 0.3350 0.2184 -0.1125 0.0185  0.0328  30  VAL   A CG1 
847  C  CG2 . VAL   A 30  ? 0.3203 0.3428 0.2367 -0.1252 0.0318  0.0225  30  VAL   A CG2 
858  N  N   . LYS   A 31  ? 0.3218 0.3135 0.1246 -0.1024 0.0358  0.0146  31  LYS   A N   
859  C  CA  . LYS   A 31  ? 0.3317 0.3086 0.1391 -0.0919 0.0098  0.0110  31  LYS   A CA  
860  C  C   . LYS   A 31  ? 0.3055 0.2853 0.1100 -0.0768 -0.0012 0.0490  31  LYS   A C   
861  O  O   . LYS   A 31  ? 0.3140 0.2994 0.1317 -0.0757 -0.0217 0.0612  31  LYS   A O   
862  C  CB  . LYS   A 31  ? 0.3781 0.3347 0.2380 -0.0900 -0.0131 -0.0166 31  LYS   A CB  
863  C  CG  . LYS   A 31  ? 0.4287 0.3629 0.3877 -0.0792 -0.0340 -0.0279 31  LYS   A CG  
864  C  CD  . LYS   A 31  ? 0.4700 0.3858 0.4863 -0.0711 -0.0508 -0.0388 31  LYS   A CD  
865  C  CE  . LYS   A 31  ? 0.4970 0.4033 0.5613 -0.0647 -0.0652 -0.0530 31  LYS   A CE  
866  N  NZ  . LYS   A 31  ? 0.5099 0.4120 0.6046 -0.0604 -0.0758 -0.0651 31  LYS   A NZ  
880  N  N   . PRO   A 32  ? 0.2669 0.2502 0.0995 -0.0660 0.0024  0.0342  32  PRO   A N   
881  C  CA  . PRO   A 32  ? 0.2545 0.2318 0.1332 -0.0608 -0.0065 0.0456  32  PRO   A CA  
882  C  C   . PRO   A 32  ? 0.2479 0.2273 0.1400 -0.0515 -0.0172 0.0502  32  PRO   A C   
883  O  O   . PRO   A 32  ? 0.2386 0.2205 0.1536 -0.0519 -0.0303 0.0575  32  PRO   A O   
884  C  CB  . PRO   A 32  ? 0.2469 0.2355 0.1466 -0.0581 -0.0067 0.0376  32  PRO   A CB  
885  C  CG  . PRO   A 32  ? 0.2407 0.2386 0.0931 -0.0540 -0.0118 0.0266  32  PRO   A CG  
886  C  CD  . PRO   A 32  ? 0.2494 0.2420 0.0874 -0.0584 -0.0011 0.0337  32  PRO   A CD  
894  N  N   . THR   A 33  ? 0.2548 0.2261 0.1327 -0.0449 -0.0098 0.0514  33  THR   A N   
895  C  CA  . THR   A 33  ? 0.2531 0.2244 0.1395 -0.0348 -0.0211 0.0510  33  THR   A CA  
896  C  C   . THR   A 33  ? 0.2243 0.2070 0.1260 -0.0328 -0.0199 0.0405  33  THR   A C   
897  O  O   . THR   A 33  ? 0.2168 0.2041 0.1369 -0.0339 -0.0312 0.0381  33  THR   A O   
898  C  CB  . THR   A 33  ? 0.2833 0.2433 0.1608 -0.0238 -0.0372 0.0730  33  THR   A CB  
899  O  OG1 . THR   A 33  ? 0.3055 0.2536 0.1873 -0.0113 -0.0255 0.0826  33  THR   A OG1 
900  C  CG2 . THR   A 33  ? 0.2893 0.2512 0.1787 -0.0237 -0.0549 0.0748  33  THR   A CG2 
908  N  N   . VAL   A 34  ? 0.1990 0.1899 0.1192 -0.0349 -0.0167 0.0353  34  VAL   A N   
909  C  CA  . VAL   A 34  ? 0.1776 0.1693 0.1099 -0.0297 -0.0102 0.0340  34  VAL   A CA  
910  C  C   . VAL   A 34  ? 0.1638 0.1641 0.1035 -0.0264 -0.0014 0.0291  34  VAL   A C   
911  O  O   . VAL   A 34  ? 0.1668 0.1685 0.1337 -0.0340 0.0012  0.0357  34  VAL   A O   
912  C  CB  . VAL   A 34  ? 0.1826 0.1666 0.1387 -0.0238 -0.0055 0.0251  34  VAL   A CB  
913  C  CG1 . VAL   A 34  ? 0.1867 0.1669 0.1339 -0.0196 0.0073  0.0122  34  VAL   A CG1 
914  C  CG2 . VAL   A 34  ? 0.1822 0.1766 0.1705 -0.0132 -0.0178 0.0251  34  VAL   A CG2 
924  N  N   . VAL   A 35  ? 0.1521 0.1495 0.1036 -0.0277 -0.0050 0.0195  35  VAL   A N   
925  C  CA  . VAL   A 35  ? 0.1448 0.1460 0.1003 -0.0240 -0.0013 0.0147  35  VAL   A CA  
926  C  C   . VAL   A 35  ? 0.1316 0.1352 0.1018 -0.0157 0.0009  0.0168  35  VAL   A C   
927  O  O   . VAL   A 35  ? 0.1231 0.1453 0.1295 -0.0239 0.0085  0.0100  35  VAL   A O   
928  C  CB  . VAL   A 35  ? 0.1510 0.1553 0.1101 -0.0165 0.0100  0.0016  35  VAL   A CB  
929  C  CG1 . VAL   A 35  ? 0.1586 0.1581 0.1333 -0.0107 0.0031  -0.0004 35  VAL   A CG1 
930  C  CG2 . VAL   A 35  ? 0.1441 0.1552 0.1342 -0.0133 0.0142  0.0007  35  VAL   A CG2 
940  N  N   . VAL   A 36  ? 0.1183 0.1329 0.1046 -0.0173 0.0030  0.0207  36  VAL   A N   
941  C  CA  . VAL   A 36  ? 0.1184 0.1234 0.1041 -0.0097 0.0043  0.0111  36  VAL   A CA  
942  C  C   . VAL   A 36  ? 0.1154 0.1228 0.1055 -0.0146 0.0090  0.0127  36  VAL   A C   
943  O  O   . VAL   A 36  ? 0.1205 0.1226 0.1346 -0.0050 0.0131  0.0129  36  VAL   A O   
944  C  CB  . VAL   A 36  ? 0.1199 0.1153 0.1114 -0.0092 0.0048  0.0136  36  VAL   A CB  
945  C  CG1 . VAL   A 36  ? 0.1252 0.1174 0.1367 -0.0139 0.0045  0.0031  36  VAL   A CG1 
946  C  CG2 . VAL   A 36  ? 0.1302 0.1159 0.1388 -0.0061 0.0019  0.0181  36  VAL   A CG2 
956  N  N   A ASN   A 37  ? 0.1157 0.1189 0.1036 -0.0058 0.0108  0.0150  37  ASN   A N   
957  N  N   B ASN   A 37  ? 0.1099 0.1142 0.1034 -0.0031 0.0065  0.0120  37  ASN   A N   
958  C  CA  A ASN   A 37  ? 0.1171 0.1179 0.1047 -0.0003 0.0127  0.0228  37  ASN   A CA  
959  C  CA  B ASN   A 37  ? 0.1062 0.1090 0.1080 0.0053  0.0017  0.0148  37  ASN   A CA  
960  C  C   A ASN   A 37  ? 0.1174 0.1197 0.1039 -0.0031 0.0170  0.0357  37  ASN   A C   
961  C  C   B ASN   A 37  ? 0.1070 0.1049 0.1154 0.0093  0.0100  0.0094  37  ASN   A C   
962  O  O   A ASN   A 37  ? 0.1268 0.1297 0.1067 0.0025  0.0047  0.0222  37  ASN   A O   
963  O  O   B ASN   A 37  ? 0.1094 0.1079 0.1080 0.0100  0.0156  -0.0051 37  ASN   A O   
964  C  CB  A ASN   A 37  ? 0.1184 0.1144 0.1160 0.0025  0.0109  0.0141  37  ASN   A CB  
965  C  CB  B ASN   A 37  ? 0.1042 0.1083 0.1225 0.0061  -0.0001 0.0144  37  ASN   A CB  
966  C  CG  A ASN   A 37  ? 0.1187 0.1133 0.1042 -0.0001 0.0044  0.0059  37  ASN   A CG  
967  C  CG  B ASN   A 37  ? 0.1045 0.1104 0.1266 -0.0031 0.0016  0.0041  37  ASN   A CG  
968  O  OD1 A ASN   A 37  ? 0.1201 0.1123 0.1033 0.0007  0.0089  0.0074  37  ASN   A OD1 
969  O  OD1 B ASN   A 37  ? 0.1083 0.1164 0.1172 -0.0081 0.0043  0.0126  37  ASN   A OD1 
970  N  ND2 A ASN   A 37  ? 0.1185 0.1093 0.1022 -0.0021 -0.0007 0.0228  37  ASN   A ND2 
971  N  ND2 B ASN   A 37  ? 0.1030 0.1037 0.1262 -0.0038 0.0025  -0.0020 37  ASN   A ND2 
984  N  N   A ALA   A 38  ? 0.1098 0.1227 0.1137 -0.0059 0.0147  0.0179  38  ALA   A N   
985  N  N   B ALA   A 38  ? 0.1113 0.1081 0.1249 0.0108  0.0052  -0.0010 38  ALA   A N   
986  C  CA  A ALA   A 38  ? 0.1135 0.1143 0.1079 -0.0047 0.0076  0.0072  38  ALA   A CA  
987  C  CA  B ALA   A 38  ? 0.1228 0.1179 0.1336 0.0070  0.0005  0.0039  38  ALA   A CA  
988  C  C   A ALA   A 38  ? 0.1135 0.1140 0.1053 -0.0045 -0.0044 0.0043  38  ALA   A C   
989  C  C   B ALA   A 38  ? 0.1256 0.1238 0.1328 0.0082  -0.0061 0.0048  38  ALA   A C   
990  O  O   A ALA   A 38  ? 0.1217 0.1087 0.1043 -0.0041 -0.0040 0.0016  38  ALA   A O   
991  O  O   B ALA   A 38  ? 0.1235 0.1233 0.1402 0.0061  -0.0147 0.0171  38  ALA   A O   
992  C  CB  A ALA   A 38  ? 0.1120 0.1239 0.1226 -0.0099 0.0007  -0.0058 38  ALA   A CB  
993  C  CB  B ALA   A 38  ? 0.1280 0.1241 0.1449 -0.0002 -0.0115 -0.0058 38  ALA   A CB  
1004 N  N   A ALA   A 39  ? 0.1112 0.1128 0.1139 -0.0033 0.0034  0.0069  39  ALA   A N   
1005 N  N   B ALA   A 39  ? 0.1317 0.1305 0.1339 0.0059  0.0025  0.0159  39  ALA   A N   
1006 C  CA  A ALA   A 39  ? 0.1106 0.1112 0.1120 0.0002  0.0061  0.0025  39  ALA   A CA  
1007 C  CA  B ALA   A 39  ? 0.1364 0.1345 0.1280 0.0027  0.0029  0.0138  39  ALA   A CA  
1008 C  C   A ALA   A 39  ? 0.1161 0.1065 0.1096 0.0027  0.0054  0.0021  39  ALA   A C   
1009 C  C   B ALA   A 39  ? 0.1327 0.1259 0.1210 -0.0002 0.0050  0.0135  39  ALA   A C   
1010 O  O   A ALA   A 39  ? 0.1322 0.1134 0.1173 -0.0020 0.0049  0.0022  39  ALA   A O   
1011 O  O   B ALA   A 39  ? 0.1375 0.1300 0.1233 -0.0064 0.0114  0.0087  39  ALA   A O   
1012 C  CB  A ALA   A 39  ? 0.1091 0.1121 0.1210 -0.0027 0.0021  0.0007  39  ALA   A CB  
1013 C  CB  B ALA   A 39  ? 0.1448 0.1407 0.1411 0.0050  -0.0030 0.0123  39  ALA   A CB  
1024 N  N   A ASN   A 40  ? 0.1232 0.1140 0.1083 -0.0079 0.0141  0.0042  40  ASN   A N   
1025 N  N   B ASN   A 40  ? 0.1368 0.1248 0.1230 -0.0056 0.0126  0.0137  40  ASN   A N   
1026 C  CA  A ASN   A 40  ? 0.1373 0.1120 0.1136 -0.0040 0.0080  0.0019  40  ASN   A CA  
1027 C  CA  B ASN   A 40  ? 0.1418 0.1235 0.1333 -0.0035 0.0106  0.0091  40  ASN   A CA  
1028 C  C   A ASN   A 40  ? 0.1430 0.1075 0.1127 -0.0030 0.0251  0.0126  40  ASN   A C   
1029 C  C   B ASN   A 40  ? 0.1439 0.1159 0.1184 -0.0030 0.0254  0.0169  40  ASN   A C   
1030 O  O   A ASN   A 40  ? 0.1386 0.1092 0.1187 -0.0061 0.0200  0.0136  40  ASN   A O   
1031 O  O   B ASN   A 40  ? 0.1378 0.1169 0.1142 -0.0037 0.0259  0.0214  40  ASN   A O   
1032 C  CB  A ASN   A 40  ? 0.1473 0.1212 0.1153 0.0018  -0.0044 0.0049  40  ASN   A CB  
1033 C  CB  B ASN   A 40  ? 0.1451 0.1309 0.1446 -0.0003 0.0048  0.0024  40  ASN   A CB  
1034 C  CG  A ASN   A 40  ? 0.1594 0.1202 0.1471 0.0033  -0.0137 0.0111  40  ASN   A CG  
1035 C  CG  B ASN   A 40  ? 0.1492 0.1329 0.1687 -0.0008 0.0047  -0.0028 40  ASN   A CG  
1036 O  OD1 A ASN   A 40  ? 0.1695 0.1192 0.1825 0.0020  -0.0140 0.0140  40  ASN   A OD1 
1037 O  OD1 B ASN   A 40  ? 0.1535 0.1332 0.1890 0.0026  0.0113  -0.0073 40  ASN   A OD1 
1038 N  ND2 A ASN   A 40  ? 0.1579 0.1237 0.1588 0.0028  0.0009  0.0073  40  ASN   A ND2 
1039 N  ND2 B ASN   A 40  ? 0.1468 0.1363 0.1820 -0.0071 0.0135  -0.0107 40  ASN   A ND2 
1052 N  N   . VAL   A 41  ? 0.1513 0.1157 0.1179 -0.0056 0.0260  0.0131  41  VAL   A N   
1053 C  CA  . VAL   A 41  ? 0.1592 0.1214 0.1392 -0.0036 0.0312  0.0091  41  VAL   A CA  
1054 C  C   . VAL   A 41  ? 0.1508 0.1196 0.1349 -0.0046 0.0262  0.0108  41  VAL   A C   
1055 O  O   . VAL   A 41  ? 0.1505 0.1140 0.1577 0.0019  0.0262  0.0056  41  VAL   A O   
1056 C  CB  . VAL   A 41  ? 0.1744 0.1338 0.1479 -0.0082 0.0504  0.0042  41  VAL   A CB  
1057 C  CG1 . VAL   A 41  ? 0.1809 0.1352 0.1581 -0.0056 0.0496  0.0033  41  VAL   A CG1 
1058 C  CG2 . VAL   A 41  ? 0.1960 0.1432 0.1318 -0.0168 0.0491  0.0082  41  VAL   A CG2 
1069 N  N   . TYR   A 42  ? 0.1394 0.1152 0.1414 -0.0008 0.0318  0.0186  42  TYR   A N   
1070 C  CA  . TYR   A 42  ? 0.1418 0.1137 0.1518 -0.0073 0.0349  0.0193  42  TYR   A CA  
1071 C  C   . TYR   A 42  ? 0.1313 0.1155 0.1461 -0.0020 0.0222  0.0179  42  TYR   A C   
1072 O  O   . TYR   A 42  ? 0.1282 0.1180 0.1711 -0.0120 0.0221  0.0035  42  TYR   A O   
1073 C  CB  . TYR   A 42  ? 0.1624 0.1226 0.1462 -0.0051 0.0321  0.0211  42  TYR   A CB  
1074 C  CG  . TYR   A 42  ? 0.1811 0.1362 0.1476 -0.0083 0.0253  0.0270  42  TYR   A CG  
1075 C  CD1 . TYR   A 42  ? 0.1906 0.1471 0.1506 -0.0151 0.0279  0.0316  42  TYR   A CD1 
1076 C  CD2 . TYR   A 42  ? 0.1942 0.1538 0.1627 -0.0041 0.0185  0.0170  42  TYR   A CD2 
1077 C  CE1 . TYR   A 42  ? 0.2056 0.1568 0.1456 -0.0208 0.0294  0.0216  42  TYR   A CE1 
1078 C  CE2 . TYR   A 42  ? 0.2128 0.1709 0.1810 -0.0182 0.0165  0.0187  42  TYR   A CE2 
1079 C  CZ  . TYR   A 42  ? 0.2232 0.1705 0.1565 -0.0270 0.0341  0.0142  42  TYR   A CZ  
1080 O  OH  . TYR   A 42  ? 0.2400 0.1935 0.1806 -0.0395 0.0350  0.0052  42  TYR   A OH  
1090 N  N   A LEU   A 43  ? 0.1253 0.1118 0.1400 -0.0062 0.0170  0.0042  43  LEU   A N   
1091 N  N   B LEU   A 43  ? 0.1295 0.1183 0.1398 -0.0044 0.0111  0.0135  43  LEU   A N   
1092 C  CA  A LEU   A 43  ? 0.1139 0.1082 0.1393 -0.0045 0.0165  0.0021  43  LEU   A CA  
1093 C  CA  B LEU   A 43  ? 0.1241 0.1198 0.1366 -0.0034 0.0028  0.0148  43  LEU   A CA  
1094 C  C   A LEU   A 43  ? 0.1128 0.1103 0.1342 -0.0020 0.0145  0.0003  43  LEU   A C   
1095 C  C   B LEU   A 43  ? 0.1314 0.1256 0.1345 -0.0001 -0.0026 0.0108  43  LEU   A C   
1096 O  O   A LEU   A 43  ? 0.1295 0.1141 0.1545 -0.0010 -0.0017 0.0039  43  LEU   A O   
1097 O  O   B LEU   A 43  ? 0.1448 0.1290 0.1339 0.0056  -0.0115 0.0111  43  LEU   A O   
1098 C  CB  A LEU   A 43  ? 0.1247 0.1092 0.1535 -0.0060 0.0124  0.0042  43  LEU   A CB  
1099 C  CB  B LEU   A 43  ? 0.1214 0.1157 0.1387 -0.0061 0.0025  0.0224  43  LEU   A CB  
1100 C  CG  A LEU   A 43  ? 0.1297 0.1134 0.1558 -0.0004 0.0090  -0.0024 43  LEU   A CG  
1101 C  CG  B LEU   A 43  ? 0.1210 0.1160 0.1413 -0.0047 0.0055  0.0232  43  LEU   A CG  
1102 C  CD1 A LEU   A 43  ? 0.1317 0.1222 0.1700 -0.0001 0.0020  0.0032  43  LEU   A CD1 
1103 C  CD1 B LEU   A 43  ? 0.1232 0.1224 0.1543 -0.0055 -0.0036 0.0221  43  LEU   A CD1 
1104 C  CD2 A LEU   A 43  ? 0.1393 0.1161 0.1544 -0.0021 0.0094  -0.0009 43  LEU   A CD2 
1105 C  CD2 B LEU   A 43  ? 0.1300 0.1134 0.1464 -0.0070 0.0043  0.0364  43  LEU   A CD2 
1128 N  N   A LYS   A 44  ? 0.1219 0.1101 0.1355 -0.0033 0.0154  0.0078  44  LYS   A N   
1129 N  N   B LYS   A 44  ? 0.1359 0.1277 0.1411 -0.0014 -0.0072 0.0111  44  LYS   A N   
1130 C  CA  A LYS   A 44  ? 0.1278 0.1117 0.1461 -0.0053 0.0257  0.0179  44  LYS   A CA  
1131 C  CA  B LYS   A 44  ? 0.1457 0.1347 0.1523 0.0014  -0.0092 0.0130  44  LYS   A CA  
1132 C  C   A LYS   A 44  ? 0.1155 0.1110 0.1223 0.0009  0.0068  0.0085  44  LYS   A C   
1133 C  C   B LYS   A 44  ? 0.1411 0.1322 0.1315 0.0005  -0.0163 0.0095  44  LYS   A C   
1134 O  O   A LYS   A 44  ? 0.1219 0.1305 0.1388 0.0025  0.0041  -0.0027 44  LYS   A O   
1135 O  O   B LYS   A 44  ? 0.1467 0.1401 0.1309 -0.0058 -0.0086 0.0013  44  LYS   A O   
1136 C  CB  A LYS   A 44  ? 0.1559 0.1236 0.1779 -0.0063 0.0334  0.0341  44  LYS   A CB  
1137 C  CB  B LYS   A 44  ? 0.1694 0.1516 0.1921 0.0098  0.0015  0.0156  44  LYS   A CB  
1138 C  CG  A LYS   A 44  ? 0.1885 0.1415 0.2406 -0.0125 0.0528  0.0483  44  LYS   A CG  
1139 C  CG  B LYS   A 44  ? 0.1926 0.1755 0.2517 0.0154  0.0109  0.0209  44  LYS   A CG  
1140 C  CD  A LYS   A 44  ? 0.2276 0.1839 0.3468 -0.0162 0.0515  0.0413  44  LYS   A CD  
1141 C  CD  B LYS   A 44  ? 0.2204 0.2056 0.3262 0.0130  0.0079  0.0203  44  LYS   A CD  
1142 C  CE  A LYS   A 44  ? 0.2495 0.2181 0.4161 -0.0145 0.0511  0.0356  44  LYS   A CE  
1143 C  CE  B LYS   A 44  ? 0.2331 0.2200 0.3730 0.0083  0.0056  0.0193  44  LYS   A CE  
1144 N  NZ  A LYS   A 44  ? 0.2598 0.2384 0.4475 -0.0161 0.0468  0.0364  44  LYS   A NZ  
1145 N  NZ  B LYS   A 44  ? 0.2378 0.2221 0.3896 0.0028  0.0013  0.0185  44  LYS   A NZ  
1172 N  N   A HIS   A 45  ? 0.1050 0.1072 0.1160 0.0015  0.0087  0.0119  45  HIS   A N   
1173 N  N   B HIS   A 45  ? 0.1396 0.1291 0.1366 -0.0006 -0.0177 0.0134  45  HIS   A N   
1174 C  CA  A HIS   A 45  ? 0.1030 0.1106 0.1208 0.0042  0.0033  0.0089  45  HIS   A CA  
1175 C  CA  B HIS   A 45  ? 0.1385 0.1315 0.1444 0.0002  -0.0166 0.0096  45  HIS   A CA  
1176 C  C   A HIS   A 45  ? 0.1125 0.1227 0.1310 0.0047  0.0077  0.0175  45  HIS   A C   
1177 C  C   B HIS   A 45  ? 0.1407 0.1363 0.1488 -0.0038 -0.0110 0.0165  45  HIS   A C   
1178 O  O   A HIS   A 45  ? 0.1189 0.1196 0.1506 0.0034  0.0105  -0.0023 45  HIS   A O   
1179 O  O   B HIS   A 45  ? 0.1459 0.1406 0.1685 0.0034  -0.0118 0.0162  45  HIS   A O   
1180 C  CB  A HIS   A 45  ? 0.1027 0.1060 0.1155 -0.0028 0.0100  0.0019  45  HIS   A CB  
1181 C  CB  B HIS   A 45  ? 0.1379 0.1294 0.1426 0.0036  -0.0131 -0.0011 45  HIS   A CB  
1182 C  CG  A HIS   A 45  ? 0.1027 0.1060 0.1058 -0.0084 0.0086  0.0086  45  HIS   A CG  
1183 C  CG  B HIS   A 45  ? 0.1307 0.1259 0.1252 0.0063  -0.0025 -0.0015 45  HIS   A CG  
1184 N  ND1 A HIS   A 45  ? 0.1030 0.1132 0.1191 -0.0087 0.0000  0.0115  45  HIS   A ND1 
1185 N  ND1 B HIS   A 45  ? 0.1282 0.1271 0.1385 0.0081  -0.0031 0.0046  45  HIS   A ND1 
1186 C  CD2 A HIS   A 45  ? 0.1059 0.1115 0.1288 -0.0193 0.0006  0.0139  45  HIS   A CD2 
1187 C  CD2 B HIS   A 45  ? 0.1254 0.1194 0.1140 0.0059  -0.0059 -0.0059 45  HIS   A CD2 
1188 C  CE1 A HIS   A 45  ? 0.1085 0.1194 0.1166 -0.0100 0.0027  0.0241  45  HIS   A CE1 
1189 C  CE1 B HIS   A 45  ? 0.1263 0.1191 0.1094 0.0056  0.0005  -0.0059 45  HIS   A CE1 
1190 N  NE2 A HIS   A 45  ? 0.1103 0.1212 0.1304 -0.0091 -0.0011 0.0289  45  HIS   A NE2 
1191 N  NE2 B HIS   A 45  ? 0.1240 0.1184 0.0977 0.0041  -0.0055 -0.0115 45  HIS   A NE2 
1206 N  N   A GLY   A 46  ? 0.1185 0.1380 0.1446 0.0135  -0.0013 0.0276  46  GLY   A N   
1207 N  N   B GLY   A 46  ? 0.1372 0.1339 0.1450 -0.0111 -0.0080 0.0163  46  GLY   A N   
1208 C  CA  A GLY   A 46  ? 0.1234 0.1402 0.1663 0.0127  -0.0026 0.0356  46  GLY   A CA  
1209 C  CA  B GLY   A 46  ? 0.1330 0.1381 0.1464 -0.0057 -0.0047 0.0165  46  GLY   A CA  
1210 C  C   A GLY   A 46  ? 0.1289 0.1352 0.1568 0.0191  -0.0135 0.0496  46  GLY   A C   
1211 C  C   B GLY   A 46  ? 0.1343 0.1372 0.1342 0.0033  0.0056  0.0234  46  GLY   A C   
1212 O  O   A GLY   A 46  ? 0.1401 0.1351 0.1654 0.0224  -0.0200 0.0492  46  GLY   A O   
1213 O  O   B GLY   A 46  ? 0.1424 0.1414 0.1397 0.0017  0.0091  0.0184  46  GLY   A O   
1220 N  N   A GLY   A 47  ? 0.1254 0.1330 0.1561 0.0171  -0.0061 0.0362  47  GLY   A N   
1221 N  N   B GLY   A 47  ? 0.1309 0.1391 0.1358 0.0088  0.0124  0.0106  47  GLY   A N   
1222 C  CA  A GLY   A 47  ? 0.1261 0.1376 0.1493 0.0221  -0.0122 0.0292  47  GLY   A CA  
1223 C  CA  B GLY   A 47  ? 0.1279 0.1449 0.1365 0.0096  -0.0032 0.0117  47  GLY   A CA  
1224 C  C   A GLY   A 47  ? 0.1259 0.1302 0.1265 0.0172  -0.0124 0.0164  47  GLY   A C   
1225 C  C   B GLY   A 47  ? 0.1238 0.1370 0.1168 0.0131  -0.0070 0.0055  47  GLY   A C   
1226 O  O   A GLY   A 47  ? 0.1294 0.1263 0.1456 0.0155  -0.0136 0.0180  47  GLY   A O   
1227 O  O   B GLY   A 47  ? 0.1227 0.1331 0.1155 0.0118  -0.0061 0.0122  47  GLY   A O   
1234 N  N   A GLY   A 48  ? 0.1240 0.1320 0.1233 0.0162  -0.0119 0.0064  48  GLY   A N   
1235 N  N   B GLY   A 48  ? 0.1243 0.1389 0.1155 0.0116  -0.0020 0.0038  48  GLY   A N   
1236 C  CA  A GLY   A 48  ? 0.1212 0.1258 0.1426 0.0066  -0.0051 -0.0069 48  GLY   A CA  
1237 C  CA  B GLY   A 48  ? 0.1248 0.1308 0.1095 0.0030  -0.0075 0.0026  48  GLY   A CA  
1238 C  C   A GLY   A 48  ? 0.1253 0.1221 0.1343 0.0016  0.0073  -0.0012 48  GLY   A C   
1239 C  C   B GLY   A 48  ? 0.1257 0.1258 0.1071 -0.0044 -0.0052 0.0030  48  GLY   A C   
1240 O  O   A GLY   A 48  ? 0.1388 0.1220 0.1365 -0.0006 0.0108  0.0070  48  GLY   A O   
1241 O  O   B GLY   A 48  ? 0.1419 0.1290 0.1026 -0.0037 0.0028  0.0030  48  GLY   A O   
1248 N  N   A VAL   A 49  ? 0.1261 0.1189 0.1493 -0.0031 -0.0022 0.0010  49  VAL   A N   
1249 N  N   B VAL   A 49  ? 0.1162 0.1192 0.1254 -0.0055 -0.0100 -0.0012 49  VAL   A N   
1250 C  CA  A VAL   A 49  ? 0.1366 0.1148 0.1406 -0.0066 0.0058  0.0011  49  VAL   A CA  
1251 C  CA  B VAL   A 49  ? 0.1106 0.1180 0.1324 -0.0049 -0.0024 -0.0003 49  VAL   A CA  
1252 C  C   A VAL   A 49  ? 0.1323 0.1103 0.1262 -0.0064 0.0041  0.0128  49  VAL   A C   
1253 C  C   B VAL   A 49  ? 0.1101 0.1103 0.1115 -0.0009 0.0007  -0.0070 49  VAL   A C   
1254 O  O   A VAL   A 49  ? 0.1367 0.1217 0.1223 -0.0163 0.0020  0.0098  49  VAL   A O   
1255 O  O   B VAL   A 49  ? 0.1113 0.1145 0.1118 0.0009  0.0060  -0.0089 49  VAL   A O   
1256 C  CB  A VAL   A 49  ? 0.1518 0.1193 0.1718 -0.0081 0.0044  -0.0031 49  VAL   A CB  
1257 C  CB  B VAL   A 49  ? 0.1024 0.1155 0.1506 -0.0018 -0.0059 0.0034  49  VAL   A CB  
1258 C  CG1 A VAL   A 49  ? 0.1640 0.1146 0.1888 0.0006  0.0066  -0.0001 49  VAL   A CG1 
1259 C  CG1 B VAL   A 49  ? 0.0893 0.1106 0.1511 0.0062  -0.0071 0.0104  49  VAL   A CG1 
1260 C  CG2 A VAL   A 49  ? 0.1598 0.1302 0.2131 -0.0167 0.0059  -0.0061 49  VAL   A CG2 
1261 C  CG2 B VAL   A 49  ? 0.0999 0.1170 0.1627 -0.0027 -0.0028 0.0061  49  VAL   A CG2 
1280 N  N   A ALA   A 50  ? 0.1208 0.1101 0.1294 -0.0032 -0.0123 0.0201  50  ALA   A N   
1281 N  N   B ALA   A 50  ? 0.1093 0.1080 0.1030 0.0001  -0.0021 -0.0115 50  ALA   A N   
1282 C  CA  A ALA   A 50  ? 0.1165 0.1113 0.1304 -0.0057 -0.0081 0.0270  50  ALA   A CA  
1283 C  CA  B ALA   A 50  ? 0.1151 0.1080 0.1077 -0.0086 0.0007  -0.0107 50  ALA   A CA  
1284 C  C   A ALA   A 50  ? 0.1115 0.1134 0.1360 -0.0032 -0.0105 0.0175  50  ALA   A C   
1285 C  C   B ALA   A 50  ? 0.1135 0.1119 0.1010 -0.0112 -0.0002 -0.0082 50  ALA   A C   
1286 O  O   A ALA   A 50  ? 0.1114 0.1157 0.1466 0.0023  -0.0207 0.0134  50  ALA   A O   
1287 O  O   B ALA   A 50  ? 0.1120 0.1168 0.0930 -0.0127 0.0103  -0.0092 50  ALA   A O   
1288 C  CB  A ALA   A 50  ? 0.1199 0.1112 0.1279 -0.0036 -0.0081 0.0241  50  ALA   A CB  
1289 C  CB  B ALA   A 50  ? 0.1218 0.1026 0.1025 -0.0087 0.0072  -0.0226 50  ALA   A CB  
1300 N  N   A GLY   A 51  ? 0.1195 0.1073 0.1419 0.0073  -0.0079 0.0115  51  GLY   A N   
1301 N  N   B GLY   A 51  ? 0.1211 0.1090 0.1102 -0.0044 -0.0105 -0.0091 51  GLY   A N   
1302 C  CA  A GLY   A 51  ? 0.1207 0.1062 0.1351 0.0099  -0.0075 0.0088  51  GLY   A CA  
1303 C  CA  B GLY   A 51  ? 0.1292 0.1115 0.1114 0.0011  -0.0171 -0.0062 51  GLY   A CA  
1304 C  C   A GLY   A 51  ? 0.1110 0.1112 0.1212 0.0052  -0.0054 0.0066  51  GLY   A C   
1305 C  C   B GLY   A 51  ? 0.1274 0.1211 0.1262 0.0031  -0.0102 -0.0117 51  GLY   A C   
1306 O  O   A GLY   A 51  ? 0.1145 0.1211 0.1248 -0.0035 -0.0040 0.0048  51  GLY   A O   
1307 O  O   B GLY   A 51  ? 0.1307 0.1273 0.1219 0.0009  -0.0048 -0.0165 51  GLY   A O   
1314 N  N   A ALA   A 52  ? 0.1123 0.1186 0.1151 0.0030  -0.0067 -0.0020 52  ALA   A N   
1315 N  N   B ALA   A 52  ? 0.1298 0.1272 0.1317 0.0002  -0.0057 -0.0118 52  ALA   A N   
1316 C  CA  A ALA   A 52  ? 0.1145 0.1196 0.1308 -0.0046 -0.0016 0.0046  52  ALA   A CA  
1317 C  CA  B ALA   A 52  ? 0.1242 0.1222 0.1329 -0.0018 -0.0074 -0.0106 52  ALA   A CA  
1318 C  C   A ALA   A 52  ? 0.1126 0.1199 0.1134 -0.0104 0.0005  0.0053  52  ALA   A C   
1319 C  C   B ALA   A 52  ? 0.1172 0.1237 0.1232 -0.0060 -0.0049 -0.0110 52  ALA   A C   
1320 O  O   A ALA   A 52  ? 0.1223 0.1375 0.1289 -0.0069 -0.0017 -0.0028 52  ALA   A O   
1321 O  O   B ALA   A 52  ? 0.1243 0.1217 0.1332 -0.0058 0.0051  -0.0054 52  ALA   A O   
1322 C  CB  A ALA   A 52  ? 0.1227 0.1284 0.1458 -0.0049 -0.0025 0.0147  52  ALA   A CB  
1323 C  CB  B ALA   A 52  ? 0.1284 0.1283 0.1483 -0.0017 -0.0179 -0.0080 52  ALA   A CB  
1334 N  N   A LEU   A 53  ? 0.1108 0.1166 0.1163 -0.0055 0.0005  0.0067  53  LEU   A N   
1335 N  N   B LEU   A 53  ? 0.1103 0.1252 0.1141 -0.0002 -0.0100 -0.0172 53  LEU   A N   
1336 C  CA  A LEU   A 53  ? 0.1196 0.1284 0.1209 -0.0057 0.0064  0.0137  53  LEU   A CA  
1337 C  CA  B LEU   A 53  ? 0.1111 0.1307 0.1053 -0.0010 -0.0102 -0.0130 53  LEU   A CA  
1338 C  C   A LEU   A 53  ? 0.1237 0.1380 0.1066 0.0012  0.0052  0.0111  53  LEU   A C   
1339 C  C   B LEU   A 53  ? 0.1164 0.1376 0.0967 -0.0004 -0.0063 -0.0147 53  LEU   A C   
1340 O  O   A LEU   A 53  ? 0.1404 0.1450 0.1143 -0.0156 0.0056  0.0082  53  LEU   A O   
1341 O  O   B LEU   A 53  ? 0.1293 0.1422 0.1021 -0.0147 -0.0053 -0.0099 53  LEU   A O   
1342 C  CB  A LEU   A 53  ? 0.1213 0.1326 0.1382 -0.0079 0.0071  0.0170  53  LEU   A CB  
1343 C  CB  B LEU   A 53  ? 0.1078 0.1301 0.0985 -0.0021 -0.0169 -0.0107 53  LEU   A CB  
1344 C  CG  A LEU   A 53  ? 0.1253 0.1341 0.1458 -0.0046 0.0030  0.0128  53  LEU   A CG  
1345 C  CG  B LEU   A 53  ? 0.1094 0.1305 0.1015 -0.0012 -0.0142 -0.0077 53  LEU   A CG  
1346 C  CD1 A LEU   A 53  ? 0.1224 0.1377 0.1477 0.0021  0.0016  0.0147  53  LEU   A CD1 
1347 C  CD1 B LEU   A 53  ? 0.1109 0.1338 0.1141 -0.0012 -0.0093 -0.0142 53  LEU   A CD1 
1348 C  CD2 A LEU   A 53  ? 0.1376 0.1443 0.1555 -0.0079 0.0076  0.0186  53  LEU   A CD2 
1349 C  CD2 B LEU   A 53  ? 0.1092 0.1299 0.1090 -0.0036 -0.0011 -0.0113 53  LEU   A CD2 
1372 N  N   A ASN   A 54  ? 0.1178 0.1279 0.1032 -0.0036 -0.0011 0.0135  54  ASN   A N   
1373 N  N   B ASN   A 54  ? 0.1131 0.1323 0.1019 -0.0061 -0.0039 -0.0137 54  ASN   A N   
1374 C  CA  A ASN   A 54  ? 0.1105 0.1190 0.1196 -0.0025 -0.0088 0.0076  54  ASN   A CA  
1375 C  CA  B ASN   A 54  ? 0.1101 0.1292 0.1086 -0.0068 0.0001  -0.0161 54  ASN   A CA  
1376 C  C   A ASN   A 54  ? 0.1176 0.1247 0.1221 -0.0101 -0.0011 0.0054  54  ASN   A C   
1377 C  C   B ASN   A 54  ? 0.1169 0.1300 0.1125 -0.0114 0.0015  -0.0109 54  ASN   A C   
1378 O  O   A ASN   A 54  ? 0.1198 0.1361 0.1353 -0.0021 -0.0048 -0.0079 54  ASN   A O   
1379 O  O   B ASN   A 54  ? 0.1198 0.1368 0.1132 -0.0081 -0.0010 -0.0225 54  ASN   A O   
1380 C  CB  A ASN   A 54  ? 0.1079 0.1150 0.1330 -0.0047 -0.0178 0.0051  54  ASN   A CB  
1381 C  CB  B ASN   A 54  ? 0.1118 0.1308 0.1195 -0.0029 0.0050  -0.0148 54  ASN   A CB  
1382 C  CG  A ASN   A 54  ? 0.1094 0.1152 0.1359 -0.0038 -0.0103 0.0010  54  ASN   A CG  
1383 C  CG  B ASN   A 54  ? 0.1118 0.1333 0.1247 0.0022  0.0157  -0.0135 54  ASN   A CG  
1384 O  OD1 A ASN   A 54  ? 0.1081 0.1165 0.1233 -0.0053 -0.0169 0.0150  54  ASN   A OD1 
1385 O  OD1 B ASN   A 54  ? 0.1088 0.1384 0.1266 0.0027  0.0190  -0.0102 54  ASN   A OD1 
1386 N  ND2 A ASN   A 54  ? 0.1122 0.1172 0.1611 -0.0060 -0.0161 0.0070  54  ASN   A ND2 
1387 N  ND2 B ASN   A 54  ? 0.1195 0.1328 0.1396 -0.0020 0.0115  -0.0036 54  ASN   A ND2 
1400 N  N   . LYS   A 55  ? 0.1174 0.1284 0.1311 -0.0047 -0.0020 -0.0080 55  LYS   A N   
1401 C  CA  . LYS   A 55  ? 0.1280 0.1391 0.1326 0.0001  -0.0043 -0.0156 55  LYS   A CA  
1402 C  C   . LYS   A 55  ? 0.1232 0.1459 0.1396 -0.0023 -0.0009 -0.0263 55  LYS   A C   
1403 O  O   . LYS   A 55  ? 0.1317 0.1555 0.1452 0.0007  0.0003  -0.0247 55  LYS   A O   
1404 C  CB  . LYS   A 55  ? 0.1354 0.1458 0.1487 0.0108  -0.0092 -0.0229 55  LYS   A CB  
1405 C  CG  . LYS   A 55  ? 0.1532 0.1728 0.1692 0.0218  -0.0175 -0.0245 55  LYS   A CG  
1406 C  CD  . LYS   A 55  ? 0.1669 0.2024 0.1820 0.0347  -0.0132 -0.0211 55  LYS   A CD  
1407 C  CE  . LYS   A 55  ? 0.1866 0.2374 0.2069 0.0428  -0.0320 -0.0186 55  LYS   A CE  
1408 N  NZ  . LYS   A 55  ? 0.1946 0.2586 0.2139 0.0524  -0.0386 -0.0165 55  LYS   A NZ  
1423 N  N   . ALA   A 56  ? 0.1296 0.1510 0.1389 -0.0079 0.0051  -0.0216 56  ALA   A N   
1424 C  CA  . ALA   A 56  ? 0.1402 0.1641 0.1376 -0.0107 0.0067  -0.0181 56  ALA   A CA  
1425 C  C   . ALA   A 56  ? 0.1449 0.1733 0.1156 -0.0121 0.0144  -0.0214 56  ALA   A C   
1426 O  O   . ALA   A 56  ? 0.1511 0.2087 0.1275 -0.0012 0.0151  -0.0175 56  ALA   A O   
1427 C  CB  . ALA   A 56  ? 0.1500 0.1798 0.1516 -0.0166 0.0089  -0.0023 56  ALA   A CB  
1433 N  N   . THR   A 57  ? 0.1340 0.1577 0.1147 -0.0120 0.0129  -0.0161 57  THR   A N   
1434 C  CA  . THR   A 57  ? 0.1340 0.1571 0.1144 -0.0102 0.0010  -0.0141 57  THR   A CA  
1435 C  C   . THR   A 57  ? 0.1364 0.1628 0.1270 -0.0049 -0.0062 -0.0193 57  THR   A C   
1436 O  O   . THR   A 57  ? 0.1340 0.1656 0.1469 -0.0072 -0.0120 -0.0292 57  THR   A O   
1437 C  CB  . THR   A 57  ? 0.1338 0.1550 0.1137 -0.0108 -0.0041 -0.0122 57  THR   A CB  
1438 O  OG1 . THR   A 57  ? 0.1246 0.1483 0.1276 -0.0103 0.0007  -0.0105 57  THR   A OG1 
1439 C  CG2 . THR   A 57  ? 0.1408 0.1621 0.1109 -0.0076 -0.0057 -0.0014 57  THR   A CG2 
1447 N  N   . ASN   A 58  ? 0.1351 0.1558 0.1444 -0.0078 0.0064  -0.0295 58  ASN   A N   
1448 C  CA  . ASN   A 58  ? 0.1588 0.1500 0.1666 -0.0120 0.0131  -0.0406 58  ASN   A CA  
1449 C  C   . ASN   A 58  ? 0.1402 0.1409 0.1655 -0.0023 -0.0009 -0.0254 58  ASN   A C   
1450 O  O   . ASN   A 58  ? 0.1380 0.1482 0.1789 -0.0143 -0.0033 -0.0336 58  ASN   A O   
1451 C  CB  . ASN   A 58  ? 0.2055 0.1692 0.2030 -0.0211 0.0344  -0.0490 58  ASN   A CB  
1452 C  CG  . ASN   A 58  ? 0.2530 0.1939 0.2822 -0.0153 0.0418  -0.0384 58  ASN   A CG  
1453 O  OD1 . ASN   A 58  ? 0.2754 0.1903 0.3165 0.0141  0.0729  -0.0235 58  ASN   A OD1 
1454 N  ND2 . ASN   A 58  ? 0.2676 0.2037 0.3078 -0.0232 0.0240  -0.0508 58  ASN   A ND2 
1461 N  N   . ASN   A 59  ? 0.1238 0.1292 0.1497 -0.0080 -0.0078 -0.0178 59  ASN   A N   
1462 C  CA  . ASN   A 59  ? 0.1244 0.1230 0.1474 -0.0017 -0.0080 -0.0085 59  ASN   A CA  
1463 C  C   . ASN   A 59  ? 0.1245 0.1264 0.1296 -0.0092 -0.0075 -0.0058 59  ASN   A C   
1464 O  O   . ASN   A 59  ? 0.1269 0.1306 0.1409 -0.0091 0.0012  0.0050  59  ASN   A O   
1465 C  CB  . ASN   A 59  ? 0.1277 0.1222 0.1465 -0.0001 -0.0234 -0.0124 59  ASN   A CB  
1466 C  CG  . ASN   A 59  ? 0.1338 0.1270 0.1444 -0.0018 -0.0292 -0.0018 59  ASN   A CG  
1467 O  OD1 . ASN   A 59  ? 0.1430 0.1311 0.1414 -0.0088 -0.0247 0.0063  59  ASN   A OD1 
1468 N  ND2 . ASN   A 59  ? 0.1394 0.1362 0.1525 -0.0137 -0.0194 0.0027  59  ASN   A ND2 
1475 N  N   . ALA   A 60  ? 0.1212 0.1304 0.1257 -0.0067 -0.0014 -0.0051 60  ALA   A N   
1476 C  CA  . ALA   A 60  ? 0.1225 0.1294 0.1428 -0.0054 -0.0091 -0.0046 60  ALA   A CA  
1477 C  C   . ALA   A 60  ? 0.1208 0.1269 0.1370 -0.0024 -0.0012 -0.0001 60  ALA   A C   
1478 O  O   . ALA   A 60  ? 0.1158 0.1288 0.1607 -0.0024 -0.0061 -0.0067 60  ALA   A O   
1479 C  CB  . ALA   A 60  ? 0.1360 0.1424 0.1412 -0.0031 -0.0127 -0.0172 60  ALA   A CB  
1485 N  N   . MET   A 61  ? 0.1151 0.1247 0.1343 -0.0060 0.0017  -0.0031 61  MET   A N   
1486 C  CA  . MET   A 61  ? 0.1167 0.1188 0.1290 -0.0051 0.0016  0.0009  61  MET   A CA  
1487 C  C   . MET   A 61  ? 0.1126 0.1156 0.1430 -0.0087 -0.0062 -0.0046 61  MET   A C   
1488 O  O   . MET   A 61  ? 0.1199 0.1175 0.1439 -0.0021 0.0114  0.0005  61  MET   A O   
1489 C  CB  . MET   A 61  ? 0.1250 0.1214 0.1157 -0.0070 0.0028  0.0025  61  MET   A CB  
1490 C  CG  . MET   A 61  ? 0.1273 0.1285 0.1442 -0.0053 -0.0011 0.0009  61  MET   A CG  
1491 S  SD  . MET   A 61  ? 0.1260 0.1298 0.1730 -0.0099 -0.0006 -0.0175 61  MET   A SD  
1492 C  CE  . MET   A 61  ? 0.1422 0.1435 0.1798 -0.0142 0.0149  -0.0108 61  MET   A CE  
1502 N  N   . GLN   A 62  ? 0.1122 0.1171 0.1362 -0.0084 -0.0039 -0.0072 62  GLN   A N   
1503 C  CA  . GLN   A 62  ? 0.1181 0.1111 0.1474 -0.0066 0.0013  -0.0002 62  GLN   A CA  
1504 C  C   . GLN   A 62  ? 0.1191 0.1061 0.1453 -0.0005 0.0076  0.0012  62  GLN   A C   
1505 O  O   . GLN   A 62  ? 0.1222 0.1198 0.1498 -0.0031 0.0043  -0.0012 62  GLN   A O   
1506 C  CB  . GLN   A 62  ? 0.1176 0.1091 0.1433 -0.0041 -0.0013 -0.0011 62  GLN   A CB  
1507 C  CG  . GLN   A 62  ? 0.1254 0.1093 0.1351 -0.0058 -0.0064 0.0079  62  GLN   A CG  
1508 C  CD  . GLN   A 62  ? 0.1290 0.1145 0.1418 -0.0027 -0.0002 0.0076  62  GLN   A CD  
1509 O  OE1 . GLN   A 62  ? 0.1322 0.1268 0.1485 -0.0052 -0.0023 0.0021  62  GLN   A OE1 
1510 N  NE2 . GLN   A 62  ? 0.1388 0.1188 0.1574 -0.0017 -0.0027 -0.0118 62  GLN   A NE2 
1519 N  N   . VAL   A 63  ? 0.1199 0.1131 0.1597 -0.0029 0.0065  -0.0146 63  VAL   A N   
1520 C  CA  . VAL   A 63  ? 0.1190 0.1242 0.1796 -0.0161 -0.0023 -0.0164 63  VAL   A CA  
1521 C  C   . VAL   A 63  ? 0.1077 0.1257 0.1682 -0.0167 -0.0093 -0.0140 63  VAL   A C   
1522 O  O   . VAL   A 63  ? 0.1099 0.1291 0.1755 -0.0140 -0.0011 -0.0119 63  VAL   A O   
1523 C  CB  . VAL   A 63  ? 0.1313 0.1406 0.2063 -0.0177 -0.0003 -0.0349 63  VAL   A CB  
1524 C  CG1 . VAL   A 63  ? 0.1474 0.1628 0.2425 -0.0112 -0.0094 -0.0555 63  VAL   A CG1 
1525 C  CG2 . VAL   A 63  ? 0.1431 0.1365 0.2123 -0.0147 0.0196  -0.0245 63  VAL   A CG2 
1535 N  N   . GLU   A 64  ? 0.1114 0.1308 0.1592 -0.0038 -0.0017 -0.0061 64  GLU   A N   
1536 C  CA  . GLU   A 64  ? 0.1128 0.1301 0.1608 -0.0106 -0.0043 0.0027  64  GLU   A CA  
1537 C  C   . GLU   A 64  ? 0.1089 0.1240 0.1532 -0.0100 0.0024  0.0038  64  GLU   A C   
1538 O  O   . GLU   A 64  ? 0.1169 0.1307 0.1597 -0.0039 -0.0004 -0.0024 64  GLU   A O   
1539 C  CB  . GLU   A 64  ? 0.1230 0.1409 0.1643 -0.0064 0.0016  -0.0037 64  GLU   A CB  
1540 C  CG  . GLU   A 64  ? 0.1333 0.1431 0.1705 -0.0136 0.0040  -0.0060 64  GLU   A CG  
1541 C  CD  . GLU   A 64  ? 0.1434 0.1502 0.1622 -0.0199 0.0049  -0.0029 64  GLU   A CD  
1542 O  OE1 . GLU   A 64  ? 0.1417 0.1615 0.1861 -0.0247 0.0111  -0.0005 64  GLU   A OE1 
1543 O  OE2 . GLU   A 64  ? 0.1588 0.1522 0.1661 -0.0247 -0.0005 0.0012  64  GLU   A OE2 
1550 N  N   . SER   A 65  ? 0.1067 0.1260 0.1401 -0.0000 0.0012  0.0037  65  SER   A N   
1551 C  CA  . SER   A 65  ? 0.1154 0.1202 0.1372 -0.0061 -0.0023 -0.0009 65  SER   A CA  
1552 C  C   . SER   A 65  ? 0.1166 0.1252 0.1401 -0.0038 -0.0040 -0.0053 65  SER   A C   
1553 O  O   . SER   A 65  ? 0.1247 0.1303 0.1618 0.0006  0.0130  -0.0052 65  SER   A O   
1554 C  CB  . SER   A 65  ? 0.1179 0.1184 0.1389 -0.0082 0.0057  0.0091  65  SER   A CB  
1555 O  OG  . SER   A 65  ? 0.1183 0.1302 0.1505 -0.0092 -0.0024 0.0097  65  SER   A OG  
1561 N  N   . ASP   A 66  ? 0.1196 0.1217 0.1546 -0.0031 0.0124  0.0061  66  ASP   A N   
1562 C  CA  . ASP   A 66  ? 0.1284 0.1338 0.1600 -0.0053 0.0084  0.0113  66  ASP   A CA  
1563 C  C   . ASP   A 66  ? 0.1196 0.1272 0.1589 -0.0073 0.0142  0.0167  66  ASP   A C   
1564 O  O   . ASP   A 66  ? 0.1277 0.1392 0.1864 -0.0046 0.0250  0.0237  66  ASP   A O   
1565 C  CB  . ASP   A 66  ? 0.1356 0.1435 0.1884 0.0053  0.0090  0.0288  66  ASP   A CB  
1566 C  CG  . ASP   A 66  ? 0.1546 0.1565 0.2243 0.0015  0.0016  0.0442  66  ASP   A CG  
1567 O  OD1 . ASP   A 66  ? 0.1550 0.1836 0.2055 -0.0082 -0.0066 0.0470  66  ASP   A OD1 
1568 O  OD2 . ASP   A 66  ? 0.1747 0.1639 0.3140 0.0195  -0.0146 0.0292  66  ASP   A OD2 
1573 N  N   . ASP   A 67  ? 0.1168 0.1310 0.1714 -0.0040 0.0085  0.0109  67  ASP   A N   
1574 C  CA  . ASP   A 67  ? 0.1223 0.1456 0.1895 -0.0017 -0.0003 0.0271  67  ASP   A CA  
1575 C  C   . ASP   A 67  ? 0.1185 0.1502 0.1842 -0.0003 0.0084  0.0274  67  ASP   A C   
1576 O  O   . ASP   A 67  ? 0.1183 0.1551 0.2087 -0.0018 0.0175  0.0290  67  ASP   A O   
1577 C  CB  . ASP   A 67  ? 0.1303 0.1567 0.2198 -0.0015 -0.0169 0.0317  67  ASP   A CB  
1578 C  CG  . ASP   A 67  ? 0.1289 0.1688 0.2530 -0.0064 -0.0245 0.0322  67  ASP   A CG  
1579 O  OD1 . ASP   A 67  ? 0.1305 0.1841 0.3382 -0.0120 -0.0325 0.0377  67  ASP   A OD1 
1580 O  OD2 . ASP   A 67  ? 0.1273 0.1727 0.2335 0.0053  -0.0133 0.0309  67  ASP   A OD2 
1585 N  N   . TYR   A 68  ? 0.1208 0.1389 0.1690 0.0030  0.0162  0.0292  68  TYR   A N   
1586 C  CA  . TYR   A 68  ? 0.1354 0.1350 0.1685 0.0033  0.0179  0.0254  68  TYR   A CA  
1587 C  C   . TYR   A 68  ? 0.1302 0.1306 0.1684 -0.0012 0.0230  0.0217  68  TYR   A C   
1588 O  O   . TYR   A 68  ? 0.1356 0.1345 0.1845 0.0049  0.0284  0.0212  68  TYR   A O   
1589 C  CB  . TYR   A 68  ? 0.1375 0.1322 0.1736 0.0117  0.0387  0.0240  68  TYR   A CB  
1590 C  CG  . TYR   A 68  ? 0.1392 0.1477 0.1993 0.0019  0.0529  0.0324  68  TYR   A CG  
1591 C  CD1 . TYR   A 68  ? 0.1481 0.1568 0.2257 -0.0220 0.0446  -0.0063 68  TYR   A CD1 
1592 C  CD2 . TYR   A 68  ? 0.1570 0.1464 0.2487 0.0091  0.0533  0.0363  68  TYR   A CD2 
1593 C  CE1 . TYR   A 68  ? 0.1603 0.1638 0.2646 -0.0159 0.0444  -0.0082 68  TYR   A CE1 
1594 C  CE2 . TYR   A 68  ? 0.1608 0.1517 0.2577 0.0020  0.0599  0.0216  68  TYR   A CE2 
1595 C  CZ  . TYR   A 68  ? 0.1640 0.1569 0.2717 -0.0141 0.0438  -0.0055 68  TYR   A CZ  
1596 O  OH  . TYR   A 68  ? 0.1872 0.1558 0.2920 -0.0067 0.0229  -0.0224 68  TYR   A OH  
1606 N  N   . ILE   A 69  ? 0.1194 0.1271 0.1663 -0.0018 0.0187  0.0190  69  ILE   A N   
1607 C  CA  . ILE   A 69  ? 0.1258 0.1317 0.1602 0.0021  0.0161  0.0110  69  ILE   A CA  
1608 C  C   . ILE   A 69  ? 0.1313 0.1336 0.1515 0.0040  0.0179  0.0166  69  ILE   A C   
1609 O  O   . ILE   A 69  ? 0.1380 0.1436 0.1564 -0.0018 0.0233  0.0209  69  ILE   A O   
1610 C  CB  . ILE   A 69  ? 0.1341 0.1507 0.1636 0.0057  0.0147  0.0030  69  ILE   A CB  
1611 C  CG1 . ILE   A 69  ? 0.1334 0.1678 0.1770 0.0084  0.0135  -0.0166 69  ILE   A CG1 
1612 C  CG2 . ILE   A 69  ? 0.1500 0.1713 0.1876 0.0097  0.0065  -0.0057 69  ILE   A CG2 
1613 C  CD1 . ILE   A 69  ? 0.1324 0.1751 0.1918 -0.0019 0.0090  -0.0243 69  ILE   A CD1 
1625 N  N   . ALA   A 70  ? 0.1371 0.1312 0.1656 -0.0043 0.0195  0.0138  70  ALA   A N   
1626 C  CA  . ALA   A 70  ? 0.1397 0.1419 0.1822 -0.0135 0.0314  0.0198  70  ALA   A CA  
1627 C  C   . ALA   A 70  ? 0.1386 0.1610 0.1846 -0.0118 0.0308  0.0218  70  ALA   A C   
1628 O  O   . ALA   A 70  ? 0.1543 0.1960 0.1977 0.0049  0.0440  0.0323  70  ALA   A O   
1629 C  CB  . ALA   A 70  ? 0.1422 0.1380 0.2097 -0.0129 0.0281  0.0176  70  ALA   A CB  
1635 N  N   . THR   A 71  ? 0.1332 0.1549 0.1779 -0.0040 0.0219  0.0235  71  THR   A N   
1636 C  CA  . THR   A 71  ? 0.1408 0.1709 0.2051 0.0083  0.0242  0.0247  71  THR   A CA  
1637 C  C   . THR   A 71  ? 0.1327 0.1663 0.2267 0.0140  0.0380  0.0171  71  THR   A C   
1638 O  O   . THR   A 71  ? 0.1385 0.1944 0.2663 0.0113  0.0475  -0.0075 71  THR   A O   
1639 C  CB  . THR   A 71  ? 0.1638 0.1959 0.2251 0.0136  -0.0128 0.0316  71  THR   A CB  
1640 O  OG1 . THR   A 71  ? 0.1879 0.2132 0.2278 0.0090  -0.0362 0.0269  71  THR   A OG1 
1641 C  CG2 . THR   A 71  ? 0.1782 0.2170 0.2516 0.0185  -0.0272 0.0477  71  THR   A CG2 
1649 N  N   . ASN   A 72  ? 0.1346 0.1462 0.2014 0.0144  0.0311  0.0256  72  ASN   A N   
1650 C  CA  . ASN   A 72  ? 0.1440 0.1496 0.1980 0.0165  0.0368  0.0244  72  ASN   A CA  
1651 C  C   . ASN   A 72  ? 0.1522 0.1476 0.1980 0.0110  0.0504  0.0150  72  ASN   A C   
1652 O  O   . ASN   A 72  ? 0.1657 0.1498 0.2299 0.0129  0.0431  0.0032  72  ASN   A O   
1653 C  CB  . ASN   A 72  ? 0.1632 0.1568 0.2055 0.0178  0.0344  0.0279  72  ASN   A CB  
1654 C  CG  . ASN   A 72  ? 0.1858 0.1682 0.2113 0.0245  0.0361  0.0302  72  ASN   A CG  
1655 O  OD1 . ASN   A 72  ? 0.1970 0.2023 0.2304 0.0213  0.0402  0.0263  72  ASN   A OD1 
1656 N  ND2 . ASN   A 72  ? 0.2007 0.1688 0.2219 0.0468  0.0196  0.0151  72  ASN   A ND2 
1663 N  N   . GLY   A 73  ? 0.1538 0.1489 0.1761 0.0053  0.0461  0.0166  73  GLY   A N   
1664 C  CA  . GLY   A 73  ? 0.1619 0.1453 0.1631 -0.0063 0.0416  0.0078  73  GLY   A CA  
1665 C  C   . GLY   A 73  ? 0.1581 0.1369 0.1546 0.0001  0.0499  0.0173  73  GLY   A C   
1666 O  O   . GLY   A 73  ? 0.1562 0.1422 0.1771 0.0112  0.0405  0.0231  73  GLY   A O   
1670 N  N   . PRO   A 74  ? 0.1667 0.1375 0.1609 -0.0087 0.0487  0.0148  74  PRO   A N   
1671 C  CA  . PRO   A 74  ? 0.1602 0.1394 0.1702 0.0002  0.0449  0.0216  74  PRO   A CA  
1672 C  C   . PRO   A 74  ? 0.1566 0.1218 0.1666 0.0028  0.0319  0.0043  74  PRO   A C   
1673 O  O   . PRO   A 74  ? 0.1650 0.1282 0.1851 0.0041  0.0352  0.0006  74  PRO   A O   
1674 C  CB  . PRO   A 74  ? 0.1779 0.1659 0.1869 0.0025  0.0397  0.0362  74  PRO   A CB  
1675 C  CG  . PRO   A 74  ? 0.2022 0.1974 0.2382 -0.0142 0.0332  0.0237  74  PRO   A CG  
1676 C  CD  . PRO   A 74  ? 0.1860 0.1753 0.1821 -0.0190 0.0398  0.0101  74  PRO   A CD  
1684 N  N   . LEU   A 75  ? 0.1528 0.1113 0.1516 0.0025  0.0274  0.0066  75  LEU   A N   
1685 C  CA  . LEU   A 75  ? 0.1608 0.1190 0.1376 0.0009  0.0125  0.0087  75  LEU   A CA  
1686 C  C   . LEU   A 75  ? 0.1703 0.1284 0.1324 0.0064  0.0154  0.0124  75  LEU   A C   
1687 O  O   . LEU   A 75  ? 0.2028 0.1437 0.1440 0.0122  0.0080  0.0054  75  LEU   A O   
1688 C  CB  . LEU   A 75  ? 0.1654 0.1272 0.1316 -0.0120 0.0103  0.0184  75  LEU   A CB  
1689 C  CG  . LEU   A 75  ? 0.1787 0.1671 0.1414 -0.0348 0.0109  0.0134  75  LEU   A CG  
1690 C  CD1 . LEU   A 75  ? 0.1868 0.2120 0.1609 -0.0413 0.0126  -0.0059 75  LEU   A CD1 
1691 C  CD2 . LEU   A 75  ? 0.2007 0.2077 0.1851 -0.0181 0.0127  0.0108  75  LEU   A CD2 
1703 N  N   . LYS   A 76  ? 0.1722 0.1309 0.1389 -0.0003 0.0158  -0.0015 76  LYS   A N   
1704 C  CA  . LYS   A 76  ? 0.1696 0.1484 0.1410 -0.0020 0.0192  -0.0120 76  LYS   A CA  
1705 C  C   . LYS   A 76  ? 0.1677 0.1281 0.1196 0.0002  0.0133  -0.0013 76  LYS   A C   
1706 O  O   . LYS   A 76  ? 0.1637 0.1259 0.1246 -0.0023 0.0179  0.0065  76  LYS   A O   
1707 C  CB  . LYS   A 76  ? 0.1694 0.1717 0.1946 0.0012  0.0188  -0.0330 76  LYS   A CB  
1708 C  CG  . LYS   A 76  ? 0.1803 0.1676 0.2596 0.0083  0.0134  -0.0335 76  LYS   A CG  
1709 C  CD  . LYS   A 76  ? 0.1870 0.1681 0.3084 0.0125  -0.0013 -0.0409 76  LYS   A CD  
1710 C  CE  . LYS   A 76  ? 0.2030 0.1876 0.3671 0.0010  -0.0038 -0.0441 76  LYS   A CE  
1711 N  NZ  . LYS   A 76  ? 0.2048 0.1832 0.4058 -0.0107 -0.0149 -0.0482 76  LYS   A NZ  
1725 N  N   . VAL   A 77  ? 0.1746 0.1348 0.1259 -0.0020 0.0264  0.0129  77  VAL   A N   
1726 C  CA  . VAL   A 77  ? 0.1703 0.1361 0.1229 0.0076  0.0184  0.0121  77  VAL   A CA  
1727 C  C   . VAL   A 77  ? 0.1652 0.1311 0.1183 0.0093  0.0123  0.0007  77  VAL   A C   
1728 O  O   . VAL   A 77  ? 0.1713 0.1371 0.1224 0.0091  0.0242  -0.0016 77  VAL   A O   
1729 C  CB  . VAL   A 77  ? 0.1821 0.1526 0.1391 0.0105  0.0106  0.0232  77  VAL   A CB  
1730 C  CG1 . VAL   A 77  ? 0.1775 0.1684 0.1536 0.0188  -0.0003 0.0105  77  VAL   A CG1 
1731 C  CG2 . VAL   A 77  ? 0.2077 0.1617 0.1535 0.0041  -0.0027 0.0331  77  VAL   A CG2 
1741 N  N   . GLY   A 78  ? 0.1574 0.1283 0.1239 0.0072  0.0220  0.0054  78  GLY   A N   
1742 C  CA  . GLY   A 78  ? 0.1498 0.1252 0.1311 0.0057  0.0263  0.0147  78  GLY   A CA  
1743 C  C   . GLY   A 78  ? 0.1374 0.1221 0.1323 0.0043  0.0247  0.0163  78  GLY   A C   
1744 O  O   . GLY   A 78  ? 0.1370 0.1309 0.1456 0.0028  0.0160  0.0208  78  GLY   A O   
1748 N  N   . GLY   A 79  ? 0.1434 0.1185 0.1278 0.0037  0.0194  0.0124  79  GLY   A N   
1749 C  CA  . GLY   A 79  ? 0.1378 0.1165 0.1451 0.0050  0.0156  0.0103  79  GLY   A CA  
1750 C  C   . GLY   A 79  ? 0.1270 0.1151 0.1390 0.0030  0.0127  0.0085  79  GLY   A C   
1751 O  O   . GLY   A 79  ? 0.1347 0.1266 0.1438 0.0171  0.0125  0.0046  79  GLY   A O   
1755 N  N   . SER   A 80  ? 0.1227 0.1314 0.1515 0.0002  0.0159  -0.0024 80  SER   A N   
1756 C  CA  . SER   A 80  ? 0.1245 0.1258 0.1399 0.0018  0.0069  0.0056  80  SER   A CA  
1757 C  C   . SER   A 80  ? 0.1189 0.1299 0.1396 -0.0024 0.0073  0.0133  80  SER   A C   
1758 O  O   . SER   A 80  ? 0.1209 0.1488 0.1761 0.0060  0.0142  0.0023  80  SER   A O   
1759 C  CB  . SER   A 80  ? 0.1344 0.1296 0.1643 -0.0055 0.0120  0.0074  80  SER   A CB  
1760 O  OG  . SER   A 80  ? 0.1595 0.1274 0.2031 0.0044  0.0007  0.0232  80  SER   A OG  
1766 N  N   . CYS   A 81  ? 0.1154 0.1249 0.1366 0.0005  -0.0017 0.0109  81  CYS   A N   
1767 C  CA  . CYS   A 81  ? 0.1145 0.1330 0.1309 -0.0021 -0.0039 0.0195  81  CYS   A CA  
1768 C  C   . CYS   A 81  ? 0.1159 0.1255 0.1295 -0.0087 -0.0006 0.0244  81  CYS   A C   
1769 O  O   . CYS   A 81  ? 0.1134 0.1556 0.1494 -0.0033 0.0010  0.0306  81  CYS   A O   
1770 C  CB  . CYS   A 81  ? 0.1232 0.1400 0.1600 -0.0130 0.0018  0.0209  81  CYS   A CB  
1771 S  SG  . CYS   A 81  ? 0.1355 0.1279 0.1633 -0.0131 0.0020  0.0163  81  CYS   A SG  
1777 N  N   . VAL   A 82  ? 0.1200 0.1311 0.1322 -0.0015 -0.0090 0.0167  82  VAL   A N   
1778 C  CA  . VAL   A 82  ? 0.1327 0.1366 0.1301 0.0013  -0.0087 0.0219  82  VAL   A CA  
1779 C  C   . VAL   A 82  ? 0.1294 0.1402 0.1451 -0.0003 -0.0085 0.0219  82  VAL   A C   
1780 O  O   . VAL   A 82  ? 0.1222 0.1513 0.1759 -0.0010 -0.0066 -0.0017 82  VAL   A O   
1781 C  CB  . VAL   A 82  ? 0.1633 0.1477 0.1509 0.0017  -0.0057 0.0263  82  VAL   A CB  
1782 C  CG1 . VAL   A 82  ? 0.1877 0.1622 0.1639 0.0076  0.0013  0.0272  82  VAL   A CG1 
1783 C  CG2 . VAL   A 82  ? 0.1713 0.1547 0.1776 -0.0002 -0.0104 0.0351  82  VAL   A CG2 
1793 N  N   . LEU   A 83  ? 0.1249 0.1353 0.1338 -0.0048 -0.0049 0.0110  83  LEU   A N   
1794 C  CA  . LEU   A 83  ? 0.1275 0.1383 0.1316 -0.0080 -0.0121 0.0080  83  LEU   A CA  
1795 C  C   . LEU   A 83  ? 0.1308 0.1435 0.1285 -0.0069 -0.0097 0.0133  83  LEU   A C   
1796 O  O   . LEU   A 83  ? 0.1432 0.1460 0.1353 -0.0095 -0.0018 0.0203  83  LEU   A O   
1797 C  CB  . LEU   A 83  ? 0.1377 0.1433 0.1459 -0.0111 -0.0074 0.0118  83  LEU   A CB  
1798 C  CG  . LEU   A 83  ? 0.1453 0.1510 0.1507 -0.0109 0.0032  0.0106  83  LEU   A CG  
1799 C  CD1 . LEU   A 83  ? 0.1616 0.1566 0.1556 -0.0229 0.0004  0.0180  83  LEU   A CD1 
1800 C  CD2 . LEU   A 83  ? 0.1421 0.1656 0.1687 -0.0076 0.0121  0.0185  83  LEU   A CD2 
1812 N  N   . SER   A 84  ? 0.1467 0.1496 0.1294 -0.0112 -0.0112 0.0135  84  SER   A N   
1813 C  CA  . SER   A 84  ? 0.1554 0.1550 0.1196 -0.0150 -0.0081 0.0109  84  SER   A CA  
1814 C  C   . SER   A 84  ? 0.1609 0.1553 0.1110 -0.0184 0.0024  0.0068  84  SER   A C   
1815 O  O   . SER   A 84  ? 0.1552 0.1643 0.1149 -0.0132 -0.0092 0.0027  84  SER   A O   
1816 C  CB  . SER   A 84  ? 0.1641 0.1781 0.1319 -0.0135 -0.0116 0.0041  84  SER   A CB  
1817 O  OG  . SER   A 84  ? 0.1709 0.1945 0.1414 -0.0121 -0.0158 -0.0099 84  SER   A OG  
1823 N  N   . GLY   A 85  ? 0.1735 0.1664 0.1088 -0.0224 0.0054  0.0080  85  GLY   A N   
1824 C  CA  . GLY   A 85  ? 0.1712 0.1723 0.1297 -0.0261 0.0136  -0.0016 85  GLY   A CA  
1825 C  C   . GLY   A 85  ? 0.1638 0.1803 0.1196 -0.0184 0.0021  -0.0042 85  GLY   A C   
1826 O  O   . GLY   A 85  ? 0.1636 0.1894 0.1297 -0.0222 0.0140  -0.0086 85  GLY   A O   
1830 N  N   . HIS   A 86  ? 0.1663 0.1724 0.1171 -0.0180 -0.0004 -0.0020 86  HIS   A N   
1831 C  CA  . HIS   A 86  ? 0.1841 0.1755 0.1216 -0.0177 -0.0006 -0.0006 86  HIS   A CA  
1832 C  C   . HIS   A 86  ? 0.2069 0.1868 0.1044 -0.0193 -0.0067 -0.0016 86  HIS   A C   
1833 O  O   . HIS   A 86  ? 0.2148 0.2094 0.1136 -0.0146 0.0048  0.0022  86  HIS   A O   
1834 C  CB  . HIS   A 86  ? 0.1831 0.1671 0.1351 -0.0152 0.0068  -0.0001 86  HIS   A CB  
1835 C  CG  . HIS   A 86  ? 0.1795 0.1620 0.1352 -0.0078 0.0038  0.0073  86  HIS   A CG  
1836 N  ND1 . HIS   A 86  ? 0.1846 0.1633 0.1663 -0.0157 -0.0003 0.0058  86  HIS   A ND1 
1837 C  CD2 . HIS   A 86  ? 0.1815 0.1612 0.1309 0.0001  0.0103  0.0121  86  HIS   A CD2 
1838 C  CE1 . HIS   A 86  ? 0.1833 0.1683 0.1557 -0.0131 0.0170  0.0103  86  HIS   A CE1 
1839 N  NE2 . HIS   A 86  ? 0.1788 0.1613 0.1400 -0.0014 0.0191  0.0194  86  HIS   A NE2 
1847 N  N   . ASN   A 87  ? 0.2245 0.1956 0.1150 -0.0119 0.0177  -0.0111 87  ASN   A N   
1848 C  CA  . ASN   A 87  ? 0.2409 0.2074 0.1253 -0.0116 0.0390  -0.0181 87  ASN   A CA  
1849 C  C   . ASN   A 87  ? 0.2381 0.2209 0.1622 -0.0177 0.0592  -0.0092 87  ASN   A C   
1850 O  O   . ASN   A 87  ? 0.2596 0.2371 0.2109 -0.0296 0.0916  -0.0144 87  ASN   A O   
1851 C  CB  . ASN   A 87  ? 0.2592 0.2170 0.1309 -0.0012 0.0431  -0.0176 87  ASN   A CB  
1852 C  CG  . ASN   A 87  ? 0.2712 0.2281 0.1445 0.0045  0.0541  -0.0094 87  ASN   A CG  
1853 O  OD1 . ASN   A 87  ? 0.2862 0.2226 0.1562 0.0184  0.0510  -0.0028 87  ASN   A OD1 
1854 N  ND2 . ASN   A 87  ? 0.2737 0.2526 0.1601 0.0017  0.0514  -0.0022 87  ASN   A ND2 
1861 N  N   . LEU   A 88  ? 0.2099 0.2139 0.1541 -0.0206 0.0355  0.0117  88  LEU   A N   
1862 C  CA  . LEU   A 88  ? 0.1923 0.2155 0.1756 -0.0252 0.0277  0.0248  88  LEU   A CA  
1863 C  C   . LEU   A 88  ? 0.1878 0.2153 0.1598 -0.0256 0.0239  0.0333  88  LEU   A C   
1864 O  O   . LEU   A 88  ? 0.1892 0.2170 0.1951 -0.0273 0.0305  0.0495  88  LEU   A O   
1865 C  CB  . LEU   A 88  ? 0.1944 0.2261 0.1820 -0.0315 -0.0050 0.0328  88  LEU   A CB  
1866 C  CG  . LEU   A 88  ? 0.2130 0.2408 0.2121 -0.0306 -0.0109 0.0398  88  LEU   A CG  
1867 C  CD1 . LEU   A 88  ? 0.2237 0.2487 0.2056 -0.0319 -0.0126 0.0303  88  LEU   A CD1 
1868 C  CD2 . LEU   A 88  ? 0.2250 0.2494 0.2491 -0.0263 -0.0038 0.0330  88  LEU   A CD2 
1880 N  N   . ALA   A 89  ? 0.1876 0.2047 0.1366 -0.0273 0.0137  0.0123  89  ALA   A N   
1881 C  CA  . ALA   A 89  ? 0.1925 0.2002 0.1286 -0.0235 0.0098  0.0121  89  ALA   A CA  
1882 C  C   . ALA   A 89  ? 0.1989 0.2059 0.1334 -0.0207 -0.0066 0.0106  89  ALA   A C   
1883 O  O   . ALA   A 89  ? 0.1924 0.2025 0.1621 -0.0239 -0.0123 -0.0107 89  ALA   A O   
1884 C  CB  . ALA   A 89  ? 0.1852 0.1947 0.1205 -0.0224 0.0062  0.0161  89  ALA   A CB  
1890 N  N   . LYS   A 90  ? 0.2115 0.2181 0.1268 -0.0299 -0.0217 0.0210  90  LYS   A N   
1891 C  CA  . LYS   A 90  ? 0.2222 0.2328 0.1206 -0.0235 -0.0343 0.0240  90  LYS   A CA  
1892 C  C   . LYS   A 90  ? 0.1985 0.2119 0.1259 -0.0233 -0.0302 0.0111  90  LYS   A C   
1893 O  O   . LYS   A 90  ? 0.1990 0.2214 0.1597 -0.0296 -0.0334 -0.0014 90  LYS   A O   
1894 C  CB  . LYS   A 90  ? 0.2529 0.2698 0.1639 -0.0164 -0.0385 0.0460  90  LYS   A CB  
1895 C  CG  . LYS   A 90  ? 0.2906 0.3076 0.2732 -0.0117 -0.0369 0.0558  90  LYS   A CG  
1896 C  CD  . LYS   A 90  ? 0.3376 0.3463 0.3745 -0.0118 -0.0194 0.0543  90  LYS   A CD  
1897 C  CE  . LYS   A 90  ? 0.3772 0.3823 0.4431 -0.0130 -0.0085 0.0502  90  LYS   A CE  
1898 N  NZ  . LYS   A 90  ? 0.4059 0.4061 0.4978 -0.0133 -0.0080 0.0506  90  LYS   A NZ  
1912 N  N   . HIS   A 91  ? 0.1827 0.1886 0.1051 -0.0203 -0.0319 0.0152  91  HIS   A N   
1913 C  CA  . HIS   A 91  ? 0.1672 0.1746 0.1090 -0.0153 -0.0260 0.0125  91  HIS   A CA  
1914 C  C   . HIS   A 91  ? 0.1495 0.1588 0.1039 -0.0145 -0.0150 0.0150  91  HIS   A C   
1915 O  O   . HIS   A 91  ? 0.1461 0.1705 0.1209 -0.0198 -0.0021 0.0148  91  HIS   A O   
1916 C  CB  . HIS   A 91  ? 0.1832 0.1997 0.1624 0.0057  -0.0367 0.0152  91  HIS   A CB  
1917 C  CG  . HIS   A 91  ? 0.2238 0.2479 0.2277 0.0146  -0.0647 0.0067  91  HIS   A CG  
1918 N  ND1 . HIS   A 91  ? 0.2348 0.2787 0.2722 0.0202  -0.0735 -0.0051 91  HIS   A ND1 
1919 C  CD2 . HIS   A 91  ? 0.2509 0.2692 0.2516 0.0216  -0.0823 0.0171  91  HIS   A CD2 
1920 C  CE1 . HIS   A 91  ? 0.2491 0.2887 0.2787 0.0236  -0.0800 0.0063  91  HIS   A CE1 
1921 N  NE2 . HIS   A 91  ? 0.2606 0.2855 0.2746 0.0270  -0.0875 0.0119  91  HIS   A NE2 
1929 N  N   . CYS   A 92  ? 0.1404 0.1492 0.1055 -0.0172 -0.0116 0.0176  92  CYS   A N   
1930 C  CA  . CYS   A 92  ? 0.1305 0.1398 0.1213 -0.0129 -0.0001 0.0130  92  CYS   A CA  
1931 C  C   . CYS   A 92  ? 0.1252 0.1376 0.1111 -0.0142 0.0018  0.0147  92  CYS   A C   
1932 O  O   . CYS   A 92  ? 0.1288 0.1457 0.1255 -0.0170 -0.0007 0.0126  92  CYS   A O   
1933 C  CB  . CYS   A 92  ? 0.1343 0.1392 0.1335 -0.0035 -0.0086 0.0052  92  CYS   A CB  
1934 S  SG  . CYS   A 92  ? 0.1329 0.1302 0.1303 -0.0113 -0.0014 0.0096  92  CYS   A SG  
1940 N  N   . LEU   A 93  ? 0.1249 0.1251 0.1219 -0.0119 0.0002  0.0201  93  LEU   A N   
1941 C  CA  . LEU   A 93  ? 0.1206 0.1232 0.1091 -0.0090 0.0019  0.0121  93  LEU   A CA  
1942 C  C   . LEU   A 93  ? 0.1166 0.1138 0.1121 -0.0025 0.0042  0.0076  93  LEU   A C   
1943 O  O   . LEU   A 93  ? 0.1112 0.1211 0.1222 -0.0012 0.0051  0.0133  93  LEU   A O   
1944 C  CB  . LEU   A 93  ? 0.1260 0.1261 0.1275 -0.0043 0.0000  0.0196  93  LEU   A CB  
1945 C  CG  . LEU   A 93  ? 0.1307 0.1265 0.1279 -0.0049 0.0004  0.0230  93  LEU   A CG  
1946 C  CD1 . LEU   A 93  ? 0.1332 0.1282 0.1716 -0.0020 0.0064  0.0174  93  LEU   A CD1 
1947 C  CD2 . LEU   A 93  ? 0.1408 0.1284 0.1460 -0.0095 0.0007  0.0210  93  LEU   A CD2 
1959 N  N   . HIS   A 94  ? 0.1117 0.1107 0.1168 0.0003  0.0033  0.0172  94  HIS   A N   
1960 C  CA  . HIS   A 94  ? 0.1087 0.1094 0.1178 -0.0022 -0.0010 0.0124  94  HIS   A CA  
1961 C  C   . HIS   A 94  ? 0.1100 0.1124 0.1247 -0.0080 0.0012  0.0112  94  HIS   A C   
1962 O  O   . HIS   A 94  ? 0.1091 0.1332 0.1521 0.0021  0.0006  -0.0029 94  HIS   A O   
1963 C  CB  . HIS   A 94  ? 0.1120 0.1110 0.1258 -0.0038 -0.0017 0.0085  94  HIS   A CB  
1964 C  CG  . HIS   A 94  ? 0.1130 0.1140 0.1212 -0.0041 -0.0000 0.0166  94  HIS   A CG  
1965 N  ND1 . HIS   A 94  ? 0.1129 0.1104 0.1316 -0.0020 0.0010  0.0163  94  HIS   A ND1 
1966 C  CD2 . HIS   A 94  ? 0.1182 0.1263 0.1260 -0.0034 -0.0041 0.0102  94  HIS   A CD2 
1967 C  CE1 . HIS   A 94  ? 0.1179 0.1130 0.1317 -0.0114 -0.0058 0.0097  94  HIS   A CE1 
1968 N  NE2 . HIS   A 94  ? 0.1218 0.1184 0.1276 -0.0063 -0.0024 0.0027  94  HIS   A NE2 
1976 N  N   . VAL   A 95  ? 0.1057 0.1071 0.1098 -0.0034 0.0095  0.0083  95  VAL   A N   
1977 C  CA  . VAL   A 95  ? 0.1188 0.1096 0.1103 -0.0080 0.0085  0.0101  95  VAL   A CA  
1978 C  C   . VAL   A 95  ? 0.1199 0.1122 0.0926 -0.0102 0.0062  0.0104  95  VAL   A C   
1979 O  O   . VAL   A 95  ? 0.1211 0.1219 0.1180 0.0083  0.0052  0.0078  95  VAL   A O   
1980 C  CB  . VAL   A 95  ? 0.1220 0.1126 0.1337 -0.0080 0.0069  0.0096  95  VAL   A CB  
1981 C  CG1 . VAL   A 95  ? 0.1370 0.1143 0.1437 -0.0168 0.0063  0.0072  95  VAL   A CG1 
1982 C  CG2 . VAL   A 95  ? 0.1208 0.1146 0.1349 -0.0115 0.0092  0.0213  95  VAL   A CG2 
1992 N  N   . VAL   A 96  ? 0.1236 0.1094 0.0992 -0.0021 0.0065  0.0125  96  VAL   A N   
1993 C  CA  . VAL   A 96  ? 0.1317 0.1126 0.1163 -0.0004 0.0107  0.0162  96  VAL   A CA  
1994 C  C   . VAL   A 96  ? 0.1343 0.1196 0.1142 -0.0028 0.0139  0.0137  96  VAL   A C   
1995 O  O   . VAL   A 96  ? 0.1440 0.1244 0.1393 -0.0040 0.0188  -0.0003 96  VAL   A O   
1996 C  CB  . VAL   A 96  ? 0.1317 0.1178 0.1244 -0.0020 0.0163  0.0156  96  VAL   A CB  
1997 C  CG1 . VAL   A 96  ? 0.1382 0.1247 0.1183 -0.0025 0.0164  0.0151  96  VAL   A CG1 
1998 C  CG2 . VAL   A 96  ? 0.1335 0.1286 0.1355 -0.0092 0.0150  0.0160  96  VAL   A CG2 
2008 N  N   A GLY   A 97  ? 0.1285 0.1254 0.1245 -0.0066 0.0085  0.0064  97  GLY   A N   
2009 N  N   B GLY   A 97  ? 0.1361 0.1256 0.1108 -0.0041 0.0076  0.0108  97  GLY   A N   
2010 C  CA  A GLY   A 97  ? 0.1349 0.1364 0.1313 -0.0060 -0.0018 0.0074  97  GLY   A CA  
2011 C  CA  B GLY   A 97  ? 0.1455 0.1343 0.1093 -0.0024 0.0008  0.0148  97  GLY   A CA  
2012 C  C   A GLY   A 97  ? 0.1365 0.1452 0.1145 -0.0046 0.0013  0.0067  97  GLY   A C   
2013 C  C   B GLY   A 97  ? 0.1525 0.1407 0.1052 0.0011  0.0008  0.0187  97  GLY   A C   
2014 O  O   A GLY   A 97  ? 0.1497 0.1454 0.1325 -0.0051 0.0026  0.0044  97  GLY   A O   
2015 O  O   B GLY   A 97  ? 0.1621 0.1418 0.1074 -0.0014 -0.0011 0.0254  97  GLY   A O   
2022 N  N   A PRO   A 98  ? 0.1405 0.1473 0.0972 0.0007  -0.0082 0.0058  98  PRO   A N   
2023 N  N   B PRO   A 98  ? 0.1594 0.1439 0.1258 0.0049  -0.0017 0.0193  98  PRO   A N   
2024 C  CA  A PRO   A 98  ? 0.1557 0.1598 0.0873 0.0085  0.0016  0.0042  98  PRO   A CA  
2025 C  CA  B PRO   A 98  ? 0.1721 0.1541 0.1331 0.0059  -0.0007 0.0152  98  PRO   A CA  
2026 C  C   A PRO   A 98  ? 0.1551 0.1640 0.0957 0.0037  0.0037  0.0160  98  PRO   A C   
2027 C  C   B PRO   A 98  ? 0.1898 0.1519 0.1307 -0.0002 0.0044  0.0274  98  PRO   A C   
2028 O  O   A PRO   A 98  ? 0.1474 0.1486 0.1117 0.0061  0.0028  0.0101  98  PRO   A O   
2029 O  O   B PRO   A 98  ? 0.1891 0.1485 0.1539 0.0004  0.0107  0.0183  98  PRO   A O   
2030 C  CB  A PRO   A 98  ? 0.1661 0.1690 0.0809 0.0155  -0.0103 -0.0121 98  PRO   A CB  
2031 C  CB  B PRO   A 98  ? 0.1747 0.1533 0.1267 0.0127  -0.0079 0.0134  98  PRO   A CB  
2032 C  CG  A PRO   A 98  ? 0.1563 0.1600 0.1009 0.0181  -0.0163 -0.0174 98  PRO   A CG  
2033 C  CG  B PRO   A 98  ? 0.1779 0.1485 0.1388 0.0089  -0.0060 0.0183  98  PRO   A CG  
2034 C  CD  A PRO   A 98  ? 0.1476 0.1472 0.1037 0.0101  -0.0126 0.0019  98  PRO   A CD  
2035 C  CD  B PRO   A 98  ? 0.1666 0.1434 0.1337 0.0082  -0.0024 0.0211  98  PRO   A CD  
2050 N  N   A ASN   A 99  ? 0.1616 0.1826 0.1057 0.0039  0.0096  0.0218  99  ASN   A N   
2051 N  N   B ASN   A 99  ? 0.2136 0.1557 0.1159 -0.0030 0.0035  0.0443  99  ASN   A N   
2052 C  CA  A ASN   A 99  ? 0.1777 0.1956 0.1095 0.0045  0.0107  0.0225  99  ASN   A CA  
2053 C  CA  B ASN   A 99  ? 0.2404 0.1640 0.1120 0.0010  -0.0079 0.0613  99  ASN   A CA  
2054 C  C   A ASN   A 99  ? 0.1957 0.2218 0.1086 -0.0065 0.0153  0.0173  99  ASN   A C   
2055 C  C   B ASN   A 99  ? 0.2572 0.1773 0.1223 0.0026  -0.0185 0.0665  99  ASN   A C   
2056 O  O   A ASN   A 99  ? 0.2022 0.2350 0.1092 0.0015  0.0065  0.0125  99  ASN   A O   
2057 O  O   B ASN   A 99  ? 0.2586 0.1640 0.1208 0.0107  -0.0254 0.0531  99  ASN   A O   
2058 C  CB  A ASN   A 99  ? 0.1785 0.1922 0.1302 0.0072  0.0024  0.0171  99  ASN   A CB  
2059 C  CB  B ASN   A 99  ? 0.2491 0.1654 0.1496 0.0048  -0.0217 0.0641  99  ASN   A CB  
2060 C  CG  A ASN   A 99  ? 0.1783 0.1860 0.1461 0.0107  -0.0070 -0.0068 99  ASN   A CG  
2061 C  CG  B ASN   A 99  ? 0.2563 0.1768 0.1920 0.0076  -0.0247 0.0542  99  ASN   A CG  
2062 O  OD1 A ASN   A 99  ? 0.1813 0.1979 0.1182 0.0186  0.0011  -0.0075 99  ASN   A OD1 
2063 O  OD1 B ASN   A 99  ? 0.2611 0.1799 0.1792 0.0064  -0.0187 0.0613  99  ASN   A OD1 
2064 N  ND2 A ASN   A 99  ? 0.1794 0.1667 0.1646 -0.0047 -0.0254 0.0016  99  ASN   A ND2 
2065 N  ND2 B ASN   A 99  ? 0.2582 0.1866 0.2166 0.0158  -0.0302 0.0409  99  ASN   A ND2 
2078 N  N   A VAL   A 100 ? 0.2115 0.2297 0.1093 -0.0254 -0.0124 0.0186  100 VAL   A N   
2079 N  N   B VAL   A 100 ? 0.2730 0.2109 0.1465 -0.0043 -0.0313 0.0716  100 VAL   A N   
2080 C  CA  A VAL   A 100 ? 0.2353 0.2425 0.1180 -0.0342 -0.0251 0.0186  100 VAL   A CA  
2081 C  CA  B VAL   A 100 ? 0.2920 0.2473 0.1862 -0.0085 -0.0349 0.0679  100 VAL   A CA  
2082 C  C   A VAL   A 100 ? 0.2437 0.2514 0.1121 -0.0402 -0.0308 0.0377  100 VAL   A C   
2083 C  C   B VAL   A 100 ? 0.3022 0.2699 0.2036 -0.0090 -0.0368 0.0738  100 VAL   A C   
2084 O  O   A VAL   A 100 ? 0.2473 0.2525 0.1354 -0.0392 -0.0118 0.0428  100 VAL   A O   
2085 O  O   B VAL   A 100 ? 0.3040 0.2761 0.2095 -0.0091 -0.0291 0.0637  100 VAL   A O   
2086 C  CB  A VAL   A 100 ? 0.2541 0.2431 0.1520 -0.0441 -0.0322 0.0046  100 VAL   A CB  
2087 C  CB  B VAL   A 100 ? 0.3019 0.2603 0.2262 -0.0089 -0.0363 0.0522  100 VAL   A CB  
2088 C  CG1 A VAL   A 100 ? 0.2531 0.2444 0.1598 -0.0488 -0.0265 0.0086  100 VAL   A CG1 
2089 C  CG1 B VAL   A 100 ? 0.3038 0.2624 0.2422 -0.0093 -0.0388 0.0494  100 VAL   A CG1 
2090 C  CG2 A VAL   A 100 ? 0.2646 0.2442 0.1461 -0.0495 -0.0424 -0.0113 100 VAL   A CG2 
2091 C  CG2 B VAL   A 100 ? 0.3063 0.2664 0.2455 -0.0096 -0.0329 0.0450  100 VAL   A CG2 
2110 N  N   A ASN   A 101 ? 0.2544 0.2606 0.1318 -0.0442 -0.0374 0.0628  101 ASN   A N   
2111 N  N   B ASN   A 101 ? 0.3119 0.2839 0.2262 -0.0099 -0.0423 0.0842  101 ASN   A N   
2112 C  CA  A ASN   A 101 ? 0.2798 0.2749 0.1440 -0.0431 -0.0283 0.0846  101 ASN   A CA  
2113 C  CA  B ASN   A 101 ? 0.3256 0.3005 0.2501 -0.0084 -0.0386 0.0889  101 ASN   A CA  
2114 C  C   A ASN   A 101 ? 0.3070 0.3122 0.1706 -0.0487 0.0018  0.1176  101 ASN   A C   
2115 C  C   B ASN   A 101 ? 0.3373 0.3219 0.2700 -0.0043 -0.0208 0.1014  101 ASN   A C   
2116 O  O   A ASN   A 101 ? 0.3223 0.3180 0.2102 -0.0461 0.0084  0.1010  101 ASN   A O   
2117 O  O   B ASN   A 101 ? 0.3428 0.3248 0.2704 -0.0010 -0.0185 0.1102  101 ASN   A O   
2118 C  CB  A ASN   A 101 ? 0.2810 0.2568 0.1437 -0.0352 -0.0483 0.0694  101 ASN   A CB  
2119 C  CB  B ASN   A 101 ? 0.3276 0.2949 0.2536 -0.0127 -0.0459 0.0780  101 ASN   A CB  
2120 C  CG  A ASN   A 101 ? 0.2787 0.2406 0.1361 -0.0284 -0.0627 0.0368  101 ASN   A CG  
2121 C  CG  B ASN   A 101 ? 0.3298 0.2919 0.2625 -0.0189 -0.0489 0.0637  101 ASN   A CG  
2122 O  OD1 A ASN   A 101 ? 0.2741 0.2397 0.1393 -0.0170 -0.0582 -0.0007 101 ASN   A OD1 
2123 O  OD1 B ASN   A 101 ? 0.3303 0.2905 0.2727 -0.0238 -0.0462 0.0585  101 ASN   A OD1 
2124 N  ND2 A ASN   A 101 ? 0.2815 0.2281 0.1147 -0.0370 -0.0686 0.0440  101 ASN   A ND2 
2125 N  ND2 B ASN   A 101 ? 0.3318 0.2905 0.2628 -0.0209 -0.0503 0.0575  101 ASN   A ND2 
2138 N  N   A LYS   A 102 ? 0.3148 0.3462 0.2125 -0.0526 0.0143  0.1319  102 LYS   A N   
2139 N  N   B LYS   A 102 ? 0.3413 0.3387 0.2970 -0.0062 -0.0045 0.0927  102 LYS   A N   
2140 C  CA  A LYS   A 102 ? 0.3292 0.3818 0.2418 -0.0493 0.0112  0.1234  102 LYS   A CA  
2141 C  CA  B LYS   A 102 ? 0.3469 0.3541 0.3092 -0.0105 0.0050  0.0807  102 LYS   A CA  
2142 C  C   A LYS   A 102 ? 0.3342 0.4044 0.2185 -0.0351 0.0036  0.1164  102 LYS   A C   
2143 C  C   B LYS   A 102 ? 0.3474 0.3597 0.2950 -0.0072 -0.0001 0.0898  102 LYS   A C   
2144 O  O   A LYS   A 102 ? 0.3350 0.4171 0.2231 -0.0306 0.0035  0.1098  102 LYS   A O   
2145 O  O   B LYS   A 102 ? 0.3477 0.3626 0.2863 -0.0049 0.0023  0.1028  102 LYS   A O   
2146 C  CB  A LYS   A 102 ? 0.3421 0.3945 0.2952 -0.0564 0.0025  0.1059  102 LYS   A CB  
2147 C  CB  B LYS   A 102 ? 0.3538 0.3644 0.3402 -0.0171 0.0108  0.0597  102 LYS   A CB  
2148 C  CG  A LYS   A 102 ? 0.3541 0.4060 0.3404 -0.0607 -0.0112 0.0860  102 LYS   A CG  
2149 C  CG  B LYS   A 102 ? 0.3611 0.3740 0.3607 -0.0223 0.0128  0.0404  102 LYS   A CG  
2150 C  CD  A LYS   A 102 ? 0.3660 0.4171 0.3783 -0.0606 -0.0188 0.0637  102 LYS   A CD  
2151 C  CD  B LYS   A 102 ? 0.3702 0.3847 0.3766 -0.0241 0.0155  0.0195  102 LYS   A CD  
2152 C  CE  A LYS   A 102 ? 0.3748 0.4243 0.4121 -0.0583 -0.0245 0.0491  102 LYS   A CE  
2153 C  CE  B LYS   A 102 ? 0.3776 0.3936 0.3933 -0.0235 0.0175  0.0038  102 LYS   A CE  
2154 N  NZ  A LYS   A 102 ? 0.3789 0.4275 0.4236 -0.0582 -0.0289 0.0416  102 LYS   A NZ  
2155 N  NZ  B LYS   A 102 ? 0.3820 0.3993 0.3960 -0.0222 0.0195  -0.0043 102 LYS   A NZ  
2182 N  N   A GLY   A 103 ? 0.3368 0.4156 0.2265 -0.0231 -0.0065 0.0927  103 GLY   A N   
2183 N  N   B GLY   A 103 ? 0.3469 0.3626 0.2868 -0.0041 -0.0113 0.0813  103 GLY   A N   
2184 C  CA  A GLY   A 103 ? 0.3367 0.4217 0.2224 -0.0125 -0.0055 0.0710  103 GLY   A CA  
2185 C  CA  B GLY   A 103 ? 0.3440 0.3616 0.2702 -0.0014 -0.0171 0.0757  103 GLY   A CA  
2186 C  C   A GLY   A 103 ? 0.3318 0.4255 0.2245 -0.0060 0.0031  0.0510  103 GLY   A C   
2187 C  C   B GLY   A 103 ? 0.3361 0.3586 0.2513 0.0020  -0.0186 0.0622  103 GLY   A C   
2188 O  O   A GLY   A 103 ? 0.3382 0.4351 0.2441 0.0013  0.0021  0.0368  103 GLY   A O   
2189 O  O   B GLY   A 103 ? 0.3410 0.3658 0.2607 0.0053  -0.0238 0.0592  103 GLY   A O   
2196 N  N   A GLU   A 104 ? 0.3155 0.4147 0.1919 -0.0119 0.0166  0.0458  104 GLU   A N   
2197 N  N   B GLU   A 104 ? 0.3199 0.3435 0.2132 0.0000  -0.0167 0.0566  104 GLU   A N   
2198 C  CA  A GLU   A 104 ? 0.2950 0.4011 0.1756 -0.0225 0.0238  0.0408  104 GLU   A CA  
2199 C  CA  B GLU   A 104 ? 0.3041 0.3268 0.1832 -0.0050 -0.0185 0.0474  104 GLU   A CA  
2200 C  C   A GLU   A 104 ? 0.3010 0.4141 0.1838 -0.0267 0.0225  0.0183  104 GLU   A C   
2201 C  C   B GLU   A 104 ? 0.2989 0.3206 0.1785 -0.0060 -0.0129 0.0281  104 GLU   A C   
2202 O  O   A GLU   A 104 ? 0.2993 0.4186 0.1977 -0.0271 0.0120  0.0110  104 GLU   A O   
2203 O  O   B GLU   A 104 ? 0.2975 0.3175 0.1912 -0.0052 -0.0187 0.0310  104 GLU   A O   
2204 C  CB  A GLU   A 104 ? 0.2659 0.3743 0.1591 -0.0314 0.0291  0.0610  104 GLU   A CB  
2205 C  CB  B GLU   A 104 ? 0.2951 0.3197 0.1759 -0.0087 -0.0243 0.0559  104 GLU   A CB  
2206 C  CG  A GLU   A 104 ? 0.2456 0.3495 0.1663 -0.0383 0.0251  0.0709  104 GLU   A CG  
2207 C  CG  B GLU   A 104 ? 0.2919 0.3179 0.1886 -0.0103 -0.0317 0.0580  104 GLU   A CG  
2208 C  CD  A GLU   A 104 ? 0.2260 0.3240 0.1584 -0.0418 0.0246  0.0825  104 GLU   A CD  
2209 C  CD  B GLU   A 104 ? 0.2896 0.3182 0.1926 -0.0088 -0.0383 0.0603  104 GLU   A CD  
2210 O  OE1 A GLU   A 104 ? 0.2098 0.3037 0.1236 -0.0412 0.0173  0.0783  104 GLU   A OE1 
2211 O  OE1 B GLU   A 104 ? 0.2883 0.3159 0.1881 -0.0102 -0.0429 0.0618  104 GLU   A OE1 
2212 O  OE2 A GLU   A 104 ? 0.2305 0.3242 0.1847 -0.0472 0.0277  0.0922  104 GLU   A OE2 
2213 O  OE2 B GLU   A 104 ? 0.2917 0.3220 0.2009 -0.0065 -0.0402 0.0570  104 GLU   A OE2 
2226 N  N   A ASP   A 105 ? 0.3083 0.4211 0.1933 -0.0287 0.0287  -0.0033 105 ASP   A N   
2227 N  N   B ASP   A 105 ? 0.2988 0.3190 0.1827 -0.0088 -0.0034 0.0037  105 ASP   A N   
2228 C  CA  A ASP   A 105 ? 0.3094 0.4283 0.2251 -0.0298 0.0338  -0.0275 105 ASP   A CA  
2229 C  CA  B ASP   A 105 ? 0.2953 0.3195 0.1991 -0.0093 0.0077  -0.0278 105 ASP   A CA  
2230 C  C   A ASP   A 105 ? 0.2772 0.4172 0.1966 -0.0393 0.0199  -0.0452 105 ASP   A C   
2231 C  C   B ASP   A 105 ? 0.2783 0.3116 0.1666 -0.0190 0.0049  -0.0429 105 ASP   A C   
2232 O  O   A ASP   A 105 ? 0.2639 0.4177 0.1583 -0.0376 0.0196  -0.0652 105 ASP   A O   
2233 O  O   B ASP   A 105 ? 0.2648 0.3029 0.1112 -0.0199 -0.0037 -0.0665 105 ASP   A O   
2234 C  CB  A ASP   A 105 ? 0.3373 0.4441 0.2828 -0.0215 0.0479  -0.0353 105 ASP   A CB  
2235 C  CB  B ASP   A 105 ? 0.3083 0.3290 0.2477 -0.0016 0.0177  -0.0407 105 ASP   A CB  
2236 C  CG  A ASP   A 105 ? 0.3588 0.4587 0.3340 -0.0148 0.0507  -0.0454 105 ASP   A CG  
2237 C  CG  B ASP   A 105 ? 0.3194 0.3374 0.2929 0.0057  0.0183  -0.0540 105 ASP   A CG  
2238 O  OD1 A ASP   A 105 ? 0.3647 0.4647 0.3427 -0.0118 0.0482  -0.0564 105 ASP   A OD1 
2239 O  OD1 B ASP   A 105 ? 0.3190 0.3389 0.2930 0.0047  0.0163  -0.0614 105 ASP   A OD1 
2240 O  OD2 A ASP   A 105 ? 0.3671 0.4649 0.3668 -0.0157 0.0527  -0.0403 105 ASP   A OD2 
2241 O  OD2 B ASP   A 105 ? 0.3302 0.3426 0.3255 0.0078  0.0132  -0.0519 105 ASP   A OD2 
2250 N  N   A ILE   A 106 ? 0.2572 0.4032 0.2111 -0.0510 -0.0090 -0.0466 106 ILE   A N   
2251 N  N   B ILE   A 106 ? 0.2752 0.3136 0.1938 -0.0265 -0.0023 -0.0356 106 ILE   A N   
2252 C  CA  A ILE   A 106 ? 0.2315 0.3826 0.2259 -0.0617 -0.0318 -0.0581 106 ILE   A CA  
2253 C  CA  B ILE   A 106 ? 0.2688 0.3124 0.2221 -0.0351 -0.0066 -0.0354 106 ILE   A CA  
2254 C  C   A ILE   A 106 ? 0.2070 0.3518 0.2251 -0.0782 -0.0302 -0.0830 106 ILE   A C   
2255 C  C   B ILE   A 106 ? 0.2606 0.2995 0.2304 -0.0421 0.0028  -0.0360 106 ILE   A C   
2256 O  O   A ILE   A 106 ? 0.1875 0.3422 0.2256 -0.0791 -0.0152 -0.0888 106 ILE   A O   
2257 O  O   B ILE   A 106 ? 0.2551 0.2957 0.2280 -0.0405 0.0098  -0.0395 106 ILE   A O   
2258 C  CB  A ILE   A 106 ? 0.2371 0.3914 0.2624 -0.0479 -0.0496 -0.0335 106 ILE   A CB  
2259 C  CB  B ILE   A 106 ? 0.2733 0.3230 0.2570 -0.0325 -0.0185 -0.0261 106 ILE   A CB  
2260 C  CG1 A ILE   A 106 ? 0.2336 0.3893 0.2888 -0.0324 -0.0543 -0.0101 106 ILE   A CG1 
2261 C  CG1 B ILE   A 106 ? 0.2727 0.3239 0.2784 -0.0268 -0.0208 -0.0130 106 ILE   A CG1 
2262 C  CG2 A ILE   A 106 ? 0.2423 0.3967 0.2746 -0.0482 -0.0566 -0.0306 106 ILE   A CG2 
2263 C  CG2 B ILE   A 106 ? 0.2758 0.3283 0.2667 -0.0335 -0.0251 -0.0263 106 ILE   A CG2 
2264 C  CD1 A ILE   A 106 ? 0.2358 0.3852 0.3082 -0.0194 -0.0440 0.0054  106 ILE   A CD1 
2265 C  CD1 B ILE   A 106 ? 0.2736 0.3221 0.2899 -0.0212 -0.0171 -0.0041 106 ILE   A CD1 
2288 N  N   A GLN   A 107 ? 0.2216 0.3331 0.2549 -0.0791 -0.0177 -0.0951 107 GLN   A N   
2289 N  N   B GLN   A 107 ? 0.2623 0.2895 0.2543 -0.0464 0.0089  -0.0344 107 GLN   A N   
2290 C  CA  A GLN   A 107 ? 0.2445 0.3128 0.3089 -0.0649 0.0101  -0.0898 107 GLN   A CA  
2291 C  CA  B GLN   A 107 ? 0.2656 0.2807 0.2897 -0.0464 0.0207  -0.0330 107 GLN   A CA  
2292 C  C   A GLN   A 107 ? 0.2231 0.2673 0.2877 -0.0531 0.0391  -0.0684 107 GLN   A C   
2293 C  C   B GLN   A 107 ? 0.2379 0.2534 0.2695 -0.0480 0.0388  -0.0394 107 GLN   A C   
2294 O  O   A GLN   A 107 ? 0.2205 0.2577 0.3338 -0.0439 0.0567  -0.0777 107 GLN   A O   
2295 O  O   B GLN   A 107 ? 0.2431 0.2512 0.3024 -0.0497 0.0430  -0.0445 107 GLN   A O   
2296 C  CB  A GLN   A 107 ? 0.2831 0.3367 0.3967 -0.0682 0.0001  -0.0894 107 GLN   A CB  
2297 C  CB  B GLN   A 107 ? 0.2926 0.2984 0.3437 -0.0495 0.0109  -0.0208 107 GLN   A CB  
2298 C  CG  A GLN   A 107 ? 0.3186 0.3606 0.4847 -0.0657 -0.0094 -0.0786 107 GLN   A CG  
2299 C  CG  B GLN   A 107 ? 0.3166 0.3135 0.3992 -0.0507 0.0017  -0.0060 107 GLN   A CG  
2300 C  CD  A GLN   A 107 ? 0.3505 0.3781 0.5624 -0.0633 -0.0149 -0.0653 107 GLN   A CD  
2301 C  CD  B GLN   A 107 ? 0.3371 0.3281 0.4528 -0.0489 -0.0048 0.0094  107 GLN   A CD  
2302 O  OE1 A GLN   A 107 ? 0.3592 0.3852 0.5973 -0.0653 -0.0180 -0.0622 107 GLN   A OE1 
2303 O  OE1 B GLN   A 107 ? 0.3450 0.3312 0.4612 -0.0469 -0.0068 0.0207  107 GLN   A OE1 
2304 N  NE2 A GLN   A 107 ? 0.3565 0.3828 0.5878 -0.0617 -0.0163 -0.0626 107 GLN   A NE2 
2305 N  NE2 B GLN   A 107 ? 0.3429 0.3346 0.4656 -0.0485 -0.0086 0.0123  107 GLN   A NE2 
2322 N  N   . LEU   A 108 ? 0.2063 0.2281 0.2240 -0.0498 0.0422  -0.0499 108 LEU   A N   
2323 C  CA  . LEU   A 108 ? 0.1824 0.1821 0.1995 -0.0209 0.0310  -0.0175 108 LEU   A CA  
2324 C  C   . LEU   A 108 ? 0.1597 0.1456 0.1866 -0.0087 0.0209  0.0074  108 LEU   A C   
2325 O  O   . LEU   A 108 ? 0.1535 0.1442 0.2013 -0.0025 0.0267  0.0123  108 LEU   A O   
2326 C  CB  . LEU   A 108 ? 0.1855 0.1905 0.1718 -0.0226 0.0345  -0.0110 108 LEU   A CB  
2327 C  CG  . LEU   A 108 ? 0.1995 0.2137 0.1983 -0.0225 0.0373  -0.0151 108 LEU   A CG  
2328 C  CD1 . LEU   A 108 ? 0.2211 0.2240 0.2008 -0.0320 0.0480  -0.0168 108 LEU   A CD1 
2329 C  CD2 . LEU   A 108 ? 0.2018 0.2351 0.2467 -0.0115 0.0285  -0.0087 108 LEU   A CD2 
2342 N  N   . LEU   A 109 ? 0.1448 0.1414 0.1766 0.0013  0.0183  0.0176  109 LEU   A N   
2343 C  CA  . LEU   A 109 ? 0.1413 0.1334 0.1545 -0.0003 0.0054  0.0192  109 LEU   A CA  
2344 C  C   . LEU   A 109 ? 0.1271 0.1269 0.1519 -0.0056 0.0096  0.0099  109 LEU   A C   
2345 O  O   . LEU   A 109 ? 0.1389 0.1227 0.1728 -0.0031 -0.0004 0.0024  109 LEU   A O   
2346 C  CB  . LEU   A 109 ? 0.1470 0.1393 0.1746 0.0081  0.0013  0.0281  109 LEU   A CB  
2347 C  CG  . LEU   A 109 ? 0.1446 0.1473 0.1851 0.0029  0.0038  0.0359  109 LEU   A CG  
2348 C  CD1 . LEU   A 109 ? 0.1512 0.1414 0.1943 -0.0013 0.0105  0.0151  109 LEU   A CD1 
2349 C  CD2 . LEU   A 109 ? 0.1449 0.1680 0.2103 0.0007  0.0057  0.0387  109 LEU   A CD2 
2361 N  N   . LYS   A 110 ? 0.1315 0.1247 0.1555 -0.0059 0.0006  0.0043  110 LYS   A N   
2362 C  CA  . LYS   A 110 ? 0.1306 0.1196 0.1643 -0.0063 0.0019  0.0117  110 LYS   A CA  
2363 C  C   . LYS   A 110 ? 0.1314 0.1160 0.1497 -0.0080 0.0035  -0.0008 110 LYS   A C   
2364 O  O   . LYS   A 110 ? 0.1270 0.1208 0.1587 -0.0055 0.0035  -0.0033 110 LYS   A O   
2365 C  CB  . LYS   A 110 ? 0.1401 0.1272 0.1884 -0.0056 -0.0089 -0.0054 110 LYS   A CB  
2366 C  CG  . LYS   A 110 ? 0.1400 0.1247 0.1880 -0.0067 -0.0100 -0.0030 110 LYS   A CG  
2367 C  CD  . LYS   A 110 ? 0.1409 0.1272 0.2123 -0.0092 -0.0113 -0.0103 110 LYS   A CD  
2368 C  CE  . LYS   A 110 ? 0.1495 0.1331 0.2203 -0.0088 0.0084  -0.0088 110 LYS   A CE  
2369 N  NZ  . LYS   A 110 ? 0.1479 0.1368 0.2316 -0.0174 0.0166  -0.0051 110 LYS   A NZ  
2383 N  N   . SER   A 111 ? 0.1288 0.1202 0.1485 -0.0023 0.0057  0.0070  111 SER   A N   
2384 C  CA  . SER   A 111 ? 0.1265 0.1249 0.1552 -0.0032 0.0115  0.0033  111 SER   A CA  
2385 C  C   . SER   A 111 ? 0.1195 0.1174 0.1507 -0.0102 0.0073  0.0066  111 SER   A C   
2386 O  O   . SER   A 111 ? 0.1339 0.1119 0.1620 -0.0069 0.0119  0.0077  111 SER   A O   
2387 C  CB  . SER   A 111 ? 0.1475 0.1427 0.1660 -0.0023 0.0129  -0.0081 111 SER   A CB  
2388 O  OG  . SER   A 111 ? 0.1933 0.1634 0.1833 0.0016  0.0277  -0.0219 111 SER   A OG  
2394 N  N   . ALA   A 112 ? 0.1237 0.1129 0.1554 -0.0029 0.0091  0.0054  112 ALA   A N   
2395 C  CA  . ALA   A 112 ? 0.1285 0.1108 0.1476 -0.0049 0.0086  -0.0001 112 ALA   A CA  
2396 C  C   . ALA   A 112 ? 0.1218 0.1061 0.1468 -0.0004 0.0074  0.0046  112 ALA   A C   
2397 O  O   . ALA   A 112 ? 0.1261 0.1078 0.1536 -0.0120 0.0154  0.0083  112 ALA   A O   
2398 C  CB  . ALA   A 112 ? 0.1391 0.1164 0.1538 -0.0054 0.0096  0.0031  112 ALA   A CB  
2404 N  N   . TYR   A 113 ? 0.1151 0.1140 0.1509 -0.0032 0.0085  0.0108  113 TYR   A N   
2405 C  CA  . TYR   A 113 ? 0.1123 0.1136 0.1513 -0.0014 0.0138  0.0109  113 TYR   A CA  
2406 C  C   . TYR   A 113 ? 0.1114 0.1119 0.1382 -0.0072 0.0092  0.0034  113 TYR   A C   
2407 O  O   . TYR   A 113 ? 0.1182 0.1157 0.1544 -0.0042 0.0130  0.0037  113 TYR   A O   
2408 C  CB  . TYR   A 113 ? 0.1135 0.1202 0.1557 -0.0025 0.0030  0.0204  113 TYR   A CB  
2409 C  CG  . TYR   A 113 ? 0.1165 0.1253 0.1487 -0.0069 0.0091  0.0204  113 TYR   A CG  
2410 C  CD1 . TYR   A 113 ? 0.1203 0.1352 0.1425 0.0041  0.0081  0.0289  113 TYR   A CD1 
2411 C  CD2 . TYR   A 113 ? 0.1211 0.1287 0.1489 -0.0070 0.0003  0.0124  113 TYR   A CD2 
2412 C  CE1 . TYR   A 113 ? 0.1216 0.1395 0.1464 0.0016  0.0115  0.0229  113 TYR   A CE1 
2413 C  CE2 . TYR   A 113 ? 0.1193 0.1360 0.1485 -0.0077 -0.0011 0.0222  113 TYR   A CE2 
2414 C  CZ  . TYR   A 113 ? 0.1191 0.1379 0.1483 0.0052  0.0075  0.0262  113 TYR   A CZ  
2415 O  OH  . TYR   A 113 ? 0.1192 0.1524 0.1653 0.0106  0.0075  0.0230  113 TYR   A OH  
2425 N  N   . GLU   A 114 ? 0.1157 0.1112 0.1491 -0.0066 0.0138  0.0120  114 GLU   A N   
2426 C  CA  . GLU   A 114 ? 0.1148 0.1084 0.1575 0.0023  0.0064  0.0140  114 GLU   A CA  
2427 C  C   . GLU   A 114 ? 0.1164 0.1148 0.1552 0.0053  0.0103  0.0110  114 GLU   A C   
2428 O  O   . GLU   A 114 ? 0.1256 0.1152 0.1602 -0.0000 0.0027  0.0100  114 GLU   A O   
2429 C  CB  . GLU   A 114 ? 0.1173 0.1123 0.1609 -0.0043 0.0092  0.0092  114 GLU   A CB  
2430 C  CG  . GLU   A 114 ? 0.1266 0.1178 0.1619 -0.0008 0.0136  0.0047  114 GLU   A CG  
2431 C  CD  . GLU   A 114 ? 0.1344 0.1138 0.1682 -0.0011 -0.0001 0.0076  114 GLU   A CD  
2432 O  OE1 . GLU   A 114 ? 0.1365 0.1158 0.1802 -0.0070 0.0141  0.0011  114 GLU   A OE1 
2433 O  OE2 . GLU   A 114 ? 0.1541 0.1221 0.1940 -0.0098 0.0085  -0.0098 114 GLU   A OE2 
2440 N  N   . ASN   A 115 ? 0.1193 0.1104 0.1421 -0.0018 0.0080  0.0059  115 ASN   A N   
2441 C  CA  . ASN   A 115 ? 0.1221 0.1152 0.1483 -0.0072 0.0088  0.0066  115 ASN   A CA  
2442 C  C   . ASN   A 115 ? 0.1216 0.1089 0.1397 -0.0046 0.0036  0.0085  115 ASN   A C   
2443 O  O   . ASN   A 115 ? 0.1213 0.1269 0.1456 -0.0088 0.0078  0.0150  115 ASN   A O   
2444 C  CB  . ASN   A 115 ? 0.1268 0.1259 0.1432 -0.0123 0.0055  0.0053  115 ASN   A CB  
2445 C  CG  . ASN   A 115 ? 0.1277 0.1479 0.1529 -0.0181 0.0209  0.0085  115 ASN   A CG  
2446 O  OD1 . ASN   A 115 ? 0.1247 0.2396 0.1908 -0.0156 0.0241  0.0266  115 ASN   A OD1 
2447 N  ND2 . ASN   A 115 ? 0.1304 0.1274 0.1492 -0.0145 0.0258  0.0122  115 ASN   A ND2 
2454 N  N   . PHE   A 116 ? 0.1146 0.1139 0.1532 0.0017  0.0115  0.0165  116 PHE   A N   
2455 C  CA  . PHE   A 116 ? 0.1172 0.1211 0.1428 -0.0029 0.0090  0.0199  116 PHE   A CA  
2456 C  C   . PHE   A 116 ? 0.1144 0.1276 0.1475 -0.0050 0.0127  0.0189  116 PHE   A C   
2457 O  O   . PHE   A 116 ? 0.1207 0.1342 0.1586 0.0015  0.0146  0.0230  116 PHE   A O   
2458 C  CB  . PHE   A 116 ? 0.1193 0.1144 0.1571 -0.0045 0.0187  0.0204  116 PHE   A CB  
2459 C  CG  . PHE   A 116 ? 0.1191 0.1142 0.1386 -0.0039 0.0154  0.0145  116 PHE   A CG  
2460 C  CD1 . PHE   A 116 ? 0.1197 0.1162 0.1461 -0.0046 0.0138  0.0109  116 PHE   A CD1 
2461 C  CD2 . PHE   A 116 ? 0.1236 0.1206 0.1589 -0.0058 0.0166  0.0155  116 PHE   A CD2 
2462 C  CE1 . PHE   A 116 ? 0.1234 0.1134 0.1599 -0.0080 0.0073  0.0093  116 PHE   A CE1 
2463 C  CE2 . PHE   A 116 ? 0.1209 0.1197 0.1674 -0.0047 0.0143  0.0092  116 PHE   A CE2 
2464 C  CZ  . PHE   A 116 ? 0.1253 0.1074 0.1597 0.0006  -0.0028 0.0135  116 PHE   A CZ  
2474 N  N   . ASN   A 117 ? 0.1139 0.1234 0.1608 -0.0026 0.0162  0.0202  117 ASN   A N   
2475 C  CA  . ASN   A 117 ? 0.1199 0.1182 0.1662 -0.0006 0.0170  0.0235  117 ASN   A CA  
2476 C  C   . ASN   A 117 ? 0.1212 0.1250 0.1777 0.0029  0.0147  0.0235  117 ASN   A C   
2477 O  O   . ASN   A 117 ? 0.1283 0.1335 0.1968 -0.0031 -0.0043 0.0337  117 ASN   A O   
2478 C  CB  . ASN   A 117 ? 0.1177 0.1196 0.1737 0.0015  0.0155  0.0290  117 ASN   A CB  
2479 C  CG  . ASN   A 117 ? 0.1158 0.1215 0.1743 -0.0014 0.0164  0.0249  117 ASN   A CG  
2480 O  OD1 . ASN   A 117 ? 0.1232 0.1416 0.1867 -0.0098 0.0173  0.0153  117 ASN   A OD1 
2481 N  ND2 . ASN   A 117 ? 0.1119 0.1259 0.1787 0.0001  0.0107  0.0245  117 ASN   A ND2 
2488 N  N   . GLN   A 118 ? 0.1180 0.1257 0.1739 -0.0029 0.0024  0.0261  118 GLN   A N   
2489 C  CA  . GLN   A 118 ? 0.1243 0.1381 0.1750 -0.0045 -0.0009 0.0190  118 GLN   A CA  
2490 C  C   . GLN   A 118 ? 0.1287 0.1523 0.1576 -0.0047 -0.0039 0.0256  118 GLN   A C   
2491 O  O   . GLN   A 118 ? 0.1280 0.1789 0.1856 0.0042  -0.0099 0.0031  118 GLN   A O   
2492 C  CB  . GLN   A 118 ? 0.1248 0.1429 0.1841 -0.0034 0.0074  0.0205  118 GLN   A CB  
2493 C  CG  . GLN   A 118 ? 0.1178 0.1469 0.1798 -0.0019 0.0070  0.0273  118 GLN   A CG  
2494 C  CD  . GLN   A 118 ? 0.1138 0.1490 0.1922 0.0018  0.0104  0.0218  118 GLN   A CD  
2495 O  OE1 . GLN   A 118 ? 0.1222 0.1608 0.2049 0.0147  0.0036  0.0117  118 GLN   A OE1 
2496 N  NE2 . GLN   A 118 ? 0.1292 0.1427 0.1969 0.0015  0.0025  0.0255  118 GLN   A NE2 
2505 N  N   . HIS   A 119 ? 0.1302 0.1416 0.1579 -0.0047 0.0046  0.0272  119 HIS   A N   
2506 C  CA  . HIS   A 119 ? 0.1347 0.1490 0.1685 -0.0090 0.0059  0.0333  119 HIS   A CA  
2507 C  C   . HIS   A 119 ? 0.1443 0.1569 0.1533 -0.0041 0.0044  0.0314  119 HIS   A C   
2508 O  O   . HIS   A 119 ? 0.1480 0.1648 0.1590 -0.0176 0.0043  0.0292  119 HIS   A O   
2509 C  CB  . HIS   A 119 ? 0.1390 0.1467 0.1929 -0.0068 0.0216  0.0329  119 HIS   A CB  
2510 C  CG  . HIS   A 119 ? 0.1419 0.1514 0.2344 -0.0006 0.0128  0.0473  119 HIS   A CG  
2511 N  ND1 . HIS   A 119 ? 0.1513 0.1727 0.2862 -0.0050 0.0084  0.0325  119 HIS   A ND1 
2512 C  CD2 . HIS   A 119 ? 0.1532 0.1597 0.2514 0.0130  0.0313  0.0688  119 HIS   A CD2 
2513 C  CE1 . HIS   A 119 ? 0.1499 0.1678 0.2964 -0.0117 0.0243  0.0508  119 HIS   A CE1 
2514 N  NE2 . HIS   A 119 ? 0.1577 0.1631 0.2827 0.0049  0.0433  0.0698  119 HIS   A NE2 
2522 N  N   . GLU   A 120 ? 0.1558 0.1782 0.1543 -0.0003 -0.0031 0.0563  120 GLU   A N   
2523 C  CA  . GLU   A 120 ? 0.1808 0.2099 0.1869 0.0088  0.0014  0.0916  120 GLU   A CA  
2524 C  C   . GLU   A 120 ? 0.1593 0.1951 0.1598 -0.0050 -0.0019 0.0818  120 GLU   A C   
2525 O  O   . GLU   A 120 ? 0.1552 0.1858 0.1812 -0.0102 0.0003  0.0738  120 GLU   A O   
2526 C  CB  . GLU   A 120 ? 0.2525 0.2763 0.2379 0.0289  -0.0022 0.1482  120 GLU   A CB  
2527 C  CG  . GLU   A 120 ? 0.3538 0.3635 0.3589 0.0396  -0.0012 0.1559  120 GLU   A CG  
2528 C  CD  . GLU   A 120 ? 0.4657 0.4549 0.4899 0.0450  0.0110  0.1406  120 GLU   A CD  
2529 O  OE1 . GLU   A 120 ? 0.4867 0.4631 0.5160 0.0454  0.0141  0.1339  120 GLU   A OE1 
2530 O  OE2 . GLU   A 120 ? 0.5114 0.5056 0.5503 0.0462  0.0170  0.1334  120 GLU   A OE2 
2537 N  N   . VAL   A 121 ? 0.1564 0.1924 0.1339 -0.0055 0.0038  0.0633  121 VAL   A N   
2538 C  CA  . VAL   A 121 ? 0.1594 0.1969 0.1308 -0.0114 0.0125  0.0554  121 VAL   A CA  
2539 C  C   . VAL   A 121 ? 0.1515 0.1791 0.1275 -0.0187 0.0135  0.0463  121 VAL   A C   
2540 O  O   . VAL   A 121 ? 0.1539 0.1812 0.1418 -0.0282 -0.0040 0.0386  121 VAL   A O   
2541 C  CB  . VAL   A 121 ? 0.1978 0.2315 0.1749 0.0018  0.0289  0.0657  121 VAL   A CB  
2542 C  CG1 . VAL   A 121 ? 0.1989 0.2478 0.1782 0.0114  0.0359  0.0666  121 VAL   A CG1 
2543 C  CG2 . VAL   A 121 ? 0.2216 0.2486 0.2263 -0.0057 0.0287  0.0486  121 VAL   A CG2 
2553 N  N   . LEU   A 122 ? 0.1421 0.1554 0.1463 -0.0156 0.0123  0.0434  122 LEU   A N   
2554 C  CA  . LEU   A 122 ? 0.1464 0.1431 0.1452 -0.0192 0.0219  0.0379  122 LEU   A CA  
2555 C  C   . LEU   A 122 ? 0.1399 0.1409 0.1377 -0.0199 0.0070  0.0317  122 LEU   A C   
2556 O  O   . LEU   A 122 ? 0.1428 0.1481 0.1659 -0.0237 0.0040  0.0328  122 LEU   A O   
2557 C  CB  . LEU   A 122 ? 0.1636 0.1483 0.1714 -0.0074 0.0140  0.0437  122 LEU   A CB  
2558 C  CG  . LEU   A 122 ? 0.1659 0.1512 0.1598 -0.0081 0.0205  0.0356  122 LEU   A CG  
2559 C  CD1 . LEU   A 122 ? 0.1798 0.1536 0.1790 -0.0159 0.0207  0.0387  122 LEU   A CD1 
2560 C  CD2 . LEU   A 122 ? 0.1597 0.1433 0.1624 -0.0057 0.0302  0.0219  122 LEU   A CD2 
2572 N  N   . LEU   A 123 ? 0.1343 0.1398 0.1311 -0.0191 0.0039  0.0261  123 LEU   A N   
2573 C  CA  . LEU   A 123 ? 0.1360 0.1389 0.1292 -0.0184 0.0107  0.0290  123 LEU   A CA  
2574 C  C   . LEU   A 123 ? 0.1336 0.1359 0.1173 -0.0122 0.0116  0.0290  123 LEU   A C   
2575 O  O   . LEU   A 123 ? 0.1281 0.1497 0.1273 -0.0217 0.0079  0.0299  123 LEU   A O   
2576 C  CB  . LEU   A 123 ? 0.1493 0.1523 0.1329 -0.0181 0.0191  0.0233  123 LEU   A CB  
2577 C  CG  . LEU   A 123 ? 0.1528 0.1644 0.1445 -0.0171 0.0305  0.0118  123 LEU   A CG  
2578 C  CD1 . LEU   A 123 ? 0.1559 0.1722 0.1671 -0.0077 0.0232  0.0135  123 LEU   A CD1 
2579 C  CD2 . LEU   A 123 ? 0.1658 0.1700 0.1472 -0.0190 0.0206  0.0012  123 LEU   A CD2 
2591 N  N   A ALA   A 124 ? 0.1305 0.1294 0.1095 -0.0092 0.0031  0.0196  124 ALA   A N   
2592 N  N   B ALA   A 124 ? 0.1376 0.1319 0.1257 -0.0190 0.0071  0.0236  124 ALA   A N   
2593 C  CA  A ALA   A 124 ? 0.1191 0.1228 0.1168 -0.0013 0.0001  0.0222  124 ALA   A CA  
2594 C  CA  B ALA   A 124 ? 0.1368 0.1284 0.1439 -0.0241 0.0073  0.0264  124 ALA   A CA  
2595 C  C   A ALA   A 124 ? 0.1136 0.1222 0.1122 -0.0051 0.0093  0.0200  124 ALA   A C   
2596 C  C   B ALA   A 124 ? 0.1254 0.1151 0.1455 -0.0148 0.0153  0.0233  124 ALA   A C   
2597 O  O   A ALA   A 124 ? 0.1175 0.1275 0.1283 -0.0066 0.0126  0.0274  124 ALA   A O   
2598 O  O   B ALA   A 124 ? 0.1218 0.1161 0.1616 -0.0026 0.0253  0.0211  124 ALA   A O   
2599 C  CB  A ALA   A 124 ? 0.1114 0.1172 0.1351 0.0073  0.0001  0.0293  124 ALA   A CB  
2600 C  CB  B ALA   A 124 ? 0.1456 0.1309 0.1526 -0.0318 0.0122  0.0323  124 ALA   A CB  
2611 N  N   A PRO   A 125 ? 0.1129 0.1268 0.1255 -0.0004 0.0105  0.0246  125 PRO   A N   
2612 N  N   B PRO   A 125 ? 0.1119 0.1050 0.1270 -0.0053 0.0150  0.0265  125 PRO   A N   
2613 C  CA  A PRO   A 125 ? 0.1238 0.1355 0.1397 -0.0013 0.0053  0.0210  125 PRO   A CA  
2614 C  CA  B PRO   A 125 ? 0.1172 0.1108 0.1311 -0.0053 0.0136  0.0288  125 PRO   A CA  
2615 C  C   A PRO   A 125 ? 0.1145 0.1391 0.1264 -0.0073 0.0097  0.0244  125 PRO   A C   
2616 C  C   B PRO   A 125 ? 0.1215 0.1193 0.1359 -0.0092 0.0039  0.0299  125 PRO   A C   
2617 O  O   A PRO   A 125 ? 0.1232 0.1389 0.1306 -0.0024 0.0011  0.0112  125 PRO   A O   
2618 O  O   B PRO   A 125 ? 0.1255 0.1181 0.1426 -0.0052 -0.0041 0.0201  125 PRO   A O   
2619 C  CB  A PRO   A 125 ? 0.1338 0.1360 0.1409 -0.0038 0.0078  0.0138  125 PRO   A CB  
2620 C  CB  B PRO   A 125 ? 0.1133 0.1041 0.1183 -0.0057 0.0207  0.0282  125 PRO   A CB  
2621 C  CG  A PRO   A 125 ? 0.1365 0.1324 0.1521 -0.0065 0.0038  0.0156  125 PRO   A CG  
2622 C  CG  B PRO   A 125 ? 0.1071 0.0940 0.1136 -0.0018 0.0286  0.0182  125 PRO   A CG  
2623 C  CD  A PRO   A 125 ? 0.1214 0.1328 0.1420 -0.0000 0.0089  0.0148  125 PRO   A CD  
2624 C  CD  B PRO   A 125 ? 0.1049 0.0919 0.1179 -0.0043 0.0198  0.0181  125 PRO   A CD  
2639 N  N   A LEU   A 126 ? 0.1064 0.1488 0.1356 -0.0013 0.0070  0.0205  126 LEU   A N   
2640 N  N   B LEU   A 126 ? 0.1279 0.1368 0.1592 -0.0030 -0.0047 0.0178  126 LEU   A N   
2641 C  CA  A LEU   A 126 ? 0.1083 0.1446 0.1452 -0.0044 0.0030  0.0217  126 LEU   A CA  
2642 C  CA  B LEU   A 126 ? 0.1347 0.1386 0.1683 -0.0031 -0.0074 0.0173  126 LEU   A CA  
2643 C  C   A LEU   A 126 ? 0.1217 0.1426 0.1428 0.0070  -0.0046 0.0249  126 LEU   A C   
2644 C  C   B LEU   A 126 ? 0.1312 0.1338 0.1429 -0.0014 -0.0049 0.0125  126 LEU   A C   
2645 O  O   A LEU   A 126 ? 0.1338 0.1438 0.1591 0.0150  0.0048  0.0280  126 LEU   A O   
2646 O  O   B LEU   A 126 ? 0.1410 0.1363 0.1467 -0.0064 0.0027  0.0121  126 LEU   A O   
2647 C  CB  A LEU   A 126 ? 0.1098 0.1442 0.1476 -0.0064 0.0039  0.0232  126 LEU   A CB  
2648 C  CB  B LEU   A 126 ? 0.1483 0.1549 0.1976 -0.0060 -0.0159 0.0215  126 LEU   A CB  
2649 C  CG  A LEU   A 126 ? 0.1089 0.1636 0.1576 -0.0115 0.0019  0.0242  126 LEU   A CG  
2650 C  CG  B LEU   A 126 ? 0.1570 0.1698 0.2313 -0.0044 -0.0177 0.0281  126 LEU   A CG  
2651 C  CD1 A LEU   A 126 ? 0.1165 0.1771 0.1511 -0.0183 -0.0040 0.0194  126 LEU   A CD1 
2652 C  CD1 B LEU   A 126 ? 0.1583 0.1767 0.2464 -0.0025 -0.0263 0.0248  126 LEU   A CD1 
2653 C  CD2 A LEU   A 126 ? 0.1274 0.1578 0.1712 -0.0234 0.0081  0.0337  126 LEU   A CD2 
2654 C  CD2 B LEU   A 126 ? 0.1633 0.1714 0.2414 -0.0090 -0.0169 0.0323  126 LEU   A CD2 
2677 N  N   A LEU   A 127 ? 0.1310 0.1423 0.1548 0.0069  0.0036  0.0219  127 LEU   A N   
2678 N  N   B LEU   A 127 ? 0.1257 0.1294 0.1326 0.0003  0.0051  0.0204  127 LEU   A N   
2679 C  CA  A LEU   A 127 ? 0.1351 0.1376 0.1426 0.0018  -0.0005 0.0189  127 LEU   A CA  
2680 C  CA  B LEU   A 127 ? 0.1235 0.1319 0.1384 -0.0028 0.0031  0.0164  127 LEU   A CA  
2681 C  C   A LEU   A 127 ? 0.1369 0.1267 0.1251 0.0023  -0.0091 0.0158  127 LEU   A C   
2682 C  C   B LEU   A 127 ? 0.1242 0.1311 0.1460 -0.0065 -0.0071 0.0033  127 LEU   A C   
2683 O  O   A LEU   A 127 ? 0.1457 0.1258 0.1306 -0.0024 -0.0077 0.0143  127 LEU   A O   
2684 O  O   B LEU   A 127 ? 0.1244 0.1325 0.1389 -0.0182 0.0080  0.0078  127 LEU   A O   
2685 C  CB  A LEU   A 127 ? 0.1391 0.1367 0.1343 0.0074  0.0019  0.0187  127 LEU   A CB  
2686 C  CB  B LEU   A 127 ? 0.1267 0.1436 0.1440 0.0030  0.0011  0.0100  127 LEU   A CB  
2687 C  CG  A LEU   A 127 ? 0.1386 0.1289 0.1263 0.0039  -0.0030 0.0211  127 LEU   A CG  
2688 C  CG  B LEU   A 127 ? 0.1331 0.1582 0.1448 0.0050  -0.0027 0.0144  127 LEU   A CG  
2689 C  CD1 A LEU   A 127 ? 0.1415 0.1236 0.1359 -0.0039 -0.0033 0.0144  127 LEU   A CD1 
2690 C  CD1 B LEU   A 127 ? 0.1319 0.1667 0.1656 0.0116  0.0011  0.0160  127 LEU   A CD1 
2691 C  CD2 A LEU   A 127 ? 0.1514 0.1218 0.1325 0.0092  -0.0168 0.0225  127 LEU   A CD2 
2692 C  CD2 B LEU   A 127 ? 0.1463 0.1667 0.1433 0.0007  -0.0130 0.0090  127 LEU   A CD2 
2715 N  N   A SER   A 128 ? 0.1376 0.1268 0.1169 -0.0009 -0.0012 0.0192  128 SER   A N   
2716 N  N   B SER   A 128 ? 0.1308 0.1298 0.1620 -0.0063 -0.0183 0.0001  128 SER   A N   
2717 C  CA  A SER   A 128 ? 0.1441 0.1257 0.1168 0.0006  0.0025  0.0179  128 SER   A CA  
2718 C  CA  B SER   A 128 ? 0.1369 0.1282 0.1601 -0.0015 -0.0184 0.0012  128 SER   A CA  
2719 C  C   A SER   A 128 ? 0.1500 0.1316 0.1150 0.0087  0.0008  0.0193  128 SER   A C   
2720 C  C   B SER   A 128 ? 0.1443 0.1293 0.1576 -0.0014 -0.0280 0.0147  128 SER   A C   
2721 O  O   A SER   A 128 ? 0.1548 0.1528 0.1322 0.0129  0.0068  0.0135  128 SER   A O   
2722 O  O   B SER   A 128 ? 0.1442 0.1365 0.1606 -0.0019 -0.0302 0.0121  128 SER   A O   
2723 C  CB  A SER   A 128 ? 0.1386 0.1233 0.1153 -0.0024 -0.0009 0.0151  128 SER   A CB  
2724 C  CB  B SER   A 128 ? 0.1390 0.1349 0.1673 -0.0022 -0.0143 0.0078  128 SER   A CB  
2725 O  OG  A SER   A 128 ? 0.1424 0.1310 0.1184 -0.0004 0.0012  0.0128  128 SER   A OG  
2726 O  OG  B SER   A 128 ? 0.1397 0.1423 0.1652 -0.0031 -0.0089 0.0192  128 SER   A OG  
2737 N  N   A ALA   A 129 ? 0.1429 0.1341 0.1209 0.0048  -0.0033 0.0196  129 ALA   A N   
2738 N  N   B ALA   A 129 ? 0.1450 0.1382 0.1717 -0.0003 -0.0335 0.0193  129 ALA   A N   
2739 C  CA  A ALA   A 129 ? 0.1377 0.1344 0.1230 0.0015  -0.0039 0.0144  129 ALA   A CA  
2740 C  CA  B ALA   A 129 ? 0.1542 0.1450 0.1833 0.0005  -0.0231 0.0139  129 ALA   A CA  
2741 C  C   A ALA   A 129 ? 0.1408 0.1327 0.1347 0.0008  -0.0067 -0.0028 129 ALA   A C   
2742 C  C   B ALA   A 129 ? 0.1671 0.1479 0.1639 0.0010  -0.0242 0.0149  129 ALA   A C   
2743 O  O   A ALA   A 129 ? 0.1474 0.1409 0.1389 -0.0101 0.0038  0.0066  129 ALA   A O   
2744 O  O   B ALA   A 129 ? 0.1710 0.1530 0.1471 -0.0022 -0.0252 0.0288  129 ALA   A O   
2745 C  CB  A ALA   A 129 ? 0.1388 0.1441 0.1393 -0.0010 0.0032  0.0130  129 ALA   A CB  
2746 C  CB  B ALA   A 129 ? 0.1554 0.1536 0.2015 -0.0021 -0.0169 0.0119  129 ALA   A CB  
2757 N  N   A GLY   A 130 ? 0.1427 0.1225 0.1779 0.0007  -0.0015 -0.0123 130 GLY   A N   
2758 N  N   B GLY   A 130 ? 0.1729 0.1437 0.1689 -0.0013 -0.0176 0.0097  130 GLY   A N   
2759 C  CA  A GLY   A 130 ? 0.1659 0.1290 0.1936 -0.0001 -0.0060 -0.0078 130 GLY   A CA  
2760 C  CA  B GLY   A 130 ? 0.1874 0.1469 0.1661 0.0000  -0.0063 0.0015  130 GLY   A CA  
2761 C  C   A GLY   A 130 ? 0.1632 0.1317 0.1892 0.0019  -0.0217 -0.0008 130 GLY   A C   
2762 C  C   B GLY   A 130 ? 0.1872 0.1480 0.1530 0.0017  0.0009  -0.0036 130 GLY   A C   
2763 O  O   A GLY   A 130 ? 0.1657 0.1310 0.2001 0.0082  -0.0370 0.0035  130 GLY   A O   
2764 O  O   B GLY   A 130 ? 0.1880 0.1495 0.1594 -0.0004 -0.0067 0.0027  130 GLY   A O   
2771 N  N   A ILE   A 131 ? 0.1622 0.1270 0.1763 -0.0038 -0.0247 0.0175  131 ILE   A N   
2772 N  N   B ILE   A 131 ? 0.1895 0.1445 0.1511 0.0068  0.0079  -0.0040 131 ILE   A N   
2773 C  CA  A ILE   A 131 ? 0.1681 0.1287 0.1512 -0.0047 -0.0376 0.0210  131 ILE   A CA  
2774 C  CA  B ILE   A 131 ? 0.1936 0.1486 0.1436 0.0077  0.0009  -0.0073 131 ILE   A CA  
2775 C  C   A ILE   A 131 ? 0.1683 0.1349 0.1438 -0.0036 -0.0346 0.0277  131 ILE   A C   
2776 C  C   B ILE   A 131 ? 0.1945 0.1523 0.1484 0.0078  -0.0022 0.0016  131 ILE   A C   
2777 O  O   A ILE   A 131 ? 0.1815 0.1416 0.1614 0.0016  -0.0339 0.0257  131 ILE   A O   
2778 O  O   B ILE   A 131 ? 0.1980 0.1501 0.1615 0.0107  -0.0038 0.0032  131 ILE   A O   
2779 C  CB  A ILE   A 131 ? 0.1721 0.1409 0.1739 -0.0067 -0.0434 0.0088  131 ILE   A CB  
2780 C  CB  B ILE   A 131 ? 0.1953 0.1549 0.1626 0.0097  -0.0050 -0.0183 131 ILE   A CB  
2781 C  CG1 A ILE   A 131 ? 0.1742 0.1670 0.1840 -0.0087 -0.0406 -0.0014 131 ILE   A CG1 
2782 C  CG1 B ILE   A 131 ? 0.2036 0.1742 0.1762 0.0148  -0.0146 -0.0277 131 ILE   A CG1 
2783 C  CG2 A ILE   A 131 ? 0.1763 0.1345 0.1940 -0.0059 -0.0422 -0.0089 131 ILE   A CG2 
2784 C  CG2 B ILE   A 131 ? 0.1913 0.1451 0.1786 0.0134  -0.0090 -0.0241 131 ILE   A CG2 
2785 C  CD1 A ILE   A 131 ? 0.1800 0.1798 0.2090 -0.0085 -0.0390 -0.0162 131 ILE   A CD1 
2786 C  CD1 B ILE   A 131 ? 0.2082 0.1871 0.2002 0.0184  -0.0232 -0.0269 131 ILE   A CD1 
2809 N  N   A PHE   A 132 ? 0.1589 0.1311 0.1349 0.0028  -0.0258 0.0232  132 PHE   A N   
2810 N  N   B PHE   A 132 ? 0.1892 0.1553 0.1460 0.0106  -0.0024 0.0003  132 PHE   A N   
2811 C  CA  A PHE   A 132 ? 0.1644 0.1316 0.1333 -0.0017 -0.0156 0.0166  132 PHE   A CA  
2812 C  CA  B PHE   A 132 ? 0.1910 0.1628 0.1440 0.0085  -0.0074 -0.0037 132 PHE   A CA  
2813 C  C   A PHE   A 132 ? 0.1719 0.1428 0.1351 -0.0049 -0.0141 0.0192  132 PHE   A C   
2814 C  C   B PHE   A 132 ? 0.1960 0.1698 0.1533 0.0052  -0.0213 0.0045  132 PHE   A C   
2815 O  O   A PHE   A 132 ? 0.1731 0.1487 0.1377 -0.0138 -0.0062 0.0116  132 PHE   A O   
2816 O  O   B PHE   A 132 ? 0.2035 0.1752 0.1554 -0.0017 -0.0142 0.0104  132 PHE   A O   
2817 C  CB  A PHE   A 132 ? 0.1595 0.1237 0.1269 0.0015  -0.0158 0.0280  132 PHE   A CB  
2818 C  CB  B PHE   A 132 ? 0.1861 0.1620 0.1392 0.0132  -0.0036 -0.0072 132 PHE   A CB  
2819 C  CG  A PHE   A 132 ? 0.1576 0.1264 0.1242 0.0068  -0.0198 0.0207  132 PHE   A CG  
2820 C  CG  B PHE   A 132 ? 0.1809 0.1679 0.1319 0.0187  0.0042  -0.0091 132 PHE   A CG  
2821 C  CD1 A PHE   A 132 ? 0.1559 0.1371 0.1329 0.0096  -0.0137 0.0036  132 PHE   A CD1 
2822 C  CD1 B PHE   A 132 ? 0.1773 0.1739 0.1411 0.0186  0.0081  -0.0139 132 PHE   A CD1 
2823 C  CD2 A PHE   A 132 ? 0.1618 0.1444 0.1453 0.0142  -0.0331 0.0065  132 PHE   A CD2 
2824 C  CD2 B PHE   A 132 ? 0.1792 0.1739 0.1324 0.0227  0.0117  -0.0171 132 PHE   A CD2 
2825 C  CE1 A PHE   A 132 ? 0.1530 0.1450 0.1250 0.0096  -0.0215 -0.0039 132 PHE   A CE1 
2826 C  CE1 B PHE   A 132 ? 0.1759 0.1767 0.1292 0.0186  0.0114  -0.0140 132 PHE   A CE1 
2827 C  CE2 A PHE   A 132 ? 0.1584 0.1578 0.1608 0.0181  -0.0321 0.0045  132 PHE   A CE2 
2828 C  CE2 B PHE   A 132 ? 0.1774 0.1789 0.1340 0.0257  0.0170  -0.0128 132 PHE   A CE2 
2829 C  CZ  A PHE   A 132 ? 0.1512 0.1531 0.1478 0.0084  -0.0340 0.0059  132 PHE   A CZ  
2830 C  CZ  B PHE   A 132 ? 0.1749 0.1773 0.1235 0.0216  0.0141  -0.0086 132 PHE   A CZ  
2849 N  N   A GLY   A 133 ? 0.1785 0.1522 0.1344 -0.0067 -0.0217 0.0200  133 GLY   A N   
2850 N  N   B GLY   A 133 ? 0.1929 0.1704 0.1507 0.0043  -0.0360 0.0045  133 GLY   A N   
2851 C  CA  A GLY   A 133 ? 0.1824 0.1684 0.1434 -0.0084 -0.0253 0.0086  133 GLY   A CA  
2852 C  CA  B GLY   A 133 ? 0.1876 0.1752 0.1448 0.0026  -0.0393 -0.0026 133 GLY   A CA  
2853 C  C   A GLY   A 133 ? 0.1860 0.1820 0.1465 -0.0092 -0.0374 0.0018  133 GLY   A C   
2854 C  C   B GLY   A 133 ? 0.1835 0.1803 0.1448 0.0031  -0.0494 -0.0080 133 GLY   A C   
2855 O  O   A GLY   A 133 ? 0.1995 0.1996 0.1719 -0.0118 -0.0437 -0.0164 133 GLY   A O   
2856 O  O   B GLY   A 133 ? 0.1881 0.1929 0.1614 0.0051  -0.0586 -0.0148 133 GLY   A O   
2863 N  N   A ALA   A 134 ? 0.1800 0.1724 0.1429 -0.0143 -0.0271 0.0064  134 ALA   A N   
2864 N  N   B ALA   A 134 ? 0.1784 0.1699 0.1373 -0.0013 -0.0410 -0.0090 134 ALA   A N   
2865 C  CA  A ALA   A 134 ? 0.1789 0.1729 0.1709 -0.0139 -0.0261 0.0054  134 ALA   A CA  
2866 C  CA  B ALA   A 134 ? 0.1761 0.1669 0.1500 -0.0003 -0.0352 -0.0087 134 ALA   A CA  
2867 C  C   A ALA   A 134 ? 0.1802 0.1824 0.1837 -0.0123 -0.0234 0.0179  134 ALA   A C   
2868 C  C   B ALA   A 134 ? 0.1751 0.1720 0.1556 -0.0003 -0.0355 0.0024  134 ALA   A C   
2869 O  O   A ALA   A 134 ? 0.1886 0.1924 0.2082 -0.0071 -0.0015 0.0281  134 ALA   A O   
2870 O  O   B ALA   A 134 ? 0.1814 0.1789 0.1761 0.0052  -0.0186 0.0079  134 ALA   A O   
2871 C  CB  A ALA   A 134 ? 0.1869 0.1665 0.1981 -0.0128 -0.0244 0.0002  134 ALA   A CB  
2872 C  CB  B ALA   A 134 ? 0.1801 0.1603 0.1725 0.0014  -0.0305 -0.0137 134 ALA   A CB  
2883 N  N   A ASP   A 135 ? 0.1823 0.1893 0.2021 -0.0169 -0.0310 0.0287  135 ASP   A N   
2884 N  N   B ASP   A 135 ? 0.1766 0.1795 0.1768 -0.0073 -0.0395 0.0106  135 ASP   A N   
2885 C  CA  A ASP   A 135 ? 0.1799 0.2054 0.2312 -0.0221 -0.0449 0.0410  135 ASP   A CA  
2886 C  CA  B ASP   A 135 ? 0.1751 0.1948 0.2112 -0.0133 -0.0447 0.0224  135 ASP   A CA  
2887 C  C   A ASP   A 135 ? 0.1680 0.1969 0.2242 -0.0152 -0.0346 0.0515  135 ASP   A C   
2888 C  C   B ASP   A 135 ? 0.1646 0.1931 0.2137 -0.0107 -0.0338 0.0412  135 ASP   A C   
2889 O  O   A ASP   A 135 ? 0.1654 0.1855 0.2263 -0.0177 -0.0308 0.0527  135 ASP   A O   
2890 O  O   B ASP   A 135 ? 0.1617 0.1852 0.2109 -0.0137 -0.0303 0.0431  135 ASP   A O   
2891 C  CB  A ASP   A 135 ? 0.1941 0.2316 0.2604 -0.0356 -0.0600 0.0342  135 ASP   A CB  
2892 C  CB  B ASP   A 135 ? 0.1862 0.2128 0.2358 -0.0214 -0.0557 0.0148  135 ASP   A CB  
2893 C  CG  A ASP   A 135 ? 0.2081 0.2510 0.2915 -0.0449 -0.0595 0.0360  135 ASP   A CG  
2894 C  CG  B ASP   A 135 ? 0.1942 0.2274 0.2580 -0.0235 -0.0623 0.0149  135 ASP   A CG  
2895 O  OD1 A ASP   A 135 ? 0.2043 0.2609 0.2933 -0.0508 -0.0700 0.0508  135 ASP   A OD1 
2896 O  OD1 B ASP   A 135 ? 0.1964 0.2299 0.2768 -0.0192 -0.0589 0.0235  135 ASP   A OD1 
2897 O  OD2 A ASP   A 135 ? 0.2301 0.2625 0.3310 -0.0418 -0.0355 0.0318  135 ASP   A OD2 
2898 O  OD2 B ASP   A 135 ? 0.1969 0.2354 0.2722 -0.0290 -0.0683 0.0093  135 ASP   A OD2 
2907 N  N   . PRO   A 136 ? 0.1532 0.1964 0.2284 -0.0015 -0.0218 0.0616  136 PRO   A N   
2908 C  CA  . PRO   A 136 ? 0.1444 0.1946 0.2409 -0.0014 -0.0106 0.0506  136 PRO   A CA  
2909 C  C   . PRO   A 136 ? 0.1285 0.1867 0.2222 0.0008  -0.0097 0.0432  136 PRO   A C   
2910 O  O   . PRO   A 136 ? 0.1244 0.1806 0.2107 -0.0031 0.0002  0.0371  136 PRO   A O   
2911 C  CB  . PRO   A 136 ? 0.1624 0.1946 0.2719 0.0057  -0.0043 0.0569  136 PRO   A CB  
2912 C  CG  . PRO   A 136 ? 0.1750 0.2087 0.2914 0.0116  -0.0057 0.0563  136 PRO   A CG  
2913 C  CD  . PRO   A 136 ? 0.1644 0.2061 0.2688 0.0144  -0.0048 0.0721  136 PRO   A CD  
2921 N  N   A ILE   A 137 ? 0.1222 0.1851 0.2328 -0.0021 -0.0212 0.0423  137 ILE   A N   
2922 N  N   B ILE   A 137 ? 0.1342 0.1886 0.2254 0.0022  -0.0169 0.0368  137 ILE   A N   
2923 C  CA  A ILE   A 137 ? 0.1253 0.1976 0.2327 -0.0148 -0.0244 0.0382  137 ILE   A CA  
2924 C  CA  B ILE   A 137 ? 0.1462 0.1988 0.2234 -0.0029 -0.0200 0.0290  137 ILE   A CA  
2925 C  C   A ILE   A 137 ? 0.1312 0.1885 0.2222 -0.0190 -0.0238 0.0358  137 ILE   A C   
2926 C  C   B ILE   A 137 ? 0.1450 0.1932 0.2152 -0.0053 -0.0168 0.0280  137 ILE   A C   
2927 O  O   A ILE   A 137 ? 0.1358 0.1829 0.2238 -0.0231 -0.0229 0.0343  137 ILE   A O   
2928 O  O   B ILE   A 137 ? 0.1469 0.1911 0.2182 -0.0083 -0.0128 0.0294  137 ILE   A O   
2929 C  CB  A ILE   A 137 ? 0.1292 0.2234 0.2458 -0.0173 -0.0289 0.0417  137 ILE   A CB  
2930 C  CB  B ILE   A 137 ? 0.1635 0.2163 0.2374 -0.0030 -0.0272 0.0256  137 ILE   A CB  
2931 C  CG1 A ILE   A 137 ? 0.1380 0.2465 0.2585 -0.0094 -0.0237 0.0510  137 ILE   A CG1 
2932 C  CG1 B ILE   A 137 ? 0.1782 0.2330 0.2496 0.0046  -0.0315 0.0281  137 ILE   A CG1 
2933 C  CG2 A ILE   A 137 ? 0.1458 0.2298 0.2692 -0.0251 -0.0415 0.0391  137 ILE   A CG2 
2934 C  CG2 B ILE   A 137 ? 0.1744 0.2196 0.2508 -0.0087 -0.0296 0.0216  137 ILE   A CG2 
2935 C  CD1 A ILE   A 137 ? 0.1557 0.2635 0.2701 -0.0032 -0.0092 0.0526  137 ILE   A CD1 
2936 C  CD1 B ILE   A 137 ? 0.1904 0.2436 0.2647 0.0082  -0.0266 0.0292  137 ILE   A CD1 
2959 N  N   A HIS   A 138 ? 0.1347 0.1990 0.2061 -0.0132 -0.0128 0.0289  138 HIS   A N   
2960 N  N   B HIS   A 138 ? 0.1436 0.1975 0.2020 -0.0037 -0.0110 0.0215  138 HIS   A N   
2961 C  CA  A HIS   A 138 ? 0.1446 0.2009 0.1965 -0.0122 -0.0092 0.0243  138 HIS   A CA  
2962 C  CA  B HIS   A 138 ? 0.1454 0.1961 0.1943 -0.0053 -0.0097 0.0162  138 HIS   A CA  
2963 C  C   A HIS   A 138 ? 0.1337 0.1867 0.1818 -0.0084 -0.0079 0.0307  138 HIS   A C   
2964 C  C   B HIS   A 138 ? 0.1355 0.1861 0.1832 -0.0052 -0.0099 0.0274  138 HIS   A C   
2965 O  O   A HIS   A 138 ? 0.1416 0.1809 0.1834 -0.0142 0.0004  0.0207  138 HIS   A O   
2966 O  O   B HIS   A 138 ? 0.1424 0.1829 0.1833 -0.0094 -0.0061 0.0211  138 HIS   A O   
2967 C  CB  A HIS   A 138 ? 0.1622 0.2182 0.1928 -0.0186 -0.0153 0.0163  138 HIS   A CB  
2968 C  CB  B HIS   A 138 ? 0.1550 0.2062 0.1943 -0.0091 -0.0139 0.0009  138 HIS   A CB  
2969 C  CG  A HIS   A 138 ? 0.1827 0.2320 0.1964 -0.0233 -0.0171 0.0147  138 HIS   A CG  
2970 C  CG  B HIS   A 138 ? 0.1666 0.2141 0.1999 -0.0119 -0.0173 -0.0103 138 HIS   A CG  
2971 N  ND1 A HIS   A 138 ? 0.1963 0.2398 0.2198 -0.0264 -0.0148 0.0095  138 HIS   A ND1 
2972 N  ND1 B HIS   A 138 ? 0.1754 0.2201 0.2173 -0.0139 -0.0177 -0.0195 138 HIS   A ND1 
2973 C  CD2 A HIS   A 138 ? 0.1874 0.2363 0.1951 -0.0217 -0.0140 0.0160  138 HIS   A CD2 
2974 C  CD2 B HIS   A 138 ? 0.1675 0.2142 0.2015 -0.0088 -0.0178 -0.0116 138 HIS   A CD2 
2975 C  CE1 A HIS   A 138 ? 0.2020 0.2430 0.2214 -0.0197 -0.0129 0.0062  138 HIS   A CE1 
2976 C  CE1 B HIS   A 138 ? 0.1775 0.2203 0.2163 -0.0099 -0.0182 -0.0225 138 HIS   A CE1 
2977 N  NE2 A HIS   A 138 ? 0.1964 0.2411 0.2019 -0.0187 -0.0081 0.0101  138 HIS   A NE2 
2978 N  NE2 B HIS   A 138 ? 0.1727 0.2177 0.2082 -0.0078 -0.0160 -0.0201 138 HIS   A NE2 
2993 N  N   . SER   A 139 ? 0.1243 0.1788 0.1840 -0.0058 -0.0070 0.0409  139 SER   A N   
2994 C  CA  . SER   A 139 ? 0.1200 0.1698 0.1805 -0.0076 -0.0102 0.0444  139 SER   A CA  
2995 C  C   . SER   A 139 ? 0.1177 0.1546 0.1738 -0.0073 -0.0032 0.0352  139 SER   A C   
2996 O  O   . SER   A 139 ? 0.1152 0.1507 0.1860 -0.0107 -0.0005 0.0301  139 SER   A O   
2997 C  CB  . SER   A 139 ? 0.1213 0.1686 0.1811 -0.0113 -0.0115 0.0477  139 SER   A CB  
2998 O  OG  . SER   A 139 ? 0.1297 0.1654 0.1844 -0.0153 -0.0122 0.0515  139 SER   A OG  
3005 N  N   . LEU   A 140 ? 0.1173 0.1533 0.1743 -0.0046 -0.0020 0.0366  140 LEU   A N   
3006 C  CA  . LEU   A 140 ? 0.1176 0.1508 0.1733 -0.0090 0.0016  0.0355  140 LEU   A CA  
3007 C  C   . LEU   A 140 ? 0.1141 0.1588 0.1710 -0.0141 -0.0015 0.0331  140 LEU   A C   
3008 O  O   . LEU   A 140 ? 0.1222 0.1563 0.1867 -0.0052 -0.0025 0.0280  140 LEU   A O   
3009 C  CB  . LEU   A 140 ? 0.1177 0.1548 0.1766 -0.0084 -0.0009 0.0257  140 LEU   A CB  
3010 C  CG  . LEU   A 140 ? 0.1200 0.1666 0.1884 -0.0135 0.0044  0.0334  140 LEU   A CG  
3011 C  CD1 . LEU   A 140 ? 0.1276 0.1694 0.1958 -0.0109 -0.0007 0.0337  140 LEU   A CD1 
3012 C  CD2 . LEU   A 140 ? 0.1270 0.1780 0.2090 -0.0110 0.0157  0.0453  140 LEU   A CD2 
3024 N  N   . ARG   A 141 ? 0.1220 0.1630 0.1922 -0.0116 -0.0031 0.0306  141 ARG   A N   
3025 C  CA  . ARG   A 141 ? 0.1364 0.1761 0.2021 -0.0271 -0.0104 0.0098  141 ARG   A CA  
3026 C  C   . ARG   A 141 ? 0.1326 0.1613 0.1859 -0.0197 -0.0063 0.0142  141 ARG   A C   
3027 O  O   . ARG   A 141 ? 0.1288 0.1579 0.1982 -0.0174 0.0035  0.0134  141 ARG   A O   
3028 C  CB  . ARG   A 141 ? 0.1546 0.2055 0.2330 -0.0350 -0.0144 -0.0054 141 ARG   A CB  
3029 C  CG  . ARG   A 141 ? 0.1882 0.2477 0.2688 -0.0341 0.0143  -0.0115 141 ARG   A CG  
3030 C  CD  . ARG   A 141 ? 0.2148 0.2797 0.2905 -0.0428 0.0190  -0.0228 141 ARG   A CD  
3031 N  NE  . ARG   A 141 ? 0.2061 0.3041 0.3007 -0.0467 0.0043  -0.0236 141 ARG   A NE  
3032 C  CZ  . ARG   A 141 ? 0.2122 0.3254 0.3096 -0.0658 0.0172  -0.0124 141 ARG   A CZ  
3033 N  NH1 . ARG   A 141 ? 0.2027 0.3312 0.3038 -0.0771 0.0498  -0.0268 141 ARG   A NH1 
3034 N  NH2 . ARG   A 141 ? 0.2159 0.3325 0.3317 -0.0640 -0.0022 0.0025  141 ARG   A NH2 
3048 N  N   . VAL   A 142 ? 0.1251 0.1541 0.1779 -0.0133 -0.0041 0.0082  142 VAL   A N   
3049 C  CA  . VAL   A 142 ? 0.1284 0.1500 0.1785 -0.0105 0.0092  0.0132  142 VAL   A CA  
3050 C  C   . VAL   A 142 ? 0.1145 0.1411 0.1779 -0.0130 0.0066  0.0136  142 VAL   A C   
3051 O  O   . VAL   A 142 ? 0.1199 0.1419 0.1858 -0.0003 0.0046  0.0124  142 VAL   A O   
3052 C  CB  . VAL   A 142 ? 0.1369 0.1567 0.1696 -0.0096 0.0067  0.0183  142 VAL   A CB  
3053 C  CG1 . VAL   A 142 ? 0.1376 0.1535 0.1770 -0.0168 0.0106  0.0134  142 VAL   A CG1 
3054 C  CG2 . VAL   A 142 ? 0.1500 0.1735 0.2011 -0.0051 -0.0006 0.0196  142 VAL   A CG2 
3064 N  N   . CYS   A 143 ? 0.1198 0.1409 0.1689 -0.0102 0.0038  0.0109  143 CYS   A N   
3065 C  CA  . CYS   A 143 ? 0.1172 0.1401 0.1767 -0.0111 0.0052  0.0137  143 CYS   A CA  
3066 C  C   . CYS   A 143 ? 0.1175 0.1420 0.1847 -0.0079 0.0076  0.0184  143 CYS   A C   
3067 O  O   . CYS   A 143 ? 0.1175 0.1389 0.1849 -0.0026 0.0037  0.0271  143 CYS   A O   
3068 C  CB  . CYS   A 143 ? 0.1273 0.1441 0.1780 -0.0067 0.0120  0.0268  143 CYS   A CB  
3069 S  SG  . CYS   A 143 ? 0.1468 0.1495 0.1734 0.0048  0.0121  0.0157  143 CYS   A SG  
3075 N  N   . VAL   A 144 ? 0.1132 0.1435 0.2027 -0.0034 0.0102  0.0287  144 VAL   A N   
3076 C  CA  . VAL   A 144 ? 0.1251 0.1516 0.2284 -0.0128 0.0171  0.0291  144 VAL   A CA  
3077 C  C   . VAL   A 144 ? 0.1266 0.1418 0.2215 -0.0182 -0.0022 0.0242  144 VAL   A C   
3078 O  O   . VAL   A 144 ? 0.1385 0.1476 0.2286 -0.0085 -0.0036 0.0279  144 VAL   A O   
3079 C  CB  . VAL   A 144 ? 0.1466 0.1769 0.2963 -0.0052 0.0370  0.0333  144 VAL   A CB  
3080 C  CG1 . VAL   A 144 ? 0.1574 0.1962 0.3353 -0.0087 0.0299  0.0301  144 VAL   A CG1 
3081 C  CG2 . VAL   A 144 ? 0.1391 0.1830 0.3053 -0.0017 0.0504  0.0501  144 VAL   A CG2 
3091 N  N   . ASP   A 145 ? 0.1278 0.1409 0.2280 -0.0183 0.0017  0.0222  145 ASP   A N   
3092 C  CA  . ASP   A 145 ? 0.1417 0.1459 0.2356 -0.0205 -0.0039 0.0049  145 ASP   A CA  
3093 C  C   . ASP   A 145 ? 0.1418 0.1338 0.2246 -0.0107 -0.0004 -0.0033 145 ASP   A C   
3094 O  O   . ASP   A 145 ? 0.1557 0.1429 0.2783 -0.0105 0.0012  -0.0306 145 ASP   A O   
3095 C  CB  . ASP   A 145 ? 0.1551 0.1741 0.2648 -0.0276 -0.0183 0.0033  145 ASP   A CB  
3096 C  CG  . ASP   A 145 ? 0.1763 0.2085 0.2865 -0.0496 -0.0279 0.0131  145 ASP   A CG  
3097 O  OD1 . ASP   A 145 ? 0.1713 0.2186 0.2928 -0.0584 -0.0174 0.0186  145 ASP   A OD1 
3098 O  OD2 . ASP   A 145 ? 0.2005 0.2303 0.2937 -0.0591 -0.0489 0.0134  145 ASP   A OD2 
3103 N  N   . THR   A 146 ? 0.1276 0.1308 0.1921 -0.0114 0.0050  0.0050  146 THR   A N   
3104 C  CA  . THR   A 146 ? 0.1233 0.1292 0.1793 -0.0058 0.0028  0.0052  146 THR   A CA  
3105 C  C   . THR   A 146 ? 0.1170 0.1276 0.1860 -0.0073 0.0081  0.0100  146 THR   A C   
3106 O  O   . THR   A 146 ? 0.1290 0.1408 0.1952 0.0058  0.0017  0.0087  146 THR   A O   
3107 C  CB  . THR   A 146 ? 0.1224 0.1308 0.1765 -0.0040 0.0113  0.0131  146 THR   A CB  
3108 O  OG1 . THR   A 146 ? 0.1207 0.1442 0.1884 -0.0032 0.0010  0.0047  146 THR   A OG1 
3109 C  CG2 . THR   A 146 ? 0.1238 0.1323 0.1935 -0.0065 0.0090  0.0136  146 THR   A CG2 
3117 N  N   . VAL   A 147 ? 0.1153 0.1300 0.1751 0.0003  0.0141  0.0196  147 VAL   A N   
3118 C  CA  . VAL   A 147 ? 0.1182 0.1286 0.1849 -0.0048 0.0215  0.0236  147 VAL   A CA  
3119 C  C   . VAL   A 147 ? 0.1193 0.1215 0.1965 -0.0113 0.0190  0.0251  147 VAL   A C   
3120 O  O   . VAL   A 147 ? 0.1200 0.1330 0.2148 -0.0110 0.0168  0.0273  147 VAL   A O   
3121 C  CB  . VAL   A 147 ? 0.1308 0.1270 0.1792 -0.0123 0.0179  0.0246  147 VAL   A CB  
3122 C  CG1 . VAL   A 147 ? 0.1605 0.1350 0.1886 -0.0096 0.0243  0.0362  147 VAL   A CG1 
3123 C  CG2 . VAL   A 147 ? 0.1379 0.1327 0.1740 -0.0156 0.0100  0.0202  147 VAL   A CG2 
3133 N  N   . ARG   A 148 ? 0.1212 0.1260 0.1981 -0.0091 0.0175  0.0344  148 ARG   A N   
3134 C  CA  . ARG   A 148 ? 0.1269 0.1308 0.1889 -0.0097 0.0081  0.0422  148 ARG   A CA  
3135 C  C   . ARG   A 148 ? 0.1364 0.1338 0.1879 -0.0144 0.0093  0.0533  148 ARG   A C   
3136 O  O   . ARG   A 148 ? 0.1621 0.1474 0.2105 -0.0179 0.0190  0.0516  148 ARG   A O   
3137 C  CB  . ARG   A 148 ? 0.1345 0.1330 0.2059 -0.0049 0.0196  0.0395  148 ARG   A CB  
3138 C  CG  . ARG   A 148 ? 0.1483 0.1325 0.2386 -0.0085 0.0317  0.0309  148 ARG   A CG  
3139 C  CD  . ARG   A 148 ? 0.1660 0.1339 0.2663 -0.0030 0.0367  0.0445  148 ARG   A CD  
3140 N  NE  . ARG   A 148 ? 0.1563 0.1355 0.2605 0.0101  0.0465  0.0501  148 ARG   A NE  
3141 C  CZ  . ARG   A 148 ? 0.1516 0.1278 0.2573 0.0087  0.0411  0.0421  148 ARG   A CZ  
3142 N  NH1 . ARG   A 148 ? 0.1625 0.1274 0.2577 -0.0021 0.0442  0.0199  148 ARG   A NH1 
3143 N  NH2 . ARG   A 148 ? 0.1526 0.1438 0.2542 0.0159  0.0444  0.0461  148 ARG   A NH2 
3157 N  N   . THR   A 149 ? 0.1388 0.1429 0.1770 -0.0200 -0.0036 0.0477  149 THR   A N   
3158 C  CA  . THR   A 149 ? 0.1427 0.1480 0.1815 -0.0139 0.0031  0.0480  149 THR   A CA  
3159 C  C   . THR   A 149 ? 0.1348 0.1418 0.1706 -0.0173 0.0097  0.0490  149 THR   A C   
3160 O  O   . THR   A 149 ? 0.1346 0.1526 0.1888 -0.0165 0.0073  0.0441  149 THR   A O   
3161 C  CB  . THR   A 149 ? 0.1373 0.1574 0.1778 -0.0131 0.0046  0.0417  149 THR   A CB  
3162 O  OG1 . THR   A 149 ? 0.1415 0.1513 0.1868 -0.0205 0.0035  0.0329  149 THR   A OG1 
3163 C  CG2 . THR   A 149 ? 0.1359 0.1710 0.1982 -0.0068 -0.0050 0.0408  149 THR   A CG2 
3171 N  N   . ASN   A 150 ? 0.1417 0.1525 0.1708 -0.0050 0.0063  0.0518  150 ASN   A N   
3172 C  CA  . ASN   A 150 ? 0.1493 0.1589 0.1734 -0.0096 0.0081  0.0457  150 ASN   A CA  
3173 C  C   . ASN   A 150 ? 0.1341 0.1511 0.1722 -0.0147 0.0067  0.0462  150 ASN   A C   
3174 O  O   . ASN   A 150 ? 0.1426 0.1603 0.2105 -0.0146 -0.0164 0.0402  150 ASN   A O   
3175 C  CB  . ASN   A 150 ? 0.1962 0.1878 0.1959 -0.0121 0.0264  0.0614  150 ASN   A CB  
3176 C  CG  . ASN   A 150 ? 0.2511 0.2253 0.2594 -0.0128 0.0111  0.0670  150 ASN   A CG  
3177 O  OD1 . ASN   A 150 ? 0.2708 0.2294 0.2791 -0.0190 0.0232  0.0868  150 ASN   A OD1 
3178 N  ND2 . ASN   A 150 ? 0.2778 0.2515 0.3008 -0.0086 -0.0073 0.0646  150 ASN   A ND2 
3185 N  N   . VAL   A 151 ? 0.1305 0.1352 0.1726 -0.0165 0.0021  0.0405  151 VAL   A N   
3186 C  CA  . VAL   A 151 ? 0.1389 0.1399 0.1612 -0.0193 0.0063  0.0374  151 VAL   A CA  
3187 C  C   . VAL   A 151 ? 0.1281 0.1394 0.1708 -0.0239 0.0087  0.0396  151 VAL   A C   
3188 O  O   . VAL   A 151 ? 0.1393 0.1483 0.2035 -0.0172 0.0120  0.0353  151 VAL   A O   
3189 C  CB  . VAL   A 151 ? 0.1661 0.1606 0.1704 -0.0047 0.0077  0.0388  151 VAL   A CB  
3190 C  CG1 . VAL   A 151 ? 0.1680 0.1837 0.1991 -0.0093 0.0003  0.0375  151 VAL   A CG1 
3191 C  CG2 . VAL   A 151 ? 0.1779 0.1538 0.1674 0.0008  0.0232  0.0295  151 VAL   A CG2 
3201 N  N   . TYR   A 152 ? 0.1300 0.1384 0.1701 -0.0162 0.0093  0.0392  152 TYR   A N   
3202 C  CA  . TYR   A 152 ? 0.1288 0.1450 0.1490 -0.0198 0.0087  0.0375  152 TYR   A CA  
3203 C  C   . TYR   A 152 ? 0.1293 0.1414 0.1488 -0.0193 0.0167  0.0365  152 TYR   A C   
3204 O  O   . TYR   A 152 ? 0.1367 0.1396 0.1548 -0.0215 0.0157  0.0300  152 TYR   A O   
3205 C  CB  . TYR   A 152 ? 0.1440 0.1586 0.1499 -0.0129 0.0197  0.0381  152 TYR   A CB  
3206 C  CG  . TYR   A 152 ? 0.1582 0.1772 0.1553 -0.0178 0.0272  0.0470  152 TYR   A CG  
3207 C  CD1 . TYR   A 152 ? 0.1747 0.1970 0.1726 -0.0043 0.0326  0.0482  152 TYR   A CD1 
3208 C  CD2 . TYR   A 152 ? 0.1637 0.1888 0.1516 -0.0306 0.0164  0.0448  152 TYR   A CD2 
3209 C  CE1 . TYR   A 152 ? 0.2001 0.2103 0.1793 -0.0070 0.0164  0.0634  152 TYR   A CE1 
3210 C  CE2 . TYR   A 152 ? 0.1904 0.2021 0.1626 -0.0345 0.0163  0.0560  152 TYR   A CE2 
3211 C  CZ  . TYR   A 152 ? 0.2137 0.2083 0.1723 -0.0249 0.0086  0.0731  152 TYR   A CZ  
3212 O  OH  . TYR   A 152 ? 0.2476 0.2285 0.2109 -0.0184 0.0177  0.0809  152 TYR   A OH  
3222 N  N   A LEU   A 153 ? 0.1255 0.1330 0.1644 -0.0198 0.0116  0.0396  153 LEU   A N   
3223 N  N   B LEU   A 153 ? 0.1309 0.1483 0.1597 -0.0191 0.0170  0.0354  153 LEU   A N   
3224 C  CA  A LEU   A 153 ? 0.1199 0.1233 0.1709 -0.0101 0.0127  0.0440  153 LEU   A CA  
3225 C  CA  B LEU   A 153 ? 0.1275 0.1519 0.1600 -0.0134 0.0229  0.0340  153 LEU   A CA  
3226 C  C   A LEU   A 153 ? 0.1208 0.1256 0.1817 -0.0090 0.0211  0.0370  153 LEU   A C   
3227 C  C   B LEU   A 153 ? 0.1310 0.1565 0.1642 -0.0111 0.0290  0.0328  153 LEU   A C   
3228 O  O   A LEU   A 153 ? 0.1244 0.1350 0.1952 -0.0021 0.0256  0.0355  153 LEU   A O   
3229 O  O   B LEU   A 153 ? 0.1304 0.1589 0.1810 -0.0153 0.0379  0.0371  153 LEU   A O   
3230 C  CB  A LEU   A 153 ? 0.1207 0.1240 0.1750 -0.0089 0.0047  0.0417  153 LEU   A CB  
3231 C  CB  B LEU   A 153 ? 0.1247 0.1571 0.1653 -0.0135 0.0191  0.0339  153 LEU   A CB  
3232 C  CG  A LEU   A 153 ? 0.1270 0.1248 0.1708 -0.0097 0.0054  0.0304  153 LEU   A CG  
3233 C  CG  B LEU   A 153 ? 0.1283 0.1612 0.1615 -0.0127 0.0157  0.0299  153 LEU   A CG  
3234 C  CD1 A LEU   A 153 ? 0.1350 0.1316 0.1766 -0.0153 -0.0020 0.0331  153 LEU   A CD1 
3235 C  CD1 B LEU   A 153 ? 0.1362 0.1651 0.1691 -0.0113 0.0120  0.0334  153 LEU   A CD1 
3236 C  CD2 A LEU   A 153 ? 0.1293 0.1271 0.1617 -0.0089 0.0134  0.0150  153 LEU   A CD2 
3237 C  CD2 B LEU   A 153 ? 0.1268 0.1647 0.1551 -0.0125 0.0103  0.0273  153 LEU   A CD2 
3260 N  N   A ALA   A 154 ? 0.1229 0.1168 0.1693 -0.0083 0.0199  0.0330  154 ALA   A N   
3261 N  N   B ALA   A 154 ? 0.1362 0.1560 0.1421 -0.0009 0.0224  0.0272  154 ALA   A N   
3262 C  CA  A ALA   A 154 ? 0.1328 0.1261 0.1702 -0.0059 0.0237  0.0333  154 ALA   A CA  
3263 C  CA  B ALA   A 154 ? 0.1454 0.1588 0.1453 0.0017  0.0165  0.0293  154 ALA   A CA  
3264 C  C   A ALA   A 154 ? 0.1398 0.1250 0.1757 0.0018  0.0278  0.0397  154 ALA   A C   
3265 C  C   B ALA   A 154 ? 0.1507 0.1611 0.1352 -0.0016 0.0164  0.0327  154 ALA   A C   
3266 O  O   A ALA   A 154 ? 0.1488 0.1377 0.1797 -0.0014 0.0327  0.0401  154 ALA   A O   
3267 O  O   B ALA   A 154 ? 0.1561 0.1655 0.1266 -0.0059 0.0173  0.0276  154 ALA   A O   
3268 C  CB  A ALA   A 154 ? 0.1425 0.1342 0.1936 -0.0015 0.0155  0.0170  154 ALA   A CB  
3269 C  CB  B ALA   A 154 ? 0.1505 0.1596 0.1450 0.0036  0.0022  0.0252  154 ALA   A CB  
3280 N  N   A VAL   A 155 ? 0.1468 0.1254 0.1868 0.0103  0.0270  0.0464  155 VAL   A N   
3281 N  N   B VAL   A 155 ? 0.1567 0.1667 0.1491 -0.0036 0.0141  0.0399  155 VAL   A N   
3282 C  CA  A VAL   A 155 ? 0.1635 0.1373 0.2091 0.0195  0.0208  0.0554  155 VAL   A CA  
3283 C  CA  B VAL   A 155 ? 0.1663 0.1736 0.1622 -0.0040 0.0157  0.0477  155 VAL   A CA  
3284 C  C   A VAL   A 155 ? 0.1634 0.1384 0.2454 0.0225  0.0230  0.0578  155 VAL   A C   
3285 C  C   B VAL   A 155 ? 0.1662 0.1786 0.2029 -0.0007 0.0104  0.0483  155 VAL   A C   
3286 O  O   A VAL   A 155 ? 0.1538 0.1338 0.2496 0.0137  0.0345  0.0418  155 VAL   A O   
3287 O  O   B VAL   A 155 ? 0.1610 0.1785 0.1963 0.0014  -0.0033 0.0312  155 VAL   A O   
3288 C  CB  A VAL   A 155 ? 0.1813 0.1490 0.1862 0.0310  0.0137  0.0488  155 VAL   A CB  
3289 C  CB  B VAL   A 155 ? 0.1803 0.1806 0.1523 0.0015  0.0109  0.0387  155 VAL   A CB  
3290 C  CG1 A VAL   A 155 ? 0.1920 0.1607 0.1872 0.0335  0.0202  0.0366  155 VAL   A CG1 
3291 C  CG1 B VAL   A 155 ? 0.1877 0.1886 0.1535 0.0047  0.0140  0.0354  155 VAL   A CG1 
3292 C  CG2 A VAL   A 155 ? 0.1929 0.1592 0.1783 0.0387  0.0066  0.0436  155 VAL   A CG2 
3293 C  CG2 B VAL   A 155 ? 0.1886 0.1848 0.1650 0.0026  0.0096  0.0335  155 VAL   A CG2 
3312 N  N   A PHE   A 156 ? 0.1740 0.1496 0.2876 0.0313  0.0242  0.0777  156 PHE   A N   
3313 N  N   B PHE   A 156 ? 0.1708 0.1849 0.2405 -0.0013 0.0193  0.0643  156 PHE   A N   
3314 C  CA  A PHE   A 156 ? 0.1980 0.1582 0.3181 0.0386  0.0226  0.0832  156 PHE   A CA  
3315 C  CA  B PHE   A 156 ? 0.1868 0.1882 0.2664 0.0021  0.0214  0.0740  156 PHE   A CA  
3316 C  C   A PHE   A 156 ? 0.1973 0.1706 0.3186 0.0474  0.0362  0.0791  156 PHE   A C   
3317 C  C   B PHE   A 156 ? 0.1945 0.2027 0.2816 0.0146  0.0324  0.0761  156 PHE   A C   
3318 O  O   A PHE   A 156 ? 0.2030 0.1839 0.3345 0.0485  0.0378  0.0466  156 PHE   A O   
3319 O  O   B PHE   A 156 ? 0.1990 0.2128 0.2974 0.0151  0.0386  0.0618  156 PHE   A O   
3320 C  CB  A PHE   A 156 ? 0.2337 0.1703 0.3428 0.0325  0.0117  0.0877  156 PHE   A CB  
3321 C  CB  B PHE   A 156 ? 0.1930 0.1812 0.2647 -0.0044 0.0156  0.0814  156 PHE   A CB  
3322 C  CG  A PHE   A 156 ? 0.2677 0.1801 0.3658 0.0389  -0.0059 0.0785  156 PHE   A CG  
3323 C  CG  B PHE   A 156 ? 0.1983 0.1725 0.2528 -0.0045 0.0088  0.0836  156 PHE   A CG  
3324 C  CD1 A PHE   A 156 ? 0.2829 0.1901 0.3752 0.0405  -0.0130 0.0739  156 PHE   A CD1 
3325 C  CD1 B PHE   A 156 ? 0.1984 0.1730 0.2570 -0.0070 0.0073  0.0771  156 PHE   A CD1 
3326 C  CD2 A PHE   A 156 ? 0.2864 0.1924 0.3802 0.0469  -0.0153 0.0712  156 PHE   A CD2 
3327 C  CD2 B PHE   A 156 ? 0.2065 0.1736 0.2642 -0.0068 0.0024  0.0735  156 PHE   A CD2 
3328 C  CE1 A PHE   A 156 ? 0.2973 0.1979 0.3910 0.0423  -0.0138 0.0621  156 PHE   A CE1 
3329 C  CE1 B PHE   A 156 ? 0.2004 0.1730 0.2618 -0.0106 0.0057  0.0667  156 PHE   A CE1 
3330 C  CE2 A PHE   A 156 ? 0.3003 0.1994 0.3867 0.0480  -0.0181 0.0582  156 PHE   A CE2 
3331 C  CE2 B PHE   A 156 ? 0.2109 0.1721 0.2684 -0.0127 -0.0019 0.0664  156 PHE   A CE2 
3332 C  CZ  A PHE   A 156 ? 0.3036 0.2017 0.3909 0.0468  -0.0149 0.0553  156 PHE   A CZ  
3333 C  CZ  B PHE   A 156 ? 0.2046 0.1679 0.2673 -0.0144 0.0035  0.0683  156 PHE   A CZ  
3352 N  N   A ASP   A 157 ? 0.2002 0.1818 0.3010 0.0451  0.0378  0.0956  157 ASP   A N   
3353 N  N   B ASP   A 157 ? 0.1980 0.2109 0.2812 0.0226  0.0274  0.0905  157 ASP   A N   
3354 C  CA  A ASP   A 157 ? 0.2147 0.2053 0.3143 0.0424  0.0287  0.0959  157 ASP   A CA  
3355 C  CA  B ASP   A 157 ? 0.2057 0.2202 0.2749 0.0349  0.0211  0.0958  157 ASP   A CA  
3356 C  C   A ASP   A 157 ? 0.1993 0.2190 0.3228 0.0462  0.0381  0.1032  157 ASP   A C   
3357 C  C   B ASP   A 157 ? 0.2047 0.2301 0.2676 0.0437  0.0238  0.1023  157 ASP   A C   
3358 O  O   A ASP   A 157 ? 0.1906 0.2107 0.3227 0.0478  0.0364  0.1054  157 ASP   A O   
3359 O  O   B ASP   A 157 ? 0.1995 0.2259 0.2653 0.0472  0.0287  0.1028  157 ASP   A O   
3360 C  CB  A ASP   A 157 ? 0.2436 0.2161 0.3335 0.0430  0.0097  0.0894  157 ASP   A CB  
3361 C  CB  B ASP   A 157 ? 0.2143 0.2198 0.2780 0.0426  0.0101  0.0968  157 ASP   A CB  
3362 C  CG  A ASP   A 157 ? 0.2705 0.2280 0.3640 0.0459  -0.0003 0.0779  157 ASP   A CG  
3363 C  CG  B ASP   A 157 ? 0.2208 0.2173 0.2819 0.0524  0.0049  0.1048  157 ASP   A CG  
3364 O  OD1 A ASP   A 157 ? 0.2910 0.2336 0.3834 0.0477  -0.0074 0.0623  157 ASP   A OD1 
3365 O  OD1 B ASP   A 157 ? 0.2234 0.2133 0.2993 0.0515  -0.0022 0.0952  157 ASP   A OD1 
3366 O  OD2 A ASP   A 157 ? 0.2706 0.2283 0.3772 0.0438  0.0004  0.0826  157 ASP   A OD2 
3367 O  OD2 B ASP   A 157 ? 0.2229 0.2167 0.2661 0.0586  0.0071  0.1196  157 ASP   A OD2 
3376 N  N   A LYS   A 158 ? 0.2041 0.2417 0.3444 0.0454  0.0479  0.1048  158 LYS   A N   
3377 N  N   B LYS   A 158 ? 0.2124 0.2443 0.2768 0.0486  0.0242  0.0986  158 LYS   A N   
3378 C  CA  A LYS   A 158 ? 0.2061 0.2673 0.3642 0.0435  0.0581  0.1065  158 LYS   A CA  
3379 C  CA  B LYS   A 158 ? 0.2155 0.2581 0.2913 0.0511  0.0242  0.0880  158 LYS   A CA  
3380 C  C   A LYS   A 158 ? 0.1880 0.2767 0.3572 0.0443  0.0435  0.1208  158 LYS   A C   
3381 C  C   B LYS   A 158 ? 0.2090 0.2633 0.2895 0.0600  0.0237  0.0926  158 LYS   A C   
3382 O  O   A LYS   A 158 ? 0.1792 0.2810 0.3584 0.0368  0.0496  0.1218  158 LYS   A O   
3383 O  O   B LYS   A 158 ? 0.2058 0.2683 0.2905 0.0592  0.0316  0.0901  158 LYS   A O   
3384 C  CB  A LYS   A 158 ? 0.2261 0.2801 0.3781 0.0426  0.0811  0.0991  158 LYS   A CB  
3385 C  CB  B LYS   A 158 ? 0.2252 0.2644 0.3044 0.0398  0.0287  0.0691  158 LYS   A CB  
3386 C  CG  A LYS   A 158 ? 0.2457 0.2934 0.4005 0.0414  0.0902  0.0958  158 LYS   A CG  
3387 C  CG  B LYS   A 158 ? 0.2331 0.2705 0.3251 0.0300  0.0250  0.0532  158 LYS   A CG  
3388 C  CD  A LYS   A 158 ? 0.2585 0.3041 0.4152 0.0405  0.1059  0.0943  158 LYS   A CD  
3389 C  CD  B LYS   A 158 ? 0.2378 0.2761 0.3426 0.0238  0.0220  0.0398  158 LYS   A CD  
3390 C  CE  A LYS   A 158 ? 0.2666 0.3100 0.4211 0.0366  0.1202  0.1034  158 LYS   A CE  
3391 C  CE  B LYS   A 158 ? 0.2394 0.2790 0.3509 0.0223  0.0155  0.0326  158 LYS   A CE  
3392 N  NZ  A LYS   A 158 ? 0.2699 0.3114 0.4250 0.0311  0.1279  0.1146  158 LYS   A NZ  
3393 N  NZ  B LYS   A 158 ? 0.2399 0.2796 0.3567 0.0235  0.0074  0.0313  158 LYS   A NZ  
3420 N  N   A ASN   A 159 ? 0.1840 0.2832 0.3651 0.0474  0.0200  0.1237  159 ASN   A N   
3421 N  N   B ASN   A 159 ? 0.2095 0.2655 0.3033 0.0633  0.0174  0.0889  159 ASN   A N   
3422 C  CA  A ASN   A 159 ? 0.1838 0.2893 0.3669 0.0436  0.0019  0.1304  159 ASN   A CA  
3423 C  CA  B ASN   A 159 ? 0.2155 0.2705 0.3178 0.0564  0.0133  0.0833  159 ASN   A CA  
3424 C  C   A ASN   A 159 ? 0.1653 0.2880 0.3308 0.0316  0.0054  0.1235  159 ASN   A C   
3425 C  C   B ASN   A 159 ? 0.2035 0.2675 0.2991 0.0503  0.0179  0.0671  159 ASN   A C   
3426 O  O   A ASN   A 159 ? 0.1549 0.2946 0.3010 0.0351  -0.0037 0.1233  159 ASN   A O   
3427 O  O   B ASN   A 159 ? 0.1985 0.2712 0.2902 0.0492  0.0172  0.0591  159 ASN   A O   
3428 C  CB  A ASN   A 159 ? 0.2018 0.2992 0.4070 0.0472  -0.0073 0.1371  159 ASN   A CB  
3429 C  CB  B ASN   A 159 ? 0.2348 0.2794 0.3561 0.0533  0.0064  0.0886  159 ASN   A CB  
3430 C  CG  A ASN   A 159 ? 0.2207 0.3111 0.4510 0.0448  -0.0086 0.1294  159 ASN   A CG  
3431 C  CG  B ASN   A 159 ? 0.2533 0.2877 0.3953 0.0475  0.0050  0.0792  159 ASN   A CG  
3432 O  OD1 A ASN   A 159 ? 0.2305 0.3171 0.4747 0.0471  -0.0014 0.1258  159 ASN   A OD1 
3433 O  OD1 B ASN   A 159 ? 0.2633 0.2942 0.4167 0.0416  0.0023  0.0688  159 ASN   A OD1 
3434 N  ND2 A ASN   A 159 ? 0.2274 0.3183 0.4759 0.0402  -0.0110 0.1194  159 ASN   A ND2 
3435 N  ND2 B ASN   A 159 ? 0.2569 0.2910 0.4114 0.0488  0.0133  0.0753  159 ASN   A ND2 
3448 N  N   A LEU   A 160 ? 0.1549 0.2736 0.3153 0.0203  0.0026  0.1178  160 LEU   A N   
3449 N  N   B LEU   A 160 ? 0.1945 0.2564 0.2860 0.0462  0.0125  0.0646  160 LEU   A N   
3450 C  CA  A LEU   A 160 ? 0.1544 0.2630 0.3004 0.0055  0.0126  0.1148  160 LEU   A CA  
3451 C  CA  B LEU   A 160 ? 0.1884 0.2467 0.2709 0.0360  0.0123  0.0671  160 LEU   A CA  
3452 C  C   A LEU   A 160 ? 0.1415 0.2558 0.2874 0.0049  0.0140  0.1080  160 LEU   A C   
3453 C  C   B LEU   A 160 ? 0.1704 0.2401 0.2597 0.0303  0.0190  0.0675  160 LEU   A C   
3454 O  O   A LEU   A 160 ? 0.1348 0.2628 0.3010 0.0016  0.0047  0.1027  160 LEU   A O   
3455 O  O   B LEU   A 160 ? 0.1672 0.2448 0.2702 0.0246  0.0133  0.0670  160 LEU   A O   
3456 C  CB  A LEU   A 160 ? 0.1599 0.2615 0.2890 -0.0039 0.0144  0.1179  160 LEU   A CB  
3457 C  CB  B LEU   A 160 ? 0.2005 0.2460 0.2638 0.0276  0.0101  0.0665  160 LEU   A CB  
3458 C  CG  A LEU   A 160 ? 0.1654 0.2625 0.2930 -0.0179 0.0124  0.1019  160 LEU   A CG  
3459 C  CG  B LEU   A 160 ? 0.2072 0.2460 0.2653 0.0172  0.0107  0.0535  160 LEU   A CG  
3460 C  CD1 A LEU   A 160 ? 0.1745 0.2657 0.2903 -0.0222 0.0097  0.1002  160 LEU   A CD1 
3461 C  CD1 B LEU   A 160 ? 0.2084 0.2466 0.2603 0.0123  0.0116  0.0515  160 LEU   A CD1 
3462 C  CD2 A LEU   A 160 ? 0.1663 0.2604 0.2981 -0.0221 0.0169  0.0888  160 LEU   A CD2 
3463 C  CD2 B LEU   A 160 ? 0.2118 0.2452 0.2628 0.0139  0.0109  0.0451  160 LEU   A CD2 
3486 N  N   A TYR   A 161 ? 0.1426 0.2387 0.2727 0.0052  0.0138  0.1049  161 TYR   A N   
3487 N  N   B TYR   A 161 ? 0.1615 0.2276 0.2452 0.0293  0.0241  0.0672  161 TYR   A N   
3488 C  CA  A TYR   A 161 ? 0.1451 0.2283 0.2651 0.0051  0.0147  0.1008  161 TYR   A CA  
3489 C  CA  B TYR   A 161 ? 0.1583 0.2214 0.2363 0.0274  0.0272  0.0636  161 TYR   A CA  
3490 C  C   A TYR   A 161 ? 0.1367 0.2387 0.2759 0.0083  0.0122  0.0984  161 TYR   A C   
3491 C  C   B TYR   A 161 ? 0.1553 0.2348 0.2430 0.0240  0.0244  0.0639  161 TYR   A C   
3492 O  O   A TYR   A 161 ? 0.1292 0.2373 0.2723 0.0038  0.0161  0.0883  161 TYR   A O   
3493 O  O   B TYR   A 161 ? 0.1497 0.2328 0.2455 0.0224  0.0246  0.0511  161 TYR   A O   
3494 C  CB  A TYR   A 161 ? 0.1571 0.2174 0.2685 0.0028  0.0113  0.0803  161 TYR   A CB  
3495 C  CB  B TYR   A 161 ? 0.1599 0.2078 0.2362 0.0280  0.0284  0.0517  161 TYR   A CB  
3496 C  CG  A TYR   A 161 ? 0.1570 0.2054 0.2569 0.0033  0.0073  0.0551  161 TYR   A CG  
3497 C  CG  B TYR   A 161 ? 0.1543 0.1935 0.2273 0.0295  0.0310  0.0407  161 TYR   A CG  
3498 C  CD1 A TYR   A 161 ? 0.1581 0.1996 0.2610 0.0037  0.0112  0.0427  161 TYR   A CD1 
3499 C  CD1 B TYR   A 161 ? 0.1539 0.1883 0.2280 0.0275  0.0323  0.0326  161 TYR   A CD1 
3500 C  CD2 A TYR   A 161 ? 0.1590 0.2032 0.2524 0.0053  -0.0066 0.0422  161 TYR   A CD2 
3501 C  CD2 B TYR   A 161 ? 0.1557 0.1886 0.2282 0.0318  0.0253  0.0398  161 TYR   A CD2 
3502 C  CE1 A TYR   A 161 ? 0.1624 0.1919 0.2590 0.0027  0.0041  0.0456  161 TYR   A CE1 
3503 C  CE1 B TYR   A 161 ? 0.1600 0.1872 0.2330 0.0280  0.0283  0.0351  161 TYR   A CE1 
3504 C  CE2 A TYR   A 161 ? 0.1635 0.1917 0.2488 0.0036  -0.0057 0.0464  161 TYR   A CE2 
3505 C  CE2 B TYR   A 161 ? 0.1617 0.1847 0.2320 0.0292  0.0239  0.0451  161 TYR   A CE2 
3506 C  CZ  A TYR   A 161 ? 0.1709 0.1857 0.2578 -0.0001 -0.0056 0.0496  161 TYR   A CZ  
3507 C  CZ  B TYR   A 161 ? 0.1704 0.1846 0.2419 0.0279  0.0236  0.0418  161 TYR   A CZ  
3508 O  OH  A TYR   A 161 ? 0.1863 0.1790 0.2651 -0.0055 -0.0050 0.0584  161 TYR   A OH  
3509 O  OH  B TYR   A 161 ? 0.1874 0.1856 0.2664 0.0222  0.0135  0.0442  161 TYR   A OH  
3528 N  N   A ASP   A 162 ? 0.1362 0.2523 0.2931 0.0101  0.0174  0.1044  162 ASP   A N   
3529 N  N   B ASP   A 162 ? 0.1561 0.2521 0.2510 0.0207  0.0272  0.0757  162 ASP   A N   
3530 C  CA  A ASP   A 162 ? 0.1397 0.2665 0.3014 0.0032  0.0216  0.1082  162 ASP   A CA  
3531 C  CA  B ASP   A 162 ? 0.1605 0.2708 0.2658 0.0202  0.0221  0.0762  162 ASP   A CA  
3532 C  C   A ASP   A 162 ? 0.1302 0.2799 0.2990 -0.0060 0.0182  0.1087  162 ASP   A C   
3533 C  C   B ASP   A 162 ? 0.1634 0.2833 0.2722 0.0156  0.0156  0.0701  162 ASP   A C   
3534 O  O   A ASP   A 162 ? 0.1294 0.2812 0.3160 -0.0132 0.0179  0.1037  162 ASP   A O   
3535 O  O   B ASP   A 162 ? 0.1657 0.2869 0.2818 0.0168  0.0159  0.0602  162 ASP   A O   
3536 C  CB  A ASP   A 162 ? 0.1576 0.2706 0.3176 0.0089  0.0319  0.1036  162 ASP   A CB  
3537 C  CB  B ASP   A 162 ? 0.1637 0.2748 0.2853 0.0262  0.0236  0.0833  162 ASP   A CB  
3538 C  CG  A ASP   A 162 ? 0.1739 0.2791 0.3398 0.0128  0.0421  0.0936  162 ASP   A CG  
3539 C  CG  B ASP   A 162 ? 0.1660 0.2773 0.2907 0.0292  0.0216  0.1030  162 ASP   A CG  
3540 O  OD1 A ASP   A 162 ? 0.1844 0.2833 0.3529 0.0110  0.0358  0.0993  162 ASP   A OD1 
3541 O  OD1 B ASP   A 162 ? 0.1686 0.2771 0.2934 0.0328  0.0184  0.1155  162 ASP   A OD1 
3542 O  OD2 A ASP   A 162 ? 0.1815 0.2819 0.3507 0.0181  0.0603  0.0826  162 ASP   A OD2 
3543 O  OD2 B ASP   A 162 ? 0.1672 0.2810 0.2918 0.0310  0.0231  0.1073  162 ASP   A OD2 
3552 N  N   A LYS   A 163 ? 0.1354 0.2979 0.3005 -0.0070 -0.0005 0.0954  163 LYS   A N   
3553 N  N   B LYS   A 163 ? 0.1704 0.2964 0.2815 0.0099  0.0079  0.0670  163 LYS   A N   
3554 C  CA  A LYS   A 163 ? 0.1492 0.3175 0.2983 -0.0108 -0.0067 0.0835  163 LYS   A CA  
3555 C  CA  B LYS   A 163 ? 0.1770 0.3092 0.2870 0.0011  0.0062  0.0665  163 LYS   A CA  
3556 C  C   A LYS   A 163 ? 0.1445 0.3091 0.2962 -0.0143 0.0097  0.0771  163 LYS   A C   
3557 C  C   B LYS   A 163 ? 0.1603 0.3025 0.2835 -0.0075 0.0112  0.0678  163 LYS   A C   
3558 O  O   A LYS   A 163 ? 0.1393 0.3174 0.3088 -0.0220 0.0190  0.0707  163 LYS   A O   
3559 O  O   B LYS   A 163 ? 0.1618 0.3079 0.2863 -0.0094 0.0140  0.0597  163 LYS   A O   
3560 C  CB  A LYS   A 163 ? 0.1833 0.3432 0.3276 -0.0037 -0.0250 0.0766  163 LYS   A CB  
3561 C  CB  B LYS   A 163 ? 0.2057 0.3264 0.3169 0.0045  0.0006  0.0640  163 LYS   A CB  
3562 C  CG  A LYS   A 163 ? 0.2163 0.3643 0.3624 -0.0051 -0.0244 0.0666  163 LYS   A CG  
3563 C  CG  B LYS   A 163 ? 0.2331 0.3396 0.3506 0.0025  0.0039  0.0613  163 LYS   A CG  
3564 C  CD  A LYS   A 163 ? 0.2411 0.3807 0.4087 -0.0074 -0.0276 0.0548  163 LYS   A CD  
3565 C  CD  B LYS   A 163 ? 0.2572 0.3488 0.3944 -0.0002 0.0055  0.0589  163 LYS   A CD  
3566 C  CE  A LYS   A 163 ? 0.2661 0.3909 0.4345 -0.0109 -0.0258 0.0502  163 LYS   A CE  
3567 C  CE  B LYS   A 163 ? 0.2734 0.3526 0.4174 -0.0039 0.0101  0.0616  163 LYS   A CE  
3568 N  NZ  A LYS   A 163 ? 0.2758 0.3961 0.4534 -0.0147 -0.0253 0.0533  163 LYS   A NZ  
3569 N  NZ  B LYS   A 163 ? 0.2817 0.3536 0.4375 -0.0068 0.0147  0.0639  163 LYS   A NZ  
3596 N  N   . LEU   A 164 ? 0.1376 0.2863 0.2781 -0.0169 0.0109  0.0727  164 LEU   A N   
3597 C  CA  . LEU   A 164 ? 0.1363 0.2568 0.2654 -0.0242 0.0248  0.0619  164 LEU   A CA  
3598 C  C   . LEU   A 164 ? 0.1398 0.2483 0.2690 -0.0189 0.0330  0.0513  164 LEU   A C   
3599 O  O   . LEU   A 164 ? 0.1470 0.2510 0.2807 -0.0281 0.0566  0.0383  164 LEU   A O   
3600 C  CB  . LEU   A 164 ? 0.1380 0.2431 0.2561 -0.0266 0.0303  0.0622  164 LEU   A CB  
3601 C  CG  . LEU   A 164 ? 0.1474 0.2384 0.2623 -0.0182 0.0205  0.0569  164 LEU   A CG  
3602 C  CD1 . LEU   A 164 ? 0.1419 0.2330 0.2741 -0.0150 0.0140  0.0516  164 LEU   A CD1 
3603 C  CD2 . LEU   A 164 ? 0.1634 0.2408 0.2548 -0.0225 0.0399  0.0572  164 LEU   A CD2 
3616 N  N   . VAL   A 165 ? 0.1349 0.2428 0.2645 -0.0160 0.0262  0.0557  165 VAL   A N   
3617 C  CA  . VAL   A 165 ? 0.1468 0.2478 0.2668 -0.0197 0.0311  0.0633  165 VAL   A CA  
3618 C  C   . VAL   A 165 ? 0.1390 0.2557 0.2674 -0.0177 0.0317  0.0664  165 VAL   A C   
3619 O  O   . VAL   A 165 ? 0.1373 0.2543 0.2720 -0.0240 0.0283  0.0597  165 VAL   A O   
3620 C  CB  . VAL   A 165 ? 0.1712 0.2495 0.2685 -0.0211 0.0297  0.0595  165 VAL   A CB  
3621 C  CG1 . VAL   A 165 ? 0.1787 0.2530 0.2659 -0.0260 0.0359  0.0558  165 VAL   A CG1 
3622 C  CG2 . VAL   A 165 ? 0.1852 0.2501 0.2788 -0.0179 0.0200  0.0706  165 VAL   A CG2 
3632 N  N   . SER   A 166 ? 0.1306 0.2718 0.2879 -0.0110 0.0349  0.0638  166 SER   A N   
3633 C  CA  . SER   A 166 ? 0.1372 0.2999 0.3148 -0.0117 0.0260  0.0516  166 SER   A CA  
3634 C  C   . SER   A 166 ? 0.1400 0.3211 0.3070 -0.0213 0.0108  0.0379  166 SER   A C   
3635 O  O   . SER   A 166 ? 0.1596 0.3378 0.3405 -0.0356 0.0210  0.0009  166 SER   A O   
3636 C  CB  . SER   A 166 ? 0.1628 0.3160 0.3766 0.0066  0.0143  0.0443  166 SER   A CB  
3637 O  OG  . SER   A 166 ? 0.2081 0.3339 0.4178 0.0086  0.0133  0.0500  166 SER   A OG  
3643 N  N   . SER   A 167 ? 0.1473 0.3269 0.2640 -0.0067 0.0004  0.0524  167 SER   A N   
3644 C  CA  . SER   A 167 ? 0.1735 0.3366 0.2565 0.0048  -0.0078 0.0369  167 SER   A CA  
3645 C  C   . SER   A 167 ? 0.1763 0.3325 0.2554 0.0162  0.0078  0.0274  167 SER   A C   
3646 O  O   . SER   A 167 ? 0.1943 0.3312 0.2636 0.0206  -0.0013 0.0217  167 SER   A O   
3647 C  CB  . SER   A 167 ? 0.1855 0.3517 0.2558 0.0065  -0.0049 0.0354  167 SER   A CB  
3648 O  OG  . SER   A 167 ? 0.1868 0.3590 0.2627 0.0043  0.0168  0.0381  167 SER   A OG  
3654 N  N   . PHE   A 168 ? 0.1666 0.3321 0.2524 0.0242  0.0112  0.0235  168 PHE   A N   
3655 C  CA  . PHE   A 168 ? 0.1687 0.3352 0.2654 0.0159  0.0233  0.0173  168 PHE   A CA  
3656 C  C   . PHE   A 168 ? 0.1912 0.3687 0.3040 0.0045  0.0617  -0.0051 168 PHE   A C   
3657 O  O   . PHE   A 168 ? 0.1833 0.3721 0.3401 -0.0159 0.0648  0.0027  168 PHE   A O   
3658 C  CB  . PHE   A 168 ? 0.1682 0.3104 0.2460 0.0111  0.0046  0.0226  168 PHE   A CB  
3659 C  CG  . PHE   A 168 ? 0.1595 0.2873 0.2309 -0.0046 -0.0017 0.0353  168 PHE   A CG  
3660 C  CD1 . PHE   A 168 ? 0.1593 0.2859 0.2353 -0.0133 -0.0042 0.0481  168 PHE   A CD1 
3661 C  CD2 . PHE   A 168 ? 0.1540 0.2729 0.2266 -0.0089 0.0036  0.0284  168 PHE   A CD2 
3662 C  CE1 . PHE   A 168 ? 0.1520 0.2795 0.2342 -0.0143 -0.0057 0.0536  168 PHE   A CE1 
3663 C  CE2 . PHE   A 168 ? 0.1604 0.2626 0.2337 -0.0079 0.0099  0.0401  168 PHE   A CE2 
3664 C  CZ  . PHE   A 168 ? 0.1572 0.2680 0.2289 -0.0150 0.0004  0.0439  168 PHE   A CZ  
3674 N  N   . LEU   A 169 ? 0.2600 0.3988 0.3635 0.0009  0.0561  -0.0276 169 LEU   A N   
3675 C  CA  . LEU   A 169 ? 0.3568 0.4349 0.4680 0.0024  0.0100  -0.0356 169 LEU   A CA  
3676 C  C   . LEU   A 169 ? 0.3875 0.4449 0.5028 0.0010  -0.0115 -0.0311 169 LEU   A C   
3677 O  O   . LEU   A 169 ? 0.4055 0.4513 0.5082 0.0033  -0.0160 -0.0335 169 LEU   A O   
3678 C  CB  . LEU   A 169 ? 0.4016 0.4590 0.5064 0.0020  -0.0107 -0.0484 169 LEU   A CB  
3679 C  CG  . LEU   A 169 ? 0.4449 0.4789 0.5445 -0.0017 -0.0249 -0.0667 169 LEU   A CG  
3680 C  CD1 . LEU   A 169 ? 0.4549 0.4850 0.5597 -0.0038 -0.0304 -0.0721 169 LEU   A CD1 
3681 C  CD2 . LEU   A 169 ? 0.4611 0.4873 0.5551 -0.0028 -0.0276 -0.0743 169 LEU   A CD2 
3682 O  OXT . LEU   A 169 ? 0.3881 0.4437 0.5046 -0.0030 -0.0143 -0.0287 169 LEU   A OXT 
3694 N  N   A SER   B 1   ? 0.3808 0.3737 0.4010 -0.0989 -0.0812 0.0621  1   SER   B N   
3695 N  N   B SER   B 1   ? 0.3455 0.3449 0.3668 -0.0886 -0.0604 0.0392  1   SER   B N   
3696 C  CA  A SER   B 1   ? 0.3741 0.3743 0.4063 -0.1026 -0.0787 0.0588  1   SER   B CA  
3697 C  CA  B SER   B 1   ? 0.3397 0.3466 0.3686 -0.0901 -0.0586 0.0361  1   SER   B CA  
3698 C  C   A SER   B 1   ? 0.3488 0.3669 0.3793 -0.1062 -0.0848 0.0732  1   SER   B C   
3699 C  C   B SER   B 1   ? 0.3214 0.3444 0.3445 -0.0886 -0.0639 0.0494  1   SER   B C   
3700 O  O   A SER   B 1   ? 0.3554 0.3688 0.3505 -0.1032 -0.0844 0.0704  1   SER   B O   
3701 O  O   B SER   B 1   ? 0.3227 0.3442 0.3194 -0.0883 -0.0681 0.0473  1   SER   B O   
3702 C  CB  A SER   B 1   ? 0.3880 0.3789 0.4148 -0.1019 -0.0712 0.0471  1   SER   B CB  
3703 C  CB  B SER   B 1   ? 0.3488 0.3474 0.3754 -0.0914 -0.0514 0.0231  1   SER   B CB  
3704 O  OG  A SER   B 1   ? 0.3989 0.3859 0.4549 -0.1011 -0.0706 0.0447  1   SER   B OG  
3705 O  OG  B SER   B 1   ? 0.3561 0.3507 0.4056 -0.0922 -0.0507 0.0185  1   SER   B OG  
3720 N  N   A MET   B 2   ? 0.3186 0.3565 0.3665 -0.1070 -0.0885 0.1013  2   MET   B N   
3721 N  N   B MET   B 2   ? 0.3047 0.3419 0.3331 -0.0818 -0.0619 0.0727  2   MET   B N   
3722 C  CA  A MET   B 2   ? 0.2927 0.3495 0.3707 -0.0954 -0.0896 0.1166  2   MET   B CA  
3723 C  CA  B MET   B 2   ? 0.2910 0.3394 0.3300 -0.0671 -0.0575 0.0877  2   MET   B CA  
3724 C  C   A MET   B 2   ? 0.2444 0.3174 0.3188 -0.0882 -0.1043 0.1385  2   MET   B C   
3725 C  C   B MET   B 2   ? 0.2651 0.3217 0.2915 -0.0574 -0.0529 0.0963  2   MET   B C   
3726 O  O   A MET   B 2   ? 0.2332 0.3222 0.3070 -0.0814 -0.1147 0.1467  2   MET   B O   
3727 O  O   B MET   B 2   ? 0.2676 0.3312 0.2930 -0.0521 -0.0419 0.0953  2   MET   B O   
3728 C  CB  A MET   B 2   ? 0.3227 0.3809 0.4482 -0.0789 -0.0670 0.0917  2   MET   B CB  
3729 C  CB  B MET   B 2   ? 0.3079 0.3582 0.3776 -0.0554 -0.0532 0.0849  2   MET   B CB  
3730 C  CG  A MET   B 2   ? 0.3512 0.4082 0.5175 -0.0599 -0.0462 0.0737  2   MET   B CG  
3731 C  CG  B MET   B 2   ? 0.3235 0.3767 0.4149 -0.0431 -0.0478 0.0899  2   MET   B CG  
3732 S  SD  A MET   B 2   ? 0.3767 0.4310 0.5820 -0.0432 -0.0337 0.0637  2   MET   B SD  
3733 S  SD  B MET   B 2   ? 0.3386 0.3954 0.4548 -0.0320 -0.0471 0.0965  2   MET   B SD  
3734 C  CE  A MET   B 2   ? 0.3824 0.4355 0.5884 -0.0403 -0.0309 0.0661  2   MET   B CE  
3735 C  CE  B MET   B 2   ? 0.3405 0.4009 0.4571 -0.0318 -0.0471 0.0922  2   MET   B CE  
3754 N  N   A VAL   B 3   ? 0.2156 0.2781 0.2954 -0.0911 -0.0920 0.1453  3   VAL   B N   
3755 N  N   B VAL   B 3   ? 0.2397 0.2920 0.2636 -0.0557 -0.0527 0.1012  3   VAL   B N   
3756 C  CA  A VAL   B 3   ? 0.2074 0.2462 0.2911 -0.0760 -0.0794 0.1294  3   VAL   B CA  
3757 C  CA  B VAL   B 3   ? 0.2218 0.2632 0.2501 -0.0476 -0.0481 0.0939  3   VAL   B CA  
3758 C  C   A VAL   B 3   ? 0.1883 0.2278 0.2581 -0.0621 -0.0691 0.1134  3   VAL   B C   
3759 C  C   B VAL   B 3   ? 0.1964 0.2407 0.2259 -0.0431 -0.0494 0.0944  3   VAL   B C   
3760 O  O   A VAL   B 3   ? 0.1861 0.2253 0.2629 -0.0619 -0.0688 0.1164  3   VAL   B O   
3761 O  O   B VAL   B 3   ? 0.1911 0.2432 0.2190 -0.0310 -0.0494 0.0939  3   VAL   B O   
3762 C  CB  A VAL   B 3   ? 0.2259 0.2449 0.3296 -0.0760 -0.0710 0.1103  3   VAL   B CB  
3763 C  CB  B VAL   B 3   ? 0.2324 0.2585 0.2655 -0.0447 -0.0402 0.0835  3   VAL   B CB  
3764 C  CG1 A VAL   B 3   ? 0.2363 0.2448 0.3467 -0.0732 -0.0700 0.1061  3   VAL   B CG1 
3765 C  CG1 B VAL   B 3   ? 0.2378 0.2571 0.2736 -0.0442 -0.0378 0.0820  3   VAL   B CG1 
3766 C  CG2 A VAL   B 3   ? 0.2292 0.2498 0.3489 -0.0753 -0.0625 0.1067  3   VAL   B CG2 
3767 C  CG2 B VAL   B 3   ? 0.2351 0.2584 0.2697 -0.0434 -0.0385 0.0793  3   VAL   B CG2 
3786 N  N   . ASN   B 4   ? 0.1817 0.2166 0.2211 -0.0516 -0.0599 0.0896  4   ASN   B N   
3787 C  CA  . ASN   B 4   ? 0.1810 0.2075 0.1854 -0.0544 -0.0471 0.0492  4   ASN   B CA  
3788 C  C   . ASN   B 4   ? 0.1877 0.2253 0.1720 -0.0563 -0.0305 0.0315  4   ASN   B C   
3789 O  O   . ASN   B 4   ? 0.1904 0.2314 0.1948 -0.0518 -0.0244 0.0153  4   ASN   B O   
3790 C  CB  . ASN   B 4   ? 0.1773 0.1992 0.1678 -0.0485 -0.0488 0.0404  4   ASN   B CB  
3791 C  CG  . ASN   B 4   ? 0.1788 0.1852 0.1602 -0.0426 -0.0456 0.0319  4   ASN   B CG  
3792 O  OD1 . ASN   B 4   ? 0.1767 0.1732 0.1693 -0.0418 -0.0486 0.0286  4   ASN   B OD1 
3793 N  ND2 . ASN   B 4   ? 0.1930 0.1911 0.1651 -0.0235 -0.0324 0.0276  4   ASN   B ND2 
3801 N  N   . SER   B 5   ? 0.2002 0.2438 0.1871 -0.0601 -0.0209 0.0340  5   SER   B N   
3802 C  CA  . SER   B 5   ? 0.2302 0.2746 0.2147 -0.0536 -0.0075 0.0362  5   SER   B CA  
3803 C  C   . SER   B 5   ? 0.2513 0.2794 0.2411 -0.0660 0.0247  0.0337  5   SER   B C   
3804 O  O   . SER   B 5   ? 0.2688 0.2801 0.3165 -0.0624 0.0562  0.0277  5   SER   B O   
3805 C  CB  . SER   B 5   ? 0.2429 0.2916 0.2310 -0.0419 -0.0076 0.0453  5   SER   B CB  
3806 O  OG  . SER   B 5   ? 0.2638 0.3120 0.2871 -0.0294 -0.0040 0.0481  5   SER   B OG  
3812 N  N   . PHE   B 6   ? 0.2650 0.2910 0.2168 -0.0699 0.0363  0.0373  6   PHE   B N   
3813 C  CA  . PHE   B 6   ? 0.2730 0.2942 0.1919 -0.0839 0.0446  0.0152  6   PHE   B CA  
3814 C  C   . PHE   B 6   ? 0.3281 0.3309 0.2229 -0.0903 0.0665  -0.0047 6   PHE   B C   
3815 O  O   . PHE   B 6   ? 0.3440 0.3617 0.2665 -0.0867 0.0490  -0.0215 6   PHE   B O   
3816 C  CB  . PHE   B 6   ? 0.2384 0.2678 0.1663 -0.0733 0.0282  0.0072  6   PHE   B CB  
3817 C  CG  . PHE   B 6   ? 0.2047 0.2370 0.1584 -0.0666 0.0082  0.0087  6   PHE   B CG  
3818 C  CD1 . PHE   B 6   ? 0.2053 0.2099 0.1395 -0.0602 -0.0035 0.0066  6   PHE   B CD1 
3819 C  CD2 . PHE   B 6   ? 0.1859 0.2361 0.1627 -0.0562 0.0030  0.0297  6   PHE   B CD2 
3820 C  CE1 . PHE   B 6   ? 0.2010 0.1944 0.1475 -0.0505 -0.0057 0.0047  6   PHE   B CE1 
3821 C  CE2 . PHE   B 6   ? 0.1872 0.2252 0.1871 -0.0458 0.0086  0.0241  6   PHE   B CE2 
3822 C  CZ  . PHE   B 6   ? 0.1907 0.2021 0.1626 -0.0458 0.0016  0.0065  6   PHE   B CZ  
3832 N  N   . SER   B 7   ? 0.3633 0.3218 0.2414 -0.1069 0.1019  -0.0213 7   SER   B N   
3833 C  CA  . SER   B 7   ? 0.3916 0.3279 0.2861 -0.1071 0.1223  -0.0310 7   SER   B CA  
3834 C  C   . SER   B 7   ? 0.3853 0.3126 0.2714 -0.1094 0.1380  -0.0496 7   SER   B C   
3835 O  O   . SER   B 7   ? 0.3847 0.3131 0.3068 -0.1102 0.1266  -0.0504 7   SER   B O   
3836 C  CB  . SER   B 7   ? 0.4156 0.3528 0.3497 -0.1021 0.1293  -0.0264 7   SER   B CB  
3837 O  OG  . SER   B 7   ? 0.4286 0.3685 0.4015 -0.1002 0.1265  -0.0256 7   SER   B OG  
3843 N  N   . GLY   B 8   ? 0.3848 0.3030 0.2822 -0.0987 0.1478  -0.0617 8   GLY   B N   
3844 C  CA  . GLY   B 8   ? 0.3700 0.2860 0.2822 -0.0934 0.1472  -0.0656 8   GLY   B CA  
3845 C  C   . GLY   B 8   ? 0.3456 0.2587 0.2779 -0.0892 0.1360  -0.0641 8   GLY   B C   
3846 O  O   . GLY   B 8   ? 0.3524 0.2639 0.3171 -0.0830 0.1347  -0.0724 8   GLY   B O   
3850 N  N   . TYR   B 9   ? 0.3226 0.2335 0.2533 -0.0769 0.1076  -0.0670 9   TYR   B N   
3851 C  CA  . TYR   B 9   ? 0.2984 0.2064 0.2193 -0.0644 0.0773  -0.0523 9   TYR   B CA  
3852 C  C   . TYR   B 9   ? 0.2932 0.2068 0.2005 -0.0602 0.0483  -0.0411 9   TYR   B C   
3853 O  O   . TYR   B 9   ? 0.3117 0.2332 0.2418 -0.0658 0.0503  -0.0273 9   TYR   B O   
3854 C  CB  . TYR   B 9   ? 0.2870 0.1867 0.2329 -0.0541 0.0717  -0.0471 9   TYR   B CB  
3855 C  CG  . TYR   B 9   ? 0.2759 0.1709 0.2310 -0.0579 0.0677  -0.0525 9   TYR   B CG  
3856 C  CD1 . TYR   B 9   ? 0.2813 0.1718 0.2466 -0.0719 0.0712  -0.0416 9   TYR   B CD1 
3857 C  CD2 . TYR   B 9   ? 0.2583 0.1677 0.2260 -0.0545 0.0660  -0.0584 9   TYR   B CD2 
3858 C  CE1 . TYR   B 9   ? 0.2772 0.1782 0.2455 -0.0798 0.0672  -0.0537 9   TYR   B CE1 
3859 C  CE2 . TYR   B 9   ? 0.2592 0.1684 0.2369 -0.0589 0.0649  -0.0578 9   TYR   B CE2 
3860 C  CZ  . TYR   B 9   ? 0.2662 0.1830 0.2399 -0.0727 0.0715  -0.0643 9   TYR   B CZ  
3861 O  OH  . TYR   B 9   ? 0.2666 0.2016 0.2612 -0.0836 0.0700  -0.0795 9   TYR   B OH  
3871 N  N   . LEU   B 10  ? 0.2682 0.1799 0.1785 -0.0495 0.0265  -0.0419 10  LEU   B N   
3872 C  CA  . LEU   B 10  ? 0.2627 0.1769 0.1814 -0.0539 -0.0070 -0.0333 10  LEU   B CA  
3873 C  C   . LEU   B 10  ? 0.2416 0.1749 0.1821 -0.0544 -0.0169 -0.0304 10  LEU   B C   
3874 O  O   . LEU   B 10  ? 0.2275 0.1768 0.1951 -0.0403 -0.0120 -0.0227 10  LEU   B O   
3875 C  CB  . LEU   B 10  ? 0.2819 0.1721 0.2008 -0.0574 -0.0265 -0.0183 10  LEU   B CB  
3876 C  CG  . LEU   B 10  ? 0.3088 0.1809 0.2438 -0.0523 -0.0541 -0.0112 10  LEU   B CG  
3877 C  CD1 . LEU   B 10  ? 0.3261 0.1954 0.2758 -0.0493 -0.0545 -0.0171 10  LEU   B CD1 
3878 C  CD2 . LEU   B 10  ? 0.3189 0.1846 0.2754 -0.0521 -0.0550 0.0106  10  LEU   B CD2 
3890 N  N   . LYS   B 11  ? 0.2592 0.2006 0.1835 -0.0458 -0.0271 -0.0192 11  LYS   B N   
3891 C  CA  . LYS   B 11  ? 0.2810 0.2319 0.2142 -0.0357 -0.0412 -0.0223 11  LYS   B CA  
3892 C  C   . LYS   B 11  ? 0.2672 0.2132 0.2183 -0.0632 -0.0358 -0.0399 11  LYS   B C   
3893 O  O   . LYS   B 11  ? 0.2827 0.2303 0.2522 -0.0808 -0.0259 -0.0761 11  LYS   B O   
3894 C  CB  . LYS   B 11  ? 0.3166 0.2841 0.2706 -0.0071 -0.0504 -0.0193 11  LYS   B CB  
3895 C  CG  . LYS   B 11  ? 0.3489 0.3195 0.3381 0.0071  -0.0471 -0.0191 11  LYS   B CG  
3896 C  CD  . LYS   B 11  ? 0.3737 0.3427 0.4027 0.0125  -0.0408 -0.0165 11  LYS   B CD  
3897 C  CE  . LYS   B 11  ? 0.3914 0.3575 0.4510 0.0075  -0.0433 -0.0192 11  LYS   B CE  
3898 N  NZ  . LYS   B 11  ? 0.3999 0.3666 0.4740 0.0020  -0.0504 -0.0207 11  LYS   B NZ  
3912 N  N   . LEU   B 12  ? 0.2341 0.1872 0.2188 -0.0580 -0.0367 -0.0395 12  LEU   B N   
3913 C  CA  . LEU   B 12  ? 0.2162 0.1715 0.2457 -0.0476 -0.0261 -0.0322 12  LEU   B CA  
3914 C  C   . LEU   B 12  ? 0.2015 0.1718 0.2574 -0.0476 -0.0356 -0.0240 12  LEU   B C   
3915 O  O   . LEU   B 12  ? 0.2011 0.1753 0.2684 -0.0589 -0.0500 -0.0202 12  LEU   B O   
3916 C  CB  . LEU   B 12  ? 0.2135 0.1516 0.2420 -0.0375 -0.0181 -0.0356 12  LEU   B CB  
3917 C  CG  . LEU   B 12  ? 0.2075 0.1491 0.2487 -0.0372 -0.0155 -0.0278 12  LEU   B CG  
3918 C  CD1 . LEU   B 12  ? 0.2166 0.1481 0.2441 -0.0221 -0.0184 -0.0164 12  LEU   B CD1 
3919 C  CD2 . LEU   B 12  ? 0.2115 0.1538 0.2580 -0.0348 -0.0108 -0.0357 12  LEU   B CD2 
3931 N  N   . THR   B 13  ? 0.1936 0.1737 0.2517 -0.0474 -0.0403 -0.0390 13  THR   B N   
3932 C  CA  . THR   B 13  ? 0.1928 0.1837 0.2386 -0.0559 -0.0493 -0.0296 13  THR   B CA  
3933 C  C   . THR   B 13  ? 0.2309 0.2018 0.2627 -0.0630 -0.0597 -0.0170 13  THR   B C   
3934 O  O   . THR   B 13  ? 0.2457 0.2016 0.2756 -0.0623 -0.0263 -0.0149 13  THR   B O   
3935 C  CB  . THR   B 13  ? 0.1768 0.1865 0.2351 -0.0456 -0.0461 -0.0213 13  THR   B CB  
3936 O  OG1 . THR   B 13  ? 0.1706 0.1762 0.2493 -0.0390 -0.0407 -0.0261 13  THR   B OG1 
3937 C  CG2 . THR   B 13  ? 0.1876 0.1949 0.2470 -0.0409 -0.0236 -0.0078 13  THR   B CG2 
3945 N  N   A ASP   B 14  ? 0.2432 0.2171 0.2740 -0.0680 -0.0935 -0.0078 14  ASP   B N   
3946 N  N   B ASP   B 14  ? 0.2410 0.2140 0.2713 -0.0621 -0.0800 -0.0053 14  ASP   B N   
3947 C  CA  A ASP   B 14  ? 0.2576 0.2302 0.2970 -0.0674 -0.1040 0.0129  14  ASP   B CA  
3948 C  CA  B ASP   B 14  ? 0.2532 0.2247 0.2852 -0.0590 -0.0864 0.0103  14  ASP   B CA  
3949 C  C   A ASP   B 14  ? 0.2461 0.2086 0.2550 -0.0688 -0.0888 0.0153  14  ASP   B C   
3950 C  C   B ASP   B 14  ? 0.2398 0.2049 0.2484 -0.0608 -0.0834 0.0117  14  ASP   B C   
3951 O  O   A ASP   B 14  ? 0.2691 0.2181 0.2639 -0.0685 -0.0817 0.0286  14  ASP   B O   
3952 O  O   B ASP   B 14  ? 0.2540 0.2098 0.2464 -0.0589 -0.0850 0.0188  14  ASP   B O   
3953 C  CB  A ASP   B 14  ? 0.2791 0.2613 0.3786 -0.0678 -0.1239 0.0127  14  ASP   B CB  
3954 C  CB  B ASP   B 14  ? 0.2762 0.2533 0.3453 -0.0568 -0.0924 0.0129  14  ASP   B CB  
3955 C  CG  A ASP   B 14  ? 0.3069 0.2880 0.4538 -0.0608 -0.1169 0.0014  14  ASP   B CG  
3956 C  CG  B ASP   B 14  ? 0.3011 0.2785 0.3996 -0.0520 -0.0854 0.0070  14  ASP   B CG  
3957 O  OD1 A ASP   B 14  ? 0.3207 0.2933 0.4727 -0.0601 -0.1157 -0.0111 14  ASP   B OD1 
3958 O  OD1 B ASP   B 14  ? 0.3129 0.2872 0.4123 -0.0501 -0.0794 0.0020  14  ASP   B OD1 
3959 O  OD2 A ASP   B 14  ? 0.3120 0.2973 0.4871 -0.0591 -0.1098 0.0031  14  ASP   B OD2 
3960 O  OD2 B ASP   B 14  ? 0.3072 0.2866 0.4193 -0.0540 -0.0852 0.0055  14  ASP   B OD2 
3969 N  N   . ASN   B 15  ? 0.2147 0.1835 0.2251 -0.0562 -0.0751 0.0103  15  ASN   B N   
3970 C  CA  . ASN   B 15  ? 0.1758 0.1588 0.2073 -0.0341 -0.0515 0.0029  15  ASN   B CA  
3971 C  C   . ASN   B 15  ? 0.1574 0.1471 0.2023 -0.0231 -0.0357 -0.0103 15  ASN   B C   
3972 O  O   . ASN   B 15  ? 0.1522 0.1405 0.2139 -0.0186 -0.0367 -0.0257 15  ASN   B O   
3973 C  CB  . ASN   B 15  ? 0.1717 0.1528 0.2324 -0.0159 -0.0490 0.0038  15  ASN   B CB  
3974 C  CG  . ASN   B 15  ? 0.1587 0.1553 0.2303 -0.0196 -0.0244 0.0033  15  ASN   B CG  
3975 O  OD1 . ASN   B 15  ? 0.1583 0.1778 0.2624 -0.0396 -0.0302 0.0086  15  ASN   B OD1 
3976 N  ND2 . ASN   B 15  ? 0.1551 0.1332 0.2235 -0.0099 -0.0008 -0.0132 15  ASN   B ND2 
3984 N  N   . VAL   B 16  ? 0.1607 0.1360 0.2058 -0.0269 -0.0442 -0.0078 16  VAL   B N   
3985 C  CA  . VAL   B 16  ? 0.1593 0.1366 0.1875 -0.0231 -0.0329 -0.0190 16  VAL   B CA  
3986 C  C   . VAL   B 16  ? 0.1585 0.1467 0.1886 -0.0331 -0.0292 -0.0174 16  VAL   B C   
3987 O  O   . VAL   B 16  ? 0.1632 0.1606 0.2100 -0.0321 -0.0278 -0.0260 16  VAL   B O   
3988 C  CB  . VAL   B 16  ? 0.1654 0.1386 0.1985 -0.0133 -0.0212 -0.0179 16  VAL   B CB  
3989 C  CG1 . VAL   B 16  ? 0.1745 0.1330 0.1961 -0.0020 -0.0211 -0.0186 16  VAL   B CG1 
3990 C  CG2 . VAL   B 16  ? 0.1693 0.1477 0.2157 -0.0055 -0.0201 -0.0154 16  VAL   B CG2 
4000 N  N   . TYR   B 17  ? 0.1617 0.1532 0.1782 -0.0343 -0.0243 -0.0200 17  TYR   B N   
4001 C  CA  . TYR   B 17  ? 0.1714 0.1699 0.1720 -0.0354 -0.0277 -0.0019 17  TYR   B CA  
4002 C  C   . TYR   B 17  ? 0.1654 0.1468 0.1717 -0.0378 -0.0154 -0.0084 17  TYR   B C   
4003 O  O   . TYR   B 17  ? 0.1655 0.1503 0.1746 -0.0286 -0.0227 -0.0298 17  TYR   B O   
4004 C  CB  . TYR   B 17  ? 0.2031 0.2072 0.2010 -0.0226 -0.0239 0.0289  17  TYR   B CB  
4005 C  CG  . TYR   B 17  ? 0.2322 0.2552 0.2314 -0.0148 -0.0320 0.0423  17  TYR   B CG  
4006 C  CD1 . TYR   B 17  ? 0.2477 0.2709 0.2549 -0.0111 -0.0418 0.0519  17  TYR   B CD1 
4007 C  CD2 . TYR   B 17  ? 0.2530 0.2851 0.2592 -0.0054 -0.0394 0.0363  17  TYR   B CD2 
4008 C  CE1 . TYR   B 17  ? 0.2656 0.2954 0.2690 -0.0029 -0.0523 0.0430  17  TYR   B CE1 
4009 C  CE2 . TYR   B 17  ? 0.2685 0.3051 0.2871 0.0041  -0.0533 0.0395  17  TYR   B CE2 
4010 C  CZ  . TYR   B 17  ? 0.2785 0.3172 0.2905 0.0069  -0.0586 0.0447  17  TYR   B CZ  
4011 O  OH  . TYR   B 17  ? 0.2950 0.3360 0.3109 0.0140  -0.0624 0.0516  17  TYR   B OH  
4021 N  N   . ILE   B 18  ? 0.1736 0.1406 0.1701 -0.0327 -0.0056 -0.0180 18  ILE   B N   
4022 C  CA  . ILE   B 18  ? 0.1773 0.1429 0.1701 -0.0346 -0.0054 -0.0211 18  ILE   B CA  
4023 C  C   . ILE   B 18  ? 0.1874 0.1479 0.1662 -0.0394 -0.0005 -0.0332 18  ILE   B C   
4024 O  O   . ILE   B 18  ? 0.2091 0.1601 0.1801 -0.0339 0.0094  -0.0386 18  ILE   B O   
4025 C  CB  . ILE   B 18  ? 0.1839 0.1468 0.1823 -0.0364 -0.0027 -0.0192 18  ILE   B CB  
4026 C  CG1 . ILE   B 18  ? 0.1835 0.1545 0.1956 -0.0389 0.0003  -0.0074 18  ILE   B CG1 
4027 C  CG2 . ILE   B 18  ? 0.1893 0.1464 0.1848 -0.0403 -0.0086 -0.0230 18  ILE   B CG2 
4028 C  CD1 . ILE   B 18  ? 0.1892 0.1782 0.2227 -0.0387 -0.0157 0.0126  18  ILE   B CD1 
4040 N  N   . LYS   B 19  ? 0.1870 0.1453 0.1867 -0.0242 0.0255  -0.0356 19  LYS   B N   
4041 C  CA  . LYS   B 19  ? 0.1969 0.1515 0.2052 -0.0245 0.0262  -0.0374 19  LYS   B CA  
4042 C  C   . LYS   B 19  ? 0.1790 0.1464 0.2245 -0.0253 0.0323  -0.0475 19  LYS   B C   
4043 O  O   . LYS   B 19  ? 0.1740 0.1521 0.2040 -0.0130 0.0200  -0.0439 19  LYS   B O   
4044 C  CB  . LYS   B 19  ? 0.2192 0.1715 0.2120 -0.0292 0.0364  -0.0255 19  LYS   B CB  
4045 C  CG  . LYS   B 19  ? 0.2436 0.1926 0.2371 -0.0403 0.0460  -0.0320 19  LYS   B CG  
4046 C  CD  . LYS   B 19  ? 0.2693 0.2209 0.2438 -0.0506 0.0624  -0.0288 19  LYS   B CD  
4047 C  CE  . LYS   B 19  ? 0.2906 0.2460 0.2735 -0.0497 0.0652  -0.0321 19  LYS   B CE  
4048 N  NZ  . LYS   B 19  ? 0.3013 0.2626 0.2756 -0.0547 0.0659  -0.0265 19  LYS   B NZ  
4062 N  N   . ASN   B 20  ? 0.1784 0.1542 0.2522 -0.0190 0.0432  -0.0596 20  ASN   B N   
4063 C  CA  . ASN   B 20  ? 0.1833 0.1737 0.2730 -0.0116 0.0410  -0.0746 20  ASN   B CA  
4064 C  C   . ASN   B 20  ? 0.1792 0.1896 0.2684 -0.0197 0.0527  -0.0859 20  ASN   B C   
4065 O  O   . ASN   B 20  ? 0.1972 0.2248 0.2846 -0.0315 0.0530  -0.0828 20  ASN   B O   
4066 C  CB  . ASN   B 20  ? 0.2102 0.1835 0.3101 0.0103  0.0273  -0.0733 20  ASN   B CB  
4067 C  CG  . ASN   B 20  ? 0.2353 0.1933 0.3326 0.0395  0.0229  -0.0772 20  ASN   B CG  
4068 O  OD1 . ASN   B 20  ? 0.2619 0.2182 0.3586 0.0574  0.0201  -0.0847 20  ASN   B OD1 
4069 N  ND2 . ASN   B 20  ? 0.2274 0.1920 0.3187 0.0390  0.0125  -0.0674 20  ASN   B ND2 
4076 N  N   . ALA   B 21  ? 0.1812 0.1771 0.2611 -0.0268 0.0462  -0.0685 21  ALA   B N   
4077 C  CA  . ALA   B 21  ? 0.1861 0.1814 0.2741 -0.0321 0.0296  -0.0532 21  ALA   B CA  
4078 C  C   . ALA   B 21  ? 0.1852 0.1568 0.2588 -0.0212 0.0330  -0.0360 21  ALA   B C   
4079 O  O   . ALA   B 21  ? 0.1924 0.1466 0.2571 -0.0282 0.0339  -0.0245 21  ALA   B O   
4080 C  CB  . ALA   B 21  ? 0.2044 0.2062 0.2826 -0.0413 0.0316  -0.0388 21  ALA   B CB  
4086 N  N   . ASP   B 22  ? 0.1739 0.1499 0.2584 -0.0206 0.0236  -0.0292 22  ASP   B N   
4087 C  CA  . ASP   B 22  ? 0.1707 0.1435 0.2509 -0.0103 0.0176  -0.0188 22  ASP   B CA  
4088 C  C   . ASP   B 22  ? 0.1680 0.1392 0.2059 -0.0125 0.0183  -0.0070 22  ASP   B C   
4089 O  O   . ASP   B 22  ? 0.1666 0.1424 0.2080 -0.0133 0.0083  -0.0061 22  ASP   B O   
4090 C  CB  . ASP   B 22  ? 0.1803 0.1560 0.2874 -0.0052 0.0153  -0.0083 22  ASP   B CB  
4091 C  CG  . ASP   B 22  ? 0.1823 0.1738 0.3307 0.0001  -0.0074 -0.0063 22  ASP   B CG  
4092 O  OD1 . ASP   B 22  ? 0.1933 0.1656 0.3311 0.0057  -0.0199 -0.0037 22  ASP   B OD1 
4093 O  OD2 . ASP   B 22  ? 0.1908 0.2061 0.3846 0.0089  -0.0256 -0.0244 22  ASP   B OD2 
4098 N  N   . ILE   B 23  ? 0.1706 0.1349 0.1890 -0.0094 0.0084  0.0166  23  ILE   B N   
4099 C  CA  . ILE   B 23  ? 0.1622 0.1342 0.1725 -0.0121 0.0038  0.0070  23  ILE   B CA  
4100 C  C   . ILE   B 23  ? 0.1551 0.1330 0.1766 -0.0099 -0.0011 0.0008  23  ILE   B C   
4101 O  O   . ILE   B 23  ? 0.1491 0.1339 0.1576 -0.0097 -0.0002 0.0039  23  ILE   B O   
4102 C  CB  . ILE   B 23  ? 0.1573 0.1412 0.1787 -0.0207 0.0029  0.0100  23  ILE   B CB  
4103 C  CG1 . ILE   B 23  ? 0.1644 0.1535 0.1861 -0.0151 0.0055  0.0176  23  ILE   B CG1 
4104 C  CG2 . ILE   B 23  ? 0.1624 0.1612 0.1932 -0.0220 0.0039  0.0088  23  ILE   B CG2 
4105 C  CD1 . ILE   B 23  ? 0.1642 0.1649 0.1961 -0.0080 0.0095  0.0196  23  ILE   B CD1 
4117 N  N   . VAL   B 24  ? 0.1545 0.1329 0.1791 -0.0093 -0.0041 0.0009  24  VAL   B N   
4118 C  CA  . VAL   B 24  ? 0.1527 0.1393 0.1982 -0.0046 -0.0130 -0.0035 24  VAL   B CA  
4119 C  C   . VAL   B 24  ? 0.1500 0.1440 0.1998 -0.0115 -0.0095 0.0003  24  VAL   B C   
4120 O  O   . VAL   B 24  ? 0.1484 0.1474 0.2204 -0.0160 -0.0054 0.0102  24  VAL   B O   
4121 C  CB  . VAL   B 24  ? 0.1627 0.1605 0.2060 0.0027  -0.0265 -0.0034 24  VAL   B CB  
4122 C  CG1 . VAL   B 24  ? 0.1641 0.1667 0.2265 -0.0054 -0.0312 -0.0029 24  VAL   B CG1 
4123 C  CG2 . VAL   B 24  ? 0.1710 0.1871 0.2149 0.0113  -0.0287 -0.0073 24  VAL   B CG2 
4133 N  N   . GLU   B 25  ? 0.1712 0.1575 0.1986 -0.0094 0.0003  0.0000  25  GLU   B N   
4134 C  CA  . GLU   B 25  ? 0.1823 0.1843 0.2206 0.0059  0.0151  -0.0063 25  GLU   B CA  
4135 C  C   . GLU   B 25  ? 0.1789 0.1738 0.1931 -0.0073 0.0142  0.0009  25  GLU   B C   
4136 O  O   . GLU   B 25  ? 0.1863 0.1876 0.2051 -0.0097 0.0237  0.0121  25  GLU   B O   
4137 C  CB  . GLU   B 25  ? 0.2185 0.2295 0.2826 0.0295  0.0271  -0.0063 25  GLU   B CB  
4138 C  CG  . GLU   B 25  ? 0.2657 0.2899 0.3912 0.0382  0.0286  -0.0059 25  GLU   B CG  
4139 C  CD  . GLU   B 25  ? 0.3019 0.3572 0.4880 0.0363  0.0198  -0.0071 25  GLU   B CD  
4140 O  OE1 . GLU   B 25  ? 0.3319 0.3816 0.5120 0.0398  0.0229  -0.0035 25  GLU   B OE1 
4141 O  OE2 . GLU   B 25  ? 0.3273 0.3773 0.5136 0.0354  0.0087  -0.0149 25  GLU   B OE2 
4148 N  N   . GLU   B 26  ? 0.1751 0.1658 0.1764 -0.0278 0.0095  0.0024  26  GLU   B N   
4149 C  CA  . GLU   B 26  ? 0.1747 0.1788 0.1833 -0.0363 -0.0001 0.0048  26  GLU   B CA  
4150 C  C   . GLU   B 26  ? 0.1606 0.1788 0.1642 -0.0275 0.0069  0.0171  26  GLU   B C   
4151 O  O   . GLU   B 26  ? 0.1817 0.1998 0.1679 -0.0256 0.0014  0.0215  26  GLU   B O   
4152 C  CB  . GLU   B 26  ? 0.2065 0.1983 0.2130 -0.0464 0.0025  0.0151  26  GLU   B CB  
4153 C  CG  . GLU   B 26  ? 0.2491 0.2350 0.2747 -0.0468 0.0101  -0.0110 26  GLU   B CG  
4154 C  CD  . GLU   B 26  ? 0.2705 0.2584 0.2717 -0.0670 0.0218  -0.0462 26  GLU   B CD  
4155 O  OE1 . GLU   B 26  ? 0.2855 0.2408 0.2711 -0.0773 0.0605  -0.0519 26  GLU   B OE1 
4156 O  OE2 . GLU   B 26  ? 0.2740 0.2981 0.3262 -0.0595 0.0142  -0.0371 26  GLU   B OE2 
4163 N  N   . ALA   B 27  ? 0.1480 0.1619 0.1610 -0.0213 0.0068  0.0251  27  ALA   B N   
4164 C  CA  . ALA   B 27  ? 0.1481 0.1583 0.1822 -0.0127 0.0031  0.0363  27  ALA   B CA  
4165 C  C   . ALA   B 27  ? 0.1503 0.1680 0.2065 -0.0120 0.0131  0.0459  27  ALA   B C   
4166 O  O   . ALA   B 27  ? 0.1596 0.1723 0.2091 -0.0037 0.0218  0.0432  27  ALA   B O   
4167 C  CB  . ALA   B 27  ? 0.1643 0.1401 0.1928 -0.0091 0.0013  0.0320  27  ALA   B CB  
4173 N  N   . LYS   B 28  ? 0.1425 0.1891 0.2467 -0.0222 0.0209  0.0607  28  LYS   B N   
4174 C  CA  . LYS   B 28  ? 0.1621 0.2304 0.2719 -0.0077 0.0573  0.0865  28  LYS   B CA  
4175 C  C   . LYS   B 28  ? 0.1865 0.2452 0.2637 0.0003  0.0681  0.0766  28  LYS   B C   
4176 O  O   . LYS   B 28  ? 0.2094 0.2477 0.2788 -0.0034 0.0629  0.0762  28  LYS   B O   
4177 C  CB  . LYS   B 28  ? 0.1849 0.2734 0.3334 0.0058  0.0874  0.1104  28  LYS   B CB  
4178 C  CG  . LYS   B 28  ? 0.2278 0.3255 0.3769 0.0198  0.0930  0.1280  28  LYS   B CG  
4179 C  CD  . LYS   B 28  ? 0.2837 0.3895 0.4339 0.0295  0.1088  0.1337  28  LYS   B CD  
4180 C  CE  . LYS   B 28  ? 0.3487 0.4441 0.4873 0.0372  0.1101  0.1386  28  LYS   B CE  
4181 N  NZ  . LYS   B 28  ? 0.3814 0.4768 0.5005 0.0411  0.1076  0.1436  28  LYS   B NZ  
4195 N  N   . LYS   B 29  ? 0.2050 0.2675 0.2650 0.0207  0.0764  0.0630  29  LYS   B N   
4196 C  CA  . LYS   B 29  ? 0.2475 0.3007 0.2909 0.0232  0.0766  0.0598  29  LYS   B CA  
4197 C  C   . LYS   B 29  ? 0.2385 0.2975 0.2487 0.0175  0.0586  0.0746  29  LYS   B C   
4198 O  O   . LYS   B 29  ? 0.2546 0.3152 0.2471 0.0218  0.0548  0.0768  29  LYS   B O   
4199 C  CB  . LYS   B 29  ? 0.3049 0.3386 0.3666 0.0243  0.0770  0.0458  29  LYS   B CB  
4200 C  CG  . LYS   B 29  ? 0.3539 0.3709 0.4579 0.0206  0.0787  0.0425  29  LYS   B CG  
4201 C  CD  . LYS   B 29  ? 0.3975 0.3934 0.5268 0.0133  0.0870  0.0403  29  LYS   B CD  
4202 C  CE  . LYS   B 29  ? 0.4324 0.4093 0.5692 0.0067  0.0948  0.0356  29  LYS   B CE  
4203 N  NZ  . LYS   B 29  ? 0.4546 0.4168 0.6052 0.0035  0.0967  0.0293  29  LYS   B NZ  
4217 N  N   . VAL   B 30  ? 0.2081 0.2779 0.2340 0.0066  0.0433  0.0770  30  VAL   B N   
4218 C  CA  . VAL   B 30  ? 0.1977 0.2669 0.2650 -0.0070 0.0081  0.0804  30  VAL   B CA  
4219 C  C   . VAL   B 30  ? 0.1823 0.2588 0.2560 -0.0049 0.0159  0.0944  30  VAL   B C   
4220 O  O   . VAL   B 30  ? 0.1938 0.2766 0.2506 -0.0005 0.0159  0.1079  30  VAL   B O   
4221 C  CB  . VAL   B 30  ? 0.2038 0.2640 0.3081 -0.0241 -0.0271 0.0750  30  VAL   B CB  
4222 C  CG1 . VAL   B 30  ? 0.2069 0.2680 0.3113 -0.0266 -0.0245 0.0698  30  VAL   B CG1 
4223 C  CG2 . VAL   B 30  ? 0.2138 0.2669 0.3283 -0.0326 -0.0451 0.0663  30  VAL   B CG2 
4233 N  N   . LYS   B 31  ? 0.1688 0.2260 0.2824 -0.0207 0.0148  0.1013  31  LYS   B N   
4234 C  CA  . LYS   B 31  ? 0.1589 0.2235 0.3228 -0.0374 0.0072  0.1035  31  LYS   B CA  
4235 C  C   . LYS   B 31  ? 0.1493 0.1865 0.2768 -0.0362 -0.0223 0.0889  31  LYS   B C   
4236 O  O   . LYS   B 31  ? 0.1558 0.2015 0.3000 -0.0283 -0.0177 0.1019  31  LYS   B O   
4237 C  CB  . LYS   B 31  ? 0.1803 0.2774 0.3845 -0.0378 0.0264  0.1177  31  LYS   B CB  
4238 C  CG  . LYS   B 31  ? 0.2153 0.3283 0.4266 -0.0353 0.0325  0.1156  31  LYS   B CG  
4239 C  CD  . LYS   B 31  ? 0.2589 0.3818 0.4645 -0.0306 0.0280  0.1042  31  LYS   B CD  
4240 C  CE  . LYS   B 31  ? 0.2865 0.4240 0.5052 -0.0302 0.0197  0.0931  31  LYS   B CE  
4241 N  NZ  . LYS   B 31  ? 0.3157 0.4544 0.5121 -0.0262 0.0090  0.0886  31  LYS   B NZ  
4255 N  N   . PRO   B 32  ? 0.1614 0.1512 0.2093 -0.0315 -0.0395 0.0432  32  PRO   B N   
4256 C  CA  . PRO   B 32  ? 0.1694 0.1449 0.1713 -0.0346 -0.0409 0.0293  32  PRO   B CA  
4257 C  C   . PRO   B 32  ? 0.1804 0.1407 0.1698 -0.0338 -0.0510 0.0388  32  PRO   B C   
4258 O  O   . PRO   B 32  ? 0.1883 0.1425 0.2017 -0.0392 -0.0695 0.0381  32  PRO   B O   
4259 C  CB  . PRO   B 32  ? 0.1816 0.1379 0.1684 -0.0387 -0.0308 0.0127  32  PRO   B CB  
4260 C  CG  . PRO   B 32  ? 0.1970 0.1306 0.1786 -0.0341 -0.0458 0.0203  32  PRO   B CG  
4261 C  CD  . PRO   B 32  ? 0.1811 0.1364 0.1977 -0.0254 -0.0543 0.0279  32  PRO   B CD  
4269 N  N   . THR   B 33  ? 0.1823 0.1308 0.1608 -0.0287 -0.0475 0.0229  33  THR   B N   
4270 C  CA  . THR   B 33  ? 0.1853 0.1356 0.1585 -0.0329 -0.0411 0.0291  33  THR   B CA  
4271 C  C   . THR   B 33  ? 0.1860 0.1258 0.1550 -0.0320 -0.0405 0.0161  33  THR   B C   
4272 O  O   . THR   B 33  ? 0.2078 0.1300 0.1676 -0.0427 -0.0507 0.0175  33  THR   B O   
4273 C  CB  . THR   B 33  ? 0.1945 0.1464 0.1643 -0.0204 -0.0468 0.0273  33  THR   B CB  
4274 O  OG1 . THR   B 33  ? 0.1846 0.1526 0.1710 -0.0247 -0.0439 0.0337  33  THR   B OG1 
4275 C  CG2 . THR   B 33  ? 0.2188 0.1530 0.1761 -0.0090 -0.0463 0.0254  33  THR   B CG2 
4283 N  N   . VAL   B 34  ? 0.1674 0.1229 0.1439 -0.0332 -0.0351 0.0120  34  VAL   B N   
4284 C  CA  . VAL   B 34  ? 0.1542 0.1240 0.1349 -0.0262 -0.0314 0.0036  34  VAL   B CA  
4285 C  C   . VAL   B 34  ? 0.1402 0.1179 0.1222 -0.0288 -0.0203 0.0046  34  VAL   B C   
4286 O  O   . VAL   B 34  ? 0.1605 0.1223 0.1311 -0.0232 -0.0304 0.0028  34  VAL   B O   
4287 C  CB  . VAL   B 34  ? 0.1619 0.1323 0.1627 -0.0116 -0.0248 0.0055  34  VAL   B CB  
4288 C  CG1 . VAL   B 34  ? 0.1613 0.1451 0.1633 -0.0057 -0.0174 0.0020  34  VAL   B CG1 
4289 C  CG2 . VAL   B 34  ? 0.1717 0.1354 0.1919 -0.0066 -0.0204 0.0102  34  VAL   B CG2 
4299 N  N   . VAL   B 35  ? 0.1367 0.1140 0.1181 -0.0228 -0.0120 0.0079  35  VAL   B N   
4300 C  CA  . VAL   B 35  ? 0.1323 0.1155 0.1153 -0.0216 -0.0099 0.0038  35  VAL   B CA  
4301 C  C   . VAL   B 35  ? 0.1252 0.1098 0.1183 -0.0166 -0.0123 0.0037  35  VAL   B C   
4302 O  O   . VAL   B 35  ? 0.1310 0.1148 0.1292 -0.0195 -0.0038 -0.0036 35  VAL   B O   
4303 C  CB  . VAL   B 35  ? 0.1306 0.1326 0.1288 -0.0181 0.0081  0.0053  35  VAL   B CB  
4304 C  CG1 . VAL   B 35  ? 0.1266 0.1432 0.1542 -0.0163 -0.0026 0.0026  35  VAL   B CG1 
4305 C  CG2 . VAL   B 35  ? 0.1366 0.1341 0.1467 -0.0093 0.0024  -0.0054 35  VAL   B CG2 
4315 N  N   . VAL   B 36  ? 0.1292 0.1108 0.1193 -0.0171 -0.0120 0.0079  36  VAL   B N   
4316 C  CA  . VAL   B 36  ? 0.1222 0.1113 0.1088 -0.0116 -0.0069 0.0074  36  VAL   B CA  
4317 C  C   . VAL   B 36  ? 0.1175 0.1115 0.1054 -0.0132 -0.0001 0.0048  36  VAL   B C   
4318 O  O   . VAL   B 36  ? 0.1283 0.1199 0.1343 -0.0091 -0.0024 -0.0089 36  VAL   B O   
4319 C  CB  . VAL   B 36  ? 0.1216 0.1176 0.1200 -0.0121 -0.0040 0.0007  36  VAL   B CB  
4320 C  CG1 . VAL   B 36  ? 0.1206 0.1306 0.1379 -0.0139 -0.0062 -0.0010 36  VAL   B CG1 
4321 C  CG2 . VAL   B 36  ? 0.1253 0.1202 0.1390 -0.0127 -0.0112 0.0088  36  VAL   B CG2 
4331 N  N   . ASN   B 37  ? 0.1232 0.1175 0.1119 -0.0025 -0.0088 0.0052  37  ASN   B N   
4332 C  CA  . ASN   B 37  ? 0.1240 0.1199 0.1229 0.0012  -0.0031 0.0052  37  ASN   B CA  
4333 C  C   . ASN   B 37  ? 0.1236 0.1187 0.1167 0.0047  -0.0033 0.0011  37  ASN   B C   
4334 O  O   . ASN   B 37  ? 0.1315 0.1262 0.1273 0.0011  0.0034  0.0077  37  ASN   B O   
4335 C  CB  . ASN   B 37  ? 0.1233 0.1195 0.1153 -0.0014 -0.0072 0.0056  37  ASN   B CB  
4336 C  CG  . ASN   B 37  ? 0.1269 0.1230 0.1237 -0.0019 -0.0104 0.0042  37  ASN   B CG  
4337 O  OD1 . ASN   B 37  ? 0.1330 0.1246 0.1444 0.0087  -0.0120 0.0002  37  ASN   B OD1 
4338 N  ND2 . ASN   B 37  ? 0.1278 0.1198 0.1274 -0.0005 -0.0147 0.0054  37  ASN   B ND2 
4345 N  N   . ALA   B 38  ? 0.1315 0.1156 0.1193 0.0074  0.0065  0.0017  38  ALA   B N   
4346 C  CA  . ALA   B 38  ? 0.1423 0.1224 0.1221 0.0029  0.0071  0.0086  38  ALA   B CA  
4347 C  C   . ALA   B 38  ? 0.1369 0.1188 0.1196 0.0008  0.0040  0.0132  38  ALA   B C   
4348 O  O   . ALA   B 38  ? 0.1460 0.1307 0.1355 0.0073  0.0026  0.0121  38  ALA   B O   
4349 C  CB  . ALA   B 38  ? 0.1630 0.1263 0.1357 -0.0107 0.0104  0.0072  38  ALA   B CB  
4355 N  N   . ALA   B 39  ? 0.1339 0.1220 0.1178 0.0073  -0.0029 0.0064  39  ALA   B N   
4356 C  CA  . ALA   B 39  ? 0.1435 0.1272 0.1219 0.0050  -0.0061 0.0003  39  ALA   B CA  
4357 C  C   . ALA   B 39  ? 0.1455 0.1362 0.0997 0.0096  0.0005  0.0049  39  ALA   B C   
4358 O  O   . ALA   B 39  ? 0.1454 0.1398 0.1353 -0.0014 0.0043  0.0088  39  ALA   B O   
4359 C  CB  . ALA   B 39  ? 0.1494 0.1311 0.1378 -0.0025 0.0039  0.0004  39  ALA   B CB  
4365 N  N   . ASN   B 40  ? 0.1512 0.1566 0.1200 -0.0009 0.0039  -0.0060 40  ASN   B N   
4366 C  CA  . ASN   B 40  ? 0.1537 0.1605 0.1267 0.0043  0.0034  -0.0061 40  ASN   B CA  
4367 C  C   . ASN   B 40  ? 0.1582 0.1614 0.1082 0.0096  -0.0059 0.0040  40  ASN   B C   
4368 O  O   . ASN   B 40  ? 0.1511 0.1545 0.1251 0.0125  -0.0093 0.0046  40  ASN   B O   
4369 C  CB  . ASN   B 40  ? 0.1664 0.1610 0.1515 0.0109  -0.0060 0.0089  40  ASN   B CB  
4370 C  CG  . ASN   B 40  ? 0.1716 0.1645 0.1812 0.0069  -0.0192 0.0150  40  ASN   B CG  
4371 O  OD1 . ASN   B 40  ? 0.1695 0.1615 0.2510 0.0037  -0.0311 0.0167  40  ASN   B OD1 
4372 N  ND2 . ASN   B 40  ? 0.1752 0.1635 0.1626 0.0071  -0.0130 0.0098  40  ASN   B ND2 
4379 N  N   . VAL   B 41  ? 0.1665 0.1637 0.1183 0.0142  0.0031  0.0025  41  VAL   B N   
4380 C  CA  . VAL   B 41  ? 0.1729 0.1787 0.1267 0.0110  0.0026  -0.0083 41  VAL   B CA  
4381 C  C   . VAL   B 41  ? 0.1710 0.1763 0.1184 0.0171  -0.0050 -0.0105 41  VAL   B C   
4382 O  O   . VAL   B 41  ? 0.1709 0.1701 0.1289 0.0148  -0.0116 -0.0175 41  VAL   B O   
4383 C  CB  . VAL   B 41  ? 0.1880 0.2023 0.1444 -0.0042 0.0238  -0.0179 41  VAL   B CB  
4384 C  CG1 . VAL   B 41  ? 0.1853 0.2047 0.1711 -0.0059 0.0380  -0.0181 41  VAL   B CG1 
4385 C  CG2 . VAL   B 41  ? 0.2022 0.2215 0.1514 -0.0124 0.0202  -0.0153 41  VAL   B CG2 
4395 N  N   . TYR   B 42  ? 0.1736 0.1792 0.1314 0.0190  -0.0189 -0.0007 42  TYR   B N   
4396 C  CA  . TYR   B 42  ? 0.1792 0.1866 0.1384 0.0167  -0.0223 -0.0122 42  TYR   B CA  
4397 C  C   . TYR   B 42  ? 0.1612 0.1652 0.1410 0.0211  -0.0197 -0.0108 42  TYR   B C   
4398 O  O   . TYR   B 42  ? 0.1627 0.1705 0.1652 0.0135  -0.0246 -0.0241 42  TYR   B O   
4399 C  CB  . TYR   B 42  ? 0.2083 0.2222 0.1499 0.0069  -0.0282 -0.0017 42  TYR   B CB  
4400 C  CG  . TYR   B 42  ? 0.2110 0.2444 0.1418 -0.0007 -0.0237 0.0037  42  TYR   B CG  
4401 C  CD1 . TYR   B 42  ? 0.2118 0.2463 0.1148 -0.0026 -0.0103 -0.0055 42  TYR   B CD1 
4402 C  CD2 . TYR   B 42  ? 0.2229 0.2621 0.1912 -0.0012 -0.0086 0.0173  42  TYR   B CD2 
4403 C  CE1 . TYR   B 42  ? 0.2270 0.2666 0.1333 0.0049  0.0021  0.0064  42  TYR   B CE1 
4404 C  CE2 . TYR   B 42  ? 0.2283 0.2763 0.1920 0.0037  0.0158  0.0308  42  TYR   B CE2 
4405 C  CZ  . TYR   B 42  ? 0.2421 0.2904 0.1800 0.0192  0.0245  0.0190  42  TYR   B CZ  
4406 O  OH  . TYR   B 42  ? 0.2743 0.3213 0.2234 0.0386  0.0281  0.0309  42  TYR   B OH  
4416 N  N   . LEU   B 43  ? 0.1502 0.1470 0.1300 0.0098  -0.0136 -0.0114 43  LEU   B N   
4417 C  CA  . LEU   B 43  ? 0.1549 0.1469 0.1284 0.0046  -0.0128 -0.0046 43  LEU   B CA  
4418 C  C   . LEU   B 43  ? 0.1594 0.1483 0.1369 0.0048  -0.0147 0.0008  43  LEU   B C   
4419 O  O   . LEU   B 43  ? 0.1554 0.1521 0.1554 0.0066  -0.0177 0.0050  43  LEU   B O   
4420 C  CB  . LEU   B 43  ? 0.1501 0.1401 0.1381 0.0012  -0.0227 -0.0090 43  LEU   B CB  
4421 C  CG  . LEU   B 43  ? 0.1560 0.1395 0.1407 0.0008  -0.0217 -0.0068 43  LEU   B CG  
4422 C  CD1 . LEU   B 43  ? 0.1670 0.1461 0.1788 -0.0044 -0.0412 -0.0116 43  LEU   B CD1 
4423 C  CD2 . LEU   B 43  ? 0.1556 0.1387 0.1467 -0.0056 -0.0274 -0.0054 43  LEU   B CD2 
4435 N  N   . LYS   B 44  ? 0.1564 0.1481 0.1310 0.0086  -0.0049 -0.0046 44  LYS   B N   
4436 C  CA  . LYS   B 44  ? 0.1668 0.1577 0.1400 0.0105  -0.0134 0.0057  44  LYS   B CA  
4437 C  C   . LYS   B 44  ? 0.1564 0.1488 0.1454 0.0131  -0.0120 0.0032  44  LYS   B C   
4438 O  O   . LYS   B 44  ? 0.1725 0.1510 0.1636 0.0033  -0.0045 0.0065  44  LYS   B O   
4439 C  CB  . LYS   B 44  ? 0.1968 0.1782 0.1579 0.0179  -0.0250 0.0107  44  LYS   B CB  
4440 C  CG  . LYS   B 44  ? 0.2372 0.2050 0.1919 0.0096  -0.0459 0.0040  44  LYS   B CG  
4441 C  CD  . LYS   B 44  ? 0.2751 0.2291 0.2539 -0.0025 -0.0493 0.0012  44  LYS   B CD  
4442 C  CE  . LYS   B 44  ? 0.3049 0.2495 0.2925 -0.0052 -0.0559 0.0168  44  LYS   B CE  
4443 N  NZ  . LYS   B 44  ? 0.3140 0.2554 0.3146 -0.0019 -0.0698 0.0389  44  LYS   B NZ  
4457 N  N   . HIS   B 45  ? 0.1512 0.1499 0.1370 0.0081  -0.0092 0.0073  45  HIS   B N   
4458 C  CA  . HIS   B 45  ? 0.1566 0.1473 0.1364 0.0111  -0.0098 -0.0028 45  HIS   B CA  
4459 C  C   . HIS   B 45  ? 0.1785 0.1692 0.1725 0.0179  -0.0209 -0.0006 45  HIS   B C   
4460 O  O   . HIS   B 45  ? 0.1853 0.1980 0.2195 0.0385  0.0071  0.0012  45  HIS   B O   
4461 C  CB  . HIS   B 45  ? 0.1500 0.1506 0.1385 -0.0012 -0.0092 -0.0047 45  HIS   B CB  
4462 C  CG  . HIS   B 45  ? 0.1504 0.1455 0.1377 -0.0026 -0.0132 -0.0025 45  HIS   B CG  
4463 N  ND1 . HIS   B 45  ? 0.1531 0.1382 0.1466 0.0013  -0.0205 -0.0061 45  HIS   B ND1 
4464 C  CD2 . HIS   B 45  ? 0.1592 0.1492 0.1553 -0.0071 -0.0174 -0.0009 45  HIS   B CD2 
4465 C  CE1 . HIS   B 45  ? 0.1654 0.1324 0.1331 -0.0035 -0.0226 -0.0066 45  HIS   B CE1 
4466 N  NE2 . HIS   B 45  ? 0.1687 0.1398 0.1384 -0.0041 -0.0194 -0.0039 45  HIS   B NE2 
4474 N  N   A GLY   B 46  ? 0.1877 0.1638 0.2010 0.0209  -0.0362 0.0045  46  GLY   B N   
4475 N  N   B GLY   B 46  ? 0.1866 0.1695 0.1926 0.0187  -0.0302 0.0072  46  GLY   B N   
4476 C  CA  A GLY   B 46  ? 0.2010 0.1767 0.2366 0.0218  -0.0385 0.0078  46  GLY   B CA  
4477 C  CA  B GLY   B 46  ? 0.1978 0.1822 0.2162 0.0194  -0.0325 0.0150  46  GLY   B CA  
4478 C  C   A GLY   B 46  ? 0.2042 0.1924 0.2820 0.0265  -0.0362 0.0052  46  GLY   B C   
4479 C  C   B GLY   B 46  ? 0.2038 0.1978 0.2505 0.0234  -0.0309 0.0205  46  GLY   B C   
4480 O  O   A GLY   B 46  ? 0.2172 0.2052 0.3580 0.0323  -0.0258 -0.0143 46  GLY   B O   
4481 O  O   B GLY   B 46  ? 0.2155 0.2107 0.2722 0.0297  -0.0279 0.0355  46  GLY   B O   
4488 N  N   . GLY   B 47  ? 0.1994 0.1985 0.2559 0.0143  -0.0203 -0.0006 47  GLY   B N   
4489 C  CA  . GLY   B 47  ? 0.1853 0.1696 0.2185 0.0103  -0.0169 -0.0009 47  GLY   B CA  
4490 C  C   . GLY   B 47  ? 0.1653 0.1480 0.1857 0.0038  -0.0041 0.0102  47  GLY   B C   
4491 O  O   . GLY   B 47  ? 0.1749 0.1331 0.1914 0.0053  -0.0078 0.0096  47  GLY   B O   
4496 N  N   . GLY   B 48  ? 0.1504 0.1416 0.1750 0.0057  -0.0057 0.0159  48  GLY   B N   
4497 C  CA  . GLY   B 48  ? 0.1470 0.1356 0.1751 0.0008  0.0001  0.0111  48  GLY   B CA  
4498 C  C   . GLY   B 48  ? 0.1408 0.1318 0.1743 0.0004  0.0030  0.0053  48  GLY   B C   
4499 O  O   . GLY   B 48  ? 0.1369 0.1346 0.1890 0.0053  -0.0064 0.0041  48  GLY   B O   
4503 N  N   . VAL   B 49  ? 0.1413 0.1387 0.1564 0.0091  0.0028  0.0061  49  VAL   B N   
4504 C  CA  . VAL   B 49  ? 0.1464 0.1479 0.1448 0.0123  -0.0130 -0.0032 49  VAL   B CA  
4505 C  C   . VAL   B 49  ? 0.1342 0.1372 0.1248 0.0134  -0.0034 0.0090  49  VAL   B C   
4506 O  O   . VAL   B 49  ? 0.1432 0.1414 0.1406 0.0075  0.0037  0.0095  49  VAL   B O   
4507 C  CB  . VAL   B 49  ? 0.1486 0.1620 0.1735 0.0067  -0.0239 -0.0055 49  VAL   B CB  
4508 C  CG1 . VAL   B 49  ? 0.1450 0.1717 0.1703 0.0118  -0.0272 -0.0006 49  VAL   B CG1 
4509 C  CG2 . VAL   B 49  ? 0.1657 0.1740 0.2025 -0.0049 -0.0429 -0.0154 49  VAL   B CG2 
4519 N  N   . ALA   B 50  ? 0.1314 0.1300 0.1309 0.0059  0.0003  0.0042  50  ALA   B N   
4520 C  CA  . ALA   B 50  ? 0.1310 0.1245 0.1322 0.0054  -0.0038 0.0059  50  ALA   B CA  
4521 C  C   . ALA   B 50  ? 0.1389 0.1300 0.1290 0.0062  0.0041  0.0019  50  ALA   B C   
4522 O  O   . ALA   B 50  ? 0.1388 0.1327 0.1353 0.0061  0.0027  0.0024  50  ALA   B O   
4523 C  CB  . ALA   B 50  ? 0.1373 0.1293 0.1432 -0.0026 -0.0036 0.0111  50  ALA   B CB  
4529 N  N   . GLY   B 51  ? 0.1376 0.1396 0.1455 0.0129  -0.0093 0.0117  51  GLY   B N   
4530 C  CA  . GLY   B 51  ? 0.1372 0.1446 0.1708 0.0155  -0.0123 0.0169  51  GLY   B CA  
4531 C  C   . GLY   B 51  ? 0.1342 0.1414 0.1593 0.0179  -0.0112 0.0109  51  GLY   B C   
4532 O  O   . GLY   B 51  ? 0.1393 0.1546 0.1779 0.0105  -0.0098 -0.0009 51  GLY   B O   
4536 N  N   . ALA   B 52  ? 0.1349 0.1373 0.1579 0.0144  -0.0068 0.0140  52  ALA   B N   
4537 C  CA  . ALA   B 52  ? 0.1431 0.1435 0.1609 0.0164  -0.0010 0.0055  52  ALA   B CA  
4538 C  C   . ALA   B 52  ? 0.1337 0.1438 0.1560 0.0101  0.0004  0.0059  52  ALA   B C   
4539 O  O   . ALA   B 52  ? 0.1377 0.1456 0.1673 0.0107  0.0050  0.0060  52  ALA   B O   
4540 C  CB  . ALA   B 52  ? 0.1596 0.1435 0.1666 0.0081  0.0080  0.0037  52  ALA   B CB  
4546 N  N   . LEU   B 53  ? 0.1301 0.1395 0.1422 0.0147  0.0020  0.0039  53  LEU   B N   
4547 C  CA  . LEU   B 53  ? 0.1294 0.1469 0.1338 0.0114  -0.0010 0.0089  53  LEU   B CA  
4548 C  C   . LEU   B 53  ? 0.1367 0.1397 0.1373 0.0102  0.0093  0.0068  53  LEU   B C   
4549 O  O   . LEU   B 53  ? 0.1384 0.1500 0.1538 0.0024  0.0085  0.0120  53  LEU   B O   
4550 C  CB  . LEU   B 53  ? 0.1272 0.1521 0.1485 0.0082  0.0020  0.0205  53  LEU   B CB  
4551 C  CG  . LEU   B 53  ? 0.1299 0.1595 0.1535 0.0024  0.0010  0.0211  53  LEU   B CG  
4552 C  CD1 . LEU   B 53  ? 0.1380 0.1769 0.1802 0.0127  0.0007  0.0041  53  LEU   B CD1 
4553 C  CD2 . LEU   B 53  ? 0.1440 0.1899 0.1806 -0.0071 -0.0066 -0.0059 53  LEU   B CD2 
4565 N  N   . ASN   B 54  ? 0.1310 0.1349 0.1369 0.0033  -0.0028 0.0060  54  ASN   B N   
4566 C  CA  . ASN   B 54  ? 0.1374 0.1438 0.1437 0.0044  -0.0017 -0.0005 54  ASN   B CA  
4567 C  C   . ASN   B 54  ? 0.1339 0.1451 0.1539 0.0009  0.0030  0.0019  54  ASN   B C   
4568 O  O   . ASN   B 54  ? 0.1323 0.1494 0.1729 -0.0035 0.0005  0.0053  54  ASN   B O   
4569 C  CB  . ASN   B 54  ? 0.1442 0.1588 0.1565 0.0067  0.0021  -0.0046 54  ASN   B CB  
4570 C  CG  . ASN   B 54  ? 0.1415 0.1665 0.1573 0.0066  -0.0065 0.0010  54  ASN   B CG  
4571 O  OD1 . ASN   B 54  ? 0.1378 0.1610 0.1652 0.0042  -0.0150 -0.0167 54  ASN   B OD1 
4572 N  ND2 . ASN   B 54  ? 0.1560 0.1877 0.1851 -0.0033 -0.0321 0.0171  54  ASN   B ND2 
4579 N  N   . LYS   B 55  ? 0.1368 0.1538 0.1731 0.0071  0.0031  0.0029  55  LYS   B N   
4580 C  CA  . LYS   B 55  ? 0.1400 0.1652 0.1930 0.0146  0.0001  0.0059  55  LYS   B CA  
4581 C  C   . LYS   B 55  ? 0.1373 0.1632 0.1957 0.0122  0.0045  -0.0034 55  LYS   B C   
4582 O  O   . LYS   B 55  ? 0.1303 0.1741 0.2159 0.0110  0.0087  -0.0008 55  LYS   B O   
4583 C  CB  . LYS   B 55  ? 0.1511 0.1748 0.2399 0.0217  0.0012  0.0148  55  LYS   B CB  
4584 C  CG  . LYS   B 55  ? 0.1883 0.2035 0.3184 0.0288  0.0199  0.0253  55  LYS   B CG  
4585 C  CD  . LYS   B 55  ? 0.2284 0.2278 0.3902 0.0408  0.0333  0.0349  55  LYS   B CD  
4586 C  CE  . LYS   B 55  ? 0.2538 0.2495 0.4606 0.0406  0.0502  0.0339  55  LYS   B CE  
4587 N  NZ  . LYS   B 55  ? 0.2584 0.2629 0.4929 0.0399  0.0406  0.0390  55  LYS   B NZ  
4601 N  N   . ALA   B 56  ? 0.1369 0.1668 0.1707 0.0106  0.0047  -0.0069 56  ALA   B N   
4602 C  CA  . ALA   B 56  ? 0.1508 0.1844 0.1740 0.0056  0.0050  -0.0058 56  ALA   B CA  
4603 C  C   . ALA   B 56  ? 0.1491 0.1782 0.1757 0.0056  0.0122  0.0040  56  ALA   B C   
4604 O  O   . ALA   B 56  ? 0.1615 0.1886 0.1952 0.0074  0.0290  0.0062  56  ALA   B O   
4605 C  CB  . ALA   B 56  ? 0.1620 0.2012 0.1810 -0.0088 0.0004  -0.0016 56  ALA   B CB  
4611 N  N   . THR   B 57  ? 0.1446 0.1665 0.1773 0.0044  0.0151  0.0074  57  THR   B N   
4612 C  CA  . THR   B 57  ? 0.1467 0.1672 0.1777 -0.0006 0.0229  0.0134  57  THR   B CA  
4613 C  C   . THR   B 57  ? 0.1496 0.1756 0.1979 -0.0006 0.0234  0.0037  57  THR   B C   
4614 O  O   . THR   B 57  ? 0.1567 0.1748 0.2072 -0.0137 0.0176  0.0080  57  THR   B O   
4615 C  CB  . THR   B 57  ? 0.1500 0.1542 0.1636 -0.0016 0.0167  0.0127  57  THR   B CB  
4616 O  OG1 . THR   B 57  ? 0.1511 0.1523 0.1723 -0.0031 0.0173  0.0078  57  THR   B OG1 
4617 C  CG2 . THR   B 57  ? 0.1427 0.1571 0.1667 -0.0021 0.0148  0.0099  57  THR   B CG2 
4625 N  N   . ASN   B 58  ? 0.1353 0.1918 0.2249 -0.0095 0.0133  -0.0096 58  ASN   B N   
4626 C  CA  . ASN   B 58  ? 0.1514 0.2327 0.2647 -0.0239 0.0291  -0.0015 58  ASN   B CA  
4627 C  C   . ASN   B 58  ? 0.1384 0.2136 0.2292 -0.0160 0.0019  -0.0047 58  ASN   B C   
4628 O  O   . ASN   B 58  ? 0.1428 0.2224 0.2363 -0.0162 0.0033  -0.0088 58  ASN   B O   
4629 C  CB  . ASN   B 58  ? 0.2398 0.3064 0.3875 -0.0439 0.0511  0.0179  58  ASN   B CB  
4630 C  CG  . ASN   B 58  ? 0.3643 0.3910 0.5286 -0.0493 0.0609  0.0378  58  ASN   B CG  
4631 O  OD1 . ASN   B 58  ? 0.3848 0.3974 0.5755 -0.0530 0.0648  0.0423  58  ASN   B OD1 
4632 N  ND2 . ASN   B 58  ? 0.4341 0.4461 0.5743 -0.0499 0.0665  0.0412  58  ASN   B ND2 
4639 N  N   . ASN   B 59  ? 0.1347 0.1955 0.2024 -0.0107 -0.0044 0.0049  59  ASN   B N   
4640 C  CA  . ASN   B 59  ? 0.1378 0.1962 0.1959 -0.0117 -0.0173 0.0147  59  ASN   B CA  
4641 C  C   . ASN   B 59  ? 0.1339 0.1878 0.1949 -0.0174 -0.0134 0.0064  59  ASN   B C   
4642 O  O   . ASN   B 59  ? 0.1408 0.1933 0.1864 -0.0161 -0.0137 0.0037  59  ASN   B O   
4643 C  CB  . ASN   B 59  ? 0.1461 0.2160 0.2047 -0.0103 -0.0197 0.0127  59  ASN   B CB  
4644 C  CG  . ASN   B 59  ? 0.1617 0.2328 0.2237 -0.0004 -0.0377 0.0096  59  ASN   B CG  
4645 O  OD1 . ASN   B 59  ? 0.1632 0.2406 0.2195 0.0035  -0.0241 0.0231  59  ASN   B OD1 
4646 N  ND2 . ASN   B 59  ? 0.1730 0.2435 0.2285 -0.0056 -0.0376 0.0045  59  ASN   B ND2 
4653 N  N   . ALA   B 60  ? 0.1357 0.1759 0.1924 -0.0121 -0.0046 0.0015  60  ALA   B N   
4654 C  CA  . ALA   B 60  ? 0.1454 0.1635 0.1872 -0.0184 -0.0059 0.0071  60  ALA   B CA  
4655 C  C   . ALA   B 60  ? 0.1463 0.1519 0.1669 -0.0115 -0.0077 0.0094  60  ALA   B C   
4656 O  O   . ALA   B 60  ? 0.1478 0.1564 0.1853 -0.0142 0.0037  -0.0024 60  ALA   B O   
4657 C  CB  . ALA   B 60  ? 0.1596 0.1605 0.2123 -0.0143 0.0051  0.0071  60  ALA   B CB  
4663 N  N   . MET   B 61  ? 0.1388 0.1466 0.1665 -0.0103 -0.0045 0.0099  61  MET   B N   
4664 C  CA  . MET   B 61  ? 0.1293 0.1431 0.1614 -0.0084 -0.0080 0.0082  61  MET   B CA  
4665 C  C   . MET   B 61  ? 0.1373 0.1423 0.1553 -0.0128 -0.0109 0.0063  61  MET   B C   
4666 O  O   . MET   B 61  ? 0.1439 0.1433 0.1558 -0.0025 -0.0057 -0.0071 61  MET   B O   
4667 C  CB  . MET   B 61  ? 0.1265 0.1454 0.1575 0.0007  -0.0018 -0.0034 61  MET   B CB  
4668 C  CG  . MET   B 61  ? 0.1274 0.1449 0.1513 0.0029  -0.0071 0.0038  61  MET   B CG  
4669 S  SD  . MET   B 61  ? 0.1344 0.1432 0.1758 -0.0035 -0.0048 -0.0076 61  MET   B SD  
4670 C  CE  . MET   B 61  ? 0.1445 0.1597 0.1819 0.0021  0.0044  -0.0191 61  MET   B CE  
4680 N  N   . GLN   B 62  ? 0.1388 0.1471 0.1522 -0.0049 -0.0138 0.0074  62  GLN   B N   
4681 C  CA  . GLN   B 62  ? 0.1432 0.1530 0.1567 -0.0010 -0.0177 -0.0010 62  GLN   B CA  
4682 C  C   . GLN   B 62  ? 0.1384 0.1579 0.1607 -0.0038 -0.0245 -0.0071 62  GLN   B C   
4683 O  O   . GLN   B 62  ? 0.1508 0.1575 0.1690 -0.0041 -0.0311 -0.0140 62  GLN   B O   
4684 C  CB  . GLN   B 62  ? 0.1449 0.1597 0.1620 0.0039  -0.0170 0.0061  62  GLN   B CB  
4685 C  CG  . GLN   B 62  ? 0.1466 0.1673 0.1593 0.0023  -0.0265 -0.0002 62  GLN   B CG  
4686 C  CD  . GLN   B 62  ? 0.1484 0.1602 0.1482 0.0040  -0.0279 0.0020  62  GLN   B CD  
4687 O  OE1 . GLN   B 62  ? 0.1498 0.1524 0.1693 0.0007  -0.0290 -0.0065 62  GLN   B OE1 
4688 N  NE2 . GLN   B 62  ? 0.1530 0.1618 0.1613 0.0018  -0.0197 -0.0090 62  GLN   B NE2 
4697 N  N   . VAL   B 63  ? 0.1402 0.1620 0.1817 -0.0089 -0.0258 -0.0050 63  VAL   B N   
4698 C  CA  . VAL   B 63  ? 0.1522 0.1646 0.1955 -0.0144 -0.0314 -0.0014 63  VAL   B CA  
4699 C  C   . VAL   B 63  ? 0.1545 0.1495 0.1716 -0.0170 -0.0337 -0.0139 63  VAL   B C   
4700 O  O   . VAL   B 63  ? 0.1701 0.1495 0.1922 -0.0147 -0.0377 -0.0138 63  VAL   B O   
4701 C  CB  . VAL   B 63  ? 0.1547 0.1798 0.2288 -0.0209 -0.0346 -0.0081 63  VAL   B CB  
4702 C  CG1 . VAL   B 63  ? 0.1645 0.1854 0.2484 -0.0304 -0.0304 -0.0097 63  VAL   B CG1 
4703 C  CG2 . VAL   B 63  ? 0.1526 0.1944 0.2378 -0.0141 -0.0367 -0.0067 63  VAL   B CG2 
4713 N  N   . GLU   B 64  ? 0.1566 0.1439 0.1697 -0.0090 -0.0267 -0.0037 64  GLU   B N   
4714 C  CA  . GLU   B 64  ? 0.1557 0.1381 0.1662 -0.0091 -0.0302 -0.0053 64  GLU   B CA  
4715 C  C   . GLU   B 64  ? 0.1484 0.1337 0.1684 -0.0058 -0.0317 -0.0133 64  GLU   B C   
4716 O  O   . GLU   B 64  ? 0.1633 0.1435 0.1685 -0.0086 -0.0292 -0.0133 64  GLU   B O   
4717 C  CB  . GLU   B 64  ? 0.1547 0.1481 0.1654 -0.0167 -0.0189 -0.0013 64  GLU   B CB  
4718 C  CG  . GLU   B 64  ? 0.1568 0.1538 0.1696 -0.0224 -0.0273 -0.0168 64  GLU   B CG  
4719 C  CD  . GLU   B 64  ? 0.1617 0.1617 0.1719 -0.0256 -0.0278 -0.0103 64  GLU   B CD  
4720 O  OE1 . GLU   B 64  ? 0.1613 0.1758 0.1780 -0.0291 -0.0174 -0.0256 64  GLU   B OE1 
4721 O  OE2 . GLU   B 64  ? 0.1781 0.1700 0.1780 -0.0297 -0.0400 -0.0131 64  GLU   B OE2 
4728 N  N   . SER   B 65  ? 0.1473 0.1321 0.1573 -0.0058 -0.0155 -0.0152 65  SER   B N   
4729 C  CA  . SER   B 65  ? 0.1490 0.1345 0.1601 -0.0015 -0.0186 -0.0150 65  SER   B CA  
4730 C  C   . SER   B 65  ? 0.1543 0.1370 0.1566 -0.0017 -0.0241 -0.0204 65  SER   B C   
4731 O  O   . SER   B 65  ? 0.1602 0.1469 0.1558 -0.0008 -0.0229 -0.0248 65  SER   B O   
4732 C  CB  . SER   B 65  ? 0.1476 0.1409 0.1594 -0.0074 -0.0156 -0.0121 65  SER   B CB  
4733 O  OG  . SER   B 65  ? 0.1475 0.1432 0.1631 -0.0091 -0.0157 -0.0237 65  SER   B OG  
4739 N  N   . ASP   B 66  ? 0.1621 0.1501 0.1556 -0.0040 -0.0251 -0.0183 66  ASP   B N   
4740 C  CA  . ASP   B 66  ? 0.1678 0.1593 0.1489 -0.0003 -0.0285 -0.0100 66  ASP   B CA  
4741 C  C   . ASP   B 66  ? 0.1703 0.1587 0.1503 -0.0035 -0.0256 -0.0118 66  ASP   B C   
4742 O  O   . ASP   B 66  ? 0.1724 0.1588 0.1659 0.0023  -0.0268 -0.0188 66  ASP   B O   
4743 C  CB  . ASP   B 66  ? 0.1810 0.1740 0.1760 0.0083  -0.0404 -0.0145 66  ASP   B CB  
4744 C  CG  . ASP   B 66  ? 0.2040 0.1896 0.2028 0.0122  -0.0599 -0.0015 66  ASP   B CG  
4745 O  OD1 . ASP   B 66  ? 0.2230 0.1820 0.2091 0.0054  -0.0620 0.0025  66  ASP   B OD1 
4746 O  OD2 . ASP   B 66  ? 0.2208 0.2094 0.2628 0.0308  -0.0573 -0.0001 66  ASP   B OD2 
4751 N  N   . ASP   B 67  ? 0.1665 0.1489 0.1455 -0.0082 -0.0284 -0.0161 67  ASP   B N   
4752 C  CA  . ASP   B 67  ? 0.1822 0.1505 0.1605 -0.0098 -0.0302 -0.0135 67  ASP   B CA  
4753 C  C   . ASP   B 67  ? 0.1789 0.1455 0.1796 0.0002  -0.0292 -0.0215 67  ASP   B C   
4754 O  O   . ASP   B 67  ? 0.1805 0.1517 0.1903 -0.0019 -0.0230 -0.0272 67  ASP   B O   
4755 C  CB  . ASP   B 67  ? 0.2080 0.1601 0.1667 -0.0156 -0.0399 -0.0088 67  ASP   B CB  
4756 C  CG  . ASP   B 67  ? 0.2476 0.1675 0.1744 -0.0133 -0.0654 -0.0100 67  ASP   B CG  
4757 O  OD1 . ASP   B 67  ? 0.2682 0.1722 0.1822 -0.0156 -0.0645 -0.0103 67  ASP   B OD1 
4758 O  OD2 . ASP   B 67  ? 0.2630 0.1719 0.2013 -0.0021 -0.0771 -0.0152 67  ASP   B OD2 
4763 N  N   . TYR   B 68  ? 0.1691 0.1463 0.1648 -0.0017 -0.0396 -0.0275 68  TYR   B N   
4764 C  CA  . TYR   B 68  ? 0.1654 0.1629 0.1815 0.0016  -0.0406 -0.0360 68  TYR   B CA  
4765 C  C   . TYR   B 68  ? 0.1578 0.1613 0.1769 0.0039  -0.0361 -0.0447 68  TYR   B C   
4766 O  O   . TYR   B 68  ? 0.1631 0.1704 0.1890 0.0089  -0.0296 -0.0541 68  TYR   B O   
4767 C  CB  . TYR   B 68  ? 0.1696 0.1826 0.1862 0.0073  -0.0411 -0.0465 68  TYR   B CB  
4768 C  CG  . TYR   B 68  ? 0.1815 0.2027 0.1891 0.0103  -0.0367 -0.0633 68  TYR   B CG  
4769 C  CD1 . TYR   B 68  ? 0.1847 0.2031 0.2175 -0.0055 -0.0284 -0.0671 68  TYR   B CD1 
4770 C  CD2 . TYR   B 68  ? 0.1853 0.2247 0.2096 0.0213  -0.0527 -0.0555 68  TYR   B CD2 
4771 C  CE1 . TYR   B 68  ? 0.1901 0.2215 0.2465 -0.0017 -0.0340 -0.0545 68  TYR   B CE1 
4772 C  CE2 . TYR   B 68  ? 0.1910 0.2332 0.2244 0.0226  -0.0434 -0.0628 68  TYR   B CE2 
4773 C  CZ  . TYR   B 68  ? 0.1876 0.2324 0.2465 0.0062  -0.0433 -0.0642 68  TYR   B CZ  
4774 O  OH  . TYR   B 68  ? 0.1834 0.2516 0.2717 0.0054  -0.0331 -0.0589 68  TYR   B OH  
4784 N  N   . ILE   B 69  ? 0.1622 0.1515 0.1776 0.0034  -0.0325 -0.0391 69  ILE   B N   
4785 C  CA  . ILE   B 69  ? 0.1710 0.1608 0.1803 -0.0041 -0.0231 -0.0360 69  ILE   B CA  
4786 C  C   . ILE   B 69  ? 0.1691 0.1612 0.1702 0.0035  -0.0353 -0.0360 69  ILE   B C   
4787 O  O   . ILE   B 69  ? 0.1770 0.1708 0.1659 0.0021  -0.0225 -0.0392 69  ILE   B O   
4788 C  CB  . ILE   B 69  ? 0.1777 0.1657 0.1935 -0.0060 0.0032  -0.0311 69  ILE   B CB  
4789 C  CG1 . ILE   B 69  ? 0.1794 0.1721 0.1983 -0.0086 0.0123  -0.0333 69  ILE   B CG1 
4790 C  CG2 . ILE   B 69  ? 0.1949 0.1706 0.2030 0.0016  0.0058  -0.0198 69  ILE   B CG2 
4791 C  CD1 . ILE   B 69  ? 0.1772 0.1767 0.2220 -0.0197 0.0160  -0.0321 69  ILE   B CD1 
4803 N  N   . ALA   B 70  ? 0.1649 0.1639 0.1773 0.0079  -0.0369 -0.0302 70  ALA   B N   
4804 C  CA  . ALA   B 70  ? 0.1712 0.1667 0.1648 0.0038  -0.0344 -0.0302 70  ALA   B CA  
4805 C  C   . ALA   B 70  ? 0.1810 0.1618 0.1576 0.0013  -0.0418 -0.0420 70  ALA   B C   
4806 O  O   . ALA   B 70  ? 0.1836 0.1658 0.1604 0.0036  -0.0369 -0.0379 70  ALA   B O   
4807 C  CB  . ALA   B 70  ? 0.1736 0.1784 0.1645 -0.0029 -0.0357 -0.0346 70  ALA   B CB  
4813 N  N   . THR   B 71  ? 0.1860 0.1603 0.1767 0.0062  -0.0504 -0.0406 71  THR   B N   
4814 C  CA  . THR   B 71  ? 0.1965 0.1654 0.2022 0.0091  -0.0663 -0.0371 71  THR   B CA  
4815 C  C   . THR   B 71  ? 0.1897 0.1710 0.2216 0.0267  -0.0641 -0.0598 71  THR   B C   
4816 O  O   . THR   B 71  ? 0.1980 0.1784 0.2596 0.0289  -0.0560 -0.0742 71  THR   B O   
4817 C  CB  . THR   B 71  ? 0.2203 0.1879 0.2220 -0.0011 -0.0746 -0.0108 71  THR   B CB  
4818 O  OG1 . THR   B 71  ? 0.2334 0.2127 0.2559 -0.0162 -0.0707 0.0100  71  THR   B OG1 
4819 C  CG2 . THR   B 71  ? 0.2355 0.1839 0.2519 0.0032  -0.0591 0.0046  71  THR   B CG2 
4827 N  N   . ASN   B 72  ? 0.1739 0.1775 0.2210 0.0214  -0.0645 -0.0776 72  ASN   B N   
4828 C  CA  . ASN   B 72  ? 0.1778 0.1924 0.2274 0.0182  -0.0526 -0.0793 72  ASN   B CA  
4829 C  C   . ASN   B 72  ? 0.1808 0.2041 0.2325 0.0086  -0.0258 -0.0831 72  ASN   B C   
4830 O  O   . ASN   B 72  ? 0.1788 0.2180 0.2579 0.0102  -0.0100 -0.0834 72  ASN   B O   
4831 C  CB  . ASN   B 72  ? 0.1856 0.2044 0.2328 0.0119  -0.0597 -0.0679 72  ASN   B CB  
4832 C  CG  . ASN   B 72  ? 0.2027 0.2164 0.2408 0.0269  -0.0666 -0.0423 72  ASN   B CG  
4833 O  OD1 . ASN   B 72  ? 0.2225 0.2322 0.2504 0.0165  -0.0526 -0.0420 72  ASN   B OD1 
4834 N  ND2 . ASN   B 72  ? 0.2133 0.2216 0.2904 0.0390  -0.0542 -0.0108 72  ASN   B ND2 
4841 N  N   . GLY   B 73  ? 0.1840 0.2017 0.2108 0.0060  -0.0272 -0.0747 73  GLY   B N   
4842 C  CA  . GLY   B 73  ? 0.1781 0.2061 0.1928 0.0051  -0.0251 -0.0613 73  GLY   B CA  
4843 C  C   . GLY   B 73  ? 0.1736 0.2041 0.1479 0.0092  -0.0259 -0.0533 73  GLY   B C   
4844 O  O   . GLY   B 73  ? 0.1636 0.1925 0.1599 0.0109  -0.0245 -0.0396 73  GLY   B O   
4848 N  N   . PRO   B 74  ? 0.1751 0.2125 0.1383 0.0056  -0.0268 -0.0410 74  PRO   B N   
4849 C  CA  . PRO   B 74  ? 0.1698 0.2134 0.1299 0.0090  -0.0199 -0.0279 74  PRO   B CA  
4850 C  C   . PRO   B 74  ? 0.1553 0.1938 0.1373 0.0086  -0.0123 -0.0243 74  PRO   B C   
4851 O  O   . PRO   B 74  ? 0.1602 0.1949 0.1719 0.0117  -0.0107 -0.0331 74  PRO   B O   
4852 C  CB  . PRO   B 74  ? 0.1829 0.2322 0.1351 0.0051  -0.0193 -0.0262 74  PRO   B CB  
4853 C  CG  . PRO   B 74  ? 0.1982 0.2402 0.1566 0.0031  -0.0148 -0.0208 74  PRO   B CG  
4854 C  CD  . PRO   B 74  ? 0.1968 0.2318 0.1518 0.0041  -0.0131 -0.0342 74  PRO   B CD  
4862 N  N   . LEU   B 75  ? 0.1504 0.1832 0.1176 0.0112  -0.0142 -0.0191 75  LEU   B N   
4863 C  CA  . LEU   B 75  ? 0.1540 0.1841 0.1212 0.0045  -0.0185 -0.0027 75  LEU   B CA  
4864 C  C   . LEU   B 75  ? 0.1564 0.1916 0.1291 0.0049  -0.0066 -0.0053 75  LEU   B C   
4865 O  O   . LEU   B 75  ? 0.1724 0.2035 0.1372 0.0008  -0.0052 -0.0006 75  LEU   B O   
4866 C  CB  . LEU   B 75  ? 0.1670 0.1851 0.1145 -0.0042 -0.0221 0.0063  75  LEU   B CB  
4867 C  CG  . LEU   B 75  ? 0.2032 0.1981 0.1319 -0.0268 -0.0058 -0.0028 75  LEU   B CG  
4868 C  CD1 . LEU   B 75  ? 0.2323 0.2095 0.1496 -0.0351 0.0102  -0.0074 75  LEU   B CD1 
4869 C  CD2 . LEU   B 75  ? 0.2376 0.2169 0.2024 -0.0220 0.0134  0.0080  75  LEU   B CD2 
4881 N  N   . LYS   B 76  ? 0.1576 0.2084 0.1504 0.0034  -0.0026 -0.0023 76  LYS   B N   
4882 C  CA  . LYS   B 76  ? 0.1693 0.2167 0.1831 -0.0006 0.0254  -0.0050 76  LYS   B CA  
4883 C  C   . LYS   B 76  ? 0.1605 0.2012 0.1531 0.0085  0.0121  0.0139  76  LYS   B C   
4884 O  O   . LYS   B 76  ? 0.1590 0.1846 0.1553 0.0062  0.0041  0.0152  76  LYS   B O   
4885 C  CB  . LYS   B 76  ? 0.1891 0.2272 0.2534 -0.0060 0.0433  -0.0373 76  LYS   B CB  
4886 C  CG  . LYS   B 76  ? 0.1995 0.2485 0.3070 0.0035  0.0328  -0.0454 76  LYS   B CG  
4887 C  CD  . LYS   B 76  ? 0.1967 0.2591 0.3438 0.0094  0.0125  -0.0618 76  LYS   B CD  
4888 C  CE  . LYS   B 76  ? 0.2035 0.2767 0.4095 0.0087  -0.0060 -0.0698 76  LYS   B CE  
4889 N  NZ  . LYS   B 76  ? 0.2036 0.2854 0.4211 0.0083  -0.0264 -0.0881 76  LYS   B NZ  
4903 N  N   . VAL   B 77  ? 0.1698 0.2124 0.1460 0.0165  0.0133  0.0187  77  VAL   B N   
4904 C  CA  . VAL   B 77  ? 0.1662 0.1982 0.1612 0.0243  0.0194  0.0379  77  VAL   B CA  
4905 C  C   . VAL   B 77  ? 0.1558 0.1742 0.1620 0.0199  0.0195  0.0282  77  VAL   B C   
4906 O  O   . VAL   B 77  ? 0.1559 0.1707 0.1705 0.0239  0.0252  0.0244  77  VAL   B O   
4907 C  CB  . VAL   B 77  ? 0.1764 0.2071 0.1869 0.0223  0.0275  0.0581  77  VAL   B CB  
4908 C  CG1 . VAL   B 77  ? 0.1865 0.2007 0.2192 0.0184  0.0319  0.0725  77  VAL   B CG1 
4909 C  CG2 . VAL   B 77  ? 0.1883 0.2277 0.2163 0.0162  0.0100  0.0559  77  VAL   B CG2 
4919 N  N   . GLY   B 78  ? 0.1541 0.1646 0.1515 0.0139  0.0134  0.0222  78  GLY   B N   
4920 C  CA  . GLY   B 78  ? 0.1513 0.1612 0.1435 0.0153  0.0180  0.0138  78  GLY   B CA  
4921 C  C   . GLY   B 78  ? 0.1417 0.1541 0.1396 0.0126  0.0161  0.0214  78  GLY   B C   
4922 O  O   . GLY   B 78  ? 0.1509 0.1479 0.1538 0.0202  0.0142  0.0227  78  GLY   B O   
4926 N  N   . GLY   B 79  ? 0.1339 0.1576 0.1405 0.0121  0.0151  0.0139  79  GLY   B N   
4927 C  CA  . GLY   B 79  ? 0.1393 0.1479 0.1364 0.0135  0.0088  0.0089  79  GLY   B CA  
4928 C  C   . GLY   B 79  ? 0.1362 0.1389 0.1364 0.0116  0.0094  0.0028  79  GLY   B C   
4929 O  O   . GLY   B 79  ? 0.1439 0.1387 0.1472 0.0129  0.0164  0.0122  79  GLY   B O   
4933 N  N   . SER   B 80  ? 0.1333 0.1310 0.1506 0.0066  0.0177  0.0035  80  SER   B N   
4934 C  CA  . SER   B 80  ? 0.1313 0.1317 0.1474 0.0045  0.0030  0.0065  80  SER   B CA  
4935 C  C   . SER   B 80  ? 0.1337 0.1280 0.1430 0.0058  -0.0088 -0.0020 80  SER   B C   
4936 O  O   . SER   B 80  ? 0.1467 0.1271 0.1717 0.0094  -0.0004 -0.0070 80  SER   B O   
4937 C  CB  . SER   B 80  ? 0.1354 0.1332 0.1499 -0.0044 0.0051  0.0075  80  SER   B CB  
4938 O  OG  . SER   B 80  ? 0.1449 0.1506 0.1662 -0.0014 -0.0102 0.0117  80  SER   B OG  
4944 N  N   . CYS   B 81  ? 0.1308 0.1175 0.1474 0.0022  -0.0103 -0.0038 81  CYS   B N   
4945 C  CA  . CYS   B 81  ? 0.1379 0.1196 0.1484 0.0093  -0.0114 -0.0040 81  CYS   B CA  
4946 C  C   . CYS   B 81  ? 0.1345 0.1144 0.1328 0.0020  -0.0179 -0.0022 81  CYS   B C   
4947 O  O   . CYS   B 81  ? 0.1583 0.1182 0.1413 0.0068  -0.0019 -0.0044 81  CYS   B O   
4948 C  CB  . CYS   B 81  ? 0.1525 0.1326 0.1498 0.0012  -0.0080 -0.0019 81  CYS   B CB  
4949 S  SG  . CYS   B 81  ? 0.1510 0.1495 0.1522 -0.0029 -0.0267 -0.0132 81  CYS   B SG  
4955 N  N   . VAL   B 82  ? 0.1376 0.1128 0.1497 0.0005  -0.0113 -0.0012 82  VAL   B N   
4956 C  CA  . VAL   B 82  ? 0.1449 0.1177 0.1416 -0.0030 -0.0127 0.0016  82  VAL   B CA  
4957 C  C   . VAL   B 82  ? 0.1532 0.1105 0.1486 0.0003  -0.0052 -0.0012 82  VAL   B C   
4958 O  O   . VAL   B 82  ? 0.1610 0.1156 0.1737 -0.0014 -0.0070 -0.0126 82  VAL   B O   
4959 C  CB  . VAL   B 82  ? 0.1560 0.1397 0.1535 -0.0031 -0.0129 0.0087  82  VAL   B CB  
4960 C  CG1 . VAL   B 82  ? 0.1694 0.1651 0.1609 -0.0005 -0.0203 0.0196  82  VAL   B CG1 
4961 C  CG2 . VAL   B 82  ? 0.1636 0.1584 0.1644 -0.0055 -0.0298 0.0067  82  VAL   B CG2 
4971 N  N   . LEU   B 83  ? 0.1400 0.1142 0.1462 -0.0118 -0.0194 -0.0071 83  LEU   B N   
4972 C  CA  . LEU   B 83  ? 0.1448 0.1214 0.1376 -0.0140 -0.0198 -0.0005 83  LEU   B CA  
4973 C  C   . LEU   B 83  ? 0.1422 0.1197 0.1390 -0.0173 -0.0217 -0.0005 83  LEU   B C   
4974 O  O   . LEU   B 83  ? 0.1435 0.1263 0.1295 -0.0171 -0.0184 0.0067  83  LEU   B O   
4975 C  CB  . LEU   B 83  ? 0.1494 0.1340 0.1399 -0.0141 -0.0204 -0.0118 83  LEU   B CB  
4976 C  CG  . LEU   B 83  ? 0.1658 0.1540 0.1515 -0.0101 -0.0206 -0.0153 83  LEU   B CG  
4977 C  CD1 . LEU   B 83  ? 0.1730 0.1633 0.1560 -0.0066 -0.0250 -0.0057 83  LEU   B CD1 
4978 C  CD2 . LEU   B 83  ? 0.1836 0.1556 0.1670 -0.0011 -0.0170 -0.0314 83  LEU   B CD2 
4990 N  N   . SER   B 84  ? 0.1464 0.1330 0.1556 -0.0251 -0.0180 0.0016  84  SER   B N   
4991 C  CA  . SER   B 84  ? 0.1461 0.1477 0.1444 -0.0257 -0.0158 0.0154  84  SER   B CA  
4992 C  C   . SER   B 84  ? 0.1393 0.1673 0.1112 -0.0201 -0.0178 0.0223  84  SER   B C   
4993 O  O   . SER   B 84  ? 0.1435 0.1508 0.1165 -0.0171 -0.0160 0.0070  84  SER   B O   
4994 C  CB  . SER   B 84  ? 0.1650 0.1546 0.1846 -0.0303 0.0077  0.0114  84  SER   B CB  
4995 O  OG  . SER   B 84  ? 0.1663 0.1713 0.2275 -0.0381 0.0074  0.0240  84  SER   B OG  
5001 N  N   . GLY   B 85  ? 0.1414 0.1873 0.1316 -0.0301 -0.0121 0.0252  85  GLY   B N   
5002 C  CA  . GLY   B 85  ? 0.1408 0.1921 0.1476 -0.0368 -0.0018 -0.0009 85  GLY   B CA  
5003 C  C   . GLY   B 85  ? 0.1403 0.1737 0.1387 -0.0399 -0.0046 0.0080  85  GLY   B C   
5004 O  O   . GLY   B 85  ? 0.1472 0.1767 0.1387 -0.0474 0.0117  -0.0064 85  GLY   B O   
5008 N  N   . HIS   B 86  ? 0.1437 0.1612 0.1471 -0.0327 -0.0168 0.0242  86  HIS   B N   
5009 C  CA  . HIS   B 86  ? 0.1424 0.1565 0.1532 -0.0304 -0.0175 0.0227  86  HIS   B CA  
5010 C  C   . HIS   B 86  ? 0.1429 0.1702 0.1475 -0.0382 -0.0111 0.0321  86  HIS   B C   
5011 O  O   . HIS   B 86  ? 0.1525 0.1829 0.1519 -0.0332 0.0031  0.0320  86  HIS   B O   
5012 C  CB  . HIS   B 86  ? 0.1509 0.1570 0.1623 -0.0194 -0.0197 0.0118  86  HIS   B CB  
5013 C  CG  . HIS   B 86  ? 0.1547 0.1665 0.1528 -0.0128 -0.0206 0.0093  86  HIS   B CG  
5014 N  ND1 . HIS   B 86  ? 0.1675 0.1887 0.1706 -0.0229 -0.0261 -0.0096 86  HIS   B ND1 
5015 C  CD2 . HIS   B 86  ? 0.1535 0.1698 0.1608 -0.0116 -0.0179 0.0087  86  HIS   B CD2 
5016 C  CE1 . HIS   B 86  ? 0.1691 0.1854 0.1674 -0.0197 -0.0111 -0.0254 86  HIS   B CE1 
5017 N  NE2 . HIS   B 86  ? 0.1624 0.1787 0.1540 -0.0056 -0.0148 -0.0011 86  HIS   B NE2 
5025 N  N   . ASN   B 87  ? 0.1415 0.1714 0.1595 -0.0335 -0.0012 0.0306  87  ASN   B N   
5026 C  CA  . ASN   B 87  ? 0.1478 0.1894 0.1549 -0.0326 0.0208  0.0213  87  ASN   B CA  
5027 C  C   . ASN   B 87  ? 0.1653 0.1758 0.1479 -0.0293 0.0276  0.0184  87  ASN   B C   
5028 O  O   . ASN   B 87  ? 0.1904 0.1831 0.1813 -0.0227 0.0466  0.0140  87  ASN   B O   
5029 C  CB  . ASN   B 87  ? 0.1510 0.2233 0.1822 -0.0255 0.0220  0.0173  87  ASN   B CB  
5030 C  CG  . ASN   B 87  ? 0.1606 0.2421 0.1934 0.0040  0.0284  0.0401  87  ASN   B CG  
5031 O  OD1 . ASN   B 87  ? 0.1554 0.2287 0.1840 0.0084  0.0447  0.0592  87  ASN   B OD1 
5032 N  ND2 . ASN   B 87  ? 0.1965 0.2563 0.2371 0.0098  0.0362  0.0351  87  ASN   B ND2 
5039 N  N   . LEU   B 88  ? 0.1559 0.1640 0.1306 -0.0342 0.0153  0.0142  88  LEU   B N   
5040 C  CA  . LEU   B 88  ? 0.1649 0.1589 0.1366 -0.0348 0.0076  -0.0004 88  LEU   B CA  
5041 C  C   . LEU   B 88  ? 0.1632 0.1477 0.1333 -0.0356 0.0028  0.0052  88  LEU   B C   
5042 O  O   . LEU   B 88  ? 0.1893 0.1548 0.1655 -0.0223 -0.0215 -0.0060 88  LEU   B O   
5043 C  CB  . LEU   B 88  ? 0.1769 0.1648 0.1565 -0.0411 -0.0065 0.0112  88  LEU   B CB  
5044 C  CG  . LEU   B 88  ? 0.2127 0.1975 0.1732 -0.0315 -0.0214 0.0340  88  LEU   B CG  
5045 C  CD1 . LEU   B 88  ? 0.2235 0.2224 0.1972 -0.0429 -0.0207 0.0453  88  LEU   B CD1 
5046 C  CD2 . LEU   B 88  ? 0.2483 0.2219 0.2336 0.0055  -0.0448 0.0144  88  LEU   B CD2 
5058 N  N   . ALA   B 89  ? 0.1500 0.1448 0.1269 -0.0357 0.0122  0.0094  89  ALA   B N   
5059 C  CA  . ALA   B 89  ? 0.1486 0.1407 0.1178 -0.0306 0.0002  0.0098  89  ALA   B CA  
5060 C  C   . ALA   B 89  ? 0.1561 0.1425 0.1251 -0.0343 0.0197  0.0003  89  ALA   B C   
5061 O  O   . ALA   B 89  ? 0.1452 0.1498 0.1615 -0.0351 0.0152  -0.0217 89  ALA   B O   
5062 C  CB  . ALA   B 89  ? 0.1413 0.1446 0.1487 -0.0378 -0.0002 0.0186  89  ALA   B CB  
5068 N  N   . LYS   B 90  ? 0.1862 0.1338 0.1338 -0.0409 -0.0008 0.0111  90  LYS   B N   
5069 C  CA  . LYS   B 90  ? 0.2055 0.1300 0.1261 -0.0370 -0.0027 0.0143  90  LYS   B CA  
5070 C  C   . LYS   B 90  ? 0.1920 0.1251 0.1427 -0.0388 -0.0051 0.0018  90  LYS   B C   
5071 O  O   . LYS   B 90  ? 0.1982 0.1451 0.1577 -0.0544 -0.0018 -0.0009 90  LYS   B O   
5072 C  CB  . LYS   B 90  ? 0.2256 0.1403 0.1633 -0.0288 0.0044  0.0162  90  LYS   B CB  
5073 C  CG  . LYS   B 90  ? 0.2285 0.1545 0.1647 -0.0163 0.0271  0.0121  90  LYS   B CG  
5074 C  CD  . LYS   B 90  ? 0.2568 0.1792 0.2240 -0.0122 0.0472  -0.0058 90  LYS   B CD  
5075 C  CE  . LYS   B 90  ? 0.2659 0.1951 0.2802 -0.0186 0.0638  -0.0095 90  LYS   B CE  
5076 N  NZ  . LYS   B 90  ? 0.2811 0.1906 0.2830 -0.0307 0.0782  0.0016  90  LYS   B NZ  
5090 N  N   . HIS   B 91  ? 0.1649 0.1180 0.1197 -0.0295 -0.0119 0.0093  91  HIS   B N   
5091 C  CA  . HIS   B 91  ? 0.1539 0.1207 0.1319 -0.0245 -0.0164 -0.0003 91  HIS   B CA  
5092 C  C   . HIS   B 91  ? 0.1438 0.1222 0.1141 -0.0251 -0.0044 0.0005  91  HIS   B C   
5093 O  O   . HIS   B 91  ? 0.1566 0.1241 0.1200 -0.0255 -0.0154 0.0001  91  HIS   B O   
5094 C  CB  . HIS   B 91  ? 0.1712 0.1268 0.1583 -0.0058 -0.0103 0.0112  91  HIS   B CB  
5095 C  CG  . HIS   B 91  ? 0.2128 0.1404 0.2407 0.0034  0.0208  0.0247  91  HIS   B CG  
5096 N  ND1 . HIS   B 91  ? 0.2438 0.1477 0.3101 0.0033  0.0277  0.0114  91  HIS   B ND1 
5097 C  CD2 . HIS   B 91  ? 0.2244 0.1703 0.2917 0.0173  0.0151  0.0558  91  HIS   B CD2 
5098 C  CE1 . HIS   B 91  ? 0.2477 0.1643 0.3226 0.0184  0.0245  0.0224  91  HIS   B CE1 
5099 N  NE2 . HIS   B 91  ? 0.2367 0.1768 0.3259 0.0281  0.0242  0.0597  91  HIS   B NE2 
5107 N  N   . CYS   B 92  ? 0.1343 0.1203 0.1146 -0.0230 -0.0088 -0.0068 92  CYS   B N   
5108 C  CA  . CYS   B 92  ? 0.1311 0.1179 0.1204 -0.0190 -0.0054 -0.0011 92  CYS   B CA  
5109 C  C   . CYS   B 92  ? 0.1263 0.1127 0.1093 -0.0139 -0.0104 0.0004  92  CYS   B C   
5110 O  O   . CYS   B 92  ? 0.1363 0.1207 0.1336 -0.0121 0.0004  -0.0022 92  CYS   B O   
5111 C  CB  . CYS   B 92  ? 0.1300 0.1277 0.1270 -0.0113 -0.0046 0.0023  92  CYS   B CB  
5112 S  SG  . CYS   B 92  ? 0.1335 0.1288 0.1325 -0.0108 -0.0122 0.0060  92  CYS   B SG  
5118 N  N   . LEU   B 93  ? 0.1257 0.1157 0.1148 -0.0101 -0.0052 -0.0038 93  LEU   B N   
5119 C  CA  . LEU   B 93  ? 0.1268 0.1189 0.1161 -0.0007 -0.0040 0.0023  93  LEU   B CA  
5120 C  C   . LEU   B 93  ? 0.1208 0.1127 0.1081 -0.0017 -0.0035 0.0076  93  LEU   B C   
5121 O  O   . LEU   B 93  ? 0.1287 0.1096 0.1282 -0.0063 -0.0045 0.0013  93  LEU   B O   
5122 C  CB  . LEU   B 93  ? 0.1249 0.1169 0.1241 0.0010  -0.0035 0.0041  93  LEU   B CB  
5123 C  CG  . LEU   B 93  ? 0.1235 0.1284 0.1395 -0.0001 -0.0055 0.0087  93  LEU   B CG  
5124 C  CD1 . LEU   B 93  ? 0.1289 0.1377 0.1458 0.0060  0.0012  -0.0025 93  LEU   B CD1 
5125 C  CD2 . LEU   B 93  ? 0.1242 0.1312 0.1564 -0.0048 -0.0063 0.0057  93  LEU   B CD2 
5137 N  N   . HIS   B 94  ? 0.1248 0.1117 0.1099 -0.0074 -0.0069 0.0063  94  HIS   B N   
5138 C  CA  . HIS   B 94  ? 0.1217 0.1117 0.1136 0.0004  -0.0034 0.0063  94  HIS   B CA  
5139 C  C   . HIS   B 94  ? 0.1229 0.1160 0.1249 -0.0013 -0.0027 0.0103  94  HIS   B C   
5140 O  O   . HIS   B 94  ? 0.1275 0.1240 0.1668 -0.0026 0.0125  -0.0065 94  HIS   B O   
5141 C  CB  . HIS   B 94  ? 0.1235 0.1199 0.1283 0.0005  -0.0074 0.0058  94  HIS   B CB  
5142 C  CG  . HIS   B 94  ? 0.1299 0.1157 0.1293 -0.0027 -0.0213 -0.0001 94  HIS   B CG  
5143 N  ND1 . HIS   B 94  ? 0.1342 0.1229 0.1289 -0.0043 -0.0218 0.0042  94  HIS   B ND1 
5144 C  CD2 . HIS   B 94  ? 0.1342 0.1176 0.1372 -0.0008 -0.0186 0.0058  94  HIS   B CD2 
5145 C  CE1 . HIS   B 94  ? 0.1310 0.1224 0.1227 -0.0140 -0.0265 0.0028  94  HIS   B CE1 
5146 N  NE2 . HIS   B 94  ? 0.1277 0.1257 0.1323 -0.0145 -0.0179 0.0058  94  HIS   B NE2 
5154 N  N   . VAL   B 95  ? 0.1204 0.1119 0.1286 -0.0011 0.0041  0.0027  95  VAL   B N   
5155 C  CA  . VAL   B 95  ? 0.1208 0.1184 0.1231 0.0014  0.0016  0.0057  95  VAL   B CA  
5156 C  C   . VAL   B 95  ? 0.1282 0.1189 0.1186 -0.0006 0.0085  0.0055  95  VAL   B C   
5157 O  O   . VAL   B 95  ? 0.1335 0.1198 0.1449 0.0048  0.0054  0.0094  95  VAL   B O   
5158 C  CB  . VAL   B 95  ? 0.1271 0.1188 0.1366 -0.0020 -0.0059 0.0041  95  VAL   B CB  
5159 C  CG1 . VAL   B 95  ? 0.1325 0.1371 0.1529 -0.0065 -0.0024 0.0172  95  VAL   B CG1 
5160 C  CG2 . VAL   B 95  ? 0.1361 0.1145 0.1385 0.0009  -0.0143 0.0060  95  VAL   B CG2 
5170 N  N   . VAL   B 96  ? 0.1362 0.1287 0.1217 0.0078  0.0046  0.0125  96  VAL   B N   
5171 C  CA  . VAL   B 96  ? 0.1400 0.1458 0.1236 0.0088  0.0077  0.0124  96  VAL   B CA  
5172 C  C   . VAL   B 96  ? 0.1404 0.1427 0.1291 0.0083  0.0106  0.0171  96  VAL   B C   
5173 O  O   . VAL   B 96  ? 0.1427 0.1481 0.1526 0.0030  0.0210  0.0050  96  VAL   B O   
5174 C  CB  . VAL   B 96  ? 0.1447 0.1596 0.1226 0.0108  0.0088  0.0034  96  VAL   B CB  
5175 C  CG1 . VAL   B 96  ? 0.1433 0.1729 0.1458 0.0173  0.0099  0.0056  96  VAL   B CG1 
5176 C  CG2 . VAL   B 96  ? 0.1568 0.1628 0.1415 0.0099  0.0106  -0.0016 96  VAL   B CG2 
5186 N  N   . GLY   B 97  ? 0.1468 0.1406 0.1368 0.0066  0.0114  0.0203  97  GLY   B N   
5187 C  CA  . GLY   B 97  ? 0.1610 0.1405 0.1431 0.0049  0.0139  0.0198  97  GLY   B CA  
5188 C  C   . GLY   B 97  ? 0.1740 0.1493 0.1513 0.0123  0.0112  0.0198  97  GLY   B C   
5189 O  O   . GLY   B 97  ? 0.1870 0.1586 0.1450 0.0075  0.0068  0.0183  97  GLY   B O   
5193 N  N   . PRO   B 98  ? 0.1845 0.1604 0.1619 0.0134  0.0295  0.0331  98  PRO   B N   
5194 C  CA  . PRO   B 98  ? 0.1960 0.1735 0.1697 0.0208  0.0415  0.0289  98  PRO   B CA  
5195 C  C   . PRO   B 98  ? 0.2069 0.1769 0.1370 0.0318  0.0376  0.0381  98  PRO   B C   
5196 O  O   . PRO   B 98  ? 0.1972 0.1741 0.1570 0.0332  0.0395  0.0376  98  PRO   B O   
5197 C  CB  . PRO   B 98  ? 0.1850 0.1764 0.1829 0.0139  0.0498  0.0349  98  PRO   B CB  
5198 C  CG  . PRO   B 98  ? 0.1767 0.1713 0.1773 0.0134  0.0337  0.0438  98  PRO   B CG  
5199 C  CD  . PRO   B 98  ? 0.1701 0.1647 0.1701 0.0134  0.0315  0.0423  98  PRO   B CD  
5207 N  N   . ASN   B 99  ? 0.2187 0.1866 0.1518 0.0418  0.0378  0.0267  99  ASN   B N   
5208 C  CA  . ASN   B 99  ? 0.2386 0.1958 0.1573 0.0507  0.0327  0.0428  99  ASN   B CA  
5209 C  C   . ASN   B 99  ? 0.2683 0.2276 0.1786 0.0469  0.0551  0.0741  99  ASN   B C   
5210 O  O   . ASN   B 99  ? 0.2820 0.2388 0.1858 0.0467  0.0510  0.0702  99  ASN   B O   
5211 C  CB  . ASN   B 99  ? 0.2460 0.1915 0.1625 0.0510  0.0180  0.0349  99  ASN   B CB  
5212 C  CG  . ASN   B 99  ? 0.2503 0.1979 0.1830 0.0479  0.0052  0.0333  99  ASN   B CG  
5213 O  OD1 . ASN   B 99  ? 0.2542 0.1999 0.2148 0.0505  0.0086  0.0415  99  ASN   B OD1 
5214 N  ND2 . ASN   B 99  ? 0.2521 0.1974 0.1975 0.0466  -0.0170 0.0258  99  ASN   B ND2 
5221 N  N   A VAL   B 100 ? 0.2861 0.2410 0.2261 0.0364  0.0591  0.0899  100 VAL   B N   
5222 N  N   B VAL   B 100 ? 0.2881 0.2416 0.2252 0.0377  0.0549  0.0864  100 VAL   B N   
5223 C  CA  A VAL   B 100 ? 0.3141 0.2577 0.2763 0.0273  0.0608  0.1015  100 VAL   B CA  
5224 C  CA  B VAL   B 100 ? 0.3148 0.2564 0.2691 0.0295  0.0525  0.0977  100 VAL   B CA  
5225 C  C   A VAL   B 100 ? 0.3350 0.2604 0.2646 0.0328  0.0623  0.1201  100 VAL   B C   
5226 C  C   B VAL   B 100 ? 0.3348 0.2602 0.2648 0.0345  0.0531  0.1160  100 VAL   B C   
5227 O  O   A VAL   B 100 ? 0.3420 0.2693 0.2705 0.0306  0.0766  0.1183  100 VAL   B O   
5228 O  O   B VAL   B 100 ? 0.3398 0.2662 0.2665 0.0327  0.0613  0.1146  100 VAL   B O   
5229 C  CB  A VAL   B 100 ? 0.3250 0.2745 0.3394 0.0102  0.0590  0.1021  100 VAL   B CB  
5230 C  CB  B VAL   B 100 ? 0.3238 0.2687 0.3181 0.0152  0.0492  0.0965  100 VAL   B CB  
5231 C  CG1 A VAL   B 100 ? 0.3324 0.2821 0.3695 0.0103  0.0565  0.0963  100 VAL   B CG1 
5232 C  CG1 B VAL   B 100 ? 0.3293 0.2736 0.3412 0.0148  0.0465  0.0926  100 VAL   B CG1 
5233 C  CG2 A VAL   B 100 ? 0.3255 0.2784 0.3534 0.0011  0.0639  0.1129  100 VAL   B CG2 
5234 C  CG2 B VAL   B 100 ? 0.3247 0.2718 0.3306 0.0079  0.0515  0.1026  100 VAL   B CG2 
5253 N  N   . ASN   B 101 ? 0.3509 0.2638 0.2712 0.0423  0.0435  0.1258  101 ASN   B N   
5254 C  CA  . ASN   B 101 ? 0.3916 0.2829 0.2878 0.0525  0.0147  0.1307  101 ASN   B CA  
5255 C  C   . ASN   B 101 ? 0.4364 0.3185 0.2862 0.0569  -0.0012 0.1521  101 ASN   B C   
5256 O  O   . ASN   B 101 ? 0.4447 0.3345 0.3203 0.0615  -0.0001 0.1256  101 ASN   B O   
5257 C  CB  . ASN   B 101 ? 0.3889 0.2696 0.3082 0.0493  0.0166  0.1144  101 ASN   B CB  
5258 C  CG  . ASN   B 101 ? 0.3875 0.2567 0.3104 0.0459  0.0250  0.1165  101 ASN   B CG  
5259 O  OD1 . ASN   B 101 ? 0.3904 0.2560 0.3318 0.0340  0.0461  0.1152  101 ASN   B OD1 
5260 N  ND2 . ASN   B 101 ? 0.3862 0.2566 0.2939 0.0483  0.0197  0.1035  101 ASN   B ND2 
5268 N  N   . LYS   B 102 ? 0.4684 0.3465 0.3027 0.0477  -0.0003 0.1571  102 LYS   B N   
5269 C  CA  . LYS   B 102 ? 0.4981 0.3870 0.3253 0.0310  0.0104  0.1246  102 LYS   B CA  
5270 C  C   . LYS   B 102 ? 0.4930 0.3879 0.3014 0.0301  0.0241  0.1263  102 LYS   B C   
5271 O  O   . LYS   B 102 ? 0.5030 0.3950 0.3301 0.0345  0.0071  0.1118  102 LYS   B O   
5272 C  CB  . LYS   B 102 ? 0.5291 0.4250 0.3927 0.0156  0.0171  0.0780  102 LYS   B CB  
5273 C  CG  . LYS   B 102 ? 0.5565 0.4587 0.4507 0.0036  0.0289  0.0384  102 LYS   B CG  
5274 C  CD  . LYS   B 102 ? 0.5787 0.4858 0.5185 -0.0042 0.0422  0.0085  102 LYS   B CD  
5275 C  CE  . LYS   B 102 ? 0.5954 0.5038 0.5714 -0.0088 0.0459  -0.0166 102 LYS   B CE  
5276 N  NZ  . LYS   B 102 ? 0.6026 0.5136 0.5982 -0.0099 0.0422  -0.0320 102 LYS   B NZ  
5290 N  N   . GLY   B 103 ? 0.4727 0.3776 0.2877 0.0223  0.0562  0.1318  103 GLY   B N   
5291 C  CA  . GLY   B 103 ? 0.4510 0.3684 0.3006 0.0200  0.0787  0.1060  103 GLY   B CA  
5292 C  C   . GLY   B 103 ? 0.4245 0.3533 0.2883 0.0182  0.0975  0.0822  103 GLY   B C   
5293 O  O   . GLY   B 103 ? 0.4325 0.3630 0.2994 0.0196  0.1010  0.0829  103 GLY   B O   
5297 N  N   A GLU   B 104 ? 0.4039 0.3385 0.2734 0.0196  0.1139  0.0652  104 GLU   B N   
5298 N  N   B GLU   B 104 ? 0.4066 0.3409 0.2877 0.0143  0.0917  0.0627  104 GLU   B N   
5299 C  CA  A GLU   B 104 ? 0.3832 0.3257 0.2561 0.0250  0.1202  0.0468  104 GLU   B CA  
5300 C  CA  B GLU   B 104 ? 0.3879 0.3290 0.2806 0.0120  0.0819  0.0427  104 GLU   B CA  
5301 C  C   A GLU   B 104 ? 0.3855 0.3323 0.2756 0.0104  0.1497  0.0449  104 GLU   B C   
5302 C  C   B GLU   B 104 ? 0.3838 0.3293 0.2950 0.0038  0.0975  0.0372  104 GLU   B C   
5303 O  O   A GLU   B 104 ? 0.3899 0.3394 0.2996 0.0041  0.1424  0.0387  104 GLU   B O   
5304 O  O   B GLU   B 104 ? 0.3864 0.3325 0.3079 0.0005  0.0938  0.0305  104 GLU   B O   
5305 C  CB  A GLU   B 104 ? 0.3653 0.3058 0.2452 0.0448  0.0833  0.0223  104 GLU   B CB  
5306 C  CB  B GLU   B 104 ? 0.3758 0.3164 0.2698 0.0169  0.0528  0.0237  104 GLU   B CB  
5307 C  CG  A GLU   B 104 ? 0.3501 0.2913 0.2292 0.0630  0.0441  -0.0053 104 GLU   B CG  
5308 C  CG  B GLU   B 104 ? 0.3666 0.3074 0.2584 0.0207  0.0236  0.0029  104 GLU   B CG  
5309 C  CD  A GLU   B 104 ? 0.3370 0.2777 0.2069 0.0788  0.0070  -0.0164 104 GLU   B CD  
5310 C  CD  B GLU   B 104 ? 0.3604 0.2999 0.2458 0.0223  -0.0016 -0.0078 104 GLU   B CD  
5311 O  OE1 A GLU   B 104 ? 0.3192 0.2602 0.1570 0.0954  0.0152  -0.0161 104 GLU   B OE1 
5312 O  OE1 B GLU   B 104 ? 0.3545 0.2935 0.2263 0.0231  0.0003  -0.0070 104 GLU   B OE1 
5313 O  OE2 A GLU   B 104 ? 0.3429 0.2864 0.2194 0.0736  -0.0275 -0.0228 104 GLU   B OE2 
5314 O  OE2 B GLU   B 104 ? 0.3619 0.3019 0.2498 0.0211  -0.0226 -0.0146 104 GLU   B OE2 
5327 N  N   A ASP   B 105 ? 0.3811 0.3324 0.2759 0.0021  0.1745  0.0497  105 ASP   B N   
5328 N  N   B ASP   B 105 ? 0.3762 0.3268 0.2919 -0.0016 0.1114  0.0385  105 ASP   B N   
5329 C  CA  A ASP   B 105 ? 0.3804 0.3335 0.2979 -0.0057 0.1885  0.0404  105 ASP   B CA  
5330 C  CA  B ASP   B 105 ? 0.3715 0.3243 0.3040 -0.0072 0.1193  0.0323  105 ASP   B CA  
5331 C  C   A ASP   B 105 ? 0.3670 0.3080 0.2776 -0.0154 0.1796  0.0392  105 ASP   B C   
5332 C  C   B ASP   B 105 ? 0.3633 0.3110 0.2893 -0.0117 0.1178  0.0257  105 ASP   B C   
5333 O  O   A ASP   B 105 ? 0.3509 0.3033 0.2687 -0.0153 0.1723  0.0407  105 ASP   B O   
5334 O  O   B ASP   B 105 ? 0.3587 0.3076 0.2747 -0.0130 0.1217  0.0285  105 ASP   B O   
5335 C  CB  A ASP   B 105 ? 0.3963 0.3573 0.3687 -0.0013 0.1923  0.0230  105 ASP   B CB  
5336 C  CB  B ASP   B 105 ? 0.3745 0.3338 0.3384 -0.0064 0.1242  0.0295  105 ASP   B CB  
5337 C  CG  A ASP   B 105 ? 0.4098 0.3775 0.4368 -0.0013 0.2011  0.0125  105 ASP   B CG  
5338 C  CG  B ASP   B 105 ? 0.3772 0.3406 0.3732 -0.0096 0.1344  0.0320  105 ASP   B CG  
5339 O  OD1 A ASP   B 105 ? 0.4103 0.3815 0.4440 -0.0070 0.2142  0.0164  105 ASP   B OD1 
5340 O  OD1 B ASP   B 105 ? 0.3773 0.3448 0.3783 -0.0150 0.1378  0.0339  105 ASP   B OD1 
5341 O  OD2 A ASP   B 105 ? 0.4181 0.3885 0.4718 0.0042  0.1928  0.0007  105 ASP   B OD2 
5342 O  OD2 B ASP   B 105 ? 0.3761 0.3412 0.3782 -0.0101 0.1440  0.0370  105 ASP   B OD2 
5351 N  N   A ILE   B 106 ? 0.3593 0.2853 0.2928 -0.0236 0.1689  0.0424  106 ILE   B N   
5352 N  N   B ILE   B 106 ? 0.3565 0.2999 0.2911 -0.0135 0.1073  0.0196  106 ILE   B N   
5353 C  CA  A ILE   B 106 ? 0.3421 0.2576 0.3005 -0.0347 0.1696  0.0372  106 ILE   B CA  
5354 C  CA  B ILE   B 106 ? 0.3440 0.2872 0.2951 -0.0158 0.1031  0.0108  106 ILE   B CA  
5355 C  C   A ILE   B 106 ? 0.3102 0.2457 0.2974 -0.0304 0.1687  0.0213  106 ILE   B C   
5356 C  C   B ILE   B 106 ? 0.3221 0.2808 0.2942 -0.0126 0.0994  -0.0011 106 ILE   B C   
5357 O  O   A ILE   B 106 ? 0.3014 0.2215 0.2972 -0.0306 0.1683  0.0132  106 ILE   B O   
5358 O  O   B ILE   B 106 ? 0.3177 0.2704 0.2925 -0.0145 0.0941  -0.0078 106 ILE   B O   
5359 C  CB  A ILE   B 106 ? 0.3594 0.2476 0.3276 -0.0439 0.1573  0.0418  106 ILE   B CB  
5360 C  CB  B ILE   B 106 ? 0.3536 0.2838 0.3072 -0.0197 0.1004  0.0130  106 ILE   B CB  
5361 C  CG1 A ILE   B 106 ? 0.3665 0.2435 0.3355 -0.0346 0.1458  0.0374  106 ILE   B CG1 
5362 C  CG1 B ILE   B 106 ? 0.3565 0.2812 0.3118 -0.0149 0.0952  0.0131  106 ILE   B CG1 
5363 C  CG2 A ILE   B 106 ? 0.3649 0.2502 0.3458 -0.0549 0.1597  0.0454  106 ILE   B CG2 
5364 C  CG2 B ILE   B 106 ? 0.3580 0.2869 0.3197 -0.0246 0.1022  0.0133  106 ILE   B CG2 
5365 C  CD1 A ILE   B 106 ? 0.3692 0.2453 0.3373 -0.0254 0.1405  0.0386  106 ILE   B CD1 
5366 C  CD1 B ILE   B 106 ? 0.3572 0.2812 0.3141 -0.0100 0.0923  0.0152  106 ILE   B CD1 
5389 N  N   A GLN   B 107 ? 0.2924 0.2622 0.3145 -0.0275 0.1592  0.0183  107 GLN   B N   
5390 N  N   B GLN   B 107 ? 0.3072 0.2867 0.3086 -0.0090 0.0975  -0.0038 107 GLN   B N   
5391 C  CA  A GLN   B 107 ? 0.2762 0.2804 0.3294 -0.0222 0.1414  0.0154  107 GLN   B CA  
5392 C  CA  B GLN   B 107 ? 0.2936 0.2920 0.3233 -0.0051 0.0909  -0.0007 107 GLN   B CA  
5393 C  C   A GLN   B 107 ? 0.2473 0.2621 0.2972 -0.0116 0.1080  0.0084  107 GLN   B C   
5394 C  C   B GLN   B 107 ? 0.2607 0.2706 0.2927 -0.0010 0.0836  -0.0003 107 GLN   B C   
5395 O  O   A GLN   B 107 ? 0.2390 0.2626 0.3312 -0.0050 0.0797  -0.0083 107 GLN   B O   
5396 O  O   B GLN   B 107 ? 0.2576 0.2742 0.3107 0.0020  0.0675  -0.0129 107 GLN   B O   
5397 C  CB  A GLN   B 107 ? 0.3036 0.3194 0.3938 -0.0188 0.1238  0.0156  107 GLN   B CB  
5398 C  CB  B GLN   B 107 ? 0.3170 0.3195 0.3780 -0.0026 0.0798  0.0018  107 GLN   B CB  
5399 C  CG  A GLN   B 107 ? 0.3342 0.3555 0.4667 -0.0118 0.0886  0.0120  107 GLN   B CG  
5400 C  CG  B GLN   B 107 ? 0.3396 0.3458 0.4364 0.0008  0.0600  0.0032  107 GLN   B CG  
5401 C  CD  A GLN   B 107 ? 0.3559 0.3849 0.5252 -0.0100 0.0640  0.0120  107 GLN   B CD  
5402 C  CD  B GLN   B 107 ? 0.3557 0.3670 0.4848 0.0013  0.0454  0.0053  107 GLN   B CD  
5403 O  OE1 A GLN   B 107 ? 0.3646 0.3938 0.5455 -0.0126 0.0626  0.0082  107 GLN   B OE1 
5404 O  OE1 B GLN   B 107 ? 0.3623 0.3760 0.5008 -0.0011 0.0456  0.0040  107 GLN   B OE1 
5405 N  NE2 A GLN   B 107 ? 0.3634 0.3928 0.5443 -0.0040 0.0509  0.0166  107 GLN   B NE2 
5406 N  NE2 B GLN   B 107 ? 0.3610 0.3736 0.5013 0.0054  0.0374  0.0087  107 GLN   B NE2 
5423 N  N   . LEU   B 108 ? 0.2324 0.2455 0.2611 0.0076  0.0854  0.0074  108 LEU   B N   
5424 C  CA  . LEU   B 108 ? 0.2125 0.2154 0.2157 0.0273  0.0588  0.0168  108 LEU   B CA  
5425 C  C   . LEU   B 108 ? 0.1813 0.1755 0.2090 0.0284  0.0366  0.0317  108 LEU   B C   
5426 O  O   . LEU   B 108 ? 0.1829 0.1690 0.2088 0.0255  0.0246  0.0306  108 LEU   B O   
5427 C  CB  . LEU   B 108 ? 0.2296 0.2341 0.1999 0.0254  0.0614  0.0216  108 LEU   B CB  
5428 C  CG  . LEU   B 108 ? 0.2472 0.2624 0.2040 0.0232  0.0484  -0.0040 108 LEU   B CG  
5429 C  CD1 . LEU   B 108 ? 0.2554 0.2726 0.1869 0.0081  0.0459  -0.0050 108 LEU   B CD1 
5430 C  CD2 . LEU   B 108 ? 0.2636 0.2767 0.2253 0.0332  0.0321  -0.0184 108 LEU   B CD2 
5443 N  N   . LEU   B 109 ? 0.1695 0.1588 0.1994 0.0210  0.0364  0.0255  109 LEU   B N   
5444 C  CA  . LEU   B 109 ? 0.1494 0.1384 0.2160 0.0146  0.0319  0.0283  109 LEU   B CA  
5445 C  C   . LEU   B 109 ? 0.1412 0.1278 0.2068 0.0061  0.0312  0.0232  109 LEU   B C   
5446 O  O   . LEU   B 109 ? 0.1360 0.1252 0.2048 0.0080  0.0310  0.0310  109 LEU   B O   
5447 C  CB  . LEU   B 109 ? 0.1549 0.1302 0.2267 0.0164  0.0261  0.0372  109 LEU   B CB  
5448 C  CG  . LEU   B 109 ? 0.1592 0.1281 0.2265 0.0107  0.0229  0.0197  109 LEU   B CG  
5449 C  CD1 . LEU   B 109 ? 0.1550 0.1416 0.2034 0.0145  0.0222  0.0156  109 LEU   B CD1 
5450 C  CD2 . LEU   B 109 ? 0.1684 0.1337 0.2276 0.0063  0.0212  0.0255  109 LEU   B CD2 
5462 N  N   . LYS   B 110 ? 0.1360 0.1298 0.2017 0.0002  0.0301  0.0266  110 LYS   B N   
5463 C  CA  . LYS   B 110 ? 0.1352 0.1271 0.1967 0.0023  0.0284  0.0160  110 LYS   B CA  
5464 C  C   . LYS   B 110 ? 0.1301 0.1266 0.1840 0.0015  0.0280  0.0105  110 LYS   B C   
5465 O  O   . LYS   B 110 ? 0.1290 0.1277 0.1844 -0.0018 0.0182  0.0089  110 LYS   B O   
5466 C  CB  . LYS   B 110 ? 0.1373 0.1241 0.2168 -0.0017 0.0285  0.0107  110 LYS   B CB  
5467 C  CG  . LYS   B 110 ? 0.1338 0.1269 0.2405 -0.0089 0.0181  0.0148  110 LYS   B CG  
5468 C  CD  . LYS   B 110 ? 0.1394 0.1297 0.2422 -0.0059 0.0173  0.0109  110 LYS   B CD  
5469 C  CE  . LYS   B 110 ? 0.1358 0.1455 0.2502 -0.0037 0.0141  0.0054  110 LYS   B CE  
5470 N  NZ  . LYS   B 110 ? 0.1394 0.1534 0.2433 -0.0000 0.0073  0.0006  110 LYS   B NZ  
5484 N  N   . SER   B 111 ? 0.1361 0.1273 0.1990 0.0001  0.0299  0.0138  111 SER   B N   
5485 C  CA  . SER   B 111 ? 0.1442 0.1295 0.1865 0.0033  0.0173  0.0149  111 SER   B CA  
5486 C  C   . SER   B 111 ? 0.1402 0.1242 0.1742 0.0016  0.0077  0.0083  111 SER   B C   
5487 O  O   . SER   B 111 ? 0.1320 0.1290 0.1861 -0.0006 0.0090  0.0131  111 SER   B O   
5488 C  CB  . SER   B 111 ? 0.1554 0.1558 0.1940 0.0076  0.0318  0.0195  111 SER   B CB  
5489 O  OG  . SER   B 111 ? 0.1711 0.1914 0.1975 0.0068  0.0371  0.0212  111 SER   B OG  
5495 N  N   . ALA   B 112 ? 0.1337 0.1238 0.1847 0.0084  0.0173  0.0194  112 ALA   B N   
5496 C  CA  . ALA   B 112 ? 0.1292 0.1304 0.1662 0.0047  0.0097  0.0065  112 ALA   B CA  
5497 C  C   . ALA   B 112 ? 0.1221 0.1231 0.1619 0.0062  0.0033  0.0084  112 ALA   B C   
5498 O  O   . ALA   B 112 ? 0.1235 0.1253 0.1745 -0.0033 0.0094  0.0006  112 ALA   B O   
5499 C  CB  . ALA   B 112 ? 0.1346 0.1356 0.1774 0.0085  0.0056  0.0113  112 ALA   B CB  
5505 N  N   . TYR   B 113 ? 0.1168 0.1162 0.1721 0.0008  0.0102  0.0066  113 TYR   B N   
5506 C  CA  . TYR   B 113 ? 0.1179 0.1141 0.1683 -0.0041 0.0135  -0.0017 113 TYR   B CA  
5507 C  C   . TYR   B 113 ? 0.1159 0.1101 0.1616 -0.0099 0.0100  -0.0013 113 TYR   B C   
5508 O  O   . TYR   B 113 ? 0.1163 0.1187 0.1623 -0.0064 0.0073  0.0019  113 TYR   B O   
5509 C  CB  . TYR   B 113 ? 0.1232 0.1093 0.1804 -0.0009 0.0211  0.0092  113 TYR   B CB  
5510 C  CG  . TYR   B 113 ? 0.1228 0.1127 0.1938 -0.0010 0.0102  0.0110  113 TYR   B CG  
5511 C  CD1 . TYR   B 113 ? 0.1282 0.1112 0.1983 -0.0035 0.0161  0.0092  113 TYR   B CD1 
5512 C  CD2 . TYR   B 113 ? 0.1312 0.1135 0.1905 -0.0015 0.0030  0.0080  113 TYR   B CD2 
5513 C  CE1 . TYR   B 113 ? 0.1273 0.1131 0.1889 0.0008  0.0151  0.0059  113 TYR   B CE1 
5514 C  CE2 . TYR   B 113 ? 0.1327 0.1085 0.1975 0.0013  0.0083  0.0144  113 TYR   B CE2 
5515 C  CZ  . TYR   B 113 ? 0.1266 0.1135 0.2057 0.0057  0.0065  0.0031  113 TYR   B CZ  
5516 O  OH  . TYR   B 113 ? 0.1342 0.1180 0.2240 0.0107  0.0188  0.0035  113 TYR   B OH  
5526 N  N   . GLU   B 114 ? 0.1149 0.1075 0.1756 -0.0005 0.0129  0.0024  114 GLU   B N   
5527 C  CA  . GLU   B 114 ? 0.1160 0.1049 0.1760 0.0025  0.0027  -0.0013 114 GLU   B CA  
5528 C  C   . GLU   B 114 ? 0.1153 0.1098 0.1660 -0.0011 0.0044  0.0005  114 GLU   B C   
5529 O  O   . GLU   B 114 ? 0.1172 0.1121 0.1794 0.0017  -0.0003 0.0070  114 GLU   B O   
5530 C  CB  . GLU   B 114 ? 0.1144 0.1137 0.1824 -0.0028 0.0114  0.0041  114 GLU   B CB  
5531 C  CG  . GLU   B 114 ? 0.1221 0.1152 0.1853 -0.0046 0.0095  0.0076  114 GLU   B CG  
5532 C  CD  . GLU   B 114 ? 0.1172 0.1195 0.1946 -0.0014 0.0072  0.0019  114 GLU   B CD  
5533 O  OE1 . GLU   B 114 ? 0.1152 0.1363 0.1902 -0.0047 0.0147  0.0062  114 GLU   B OE1 
5534 O  OE2 . GLU   B 114 ? 0.1177 0.1356 0.2133 -0.0132 0.0150  0.0047  114 GLU   B OE2 
5541 N  N   . ASN   B 115 ? 0.1181 0.1066 0.1619 -0.0042 0.0003  0.0062  115 ASN   B N   
5542 C  CA  . ASN   B 115 ? 0.1182 0.1153 0.1534 -0.0071 0.0056  0.0036  115 ASN   B CA  
5543 C  C   . ASN   B 115 ? 0.1155 0.1087 0.1516 -0.0063 -0.0006 0.0060  115 ASN   B C   
5544 O  O   . ASN   B 115 ? 0.1255 0.1162 0.1584 -0.0101 0.0061  0.0047  115 ASN   B O   
5545 C  CB  . ASN   B 115 ? 0.1282 0.1232 0.1640 -0.0108 0.0038  0.0007  115 ASN   B CB  
5546 C  CG  . ASN   B 115 ? 0.1399 0.1323 0.1619 0.0024  -0.0019 -0.0051 115 ASN   B CG  
5547 O  OD1 . ASN   B 115 ? 0.1778 0.1424 0.1866 -0.0015 0.0099  -0.0096 115 ASN   B OD1 
5548 N  ND2 . ASN   B 115 ? 0.1375 0.1392 0.1543 -0.0020 0.0051  0.0053  115 ASN   B ND2 
5555 N  N   . PHE   B 116 ? 0.1154 0.1092 0.1436 -0.0005 -0.0014 0.0029  116 PHE   B N   
5556 C  CA  . PHE   B 116 ? 0.1192 0.1137 0.1485 -0.0073 0.0012  0.0049  116 PHE   B CA  
5557 C  C   . PHE   B 116 ? 0.1194 0.1072 0.1495 -0.0103 -0.0043 0.0037  116 PHE   B C   
5558 O  O   . PHE   B 116 ? 0.1228 0.1157 0.1605 -0.0034 -0.0010 0.0058  116 PHE   B O   
5559 C  CB  . PHE   B 116 ? 0.1160 0.1083 0.1449 -0.0034 -0.0015 -0.0005 116 PHE   B CB  
5560 C  CG  . PHE   B 116 ? 0.1129 0.1124 0.1491 -0.0058 0.0011  -0.0002 116 PHE   B CG  
5561 C  CD1 . PHE   B 116 ? 0.1227 0.1165 0.1676 -0.0038 0.0017  0.0026  116 PHE   B CD1 
5562 C  CD2 . PHE   B 116 ? 0.1183 0.1200 0.1492 -0.0029 -0.0000 -0.0098 116 PHE   B CD2 
5563 C  CE1 . PHE   B 116 ? 0.1264 0.1207 0.1613 -0.0032 -0.0081 0.0026  116 PHE   B CE1 
5564 C  CE2 . PHE   B 116 ? 0.1228 0.1166 0.1526 -0.0034 0.0034  -0.0053 116 PHE   B CE2 
5565 C  CZ  . PHE   B 116 ? 0.1162 0.1176 0.1612 -0.0035 -0.0047 0.0032  116 PHE   B CZ  
5575 N  N   . ASN   B 117 ? 0.1204 0.1097 0.1589 -0.0023 -0.0071 0.0060  117 ASN   B N   
5576 C  CA  . ASN   B 117 ? 0.1267 0.1139 0.1569 -0.0006 -0.0049 0.0025  117 ASN   B CA  
5577 C  C   . ASN   B 117 ? 0.1256 0.1129 0.1698 0.0013  -0.0081 0.0050  117 ASN   B C   
5578 O  O   . ASN   B 117 ? 0.1376 0.1193 0.1941 -0.0051 -0.0238 0.0053  117 ASN   B O   
5579 C  CB  . ASN   B 117 ? 0.1282 0.1154 0.1619 -0.0002 -0.0048 0.0009  117 ASN   B CB  
5580 C  CG  . ASN   B 117 ? 0.1265 0.1148 0.1692 0.0024  -0.0041 -0.0046 117 ASN   B CG  
5581 O  OD1 . ASN   B 117 ? 0.1471 0.1147 0.1878 -0.0141 0.0080  -0.0032 117 ASN   B OD1 
5582 N  ND2 . ASN   B 117 ? 0.1253 0.1162 0.1833 -0.0018 -0.0005 -0.0047 117 ASN   B ND2 
5589 N  N   . GLN   B 118 ? 0.1253 0.1102 0.1614 -0.0032 -0.0146 -0.0017 118 GLN   B N   
5590 C  CA  . GLN   B 118 ? 0.1341 0.1108 0.1811 0.0011  -0.0101 -0.0014 118 GLN   B CA  
5591 C  C   . GLN   B 118 ? 0.1396 0.1072 0.1864 -0.0011 -0.0050 -0.0010 118 GLN   B C   
5592 O  O   . GLN   B 118 ? 0.1558 0.1096 0.2100 -0.0071 0.0071  0.0040  118 GLN   B O   
5593 C  CB  . GLN   B 118 ? 0.1428 0.1154 0.1859 0.0043  -0.0124 0.0022  118 GLN   B CB  
5594 C  CG  . GLN   B 118 ? 0.1509 0.1176 0.1732 0.0082  -0.0054 -0.0060 118 GLN   B CG  
5595 C  CD  . GLN   B 118 ? 0.1532 0.1170 0.1728 0.0044  -0.0079 -0.0139 118 GLN   B CD  
5596 O  OE1 . GLN   B 118 ? 0.1625 0.1151 0.1974 0.0039  0.0097  0.0032  118 GLN   B OE1 
5597 N  NE2 . GLN   B 118 ? 0.1580 0.1183 0.1826 0.0048  -0.0080 0.0016  118 GLN   B NE2 
5606 N  N   . HIS   B 119 ? 0.1348 0.1148 0.1591 -0.0045 -0.0031 0.0075  119 HIS   B N   
5607 C  CA  . HIS   B 119 ? 0.1445 0.1281 0.1522 -0.0015 -0.0118 0.0090  119 HIS   B CA  
5608 C  C   . HIS   B 119 ? 0.1442 0.1262 0.1492 -0.0031 -0.0239 0.0065  119 HIS   B C   
5609 O  O   . HIS   B 119 ? 0.1539 0.1219 0.1690 -0.0223 -0.0154 0.0097  119 HIS   B O   
5610 C  CB  . HIS   B 119 ? 0.1444 0.1410 0.1581 -0.0024 -0.0175 -0.0010 119 HIS   B CB  
5611 C  CG  . HIS   B 119 ? 0.1520 0.1616 0.1690 0.0098  -0.0284 -0.0167 119 HIS   B CG  
5612 N  ND1 . HIS   B 119 ? 0.1649 0.1737 0.2093 0.0014  -0.0398 -0.0305 119 HIS   B ND1 
5613 C  CD2 . HIS   B 119 ? 0.1693 0.1782 0.1665 0.0344  -0.0388 -0.0174 119 HIS   B CD2 
5614 C  CE1 . HIS   B 119 ? 0.1847 0.1890 0.2157 0.0155  -0.0410 -0.0493 119 HIS   B CE1 
5615 N  NE2 . HIS   B 119 ? 0.1905 0.2001 0.1970 0.0295  -0.0454 -0.0387 119 HIS   B NE2 
5623 N  N   . GLU   B 120 ? 0.1652 0.1280 0.1449 -0.0096 -0.0308 0.0113  120 GLU   B N   
5624 C  CA  . GLU   B 120 ? 0.1943 0.1426 0.1581 -0.0036 -0.0385 0.0253  120 GLU   B CA  
5625 C  C   . GLU   B 120 ? 0.1701 0.1332 0.1553 -0.0128 -0.0266 0.0203  120 GLU   B C   
5626 O  O   . GLU   B 120 ? 0.1652 0.1412 0.1558 -0.0133 -0.0258 0.0115  120 GLU   B O   
5627 C  CB  . GLU   B 120 ? 0.2604 0.1775 0.2338 0.0193  -0.0718 0.0494  120 GLU   B CB  
5628 C  CG  . GLU   B 120 ? 0.3222 0.2576 0.3397 0.0316  -0.0961 0.0778  120 GLU   B CG  
5629 C  CD  . GLU   B 120 ? 0.3751 0.3414 0.4543 0.0315  -0.1047 0.0962  120 GLU   B CD  
5630 O  OE1 . GLU   B 120 ? 0.3962 0.3676 0.4887 0.0237  -0.1026 0.1121  120 GLU   B OE1 
5631 O  OE2 . GLU   B 120 ? 0.3992 0.3849 0.5069 0.0327  -0.1038 0.0900  120 GLU   B OE2 
5638 N  N   . VAL   B 121 ? 0.1579 0.1254 0.1569 -0.0188 -0.0194 0.0199  121 VAL   B N   
5639 C  CA  . VAL   B 121 ? 0.1556 0.1380 0.1395 -0.0194 -0.0190 0.0128  121 VAL   B CA  
5640 C  C   . VAL   B 121 ? 0.1506 0.1324 0.1311 -0.0229 -0.0154 0.0079  121 VAL   B C   
5641 O  O   . VAL   B 121 ? 0.1560 0.1313 0.1549 -0.0255 -0.0221 0.0033  121 VAL   B O   
5642 C  CB  . VAL   B 121 ? 0.1746 0.1730 0.1560 -0.0071 -0.0208 0.0154  121 VAL   B CB  
5643 C  CG1 . VAL   B 121 ? 0.1796 0.1814 0.1847 -0.0126 -0.0133 0.0163  121 VAL   B CG1 
5644 C  CG2 . VAL   B 121 ? 0.2013 0.1973 0.1551 0.0037  -0.0108 0.0051  121 VAL   B CG2 
5654 N  N   . LEU   B 122 ? 0.1409 0.1263 0.1298 -0.0140 -0.0196 0.0032  122 LEU   B N   
5655 C  CA  . LEU   B 122 ? 0.1297 0.1298 0.1185 -0.0186 -0.0148 0.0054  122 LEU   B CA  
5656 C  C   . LEU   B 122 ? 0.1345 0.1222 0.1249 -0.0253 -0.0135 0.0011  122 LEU   B C   
5657 O  O   . LEU   B 122 ? 0.1450 0.1256 0.1614 -0.0281 -0.0222 -0.0001 122 LEU   B O   
5658 C  CB  . LEU   B 122 ? 0.1528 0.1394 0.1553 -0.0030 -0.0252 0.0110  122 LEU   B CB  
5659 C  CG  . LEU   B 122 ? 0.1473 0.1461 0.1661 -0.0117 -0.0127 0.0092  122 LEU   B CG  
5660 C  CD1 . LEU   B 122 ? 0.1526 0.1655 0.1731 -0.0171 -0.0118 0.0008  122 LEU   B CD1 
5661 C  CD2 . LEU   B 122 ? 0.1495 0.1471 0.1522 -0.0098 -0.0088 -0.0037 122 LEU   B CD2 
5673 N  N   . LEU   B 123 ? 0.1336 0.1140 0.1225 -0.0226 -0.0107 0.0034  123 LEU   B N   
5674 C  CA  . LEU   B 123 ? 0.1394 0.1153 0.1227 -0.0236 -0.0123 -0.0064 123 LEU   B CA  
5675 C  C   . LEU   B 123 ? 0.1337 0.1145 0.1207 -0.0248 -0.0107 -0.0040 123 LEU   B C   
5676 O  O   . LEU   B 123 ? 0.1441 0.1146 0.1328 -0.0293 -0.0130 -0.0009 123 LEU   B O   
5677 C  CB  . LEU   B 123 ? 0.1433 0.1243 0.1327 -0.0229 -0.0094 -0.0030 123 LEU   B CB  
5678 C  CG  . LEU   B 123 ? 0.1379 0.1293 0.1420 -0.0155 -0.0079 0.0063  123 LEU   B CG  
5679 C  CD1 . LEU   B 123 ? 0.1432 0.1342 0.1498 -0.0171 -0.0007 -0.0080 123 LEU   B CD1 
5680 C  CD2 . LEU   B 123 ? 0.1449 0.1343 0.1671 -0.0152 0.0030  0.0188  123 LEU   B CD2 
5692 N  N   . ALA   B 124 ? 0.1320 0.1142 0.1255 -0.0178 -0.0017 -0.0028 124 ALA   B N   
5693 C  CA  . ALA   B 124 ? 0.1235 0.1134 0.1436 -0.0145 -0.0082 -0.0083 124 ALA   B CA  
5694 C  C   . ALA   B 124 ? 0.1211 0.1152 0.1374 -0.0160 -0.0058 -0.0034 124 ALA   B C   
5695 O  O   . ALA   B 124 ? 0.1327 0.1184 0.1428 -0.0107 -0.0071 -0.0006 124 ALA   B O   
5696 C  CB  . ALA   B 124 ? 0.1299 0.1168 0.1466 -0.0088 0.0032  0.0022  124 ALA   B CB  
5702 N  N   . PRO   B 125 ? 0.1290 0.1174 0.1350 -0.0139 -0.0120 0.0090  125 PRO   B N   
5703 C  CA  . PRO   B 125 ? 0.1385 0.1195 0.1472 -0.0102 -0.0141 0.0187  125 PRO   B CA  
5704 C  C   . PRO   B 125 ? 0.1314 0.1112 0.1585 -0.0137 -0.0068 0.0046  125 PRO   B C   
5705 O  O   . PRO   B 125 ? 0.1349 0.1124 0.1767 -0.0073 0.0025  0.0070  125 PRO   B O   
5706 C  CB  . PRO   B 125 ? 0.1411 0.1420 0.1558 -0.0193 -0.0160 0.0319  125 PRO   B CB  
5707 C  CG  . PRO   B 125 ? 0.1449 0.1481 0.1425 -0.0248 -0.0101 0.0129  125 PRO   B CG  
5708 C  CD  . PRO   B 125 ? 0.1389 0.1287 0.1311 -0.0264 -0.0068 0.0075  125 PRO   B CD  
5716 N  N   . LEU   B 126 ? 0.1362 0.1088 0.1818 -0.0121 0.0091  0.0127  126 LEU   B N   
5717 C  CA  . LEU   B 126 ? 0.1438 0.1177 0.1816 -0.0074 0.0206  0.0117  126 LEU   B CA  
5718 C  C   . LEU   B 126 ? 0.1411 0.1225 0.1974 0.0010  0.0277  0.0175  126 LEU   B C   
5719 O  O   . LEU   B 126 ? 0.1609 0.1480 0.2074 0.0167  0.0013  -0.0000 126 LEU   B O   
5720 C  CB  . LEU   B 126 ? 0.1615 0.1226 0.2169 -0.0129 0.0236  0.0067  126 LEU   B CB  
5721 C  CG  . LEU   B 126 ? 0.1743 0.1301 0.2239 -0.0229 0.0244  -0.0139 126 LEU   B CG  
5722 C  CD1 . LEU   B 126 ? 0.1879 0.1374 0.2659 -0.0183 0.0109  -0.0213 126 LEU   B CD1 
5723 C  CD2 . LEU   B 126 ? 0.1750 0.1471 0.2126 -0.0321 0.0211  -0.0090 126 LEU   B CD2 
5735 N  N   . LEU   B 127 ? 0.1371 0.1128 0.1997 0.0021  0.0293  0.0059  127 LEU   B N   
5736 C  CA  . LEU   B 127 ? 0.1374 0.1228 0.1998 -0.0008 0.0310  0.0183  127 LEU   B CA  
5737 C  C   . LEU   B 127 ? 0.1326 0.1222 0.1979 0.0012  0.0173  0.0186  127 LEU   B C   
5738 O  O   . LEU   B 127 ? 0.1350 0.1263 0.1977 -0.0098 0.0074  0.0184  127 LEU   B O   
5739 C  CB  . LEU   B 127 ? 0.1499 0.1243 0.1994 0.0021  0.0245  0.0193  127 LEU   B CB  
5740 C  CG  . LEU   B 127 ? 0.1620 0.1242 0.2056 0.0027  0.0222  0.0228  127 LEU   B CG  
5741 C  CD1 . LEU   B 127 ? 0.1720 0.1251 0.2113 0.0050  0.0175  0.0142  127 LEU   B CD1 
5742 C  CD2 . LEU   B 127 ? 0.1638 0.1318 0.2295 -0.0029 0.0225  0.0366  127 LEU   B CD2 
5754 N  N   . SER   B 128 ? 0.1329 0.1216 0.1949 0.0032  0.0060  0.0119  128 SER   B N   
5755 C  CA  . SER   B 128 ? 0.1465 0.1315 0.1898 0.0119  -0.0034 0.0198  128 SER   B CA  
5756 C  C   . SER   B 128 ? 0.1618 0.1361 0.2031 0.0099  -0.0223 0.0208  128 SER   B C   
5757 O  O   . SER   B 128 ? 0.1756 0.1402 0.2312 0.0069  -0.0140 0.0282  128 SER   B O   
5758 C  CB  . SER   B 128 ? 0.1605 0.1307 0.1913 0.0060  0.0056  0.0308  128 SER   B CB  
5759 O  OG  . SER   B 128 ? 0.1662 0.1429 0.2018 0.0090  0.0165  0.0307  128 SER   B OG  
5765 N  N   . ALA   B 129 ? 0.1752 0.1380 0.2258 0.0251  -0.0088 0.0070  129 ALA   B N   
5766 C  CA  . ALA   B 129 ? 0.1902 0.1436 0.2368 0.0270  -0.0090 -0.0048 129 ALA   B CA  
5767 C  C   . ALA   B 129 ? 0.1742 0.1363 0.2267 0.0197  0.0075  0.0049  129 ALA   B C   
5768 O  O   . ALA   B 129 ? 0.1609 0.1444 0.2371 0.0149  0.0001  0.0124  129 ALA   B O   
5769 C  CB  . ALA   B 129 ? 0.2154 0.1659 0.2654 0.0350  0.0027  -0.0165 129 ALA   B CB  
5775 N  N   . GLY   B 130 ? 0.1747 0.1349 0.2389 0.0252  0.0059  -0.0026 130 GLY   B N   
5776 C  CA  . GLY   B 130 ? 0.1771 0.1488 0.2375 0.0246  0.0256  0.0020  130 GLY   B CA  
5777 C  C   . GLY   B 130 ? 0.1810 0.1533 0.2338 0.0194  0.0162  0.0089  130 GLY   B C   
5778 O  O   . GLY   B 130 ? 0.1973 0.1599 0.2387 0.0163  0.0070  0.0175  130 GLY   B O   
5782 N  N   . ILE   B 131 ? 0.1747 0.1624 0.2378 0.0320  0.0138  0.0127  131 ILE   B N   
5783 C  CA  . ILE   B 131 ? 0.1934 0.1755 0.2374 0.0280  0.0028  0.0212  131 ILE   B CA  
5784 C  C   . ILE   B 131 ? 0.2070 0.1677 0.2117 0.0199  0.0010  0.0233  131 ILE   B C   
5785 O  O   . ILE   B 131 ? 0.2329 0.1781 0.2248 0.0198  -0.0218 0.0216  131 ILE   B O   
5786 C  CB  . ILE   B 131 ? 0.1929 0.2153 0.2752 0.0226  -0.0066 0.0266  131 ILE   B CB  
5787 C  CG1 . ILE   B 131 ? 0.1881 0.2408 0.2923 0.0020  0.0019  0.0284  131 ILE   B CG1 
5788 C  CG2 . ILE   B 131 ? 0.1949 0.2318 0.2983 0.0284  -0.0010 0.0183  131 ILE   B CG2 
5789 C  CD1 . ILE   B 131 ? 0.1945 0.2603 0.3064 -0.0132 -0.0031 0.0347  131 ILE   B CD1 
5801 N  N   . PHE   B 132 ? 0.1917 0.1482 0.2052 0.0174  0.0148  0.0218  132 PHE   B N   
5802 C  CA  . PHE   B 132 ? 0.2019 0.1508 0.1900 0.0092  0.0325  0.0111  132 PHE   B CA  
5803 C  C   . PHE   B 132 ? 0.2226 0.1649 0.2087 0.0102  0.0410  0.0142  132 PHE   B C   
5804 O  O   . PHE   B 132 ? 0.2397 0.1856 0.2378 0.0054  0.0504  0.0189  132 PHE   B O   
5805 C  CB  . PHE   B 132 ? 0.1867 0.1496 0.1764 0.0131  0.0281  0.0178  132 PHE   B CB  
5806 C  CG  . PHE   B 132 ? 0.1787 0.1513 0.1730 0.0152  0.0210  0.0161  132 PHE   B CG  
5807 C  CD1 . PHE   B 132 ? 0.1824 0.1536 0.2140 0.0127  0.0183  0.0200  132 PHE   B CD1 
5808 C  CD2 . PHE   B 132 ? 0.1812 0.1538 0.1541 0.0206  0.0154  0.0162  132 PHE   B CD2 
5809 C  CE1 . PHE   B 132 ? 0.1883 0.1592 0.2218 0.0070  0.0141  0.0182  132 PHE   B CE1 
5810 C  CE2 . PHE   B 132 ? 0.1854 0.1578 0.1615 0.0200  0.0084  0.0147  132 PHE   B CE2 
5811 C  CZ  . PHE   B 132 ? 0.1864 0.1571 0.1958 0.0076  -0.0037 0.0201  132 PHE   B CZ  
5821 N  N   . GLY   B 133 ? 0.2224 0.1569 0.2137 0.0085  0.0305  0.0370  133 GLY   B N   
5822 C  CA  . GLY   B 133 ? 0.2322 0.1690 0.2268 -0.0112 0.0277  0.0455  133 GLY   B CA  
5823 C  C   . GLY   B 133 ? 0.2362 0.1795 0.2214 -0.0252 0.0319  0.0471  133 GLY   B C   
5824 O  O   . GLY   B 133 ? 0.2536 0.1916 0.2750 -0.0401 0.0337  0.0580  133 GLY   B O   
5828 N  N   . ALA   B 134 ? 0.2142 0.1774 0.2130 -0.0237 0.0380  0.0331  134 ALA   B N   
5829 C  CA  . ALA   B 134 ? 0.2007 0.1770 0.2294 -0.0153 0.0435  0.0170  134 ALA   B CA  
5830 C  C   . ALA   B 134 ? 0.2074 0.1661 0.2398 -0.0070 0.0394  0.0232  134 ALA   B C   
5831 O  O   . ALA   B 134 ? 0.2123 0.1810 0.2490 0.0050  0.0348  0.0178  134 ALA   B O   
5832 C  CB  . ALA   B 134 ? 0.1944 0.1809 0.2446 -0.0077 0.0329  0.0123  134 ALA   B CB  
5838 N  N   . ASP   B 135 ? 0.2196 0.1603 0.2318 -0.0098 0.0204  0.0320  135 ASP   B N   
5839 C  CA  . ASP   B 135 ? 0.2374 0.1537 0.2571 -0.0154 0.0082  0.0324  135 ASP   B CA  
5840 C  C   . ASP   B 135 ? 0.2199 0.1404 0.2386 -0.0039 0.0098  0.0302  135 ASP   B C   
5841 O  O   . ASP   B 135 ? 0.2140 0.1334 0.2502 -0.0023 0.0046  0.0305  135 ASP   B O   
5842 C  CB  . ASP   B 135 ? 0.2694 0.1635 0.2818 -0.0405 0.0087  0.0355  135 ASP   B CB  
5843 C  CG  . ASP   B 135 ? 0.2989 0.1669 0.3340 -0.0584 0.0029  0.0293  135 ASP   B CG  
5844 O  OD1 . ASP   B 135 ? 0.3048 0.1522 0.3263 -0.0391 0.0046  0.0302  135 ASP   B OD1 
5845 O  OD2 . ASP   B 135 ? 0.3211 0.2003 0.3827 -0.0744 -0.0098 0.0074  135 ASP   B OD2 
5850 N  N   . PRO   B 136 ? 0.2141 0.1430 0.2450 0.0159  0.0002  0.0242  136 PRO   B N   
5851 C  CA  . PRO   B 136 ? 0.1918 0.1393 0.2431 0.0142  -0.0006 0.0081  136 PRO   B CA  
5852 C  C   . PRO   B 136 ? 0.1734 0.1248 0.2478 0.0118  -0.0018 0.0072  136 PRO   B C   
5853 O  O   . PRO   B 136 ? 0.1543 0.1267 0.2336 0.0081  0.0025  0.0110  136 PRO   B O   
5854 C  CB  . PRO   B 136 ? 0.1969 0.1594 0.2604 0.0283  -0.0041 -0.0014 136 PRO   B CB  
5855 C  CG  . PRO   B 136 ? 0.2190 0.1620 0.2835 0.0325  0.0012  0.0005  136 PRO   B CG  
5856 C  CD  . PRO   B 136 ? 0.2243 0.1567 0.2599 0.0351  0.0045  0.0087  136 PRO   B CD  
5864 N  N   . ILE   B 137 ? 0.1851 0.1156 0.2669 0.0115  -0.0069 0.0103  137 ILE   B N   
5865 C  CA  . ILE   B 137 ? 0.1914 0.1174 0.2763 0.0002  0.0009  0.0043  137 ILE   B CA  
5866 C  C   . ILE   B 137 ? 0.1816 0.1219 0.2668 -0.0045 0.0076  0.0138  137 ILE   B C   
5867 O  O   . ILE   B 137 ? 0.1705 0.1274 0.2583 -0.0106 0.0071  0.0107  137 ILE   B O   
5868 C  CB  . ILE   B 137 ? 0.2165 0.1266 0.3238 -0.0024 -0.0030 0.0074  137 ILE   B CB  
5869 C  CG1 . ILE   B 137 ? 0.2480 0.1420 0.3785 0.0058  0.0047  -0.0062 137 ILE   B CG1 
5870 C  CG2 . ILE   B 137 ? 0.2191 0.1313 0.3332 -0.0223 -0.0065 0.0128  137 ILE   B CG2 
5871 C  CD1 . ILE   B 137 ? 0.2718 0.1690 0.4232 0.0161  0.0022  -0.0008 137 ILE   B CD1 
5883 N  N   . HIS   B 138 ? 0.1837 0.1205 0.2706 -0.0093 0.0119  0.0134  138 HIS   B N   
5884 C  CA  . HIS   B 138 ? 0.1944 0.1319 0.2605 -0.0055 0.0246  0.0168  138 HIS   B CA  
5885 C  C   . HIS   B 138 ? 0.1758 0.1276 0.2372 -0.0031 0.0275  0.0258  138 HIS   B C   
5886 O  O   . HIS   B 138 ? 0.1692 0.1360 0.2528 0.0030  0.0341  0.0353  138 HIS   B O   
5887 C  CB  . HIS   B 138 ? 0.2189 0.1449 0.2779 -0.0075 0.0415  0.0102  138 HIS   B CB  
5888 C  CG  . HIS   B 138 ? 0.2414 0.1631 0.2784 -0.0112 0.0632  0.0361  138 HIS   B CG  
5889 N  ND1 . HIS   B 138 ? 0.2503 0.1813 0.3068 -0.0124 0.0812  0.0310  138 HIS   B ND1 
5890 C  CD2 . HIS   B 138 ? 0.2548 0.1718 0.2750 -0.0079 0.0703  0.0299  138 HIS   B CD2 
5891 C  CE1 . HIS   B 138 ? 0.2583 0.1797 0.3017 -0.0101 0.0846  0.0306  138 HIS   B CE1 
5892 N  NE2 . HIS   B 138 ? 0.2625 0.1702 0.2816 -0.0014 0.0792  0.0224  138 HIS   B NE2 
5900 N  N   . SER   B 139 ? 0.1710 0.1174 0.2367 0.0017  0.0244  0.0145  139 SER   B N   
5901 C  CA  . SER   B 139 ? 0.1637 0.1100 0.2310 0.0041  0.0237  -0.0025 139 SER   B CA  
5902 C  C   . SER   B 139 ? 0.1446 0.1064 0.2277 -0.0023 0.0199  0.0046  139 SER   B C   
5903 O  O   . SER   B 139 ? 0.1468 0.1115 0.2156 0.0009  0.0040  0.0026  139 SER   B O   
5904 C  CB  . SER   B 139 ? 0.1728 0.1154 0.2253 0.0040  0.0104  0.0033  139 SER   B CB  
5905 O  OG  . SER   B 139 ? 0.1783 0.1194 0.2204 0.0012  -0.0063 0.0101  139 SER   B OG  
5911 N  N   . LEU   B 140 ? 0.1431 0.1032 0.2301 -0.0051 0.0156  -0.0011 140 LEU   B N   
5912 C  CA  . LEU   B 140 ? 0.1420 0.1071 0.2311 -0.0024 0.0068  -0.0015 140 LEU   B CA  
5913 C  C   . LEU   B 140 ? 0.1384 0.1088 0.2361 -0.0054 0.0028  -0.0054 140 LEU   B C   
5914 O  O   . LEU   B 140 ? 0.1334 0.1166 0.2296 -0.0025 -0.0024 -0.0002 140 LEU   B O   
5915 C  CB  . LEU   B 140 ? 0.1349 0.1091 0.2270 -0.0089 0.0144  -0.0107 140 LEU   B CB  
5916 C  CG  . LEU   B 140 ? 0.1465 0.1133 0.2192 -0.0121 0.0032  -0.0009 140 LEU   B CG  
5917 C  CD1 . LEU   B 140 ? 0.1572 0.1214 0.2296 -0.0107 0.0071  -0.0001 140 LEU   B CD1 
5918 C  CD2 . LEU   B 140 ? 0.1641 0.1220 0.2402 -0.0128 -0.0006 -0.0105 140 LEU   B CD2 
5930 N  N   . ARG   B 141 ? 0.1301 0.1094 0.2426 -0.0114 0.0052  -0.0038 141 ARG   B N   
5931 C  CA  . ARG   B 141 ? 0.1338 0.1122 0.2793 -0.0163 0.0225  -0.0048 141 ARG   B CA  
5932 C  C   . ARG   B 141 ? 0.1292 0.1118 0.2627 -0.0132 0.0153  -0.0026 141 ARG   B C   
5933 O  O   . ARG   B 141 ? 0.1357 0.1158 0.2571 -0.0116 0.0091  -0.0129 141 ARG   B O   
5934 C  CB  . ARG   B 141 ? 0.1510 0.1226 0.3144 -0.0165 0.0404  -0.0027 141 ARG   B CB  
5935 C  CG  . ARG   B 141 ? 0.1834 0.1501 0.3372 -0.0201 0.0353  -0.0019 141 ARG   B CG  
5936 C  CD  . ARG   B 141 ? 0.2232 0.1749 0.3405 -0.0196 0.0232  -0.0151 141 ARG   B CD  
5937 N  NE  . ARG   B 141 ? 0.2436 0.1767 0.3411 -0.0318 0.0356  -0.0203 141 ARG   B NE  
5938 C  CZ  . ARG   B 141 ? 0.2611 0.1590 0.3194 -0.0277 0.0465  -0.0281 141 ARG   B CZ  
5939 N  NH1 . ARG   B 141 ? 0.2694 0.1514 0.3045 -0.0268 0.0413  -0.0306 141 ARG   B NH1 
5940 N  NH2 . ARG   B 141 ? 0.2791 0.1639 0.3325 -0.0116 0.0416  -0.0191 141 ARG   B NH2 
5954 N  N   . VAL   B 142 ? 0.1326 0.1107 0.2439 -0.0073 0.0176  -0.0045 142 VAL   B N   
5955 C  CA  . VAL   B 142 ? 0.1314 0.1152 0.2390 -0.0063 0.0213  -0.0044 142 VAL   B CA  
5956 C  C   . VAL   B 142 ? 0.1264 0.1120 0.2379 -0.0030 0.0138  -0.0033 142 VAL   B C   
5957 O  O   . VAL   B 142 ? 0.1358 0.1101 0.2494 0.0011  0.0130  -0.0040 142 VAL   B O   
5958 C  CB  . VAL   B 142 ? 0.1407 0.1267 0.2476 0.0003  0.0256  0.0093  142 VAL   B CB  
5959 C  CG1 . VAL   B 142 ? 0.1400 0.1227 0.2455 0.0061  0.0224  0.0054  142 VAL   B CG1 
5960 C  CG2 . VAL   B 142 ? 0.1627 0.1350 0.2491 0.0025  0.0209  0.0088  142 VAL   B CG2 
5970 N  N   . CYS   B 143 ? 0.1242 0.1102 0.2264 -0.0006 0.0059  0.0041  143 CYS   B N   
5971 C  CA  . CYS   B 143 ? 0.1250 0.1103 0.2202 -0.0083 0.0039  0.0012  143 CYS   B CA  
5972 C  C   . CYS   B 143 ? 0.1211 0.1142 0.2225 -0.0065 0.0083  -0.0065 143 CYS   B C   
5973 O  O   . CYS   B 143 ? 0.1251 0.1173 0.2260 -0.0053 0.0027  -0.0014 143 CYS   B O   
5974 C  CB  . CYS   B 143 ? 0.1305 0.1187 0.2178 -0.0068 0.0046  0.0003  143 CYS   B CB  
5975 S  SG  . CYS   B 143 ? 0.1340 0.1352 0.2209 -0.0037 0.0090  0.0013  143 CYS   B SG  
5981 N  N   . VAL   B 144 ? 0.1293 0.1130 0.2345 -0.0063 0.0079  -0.0153 144 VAL   B N   
5982 C  CA  . VAL   B 144 ? 0.1309 0.1214 0.2579 -0.0136 -0.0006 -0.0202 144 VAL   B CA  
5983 C  C   . VAL   B 144 ? 0.1301 0.1242 0.2645 -0.0097 -0.0026 -0.0042 144 VAL   B C   
5984 O  O   . VAL   B 144 ? 0.1428 0.1446 0.2821 0.0037  -0.0017 0.0099  144 VAL   B O   
5985 C  CB  . VAL   B 144 ? 0.1570 0.1408 0.3151 -0.0142 -0.0120 -0.0315 144 VAL   B CB  
5986 C  CG1 . VAL   B 144 ? 0.1822 0.1780 0.3481 -0.0074 -0.0190 -0.0295 144 VAL   B CG1 
5987 C  CG2 . VAL   B 144 ? 0.1687 0.1368 0.3206 0.0013  -0.0262 -0.0336 144 VAL   B CG2 
5997 N  N   . ASP   B 145 ? 0.1300 0.1193 0.2733 -0.0092 0.0046  -0.0147 145 ASP   B N   
5998 C  CA  . ASP   B 145 ? 0.1293 0.1245 0.2981 -0.0062 0.0109  -0.0168 145 ASP   B CA  
5999 C  C   . ASP   B 145 ? 0.1236 0.1290 0.2715 -0.0054 0.0065  -0.0093 145 ASP   B C   
6000 O  O   . ASP   B 145 ? 0.1265 0.1446 0.3191 -0.0118 0.0156  -0.0278 145 ASP   B O   
6001 C  CB  . ASP   B 145 ? 0.1422 0.1353 0.3429 -0.0123 0.0260  -0.0078 145 ASP   B CB  
6002 C  CG  . ASP   B 145 ? 0.1593 0.1393 0.3973 -0.0211 0.0339  -0.0027 145 ASP   B CG  
6003 O  OD1 . ASP   B 145 ? 0.1589 0.1425 0.3991 -0.0224 -0.0015 -0.0160 145 ASP   B OD1 
6004 O  OD2 . ASP   B 145 ? 0.1882 0.1461 0.4403 -0.0305 0.0492  0.0088  145 ASP   B OD2 
6009 N  N   . THR   B 146 ? 0.1188 0.1200 0.2280 -0.0067 0.0007  0.0012  146 THR   B N   
6010 C  CA  . THR   B 146 ? 0.1281 0.1165 0.2084 -0.0057 0.0108  0.0010  146 THR   B CA  
6011 C  C   . THR   B 146 ? 0.1250 0.1143 0.2072 -0.0039 -0.0007 -0.0019 146 THR   B C   
6012 O  O   . THR   B 146 ? 0.1296 0.1151 0.2179 -0.0054 0.0003  -0.0020 146 THR   B O   
6013 C  CB  . THR   B 146 ? 0.1328 0.1152 0.2155 -0.0038 0.0224  0.0019  146 THR   B CB  
6014 O  OG1 . THR   B 146 ? 0.1330 0.1142 0.2322 -0.0074 0.0166  0.0084  146 THR   B OG1 
6015 C  CG2 . THR   B 146 ? 0.1398 0.1227 0.2014 -0.0025 0.0198  -0.0042 146 THR   B CG2 
6023 N  N   . VAL   B 147 ? 0.1311 0.1169 0.2001 -0.0022 0.0107  0.0010  147 VAL   B N   
6024 C  CA  . VAL   B 147 ? 0.1282 0.1127 0.1878 -0.0072 -0.0033 -0.0028 147 VAL   B CA  
6025 C  C   . VAL   B 147 ? 0.1279 0.1159 0.1970 -0.0141 -0.0100 -0.0072 147 VAL   B C   
6026 O  O   . VAL   B 147 ? 0.1388 0.1266 0.2055 -0.0158 -0.0232 -0.0118 147 VAL   B O   
6027 C  CB  . VAL   B 147 ? 0.1363 0.1211 0.1803 -0.0101 -0.0066 -0.0050 147 VAL   B CB  
6028 C  CG1 . VAL   B 147 ? 0.1349 0.1398 0.1817 -0.0120 -0.0008 0.0041  147 VAL   B CG1 
6029 C  CG2 . VAL   B 147 ? 0.1395 0.1255 0.1816 -0.0123 -0.0005 0.0085  147 VAL   B CG2 
6039 N  N   . ARG   B 148 ? 0.1289 0.1161 0.2030 -0.0074 -0.0139 -0.0096 148 ARG   B N   
6040 C  CA  . ARG   B 148 ? 0.1306 0.1266 0.1862 -0.0066 -0.0245 -0.0123 148 ARG   B CA  
6041 C  C   . ARG   B 148 ? 0.1383 0.1333 0.1832 -0.0068 -0.0207 -0.0098 148 ARG   B C   
6042 O  O   . ARG   B 148 ? 0.1578 0.1614 0.1858 -0.0197 -0.0266 -0.0027 148 ARG   B O   
6043 C  CB  . ARG   B 148 ? 0.1392 0.1373 0.1873 -0.0021 -0.0297 -0.0168 148 ARG   B CB  
6044 C  CG  . ARG   B 148 ? 0.1399 0.1552 0.2074 -0.0060 -0.0270 -0.0322 148 ARG   B CG  
6045 C  CD  . ARG   B 148 ? 0.1452 0.1662 0.2210 0.0038  -0.0215 -0.0318 148 ARG   B CD  
6046 N  NE  . ARG   B 148 ? 0.1499 0.1585 0.2088 0.0252  -0.0245 -0.0285 148 ARG   B NE  
6047 C  CZ  . ARG   B 148 ? 0.1449 0.1496 0.1923 0.0176  -0.0161 -0.0212 148 ARG   B CZ  
6048 N  NH1 . ARG   B 148 ? 0.1364 0.1566 0.1928 -0.0015 -0.0050 -0.0154 148 ARG   B NH1 
6049 N  NH2 . ARG   B 148 ? 0.1667 0.1391 0.1951 0.0193  -0.0141 -0.0111 148 ARG   B NH2 
6063 N  N   . THR   B 149 ? 0.1410 0.1288 0.1856 -0.0127 -0.0197 -0.0011 149 THR   B N   
6064 C  CA  . THR   B 149 ? 0.1479 0.1326 0.1766 -0.0138 -0.0232 0.0036  149 THR   B CA  
6065 C  C   . THR   B 149 ? 0.1454 0.1270 0.1634 -0.0178 -0.0289 0.0028  149 THR   B C   
6066 O  O   . THR   B 149 ? 0.1535 0.1268 0.1794 -0.0193 -0.0144 -0.0029 149 THR   B O   
6067 C  CB  . THR   B 149 ? 0.1497 0.1304 0.1697 -0.0148 -0.0182 0.0015  149 THR   B CB  
6068 O  OG1 . THR   B 149 ? 0.1503 0.1386 0.1596 -0.0208 -0.0189 0.0013  149 THR   B OG1 
6069 C  CG2 . THR   B 149 ? 0.1549 0.1357 0.1841 -0.0078 -0.0119 -0.0013 149 THR   B CG2 
6077 N  N   . ASN   B 150 ? 0.1538 0.1237 0.1636 -0.0150 -0.0258 -0.0007 150 ASN   B N   
6078 C  CA  . ASN   B 150 ? 0.1568 0.1421 0.1671 -0.0210 -0.0299 -0.0099 150 ASN   B CA  
6079 C  C   . ASN   B 150 ? 0.1486 0.1386 0.1616 -0.0153 -0.0271 -0.0015 150 ASN   B C   
6080 O  O   . ASN   B 150 ? 0.1564 0.1358 0.1867 -0.0278 -0.0390 -0.0014 150 ASN   B O   
6081 C  CB  . ASN   B 150 ? 0.1757 0.1788 0.1720 -0.0240 -0.0311 0.0043  150 ASN   B CB  
6082 C  CG  . ASN   B 150 ? 0.1993 0.2217 0.1993 -0.0206 -0.0352 0.0240  150 ASN   B CG  
6083 O  OD1 . ASN   B 150 ? 0.2095 0.2341 0.2192 -0.0308 -0.0463 0.0146  150 ASN   B OD1 
6084 N  ND2 . ASN   B 150 ? 0.2076 0.2404 0.2308 -0.0066 -0.0373 0.0649  150 ASN   B ND2 
6091 N  N   . VAL   B 151 ? 0.1402 0.1354 0.1557 -0.0166 -0.0215 -0.0010 151 VAL   B N   
6092 C  CA  . VAL   B 151 ? 0.1376 0.1351 0.1586 -0.0227 -0.0217 -0.0008 151 VAL   B CA  
6093 C  C   . VAL   B 151 ? 0.1434 0.1298 0.1599 -0.0261 -0.0238 -0.0036 151 VAL   B C   
6094 O  O   . VAL   B 151 ? 0.1494 0.1343 0.1889 -0.0247 -0.0160 -0.0115 151 VAL   B O   
6095 C  CB  . VAL   B 151 ? 0.1625 0.1518 0.1788 -0.0092 -0.0124 -0.0037 151 VAL   B CB  
6096 C  CG1 . VAL   B 151 ? 0.1716 0.1508 0.2070 -0.0130 -0.0001 -0.0144 151 VAL   B CG1 
6097 C  CG2 . VAL   B 151 ? 0.1698 0.1641 0.1721 0.0001  -0.0087 0.0098  151 VAL   B CG2 
6107 N  N   . TYR   B 152 ? 0.1377 0.1172 0.1508 -0.0203 -0.0184 -0.0063 152 TYR   B N   
6108 C  CA  . TYR   B 152 ? 0.1446 0.1343 0.1436 -0.0259 -0.0081 -0.0079 152 TYR   B CA  
6109 C  C   . TYR   B 152 ? 0.1412 0.1256 0.1380 -0.0204 -0.0063 -0.0094 152 TYR   B C   
6110 O  O   . TYR   B 152 ? 0.1446 0.1295 0.1520 -0.0250 -0.0056 -0.0020 152 TYR   B O   
6111 C  CB  . TYR   B 152 ? 0.1586 0.1473 0.1586 -0.0253 -0.0064 -0.0002 152 TYR   B CB  
6112 C  CG  . TYR   B 152 ? 0.1687 0.1537 0.1469 -0.0359 -0.0096 -0.0029 152 TYR   B CG  
6113 C  CD1 . TYR   B 152 ? 0.1753 0.1671 0.1447 -0.0246 -0.0188 0.0019  152 TYR   B CD1 
6114 C  CD2 . TYR   B 152 ? 0.1867 0.1709 0.1611 -0.0337 -0.0077 -0.0081 152 TYR   B CD2 
6115 C  CE1 . TYR   B 152 ? 0.1930 0.1879 0.1594 -0.0227 -0.0271 0.0161  152 TYR   B CE1 
6116 C  CE2 . TYR   B 152 ? 0.1964 0.1938 0.1620 -0.0339 -0.0153 -0.0080 152 TYR   B CE2 
6117 C  CZ  . TYR   B 152 ? 0.2030 0.2094 0.1517 -0.0292 -0.0395 0.0158  152 TYR   B CZ  
6118 O  OH  . TYR   B 152 ? 0.2303 0.2457 0.1855 -0.0198 -0.0450 0.0169  152 TYR   B OH  
6128 N  N   . LEU   B 153 ? 0.1421 0.1222 0.1538 -0.0266 -0.0106 -0.0052 153 LEU   B N   
6129 C  CA  . LEU   B 153 ? 0.1453 0.1172 0.1382 -0.0205 -0.0052 -0.0103 153 LEU   B CA  
6130 C  C   . LEU   B 153 ? 0.1456 0.1181 0.1456 -0.0231 -0.0059 -0.0126 153 LEU   B C   
6131 O  O   . LEU   B 153 ? 0.1542 0.1373 0.1656 -0.0115 -0.0087 -0.0319 153 LEU   B O   
6132 C  CB  . LEU   B 153 ? 0.1415 0.1175 0.1601 -0.0253 -0.0032 -0.0081 153 LEU   B CB  
6133 C  CG  . LEU   B 153 ? 0.1382 0.1293 0.1865 -0.0252 -0.0029 -0.0042 153 LEU   B CG  
6134 C  CD1 . LEU   B 153 ? 0.1475 0.1435 0.1961 -0.0243 0.0061  0.0008  153 LEU   B CD1 
6135 C  CD2 . LEU   B 153 ? 0.1443 0.1400 0.1878 -0.0278 0.0101  0.0030  153 LEU   B CD2 
6147 N  N   . ALA   B 154 ? 0.1391 0.1193 0.1569 -0.0046 -0.0105 -0.0093 154 ALA   B N   
6148 C  CA  . ALA   B 154 ? 0.1513 0.1304 0.1900 0.0011  -0.0159 -0.0240 154 ALA   B CA  
6149 C  C   . ALA   B 154 ? 0.1603 0.1302 0.1998 0.0039  -0.0244 -0.0294 154 ALA   B C   
6150 O  O   . ALA   B 154 ? 0.1912 0.1326 0.2085 0.0047  -0.0107 -0.0113 154 ALA   B O   
6151 C  CB  . ALA   B 154 ? 0.1453 0.1470 0.2081 -0.0012 -0.0195 -0.0295 154 ALA   B CB  
6157 N  N   . VAL   B 155 ? 0.1317 0.1211 0.2141 0.0002  -0.0050 -0.0218 155 VAL   B N   
6158 C  CA  . VAL   B 155 ? 0.1300 0.1247 0.2140 -0.0002 -0.0092 -0.0110 155 VAL   B CA  
6159 C  C   . VAL   B 155 ? 0.1320 0.1241 0.2090 -0.0024 -0.0107 -0.0179 155 VAL   B C   
6160 O  O   . VAL   B 155 ? 0.1446 0.1408 0.2516 0.0042  -0.0114 -0.0389 155 VAL   B O   
6161 C  CB  . VAL   B 155 ? 0.1334 0.1389 0.2419 -0.0075 -0.0179 0.0031  155 VAL   B CB  
6162 C  CG1 . VAL   B 155 ? 0.1337 0.1365 0.2405 -0.0091 -0.0134 -0.0010 155 VAL   B CG1 
6163 C  CG2 . VAL   B 155 ? 0.1275 0.1490 0.2735 -0.0097 -0.0192 0.0307  155 VAL   B CG2 
6173 N  N   . PHE   B 156 ? 0.1246 0.1330 0.2230 0.0013  -0.0051 -0.0168 156 PHE   B N   
6174 C  CA  . PHE   B 156 ? 0.1252 0.1418 0.2550 0.0027  -0.0091 -0.0148 156 PHE   B CA  
6175 C  C   . PHE   B 156 ? 0.1290 0.1471 0.2840 0.0106  -0.0127 -0.0369 156 PHE   B C   
6176 O  O   . PHE   B 156 ? 0.1470 0.1640 0.3096 0.0222  -0.0016 -0.0472 156 PHE   B O   
6177 C  CB  . PHE   B 156 ? 0.1348 0.1361 0.2512 -0.0013 -0.0186 -0.0074 156 PHE   B CB  
6178 C  CG  . PHE   B 156 ? 0.1362 0.1473 0.2656 -0.0024 -0.0143 0.0063  156 PHE   B CG  
6179 C  CD1 . PHE   B 156 ? 0.1392 0.1721 0.3107 0.0024  -0.0071 0.0348  156 PHE   B CD1 
6180 C  CD2 . PHE   B 156 ? 0.1396 0.1610 0.2713 0.0060  -0.0172 0.0107  156 PHE   B CD2 
6181 C  CE1 . PHE   B 156 ? 0.1412 0.1879 0.3233 0.0055  -0.0046 0.0402  156 PHE   B CE1 
6182 C  CE2 . PHE   B 156 ? 0.1480 0.1814 0.2952 0.0084  -0.0131 0.0154  156 PHE   B CE2 
6183 C  CZ  . PHE   B 156 ? 0.1394 0.1882 0.3178 0.0163  -0.0171 0.0225  156 PHE   B CZ  
6193 N  N   . ASP   B 157 ? 0.1295 0.1383 0.3054 0.0105  -0.0231 -0.0205 157 ASP   B N   
6194 C  CA  . ASP   B 157 ? 0.1370 0.1419 0.3436 0.0128  -0.0254 -0.0234 157 ASP   B CA  
6195 C  C   . ASP   B 157 ? 0.1366 0.1345 0.3503 0.0136  -0.0192 -0.0383 157 ASP   B C   
6196 O  O   . ASP   B 157 ? 0.1281 0.1395 0.3354 0.0063  -0.0178 -0.0316 157 ASP   B O   
6197 C  CB  . ASP   B 157 ? 0.1603 0.1630 0.3599 0.0090  -0.0511 -0.0083 157 ASP   B CB  
6198 C  CG  . ASP   B 157 ? 0.1876 0.1828 0.3796 0.0077  -0.0389 -0.0097 157 ASP   B CG  
6199 O  OD1 . ASP   B 157 ? 0.1954 0.1817 0.3967 0.0129  -0.0247 -0.0043 157 ASP   B OD1 
6200 O  OD2 . ASP   B 157 ? 0.2202 0.2043 0.3984 0.0034  -0.0235 -0.0101 157 ASP   B OD2 
6205 N  N   . LYS   B 158 ? 0.1420 0.1627 0.3699 0.0114  -0.0066 -0.0703 158 LYS   B N   
6206 C  CA  . LYS   B 158 ? 0.1611 0.1845 0.3736 0.0055  0.0001  -0.0892 158 LYS   B CA  
6207 C  C   . LYS   B 158 ? 0.1578 0.1685 0.3820 0.0088  -0.0041 -0.0844 158 LYS   B C   
6208 O  O   . LYS   B 158 ? 0.1602 0.1657 0.3790 -0.0025 -0.0069 -0.0912 158 LYS   B O   
6209 C  CB  . LYS   B 158 ? 0.1843 0.2232 0.3731 0.0092  0.0145  -0.1099 158 LYS   B CB  
6210 C  CG  . LYS   B 158 ? 0.2175 0.2630 0.3877 0.0135  0.0166  -0.1169 158 LYS   B CG  
6211 C  CD  . LYS   B 158 ? 0.2423 0.3139 0.4022 0.0134  0.0189  -0.1146 158 LYS   B CD  
6212 C  CE  . LYS   B 158 ? 0.2520 0.3495 0.4204 0.0166  0.0142  -0.1153 158 LYS   B CE  
6213 N  NZ  . LYS   B 158 ? 0.2520 0.3721 0.4169 0.0145  0.0114  -0.1152 158 LYS   B NZ  
6227 N  N   . ASN   B 159 ? 0.1578 0.1588 0.3975 0.0109  -0.0165 -0.0695 159 ASN   B N   
6228 C  CA  . ASN   B 159 ? 0.1716 0.1548 0.4192 0.0203  -0.0284 -0.0584 159 ASN   B CA  
6229 C  C   . ASN   B 159 ? 0.1555 0.1442 0.4057 0.0156  -0.0412 -0.0455 159 ASN   B C   
6230 O  O   . ASN   B 159 ? 0.1561 0.1366 0.4228 -0.0001 -0.0479 -0.0348 159 ASN   B O   
6231 C  CB  . ASN   B 159 ? 0.1926 0.1678 0.4504 0.0274  -0.0349 -0.0542 159 ASN   B CB  
6232 C  CG  . ASN   B 159 ? 0.2204 0.1881 0.4815 0.0297  -0.0521 -0.0619 159 ASN   B CG  
6233 O  OD1 . ASN   B 159 ? 0.2353 0.1913 0.4794 0.0359  -0.0552 -0.0730 159 ASN   B OD1 
6234 N  ND2 . ASN   B 159 ? 0.2253 0.2004 0.4949 0.0330  -0.0609 -0.0536 159 ASN   B ND2 
6241 N  N   . LEU   B 160 ? 0.1465 0.1408 0.3766 0.0132  -0.0385 -0.0447 160 LEU   B N   
6242 C  CA  . LEU   B 160 ? 0.1467 0.1432 0.3411 0.0069  -0.0339 -0.0273 160 LEU   B CA  
6243 C  C   . LEU   B 160 ? 0.1379 0.1304 0.3259 -0.0017 -0.0224 -0.0352 160 LEU   B C   
6244 O  O   . LEU   B 160 ? 0.1303 0.1346 0.3142 -0.0083 -0.0193 -0.0244 160 LEU   B O   
6245 C  CB  . LEU   B 160 ? 0.1421 0.1497 0.3123 0.0044  -0.0368 -0.0220 160 LEU   B CB  
6246 C  CG  . LEU   B 160 ? 0.1454 0.1612 0.2954 0.0105  -0.0316 -0.0093 160 LEU   B CG  
6247 C  CD1 . LEU   B 160 ? 0.1600 0.1766 0.2913 0.0035  -0.0106 -0.0118 160 LEU   B CD1 
6248 C  CD2 . LEU   B 160 ? 0.1482 0.1595 0.2996 0.0228  -0.0287 -0.0188 160 LEU   B CD2 
6260 N  N   . TYR   B 161 ? 0.1329 0.1336 0.3275 -0.0061 -0.0002 -0.0363 161 TYR   B N   
6261 C  CA  . TYR   B 161 ? 0.1449 0.1388 0.3106 -0.0102 0.0171  -0.0421 161 TYR   B CA  
6262 C  C   . TYR   B 161 ? 0.1472 0.1370 0.2989 -0.0130 0.0118  -0.0430 161 TYR   B C   
6263 O  O   . TYR   B 161 ? 0.1500 0.1361 0.2870 -0.0173 0.0037  -0.0383 161 TYR   B O   
6264 C  CB  . TYR   B 161 ? 0.1595 0.1437 0.3133 -0.0237 0.0335  -0.0430 161 TYR   B CB  
6265 C  CG  . TYR   B 161 ? 0.1843 0.1518 0.3003 -0.0247 0.0408  -0.0487 161 TYR   B CG  
6266 C  CD1 . TYR   B 161 ? 0.1902 0.1505 0.2955 -0.0369 0.0461  -0.0450 161 TYR   B CD1 
6267 C  CD2 . TYR   B 161 ? 0.2060 0.1578 0.2842 -0.0251 0.0289  -0.0599 161 TYR   B CD2 
6268 C  CE1 . TYR   B 161 ? 0.2093 0.1673 0.2981 -0.0409 0.0414  -0.0473 161 TYR   B CE1 
6269 C  CE2 . TYR   B 161 ? 0.2257 0.1732 0.2974 -0.0306 0.0316  -0.0558 161 TYR   B CE2 
6270 C  CZ  . TYR   B 161 ? 0.2249 0.1786 0.2949 -0.0442 0.0267  -0.0502 161 TYR   B CZ  
6271 O  OH  . TYR   B 161 ? 0.2510 0.2074 0.3123 -0.0423 0.0195  -0.0480 161 TYR   B OH  
6281 N  N   . ASP   B 162 ? 0.1484 0.1368 0.3185 -0.0078 -0.0004 -0.0525 162 ASP   B N   
6282 C  CA  . ASP   B 162 ? 0.1653 0.1450 0.3247 -0.0066 -0.0064 -0.0524 162 ASP   B CA  
6283 C  C   . ASP   B 162 ? 0.1605 0.1306 0.3195 -0.0118 -0.0106 -0.0406 162 ASP   B C   
6284 O  O   . ASP   B 162 ? 0.1683 0.1380 0.3150 -0.0167 -0.0161 -0.0385 162 ASP   B O   
6285 C  CB  . ASP   B 162 ? 0.1844 0.1628 0.3491 -0.0018 -0.0089 -0.0703 162 ASP   B CB  
6286 C  CG  . ASP   B 162 ? 0.1888 0.1895 0.3731 0.0099  -0.0100 -0.0855 162 ASP   B CG  
6287 O  OD1 . ASP   B 162 ? 0.1884 0.2078 0.3592 0.0025  0.0025  -0.0855 162 ASP   B OD1 
6288 O  OD2 . ASP   B 162 ? 0.2019 0.2097 0.4013 0.0304  -0.0107 -0.0838 162 ASP   B OD2 
6293 N  N   . LYS   B 163 ? 0.1564 0.1202 0.3138 -0.0109 -0.0241 -0.0258 163 LYS   B N   
6294 C  CA  . LYS   B 163 ? 0.1669 0.1327 0.3097 -0.0185 -0.0289 -0.0078 163 LYS   B CA  
6295 C  C   . LYS   B 163 ? 0.1415 0.1279 0.2980 -0.0149 -0.0263 -0.0027 163 LYS   B C   
6296 O  O   . LYS   B 163 ? 0.1422 0.1360 0.3227 -0.0152 -0.0227 -0.0043 163 LYS   B O   
6297 C  CB  . LYS   B 163 ? 0.2083 0.1685 0.3425 -0.0202 -0.0329 0.0149  163 LYS   B CB  
6298 C  CG  . LYS   B 163 ? 0.2887 0.2451 0.4082 -0.0276 -0.0285 0.0242  163 LYS   B CG  
6299 C  CD  . LYS   B 163 ? 0.3665 0.3271 0.4763 -0.0379 -0.0287 0.0277  163 LYS   B CD  
6300 C  CE  . LYS   B 163 ? 0.4322 0.3985 0.5151 -0.0429 -0.0240 0.0289  163 LYS   B CE  
6301 N  NZ  . LYS   B 163 ? 0.4704 0.4466 0.5468 -0.0441 -0.0222 0.0229  163 LYS   B NZ  
6315 N  N   . LEU   B 164 ? 0.1327 0.1240 0.2692 -0.0133 -0.0204 -0.0069 164 LEU   B N   
6316 C  CA  . LEU   B 164 ? 0.1340 0.1225 0.2548 -0.0082 -0.0239 -0.0029 164 LEU   B CA  
6317 C  C   . LEU   B 164 ? 0.1384 0.1252 0.2518 -0.0104 -0.0285 -0.0017 164 LEU   B C   
6318 O  O   . LEU   B 164 ? 0.1381 0.1468 0.2621 -0.0173 -0.0219 -0.0005 164 LEU   B O   
6319 C  CB  . LEU   B 164 ? 0.1307 0.1227 0.2338 -0.0068 -0.0203 -0.0034 164 LEU   B CB  
6320 C  CG  . LEU   B 164 ? 0.1423 0.1395 0.2397 -0.0057 -0.0077 -0.0009 164 LEU   B CG  
6321 C  CD1 . LEU   B 164 ? 0.1440 0.1346 0.2456 -0.0117 -0.0139 -0.0106 164 LEU   B CD1 
6322 C  CD2 . LEU   B 164 ? 0.1579 0.1752 0.2459 -0.0025 -0.0004 -0.0176 164 LEU   B CD2 
6334 N  N   . VAL   B 165 ? 0.1617 0.1343 0.2723 -0.0204 -0.0297 -0.0114 165 VAL   B N   
6335 C  CA  . VAL   B 165 ? 0.1959 0.1471 0.2740 -0.0291 -0.0477 -0.0103 165 VAL   B CA  
6336 C  C   . VAL   B 165 ? 0.2185 0.1525 0.3024 -0.0372 -0.0701 -0.0101 165 VAL   B C   
6337 O  O   . VAL   B 165 ? 0.2336 0.1705 0.3103 -0.0446 -0.0711 -0.0093 165 VAL   B O   
6338 C  CB  . VAL   B 165 ? 0.2166 0.1679 0.2791 -0.0208 -0.0219 -0.0177 165 VAL   B CB  
6339 C  CG1 . VAL   B 165 ? 0.2339 0.1781 0.3016 -0.0200 -0.0099 -0.0153 165 VAL   B CG1 
6340 C  CG2 . VAL   B 165 ? 0.2099 0.1740 0.2756 -0.0197 -0.0100 -0.0123 165 VAL   B CG2 
6350 N  N   . SER   B 166 ? 0.2247 0.1402 0.3361 -0.0345 -0.0774 -0.0302 166 SER   B N   
6351 C  CA  . SER   B 166 ? 0.2213 0.1476 0.3996 -0.0339 -0.0641 -0.0349 166 SER   B CA  
6352 C  C   . SER   B 166 ? 0.2080 0.1571 0.4090 -0.0388 -0.0694 -0.0125 166 SER   B C   
6353 O  O   . SER   B 166 ? 0.2126 0.1765 0.4458 -0.0489 -0.0752 -0.0415 166 SER   B O   
6354 C  CB  . SER   B 166 ? 0.2218 0.1598 0.4303 -0.0238 -0.0568 -0.0492 166 SER   B CB  
6355 O  OG  . SER   B 166 ? 0.2108 0.1575 0.4464 -0.0177 -0.0576 -0.0320 166 SER   B OG  
6361 N  N   . SER   B 167 ? 0.1928 0.1518 0.3767 -0.0390 -0.0740 0.0362  167 SER   B N   
6362 C  CA  . SER   B 167 ? 0.1878 0.1588 0.3620 -0.0405 -0.0497 0.0290  167 SER   B CA  
6363 C  C   . SER   B 167 ? 0.1821 0.1634 0.3375 -0.0472 -0.0432 0.0426  167 SER   B C   
6364 O  O   . SER   B 167 ? 0.1835 0.1761 0.3243 -0.0482 -0.0347 0.0463  167 SER   B O   
6365 C  CB  . SER   B 167 ? 0.1832 0.1666 0.3613 -0.0361 -0.0192 0.0225  167 SER   B CB  
6366 O  OG  . SER   B 167 ? 0.1742 0.1737 0.3522 -0.0269 -0.0058 0.0207  167 SER   B OG  
6372 N  N   . PHE   B 168 ? 0.1822 0.1593 0.3260 -0.0418 -0.0340 0.0498  168 PHE   B N   
6373 C  CA  . PHE   B 168 ? 0.1860 0.1582 0.3003 -0.0434 -0.0301 0.0344  168 PHE   B CA  
6374 C  C   . PHE   B 168 ? 0.1626 0.1497 0.2568 -0.0249 -0.0077 0.0171  168 PHE   B C   
6375 O  O   . PHE   B 168 ? 0.1924 0.1427 0.2570 -0.0008 -0.0048 -0.0008 168 PHE   B O   
6376 C  CB  . PHE   B 168 ? 0.1998 0.1671 0.3108 -0.0511 -0.0498 0.0413  168 PHE   B CB  
6377 C  CG  . PHE   B 168 ? 0.2266 0.1563 0.3023 -0.0508 -0.0481 0.0186  168 PHE   B CG  
6378 C  CD1 . PHE   B 168 ? 0.2554 0.1619 0.3046 -0.0451 -0.0543 0.0116  168 PHE   B CD1 
6379 C  CD2 . PHE   B 168 ? 0.2188 0.1472 0.2949 -0.0439 -0.0403 0.0251  168 PHE   B CD2 
6380 C  CE1 . PHE   B 168 ? 0.2648 0.1690 0.2989 -0.0316 -0.0478 0.0130  168 PHE   B CE1 
6381 C  CE2 . PHE   B 168 ? 0.2409 0.1536 0.3014 -0.0312 -0.0473 0.0203  168 PHE   B CE2 
6382 C  CZ  . PHE   B 168 ? 0.2564 0.1536 0.2954 -0.0189 -0.0498 0.0247  168 PHE   B CZ  
6392 N  N   . LEU   B 169 ? 0.1620 0.1601 0.2533 -0.0043 0.0006  0.0006  169 LEU   B N   
6393 C  CA  . LEU   B 169 ? 0.1921 0.1948 0.2893 -0.0079 -0.0045 -0.0256 169 LEU   B CA  
6394 C  C   . LEU   B 169 ? 0.2208 0.2199 0.3470 0.0085  -0.0079 -0.0501 169 LEU   B C   
6395 O  O   . LEU   B 169 ? 0.2384 0.2427 0.3946 0.0030  -0.0047 -0.0781 169 LEU   B O   
6396 C  CB  . LEU   B 169 ? 0.2141 0.2335 0.3016 -0.0147 -0.0133 -0.0062 169 LEU   B CB  
6397 C  CG  . LEU   B 169 ? 0.2532 0.2698 0.3416 -0.0079 -0.0196 0.0015  169 LEU   B CG  
6398 C  CD1 . LEU   B 169 ? 0.2658 0.2874 0.3462 -0.0029 -0.0266 0.0171  169 LEU   B CD1 
6399 C  CD2 . LEU   B 169 ? 0.2487 0.2764 0.3514 -0.0034 -0.0122 -0.0093 169 LEU   B CD2 
6400 O  OXT . LEU   B 169 ? 0.2385 0.2276 0.3476 0.0373  -0.0073 -0.0469 169 LEU   B OXT 
6412 N  N2  B A1BAD C .   ? 0.1693 0.2007 0.2034 -0.0031 -0.0197 0.0011  201 A1BAD A N2  
6413 C  C3  B A1BAD C .   ? 0.1934 0.2244 0.2475 -0.0069 -0.0166 -0.0132 201 A1BAD A C3  
6414 C  C6  B A1BAD C .   ? 0.2076 0.2363 0.2715 -0.0060 -0.0169 -0.0205 201 A1BAD A C6  
6415 C  C9  B A1BAD C .   ? 0.1580 0.1915 0.1859 0.0004  -0.0172 0.0097  201 A1BAD A C9  
6416 C  C12 B A1BAD C .   ? 0.1510 0.1843 0.1736 0.0026  -0.0169 0.0185  201 A1BAD A C12 
6417 C  C14 B A1BAD C .   ? 0.1436 0.1809 0.1717 -0.0008 -0.0202 0.0240  201 A1BAD A C14 
6418 C  C1  B A1BAD C .   ? 0.1906 0.2204 0.2349 -0.0079 -0.0125 -0.0133 201 A1BAD A C1  
6419 C  C10 B A1BAD C .   ? 0.1512 0.1856 0.1798 0.0050  -0.0090 0.0150  201 A1BAD A C10 
6420 C  C11 B A1BAD C .   ? 0.1485 0.1808 0.1679 0.0036  -0.0153 0.0182  201 A1BAD A C11 
6421 C  C13 B A1BAD C .   ? 0.1488 0.1833 0.1719 0.0006  -0.0158 0.0249  201 A1BAD A C13 
6422 C  C2  B A1BAD C .   ? 0.1844 0.2157 0.2258 -0.0063 -0.0165 -0.0097 201 A1BAD A C2  
6423 C  C4  B A1BAD C .   ? 0.1998 0.2315 0.2587 -0.0052 -0.0181 -0.0176 201 A1BAD A C4  
6424 C  C5  B A1BAD C .   ? 0.2032 0.2345 0.2652 -0.0058 -0.0177 -0.0218 201 A1BAD A C5  
6425 C  C7  B A1BAD C .   ? 0.2069 0.2358 0.2700 -0.0041 -0.0179 -0.0163 201 A1BAD A C7  
6426 C  C8  B A1BAD C .   ? 0.2045 0.2349 0.2660 -0.0045 -0.0211 -0.0151 201 A1BAD A C8  
6427 N  N1  B A1BAD C .   ? 0.2018 0.2336 0.2597 -0.0034 -0.0198 -0.0173 201 A1BAD A N1  
6428 N  N3  B A1BAD C .   ? 0.1545 0.1892 0.1880 0.0009  -0.0115 0.0085  201 A1BAD A N3  
6429 N  N4  B A1BAD C .   ? 0.1498 0.1838 0.1662 0.0028  -0.0072 0.0171  201 A1BAD A N4  
6430 N  N5  B A1BAD C .   ? 0.1465 0.1789 0.1663 0.0045  -0.0219 0.0214  201 A1BAD A N5  
6431 O  O1  B A1BAD C .   ? 0.1915 0.2228 0.2402 -0.0091 -0.0073 -0.0106 201 A1BAD A O1  
6447 O  O1  C A1BAE D .   ? 0.1589 0.1338 0.1905 -0.0261 -0.0128 0.0160  202 A1BAE A O1  
6448 C  C1  C A1BAE D .   ? 0.1566 0.1257 0.1779 -0.0269 -0.0161 0.0156  202 A1BAE A C1  
6449 C  C2  C A1BAE D .   ? 0.1452 0.1113 0.1554 -0.0287 -0.0204 0.0206  202 A1BAE A C2  
6450 C  C3  C A1BAE D .   ? 0.1479 0.1257 0.1660 -0.0289 -0.0204 0.0161  202 A1BAE A C3  
6451 C  C4  C A1BAE D .   ? 0.1583 0.1435 0.1909 -0.0245 -0.0149 0.0117  202 A1BAE A C4  
6452 C  C5  C A1BAE D .   ? 0.1651 0.1517 0.2012 -0.0261 -0.0093 0.0060  202 A1BAE A C5  
6453 C  C6  C A1BAE D .   ? 0.1712 0.1623 0.2151 -0.0247 -0.0052 0.0028  202 A1BAE A C6  
6454 C  C7  C A1BAE D .   ? 0.1700 0.1657 0.2125 -0.0223 -0.0057 0.0088  202 A1BAE A C7  
6455 C  C8  C A1BAE D .   ? 0.1665 0.1649 0.2091 -0.0205 -0.0134 0.0083  202 A1BAE A C8  
6456 C  C10 C A1BAE D .   ? 0.1194 0.1076 0.1416 0.0025  0.0135  0.0242  202 A1BAE A C10 
6457 C  C11 C A1BAE D .   ? 0.1126 0.0985 0.1386 -0.0042 0.0031  0.0299  202 A1BAE A C11 
6458 C  C12 C A1BAE D .   ? 0.1145 0.0986 0.1370 -0.0052 -0.0024 0.0335  202 A1BAE A C12 
6459 C  C13 C A1BAE D .   ? 0.1134 0.1002 0.1442 -0.0067 -0.0042 0.0324  202 A1BAE A C13 
6460 C  C14 C A1BAE D .   ? 0.1079 0.1008 0.1479 -0.0097 -0.0120 0.0308  202 A1BAE A C14 
6461 C  C9  C A1BAE D .   ? 0.1236 0.1026 0.1323 -0.0089 -0.0054 0.0265  202 A1BAE A C9  
6462 N  N1  C A1BAE D .   ? 0.1620 0.1582 0.1997 -0.0195 -0.0173 0.0064  202 A1BAE A N1  
6463 N  N2  C A1BAE D .   ? 0.1342 0.0981 0.1380 -0.0194 -0.0174 0.0257  202 A1BAE A N2  
6464 N  N3  C A1BAE D .   ? 0.1250 0.1094 0.1404 -0.0020 0.0061  0.0151  202 A1BAE A N3  
6465 N  N4  C A1BAE D .   ? 0.1156 0.1061 0.1369 -0.0054 0.0201  0.0295  202 A1BAE A N4  
6466 N  N5  C A1BAE D .   ? 0.1106 0.0971 0.1392 -0.0014 -0.0110 0.0307  202 A1BAE A N5  
6482 CL CL  B CL    E .   ? 0.2310 0.1679 0.2893 -0.0205 0.0277  -0.0148 203 CL    A CL  
6483 O  O   . HOH   F .   ? 0.2758 0.2285 0.3790 -0.0160 -0.0492 0.0559  301 HOH   A O   
6484 O  O   . HOH   F .   ? 0.4190 0.7813 0.4578 -0.1042 0.0777  0.0710  302 HOH   A O   
6485 O  O   . HOH   F .   ? 0.2116 0.2020 0.3706 0.0107  -0.0644 0.0190  303 HOH   A O   
6486 O  O   . HOH   F .   ? 0.2814 0.2514 0.4600 -0.0318 -0.1308 0.1087  304 HOH   A O   
6487 O  O   . HOH   F .   ? 0.5585 0.4783 0.3081 0.1848  -0.1155 0.0707  305 HOH   A O   
6488 O  O   . HOH   F .   ? 0.6684 0.6082 0.4055 -0.1402 -0.0323 0.1909  306 HOH   A O   
6489 O  O   . HOH   F .   ? 0.2992 0.3021 0.1664 -0.0295 0.0345  0.0364  307 HOH   A O   
6490 O  O   . HOH   F .   ? 0.4193 0.3319 0.5650 -0.0329 0.1053  -0.0645 308 HOH   A O   
6491 O  O   . HOH   F .   ? 0.2314 0.2251 0.3068 0.0020  0.0884  0.0628  309 HOH   A O   
6492 O  O   . HOH   F .   ? 0.3099 0.6929 0.5794 -0.0433 -0.0863 0.2393  310 HOH   A O   
6493 O  O   . HOH   F .   ? 0.2814 0.2996 0.3474 -0.0907 0.0941  -0.0143 311 HOH   A O   
6494 O  O   . HOH   F .   ? 0.6333 0.6248 0.4207 -0.1191 -0.1146 -0.0945 312 HOH   A O   
6495 O  O   . HOH   F .   ? 0.5121 0.2008 0.4848 0.0699  -0.0059 -0.0064 313 HOH   A O   
6496 O  O   . HOH   F .   ? 0.1997 0.1608 0.2379 0.0229  -0.0429 -0.0060 314 HOH   A O   
6497 O  O   . HOH   F .   ? 0.5609 0.3687 0.4411 -0.0680 0.1213  0.0986  315 HOH   A O   
6498 O  O   B HOH   F .   ? 0.2215 0.2746 0.2658 -0.0581 0.0195  0.0452  316 HOH   A O   
6499 O  O   . HOH   F .   ? 0.2018 0.1806 0.3556 -0.0441 -0.0051 -0.0080 317 HOH   A O   
6500 O  O   . HOH   F .   ? 0.3095 0.2960 0.3015 -0.0908 0.0354  0.0691  318 HOH   A O   
6501 O  O   . HOH   F .   ? 0.1739 0.2531 0.2893 0.0206  -0.0189 -0.0326 319 HOH   A O   
6502 O  O   . HOH   F .   ? 0.7328 0.5151 0.3442 -0.0579 -0.0595 0.0944  320 HOH   A O   
6503 O  O   . HOH   F .   ? 0.1900 0.3342 0.3970 -0.0304 0.0414  -0.1132 321 HOH   A O   
6504 O  O   . HOH   F .   ? 0.3300 0.3928 0.3461 -0.1022 0.1520  -0.0063 322 HOH   A O   
6505 O  O   . HOH   F .   ? 0.2510 0.2039 0.2496 -0.0280 0.0131  -0.0125 323 HOH   A O   
6506 O  O   . HOH   F .   ? 0.3140 0.4231 0.2872 -0.0271 0.0585  0.0641  324 HOH   A O   
6507 O  O   A HOH   F .   ? 0.3335 0.1471 0.1717 0.0274  0.0346  0.0050  325 HOH   A O   
6508 O  O   . HOH   F .   ? 0.2428 0.2201 0.2630 0.0437  0.0136  0.0334  326 HOH   A O   
6509 O  O   . HOH   F .   ? 0.4696 0.5206 0.2474 -0.1099 0.0939  0.0930  327 HOH   A O   
6510 O  O   . HOH   F .   ? 0.5008 0.4001 0.3588 -0.1003 -0.0995 -0.0195 328 HOH   A O   
6511 O  O   . HOH   F .   ? 0.4380 0.5558 0.5386 0.1879  0.1049  -0.0947 329 HOH   A O   
6512 O  O   . HOH   F .   ? 0.8785 0.3896 0.5628 -0.0507 -0.1352 -0.0100 330 HOH   A O   
6513 O  O   A HOH   F .   ? 0.2618 0.3441 0.5329 -0.0326 0.1158  0.1448  331 HOH   A O   
6514 O  O   . HOH   F .   ? 0.6202 0.5083 0.5870 0.0604  -0.1041 0.0606  332 HOH   A O   
6515 O  O   . HOH   F .   ? 0.5339 0.2894 0.4708 0.0991  -0.0588 -0.0147 333 HOH   A O   
6516 O  O   . HOH   F .   ? 0.4082 0.1907 0.4407 0.0288  -0.1495 0.0610  334 HOH   A O   
6517 O  O   A HOH   F .   ? 0.1394 0.2740 0.2034 0.0483  0.0428  0.0725  335 HOH   A O   
6518 O  O   . HOH   F .   ? 0.2639 0.4987 0.3937 0.0146  -0.0622 0.0694  336 HOH   A O   
6519 O  O   . HOH   F .   ? 0.2542 0.3626 0.3620 -0.0739 -0.0570 -0.0552 337 HOH   A O   
6520 O  O   . HOH   F .   ? 0.4885 0.2873 0.2514 -0.0587 0.0534  0.0344  338 HOH   A O   
6521 O  O   . HOH   F .   ? 0.1401 0.3646 0.2926 -0.0084 0.0191  0.0383  339 HOH   A O   
6522 O  O   . HOH   F .   ? 0.3158 0.2835 0.3483 -0.0871 0.0036  -0.0140 340 HOH   A O   
6523 O  O   B HOH   F .   ? 0.1862 0.2082 0.1531 -0.0112 -0.0264 -0.0176 341 HOH   A O   
6524 O  O   . HOH   F .   ? 0.1406 0.2155 0.2133 0.0063  -0.0051 0.0470  342 HOH   A O   
6525 O  O   . HOH   F .   ? 0.2029 0.4415 0.3803 -0.0119 -0.0416 0.1839  343 HOH   A O   
6526 O  O   . HOH   F .   ? 0.4557 0.3912 0.4252 -0.1796 -0.0667 0.1898  344 HOH   A O   
6527 O  O   . HOH   F .   ? 0.1926 0.1848 0.3685 0.0176  0.0825  -0.0222 345 HOH   A O   
6528 O  O   . HOH   F .   ? 0.5731 0.4500 0.4920 -0.0208 -0.0915 -0.0859 346 HOH   A O   
6529 O  O   . HOH   F .   ? 0.2420 0.4078 0.3479 0.0946  -0.0579 0.0116  347 HOH   A O   
6530 O  O   . HOH   F .   ? 0.2441 0.4481 0.3179 -0.0532 0.0649  -0.0046 348 HOH   A O   
6531 O  O   . HOH   F .   ? 0.3472 0.3261 0.2382 0.0218  -0.1025 0.0247  349 HOH   A O   
6532 O  O   . HOH   F .   ? 0.1731 0.1567 0.1953 0.0125  -0.0206 0.0321  350 HOH   A O   
6533 O  O   . HOH   F .   ? 0.3328 0.4506 0.3510 0.1821  0.0655  0.0330  351 HOH   A O   
6534 O  O   . HOH   F .   ? 0.2945 0.3320 0.5260 -0.0443 -0.1021 -0.1037 352 HOH   A O   
6535 O  O   . HOH   F .   ? 0.2985 0.3470 0.2049 -0.0581 -0.0246 -0.0903 353 HOH   A O   
6536 O  O   . HOH   F .   ? 0.1993 0.1686 0.2637 0.0054  -0.0470 -0.0087 354 HOH   A O   
6537 O  O   A HOH   F .   ? 0.2500 0.4113 0.5076 0.0746  0.0442  0.0710  355 HOH   A O   
6538 O  O   . HOH   F .   ? 0.3688 0.6695 0.4913 -0.0699 -0.1431 0.0501  356 HOH   A O   
6539 O  O   B HOH   F .   ? 0.3370 0.1676 0.2374 0.0677  -0.0644 0.0366  357 HOH   A O   
6540 O  O   . HOH   F .   ? 0.1892 0.1721 0.1709 0.0095  0.0046  0.0137  358 HOH   A O   
6541 O  O   . HOH   F .   ? 0.1418 0.1800 0.2502 0.0104  -0.0083 0.0090  359 HOH   A O   
6542 O  O   . HOH   F .   ? 0.1303 0.1241 0.1289 -0.0017 0.0094  0.0068  360 HOH   A O   
6543 O  O   . HOH   F .   ? 0.5989 0.2686 0.3750 -0.1644 0.2077  -0.0672 361 HOH   A O   
6544 O  O   . HOH   F .   ? 0.1883 0.2587 0.3567 0.0297  0.0800  -0.0571 362 HOH   A O   
6545 O  O   . HOH   F .   ? 0.5989 0.3687 0.2850 0.0044  0.0543  0.1324  363 HOH   A O   
6546 O  O   . HOH   F .   ? 0.1828 0.1826 0.2332 -0.0331 0.0020  0.0368  364 HOH   A O   
6547 O  O   A HOH   F .   ? 0.2006 0.4991 0.2141 0.1178  0.0180  0.0020  365 HOH   A O   
6548 O  O   . HOH   F .   ? 0.6024 0.4950 0.5509 0.0737  0.2607  -0.0944 366 HOH   A O   
6549 O  O   B HOH   F .   ? 0.2331 0.1294 0.2273 0.0363  -0.0754 -0.0239 367 HOH   A O   
6550 O  O   . HOH   F .   ? 0.1540 0.1248 0.2013 -0.0061 0.0182  -0.0079 368 HOH   A O   
6551 O  O   . HOH   F .   ? 0.3838 0.2125 0.2087 0.1156  0.0427  0.0194  369 HOH   A O   
6552 O  O   . HOH   F .   ? 0.1410 0.1433 0.1481 -0.0028 -0.0149 -0.0060 370 HOH   A O   
6553 O  O   B HOH   F .   ? 0.1486 0.1789 0.1912 0.0021  -0.0079 0.0214  371 HOH   A O   
6554 O  O   A HOH   F .   ? 0.1324 0.1399 0.1679 0.0114  -0.0261 -0.0280 372 HOH   A O   
6555 O  O   . HOH   F .   ? 0.2421 0.4262 0.3095 0.0369  0.0679  0.1840  373 HOH   A O   
6556 O  O   . HOH   F .   ? 0.2755 0.5834 0.5022 0.0693  0.0338  0.2095  374 HOH   A O   
6557 O  O   . HOH   F .   ? 0.2954 0.2264 0.5249 -0.0600 -0.0217 0.0180  375 HOH   A O   
6558 O  O   B HOH   F .   ? 0.3981 0.2163 0.3167 -0.0796 0.0102  0.0792  376 HOH   A O   
6559 O  O   . HOH   F .   ? 0.1582 0.1611 0.2261 -0.0191 0.0152  0.0357  377 HOH   A O   
6560 O  O   . HOH   F .   ? 0.3749 0.2061 0.4451 -0.0910 0.0981  0.0271  378 HOH   A O   
6561 O  O   B HOH   F .   ? 0.3400 0.3476 0.3764 -0.0573 -0.1046 0.1017  379 HOH   A O   
6562 O  O   . HOH   F .   ? 0.2428 0.3874 0.3068 -0.0403 -0.0190 0.0648  380 HOH   A O   
6563 O  O   . HOH   F .   ? 0.1328 0.1330 0.1731 -0.0004 -0.0160 0.0046  381 HOH   A O   
6564 O  O   . HOH   F .   ? 0.5557 0.5713 0.5811 -0.0655 -0.0558 0.1669  382 HOH   A O   
6565 O  O   . HOH   F .   ? 0.1707 0.2104 0.1838 -0.0094 -0.0032 0.0600  383 HOH   A O   
6566 O  O   . HOH   F .   ? 0.1686 0.2270 0.3309 -0.0192 0.0655  0.0582  384 HOH   A O   
6567 O  O   A HOH   F .   ? 0.4904 0.3885 0.3281 -0.0705 0.1337  0.1221  385 HOH   A O   
6568 O  O   . HOH   F .   ? 0.2993 0.2795 0.2060 0.0281  0.0738  0.0144  386 HOH   A O   
6569 O  O   . HOH   F .   ? 0.1870 0.2221 0.2114 -0.0194 -0.0308 0.0370  387 HOH   A O   
6570 O  O   B HOH   F .   ? 0.2867 0.2753 0.4628 0.0178  0.0342  0.0424  388 HOH   A O   
6571 O  O   . HOH   F .   ? 0.2448 0.1967 0.1686 -0.0539 0.0203  0.0301  389 HOH   A O   
6572 O  O   . HOH   F .   ? 0.2343 0.1655 0.2556 -0.0005 0.0127  0.0196  390 HOH   A O   
6573 O  O   . HOH   F .   ? 0.3243 0.2405 0.3294 0.0018  -0.0508 0.0841  391 HOH   A O   
6574 O  O   . HOH   F .   ? 0.1796 0.1857 0.3729 0.0369  0.1090  0.1015  392 HOH   A O   
6575 O  O   . HOH   F .   ? 0.3230 0.5930 0.4908 0.1142  0.1330  -0.1017 393 HOH   A O   
6576 O  O   . HOH   F .   ? 0.5204 0.6557 0.5769 0.1554  0.1312  0.1259  394 HOH   A O   
6577 O  O   . HOH   F .   ? 0.6356 0.6316 0.3969 0.2661  -0.0441 -0.0577 395 HOH   A O   
6578 O  O   . HOH   F .   ? 0.3553 0.6049 0.3978 -0.0665 0.0139  0.1316  396 HOH   A O   
6579 O  O   . HOH   F .   ? 0.2332 0.2149 0.2606 0.0221  -0.0016 0.0512  397 HOH   A O   
6580 O  O   B HOH   F .   ? 0.1073 0.1553 0.2606 -0.0087 0.0376  0.0590  398 HOH   A O   
6581 O  O   . HOH   F .   ? 0.2304 0.2497 0.3604 0.0202  -0.0467 -0.0480 399 HOH   A O   
6582 O  O   . HOH   F .   ? 0.1841 0.2074 0.2567 -0.0148 -0.0191 0.0772  400 HOH   A O   
6583 O  O   . HOH   F .   ? 0.2396 0.3763 0.3573 -0.0141 0.0895  -0.0786 401 HOH   A O   
6584 O  O   . HOH   F .   ? 0.3115 0.3611 0.4335 -0.0581 0.1521  -0.0066 402 HOH   A O   
6585 O  O   . HOH   F .   ? 0.4809 0.3412 0.4800 0.0651  0.1412  -0.0951 403 HOH   A O   
6586 O  O   . HOH   F .   ? 0.1711 0.1358 0.1481 -0.0235 0.0050  0.0056  404 HOH   A O   
6587 O  O   . HOH   F .   ? 0.1866 0.2514 0.3468 -0.0080 -0.0312 0.0183  405 HOH   A O   
6588 O  O   . HOH   F .   ? 0.4953 0.3978 0.1811 -0.0373 0.1027  0.0303  406 HOH   A O   
6589 O  O   A HOH   F .   ? 0.1293 0.1503 0.1321 0.0105  -0.0303 0.0042  407 HOH   A O   
6590 O  O   A HOH   F .   ? 0.2234 0.2337 0.2829 -0.0081 0.0817  0.0024  408 HOH   A O   
6591 O  O   . HOH   F .   ? 0.2737 0.2513 0.2128 -0.0663 -0.0719 0.0248  409 HOH   A O   
6592 O  O   . HOH   F .   ? 0.2048 0.1603 0.2710 0.0081  -0.0333 0.0047  410 HOH   A O   
6593 O  O   . HOH   F .   ? 0.2530 0.2011 0.2397 -0.0531 -0.0026 0.0562  411 HOH   A O   
6594 O  O   A HOH   F .   ? 0.3299 0.3039 0.3950 -0.1349 0.0862  -0.0123 412 HOH   A O   
6595 O  O   . HOH   F .   ? 0.5858 0.6897 0.5360 0.0870  0.0179  0.0495  413 HOH   A O   
6596 O  O   . HOH   F .   ? 0.4696 0.3007 0.3202 -0.1256 0.0826  0.0589  414 HOH   A O   
6597 O  O   . HOH   F .   ? 0.5389 0.6078 0.5800 -0.0277 0.1092  0.0465  415 HOH   A O   
6598 O  O   . HOH   F .   ? 0.1388 0.1649 0.2755 -0.0071 -0.0026 0.0212  416 HOH   A O   
6599 O  O   A HOH   F .   ? 0.1181 0.1196 0.1294 0.0051  -0.0109 -0.0070 417 HOH   A O   
6600 O  O   . HOH   F .   ? 0.1988 0.1942 0.2672 0.0193  -0.0468 0.0381  418 HOH   A O   
6601 O  O   . HOH   F .   ? 0.3397 0.2664 0.4867 0.0781  0.0607  -0.0042 419 HOH   A O   
6602 O  O   . HOH   F .   ? 0.2000 0.2681 0.2445 -0.0061 -0.0558 0.0435  420 HOH   A O   
6603 O  O   . HOH   F .   ? 0.3974 0.6705 0.3051 -0.0949 -0.0107 0.1146  421 HOH   A O   
6604 O  O   B HOH   F .   ? 0.2978 0.3862 0.1933 -0.0424 0.0474  0.0218  422 HOH   A O   
6605 O  O   . HOH   F .   ? 0.4061 0.4584 0.3265 0.1526  -0.1077 -0.1173 423 HOH   A O   
6606 O  O   . HOH   F .   ? 0.2197 0.4399 0.2484 0.1609  0.0038  0.0316  424 HOH   A O   
6607 O  O   . HOH   F .   ? 0.2992 0.5595 0.1634 -0.0662 0.0479  0.0163  425 HOH   A O   
6608 O  O   . HOH   F .   ? 0.6216 0.5597 0.6696 -0.0896 -0.0908 -0.0769 426 HOH   A O   
6609 O  O   . HOH   F .   ? 0.3325 0.1164 0.2044 -0.0013 -0.0536 0.0066  427 HOH   A O   
6610 O  O   A HOH   F .   ? 0.5010 0.3736 0.4039 -0.1190 0.1076  0.0338  428 HOH   A O   
6611 O  O   . HOH   F .   ? 0.4218 0.2213 0.5433 -0.0789 -0.2045 0.1123  429 HOH   A O   
6612 O  O   . HOH   F .   ? 0.1656 0.1930 0.2601 -0.0158 0.0009  0.0350  430 HOH   A O   
6613 O  O   . HOH   F .   ? 0.6653 0.4084 0.5354 0.1961  -0.0891 0.1577  431 HOH   A O   
6614 O  O   . HOH   F .   ? 0.2083 0.1576 0.1468 -0.0048 0.0220  0.0121  432 HOH   A O   
6615 O  O   . HOH   F .   ? 0.3255 0.3654 0.7439 -0.0242 0.1032  -0.0562 433 HOH   A O   
6616 O  O   . HOH   F .   ? 0.2472 0.2870 0.2788 -0.0056 -0.0262 -0.0542 434 HOH   A O   
6617 O  O   A HOH   F .   ? 0.3344 0.2262 0.2602 0.0816  0.1118  0.0978  435 HOH   A O   
6618 O  O   . HOH   F .   ? 0.5406 0.7159 0.4448 0.0940  0.2649  -0.0801 436 HOH   A O   
6619 O  O   . HOH   F .   ? 0.6078 0.7393 0.4130 0.1864  -0.1030 0.1873  437 HOH   A O   
6620 O  O   . HOH   F .   ? 0.2801 0.4575 0.5051 0.0015  0.1100  -0.1920 438 HOH   A O   
6621 O  O   . HOH   F .   ? 0.6453 0.5765 0.6377 -0.1413 0.0033  -0.1265 439 HOH   A O   
6622 O  O   A HOH   F .   ? 0.1452 0.1384 0.1227 -0.0117 -0.0117 -0.0103 440 HOH   A O   
6623 O  O   B HOH   F .   ? 0.4279 0.4210 0.4839 -0.0268 -0.0668 -0.0916 441 HOH   A O   
6624 O  O   . HOH   F .   ? 0.8979 0.9610 0.7003 -0.0452 -0.0179 -0.0065 442 HOH   A O   
6625 O  O   . HOH   F .   ? 0.4352 0.4693 0.3465 -0.0350 -0.1472 0.0146  443 HOH   A O   
6626 O  O   . HOH   F .   ? 0.1834 0.2097 0.5193 -0.0245 -0.0839 0.0761  444 HOH   A O   
6627 O  O   . HOH   F .   ? 0.3539 0.2605 0.1650 -0.0774 0.0357  0.0456  445 HOH   A O   
6628 O  O   . HOH   F .   ? 0.2495 0.1515 0.2677 0.0076  0.0017  0.0040  446 HOH   A O   
6629 O  O   A HOH   F .   ? 0.1809 0.1557 0.3112 0.0284  -0.0918 -0.0641 447 HOH   A O   
6630 O  O   . HOH   F .   ? 0.4077 0.4503 0.4836 -0.0497 -0.1058 -0.1285 448 HOH   A O   
6631 O  O   . HOH   F .   ? 0.3823 0.3410 0.3111 0.2100  -0.0344 -0.0294 449 HOH   A O   
6632 O  O   B HOH   F .   ? 0.4796 0.2633 0.4079 0.1249  -0.0078 -0.0225 450 HOH   A O   
6633 O  O   . HOH   F .   ? 0.5297 0.4058 0.6132 0.0489  0.0542  -0.1169 451 HOH   A O   
6634 O  O   . HOH   F .   ? 0.7655 0.7115 0.6401 0.1998  -0.1114 0.0731  452 HOH   A O   
6635 O  O   . HOH   F .   ? 0.2335 0.1829 0.2480 0.0163  0.0264  0.0212  453 HOH   A O   
6636 O  O   . HOH   F .   ? 0.2183 0.2472 0.2431 -0.0021 -0.0040 -0.0491 454 HOH   A O   
6637 O  O   . HOH   F .   ? 0.6682 0.5745 0.7706 0.0028  -0.1253 0.2038  455 HOH   A O   
6638 O  O   . HOH   F .   ? 0.6837 0.5812 0.4701 0.0064  0.0741  0.1186  456 HOH   A O   
6639 O  O   A HOH   F .   ? 0.2694 0.1718 0.3294 0.0246  0.0894  0.0971  457 HOH   A O   
6640 O  O   . HOH   F .   ? 0.5006 0.2831 0.3760 0.0635  0.1235  0.0776  458 HOH   A O   
6641 O  O   . HOH   F .   ? 0.4593 0.4091 0.4265 0.0412  -0.0508 0.0959  459 HOH   A O   
6642 O  O   B HOH   F .   ? 0.5313 0.3681 0.2306 0.1743  0.0288  -0.0303 460 HOH   A O   
6643 O  O   . HOH   F .   ? 0.6507 0.5134 0.4991 -0.0805 0.1413  0.0496  461 HOH   A O   
6644 O  O   . HOH   F .   ? 0.2899 0.4251 0.3642 0.1021  -0.0233 0.1055  462 HOH   A O   
6645 O  O   . HOH   F .   ? 0.4699 0.3681 0.4894 0.0188  -0.0123 0.0683  463 HOH   A O   
6646 O  O   . HOH   F .   ? 0.6897 0.5680 0.6003 0.1236  0.2103  0.2361  464 HOH   A O   
6647 O  O   . HOH   F .   ? 0.2689 0.2631 0.3410 -0.0490 0.0342  -0.0661 465 HOH   A O   
6648 O  O   . HOH   F .   ? 0.7529 0.7317 0.4937 0.0102  -0.1163 -0.0108 466 HOH   A O   
6649 O  O   . HOH   F .   ? 0.2969 0.4269 0.5239 -0.1218 0.0812  -0.1849 467 HOH   A O   
6650 O  O   . HOH   F .   ? 0.3510 0.4460 0.4961 0.0717  -0.0476 0.1265  468 HOH   A O   
6651 O  O   . HOH   F .   ? 0.2719 0.3930 0.6060 0.0600  0.0543  -0.1990 469 HOH   A O   
6652 O  O   . HOH   F .   ? 0.2946 0.2688 0.6502 0.0920  -0.1346 -0.0615 470 HOH   A O   
6653 O  O   . HOH   F .   ? 0.3312 0.4179 0.3777 -0.0668 -0.0015 -0.0222 471 HOH   A O   
6654 O  O   . HOH   F .   ? 0.6668 0.3375 0.7903 0.0642  0.0260  0.2415  472 HOH   A O   
6655 O  O   . HOH   F .   ? 0.2384 0.2616 0.3301 -0.0780 0.0460  -0.0267 473 HOH   A O   
6656 O  O   . HOH   F .   ? 0.2695 0.1688 0.2554 0.0338  -0.0901 -0.0214 474 HOH   A O   
6657 O  O   B HOH   F .   ? 0.2532 0.4421 0.2315 0.0485  -0.0586 -0.0376 475 HOH   A O   
6658 O  O   B HOH   F .   ? 0.2060 0.4434 0.3595 0.1039  -0.0735 -0.0811 476 HOH   A O   
6659 O  O   . HOH   F .   ? 0.4093 0.5833 0.4253 -0.0781 -0.0856 0.2486  477 HOH   A O   
6660 O  O   . HOH   F .   ? 0.5555 0.4974 0.4789 0.0371  0.1533  0.0708  478 HOH   A O   
6661 O  O   . HOH   F .   ? 0.3229 0.2316 0.3762 0.0136  0.0897  0.0038  479 HOH   A O   
6662 O  O   . HOH   F .   ? 0.3669 0.5303 0.3469 0.0439  -0.0327 -0.0702 480 HOH   A O   
6663 O  O   . HOH   F .   ? 0.2377 0.2279 0.2433 0.0185  0.0173  0.0146  481 HOH   A O   
6664 O  O   . HOH   F .   ? 0.4591 0.5496 0.4685 0.1108  -0.0910 -0.1286 482 HOH   A O   
6665 O  O   . HOH   F .   ? 0.5057 0.5688 0.6199 -0.1657 -0.1145 0.0069  483 HOH   A O   
6666 O  O   . HOH   F .   ? 0.4643 0.2507 0.3418 -0.0621 -0.1039 0.0597  484 HOH   A O   
6667 O  O   . HOH   F .   ? 0.4643 0.4076 0.4721 -0.2127 -0.0164 0.0057  485 HOH   A O   
6668 O  O   . HOH   F .   ? 0.4202 0.4357 0.2692 -0.0196 -0.0186 -0.0147 486 HOH   A O   
6669 O  O   . HOH   F .   ? 0.4312 0.4248 0.3408 -0.0537 -0.0321 -0.0217 487 HOH   A O   
6670 O  O   . HOH   F .   ? 0.6686 0.5515 0.4358 0.1796  -0.1458 -0.0225 488 HOH   A O   
6671 O  O   . HOH   F .   ? 0.5781 0.3935 0.4202 0.0551  -0.0013 -0.1224 489 HOH   A O   
6672 O  O   . HOH   F .   ? 0.7270 0.4000 0.3106 -0.0669 -0.1114 0.0210  490 HOH   A O   
6673 O  O   . HOH   F .   ? 0.7486 0.5025 0.6248 -0.0993 0.0617  -0.0950 491 HOH   A O   
6674 O  O   B HOH   F .   ? 0.2102 0.1486 0.2687 0.0459  -0.0474 0.0464  492 HOH   A O   
6675 O  O   . HOH   F .   ? 0.3027 0.4358 0.4329 0.0203  0.1314  0.1218  493 HOH   A O   
6676 O  O   . HOH   F .   ? 0.3019 0.5074 0.3811 0.1170  0.1206  0.2368  494 HOH   A O   
6677 O  O   . HOH   F .   ? 0.4149 0.3739 0.2596 -0.0898 0.1488  -0.0672 495 HOH   A O   
6678 O  O   . HOH   F .   ? 0.7160 0.6585 0.4770 -0.0445 0.1186  0.0693  496 HOH   A O   
6679 O  O   . HOH   F .   ? 0.4726 0.5898 0.6647 0.0849  0.1188  -0.1266 497 HOH   A O   
6680 O  O   . HOH   F .   ? 0.6211 0.3737 0.4254 -0.0369 0.1116  -0.0117 498 HOH   A O   
6681 O  O   B HOH   F .   ? 0.4580 0.3861 0.4319 0.0356  -0.0981 0.0155  499 HOH   A O   
6682 O  O   . HOH   F .   ? 0.2504 0.2421 0.7394 -0.0070 -0.1349 0.0315  500 HOH   A O   
6683 O  O   . HOH   F .   ? 0.4721 0.3098 0.4482 -0.0248 0.2365  0.0086  501 HOH   A O   
6684 O  O   . HOH   F .   ? 0.4327 0.2743 0.4039 -0.0966 0.0283  0.0811  502 HOH   A O   
6685 O  O   . HOH   F .   ? 0.2914 0.2064 0.6160 0.0203  0.0653  0.1126  503 HOH   A O   
6686 O  O   . HOH   F .   ? 0.4800 0.4376 0.5223 -0.0212 -0.1119 0.0463  504 HOH   A O   
6687 O  O   . HOH   F .   ? 0.6125 0.4770 0.4958 -0.0899 -0.0797 -0.0795 505 HOH   A O   
6688 O  O   . HOH   F .   ? 0.3181 0.4594 0.3319 -0.0676 -0.0024 -0.0800 506 HOH   A O   
6689 O  O   . HOH   F .   ? 0.2515 0.2779 0.5005 -0.0072 0.1146  -0.0392 507 HOH   A O   
6690 O  O   B HOH   F .   ? 0.2652 0.1994 0.2737 0.0794  -0.0036 0.0631  508 HOH   A O   
6691 O  O   . HOH   F .   ? 0.5373 0.5050 0.4215 0.0538  -0.0724 -0.0637 509 HOH   A O   
6692 O  O   . HOH   F .   ? 0.3970 0.8595 0.5406 -0.0545 -0.0569 0.2674  510 HOH   A O   
6693 O  O   . HOH   F .   ? 0.2545 0.3449 0.3435 0.0762  -0.0736 0.0399  511 HOH   A O   
6694 O  O   . HOH   F .   ? 0.4758 0.2347 0.4106 -0.1283 0.0316  0.0140  512 HOH   A O   
6695 O  O   . HOH   F .   ? 0.6250 0.2387 0.4161 -0.0773 0.0576  0.0507  513 HOH   A O   
6696 O  O   B HOH   F .   ? 0.2450 0.3773 0.2741 0.0553  0.0147  0.1030  514 HOH   A O   
6697 O  O   . HOH   F .   ? 0.2824 0.4082 0.4231 0.0548  -0.0095 0.0180  515 HOH   A O   
6698 O  O   . HOH   F .   ? 0.8484 0.5461 0.5451 0.0035  0.0441  0.0559  516 HOH   A O   
6699 O  O   . HOH   F .   ? 0.4795 0.7394 0.5569 0.0606  -0.0518 0.1858  517 HOH   A O   
6700 O  O   . HOH   F .   ? 0.2729 0.2278 0.4489 0.0008  0.0422  0.0515  518 HOH   A O   
6701 O  O   . HOH   F .   ? 0.5005 0.6793 0.4841 0.3151  -0.0189 0.0882  519 HOH   A O   
6702 O  O   . HOH   F .   ? 0.4923 0.5812 0.4742 -0.0117 -0.0282 -0.1048 520 HOH   A O   
6703 O  O   A HOH   F .   ? 0.3529 0.6000 0.2098 0.0336  0.0307  0.0985  521 HOH   A O   
6704 O  O   . HOH   F .   ? 0.2705 0.6397 0.3806 0.0382  0.0333  -0.0177 522 HOH   A O   
6705 O  O   . HOH   F .   ? 0.4223 0.5247 0.4089 0.1322  -0.0406 0.1545  523 HOH   A O   
6706 O  O   . HOH   F .   ? 0.4814 0.6894 0.5813 -0.0704 -0.0846 0.0817  524 HOH   A O   
6707 O  O   . HOH   F .   ? 0.3248 0.4321 0.5104 -0.0392 -0.0946 0.2629  525 HOH   A O   
6708 O  O   . HOH   G .   ? 0.2186 0.2013 0.3130 0.0147  0.0827  0.0370  201 HOH   B O   
6709 O  O   . HOH   G .   ? 0.4620 0.3241 0.3727 -0.0379 0.0291  -0.1252 202 HOH   B O   
6710 O  O   . HOH   G .   ? 0.4777 0.4751 0.2567 0.0126  -0.0336 -0.1248 203 HOH   B O   
6711 O  O   . HOH   G .   ? 0.3594 0.4166 0.5778 -0.0746 0.0314  -0.1491 204 HOH   B O   
6712 O  O   . HOH   G .   ? 0.3051 0.5477 0.5293 0.0148  0.1724  -0.1658 205 HOH   B O   
6713 O  O   . HOH   G .   ? 0.2845 0.6794 0.4676 0.0734  0.0221  0.2757  206 HOH   B O   
6714 O  O   . HOH   G .   ? 0.7046 0.3447 0.4594 0.0099  0.1319  -0.0054 207 HOH   B O   
6715 O  O   . HOH   G .   ? 0.4853 0.6184 0.3351 0.2955  -0.0915 -0.0202 208 HOH   B O   
6716 O  O   . HOH   G .   ? 0.3194 0.4029 0.7259 -0.0390 0.0567  -0.0694 209 HOH   B O   
6717 O  O   . HOH   G .   ? 0.7284 0.6313 0.5397 0.2580  0.0352  0.0352  210 HOH   B O   
6718 O  O   . HOH   G .   ? 0.4151 0.3957 0.4040 -0.0313 -0.1190 0.0775  211 HOH   B O   
6719 O  O   . HOH   G .   ? 0.2603 0.2984 0.7085 0.0596  -0.1095 0.0326  212 HOH   B O   
6720 O  O   . HOH   G .   ? 0.6252 0.3004 0.4000 -0.1946 0.0489  0.0221  213 HOH   B O   
6721 O  O   . HOH   G .   ? 0.2226 0.2175 0.2652 0.0127  0.0197  -0.0339 214 HOH   B O   
6722 O  O   . HOH   G .   ? 0.2930 0.2139 0.5310 0.0318  0.1854  0.1078  215 HOH   B O   
6723 O  O   . HOH   G .   ? 0.3934 0.5299 0.4207 0.2108  -0.0586 -0.0238 216 HOH   B O   
6724 O  O   . HOH   G .   ? 0.5255 0.4005 0.6038 0.0477  -0.1103 0.2515  217 HOH   B O   
6725 O  O   . HOH   G .   ? 0.3206 0.5204 0.5044 0.1836  0.0238  -0.0810 218 HOH   B O   
6726 O  O   . HOH   G .   ? 0.1544 0.1786 0.2599 -0.0168 -0.0098 0.0017  219 HOH   B O   
6727 O  O   . HOH   G .   ? 0.1477 0.1477 0.1971 -0.0202 0.0019  0.0038  220 HOH   B O   
6728 O  O   . HOH   G .   ? 0.4641 0.1936 0.3249 -0.0119 -0.1028 0.0121  221 HOH   B O   
6729 O  O   . HOH   G .   ? 0.7800 0.4455 0.5175 0.1985  0.0518  -0.0599 222 HOH   B O   
6730 O  O   . HOH   G .   ? 0.4266 0.4333 0.3767 0.0195  0.0615  -0.1589 223 HOH   B O   
6731 O  O   . HOH   G .   ? 0.3740 0.3944 0.4587 -0.1592 0.0294  0.0619  224 HOH   B O   
6732 O  O   . HOH   G .   ? 0.6023 0.5516 0.2986 0.0868  -0.0234 0.0303  225 HOH   B O   
6733 O  O   . HOH   G .   ? 0.2143 0.2049 0.3714 -0.0267 -0.0114 -0.0526 226 HOH   B O   
6734 O  O   . HOH   G .   ? 0.4540 0.4251 0.6117 -0.0024 -0.1624 -0.1200 227 HOH   B O   
6735 O  O   . HOH   G .   ? 0.2444 0.1707 0.2762 -0.0281 0.1081  -0.0028 228 HOH   B O   
6736 O  O   . HOH   G .   ? 0.3047 0.2479 0.6320 -0.0098 0.0765  0.0290  229 HOH   B O   
6737 O  O   . HOH   G .   ? 0.3823 0.2443 0.3977 0.0709  -0.0527 -0.0705 230 HOH   B O   
6738 O  O   . HOH   G .   ? 0.3043 0.3911 0.4625 0.0514  -0.1545 0.0054  231 HOH   B O   
6739 O  O   . HOH   G .   ? 0.1625 0.2048 0.2803 -0.0127 0.0078  -0.0166 232 HOH   B O   
6740 O  O   . HOH   G .   ? 0.3518 0.3382 0.2185 0.0440  0.0694  0.0544  233 HOH   B O   
6741 O  O   . HOH   G .   ? 0.3533 0.1749 0.2047 0.0106  -0.0898 -0.0067 234 HOH   B O   
6742 O  O   . HOH   G .   ? 0.2886 0.2206 0.4682 0.0057  0.1605  0.0271  235 HOH   B O   
6743 O  O   . HOH   G .   ? 0.2592 0.2469 0.3192 0.0283  0.0239  -0.0817 236 HOH   B O   
6744 O  O   . HOH   G .   ? 0.1961 0.3850 0.2157 -0.0431 -0.0135 0.0621  237 HOH   B O   
6745 O  O   . HOH   G .   ? 0.4315 0.5664 0.3231 0.2065  0.0134  -0.0498 238 HOH   B O   
6746 O  O   . HOH   G .   ? 0.3341 0.3621 0.3966 0.0770  -0.0991 -0.1936 239 HOH   B O   
6747 O  O   . HOH   G .   ? 0.2136 0.3708 0.2995 -0.0298 -0.0739 -0.0528 240 HOH   B O   
6748 O  O   . HOH   G .   ? 0.2586 0.3727 0.3014 -0.0772 0.0588  -0.0864 241 HOH   B O   
6749 O  O   . HOH   G .   ? 0.5243 0.3054 0.3858 -0.2202 0.0385  -0.0023 242 HOH   B O   
6750 O  O   . HOH   G .   ? 0.1419 0.1387 0.1533 -0.0143 -0.0048 0.0005  243 HOH   B O   
6751 O  O   . HOH   G .   ? 0.1977 0.2091 0.3304 -0.0339 -0.0041 -0.0234 244 HOH   B O   
6752 O  O   . HOH   G .   ? 0.1980 0.1283 0.3320 0.0165  -0.0527 -0.0184 245 HOH   B O   
6753 O  O   . HOH   G .   ? 0.1506 0.1387 0.2470 -0.0062 0.0095  -0.0114 246 HOH   B O   
6754 O  O   . HOH   G .   ? 0.1356 0.1306 0.1582 -0.0029 -0.0001 0.0045  247 HOH   B O   
6755 O  O   . HOH   G .   ? 0.3075 0.2439 0.3099 -0.0194 0.0151  -0.0737 248 HOH   B O   
6756 O  O   . HOH   G .   ? 0.2034 0.2026 0.2067 -0.0287 -0.0514 0.0127  249 HOH   B O   
6757 O  O   . HOH   G .   ? 0.4373 0.3475 0.3626 -0.1034 0.1034  -0.1295 250 HOH   B O   
6758 O  O   . HOH   G .   ? 0.3018 0.1778 0.5973 -0.0167 -0.1364 -0.0417 251 HOH   B O   
6759 O  O   . HOH   G .   ? 0.2002 0.1431 0.2051 -0.0248 -0.0334 0.0315  252 HOH   B O   
6760 O  O   . HOH   G .   ? 0.3395 0.3370 0.1964 0.0536  0.0768  0.0184  253 HOH   B O   
6761 O  O   . HOH   G .   ? 0.2911 0.2240 0.2914 0.0942  0.1002  0.0208  254 HOH   B O   
6762 O  O   . HOH   G .   ? 0.2185 0.2141 0.2466 0.0684  -0.0718 -0.0716 255 HOH   B O   
6763 O  O   . HOH   G .   ? 0.5338 0.3130 0.2556 -0.0156 0.0576  -0.0174 256 HOH   B O   
6764 O  O   . HOH   G .   ? 0.3027 0.4496 0.2992 -0.1185 -0.0510 -0.0631 257 HOH   B O   
6765 O  O   . HOH   G .   ? 0.2261 0.2041 0.1789 0.0117  -0.0103 0.0033  258 HOH   B O   
6766 O  O   . HOH   G .   ? 0.1337 0.1598 0.1972 -0.0046 0.0068  0.0109  259 HOH   B O   
6767 O  O   . HOH   G .   ? 0.1549 0.1607 0.2777 -0.0223 -0.0164 0.0048  260 HOH   B O   
6768 O  O   . HOH   G .   ? 0.4392 0.3445 0.2701 0.0773  -0.0232 -0.0969 261 HOH   B O   
6769 O  O   . HOH   G .   ? 0.1762 0.2636 0.2531 0.0474  0.0514  0.0972  262 HOH   B O   
6770 O  O   . HOH   G .   ? 0.2201 0.2800 0.2190 -0.0454 0.0136  0.0503  263 HOH   B O   
6771 O  O   . HOH   G .   ? 0.2277 0.4656 0.5309 0.1219  -0.0571 -0.0593 264 HOH   B O   
6772 O  O   . HOH   G .   ? 0.2408 0.1773 0.3385 0.0120  -0.0637 -0.0306 265 HOH   B O   
6773 O  O   . HOH   G .   ? 0.2481 0.1938 0.2749 -0.0599 0.0167  -0.0070 266 HOH   B O   
6774 O  O   . HOH   G .   ? 0.2997 0.4785 0.4008 -0.0234 -0.0922 0.1483  267 HOH   B O   
6775 O  O   . HOH   G .   ? 0.2010 0.1466 0.2142 -0.0256 -0.0170 0.0195  268 HOH   B O   
6776 O  O   . HOH   G .   ? 0.2519 0.2724 0.2449 -0.0374 -0.0776 0.0147  269 HOH   B O   
6777 O  O   . HOH   G .   ? 0.2510 0.4668 0.5987 0.0341  0.0445  -0.1041 270 HOH   B O   
6778 O  O   . HOH   G .   ? 0.3837 0.3034 0.5078 -0.0314 -0.0977 -0.0940 271 HOH   B O   
6779 O  O   . HOH   G .   ? 0.2036 0.4149 0.4707 -0.0516 -0.0281 -0.1643 272 HOH   B O   
6780 O  O   . HOH   G .   ? 0.2709 0.4085 0.5118 -0.0399 0.0984  -0.0955 273 HOH   B O   
6781 O  O   . HOH   G .   ? 0.2319 0.2574 0.2332 -0.0543 -0.0573 -0.0379 274 HOH   B O   
6782 O  O   . HOH   G .   ? 0.1661 0.1332 0.4294 -0.0066 -0.0225 -0.0094 275 HOH   B O   
6783 O  O   . HOH   G .   ? 0.1781 0.1773 0.1641 -0.0446 -0.0444 0.0131  276 HOH   B O   
6784 O  O   . HOH   G .   ? 0.2264 0.2114 0.1938 0.0112  -0.0096 -0.0031 277 HOH   B O   
6785 O  O   . HOH   G .   ? 0.2206 0.2762 0.2259 0.0805  -0.0273 -0.0160 278 HOH   B O   
6786 O  O   . HOH   G .   ? 0.1568 0.1461 0.3264 -0.0154 0.0051  -0.0026 279 HOH   B O   
6787 O  O   . HOH   G .   ? 0.2187 0.3383 0.3248 -0.0377 0.0525  -0.1357 280 HOH   B O   
6788 O  O   . HOH   G .   ? 0.1518 0.1489 0.1815 0.0014  0.0083  0.0024  281 HOH   B O   
6789 O  O   . HOH   G .   ? 0.2417 0.4110 0.3516 0.0357  0.1077  0.0163  282 HOH   B O   
6790 O  O   . HOH   G .   ? 0.4048 0.7472 0.3462 0.1347  -0.0974 0.1392  283 HOH   B O   
6791 O  O   . HOH   G .   ? 0.2586 0.2051 0.4818 0.0202  0.0502  0.0326  284 HOH   B O   
6792 O  O   . HOH   G .   ? 0.3189 0.3833 0.4650 0.1283  -0.0607 -0.0961 285 HOH   B O   
6793 O  O   . HOH   G .   ? 0.2588 0.4523 0.4685 -0.1044 -0.1266 0.1021  286 HOH   B O   
6794 O  O   . HOH   G .   ? 0.2412 0.7264 0.2628 0.0622  -0.0360 -0.0811 287 HOH   B O   
6795 O  O   . HOH   G .   ? 0.2266 0.2576 0.2780 0.0235  -0.0656 0.0150  288 HOH   B O   
6796 O  O   . HOH   G .   ? 0.4939 0.6326 0.2705 -0.0389 -0.1105 0.0538  289 HOH   B O   
6797 O  O   . HOH   G .   ? 0.3732 0.5499 0.5171 -0.0093 -0.1334 0.0590  290 HOH   B O   
6798 O  O   . HOH   G .   ? 0.1518 0.1981 0.1545 -0.0148 -0.0176 0.0103  291 HOH   B O   
6799 O  O   . HOH   G .   ? 0.1587 0.1908 0.2752 0.0164  -0.0150 0.0056  292 HOH   B O   
6800 O  O   . HOH   G .   ? 0.3454 0.2645 0.2024 0.0456  -0.0778 -0.0101 293 HOH   B O   
6801 O  O   . HOH   G .   ? 0.3039 0.2804 0.2832 -0.0094 0.0127  -0.1202 294 HOH   B O   
6802 O  O   . HOH   G .   ? 0.4701 0.3863 0.2647 0.1343  -0.0966 0.0467  295 HOH   B O   
6803 O  O   . HOH   G .   ? 0.1731 0.3003 0.4425 0.0264  0.0028  -0.1273 296 HOH   B O   
6804 O  O   . HOH   G .   ? 0.3919 0.2323 0.3626 -0.1062 -0.1997 0.0805  297 HOH   B O   
6805 O  O   . HOH   G .   ? 0.2930 0.3219 0.3869 -0.1087 0.0870  -0.0521 298 HOH   B O   
6806 O  O   . HOH   G .   ? 0.1974 0.2528 0.5914 0.0352  -0.0625 -0.1085 299 HOH   B O   
6807 O  O   . HOH   G .   ? 0.1728 0.1541 0.2264 0.0125  0.0067  0.0175  300 HOH   B O   
6808 O  O   . HOH   G .   ? 0.4281 0.4453 0.2021 -0.0260 0.0764  0.0309  301 HOH   B O   
6809 O  O   . HOH   G .   ? 0.3499 0.1803 0.3367 0.0765  0.1273  0.0631  302 HOH   B O   
6810 O  O   . HOH   G .   ? 0.2955 0.2739 0.5108 -0.0198 -0.0742 0.1082  303 HOH   B O   
6811 O  O   . HOH   G .   ? 0.2080 0.1573 0.2596 -0.0202 -0.0353 -0.0107 304 HOH   B O   
6812 O  O   . HOH   G .   ? 0.2738 0.6953 0.7120 0.1354  -0.0412 -0.0869 305 HOH   B O   
6813 O  O   . HOH   G .   ? 0.1629 0.1344 0.2817 0.0013  0.0017  0.0017  306 HOH   B O   
6814 O  O   . HOH   G .   ? 0.2580 0.3180 0.4426 -0.0627 -0.1441 0.1208  307 HOH   B O   
6815 O  O   . HOH   G .   ? 0.5925 0.3763 0.3342 0.2584  0.1145  0.0881  308 HOH   B O   
6816 O  O   . HOH   G .   ? 0.4812 0.3411 0.4693 -0.0977 0.0266  0.1413  309 HOH   B O   
6817 O  O   . HOH   G .   ? 0.5288 0.4472 0.2325 0.1472  -0.0448 -0.0280 310 HOH   B O   
6818 O  O   . HOH   G .   ? 0.2147 0.1494 0.3254 0.0342  -0.0991 0.0027  311 HOH   B O   
6819 O  O   . HOH   G .   ? 0.4900 0.3019 0.2329 -0.1831 0.0816  -0.0271 312 HOH   B O   
6820 O  O   . HOH   G .   ? 0.4020 0.2302 0.2806 0.1523  0.1106  0.0389  313 HOH   B O   
6821 O  O   . HOH   G .   ? 0.1558 0.1887 0.2669 -0.0249 -0.0152 0.0107  314 HOH   B O   
6822 O  O   . HOH   G .   ? 0.2245 0.1448 0.2415 -0.0138 -0.0114 0.0284  315 HOH   B O   
6823 O  O   . HOH   G .   ? 0.3989 0.4389 0.6533 0.0778  0.0029  0.1155  316 HOH   B O   
6824 O  O   . HOH   G .   ? 0.6630 0.4446 0.4342 0.1563  0.0816  -0.0018 317 HOH   B O   
6825 O  O   . HOH   G .   ? 0.2053 0.3419 0.5038 -0.0375 -0.0437 -0.0181 318 HOH   B O   
6826 O  O   . HOH   G .   ? 0.2607 0.2716 0.3717 -0.0392 0.0984  -0.0771 319 HOH   B O   
6827 O  O   . HOH   G .   ? 0.4469 0.4322 0.2445 0.0626  -0.0467 -0.0779 320 HOH   B O   
6828 O  O   . HOH   G .   ? 0.1489 0.1557 0.2886 -0.0113 -0.0113 -0.0207 321 HOH   B O   
6829 O  O   . HOH   G .   ? 0.2134 0.2012 0.1595 -0.0099 0.0170  0.0152  322 HOH   B O   
6830 O  O   . HOH   G .   ? 0.2760 0.2118 0.2392 0.0141  -0.0343 0.0352  323 HOH   B O   
6831 O  O   . HOH   G .   ? 0.6396 0.6087 0.4607 0.2817  0.0159  0.0024  324 HOH   B O   
6832 O  O   . HOH   G .   ? 0.5681 0.5284 0.5144 -0.1079 -0.0024 0.1132  325 HOH   B O   
6833 O  O   . HOH   G .   ? 0.1676 0.2851 0.2265 -0.0034 -0.0131 0.0697  326 HOH   B O   
6834 O  O   . HOH   G .   ? 0.3103 0.4169 0.7949 -0.0235 -0.0871 0.2243  327 HOH   B O   
6835 O  O   . HOH   G .   ? 0.4408 0.3202 0.5334 0.1097  0.2301  0.1873  328 HOH   B O   
6836 O  O   . HOH   G .   ? 0.2154 0.6415 0.5785 -0.0735 0.0156  -0.0131 329 HOH   B O   
6837 O  O   . HOH   G .   ? 0.7963 0.2031 0.2937 0.0058  -0.0716 0.0040  330 HOH   B O   
6838 O  O   . HOH   G .   ? 0.1866 0.1975 0.2793 0.0362  0.0544  0.0233  331 HOH   B O   
6839 O  O   . HOH   G .   ? 0.4810 0.2400 0.2971 0.0302  0.0611  0.0871  332 HOH   B O   
6840 O  O   . HOH   G .   ? 0.1802 0.2693 0.3050 0.0274  -0.0034 -0.0704 333 HOH   B O   
6841 O  O   . HOH   G .   ? 0.5443 0.3443 0.3678 0.0041  0.0912  0.1139  334 HOH   B O   
6842 O  O   . HOH   G .   ? 0.2620 0.2043 0.4247 0.0048  0.0219  0.0241  335 HOH   B O   
6843 O  O   . HOH   G .   ? 0.5383 0.5148 0.6182 0.0138  -0.1341 0.2402  336 HOH   B O   
6844 O  O   . HOH   G .   ? 0.5271 0.3308 0.4068 0.0036  0.0898  -0.1515 337 HOH   B O   
6845 O  O   . HOH   G .   ? 0.2298 0.2213 0.5377 -0.0452 0.0120  0.1314  338 HOH   B O   
6846 O  O   . HOH   G .   ? 0.1667 0.1417 0.2267 0.0088  -0.0159 0.0026  339 HOH   B O   
6847 O  O   . HOH   G .   ? 0.5033 0.3500 0.3032 0.0634  -0.1244 -0.0873 340 HOH   B O   
6848 O  O   . HOH   G .   ? 0.5453 0.3909 0.6471 -0.0723 -0.0186 -0.1137 341 HOH   B O   
6849 O  O   . HOH   G .   ? 0.4128 0.7389 0.3700 -0.0580 -0.0513 0.2141  342 HOH   B O   
6850 O  O   . HOH   G .   ? 0.4695 0.5911 0.3486 -0.0333 -0.1044 0.0545  343 HOH   B O   
6851 O  O   . HOH   G .   ? 0.6301 0.6505 0.2757 -0.0185 -0.0298 0.1419  344 HOH   B O   
6852 O  O   . HOH   G .   ? 0.2186 0.6160 0.7004 0.0398  0.0041  0.0664  345 HOH   B O   
6853 O  O   . HOH   G .   ? 0.2045 0.1933 0.2698 -0.0045 0.0565  -0.0116 346 HOH   B O   
6854 O  O   . HOH   G .   ? 0.4258 0.4623 0.5639 0.0175  -0.0926 0.1186  347 HOH   B O   
6855 O  O   . HOH   G .   ? 0.3778 0.6163 0.3968 -0.0772 -0.0894 -0.0882 348 HOH   B O   
6856 O  O   . HOH   G .   ? 0.4940 0.5520 0.4354 -0.1204 0.0225  0.1060  349 HOH   B O   
6857 O  O   . HOH   G .   ? 0.2610 0.2220 0.4864 -0.0169 -0.0793 -0.0640 350 HOH   B O   
6858 O  O   . HOH   G .   ? 0.2566 0.6010 0.3715 0.1738  -0.0538 -0.1343 351 HOH   B O   
6859 O  O   . HOH   G .   ? 0.2021 0.4112 0.5481 0.0366  0.0443  0.0482  352 HOH   B O   
6860 O  O   . HOH   G .   ? 0.3718 0.2135 0.3230 -0.0668 0.0165  -0.0752 353 HOH   B O   
6861 O  O   . HOH   G .   ? 0.4677 0.6182 0.6593 0.0912  0.0105  -0.0665 354 HOH   B O   
6862 O  O   . HOH   G .   ? 0.3674 0.3994 0.4723 -0.1473 -0.0043 -0.0638 355 HOH   B O   
6863 O  O   . HOH   G .   ? 0.4513 0.3206 0.5232 -0.1033 0.1537  0.0686  356 HOH   B O   
6864 O  O   . HOH   G .   ? 0.5230 0.3271 0.4369 0.0758  0.1379  -0.0489 357 HOH   B O   
6865 O  O   . HOH   G .   ? 0.3702 0.2815 0.3654 -0.0881 -0.0165 -0.0682 358 HOH   B O   
6866 O  O   . HOH   G .   ? 0.3141 0.1947 0.3767 0.0451  -0.1266 -0.0539 359 HOH   B O   
6867 O  O   . HOH   G .   ? 0.5277 0.4859 0.4544 -0.0337 -0.0808 0.0391  360 HOH   B O   
6868 O  O   . HOH   G .   ? 0.4567 0.3350 0.4132 0.0362  -0.1719 -0.0172 361 HOH   B O   
6869 O  O   . HOH   G .   ? 0.4394 0.5136 0.5270 0.1470  -0.1339 0.1717  362 HOH   B O   
6870 O  O   . HOH   G .   ? 0.4640 0.3879 0.6518 0.0357  0.0696  0.1273  363 HOH   B O   
6871 O  O   . HOH   G .   ? 0.4794 0.6810 0.2960 0.2573  0.0359  0.0723  364 HOH   B O   
6872 O  O   . HOH   G .   ? 0.2099 0.3350 0.6620 -0.0639 -0.0569 -0.0638 365 HOH   B O   
6873 O  O   . HOH   G .   ? 0.5496 0.5763 0.3504 0.1853  -0.1413 0.0743  366 HOH   B O   
6874 O  O   . HOH   G .   ? 0.5976 0.4914 0.4593 0.1493  0.1282  0.0999  367 HOH   B O   
6875 O  O   . HOH   G .   ? 0.5092 0.2830 0.5784 -0.1239 -0.0662 0.0270  368 HOH   B O   
6876 O  O   . HOH   G .   ? 0.6457 0.2011 0.3197 -0.0114 0.0134  0.0315  369 HOH   B O   
6877 O  O   . HOH   G .   ? 0.5590 0.3715 0.5380 0.0551  -0.1493 0.0061  370 HOH   B O   
6878 O  O   . HOH   G .   ? 0.8377 0.7784 0.5110 0.3074  -0.1355 0.0631  371 HOH   B O   
6879 O  O   . HOH   G .   ? 0.5194 0.5557 0.4198 -0.0801 -0.0322 -0.1105 372 HOH   B O   
6880 O  O   . HOH   G .   ? 0.4240 0.6033 0.5649 0.2828  0.0295  0.0753  373 HOH   B O   
6881 O  O   . HOH   G .   ? 0.7113 0.3716 0.2897 -0.0889 -0.1079 -0.0711 374 HOH   B O   
6882 O  O   . HOH   G .   ? 0.4586 0.3179 0.4034 0.0512  -0.1618 -0.0525 375 HOH   B O   
6883 O  O   . HOH   G .   ? 0.4547 0.4641 0.4604 -0.0939 -0.0763 0.0219  376 HOH   B O   
6884 O  O   . HOH   G .   ? 0.2395 0.4195 0.4241 0.0333  -0.0638 -0.0749 377 HOH   B O   
6885 O  O   . HOH   G .   ? 0.7682 0.3771 0.5674 -0.0816 -0.0414 -0.0196 378 HOH   B O   
6886 O  O   . HOH   G .   ? 0.4839 0.6449 0.5995 0.1489  0.0659  0.2771  379 HOH   B O   
6887 O  O   . HOH   G .   ? 0.3096 0.4411 0.2137 0.0605  0.0512  0.0209  380 HOH   B O   
6888 O  O   . HOH   G .   ? 0.3357 0.5471 0.5433 0.1678  -0.0417 0.0264  381 HOH   B O   
6889 O  O   . HOH   G .   ? 0.5239 0.7003 0.3873 -0.1424 0.0282  -0.1458 382 HOH   B O   
6890 O  O   . HOH   G .   ? 0.2990 0.2357 0.3352 0.0051  0.0173  0.0287  383 HOH   B O   
6891 O  O   . HOH   G .   ? 0.6543 0.7235 0.6561 -0.0437 0.2506  0.1068  384 HOH   B O   
6892 O  O   . HOH   G .   ? 0.7080 0.6206 0.4054 0.2327  0.0167  -0.0618 385 HOH   B O   
6893 O  O   . HOH   G .   ? 0.4238 0.8125 0.5676 0.1136  0.2129  0.0936  386 HOH   B O   
6894 O  O   . HOH   G .   ? 0.6710 0.3932 0.4601 0.0833  0.0847  -0.0862 387 HOH   B O   
6895 O  O   . HOH   G .   ? 0.2461 0.4155 0.3534 -0.0675 -0.1008 -0.0503 388 HOH   B O   
6896 O  O   . HOH   G .   ? 0.4621 0.3390 0.2993 0.0078  0.0080  -0.0165 389 HOH   B O   
6897 O  O   . HOH   G .   ? 0.5104 0.4832 0.5336 -0.0726 0.0306  -0.0108 390 HOH   B O   
6898 O  O   . HOH   G .   ? 0.3929 0.2149 0.3036 0.0772  -0.0227 0.0169  391 HOH   B O   
6899 O  O   . HOH   G .   ? 0.5683 0.3959 0.3986 0.0390  0.0589  0.0689  392 HOH   B O   
6900 O  O   . HOH   G .   ? 0.4129 0.2136 0.5136 -0.0487 0.0726  0.0410  393 HOH   B O   
6901 O  O   . HOH   G .   ? 0.2507 0.3887 0.6723 -0.1184 -0.0592 -0.0295 394 HOH   B O   
6902 O  O   . HOH   G .   ? 0.4218 0.4115 0.3985 0.0312  0.0770  0.0915  395 HOH   B O   
6903 O  O   . HOH   G .   ? 0.3092 0.3390 0.3437 0.0439  0.0190  -0.0371 396 HOH   B O   
6904 O  O   . HOH   G .   ? 0.4130 0.5332 0.3510 0.0832  -0.0300 -0.0887 397 HOH   B O   
6905 O  O   . HOH   G .   ? 0.2187 0.2642 0.5863 -0.0636 -0.1033 0.0103  398 HOH   B O   
6906 O  O   . HOH   G .   ? 0.5429 0.6517 0.7396 0.1357  -0.1223 0.1759  399 HOH   B O   
6907 O  O   . HOH   G .   ? 0.5329 0.4276 0.3135 -0.2233 -0.0509 0.1271  400 HOH   B O   
6908 O  O   . HOH   G .   ? 0.5649 0.6392 0.3980 0.1637  0.0221  -0.0355 401 HOH   B O   
# 
